A class of structurally related proteins of 12-20 kDa in size. They covalently modify specific proteins in a manner analogous to UBIQUITIN.
A 1.5-kDa small ubiquitin-related modifier protein that can covalently bind via an isopeptide link to a number of cellular proteins. It may play a role in intracellular protein transport and a number of other cellular processes.
A type of POST-TRANSLATIONAL PROTEIN MODIFICATION by SMALL UBIQUITIN-RELATED MODIFIER PROTEINS (also known as SUMO proteins).
A family of structurally related proteins that are constitutively expressed and that negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. PIAS proteins inhibit the activity of signal transducers and activators of transcription.
A class of enzymes that form a thioester bond to UBIQUITIN with the assistance of UBIQUITIN-ACTIVATING ENZYMES. They transfer ubiquitin to the LYSINE of a substrate protein with the assistance of UBIQUITIN-PROTEIN LIGASES.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
An essential amino acid. It is often added to animal feed.
A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6.
A highly conserved 76-amino acid peptide universally found in eukaryotic cells that functions as a marker for intracellular PROTEIN TRANSPORT and degradation. Ubiquitin becomes activated through a series of complicated steps and forms an isopeptide bond to lysine residues of specific proteins within the cell. These "ubiquitinated" proteins can be recognized and degraded by proteosomes or be transported to specific compartments within the cell.
ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
A subclass of PEPTIDE HYDROLASES that catalyze the internal cleavage of PEPTIDES or PROTEINS.
A class of enzymes that catalyzes the ATP-dependent formation of a thioester bond between itself and UBIQUITIN. It then transfers the activated ubiquitin to one of the UBIQUITIN-PROTEIN LIGASES.
Circumscribed masses of foreign or metabolically inactive materials, within the CELL NUCLEUS. Some are VIRAL INCLUSION BODIES.
A sport consisting of hand-to-hand combat between two unarmed contestants seeking to pin or press each other's shoulders to the ground.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.
Enzymes that catalyze the cleavage of a carbon-nitrogen bond by means other than hydrolysis or oxidation. Subclasses are the AMMONIA-LYASES, the AMIDINE-LYASES, the amine-lyases, and other carbon-nitrogen lyases. EC 4.3.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
Proteins obtained from the species SACCHAROMYCES CEREVISIAE. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Structures that are part of or contained in the CELL NUCLEUS.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
The act of ligating UBIQUITINS to PROTEINS to form ubiquitin-protein ligase complexes to label proteins for transport to the PROTEASOME ENDOPEPTIDASE COMPLEX where proteolysis occurs.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.
A family of proteins that play a role in CHROMATIN REMODELING. They are best known for silencing HOX GENES and the regulation of EPIGENETIC PROCESSES.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
The area within the CELL NUCLEUS.
Established cell cultures that have the potential to propagate indefinitely.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
The three-part structure of ribbon-like proteinaceous material that serves to align and join the paired homologous CHROMOSOMES. It is formed during the ZYGOTENE STAGE of the first meiotic division. It is a prerequisite for CROSSING OVER.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
Physiological functions characteristic of plants.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
A zinc-binding domain defined by the sequence Cysteine-X2-Cysteine-X(9-39)-Cysteine-X(l-3)-His-X(2-3)-Cysteine-X2-Cysteine -X(4-48)-Cysteine-X2-Cysteine, where X is any amino acid. The RING finger motif binds two atoms of zinc, with each zinc atom ligated tetrahedrally by either four cysteines or three cysteines and a histidine. The motif also forms into a unitary structure with a central cross-brace region and is found in many proteins that are involved in protein-protein interactions. The acronym RING stands for Really Interesting New Gene.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A family of low molecular weight proteins that bind ACTIN and control actin polymerization. They are found in eukaryotes and are ubiquitously expressed.
The reconstruction of a continuous two-stranded DNA molecule without mismatch from a molecule which contained damaged regions. The major repair mechanisms are excision repair, in which defective regions in one strand are excised and resynthesized using the complementary base pairing information in the intact strand; photoreactivation repair, in which the lethal and mutagenic effects of ultraviolet light are eliminated; and post-replication repair, in which the primary lesions are not repaired, but the gaps in one daughter duplex are filled in by incorporation of portions of the other (undamaged) daughter duplex. Excision repair and post-replication repair are sometimes referred to as "dark repair" because they do not require light.
Injuries to DNA that introduce deviations from its normal, intact structure and which may, if left unrepaired, result in a MUTATION or a block of DNA REPLICATION. These deviations may be caused by physical or chemical agents and occur by natural or unnatural, introduced circumstances. They include the introduction of illegitimate bases during replication or by deamination or other modification of bases; the loss of a base from the DNA backbone leaving an abasic site; single-strand breaks; double strand breaks; and intrastrand (PYRIMIDINE DIMERS) or interstrand crosslinking. Damage can often be repaired (DNA REPAIR). If the damage is extensive, it can induce APOPTOSIS.
A large multisubunit complex that plays an important role in the degradation of most of the cytosolic and nuclear proteins in eukaryotic cells. It contains a 700-kDa catalytic sub-complex and two 700-kDa regulatory sub-complexes. The complex digests ubiquitinated proteins and protein activated via ornithine decarboxylase antizyme.
Cleavage of proteins into smaller peptides or amino acids either by PROTEASES or non-enzymatically (e.g., Hydrolysis). It does not include Protein Processing, Post-Translational.
Proteins that are normally involved in holding cellular growth in check. Deficiencies or abnormalities in these proteins may lead to unregulated cell growth and tumor development.
A genus of ascomycetous fungi of the family Schizosaccharomycetaceae, order Schizosaccharomycetales.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
Canavanine is a nonprotein amino acid, structurally similar to arginine, found in certain plants like alfalfa and jack bean, that functions as an arginine analog antimetabolite, inhibiting argininosuccinate synthetase, thereby disrupting polyamine metabolism and exhibiting anti-proliferative properties.
Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Nuclear antigen with a role in DNA synthesis, DNA repair, and cell cycle progression. PCNA is required for the coordinated synthesis of both leading and lagging strands at the replication fork during DNA replication. PCNA expression correlates with the proliferation activity of several malignant and non-malignant cell types.
The beta subunit of thyroid stimulating hormone, thyrotropin. It is a 112-amino acid glycopolypeptide of about 16 kD. Full biological activity of TSH requires the non-covalently bound heterodimers of an alpha and a beta subunit.
One of the CEPHALOSPORINS that has a broad spectrum of activity against both gram-positive and gram-negative microorganisms.
Proteins obtained from the species Schizosaccharomyces pombe. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
Proteins prepared by recombinant DNA technology.
An increased tendency of the GENOME to acquire MUTATIONS when various processes involved in maintaining and replicating the genome are dysfunctional.
A continuous cell line of high contact-inhibition established from NIH Swiss mouse embryo cultures. The cells are useful for DNA transfection and transformation studies. (From ATCC [Internet]. Virginia: American Type Culture Collection; c2002 [cited 2002 Sept 26]. Available from http://www.atcc.org/)
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
Proteins that bind to the MATRIX ATTACHMENT REGIONS of DNA.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
Nucleocytoplasmic transport molecules that bind to ALPHA KARYOPHERINS in the CYTOSOL and are involved in transport of molecules through the NUCLEAR PORE COMPLEX. Once inside the CELL NUCLEUS beta karyopherins interact with RAN GTP-BINDING PROTEIN and dissociate from alpha karyopherins. Beta karyopherins bound to RAN GTP-BINDING PROTEIN are then re-transported to the cytoplasm where hydrolysis of the GTP of RAN GTP-BINDING PROTEIN causes release of karyopherin beta.
An opening through the NUCLEAR ENVELOPE formed by the nuclear pore complex which transports nuclear proteins or RNA into or out of the CELL NUCLEUS and which, under some conditions, acts as an ion channel.
Macromolecular complexes formed from the association of defined protein subunits.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Members of the peptidase C19 family which regulate signal transduction by removing UBIQUITIN from specific protein substrates via a process known as deubiquitination or deubiquitylation.
The material of CHROMOSOMES. It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a cell.
Proteins produced from GENES that have acquired MUTATIONS.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
Interruptions in the sugar-phosphate backbone of DNA, across both strands adjacently.
The alignment of CHROMOSOMES at homologous sequences.
A member of the ternary complex family of ets-related transcription factors that is regulated by MITOGEN-ACTIVATED PROTEIN KINASES including JNK MITOGEN-ACTIVATED PROTEIN KINASES; MITOGEN-ACTIVATED PROTEIN KINASE 1; MITOGEN-ACTIVATED PROTEIN KINASE 3; and P38 MITOGEN-ACTIVATED PROTEIN KINASES.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Within most types of eukaryotic CELL NUCLEUS, a distinct region, not delimited by a membrane, in which some species of rRNA (RNA, RIBOSOMAL) are synthesized and assembled into ribonucleoprotein subunits of ribosomes. In the nucleolus rRNA is transcribed from a nucleolar organizer, i.e., a group of tandemly repeated chromosomal genes which encode rRNA and which are transcribed by RNA polymerase I. (Singleton & Sainsbury, Dictionary of Microbiology & Molecular Biology, 2d ed)
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Plants that can grow well in soils that have a high SALINITY.
The systematic study of the complete complement of proteins (PROTEOME) of organisms.
Nucleoproteins, which in contrast to HISTONES, are acid insoluble. They are involved in chromosomal functions; e.g. they bind selectively to DNA, stimulate transcription resulting in tissue-specific RNA synthesis and undergo specific changes in response to various hormones or phytomitogens.
The clear constricted portion of the chromosome at which the chromatids are joined and by which the chromosome is attached to the spindle during cell division.
Inherited conditions characterized by the partial loss of ADIPOSE TISSUE, either confined to the extremities with normal or increased fat deposits on the face, neck and trunk (type 1), or confined to the loss of SUBCUTANEOUS FAT from the limbs and trunk (type 2). Type 3 is associated with mutation in the gene encoding PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.
Binary compounds of oxygen containing the anion O(2-). The anion combines with metals to form alkaline oxides and non-metals to form acidic oxides.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.
Proteins that catalyze the unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. In addition DNA helicases are DNA-dependent ATPases that harness the free energy of ATP hydrolysis to translocate DNA strands.
A DNA-binding protein that mediates DNA REPAIR of double strand breaks, and HOMOLOGOUS RECOMBINATION.
A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.
The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
A cell line derived from cultured tumor cells.
The assembly of the QUATERNARY PROTEIN STRUCTURE of multimeric proteins (MULTIPROTEIN COMPLEXES) from their composite PROTEIN SUBUNITS.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Methods for determining interaction between PROTEINS.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
A specificity protein transcription factor that regulates expression of a variety of genes including VASCULAR ENDOTHELIAL GROWTH FACTOR and CYCLIN-DEPENDENT KINASE INHIBITOR P27.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
DNA sequences which are recognized (directly or indirectly) and bound by a DNA-dependent RNA polymerase during the initiation of transcription. Highly conserved sequences within the promoter include the Pribnow box in bacteria and the TATA BOX in eukaryotes.
Immunologically detectable substances found in the CELL NUCLEUS.
The orderly segregation of CHROMOSOMES during MEIOSIS or MITOSIS.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
Inorganic or organic compounds that contain arsenic.
Transport proteins that carry specific substances in the blood or across cell membranes.
Luciferases from RENILLA that oxidizes certain LUMINESCENT AGENTS to cause emission of PHOTONS.
An exchange of DNA between matching or similar sequences.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
A thioester hydrolase which acts on esters formed between thiols such as DITHIOTHREITOL or GLUTATHIONE and the C-terminal glycine residue of UBIQUITIN.
Short, predominantly basic amino acid sequences identified as nuclear import signals for some proteins. These sequences are believed to interact with specific receptors at the NUCLEAR PORE.
The larger of two types of nuclei in ciliate protozoans. It is the transcriptionally active nucleus of the vegetative cells as distinguished from the smaller transcriptionally inert GERMLINE MICRONUCLEUS.
Genes whose expression is easily detectable and therefore used to study promoter activity at many positions in a target genome. In recombinant DNA technology, these genes may be attached to a promoter region of interest.
The complex series of phenomena, occurring between the end of one CELL DIVISION and the end of the next, by which cellular material is duplicated and then divided between two daughter cells. The cell cycle includes INTERPHASE, which includes G0 PHASE; G1 PHASE; S PHASE; and G2 PHASE, and CELL DIVISION PHASE.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)
Structures within the nucleus of fungal cells consisting of or containing DNA, which carry genetic information essential to the cell.
A enzyme complex involved in the remodeling of NUCLEOSOMES. The complex is comprised of at least seven subunits and includes both histone deacetylase and ATPase activities.
A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells.
Interruption or suppression of the expression of a gene at transcriptional or translational levels.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
An AT-hook motif-containing protein (AT-HOOK MOTIFS) that binds to the minor grove of AT-rich regions of DNA. It is a truncated form of HMGA1a protein that is produced by alternative-splicing of the HMGA1 gene. It may function as an architectural chromatin binding protein that is involved in transcriptional regulation.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
DNA TOPOISOMERASES that catalyze ATP-dependent breakage of both strands of DNA, passage of the unbroken strands through the breaks, and rejoining of the broken strands. These enzymes bring about relaxation of the supercoiled DNA and resolution of a knotted circular DNA duplex.
DNA TOPOISOMERASES that catalyze ATP-independent breakage of one of the two strands of DNA, passage of the unbroken strand through the break, and rejoining of the broken strand. DNA Topoisomerases, Type I enzymes reduce the topological stress in the DNA structure by relaxing the superhelical turns and knotted rings in the DNA helix.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
Interruptions in one of the strands of the sugar-phosphate backbone of double-stranded DNA.
Compounds that inhibit the function or proteolytic action of the PROTEASOME.
The membrane system of the CELL NUCLEUS that surrounds the nucleoplasm. It consists of two concentric membranes separated by the perinuclear space. The structures of the envelope where it opens to the cytoplasm are called the nuclear pores (NUCLEAR PORE).
A subclass of repressor proteins that do not directly bind DNA. Instead, co-repressors generally act via their interaction with DNA-BINDING PROTEINS such as a TRANSCRIPTIONAL SILENCING FACTORS or NUCLEAR RECEPTORS.
An electrophoretic technique for assaying the binding of one compound to another. Typically one compound is labeled to follow its mobility during electrophoresis. If the labeled compound is bound by the other compound, then the mobility of the labeled compound through the electrophoretic medium will be retarded.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
Proteins that are coded by immediate-early genes, in the absence of de novo protein synthesis. The term was originally used exclusively for viral regulatory proteins that were synthesized just after viral integration into the host cell. It is also used to describe cellular proteins which are synthesized immediately after the resting cell is stimulated by extracellular signals.
Specific amino acid sequences present in the primary amino acid sequence of proteins which mediate their export from the CELL NUCLEUS. They are rich in hydrophobic residues, such as LEUCINE and ISOLEUCINE.
A family of GTP-binding proteins that were initially identified in YEASTS where they were shown to initiate the process of septation and bud formation. Septins form into hetero-oligomeric complexes that are comprised of several distinct septin subunits. These complexes can act as cytoskeletal elements that play important roles in CYTOKINESIS, cytoskeletal reorganization, BIOLOGICAL TRANSPORT, and membrane dynamics.
Regions of the CHROMATIN or DNA that bind to the NUCLEAR MATRIX. They are found in INTERGENIC DNA, especially flanking the 5' ends of genes or clusters of genes. Many of the regions that have been isolated contain a bipartite sequence motif called the MAR/SAR recognition signature sequence that binds to MATRIX ATTACHMENT REGION BINDING PROTEINS.
The facilitation of biochemical reactions with the aid of naturally occurring catalysts such as ENZYMES.
The first phase of cell nucleus division, in which the CHROMOSOMES become visible, the CELL NUCLEUS starts to lose its identity, the SPINDLE APPARATUS appears, and the CENTRIOLES migrate toward opposite poles.
The portion of chromosome material that remains condensed and is transcriptionally inactive during INTERPHASE.
Enzymes that oxidize certain LUMINESCENT AGENTS to emit light (PHYSICAL LUMINESCENCE). The luciferases from different organisms have evolved differently so have different structures and substrates.
Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.
A human liver tumor cell line used to study a variety of liver-specific metabolic functions.
The artificial induction of GENE SILENCING by the use of RNA INTERFERENCE to reduce the expression of a specific gene. It includes the use of DOUBLE-STRANDED RNA, such as SMALL INTERFERING RNA and RNA containing HAIRPIN LOOP SEQUENCE, and ANTI-SENSE OLIGONUCLEOTIDES.
A large family of structurally-related transcription factors that were originally discovered based upon their close sequence homology to an HMG-box domain found in SEX-DETERMINING REGION Y PROTEIN. Many SOX transcription factors play important roles in regulating CELL DIFFERENTIATION. The numerous members of this family are organized in several subgroups according to structural identities found within the proteins.
The GENETIC RECOMBINATION of the parts of two or more GENES resulting in a gene with different or additional regulatory regions, or a new chimeric gene product. ONCOGENE FUSION includes an ONCOGENE as at least one of the fusion partners and such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS. ARTIFICIAL GENE FUSION is carried out in vitro by RECOMBINANT DNA technology.
A constellation of responses that occur when an organism is exposed to excessive heat. Responses include synthesis of new proteins and regulation of others.
Proteins found in any species of fungus.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
Motifs in DNA- and RNA-binding proteins whose amino acids are folded into a single structural unit around a zinc atom. In the classic zinc finger, one zinc atom is bound to two cysteines and two histidines. In between the cysteines and histidines are 12 residues which form a DNA binding fingertip. By variations in the composition of the sequences in the fingertip and the number and spacing of tandem repeats of the motif, zinc fingers can form a large number of different sequence specific binding sites.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
Repair of DNA DAMAGE by exchange of DNA between matching sequences, usually between the allelic DNA (ALLELES) of sister chromatids.
A nuclear protein that regulates the expression of genes involved in a diverse array of processes related to metabolism and reproduction. The protein contains three nuclear receptor interaction domains and three repressor domains and is closely-related in structure to NUCLEAR RECEPTOR CO-REPRESSOR 2.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.
A signal transducer and activator of transcription that mediates cellular responses to INTERFERONS. Stat1 interacts with P53 TUMOR SUPPRESSOR PROTEIN and regulates expression of GENES involved in growth control and APOPTOSIS.
A group of acylated oligopeptides produced by Actinomycetes that function as protease inhibitors. They have been known to inhibit to varying degrees trypsin, plasmin, KALLIKREINS, papain and the cathepsins.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
An acute myeloid leukemia in which abnormal PROMYELOCYTES predominate. It is frequently associated with DISSEMINATED INTRAVASCULAR COAGULATION.
A family of proteins involved in NUCLEOCYTOPLASMIC TRANSPORT. Karyopherins are heteromeric molecules composed two major types of components, ALPHA KARYOPHERINS and BETA KARYOPHERINS, that function together to transport molecules through the NUCLEAR PORE COMPLEX. Several other proteins such as RAN GTP BINDING PROTEIN and CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN bind to karyopherins and participate in the transport process.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
An antineoplastic agent that inhibits DNA synthesis through the inhibition of ribonucleoside diphosphate reductase.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.

Herpes virus induced proteasome-dependent degradation of the nuclear bodies-associated PML and Sp100 proteins. (1/772)

The PML protein is associated to nuclear bodies (NBs) whose functions are as yet unknown. PML and two other NBs-associated proteins, Sp100 And ISG20 are directly induced by interferons (IFN). PML and Sp100 proteins are covalently linked to SUMO-1, and ubiquitin-like peptide. PML NBs are disorganized in acute promyelocytic leukemia and during several DNA virus infections. In particular, the HSV-1 ICP0 protein is known to delocalize PML from NBs. Thus, NBs could play an important role in oncogenesis, IFN response and viral infections. Here, we show that HSV-1 induced PML protein degradation without altering its mRNA level. This degradation was time- and multiplicity of infection-dependent. Sp100 protein was also degraded, while another SUMO-1 conjugated protein, RanGAP1 and the IFN-induced protein kinase PKR were not. The proteasome inhibitor MG132 abrogated the HSV-1-induced PML and Sp100 degradation and partially restored their NB-localization. HSV-1 induced PML and Sp100 degradation constitutes a new example of viral inactivation of IFN target gene products.  (+info)

Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1. (2/772)

The ubiquitin-like protein SUMO-1 is conjugated to a variety of proteins including Ran GTPase-activating protein 1 (RanGAP1), IkappaBalpha, and PML. SUMO-1-modified proteins display altered subcellular targeting and/or stability. We have purified the SUMO-1-activating enzyme from human cells and shown that it contains two subunits of 38 and 72 kDa. Isolation of cDNAs for each subunit indicates that they are homologous to ubiquitin-activating enzymes and to the Saccharomyces cerevisiae enzymes responsible for conjugation of Smt3p and Rub-1p. In vitro, recombinant SAE1/SAE2 (SUMO-1-activating enzyme) was capable of catalyzing the ATP-dependent formation of a thioester linkage between SUMO-1 and SAE2. The addition of the SUMO-1-conjugating enzyme Ubch9 resulted in efficient transfer of the thioester-linked SUMO-1 from SAE2 to Ubch9. In the presence of SAE1/SAE2, Ubch9, and ATP, SUMO-1 was efficiently conjugated to the protein substrate IkappaBalpha. As SAE1/SAE2, Ubch9, SUMO-1, and IkappaBalpha are all homogeneous, recombinant proteins, it appears that SUMO-1 conjugation of IkappaBalpha in vitro does not require the equivalent of an E3 ubiquitin protein ligase activity.  (+info)

Molecular cloning and characterization of human AOS1 and UBA2, components of the sentrin-activating enzyme complex. (3/772)

Sentrin-1/SUMO-1 is a novel ubiquitin-like protein, which can covalently modify a limited number of cellular proteins. Here we report the identification of the sentrin-activating enzyme complex, which consists of two proteins AOS1 and UBA2. Human AOS1 is homologous to the N-terminal half of E1, whereas human UBA2 is homologous to the C-terminal half of E1. The human UBA2 gene is located on chromosome 19q12. Human UBA2 could form a beta-mercaptoethanol-sensitive conjugate with members of the sentrin family, but not with ubiquitin of NEDD8, in the presence of AOS1. Identification of human UBA2 and AOS1 should allow a more detailed analysis of the enzymology of the activation of ubiquitin-like proteins.  (+info)

Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and Sp100 proteins, correlating with nuclear body disruption. (4/772)

PML nuclear bodies (NBs) are subnuclear structures whose integrity is compromised in certain human diseases, including leukemia and neurodegenerative disorders. Infection by a number of DNA viruses similarly triggers the reorganization of these structures, suggesting an important role for the NBs in the viral infection process. While expression of the adenovirus E4 ORF3 protein leads to only a moderate redistribution of PML to filamentous structures, the herpes simplex virus (HSV) ICP0 protein and the cytomegalovirus (CMV) IE1 protein both induce a complete disruption of the NB structure. Recently, we and others have shown that the NB proteins PML and Sp100 are posttranslationally modified by covalent linkage with the ubiquitin-related SUMO-1 protein and that this modification may promote the assembly of these structures. Here we show that the HSV ICP0 and CMV IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100, whereas the adenovirus E4 ORF3 protein does not affect this process. The potential of ICP0 and IE1 to alter SUMO-1 modification is directly linked to their capacity to disassemble NBs, thus strengthening the role for SUMO-1 conjugation in maintenance of the structural integrity of the NBs. This observation supports a model in which ICP0 and IE1 disrupt the NBs either by preventing the formation or by degrading of the SUMO-1-modified PML and Sp100 protein species. Finally, we show that the IE1 protein itself is a substrate for SUMO-1 modification, thus representing the first viral protein found to undergo this new type of posttranslational modification.  (+info)

The binding interface between an E2 (UBC9) and a ubiquitin homologue (UBL1). (5/772)

Human UBC9 is a member of the E2 (ubiquitin conjugation enzyme) family of proteins. Instead of conjugating to ubiquitin, it conjugates with a ubiquitin homologue UBL1 (also known as SUMO-1, GMP1, SMTP3, PIC1, and sentrin). UBC9 has been shown to be involved in cell cycle regulation, DNA repair, and p53-dependent processes. The binding interfaces of the UBC9 and UBL1 complex have been determined by chemical shift perturbation using nuclear magnetic resonance spectroscopy. The binding site of UBL1 resides on the ubiquitin domain, and the binding site of UBC9 is located on a structurally conserved region of E2. Because the UBC9-UBL1 system shares many similarities with the ubiquitin system in structures and in conjugation with each other and with target proteins, the observed binding interfaces may be conserved in E2-ubiquitin interactions in general.  (+info)

PIC-1/SUMO-1-modified PML-retinoic acid receptor alpha mediates arsenic trioxide-induced apoptosis in acute promyelocytic leukemia. (6/772)

Fusion proteins involving the retinoic acid receptor alpha (RARalpha) and PML or PLZF nuclear protein are the genetic markers of acute promyelocytic leukemia (APL). APLs with PML-RARalpha or PLZF-RARalpha fusion protein differ only in their response to retinoic acid (RA) treatment: the t(15;17) (PML-RARalpha-positive) APL blasts are sensitive to RA in vitro, and patients enter disease remission after RA treatment, while those with t(11;17) (PLZF-RARalpha-positive) APLs do not. Recently it has been shown that complete remission can be achieved upon treatment with arsenic trioxide (As2O3) in PML-RARalpha-positive APL, even when the patient has relapsed and the disease is RA resistant. This appears to be due to apoptosis induced by As2O3 in the APL blasts by poorly defined mechanisms. Here we report that (i) As2O3 induces apoptosis only in cells expressing the PML-RARalpha, not the PLZF-RARalpha, fusion protein; (ii) PML-RARalpha is partially modified by covalent linkage with a PIC-1/SUMO-1-like protein prior to As2O3 treatment, whereas PLZF-RARalpha is not; (iii) As2O3 treatment induces a change in the modification pattern of PML-RARalpha toward highly modified forms; (iv) redistribution of PML nuclear bodies (PML-NBs) upon As2O3 treatment is accompanied by recruitment of PIC-1/SUMO-1 into PML-NBs, probably due to hypermodification of both PML and PML-RARalpha; (v) As2O3-induced apoptosis is independent of the DNA binding activity located in the RARalpha portion of the PML-RARalpha fusion protein; and (vi) the apoptotic process is bcl-2 and caspase 3 independent and is blocked only partially by a global caspase inhibitor. Taken together, these data provide novel insights into the mechanisms involved in As2O3-induced apoptosis in APL and predict that treatment of t(11;17) (PLZF-RARalpha-positive) APLs with As2O3 will not be successful.  (+info)

Ubc9 interacts with the androgen receptor and activates receptor-dependent transcription. (7/772)

Ubc9, a homologue of the class E2 ubiquitin-conjugating enzymes, has recently been shown to catalyze conjugation of a small ubiquitin-like molecule-1 (SUMO-1) to a variety of target proteins. SUMO-1 modifications have been implicated in the targeting of proteins to the nuclear envelope and certain intranuclear structures and in converting proteins resistant to ubiquitin-mediated degradation. In the present work, we find that Ubc9 interacts with the androgen receptor (AR), a member of the steroid receptor family of ligand-activated transcription factors. In transiently transfected COS-1 cells, AR-dependent but not basal transcription is enhanced by the coexpression of Ubc9. The N-terminal half of the AR hinge region containing the C-terminal part of the bipartite nuclear localization signal is essential for the interaction with Ubc9. Deletion of this part of the nuclear localization signal, which does not completely prevent the transfer of AR to the nucleus, abolishes the AR-Ubc9 interaction and attenuates the transcriptional response to cotransfected Ubc9. The C93S substitution of Ubc9, which prevents SUMO-1 conjugation by abrogating the formation of a thiolester bond between SUMO-1 and Ubc9, does not influence the capability of Ubc9 to stimulate AR-dependent transactivation, implying that Ubc9 is able to act as an AR coregulator in a fashion independent of its ability to catalyze SUMO-1 conjugation.  (+info)

A dynamic connection between centromeres and ND10 proteins. (8/772)

ND10, otherwise known as nuclear dots, PML nuclear bodies or PODs, are punctate foci in interphase nuclei that contain several cellular proteins. The functions of ND10 have not been well defined, but they are sensitive to external stimuli such as stress and virus infection, and they are disrupted in malignant promyelocytic leukaemia cells. Herpes simplex virus type 1 regulatory protein Vmw110 induces the proteasome-dependent degradation of ND10 component proteins PML and Sp100, particularly the species of these proteins which are covalently conjugated to the ubiquitin-like protein SUMO-1. We have recently reported that Vmw110 also induces the degradation of centromere protein CENP-C with consequent disruption of centromere structure. These observations led us to examine whether there were hitherto undetected connections between ND10 and centromeres. In this paper we report that hDaxx and HP1 (which have been shown to interact with CENP-C and Sp100, respectively) are present in a proportion of both ND10 and interphase centromeres. Furthermore, the proteasome inhibitor MG132 induced an association between centromeres and ND10 proteins PML and Sp100 in a significant number of cells in the G(2) phase of the cell cycle. These results imply that there is a dynamic, cell cycle regulated connection between centromeres and ND10 proteins which can be stabilised by inhibition of proteasome-mediated proteolysis.  (+info)

Small Ubiquitin-Related Modifier (SUMO) proteins are a type of post-translational modifier, similar to ubiquitin, that can be covalently attached to other proteins in a process called sumoylation. This modification plays a crucial role in regulating various cellular processes such as nuclear transport, transcriptional regulation, DNA repair, and protein stability. Sumoylation is a dynamic and reversible process, which allows for precise control of these functions under different physiological conditions.

The human genome encodes four SUMO paralogs (SUMO1-4), among which SUMO2 and SUMO3 share 97% sequence identity and are often referred to as a single entity, SUMO2/3. The fourth member, SUMO4, is less conserved and has a more restricted expression pattern compared to the other three paralogs.

Similar to ubiquitination, sumoylation involves an enzymatic cascade consisting of an E1 activating enzyme (SAE1/UBA2 heterodimer), an E2 conjugating enzyme (UBC9), and an E3 ligase that facilitates the transfer of SUMO from the E2 to the target protein. The process can be reversed by SUMO-specific proteases, which cleave the isopeptide bond between the modified lysine residue on the target protein and the C-terminal glycine of the SUMO molecule.

Dysregulation of sumoylation has been implicated in various human diseases, including cancer, neurodegenerative disorders, and viral infections. Therefore, understanding the molecular mechanisms governing this post-translational modification is essential for developing novel therapeutic strategies targeting these conditions.

SUMO-1 (Small Ubiquitin-like Modifier 1) protein is a member of the SUMO family of post-translational modifiers, which are involved in the regulation of various cellular processes such as nuclear-cytoplasmic transport, transcriptional regulation, and DNA repair. The SUMO-1 protein is covalently attached to specific lysine residues on target proteins through a process called sumoylation, which can alter the activity, localization, or stability of the modified protein. Sumoylation plays a crucial role in maintaining cellular homeostasis and has been implicated in several human diseases, including cancer and neurodegenerative disorders.

Sumoylation is a post-translational modification process in which a small ubiquitin-like modifier (SUMO) protein is covalently attached to specific lysine residues on target proteins. This conjugation is facilitated by an enzymatic cascade involving E1 activating enzyme, E2 conjugating enzyme, and E3 ligase. Sumoylation can regulate various cellular functions such as protein stability, subcellular localization, activity, and interaction with other proteins. It plays crucial roles in numerous biological processes including DNA replication, repair, transcription, and chromatin remodeling, as well as stress response and regulation of the cell cycle. Dysregulation of sumoylation has been implicated in various human diseases, such as cancer, neurodegenerative disorders, and viral infections.

Protein Inhibitors of Activated STAT (PIAS) are a family of proteins that regulate the activity of signal transducer and activator of transcription (STAT) proteins, which are involved in various cellular processes such as differentiation, proliferation, and apoptosis. PIAS proteins function as E3 ubiquitin ligases and SUMO (small ubiquitin-like modifier) ligases, modifying STAT proteins and other transcription factors by adding SUMO molecules to them. This modification can alter the activity, localization, or stability of the target protein, thereby regulating its function in the cell. PIAS proteins have been shown to play a role in various physiological and pathological processes, including inflammation, cancer, and neurodegenerative diseases. Inhibiting PIAS proteins has emerged as a potential therapeutic strategy for the treatment of certain diseases associated with aberrant STAT activation.

Ubiquitin-conjugating enzymes (UBCs or E2 enzymes) are a family of enzymes that play a crucial role in the ubiquitination process, which is a post-translational modification of proteins. This process involves the covalent attachment of the protein ubiquitin to specific lysine residues on target proteins, ultimately leading to their degradation by the 26S proteasome.

Ubiquitination is a multi-step process that requires the coordinated action of three types of enzymes: E1 (ubiquitin-activating), E2 (ubiquitin-conjugating), and E3 (ubiquitin ligases). Ubiquitin-conjugating enzymes are responsible for transferring ubiquitin from the E1 enzyme to the target protein, which is facilitated by an E3 ubiquitin ligase. The human genome encodes around 40 different UBCs, each with unique substrate specificities and functions in various cellular processes, such as protein degradation, DNA repair, and signal transduction.

Ubiquitination is a highly regulated process that can be reversed by the action of deubiquitinating enzymes (DUBs), which remove ubiquitin molecules from target proteins. Dysregulation of the ubiquitination pathway has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.

Ubiquitin-protein ligases, also known as E3 ubiquitin ligases, are a group of enzymes that play a crucial role in the ubiquitination process. Ubiquitination is a post-translational modification where ubiquitin molecules are attached to specific target proteins, marking them for degradation by the proteasome or for other regulatory functions.

Ubiquitin-protein ligases catalyze the final step in this process by binding to both the ubiquitin protein and the target protein, facilitating the transfer of ubiquitin from an E2 ubiquitin-conjugating enzyme to the target protein. There are several different types of ubiquitin-protein ligases, each with their own specificity for particular target proteins and regulatory functions.

Ubiquitin-protein ligases have been implicated in various cellular processes such as protein degradation, DNA repair, signal transduction, and regulation of the cell cycle. Dysregulation of ubiquitination has been associated with several diseases, including cancer, neurodegenerative disorders, and inflammatory responses. Therefore, understanding the function and regulation of ubiquitin-protein ligases is an important area of research in biology and medicine.

Post-translational protein processing refers to the modifications and changes that proteins undergo after their synthesis on ribosomes, which are complex molecular machines responsible for protein synthesis. These modifications occur through various biochemical processes and play a crucial role in determining the final structure, function, and stability of the protein.

The process begins with the translation of messenger RNA (mRNA) into a linear polypeptide chain, which is then subjected to several post-translational modifications. These modifications can include:

1. Proteolytic cleavage: The removal of specific segments or domains from the polypeptide chain by proteases, resulting in the formation of mature, functional protein subunits.
2. Chemical modifications: Addition or modification of chemical groups to the side chains of amino acids, such as phosphorylation (addition of a phosphate group), glycosylation (addition of sugar moieties), methylation (addition of a methyl group), acetylation (addition of an acetyl group), and ubiquitination (addition of a ubiquitin protein).
3. Disulfide bond formation: The oxidation of specific cysteine residues within the polypeptide chain, leading to the formation of disulfide bonds between them. This process helps stabilize the three-dimensional structure of proteins, particularly in extracellular environments.
4. Folding and assembly: The acquisition of a specific three-dimensional conformation by the polypeptide chain, which is essential for its function. Chaperone proteins assist in this process to ensure proper folding and prevent aggregation.
5. Protein targeting: The directed transport of proteins to their appropriate cellular locations, such as the nucleus, mitochondria, endoplasmic reticulum, or plasma membrane. This is often facilitated by specific signal sequences within the protein that are recognized and bound by transport machinery.

Collectively, these post-translational modifications contribute to the functional diversity of proteins in living organisms, allowing them to perform a wide range of cellular processes, including signaling, catalysis, regulation, and structural support.

Lysine is an essential amino acid, which means that it cannot be synthesized by the human body and must be obtained through the diet. Its chemical formula is (2S)-2,6-diaminohexanoic acid. Lysine is necessary for the growth and maintenance of tissues in the body, and it plays a crucial role in the production of enzymes, hormones, and antibodies. It is also essential for the absorption of calcium and the formation of collagen, which is an important component of bones and connective tissue. Foods that are good sources of lysine include meat, poultry, fish, eggs, and dairy products.

Ligases are a group of enzymes that catalyze the formation of a covalent bond between two molecules, usually involving the joining of two nucleotides in a DNA or RNA strand. They play a crucial role in various biological processes such as DNA replication, repair, and recombination. In DNA ligases, the enzyme seals nicks or breaks in the phosphodiester backbone of the DNA molecule by catalyzing the formation of an ester bond between the 3'-hydroxyl group and the 5'-phosphate group of adjacent nucleotides. This process is essential for maintaining genomic integrity and stability.

Ubiquitin is a small protein that is present in all eukaryotic cells and plays a crucial role in the regulation of various cellular processes, such as protein degradation, DNA repair, and stress response. It is involved in marking proteins for destruction by attaching to them, a process known as ubiquitination. This modification can target proteins for degradation by the proteasome, a large protein complex that breaks down unneeded or damaged proteins in the cell. Ubiquitin also has other functions, such as regulating the localization and activity of certain proteins. The ability of ubiquitin to modify many different proteins and play a role in multiple cellular processes makes it an essential player in maintaining cellular homeostasis.

Cysteine endopeptidases are a type of enzymes that cleave peptide bonds within proteins. They are also known as cysteine proteases or cysteine proteinases. These enzymes contain a catalytic triad consisting of three amino acids: cysteine, histidine, and aspartate. The thiol group (-SH) of the cysteine residue acts as a nucleophile and attacks the carbonyl carbon of the peptide bond, leading to its cleavage.

Cysteine endopeptidases play important roles in various biological processes, including protein degradation, cell signaling, and inflammation. They are involved in many physiological and pathological conditions, such as apoptosis, immune response, and cancer. Some examples of cysteine endopeptidases include cathepsins, caspases, and calpains.

It is important to note that these enzymes require a reducing environment to maintain the reduced state of their active site cysteine residue. Therefore, they are sensitive to oxidizing agents and inhibitors that target the thiol group. Understanding the structure and function of cysteine endopeptidases is crucial for developing therapeutic strategies that target these enzymes in various diseases.

Endopeptidases are a type of enzyme that breaks down proteins by cleaving peptide bonds inside the polypeptide chain. They are also known as proteinases or endoproteinases. These enzymes work within the interior of the protein molecule, cutting it at specific points along its length, as opposed to exopeptidases, which remove individual amino acids from the ends of the protein chain.

Endopeptidases play a crucial role in various biological processes, such as digestion, blood coagulation, and programmed cell death (apoptosis). They are classified based on their catalytic mechanism and the structure of their active site. Some examples of endopeptidase families include serine proteases, cysteine proteases, aspartic proteases, and metalloproteases.

It is important to note that while endopeptidases are essential for normal physiological functions, they can also contribute to disease processes when their activity is unregulated or misdirected. For instance, excessive endopeptidase activity has been implicated in the pathogenesis of neurodegenerative disorders, cancer, and inflammatory conditions.

Ubiquitin-activating enzymes, also known as E1 enzymes, are a class of enzymes that play a crucial role in the ubiquitination pathway. Ubiquitination is a post-translational modification process that targets proteins for degradation or regulates their function by attaching a small protein called ubiquitin to them.

E1 enzymes initiate the ubiquitination process by activating ubiquitin through a two-step reaction. First, they catalyze the adenylation of ubiquitin's carboxyl terminus using ATP as an energy source, forming an adenylated ubiquitin intermediate. Then, the E1 enzyme transfers the activated ubiquitin to a cysteine residue on its own active site, forming a thioester bond between the ubiquitin and the E1 enzyme.

After activation, ubiquitin is transferred from the E1 enzyme to an E2 ubiquitin-conjugating enzyme, which then works with an E3 ubiquitin ligase to transfer ubiquitin to a specific lysine residue on the target protein. The addition of multiple ubiquitin molecules can create a polyubiquitin chain, leading to proteasomal degradation or other functional changes in the targeted protein.

There are two main families of E1 enzymes: UBA1 and UBA6. Dysregulation of ubiquitination pathways has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Therefore, understanding the function and regulation of E1 enzymes is essential for developing potential therapeutic strategies targeting these pathways.

Intranuclear inclusion bodies are abnormal, rounded structures found within the nucleus of a cell. They are composed of aggregated proteins or other cellular components and can be associated with various viral infections and certain genetic disorders. These inclusion bodies can interfere with normal nuclear functions, leading to cell damage and contributing to the pathogenesis of diseases such as cytomegalovirus infection, rabies, and some forms of neurodegenerative disorders like polyglutamine diseases. The presence of intranuclear inclusion bodies is often used in diagnostic pathology to help identify specific underlying conditions.

I'm sorry for any confusion, but "wrestling" is not a medical term. It is an athletic activity or sport that involves two individuals trying to physically manipulate each other into a dominant position or force their opponent to the ground. If you have any medical questions or concerns, I would be happy to try and help answer those for you.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Amino acid motifs are recurring patterns or sequences of amino acids in a protein molecule. These motifs can be identified through various sequence analysis techniques and often have functional or structural significance. They can be as short as two amino acids in length, but typically contain at least three to five residues.

Some common examples of amino acid motifs include:

1. Active site motifs: These are specific sequences of amino acids that form the active site of an enzyme and participate in catalyzing chemical reactions. For example, the catalytic triad in serine proteases consists of three residues (serine, histidine, and aspartate) that work together to hydrolyze peptide bonds.
2. Signal peptide motifs: These are sequences of amino acids that target proteins for secretion or localization to specific organelles within the cell. For example, a typical signal peptide consists of a positively charged n-region, a hydrophobic h-region, and a polar c-region that directs the protein to the endoplasmic reticulum membrane for translocation.
3. Zinc finger motifs: These are structural domains that contain conserved sequences of amino acids that bind zinc ions and play important roles in DNA recognition and regulation of gene expression.
4. Transmembrane motifs: These are sequences of hydrophobic amino acids that span the lipid bilayer of cell membranes and anchor transmembrane proteins in place.
5. Phosphorylation sites: These are specific serine, threonine, or tyrosine residues that can be phosphorylated by protein kinases to regulate protein function.

Understanding amino acid motifs is important for predicting protein structure and function, as well as for identifying potential drug targets in disease-associated proteins.

Nuclear pore complex proteins, also known as nucleoporins, are a group of specialized proteins that make up the nuclear pore complex (NPC), a large protein structure found in the nuclear envelope of eukaryotic cells. The NPC regulates the transport of molecules between the nucleus and the cytoplasm.

Nucleoporins are organized into distinct subcomplexes, which together form the NPC. They contain phenylalanine-glycine (FG) repeats, which are stretches of amino acids rich in phenylalanine and glycine residues. These FG repeats interact with transport factors, which are responsible for carrying molecules through the NPC.

Nucleoporins play a critical role in the regulation of nuclear transport, and mutations in these proteins have been linked to various human diseases, including neurological disorders and cancer.

Carbon-nitrogen (C-N) lyases are a class of enzymes that catalyze the breakdown of a carbon-nitrogen bond, releasing an ammonia molecule and leaving a double bond. These enzymes play important roles in various biological processes, such as the biosynthesis and degradation of amino acids, nucleotides, and other biomolecules.

C-N lyases are classified based on the type of bond they cleave and the cofactors or prosthetic groups they use to catalyze the reaction. Some examples of C-N lyases include:

1. Alanine racemase: This enzyme catalyzes the conversion of L-alanine to D-alanine, which is an important component of bacterial cell walls.
2. Aspartate transcarbamylase: This enzyme catalyzes the transfer of a carbamoyl group from carbamoyl phosphate to aspartate, forming N-carbamoyl aspartate and inorganic phosphate. It is an important enzyme in the biosynthesis of pyrimidines.
3. Diaminopimelate decarboxylase: This enzyme catalyzes the decarboxylation of meso-diaminopimelate to form L-lysine, which is an essential amino acid for humans.
4. Glutamate decarboxylase: This enzyme catalyzes the decarboxylation of glutamate to form Ī³-aminobutyric acid (GABA), a neurotransmitter in the brain.
5. Histidine decarboxylase: This enzyme catalyzes the decarboxylation of histidine to form histamine, which is involved in various physiological processes such as immune response and allergic reactions.

C-N lyases are important targets for drug development, particularly in the treatment of bacterial infections and neurological disorders.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

A two-hybrid system technique is a type of genetic screening method used in molecular biology to identify protein-protein interactions within an organism, most commonly baker's yeast (Saccharomyces cerevisiae) or Escherichia coli. The name "two-hybrid" refers to the fact that two separate proteins are being examined for their ability to interact with each other.

The technique is based on the modular nature of transcription factors, which typically consist of two distinct domains: a DNA-binding domain (DBD) and an activation domain (AD). In a two-hybrid system, one protein of interest is fused to the DBD, while the second protein of interest is fused to the AD. If the two proteins interact, the DBD and AD are brought in close proximity, allowing for transcriptional activation of a reporter gene that is linked to a specific promoter sequence recognized by the DBD.

The main components of a two-hybrid system include:

1. Bait protein (fused to the DNA-binding domain)
2. Prey protein (fused to the activation domain)
3. Reporter gene (transcribed upon interaction between bait and prey proteins)
4. Promoter sequence (recognized by the DBD when brought in proximity due to interaction)

The two-hybrid system technique has several advantages, including:

1. Ability to screen large libraries of potential interacting partners
2. High sensitivity for detecting weak or transient interactions
3. Applicability to various organisms and protein types
4. Potential for high-throughput analysis

However, there are also limitations to the technique, such as false positives (interactions that do not occur in vivo) and false negatives (lack of detection of true interactions). Additionally, the fusion proteins may not always fold or localize correctly, leading to potential artifacts. Despite these limitations, two-hybrid system techniques remain a valuable tool for studying protein-protein interactions and have contributed significantly to our understanding of various cellular processes.

Saccharomyces cerevisiae proteins are the proteins that are produced by the budding yeast, Saccharomyces cerevisiae. This organism is a single-celled eukaryote that has been widely used as a model organism in scientific research for many years due to its relatively simple genetic makeup and its similarity to higher eukaryotic cells.

The genome of Saccharomyces cerevisiae has been fully sequenced, and it is estimated to contain approximately 6,000 genes that encode proteins. These proteins play a wide variety of roles in the cell, including catalyzing metabolic reactions, regulating gene expression, maintaining the structure of the cell, and responding to environmental stimuli.

Many Saccharomyces cerevisiae proteins have human homologs and are involved in similar biological processes, making this organism a valuable tool for studying human disease. For example, many of the proteins involved in DNA replication, repair, and recombination in yeast have human counterparts that are associated with cancer and other diseases. By studying these proteins in yeast, researchers can gain insights into their function and regulation in humans, which may lead to new treatments for disease.

The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules bound to hist proteins, forming chromosomes. The nuclear membrane, also known as the nuclear envelope, consists of two lipid bilayers perforated by nuclear pores that regulate the transport of molecules between the nucleus and the cytoplasm.

The cell nucleus has several structures with essential functions:

1. Chromosomes: These are thread-like structures made up of DNA, hist proteins, and RNA. They carry genetic information in the form of genes and are responsible for inheritance.
2. Nucleolus: A prominent structure within the nucleus, the nucleolus is the site of ribosome biogenesis. It assembles ribosomal subunits, which are then transported to the cytoplasm for protein synthesis.
3. Nuclear matrix/nuclear lamina: A network of proteins that provides structural support and anchorage for chromosomes, the nucleolus, and other nuclear components. It is located directly inside the inner nuclear membrane.
4. Nuclear pores: These are large protein complexes embedded in the nuclear membrane that regulate the exchange of molecules between the nucleus and cytoplasm. They allow the passage of ions, small molecules, and proteins while preventing the uncontrolled release of genetic material.
5. Heterochromatin and euchromatin: These are different forms of chromatin (chromosomal material) with distinct functions. Heterochromatin is highly condensed and transcriptionally inactive, whereas euchromatin is less condensed and more accessible for gene transcription.

Together, these structures within the cell nucleus play crucial roles in maintaining genome stability, regulating gene expression, and ensuring proper cell function.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

HeLa cells are a type of immortalized cell line used in scientific research. They are derived from a cancer that developed in the cervical tissue of Henrietta Lacks, an African-American woman, in 1951. After her death, cells taken from her tumor were found to be capable of continuous division and growth in a laboratory setting, making them an invaluable resource for medical research.

HeLa cells have been used in a wide range of scientific studies, including research on cancer, viruses, genetics, and drug development. They were the first human cell line to be successfully cloned and are able to grow rapidly in culture, doubling their population every 20-24 hours. This has made them an essential tool for many areas of biomedical research.

It is important to note that while HeLa cells have been instrumental in numerous scientific breakthroughs, the story of their origin raises ethical questions about informed consent and the use of human tissue in research.

Nuclear proteins are a category of proteins that are primarily found in the nucleus of a eukaryotic cell. They play crucial roles in various nuclear functions, such as DNA replication, transcription, repair, and RNA processing. This group includes structural proteins like lamins, which form the nuclear lamina, and regulatory proteins, such as histones and transcription factors, that are involved in gene expression. Nuclear localization signals (NLS) often help target these proteins to the nucleus by interacting with importin proteins during active transport across the nuclear membrane.

Ubiquitination is a post-translational modification process in which a ubiquitin protein is covalently attached to a target protein. This process plays a crucial role in regulating various cellular functions, including protein degradation, DNA repair, and signal transduction. The addition of ubiquitin can lead to different outcomes depending on the number and location of ubiquitin molecules attached to the target protein. Monoubiquitination (the attachment of a single ubiquitin molecule) or multiubiquitination (the attachment of multiple ubiquitin molecules) can mark proteins for degradation by the 26S proteasome, while specific types of ubiquitination (e.g., K63-linked polyubiquitination) can serve as a signal for nonproteolytic functions such as endocytosis, autophagy, or DNA repair. Ubiquitination is a highly regulated process that involves the coordinated action of three enzymes: E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase. Dysregulation of ubiquitination has been implicated in various diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.

"Saccharomyces cerevisiae" is not typically considered a medical term, but it is a scientific name used in the field of microbiology. It refers to a species of yeast that is commonly used in various industrial processes, such as baking and brewing. It's also widely used in scientific research due to its genetic tractability and eukaryotic cellular organization.

However, it does have some relevance to medical fields like medicine and nutrition. For example, certain strains of S. cerevisiae are used as probiotics, which can provide health benefits when consumed. They may help support gut health, enhance the immune system, and even assist in the digestion of certain nutrients.

In summary, "Saccharomyces cerevisiae" is a species of yeast with various industrial and potential medical applications.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

Anacardic acids are a type of organic compounds that are found in the sap, bark, and fruits of the Anacardium occidentale tree, also known as the cashew tree. These compounds are primarily phenolic lipids, which means they have both alcohol and acid components. They are known for their anti-inflammatory, antioxidant, and antimicrobial properties.

Anacardic acids are of interest in medical research due to their potential health benefits. Some studies suggest that they may help to prevent or treat conditions such as cancer, cardiovascular disease, and diabetes. However, more research is needed to confirm these effects and to determine the optimal doses and methods for using anacardic acids as therapeutic agents.

It's worth noting that some people may experience allergic reactions to anacardic acids or other compounds found in cashew nuts or other parts of the cashew tree. These reactions can range from mild skin irritation to severe anaphylaxis, so it's important to use caution when handling or consuming these substances.

Polycomb-group proteins (PcG proteins) are a set of conserved epigenetic regulators that play crucial roles in the development and maintenance of multicellular organisms. They were initially identified in Drosophila melanogaster as factors required for maintaining the repressed state of homeotic genes, which are important for proper body segment identity and pattern formation.

PcG proteins function as part of large multi-protein complexes, called Polycomb Repressive Complexes (PRCs), that can be divided into two main types: PRC1 and PRC2. These complexes mediate the trimethylation of histone H3 lysine 27 (H3K27me3), a chromatin modification associated with transcriptionally repressed genes.

PRC2, which contains the core proteins EZH1 or EZH2, SUZ12, and EED, is responsible for depositing H3K27me3 marks. PRC1, on the other hand, recognizes and binds to these H3K27me3 marks through its chromodomain-containing subunit CBX. PRC1 then ubiquitinates histone H2A at lysine 119 (H2AK119ub), further reinforcing the repressed state of target genes.

PcG proteins are essential for normal development, as they help maintain cell fate decisions and prevent the inappropriate expression of genes that could lead to tumorigenesis or other developmental abnormalities. Dysregulation of PcG protein function has been implicated in various human cancers, making them attractive targets for therapeutic intervention.

Repressor proteins are a type of regulatory protein in molecular biology that suppress the transcription of specific genes into messenger RNA (mRNA) by binding to DNA. They function as part of gene regulation processes, often working in conjunction with an operator region and a promoter region within the DNA molecule. Repressor proteins can be activated or deactivated by various signals, allowing for precise control over gene expression in response to changing cellular conditions.

There are two main types of repressor proteins:

1. DNA-binding repressors: These directly bind to specific DNA sequences (operator regions) near the target gene and prevent RNA polymerase from transcribing the gene into mRNA.
2. Allosteric repressors: These bind to effector molecules, which then cause a conformational change in the repressor protein, enabling it to bind to DNA and inhibit transcription.

Repressor proteins play crucial roles in various biological processes, such as development, metabolism, and stress response, by controlling gene expression patterns in cells.

HEK293 cells, also known as human embryonic kidney 293 cells, are a line of cells used in scientific research. They were originally derived from human embryonic kidney cells and have been adapted to grow in a lab setting. HEK293 cells are widely used in molecular biology and biochemistry because they can be easily transfected (a process by which DNA is introduced into cells) and highly express foreign genes. As a result, they are often used to produce proteins for structural and functional studies. It's important to note that while HEK293 cells are derived from human tissue, they have been grown in the lab for many generations and do not retain the characteristics of the original embryonic kidney cells.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

Protein interaction domains and motifs refer to specific regions or sequences within proteins that are involved in mediating interactions between two or more proteins. These elements can be classified into two main categories: domains and motifs.

Domains are structurally conserved regions of a protein that can fold independently and perform specific functions, such as binding to other molecules like DNA, RNA, or other proteins. They typically range from 25 to 500 amino acids in length and can be found in multiple copies within a single protein or shared among different proteins.

Motifs, on the other hand, are shorter sequences of 3-10 amino acids that mediate more localized interactions with other molecules. Unlike domains, motifs may not have well-defined structures and can be found in various contexts within a protein.

Together, these protein interaction domains and motifs play crucial roles in many biological processes, including signal transduction, gene regulation, enzyme function, and protein complex formation. Understanding the specificity and dynamics of these interactions is essential for elucidating cellular functions and developing therapeutic strategies.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

COS cells are a type of cell line that are commonly used in molecular biology and genetic research. The name "COS" is an acronym for "CV-1 in Origin," as these cells were originally derived from the African green monkey kidney cell line CV-1. COS cells have been modified through genetic engineering to express high levels of a protein called SV40 large T antigen, which allows them to efficiently take up and replicate exogenous DNA.

There are several different types of COS cells that are commonly used in research, including COS-1, COS-3, and COS-7 cells. These cells are widely used for the production of recombinant proteins, as well as for studies of gene expression, protein localization, and signal transduction.

It is important to note that while COS cells have been a valuable tool in scientific research, they are not without their limitations. For example, because they are derived from monkey kidney cells, there may be differences in the way that human genes are expressed or regulated in these cells compared to human cells. Additionally, because COS cells express SV40 large T antigen, they may have altered cell cycle regulation and other phenotypic changes that could affect experimental results. Therefore, it is important to carefully consider the choice of cell line when designing experiments and interpreting results.

The cell nucleus is a membrane-bound organelle found in the eukaryotic cells (cells with a true nucleus). It contains most of the cell's genetic material, organized as DNA molecules in complex with proteins, RNA molecules, and histones to form chromosomes.

The primary function of the cell nucleus is to regulate and control the activities of the cell, including growth, metabolism, protein synthesis, and reproduction. It also plays a crucial role in the process of mitosis (cell division) by separating and protecting the genetic material during this process. The nuclear membrane, or nuclear envelope, surrounding the nucleus is composed of two lipid bilayers with numerous pores that allow for the selective transport of molecules between the nucleoplasm (nucleus interior) and the cytoplasm (cell exterior).

The cell nucleus is a vital structure in eukaryotic cells, and its dysfunction can lead to various diseases, including cancer and genetic disorders.

The intranuclear space, also known as the nucleoplasm or karyolymph, refers to the internal environment of a eukaryotic cell's nucleus. It is the fluid-filled space inside the nuclear membrane where the genetic material, chromatin, and various nuclear organelles such as the nucleolus are suspended. The intranuclear space is involved in numerous essential cellular processes, including DNA replication, transcription, and repair.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Immunoprecipitation (IP) is a research technique used in molecular biology and immunology to isolate specific antigens or antibodies from a mixture. It involves the use of an antibody that recognizes and binds to a specific antigen, which is then precipitated out of solution using various methods, such as centrifugation or chemical cross-linking.

In this technique, an antibody is first incubated with a sample containing the antigen of interest. The antibody specifically binds to the antigen, forming an immune complex. This complex can then be captured by adding protein A or G agarose beads, which bind to the constant region of the antibody. The beads are then washed to remove any unbound proteins, leaving behind the precipitated antigen-antibody complex.

Immunoprecipitation is a powerful tool for studying protein-protein interactions, post-translational modifications, and signal transduction pathways. It can also be used to detect and quantify specific proteins in biological samples, such as cells or tissues, and to identify potential biomarkers of disease.

Substrate specificity in the context of medical biochemistry and enzymology refers to the ability of an enzyme to selectively bind and catalyze a chemical reaction with a particular substrate (or a group of similar substrates) while discriminating against other molecules that are not substrates. This specificity arises from the three-dimensional structure of the enzyme, which has evolved to match the shape, charge distribution, and functional groups of its physiological substrate(s).

Substrate specificity is a fundamental property of enzymes that enables them to carry out highly selective chemical transformations in the complex cellular environment. The active site of an enzyme, where the catalysis takes place, has a unique conformation that complements the shape and charge distribution of its substrate(s). This ensures efficient recognition, binding, and conversion of the substrate into the desired product while minimizing unwanted side reactions with other molecules.

Substrate specificity can be categorized as:

1. Absolute specificity: An enzyme that can only act on a single substrate or a very narrow group of structurally related substrates, showing no activity towards any other molecule.
2. Group specificity: An enzyme that prefers to act on a particular functional group or class of compounds but can still accommodate minor structural variations within the substrate.
3. Broad or promiscuous specificity: An enzyme that can act on a wide range of structurally diverse substrates, albeit with varying catalytic efficiencies.

Understanding substrate specificity is crucial for elucidating enzymatic mechanisms, designing drugs that target specific enzymes or pathways, and developing biotechnological applications that rely on the controlled manipulation of enzyme activities.

'Cercopithecus aethiops' is the scientific name for the monkey species more commonly known as the green monkey. It belongs to the family Cercopithecidae and is native to western Africa. The green monkey is omnivorous, with a diet that includes fruits, nuts, seeds, insects, and small vertebrates. They are known for their distinctive greenish-brown fur and long tail. Green monkeys are also important animal models in biomedical research due to their susceptibility to certain diseases, such as SIV (simian immunodeficiency virus), which is closely related to HIV.

The synaptonemal complex is a protein structure that forms between two homologous chromosomes during meiosis, the type of cell division that leads to the production of gametes (sex cells). The synaptonemal complex consists of two lateral elements, which are associated with each of the homologous chromosomes, and a central element that runs parallel to the length of the complex and connects the two lateral elements.

The synaptonemal complex plays a crucial role in the process of genetic recombination, which occurs during meiosis. Genetic recombination is the exchange of genetic material between two homologous chromosomes that results in new combinations of genes on the chromosomes. This process helps to increase genetic diversity and is essential for the proper segregation of chromosomes during meiosis.

The synaptonemal complex also helps to ensure that the correct number of chromosomes are distributed to each gamete by holding the homologous chromosomes together until they can be properly aligned and separated during meiosis. Mutations in genes involved in the formation and maintenance of the synaptonemal complex can lead to fertility problems, developmental abnormalities, and other genetic disorders.

Genetic transcription is the process by which the information in a strand of DNA is used to create a complementary RNA molecule. This process is the first step in gene expression, where the genetic code in DNA is converted into a form that can be used to produce proteins or functional RNAs.

During transcription, an enzyme called RNA polymerase binds to the DNA template strand and reads the sequence of nucleotide bases. As it moves along the template, it adds complementary RNA nucleotides to the growing RNA chain, creating a single-stranded RNA molecule that is complementary to the DNA template strand. Once transcription is complete, the RNA molecule may undergo further processing before it can be translated into protein or perform its functional role in the cell.

Transcription can be either "constitutive" or "regulated." Constitutive transcription occurs at a relatively constant rate and produces essential proteins that are required for basic cellular functions. Regulated transcription, on the other hand, is subject to control by various intracellular and extracellular signals, allowing cells to respond to changing environmental conditions or developmental cues.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Protein transport, in the context of cellular biology, refers to the process by which proteins are actively moved from one location to another within or between cells. This is a crucial mechanism for maintaining proper cell function and regulation.

Intracellular protein transport involves the movement of proteins within a single cell. Proteins can be transported across membranes (such as the nuclear envelope, endoplasmic reticulum, Golgi apparatus, or plasma membrane) via specialized transport systems like vesicles and transport channels.

Intercellular protein transport refers to the movement of proteins from one cell to another, often facilitated by exocytosis (release of proteins in vesicles) and endocytosis (uptake of extracellular substances via membrane-bound vesicles). This is essential for communication between cells, immune response, and other physiological processes.

It's important to note that any disruption in protein transport can lead to various diseases, including neurological disorders, cancer, and metabolic conditions.

I'm sorry for any confusion, but "Active Transport, Cell Nucleus" is not a widely recognized or established medical term. Active transport typically refers to the energy-dependent process by which cells move molecules across their membranes against their concentration gradient. This process is facilitated by transport proteins and requires ATP as an energy source. However, this process primarily occurs in the cell membrane and not in the cell nucleus.

The cell nucleus, on the other hand, contains genetic material (DNA) and is responsible for controlling various cellular activities such as gene expression, replication, and repair. While there are transport processes that occur within the nucleus, they do not typically involve active transport in the same way that it occurs at the cell membrane.

Therefore, a medical definition of "Active Transport, Cell Nucleus" would not be applicable or informative in this context.

GTPase-activating proteins (GAPs) are a group of regulatory proteins that play a crucial role in the regulation of intracellular signaling pathways, particularly those involving GTP-binding proteins. GTPases are enzymes that can bind and hydrolyze guanosine triphosphate (GTP) to guanosine diphosphate (GDP). This biochemical reaction is essential for the regulation of various cellular processes, such as signal transduction, vesicle trafficking, and cytoskeleton organization.

GAPs function as negative regulators of GTPases by accelerating the rate of GTP hydrolysis, thereby promoting the inactive GDP-bound state of the GTPase. By doing so, GAPs help terminate GTPase-mediated signaling events and ensure proper control of downstream cellular responses.

There are various families of GAPs, each with specificity towards particular GTPases. Some well-known GAP families include:

1. p50/RhoGAP: Regulates Rho GTPases involved in cytoskeleton organization and cell migration.
2. GIT (G protein-coupled receptor kinase interactor 1) family: Regulates Arf GTPases involved in vesicle trafficking and actin remodeling.
3. IQGAPs (IQ motif-containing GTPase-activating proteins): Regulate Rac and Cdc42 GTPases, which are involved in cell adhesion, migration, and cytoskeleton organization.

In summary, GTPase-activating proteins (GAPs) are regulatory proteins that accelerate the GTP hydrolysis of GTPases, thereby acting as negative regulators of various intracellular signaling pathways and ensuring proper control of downstream cellular responses.

DNA-binding proteins are a type of protein that have the ability to bind to DNA (deoxyribonucleic acid), the genetic material of organisms. These proteins play crucial roles in various biological processes, such as regulation of gene expression, DNA replication, repair and recombination.

The binding of DNA-binding proteins to specific DNA sequences is mediated by non-covalent interactions, including electrostatic, hydrogen bonding, and van der Waals forces. The specificity of binding is determined by the recognition of particular nucleotide sequences or structural features of the DNA molecule.

DNA-binding proteins can be classified into several categories based on their structure and function, such as transcription factors, histones, and restriction enzymes. Transcription factors are a major class of DNA-binding proteins that regulate gene expression by binding to specific DNA sequences in the promoter region of genes and recruiting other proteins to modulate transcription. Histones are DNA-binding proteins that package DNA into nucleosomes, the basic unit of chromatin structure. Restriction enzymes are DNA-binding proteins that recognize and cleave specific DNA sequences, and are widely used in molecular biology research and biotechnology applications.

Molecular chaperones are a group of proteins that assist in the proper folding and assembly of other protein molecules, helping them achieve their native conformation. They play a crucial role in preventing protein misfolding and aggregation, which can lead to the formation of toxic species associated with various neurodegenerative diseases. Molecular chaperones are also involved in protein transport across membranes, degradation of misfolded proteins, and protection of cells under stress conditions. Their function is generally non-catalytic and ATP-dependent, and they often interact with their client proteins in a transient manner.

I'm sorry for any confusion, but "Plant Physiological Processes" is not a standard medical term. Instead, it falls under the domain of plant science or botany.

In a broad sense, plant physiological processes refer to the functions and mechanisms that occur within plants at the cellular and molecular levels, which enable them to grow, develop, reproduce, and respond to their environment. These processes include photosynthesis, respiration, nutrient uptake and translocation, hormone signaling, water relations, and various other biochemical reactions.

If you're looking for a term related to medical definitions, please provide more context or clarify your request, and I would be happy to help.

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Protein isoforms are different forms or variants of a protein that are produced from a single gene through the process of alternative splicing, where different exons (or parts of exons) are included in the mature mRNA molecule. This results in the production of multiple, slightly different proteins that share a common core structure but have distinct sequences and functions. Protein isoforms can also arise from genetic variations such as single nucleotide polymorphisms or mutations that alter the protein-coding sequence of a gene. These differences in protein sequence can affect the stability, localization, activity, or interaction partners of the protein isoform, leading to functional diversity and specialization within cells and organisms.

Ring finger domains (RFIDs) are a type of protein domain that contain a characteristic cysteine-rich motif. They were initially identified in the RAS-associated proteins called Ras GTPase-activating proteins (GAPs), where they are involved in mediating protein-protein interactions.

The name "ring finger" comes from the fact that these domains contain a series of cysteine and histidine residues that coordinate a central zinc ion, forming a structural ring. This ring is thought to play a role in stabilizing the overall structure of the domain and facilitating its interactions with other proteins.

RFIDs are found in a wide variety of proteins, including transcription factors, chromatin modifiers, and signaling molecules. They have been implicated in a range of cellular processes, including transcriptional regulation, DNA repair, and signal transduction. Mutations in RFID-containing proteins have been linked to various human diseases, including cancer and neurological disorders.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-Ī±) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-Ī±), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-Ī±, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to Ī±4Ī²1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-Ī±, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-Ī±, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-Ī±, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

Profilins are a type of protein that play a role in the regulation of actin filaments, which are important components of the cytoskeleton in cells. They bind to both actin and to small G-proteins called profilin-binding proteins (PBPs), and help to control the assembly and disassembly of actin filaments. Profilins have been found to be involved in various cellular processes, including cell motility, cytokinesis, and intracellular transport. They also play a role in the immune response by regulating the production of reactive oxygen species (ROS) and the release of histamine from mast cells. Mutations in profilin genes have been associated with certain diseases, such as neurodegenerative disorders and cancer.

DNA repair is the process by which cells identify and correct damage to the DNA molecules that encode their genome. DNA can be damaged by a variety of internal and external factors, such as radiation, chemicals, and metabolic byproducts. If left unrepaired, this damage can lead to mutations, which may in turn lead to cancer and other diseases.

There are several different mechanisms for repairing DNA damage, including:

1. Base excision repair (BER): This process repairs damage to a single base in the DNA molecule. An enzyme called a glycosylase removes the damaged base, leaving a gap that is then filled in by other enzymes.
2. Nucleotide excision repair (NER): This process repairs more severe damage, such as bulky adducts or crosslinks between the two strands of the DNA molecule. An enzyme cuts out a section of the damaged DNA, and the gap is then filled in by other enzymes.
3. Mismatch repair (MMR): This process repairs errors that occur during DNA replication, such as mismatched bases or small insertions or deletions. Specialized enzymes recognize the error and remove a section of the newly synthesized strand, which is then replaced by new nucleotides.
4. Double-strand break repair (DSBR): This process repairs breaks in both strands of the DNA molecule. There are two main pathways for DSBR: non-homologous end joining (NHEJ) and homologous recombination (HR). NHEJ directly rejoins the broken ends, while HR uses a template from a sister chromatid to repair the break.

Overall, DNA repair is a crucial process that helps maintain genome stability and prevent the development of diseases caused by genetic mutations.

DNA damage refers to any alteration in the structure or composition of deoxyribonucleic acid (DNA), which is the genetic material present in cells. DNA damage can result from various internal and external factors, including environmental exposures such as ultraviolet radiation, tobacco smoke, and certain chemicals, as well as normal cellular processes such as replication and oxidative metabolism.

Examples of DNA damage include base modifications, base deletions or insertions, single-strand breaks, double-strand breaks, and crosslinks between the two strands of the DNA helix. These types of damage can lead to mutations, genomic instability, and chromosomal aberrations, which can contribute to the development of diseases such as cancer, neurodegenerative disorders, and aging-related conditions.

The body has several mechanisms for repairing DNA damage, including base excision repair, nucleotide excision repair, mismatch repair, and double-strand break repair. However, if the damage is too extensive or the repair mechanisms are impaired, the cell may undergo apoptosis (programmed cell death) to prevent the propagation of potentially harmful mutations.

The proteasome endopeptidase complex is a large protein complex found in the cells of eukaryotic organisms, as well as in archaea and some bacteria. It plays a crucial role in the degradation of damaged or unneeded proteins through a process called proteolysis. The proteasome complex contains multiple subunits, including both regulatory and catalytic particles.

The catalytic core of the proteasome is composed of four stacked rings, each containing seven subunits, forming a structure known as the 20S core particle. Three of these rings are made up of beta-subunits that contain the proteolytic active sites, while the fourth ring consists of alpha-subunits that control access to the interior of the complex.

The regulatory particles, called 19S or 11S regulators, cap the ends of the 20S core particle and are responsible for recognizing, unfolding, and translocating targeted proteins into the catalytic chamber. The proteasome endopeptidase complex can cleave peptide bonds in various ways, including hydrolysis of ubiquitinated proteins, which is an essential mechanism for maintaining protein quality control and regulating numerous cellular processes, such as cell cycle progression, signal transduction, and stress response.

In summary, the proteasome endopeptidase complex is a crucial intracellular machinery responsible for targeted protein degradation through proteolysis, contributing to various essential regulatory functions in cells.

Proteolysis is the biological process of breaking down proteins into smaller polypeptides or individual amino acids by the action of enzymes called proteases. This process is essential for various physiological functions, including digestion, protein catabolism, cell signaling, and regulation of numerous biological activities. Dysregulation of proteolysis can contribute to several pathological conditions, such as cancer, neurodegenerative diseases, and inflammatory disorders.

Tumor suppressor proteins are a type of regulatory protein that helps control the cell cycle and prevent cells from dividing and growing in an uncontrolled manner. They work to inhibit tumor growth by preventing the formation of tumors or slowing down their progression. These proteins can repair damaged DNA, regulate gene expression, and initiate programmed cell death (apoptosis) if the damage is too severe for repair.

Mutations in tumor suppressor genes, which provide the code for these proteins, can lead to a decrease or loss of function in the resulting protein. This can result in uncontrolled cell growth and division, leading to the formation of tumors and cancer. Examples of tumor suppressor proteins include p53, Rb (retinoblastoma), and BRCA1/2.

I apologize for any confusion, but "Schizosaccharomyces" is not a medical term. It is a genus name in the field of microbiology and genetics, referring to a group of budding, tear-shaped yeasts that are widely used as model organisms in scientific research. The most well-known species within this genus is Schizosaccharomyces pombe, which has been extensively studied for its cell cycle regulation, DNA repair mechanisms, and other fundamental biological processes.

If you have any questions related to medical terminology or health-related topics, I would be happy to help.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Arabidopsis proteins refer to the proteins that are encoded by the genes in the Arabidopsis thaliana plant, which is a model organism commonly used in plant biology research. This small flowering plant has a compact genome and a short life cycle, making it an ideal subject for studying various biological processes in plants.

Arabidopsis proteins play crucial roles in many cellular functions, such as metabolism, signaling, regulation of gene expression, response to environmental stresses, and developmental processes. Research on Arabidopsis proteins has contributed significantly to our understanding of plant biology and has provided valuable insights into the molecular mechanisms underlying various agronomic traits.

Some examples of Arabidopsis proteins include transcription factors, kinases, phosphatases, receptors, enzymes, and structural proteins. These proteins can be studied using a variety of techniques, such as biochemical assays, protein-protein interaction studies, and genetic approaches, to understand their functions and regulatory mechanisms in plants.

Canavanine is an amino acid that is found in some plants, particularly in the almonds and seeds of certain legumes. It is structurally similar to the amino acid arginine but is toxic to many organisms, including humans. Canavanine can interfere with the function of enzymes involved in the synthesis of proteins, nucleic acids, and other important molecules, leading to a variety of adverse health effects.

In medical terms, exposure to canavanine can result in symptoms such as vomiting, diarrhea, weakness, and seizures. Prolonged or high-dose exposure may also lead to more serious complications, including liver and kidney damage. However, it is important to note that canavanine poisoning is relatively rare in humans, as the toxic effects of this compound are generally only seen at high levels of exposure.

If you suspect that you or someone else has been exposed to canavanine and is experiencing symptoms, it is important to seek medical attention promptly. A healthcare professional can evaluate the situation and provide appropriate treatment if necessary.

Histone deacetylases (HDACs) are a group of enzymes that play a crucial role in the regulation of gene expression. They work by removing acetyl groups from histone proteins, which are the structural components around which DNA is wound to form chromatin, the material that makes up chromosomes.

Histone acetylation is a modification that generally results in an "open" chromatin structure, allowing for the transcription of genes into proteins. When HDACs remove these acetyl groups, the chromatin becomes more compact and gene expression is reduced or silenced.

HDACs are involved in various cellular processes, including development, differentiation, and survival. Dysregulation of HDAC activity has been implicated in several diseases, such as cancer, neurodegenerative disorders, and cardiovascular diseases. As a result, HDAC inhibitors have emerged as promising therapeutic agents for these conditions.

A catalytic domain is a portion or region within a protein that contains the active site, where the chemical reactions necessary for the protein's function are carried out. This domain is responsible for the catalysis of biological reactions, hence the name "catalytic domain." The catalytic domain is often composed of specific amino acid residues that come together to form the active site, creating a unique three-dimensional structure that enables the protein to perform its specific function.

In enzymes, for example, the catalytic domain contains the residues that bind and convert substrates into products through chemical reactions. In receptors, the catalytic domain may be involved in signal transduction or other regulatory functions. Understanding the structure and function of catalytic domains is crucial to understanding the mechanisms of protein function and can provide valuable insights for drug design and therapeutic interventions.

Proliferating Cell Nuclear Antigen (PCNA) is a protein that plays an essential role in the process of DNA replication and repair in eukaryotic cells. It functions as a cofactor for DNA polymerase delta, enhancing its activity during DNA synthesis. PCNA forms a sliding clamp around DNA, allowing it to move along the template and coordinate the actions of various enzymes involved in DNA metabolism.

PCNA is often used as a marker for cell proliferation because its levels increase in cells that are actively dividing or have been stimulated to enter the cell cycle. Immunostaining techniques can be used to detect PCNA and determine the proliferative status of tissues or cultures. In this context, 'proliferating' refers to the rapid multiplication of cells through cell division.

Thyrotropin, also known as thyroid-stimulating hormone (TSH), is a hormone produced and released by the anterior pituitary gland. It plays a crucial role in regulating the function of the thyroid gland by stimulating the production and release of thyroid hormones, triiodothyronine (T3) and thyroxine (T4).

The TSH molecule is composed of two subunits: alpha and beta. The alpha subunit is common to several pituitary hormones, including TSH, follicle-stimulating hormone (FSH), luteinizing hormone (LH), and human chorionic gonadotropin (hCG). In contrast, the beta subunit is unique to each hormone, determining its specific biological activity.

Therefore, 'Thyrotropin, beta Subunit' refers to the distinct portion of the TSH molecule that confers its thyroid-stimulating properties and allows it to be identified and measured separately from other pituitary hormones sharing the common alpha subunit. Beta-subunit assays are sometimes used in clinical settings to evaluate thyroid function, as they can provide information about TSH levels independent of the common alpha subunit.

Cefotiam is a type of antibiotic known as a cephalosporin, which is used to treat various bacterial infections. It works by interfering with the bacteria's ability to form a cell wall, leading to bacterial cell death. Cefotiam has a broad spectrum of activity and is effective against many gram-positive and gram-negative bacteria.

Here is the medical definition of 'Cefotiam':

Cefotiam is a semisynthetic, broad-spectrum, beta-lactam antibiotic belonging to the cephalosporin class. It has activity against both gram-positive and gram-negative bacteria, including many strains that are resistant to other antibiotics. Cefotiam inhibits bacterial cell wall synthesis by binding to penicillin-binding proteins (PBPs), leading to bacterial cell death.

Cefotiam is available in various formulations, including intravenous (IV) and intramuscular (IM) injections, for the treatment of a wide range of infections, such as:

* Lower respiratory tract infections (e.g., pneumonia, bronchitis)
* Urinary tract infections (e.g., pyelonephritis, cystitis)
* Skin and soft tissue infections (e.g., cellulitis, wound infections)
* Bone and joint infections (e.g., osteomyelitis, septic arthritis)
* Intra-abdominal infections (e.g., peritonitis, appendicitis)
* Septicemia (bloodstream infections)

Cefotiam is generally well tolerated, but like other antibiotics, it can cause side effects, including gastrointestinal symptoms (e.g., nausea, vomiting, diarrhea), skin rashes, and allergic reactions. In rare cases, cefotiam may cause serious adverse effects, such as seizures, interstitial nephritis, or hemorrhagicystitis. It should be used with caution in patients with a history of allergy to beta-lactam antibiotics, impaired renal function, or a history of seizure disorders.

It is essential to complete the full course of treatment as prescribed by a healthcare professional, even if symptoms improve, to ensure that the infection is entirely eradicated and to reduce the risk of developing antibiotic resistance.

I'm sorry for any confusion, but "Schizosaccharomyces pombe proteins" is not a medical term or concept. Schizosaccharomyces pombe is a type of single-celled microorganism called a yeast, which is often used as a model organism in scientific research. Proteins are complex molecules that do most of the work in cells and are necessary for the structure, function, and regulation of the body's tissues and organs.

In the context of scientific research, "Schizosaccharomyces pombe proteins" would refer to the specific proteins found in or studied using this particular type of yeast. These proteins may have similarities to human proteins and can be used to help understand basic biological processes, as well as diseases that occur in humans. However, it is important to note that while research using model organisms like Schizosaccharomyces pombe has led to many important discoveries, the findings may not always translate directly to humans.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Recombinant proteins are artificially created proteins produced through the use of recombinant DNA technology. This process involves combining DNA molecules from different sources to create a new set of genes that encode for a specific protein. The resulting recombinant protein can then be expressed, purified, and used for various applications in research, medicine, and industry.

Recombinant proteins are widely used in biomedical research to study protein function, structure, and interactions. They are also used in the development of diagnostic tests, vaccines, and therapeutic drugs. For example, recombinant insulin is a common treatment for diabetes, while recombinant human growth hormone is used to treat growth disorders.

The production of recombinant proteins typically involves the use of host cells, such as bacteria, yeast, or mammalian cells, which are engineered to express the desired protein. The host cells are transformed with a plasmid vector containing the gene of interest, along with regulatory elements that control its expression. Once the host cells are cultured and the protein is expressed, it can be purified using various chromatography techniques.

Overall, recombinant proteins have revolutionized many areas of biology and medicine, enabling researchers to study and manipulate proteins in ways that were previously impossible.

Genomic instability is a term used in genetics and molecular biology to describe a state of increased susceptibility to genetic changes or mutations in the genome. It can be defined as a condition where the integrity and stability of the genome are compromised, leading to an increased rate of DNA alterations such as point mutations, insertions, deletions, and chromosomal rearrangements.

Genomic instability is a hallmark of cancer cells and can also be observed in various other diseases, including genetic disorders and aging. It can arise due to defects in the DNA repair mechanisms, telomere maintenance, epigenetic regulation, or chromosome segregation during cell division. These defects can result from inherited genetic mutations, acquired somatic mutations, exposure to environmental mutagens, or age-related degenerative changes.

Genomic instability is a significant factor in the development and progression of cancer as it promotes the accumulation of oncogenic mutations that contribute to tumor initiation, growth, and metastasis. Therefore, understanding the mechanisms underlying genomic instability is crucial for developing effective strategies for cancer prevention, diagnosis, and treatment.

NIH 3T3 cells are a type of mouse fibroblast cell line that was developed by the National Institutes of Health (NIH). The "3T3" designation refers to the fact that these cells were derived from embryonic Swiss mouse tissue and were able to be passaged (i.e., subcultured) more than three times in tissue culture.

NIH 3T3 cells are widely used in scientific research, particularly in studies involving cell growth and differentiation, signal transduction, and gene expression. They have also been used as a model system for studying the effects of various chemicals and drugs on cell behavior. NIH 3T3 cells are known to be relatively easy to culture and maintain, and they have a stable, flat morphology that makes them well-suited for use in microscopy studies.

It is important to note that, as with any cell line, it is essential to verify the identity and authenticity of NIH 3T3 cells before using them in research, as contamination or misidentification can lead to erroneous results.

'Arabidopsis' is a genus of small flowering plants that are part of the mustard family (Brassicaceae). The most commonly studied species within this genus is 'Arabidopsis thaliana', which is often used as a model organism in plant biology and genetics research. This plant is native to Eurasia and Africa, and it has a small genome that has been fully sequenced. It is known for its short life cycle, self-fertilization, and ease of growth, making it an ideal subject for studying various aspects of plant biology, including development, metabolism, and response to environmental stresses.

A plasmid is a small, circular, double-stranded DNA molecule that is separate from the chromosomal DNA of a bacterium or other organism. Plasmids are typically not essential for the survival of the organism, but they can confer beneficial traits such as antibiotic resistance or the ability to degrade certain types of pollutants.

Plasmids are capable of replicating independently of the chromosomal DNA and can be transferred between bacteria through a process called conjugation. They often contain genes that provide resistance to antibiotics, heavy metals, and other environmental stressors. Plasmids have also been engineered for use in molecular biology as cloning vectors, allowing scientists to replicate and manipulate specific DNA sequences.

Plasmids are important tools in genetic engineering and biotechnology because they can be easily manipulated and transferred between organisms. They have been used to produce vaccines, diagnostic tests, and genetically modified organisms (GMOs) for various applications, including agriculture, medicine, and industry.

Matrix Attachment Regions (MARs) are specific DNA sequences that serve as anchor points for the attachment of chromosomes to the nuclear matrix, a network of fibers within the nucleus of a eukaryotic cell. MAR Binding Proteins (MARBPs) are a class of proteins that selectively bind to these MARs and play crucial roles in various nuclear processes such as DNA replication, transcription, repair, and chromosome organization.

MARBPs can be categorized into two main groups: structural and functional. Structural MARBPs help tether chromatin to the nuclear matrix and maintain the higher-order structure of chromatin. Functional MARBPs are involved in regulating gene expression, DNA replication, and repair by interacting with various transcription factors, enzymes, and other proteins at the MARs.

Examples of MARBPs include SATB1 (Special AT-rich sequence-binding protein 1), CTCF (CCCTC-binding factor), and NuMA (Nuclear Mitotic Apparatus protein). These proteins have been shown to play essential roles in chromatin organization, gene regulation, and cellular processes such as differentiation and development.

In summary, Matrix Attachment Region Binding Proteins are a class of nuclear proteins that selectively bind to specific DNA sequences called Matrix Attachment Regions (MARs). They contribute to various nuclear processes, including chromatin organization, gene regulation, DNA replication, and repair.

Transcriptional activation is the process by which a cell increases the rate of transcription of specific genes from DNA to RNA. This process is tightly regulated and plays a crucial role in various biological processes, including development, differentiation, and response to environmental stimuli.

Transcriptional activation occurs when transcription factors (proteins that bind to specific DNA sequences) interact with the promoter region of a gene and recruit co-activator proteins. These co-activators help to remodel the chromatin structure around the gene, making it more accessible for the transcription machinery to bind and initiate transcription.

Transcriptional activation can be regulated at multiple levels, including the availability and activity of transcription factors, the modification of histone proteins, and the recruitment of co-activators or co-repressors. Dysregulation of transcriptional activation has been implicated in various diseases, including cancer and genetic disorders.

Transfection is a term used in molecular biology that refers to the process of deliberately introducing foreign genetic material (DNA, RNA or artificial gene constructs) into cells. This is typically done using chemical or physical methods, such as lipofection or electroporation. Transfection is widely used in research and medical settings for various purposes, including studying gene function, producing proteins, developing gene therapies, and creating genetically modified organisms. It's important to note that transfection is different from transduction, which is the process of introducing genetic material into cells using viruses as vectors.

Beta karyopherins, also known as importin-Ī²s or transportins, are a family of nuclear transport receptors that play a crucial role in the shuttling of proteins and RNAs between the cytoplasm and the nucleus. They recognize specific signals on their cargo, such as nuclear localization sequences (NLS) or nuclear export sequences (NES), and mediate their translocation through the nuclear pore complex (NPC).

Beta karyopherins function by binding to their cargo in the cytoplasm, forming a complex that is then recognized by the NPC. Once inside the nucleus, beta karyopherins release their cargo and return to the cytoplasm, where they can bind to new cargoes.

There are several members of the beta karyopherin family, each with distinct specificities for different types of cargoes. Some examples include importin-Ī²1, which is involved in the transport of classical NLS-containing proteins; importin-Ī±, which acts as an adaptor between importin-Ī²1 and its cargo; and transportin-1, which transports RNA-binding proteins.

Dysregulation of beta karyopherin function has been implicated in various diseases, including cancer, neurodegenerative disorders, and viral infections.

A nuclear pore is a complex structure that penetrates the nuclear envelope, forming a channel through which molecules can be transported between the cytoplasm and the nucleus. Nuclear pores are composed of multiple proteins called nucleoporins, which come together to form a large, ring-shaped structure with a central transport channel. This channel is selectively permeable, allowing only certain molecules to pass through based on their size, charge, and other properties.

The process of transport through the nuclear pore is mediated by specialized transport factors called karyopherins, which bind to specific cargo molecules and help them move through the pore. This active transport process requires energy in the form of ATP, and is tightly regulated to ensure that only the necessary molecules are allowed to enter or exit the nucleus.

Nuclear pores play a critical role in many cellular processes, including gene expression, DNA replication, and the regulation of cell signaling pathways. Defects in nuclear pore structure or function have been linked to a variety of human diseases, including cancer, neurodegenerative disorders, and developmental abnormalities.

Medical Definition of "Multiprotein Complexes" :

Multiprotein complexes are large molecular assemblies composed of two or more proteins that interact with each other to carry out specific cellular functions. These complexes can range from relatively simple dimers or trimers to massive structures containing hundreds of individual protein subunits. They are formed through a process known as protein-protein interaction, which is mediated by specialized regions on the protein surface called domains or motifs.

Multiprotein complexes play critical roles in many cellular processes, including signal transduction, gene regulation, DNA replication and repair, protein folding and degradation, and intracellular transport. The formation of these complexes is often dynamic and regulated in response to various stimuli, allowing for precise control of their function.

Disruption of multiprotein complexes can lead to a variety of diseases, including cancer, neurodegenerative disorders, and infectious diseases. Therefore, understanding the structure, composition, and regulation of these complexes is an important area of research in molecular biology and medicine.

Cell cycle proteins are a group of regulatory proteins that control the progression of the cell cycle, which is the series of events that take place in a eukaryotic cell leading to its division and duplication. These proteins can be classified into several categories based on their functions during different stages of the cell cycle.

The major groups of cell cycle proteins include:

1. Cyclin-dependent kinases (CDKs): CDKs are serine/threonine protein kinases that regulate key transitions in the cell cycle. They require binding to a regulatory subunit called cyclin to become active. Different CDK-cyclin complexes are activated at different stages of the cell cycle.
2. Cyclins: Cyclins are a family of regulatory proteins that bind and activate CDKs. Their levels fluctuate throughout the cell cycle, with specific cyclins expressed during particular phases. For example, cyclin D is important for the G1 to S phase transition, while cyclin B is required for the G2 to M phase transition.
3. CDK inhibitors (CKIs): CKIs are regulatory proteins that bind to and inhibit CDKs, thereby preventing their activation. CKIs can be divided into two main families: the INK4 family and the Cip/Kip family. INK4 family members specifically inhibit CDK4 and CDK6, while Cip/Kip family members inhibit a broader range of CDKs.
4. Anaphase-promoting complex/cyclosome (APC/C): APC/C is an E3 ubiquitin ligase that targets specific proteins for degradation by the 26S proteasome. During the cell cycle, APC/C regulates the metaphase to anaphase transition and the exit from mitosis by targeting securin and cyclin B for degradation.
5. Other regulatory proteins: Several other proteins play crucial roles in regulating the cell cycle, such as p53, a transcription factor that responds to DNA damage and arrests the cell cycle, and the polo-like kinases (PLKs), which are involved in various aspects of mitosis.

Overall, cell cycle proteins work together to ensure the proper progression of the cell cycle, maintain genomic stability, and prevent uncontrolled cell growth, which can lead to cancer.

Fluorescence microscopy is a type of microscopy that uses fluorescent dyes or proteins to highlight and visualize specific components within a sample. In this technique, the sample is illuminated with high-energy light, typically ultraviolet (UV) or blue light, which excites the fluorescent molecules causing them to emit lower-energy, longer-wavelength light, usually visible light in the form of various colors. This emitted light is then collected by the microscope and detected to produce an image.

Fluorescence microscopy has several advantages over traditional brightfield microscopy, including the ability to visualize specific structures or molecules within a complex sample, increased sensitivity, and the potential for quantitative analysis. It is widely used in various fields of biology and medicine, such as cell biology, neuroscience, and pathology, to study the structure, function, and interactions of cells and proteins.

There are several types of fluorescence microscopy techniques, including widefield fluorescence microscopy, confocal microscopy, two-photon microscopy, and total internal reflection fluorescence (TIRF) microscopy, each with its own strengths and limitations. These techniques can provide valuable insights into the behavior of cells and proteins in health and disease.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4Ā°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

Ubiquitin-specific proteases (USPs) are a type of deubiquitinating enzymes (DUBs) that specifically cleave ubiquitin from proteins. Ubiquitination is a post-translational modification in which ubiquitin molecules are attached to proteins, targeting them for degradation by the proteasome. USPs reverse this process by removing ubiquitin molecules from proteins, thereby regulating protein stability, localization, and activity.

USPs contain a conserved catalytic domain that is responsible for the deubiquitinating activity. They are involved in various cellular processes, including DNA damage repair, gene expression regulation, inflammation, and immune response. Dysregulation of USP function has been implicated in several diseases, such as cancer, neurodegenerative disorders, and viral infections. Therefore, USPs are considered potential therapeutic targets for the development of drugs to treat these conditions.

Chromatin is the complex of DNA, RNA, and proteins that make up the chromosomes in the nucleus of a cell. It is responsible for packaging the long DNA molecules into a more compact form that fits within the nucleus. Chromatin is made up of repeating units called nucleosomes, which consist of a histone protein octamer wrapped tightly by DNA. The structure of chromatin can be altered through chemical modifications to the histone proteins and DNA, which can influence gene expression and other cellular processes.

A mutant protein is a protein that has undergone a genetic mutation, resulting in an altered amino acid sequence and potentially changed structure and function. These changes can occur due to various reasons such as errors during DNA replication, exposure to mutagenic substances, or inherited genetic disorders. The alterations in the protein's structure and function may have no significant effects, lead to benign phenotypic variations, or cause diseases, depending on the type and location of the mutation. Some well-known examples of diseases caused by mutant proteins include cystic fibrosis, sickle cell anemia, and certain types of cancer.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

Double-stranded DNA breaks (DSBs) refer to a type of damage that occurs in the DNA molecule when both strands of the double helix are severed or broken at the same location. This kind of damage is particularly harmful to cells because it can disrupt the integrity and continuity of the genetic material, potentially leading to genomic instability, mutations, and cell death if not properly repaired.

DSBs can arise from various sources, including exposure to ionizing radiation, chemical agents, free radicals, reactive oxygen species (ROS), and errors during DNA replication or repair processes. Unrepaired or incorrectly repaired DSBs have been implicated in numerous human diseases, such as cancer, neurodegenerative disorders, and premature aging.

Cells possess several mechanisms to repair double-stranded DNA breaks, including homologous recombination (HR) and non-homologous end joining (NHEJ). HR is a more accurate repair pathway that uses a homologous template, typically the sister chromatid, to restore the original DNA sequence. NHEJ, on the other hand, directly ligates the broken ends together, often resulting in small deletions or insertions at the break site and increased risk of errors. The choice between these two pathways depends on various factors, such as the cell cycle stage, the presence of nearby breaks, and the availability of repair proteins.

In summary, double-stranded DNA breaks are severe forms of DNA damage that can have detrimental consequences for cells if not properly repaired. Cells employ multiple mechanisms to address DSBs, with homologous recombination and non-homologous end joining being the primary repair pathways.

Chromosome pairing, also known as chromosome synapsis, is a process that occurs during meiosis, which is the type of cell division that results in the formation of sex cells or gametes (sperm and eggs).

In humans, each cell contains 23 pairs of chromosomes, for a total of 46 chromosomes. Of these, 22 pairs are called autosomal chromosomes, and they are similar in size and shape between the two copies in a pair. The last pair is called the sex chromosomes (X and Y), which determine the individual's biological sex.

During meiosis, homologous chromosomes (one from each parent) come together and pair up along their lengths in a process called synapsis. This pairing allows for the precise alignment of corresponding genes and genetic regions between the two homologous chromosomes. Once paired, the chromosomes exchange genetic material through a process called crossing over, which increases genetic diversity in the resulting gametes.

After crossing over, the homologous chromosomes separate during meiosis I, followed by the separation of sister chromatids (the two copies of each chromosome) during meiosis II. The end result is four haploid cells, each containing 23 chromosomes, which then develop into sperm or eggs.

Chromosome pairing is a crucial step in the process of sexual reproduction, ensuring that genetic information is accurately passed from one generation to the next while also promoting genetic diversity through recombination and independent assortment of chromosomes.

ELK-1 is a transcription factor that belongs to the ETS domain protein family. Transcription factors are proteins that regulate gene expression by binding to specific DNA sequences, thereby controlling the rate of transcription of genetic information from DNA to RNA. The ETS domain is a conserved DNA-binding domain found in many transcription factors and is named after the E26 transformation-specific sequence, which was first identified in avian erythroblastosis virus.

ELK-1 is specifically involved in the regulation of genes that are responsible for cell growth, differentiation, and survival. It is activated by various signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway, which is critical for relaying signals from the cell surface to the nucleus in response to growth factors, hormones, and other extracellular stimuli. Once activated, ELK-1 translocates to the nucleus, where it binds to specific DNA sequences called ETS-binding sites and recruits other proteins to modulate the transcription of target genes.

Dysregulation of ELK-1 has been implicated in several human diseases, including cancer, cardiovascular disease, and neurological disorders. For example, aberrant activation of ELK-1 has been observed in various types of cancer, such as lung, breast, and prostate cancer, and is often associated with poor clinical outcomes. Therefore, understanding the molecular mechanisms that regulate ELK-1 activity and function is crucial for developing novel therapeutic strategies to treat these diseases.

Molecular models are three-dimensional representations of molecular structures that are used in the field of molecular biology and chemistry to visualize and understand the spatial arrangement of atoms and bonds within a molecule. These models can be physical or computer-generated and allow researchers to study the shape, size, and behavior of molecules, which is crucial for understanding their function and interactions with other molecules.

Physical molecular models are often made up of balls (representing atoms) connected by rods or sticks (representing bonds). These models can be constructed manually using materials such as plastic or wooden balls and rods, or they can be created using 3D printing technology.

Computer-generated molecular models, on the other hand, are created using specialized software that allows researchers to visualize and manipulate molecular structures in three dimensions. These models can be used to simulate molecular interactions, predict molecular behavior, and design new drugs or chemicals with specific properties. Overall, molecular models play a critical role in advancing our understanding of molecular structures and their functions.

Site-directed mutagenesis is a molecular biology technique used to introduce specific and targeted changes to a specific DNA sequence. This process involves creating a new variant of a gene or a specific region of interest within a DNA molecule by introducing a planned, deliberate change, or mutation, at a predetermined site within the DNA sequence.

The methodology typically involves the use of molecular tools such as PCR (polymerase chain reaction), restriction enzymes, and/or ligases to introduce the desired mutation(s) into a plasmid or other vector containing the target DNA sequence. The resulting modified DNA molecule can then be used to transform host cells, allowing for the production of large quantities of the mutated gene or protein for further study.

Site-directed mutagenesis is a valuable tool in basic research, drug discovery, and biotechnology applications where specific changes to a DNA sequence are required to understand gene function, investigate protein structure/function relationships, or engineer novel biological properties into existing genes or proteins.

The nucleolus is a structure found within the nucleus of eukaryotic cells (cells that contain a true nucleus). It plays a central role in the production and assembly of ribosomes, which are complex molecular machines responsible for protein synthesis. The nucleolus is not a distinct organelle with a membrane surrounding it, but rather a condensed region within the nucleus where ribosomal biogenesis takes place.

The process of ribosome formation begins in the nucleolus with the transcription of ribosomal DNA (rDNA) genes into long precursor RNA molecules called rRNAs (ribosomal RNAs). Within the nucleolus, these rRNA molecules are cleaved, modified, and assembled together with ribosomal proteins to form small and large ribosomal subunits. Once formed, these subunits are transported through the nuclear pores to the cytoplasm, where they come together to form functional ribosomes that can engage in protein synthesis.

In addition to its role in ribosome biogenesis, the nucleolus has been implicated in other cellular processes such as stress response, cell cycle regulation, and aging. Changes in nucleolar structure and function have been associated with various diseases, including cancer and neurodegenerative disorders.

Mass spectrometry (MS) is an analytical technique used to identify and quantify the chemical components of a mixture or compound. It works by ionizing the sample, generating charged molecules or fragments, and then measuring their mass-to-charge ratio in a vacuum. The resulting mass spectrum provides information about the molecular weight and structure of the analytes, allowing for identification and characterization.

In simpler terms, mass spectrometry is a method used to determine what chemicals are present in a sample and in what quantities, by converting the chemicals into ions, measuring their masses, and generating a spectrum that shows the relative abundances of each ion type.

Salt-tolerant plants, also known as halophytes, are plants that can grow and complete their life cycle in saline environments. These plants have specialized adaptations that allow them to survive and reproduce in the presence of high concentrations of salt, particularly sodium chloride (NaCl), which is toxic to most plants.

Salt tolerance in plants is a complex trait that involves various physiological and biochemical mechanisms, such as:

1. Exclusion: Preventing the uptake of excess salt by the roots or excluding it from entering the plant cells.
2. Compartmentalization: Storing excess salt in vacuoles or older leaves that can be shed to reduce the overall salt load.
3. Tissue tolerance: Adapting to high salt concentrations within the plant tissues without experiencing toxicity or osmotic stress.
4. Osmoregulation: Maintaining water balance and cell turgor by synthesizing and accumulating compatible solutes, such as proline and glycine betaine, which help to lower the osmotic potential of the cells.
5. Ion homeostasis: Regulating the uptake and distribution of essential ions, like potassium (K+), while minimizing the accumulation of toxic ions, such as sodium (Na+) and chloride (Cl-).

Examples of salt-tolerant plants include mangroves, sea grasses, cordgrass, glasswort, and certain species of cacti and succulents. These plants have significant ecological and agricultural importance in coastal areas and arid regions, where salinity is a major environmental constraint.

Proteomics is the large-scale study and analysis of proteins, including their structures, functions, interactions, modifications, and abundance, in a given cell, tissue, or organism. It involves the identification and quantification of all expressed proteins in a biological sample, as well as the characterization of post-translational modifications, protein-protein interactions, and functional pathways. Proteomics can provide valuable insights into various biological processes, diseases, and drug responses, and has applications in basic research, biomedicine, and clinical diagnostics. The field combines various techniques from molecular biology, chemistry, physics, and bioinformatics to study proteins at a systems level.

Chromosomal proteins, non-histone, are a diverse group of proteins that are associated with chromatin, the complex of DNA and histone proteins, but do not have the characteristic structure of histones. These proteins play important roles in various nuclear processes such as DNA replication, transcription, repair, recombination, and chromosome condensation and segregation during cell division. They can be broadly classified into several categories based on their functions, including architectural proteins, enzymes, transcription factors, and structural proteins. Examples of non-histone chromosomal proteins include high mobility group (HMG) proteins, poly(ADP-ribose) polymerases (PARPs), and condensins.

A centromere is a specialized region found on chromosomes that plays a crucial role in the separation of replicated chromosomes during cell division. It is the point where the sister chromatids (the two copies of a chromosome formed during DNA replication) are joined together. The centromere contains highly repeated DNA sequences and proteins that form a complex structure known as the kinetochore, which serves as an attachment site for microtubules of the mitotic spindle during cell division.

During mitosis or meiosis, the kinetochore facilitates the movement of chromosomes by interacting with the microtubules, allowing for the accurate distribution of genetic material to the daughter cells. Centromeres can vary in their position and structure among different species, ranging from being located near the middle of the chromosome (metacentric) to being positioned closer to one end (acrocentric). The precise location and characteristics of centromeres are essential for proper chromosome segregation and maintenance of genomic stability.

Familial Partial Lipodystrophy (FPL) is a rare genetic disorder characterized by the selective loss of fat tissue in various parts of the body. It is caused by mutations in specific genes involved in the regulation of fat metabolism. There are several types of FPL, but the most common one is called Dunnigan-type or FPLD2, which is caused by mutations in the LMNA gene.

In FPL, there is a lack of subcutaneous fat (the fat layer beneath the skin) in certain areas of the body, such as the face, arms, legs, and buttocks, while other areas may have excess fat accumulation, such as the neck, shoulders, and abdomen. This abnormal distribution of fat can lead to a variety of metabolic complications, including insulin resistance, diabetes mellitus, high levels of triglycerides in the blood (hypertriglyceridemia), and an increased risk of cardiovascular disease.

FPL is usually inherited as an autosomal dominant trait, which means that a person has a 50% chance of inheriting the mutated gene from an affected parent. However, some cases may occur spontaneously due to new mutations in the gene. The diagnosis of FPL is typically based on clinical examination, family history, and genetic testing. Treatment usually involves lifestyle modifications, such as diet and exercise, and medications to manage metabolic complications.

In genetics, sequence alignment is the process of arranging two or more DNA, RNA, or protein sequences to identify regions of similarity or homology between them. This is often done using computational methods to compare the nucleotide or amino acid sequences and identify matching patterns, which can provide insight into evolutionary relationships, functional domains, or potential genetic disorders. The alignment process typically involves adjusting gaps and mismatches in the sequences to maximize the similarity between them, resulting in an aligned sequence that can be visually represented and analyzed.

Protein stability refers to the ability of a protein to maintain its native structure and function under various physiological conditions. It is determined by the balance between forces that promote a stable conformation, such as intramolecular interactions (hydrogen bonds, van der Waals forces, and hydrophobic effects), and those that destabilize it, such as thermal motion, chemical denaturation, and environmental factors like pH and salt concentration. A protein with high stability is more resistant to changes in its structure and function, even under harsh conditions, while a protein with low stability is more prone to unfolding or aggregation, which can lead to loss of function or disease states, such as protein misfolding diseases.

Luminescent proteins are a type of protein that emit light through a chemical reaction, rather than by absorbing and re-emitting light like fluorescent proteins. This process is called bioluminescence. The light emitted by luminescent proteins is often used in scientific research as a way to visualize and track biological processes within cells and organisms.

One of the most well-known luminescent proteins is Green Fluorescent Protein (GFP), which was originally isolated from jellyfish. However, GFP is actually a fluorescent protein, not a luminescent one. A true example of a luminescent protein is the enzyme luciferase, which is found in fireflies and other bioluminescent organisms. When luciferase reacts with its substrate, luciferin, it produces light through a process called oxidation.

Luminescent proteins have many applications in research, including as reporters for gene expression, as markers for protein-protein interactions, and as tools for studying the dynamics of cellular processes. They are also used in medical imaging and diagnostics, as well as in the development of new therapies.

I'm sorry for any confusion, but "oxides" is not a term that has a specific medical definition. Oxides are a class of chemical compounds that contain at least one oxygen atom and one other element. They can be formed through the process of oxidation, which involves the combination of oxygen with another substance.

In a broader sense, you might encounter the term "oxide" in a medical context when discussing various materials or substances used in medical devices, treatments, or research. For instance, titanium dioxide is a common ingredient in medical-grade sunscreens due to its ability to block and scatter UV light. However, it's important to note that the term "oxides" itself doesn't have a direct connection to medicine or human health.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

Mitosis is a type of cell division in which the genetic material of a single cell, called the mother cell, is equally distributed into two identical daughter cells. It's a fundamental process that occurs in multicellular organisms for growth, maintenance, and repair, as well as in unicellular organisms for reproduction.

The process of mitosis can be broken down into several stages: prophase, prometaphase, metaphase, anaphase, and telophase. During prophase, the chromosomes condense and become visible, and the nuclear envelope breaks down. In prometaphase, the nuclear membrane is completely disassembled, and the mitotic spindle fibers attach to the chromosomes at their centromeres.

During metaphase, the chromosomes align at the metaphase plate, an imaginary line equidistant from the two spindle poles. In anaphase, sister chromatids are pulled apart by the spindle fibers and move toward opposite poles of the cell. Finally, in telophase, new nuclear envelopes form around each set of chromosomes, and the chromosomes decondense and become less visible.

Mitosis is followed by cytokinesis, a process that divides the cytoplasm of the mother cell into two separate daughter cells. The result of mitosis and cytokinesis is two genetically identical cells, each with the same number and kind of chromosomes as the original parent cell.

DNA helicases are a group of enzymes that are responsible for separating the two strands of DNA during processes such as replication and transcription. They do this by unwinding the double helix structure of DNA, using energy from ATP to break the hydrogen bonds between the base pairs. This allows other proteins to access the individual strands of DNA and carry out functions such as copying the genetic code or transcribing it into RNA.

During replication, DNA helicases help to create a replication fork, where the two strands of DNA are separated and new complementary strands are synthesized. In transcription, DNA helicases help to unwind the DNA double helix at the promoter region, allowing the RNA polymerase enzyme to bind and begin transcribing the DNA into RNA.

DNA helicases play a crucial role in maintaining the integrity of the genetic code and are essential for the normal functioning of cells. Defects in DNA helicases have been linked to various diseases, including cancer and neurological disorders.

Rad52 is a DNA repair and recombination protein that plays a crucial role in the maintenance of genomic stability in cells. It is highly conserved across various species, including yeast, humans, and other mammals. The primary function of Rad52 is to facilitate the process of homologous recombination (HR), which is a critical DNA repair mechanism that helps to maintain the integrity of the genetic material in the event of double-strand breaks (DSBs) or other types of DNA damage.

Rad52 has several essential roles in HR:

1. Rad52 promotes the formation of ssDNA-Rad51 nucleoprotein filaments: Rad52 interacts with single-stranded DNA (ssDNA) generated during resection of DSBs, facilitating the recruitment and loading of the Rad51 recombinase onto the ssDNA. This Rad51-ssDNA nucleoprotein filament formation is a key step in HR, as it enables the search for homologous sequences and subsequent strand invasion.

2. Rad52 mediates DNA annealing: Rad52 can catalyze the annealing of complementary ssDNA molecules, promoting the reannealing of invaded strands during HR or facilitating the pairing of RPA-coated ssDNA with homologous duplex DNA.

3. Rad52 stimulates D-loop formation and extension: Rad52 can stimulate the extension of D-loops, which are three-stranded structures formed when a single-stranded DNA invades a double-stranded DNA molecule during HR. This process is essential for the subsequent steps of homology search and strand exchange.

4. Rad52 facilitates RPA displacement: Rad52 can displace replication protein A (RPA) from ssDNA, allowing Rad51 to bind and form nucleoprotein filaments. This is a critical step in HR, as RPA inhibits Rad51 binding to ssDNA.

5. Rad52 interacts with other DNA repair proteins: Rad52 interacts with various DNA repair proteins, including BRCA1, BRCA2, and the single-strand binding protein RPA, to coordinate HR and other DNA repair pathways.

In summary, Rad52 is a crucial player in homologous recombination (HR) and DNA damage response. It functions as a mediator of DNA annealing, D-loop formation, and RPA displacement, promoting efficient HR and maintaining genome stability.

Yeasts are single-celled microorganisms that belong to the fungus kingdom. They are characterized by their ability to reproduce asexually through budding or fission, and they obtain nutrients by fermenting sugars and other organic compounds. Some species of yeast can cause infections in humans, known as candidiasis or "yeast infections." These infections can occur in various parts of the body, including the skin, mouth, genitals, and internal organs. Common symptoms of a yeast infection may include itching, redness, irritation, and discharge. Yeast infections are typically treated with antifungal medications.

Physiological stress is a response of the body to a demand or threat that disrupts homeostasis and activates the autonomic nervous system and hypothalamic-pituitary-adrenal (HPA) axis. This results in the release of stress hormones such as adrenaline, cortisol, and noradrenaline, which prepare the body for a "fight or flight" response. Increased heart rate, rapid breathing, heightened sensory perception, and increased alertness are some of the physiological changes that occur during this response. Chronic stress can have negative effects on various bodily functions, including the immune, cardiovascular, and nervous systems.

Peptide hydrolases, also known as proteases or peptidases, are a group of enzymes that catalyze the hydrolysis of peptide bonds in proteins and peptides. They play a crucial role in various biological processes such as protein degradation, digestion, cell signaling, and regulation of various physiological functions. Based on their catalytic mechanism and the specificity for the peptide bond, they are classified into several types, including serine proteases, cysteine proteases, aspartic proteases, and metalloproteases. These enzymes have important clinical applications in the diagnosis and treatment of various diseases, such as cancer, viral infections, and inflammatory disorders.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

Protein multimerization refers to the process where multiple protein subunits assemble together to form a complex, repetitive structure called a multimer or oligomer. This can involve the association of identical or similar protein subunits through non-covalent interactions such as hydrogen bonding, ionic bonding, and van der Waals forces. The resulting multimeric structures can have various shapes, sizes, and functions, including enzymatic activity, transport, or structural support. Protein multimerization plays a crucial role in many biological processes and is often necessary for the proper functioning of proteins within cells.

Green Fluorescent Protein (GFP) is not a medical term per se, but a scientific term used in the field of molecular biology. GFP is a protein that exhibits bright green fluorescence when exposed to light, particularly blue or ultraviolet light. It was originally discovered in the jellyfish Aequorea victoria.

In medical and biological research, scientists often use recombinant DNA technology to introduce the gene for GFP into other organisms, including bacteria, plants, and animals, including humans. This allows them to track the expression and localization of specific genes or proteins of interest in living cells, tissues, or even whole organisms.

The ability to visualize specific cellular structures or processes in real-time has proven invaluable for a wide range of research areas, from studying the development and function of organs and organ systems to understanding the mechanisms of diseases and the effects of therapeutic interventions.

Immunoblotting, also known as western blotting, is a laboratory technique used in molecular biology and immunogenetics to detect and quantify specific proteins in a complex mixture. This technique combines the electrophoretic separation of proteins by gel electrophoresis with their detection using antibodies that recognize specific epitopes (protein fragments) on the target protein.

The process involves several steps: first, the protein sample is separated based on size through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Next, the separated proteins are transferred onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric field. The membrane is then blocked with a blocking agent to prevent non-specific binding of antibodies.

After blocking, the membrane is incubated with a primary antibody that specifically recognizes the target protein. Following this, the membrane is washed to remove unbound primary antibodies and then incubated with a secondary antibody conjugated to an enzyme such as horseradish peroxidase (HRP) or alkaline phosphatase (AP). The enzyme catalyzes a colorimetric or chemiluminescent reaction that allows for the detection of the target protein.

Immunoblotting is widely used in research and clinical settings to study protein expression, post-translational modifications, protein-protein interactions, and disease biomarkers. It provides high specificity and sensitivity, making it a valuable tool for identifying and quantifying proteins in various biological samples.

Cytoplasm is the material within a eukaryotic cell (a cell with a true nucleus) that lies between the nuclear membrane and the cell membrane. It is composed of an aqueous solution called cytosol, in which various organelles such as mitochondria, ribosomes, endoplasmic reticulum, Golgi apparatus, lysosomes, and vacuoles are suspended. Cytoplasm also contains a variety of dissolved nutrients, metabolites, ions, and enzymes that are involved in various cellular processes such as metabolism, signaling, and transport. It is where most of the cell's metabolic activities take place, and it plays a crucial role in maintaining the structure and function of the cell.

Protein interaction mapping is a research approach used to identify and characterize the physical interactions between different proteins within a cell or organism. This process often involves the use of high-throughput experimental techniques, such as yeast two-hybrid screening, mass spectrometry-based approaches, or protein fragment complementation assays, to detect and quantify the binding affinities of protein pairs. The resulting data is then used to construct a protein interaction network, which can provide insights into functional relationships between proteins, help elucidate cellular pathways, and inform our understanding of biological processes in health and disease.

Intracellular signaling peptides and proteins are molecules that play a crucial role in transmitting signals within cells, which ultimately lead to changes in cell behavior or function. These signals can originate from outside the cell (extracellular) or within the cell itself. Intracellular signaling molecules include various types of peptides and proteins, such as:

1. G-protein coupled receptors (GPCRs): These are seven-transmembrane domain receptors that bind to extracellular signaling molecules like hormones, neurotransmitters, or chemokines. Upon activation, they initiate a cascade of intracellular signals through G proteins and secondary messengers.
2. Receptor tyrosine kinases (RTKs): These are transmembrane receptors that bind to growth factors, cytokines, or hormones. Activation of RTKs leads to autophosphorylation of specific tyrosine residues, creating binding sites for intracellular signaling proteins such as adapter proteins, phosphatases, and enzymes like Ras, PI3K, and Src family kinases.
3. Second messenger systems: Intracellular second messengers are small molecules that amplify and propagate signals within the cell. Examples include cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), diacylglycerol (DAG), inositol triphosphate (IP3), calcium ions (Ca2+), and nitric oxide (NO). These second messengers activate or inhibit various downstream effectors, leading to changes in cellular responses.
4. Signal transduction cascades: Intracellular signaling proteins often form complex networks of interacting molecules that relay signals from the plasma membrane to the nucleus. These cascades involve kinases (protein kinases A, B, C, etc.), phosphatases, and adapter proteins, which ultimately regulate gene expression, cell cycle progression, metabolism, and other cellular processes.
5. Ubiquitination and proteasome degradation: Intracellular signaling pathways can also control protein stability by modulating ubiquitin-proteasome degradation. E3 ubiquitin ligases recognize specific substrates and conjugate them with ubiquitin molecules, targeting them for proteasomal degradation. This process regulates the abundance of key signaling proteins and contributes to signal termination or amplification.

In summary, intracellular signaling pathways involve a complex network of interacting proteins that relay signals from the plasma membrane to various cellular compartments, ultimately regulating gene expression, metabolism, and other cellular processes. Dysregulation of these pathways can contribute to disease development and progression, making them attractive targets for therapeutic intervention.

I'm sorry for any confusion, but "Sp3 Transcription Factor" is not a recognized medical term. However, I can provide you with a scientific explanation:

Sp3 is a type of transcription factor that binds to specific DNA sequences and helps regulate gene expression in cells. Sp3 stands for Specificity Protein 3, which belongs to the Sp (Specificity protein) family of transcription factors. These proteins play crucial roles during development and differentiation of various tissues.

Transcription factors like Sp3 have modular structures, consisting of several functional domains that enable them to perform their regulatory functions:

1. DNA-binding domain (DBD): This region recognizes and binds to specific DNA sequences, usually located in the promoter or enhancer regions of target genes. The DBD of Sp3 proteins is a zinc finger domain, which contains multiple tandem repeats that fold into a structure that interacts with the DNA.

2. Transcriptional regulatory domain (TRD): This region can either activate or repress gene transcription depending on the context and interacting partners. The TRD of Sp3 proteins has an inhibitory effect on transcription, but it can be overcome by other activating co-factors.

3. Nuclear localization signal (NLS): This domain targets the protein to the nucleus, where it can perform its regulatory functions.

4. Protein-protein interaction domains: These regions allow Sp3 proteins to interact with other transcription factors and co-regulators, forming complexes that modulate gene expression.

In summary, Sp3 is a transcription factor that binds to specific DNA sequences and regulates the expression of target genes by either activating or repressing their transcription. It plays essential roles in various cellular processes during development and tissue differentiation.

Small interfering RNA (siRNA) is a type of short, double-stranded RNA molecule that plays a role in the RNA interference (RNAi) pathway. The RNAi pathway is a natural cellular process that regulates gene expression by targeting and destroying specific messenger RNA (mRNA) molecules, thereby preventing the translation of those mRNAs into proteins.

SiRNAs are typically 20-25 base pairs in length and are generated from longer double-stranded RNA precursors called hairpin RNAs or dsRNAs by an enzyme called Dicer. Once generated, siRNAs associate with a protein complex called the RNA-induced silencing complex (RISC), which uses one strand of the siRNA (the guide strand) to recognize and bind to complementary sequences in the target mRNA. The RISC then cleaves the target mRNA, leading to its degradation and the inhibition of protein synthesis.

SiRNAs have emerged as a powerful tool for studying gene function and have shown promise as therapeutic agents for a variety of diseases, including viral infections, cancer, and genetic disorders. However, their use as therapeutics is still in the early stages of development, and there are challenges associated with delivering siRNAs to specific cells and tissues in the body.

Promoter regions in genetics refer to specific DNA sequences located near the transcription start site of a gene. They serve as binding sites for RNA polymerase and various transcription factors that regulate the initiation of gene transcription. These regulatory elements help control the rate of transcription and, therefore, the level of gene expression. Promoter regions can be composed of different types of sequences, such as the TATA box and CAAT box, and their organization and composition can vary between different genes and species.

Nuclear antigens are proteins or other molecules found in the nucleus of a cell that can stimulate an immune response and produce antibodies when they are recognized as foreign by the body's immune system. These antigens are normally located inside the cell and are not typically exposed to the immune system, but under certain circumstances, such as during cell death or damage, they may be released and become targets of the immune system.

Nuclear antigens can play a role in the development of some autoimmune diseases, such as systemic lupus erythematosus (SLE), where the body's immune system mistakenly attacks its own cells and tissues. In SLE, nuclear antigens such as double-stranded DNA and nucleoproteins are common targets of the abnormal immune response.

Testing for nuclear antigens is often used in the diagnosis and monitoring of autoimmune diseases. For example, a positive test for anti-double-stranded DNA antibodies is a specific indicator of SLE and can help confirm the diagnosis. However, it's important to note that not all people with SLE will have positive nuclear antigen tests, and other factors must also be considered in making a diagnosis.

Chromosome segregation is the process that occurs during cell division (mitosis or meiosis) where replicated chromosomes are separated and distributed equally into two daughter cells. Each chromosome consists of two sister chromatids, which are identical copies of genetic material. During chromosome segregation, these sister chromatids are pulled apart by a structure called the mitotic spindle and moved to opposite poles of the cell. This ensures that each new cell receives one copy of each chromosome, preserving the correct number and composition of chromosomes in the organism.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Trans-activators are proteins that increase the transcriptional activity of a gene or a set of genes. They do this by binding to specific DNA sequences and interacting with the transcription machinery, thereby enhancing the recruitment and assembly of the complexes needed for transcription. In some cases, trans-activators can also modulate the chromatin structure to make the template more accessible to the transcription machinery.

In the context of HIV (Human Immunodeficiency Virus) infection, the term "trans-activator" is often used specifically to refer to the Tat protein. The Tat protein is a viral regulatory protein that plays a critical role in the replication of HIV by activating the transcription of the viral genome. It does this by binding to a specific RNA structure called the Trans-Activation Response Element (TAR) located at the 5' end of all nascent HIV transcripts, and recruiting cellular cofactors that enhance the processivity and efficiency of RNA polymerase II, leading to increased viral gene expression.

Arsenicals are a group of chemicals that contain arsenic, a naturally occurring element that is toxic to humans and animals. Arsenic can combine with other elements such as chlorine, sulfur, or carbon to form various inorganic and organic compounds known as arsenicals. These compounds have been used in a variety of industrial and agricultural applications, including wood preservatives, pesticides, and herbicides.

Exposure to high levels of arsenic can cause serious health effects, including skin damage, circulatory problems, and increased risk of cancer. Long-term exposure to lower levels of arsenic can also lead to chronic health issues, such as neurological damage and diabetes. Therefore, the use of arsenicals is regulated in many countries to minimize human and environmental exposure.

Carrier proteins, also known as transport proteins, are a type of protein that facilitates the movement of molecules across cell membranes. They are responsible for the selective and active transport of ions, sugars, amino acids, and other molecules from one side of the membrane to the other, against their concentration gradient. This process requires energy, usually in the form of ATP (adenosine triphosphate).

Carrier proteins have a specific binding site for the molecule they transport, and undergo conformational changes upon binding, which allows them to move the molecule across the membrane. Once the molecule has been transported, the carrier protein returns to its original conformation, ready to bind and transport another molecule.

Carrier proteins play a crucial role in maintaining the balance of ions and other molecules inside and outside of cells, and are essential for many physiological processes, including nerve impulse transmission, muscle contraction, and nutrient uptake.

Luciferases are enzymes that catalyze light-emitting reactions. They are named after the phenomenon of luciferin, a generic term for the light-emitting compound, being oxidized by the enzyme luciferase in fireflies. The reaction produces oxyluciferin, carbon dioxide, and a large amount of energy, which is released as light.

Renilla luciferase, specifically, is a type of luciferase that comes from the sea pansy, Renilla reniformis. It catalyzes the oxidation of coelenterazine, a substrate derived from green algae, to produce coelenteramide, carbon dioxide, and light. The reaction takes place in the presence of oxygen and magnesium ions.

Renilla luciferase is widely used as a reporter gene in molecular biology research. A reporter gene is a gene that produces a protein that can be easily detected and measured, allowing researchers to monitor the activity of other genes or regulatory elements in a cell. In this case, when the Renilla luciferase gene is introduced into cells, the amount of light emitted by the enzyme reflects the level of expression of the gene of interest.

Homologous recombination is a type of genetic recombination that occurs between two similar or identical (homologous) segments of DNA. It is a natural process that helps to maintain the stability of an organism's genome and plays a crucial role in DNA repair, particularly the repair of double-strand breaks.

In homologous recombination, the two DNA molecules exchange genetic information through a series of steps, including the formation of Holliday junctions, where the strands cross over and exchange partners. This process can result in new combinations of genetic material, which can increase genetic diversity and contribute to evolution.

Homologous recombination is also used in biotechnology and genetic engineering to introduce specific changes into DNA sequences or to create genetically modified organisms.

A conserved sequence in the context of molecular biology refers to a pattern of nucleotides (in DNA or RNA) or amino acids (in proteins) that has remained relatively unchanged over evolutionary time. These sequences are often functionally important and are highly conserved across different species, indicating strong selection pressure against changes in these regions.

In the case of protein-coding genes, the corresponding amino acid sequence is deduced from the DNA sequence through the genetic code. Conserved sequences in proteins may indicate structurally or functionally important regions, such as active sites or binding sites, that are critical for the protein's activity. Similarly, conserved non-coding sequences in DNA may represent regulatory elements that control gene expression.

Identifying conserved sequences can be useful for inferring evolutionary relationships between species and for predicting the function of unknown genes or proteins.

I'm sorry for any confusion, but "Ubiquitin Thiolesterase" is not a widely recognized medical term or a well-defined concept in the field of medicine. Ubiquitination, however, is a post-translational modification that plays a crucial role in various cellular processes, including protein degradation and regulation of signaling pathways.

Ubiquitin Thiolesterase could potentially refer to an enzyme that catalyzes the hydrolysis of a thioester bond between ubiquitin and a target protein. This process would be part of the ubiquitination cascade, where ubiquitin is transferred from one protein to another through various intermediates, including thioester bonds. However, I would recommend consulting primary literature or speaking with an expert in the field for more precise information on this topic.

Nuclear localization signals (NLSs) are specific short sequences of amino acids in a protein that serve as a targeting signal for nuclear import. They are recognized by import receptors, which facilitate the translocation of the protein through the nuclear pore complex and into the nucleus. NLSs typically contain one or more basic residues, such as lysine or arginine, and can be monopartite (a single stretch of basic amino acids) or bipartite (two stretches of basic amino acids separated by a spacer region). Once inside the nucleus, the protein can perform its specific function, such as regulating gene expression.

A macronucleus is a large, polyploid nucleus found in certain protozoa and some algal cells. It is responsible for the majority of the cell's vegetative functions, such as gene expression and protein synthesis, and it typically contains multiple copies of the genetic material. In contrast to the micronucleus, which is a smaller, diploid nucleus that is involved in the sexual reproduction of the cell, the macronucleus does not participate in the reproductive process.

In ciliates, such as Paramecium and Tetrahymena, the macronucleus is derived from the micronucleus during a process called differentiation. The micronucleus undergoes a series of divisions and develops into a multinucleated structure, which then fragments to form multiple macronuclei. These macronuclei are retained in the vegetative cells and are essential for their survival and function.

It is important to note that not all protozoa or algal cells have both a macronucleus and a micronucleus. Some species only have a single nucleus, while others may have multiple nuclei of different types. The presence and function of these various types of nuclei can vary significantly between different groups of organisms.

A "reporter gene" is a type of gene that is linked to a gene of interest in order to make the expression or activity of that gene detectable. The reporter gene encodes for a protein that can be easily measured and serves as an indicator of the presence and activity of the gene of interest. Commonly used reporter genes include those that encode for fluorescent proteins, enzymes that catalyze colorimetric reactions, or proteins that bind to specific molecules.

In the context of genetics and genomics research, a reporter gene is often used in studies involving gene expression, regulation, and function. By introducing the reporter gene into an organism or cell, researchers can monitor the activity of the gene of interest in real-time or after various experimental treatments. The information obtained from these studies can help elucidate the role of specific genes in biological processes and diseases, providing valuable insights for basic research and therapeutic development.

The cell cycle is a series of events that take place in a cell leading to its division and duplication. It consists of four main phases: G1 phase, S phase, G2 phase, and M phase.

During the G1 phase, the cell grows in size and synthesizes mRNA and proteins in preparation for DNA replication. In the S phase, the cell's DNA is copied, resulting in two complete sets of chromosomes. During the G2 phase, the cell continues to grow and produces more proteins and organelles necessary for cell division.

The M phase is the final stage of the cell cycle and consists of mitosis (nuclear division) and cytokinesis (cytoplasmic division). Mitosis results in two genetically identical daughter nuclei, while cytokinesis divides the cytoplasm and creates two separate daughter cells.

The cell cycle is regulated by various checkpoints that ensure the proper completion of each phase before progressing to the next. These checkpoints help prevent errors in DNA replication and division, which can lead to mutations and cancer.

Proteins are complex, large molecules that play critical roles in the body's functions. They are made up of amino acids, which are organic compounds that are the building blocks of proteins. Proteins are required for the structure, function, and regulation of the body's tissues and organs. They are essential for the growth, repair, and maintenance of body tissues, and they play a crucial role in many biological processes, including metabolism, immune response, and cellular signaling. Proteins can be classified into different types based on their structure and function, such as enzymes, hormones, antibodies, and structural proteins. They are found in various foods, especially animal-derived products like meat, dairy, and eggs, as well as plant-based sources like beans, nuts, and grains.

An amino acid substitution is a type of mutation in which one amino acid in a protein is replaced by another. This occurs when there is a change in the DNA sequence that codes for a particular amino acid in a protein. The genetic code is redundant, meaning that most amino acids are encoded by more than one codon (a sequence of three nucleotides). As a result, a single base pair change in the DNA sequence may not necessarily lead to an amino acid substitution. However, if a change does occur, it can have a variety of effects on the protein's structure and function, depending on the nature of the substituted amino acids. Some substitutions may be harmless, while others may alter the protein's activity or stability, leading to disease.

Subcellular fractions refer to the separation and collection of specific parts or components of a cell, including organelles, membranes, and other structures, through various laboratory techniques such as centrifugation and ultracentrifugation. These fractions can be used in further biochemical and molecular analyses to study the structure, function, and interactions of individual cellular components. Examples of subcellular fractions include nuclear extracts, mitochondrial fractions, microsomal fractions (membrane vesicles), and cytosolic fractions (cytoplasmic extracts).

Chromosomes in fungi are thread-like structures that contain genetic material, composed of DNA and proteins, present in the nucleus of a cell. Unlike humans and other eukaryotes that have a diploid number of chromosomes in their somatic cells, fungal chromosome numbers can vary widely between and within species.

Fungal chromosomes are typically smaller and fewer in number compared to those found in plants and animals. The chromosomal organization in fungi is also different from other eukaryotes. In many fungi, the chromosomes are condensed throughout the cell cycle, whereas in other eukaryotes, chromosomes are only condensed during cell division.

Fungi can have linear or circular chromosomes, depending on the species. For example, the model organism Saccharomyces cerevisiae (budding yeast) has a set of 16 small circular chromosomes, while other fungi like Neurospora crassa (red bread mold) and Aspergillus nidulans (a filamentous fungus) have linear chromosomes.

Fungal chromosomes play an essential role in the growth, development, reproduction, and survival of fungi. They carry genetic information that determines various traits such as morphology, metabolism, pathogenicity, and resistance to environmental stresses. Advances in genomic technologies have facilitated the study of fungal chromosomes, leading to a better understanding of their structure, function, and evolution.

The Mi-2/NuRD (Nucleosome Remodeling and Deacetylase) complex is a large, multi-subunit protein complex that plays a crucial role in epigenetic regulation of gene expression. It is highly conserved across many species, including humans. The complex is named after its core ATP-dependent chromatin remodeling factor, Mi-2 (also known as CHD3 or CHD4), which can reposition, eject, or slide nucleosomes along DNA to alter the accessibility of DNA to transcription factors and other regulatory proteins.

The NuRD complex also contains several histone deacetylases (HDACs), specifically HDAC1 and HDAC2, that remove acetyl groups from histone tails, leading to a more compact chromatin structure and repression of gene transcription. Additionally, the complex includes other accessory proteins, such as MTA (Metastasis Associated) proteins, RbAP46/48 (Retinoblastoma-Associated Proteins), MBD (Methyl-CpG Binding Domain) proteins, and others.

The Mi-2/NuRD complex is involved in various cellular processes, including development, differentiation, and tumor suppression. Dysregulation of this complex has been implicated in several human diseases, particularly cancers.

Meiosis is a type of cell division that results in the formation of four daughter cells, each with half the number of chromosomes as the parent cell. It is a key process in sexual reproduction, where it generates gametes or sex cells (sperm and eggs).

The process of meiosis involves one round of DNA replication followed by two successive nuclear divisions, meiosis I and meiosis II. In meiosis I, homologous chromosomes pair, form chiasma and exchange genetic material through crossing over, then separate from each other. In meiosis II, sister chromatids separate, leading to the formation of four haploid cells. This process ensures genetic diversity in offspring by shuffling and recombining genetic information during the formation of gametes.

Gene silencing is a process by which the expression of a gene is blocked or inhibited, preventing the production of its corresponding protein. This can occur naturally through various mechanisms such as RNA interference (RNAi), where small RNAs bind to and degrade specific mRNAs, or DNA methylation, where methyl groups are added to the DNA molecule, preventing transcription. Gene silencing can also be induced artificially using techniques such as RNAi-based therapies, antisense oligonucleotides, or CRISPR-Cas9 systems, which allow for targeted suppression of gene expression in research and therapeutic applications.

Glutathione transferases (GSTs) are a group of enzymes involved in the detoxification of xenobiotics and endogenous compounds. They facilitate the conjugation of these compounds with glutathione, a tripeptide consisting of cysteine, glutamic acid, and glycine, which results in more water-soluble products that can be easily excreted from the body.

GSTs play a crucial role in protecting cells against oxidative stress and chemical injury by neutralizing reactive electrophilic species and peroxides. They are found in various tissues, including the liver, kidneys, lungs, and intestines, and are classified into several families based on their structure and function.

Abnormalities in GST activity have been associated with increased susceptibility to certain diseases, such as cancer, neurological disorders, and respiratory diseases. Therefore, GSTs have become a subject of interest in toxicology, pharmacology, and clinical research.

High Mobility Group AT-Hook 1b (HMGA1b) protein is a subtype of the HMGA1 protein, which belongs to the High Mobility Group AT-hook (HMGA) family of non-histone chromatin proteins. These proteins are characterized by their ability to bind to the minor groove of AT-rich DNA sequences and modulate chromatin structure and gene expression.

The HMGA1 protein exists in two isoforms, HMGA1a and HMGA1b, which are generated through alternative splicing of the same gene. Both isoforms share a similar structure, consisting of three AT-hook DNA binding domains and a C-terminal acidic tail. However, they differ in their N-terminal regions, with HMGA1b having a unique 29-amino acid sequence that is not present in HMGA1a.

HMGA1 proteins play important roles in various cellular processes, including transcription regulation, DNA replication, and repair. Dysregulation of HMGA1 expression has been implicated in several human diseases, such as cancer, where it can act as a potent oncogene by promoting tumor cell proliferation, migration, and invasion.

Quaternary protein structure refers to the arrangement and interaction of multiple folded protein molecules in a multi-subunit complex. These subunits can be identical or different forms of the same protein or distinctly different proteins that associate to form a functional complex. The quaternary structure is held together by non-covalent interactions, such as hydrogen bonds, ionic bonds, and van der Waals forces. Understanding quaternary structure is crucial for comprehending the function, regulation, and assembly of many protein complexes involved in various cellular processes.

A Structure-Activity Relationship (SAR) in the context of medicinal chemistry and pharmacology refers to the relationship between the chemical structure of a drug or molecule and its biological activity or effect on a target protein, cell, or organism. SAR studies aim to identify patterns and correlations between structural features of a compound and its ability to interact with a specific biological target, leading to a desired therapeutic response or undesired side effects.

By analyzing the SAR, researchers can optimize the chemical structure of lead compounds to enhance their potency, selectivity, safety, and pharmacokinetic properties, ultimately guiding the design and development of novel drugs with improved efficacy and reduced toxicity.

DNA topoisomerases are enzymes that regulate the topological state of DNA during various cellular processes such as replication, transcription, and repair. They do this by introducing temporary breaks in the DNA strands and allowing the strands to rotate around each other, thereby relieving torsional stress and supercoiling. Topoisomerases are classified into two types: type I and type II.

Type II topoisomerases are further divided into two subtypes: type IIA and type IIB. These enzymes function by forming a covalent bond with the DNA strands, cleaving them, and then passing another segment of DNA through the break before resealing the original strands. This process allows for the removal of both positive and negative supercoils from DNA as well as the separation of interlinked circular DNA molecules (catenanes) or knotted DNA structures.

Type II topoisomerases are essential for cell viability, and their dysfunction has been linked to various human diseases, including cancer and neurodegenerative disorders. They have also emerged as important targets for the development of anticancer drugs that inhibit their activity and induce DNA damage leading to cell death. Examples of type II topoisomerase inhibitors include etoposide, doxorubicin, and mitoxantrone.

DNA topoisomerases are enzymes that modify the topological structure of DNA by regulating the number of twists or supercoils in the double helix. There are two main types of DNA topoisomerases: type I and type II.

Type I DNA topoisomerases function by cutting one strand of the DNA duplex, allowing the uncut strand to rotate around the break, and then resealing the break. This process can relieve both positive and negative supercoiling in DNA, as well as introduce single-stranded breaks into the DNA molecule.

Type I topoisomerases are further divided into three subtypes: type IA, type IB, and type IC. These subtypes differ in their mechanism of action and the structure of the active site tyrosine residue that makes the transient break in the DNA strand.

Overall, DNA topoisomerases play a crucial role in many cellular processes involving DNA, including replication, transcription, recombination, and chromosome segregation. Dysregulation of these enzymes has been implicated in various human diseases, including cancer and genetic disorders.

'Drosophila proteins' refer to the proteins that are expressed in the fruit fly, Drosophila melanogaster. This organism is a widely used model system in genetics, developmental biology, and molecular biology research. The study of Drosophila proteins has contributed significantly to our understanding of various biological processes, including gene regulation, cell signaling, development, and aging.

Some examples of well-studied Drosophila proteins include:

1. HSP70 (Heat Shock Protein 70): A chaperone protein involved in protein folding and protection from stress conditions.
2. TUBULIN: A structural protein that forms microtubules, important for cell division and intracellular transport.
3. ACTIN: A cytoskeletal protein involved in muscle contraction, cell motility, and maintenance of cell shape.
4. BETA-GALACTOSIDASE (LACZ): A reporter protein often used to monitor gene expression patterns in transgenic flies.
5. ENDOGLIN: A protein involved in the development of blood vessels during embryogenesis.
6. P53: A tumor suppressor protein that plays a crucial role in preventing cancer by regulating cell growth and division.
7. JUN-KINASE (JNK): A signaling protein involved in stress response, apoptosis, and developmental processes.
8. DECAPENTAPLEGIC (DPP): A member of the TGF-Ī² (Transforming Growth Factor Beta) superfamily, playing essential roles in embryonic development and tissue homeostasis.

These proteins are often studied using various techniques such as biochemistry, genetics, molecular biology, and structural biology to understand their functions, interactions, and regulation within the cell.

Single-stranded DNA breaks (SSBs) refer to a type of DNA damage in which one strand of the double-helix structure is cleaved or broken. This kind of damage can occur spontaneously due to cellular metabolism or can be induced by various genotoxic agents, such as ionizing radiation and certain chemicals.

SSBs are typically repaired rapidly and efficiently by enzymes known as DNA repair proteins. However, if left unrepaired or misrepaired, they can lead to mutations, genomic instability, and increased risk of diseases, including cancer. In some cases, single-stranded breaks may also precede the formation of more severe double-stranded DNA breaks (DSBs).

It is important to note that while SSBs are less catastrophic than DSBs, they still play a significant role in genome maintenance and cellular health.

Proteasome inhibitors are a class of medications that work by blocking the action of proteasomes, which are protein complexes that play a critical role in the breakdown and recycling of damaged or unwanted proteins within cells. By inhibiting the activity of these proteasomes, proteasome inhibitors can cause an accumulation of abnormal proteins within cells, leading to cell death.

This effect is particularly useful in the treatment of certain types of cancer, such as multiple myeloma and mantle cell lymphoma, where malignant cells often have an overproduction of abnormal proteins that can be targeted by proteasome inhibitors. The three main proteasome inhibitors currently approved for use in cancer therapy are bortezomib (Velcade), carfilzomib (Kyprolis), and ixazomib (Ninlaro). These medications have been shown to improve outcomes and extend survival in patients with these types of cancers.

It's important to note that proteasome inhibitors can also have off-target effects on other cells in the body, leading to side effects such as neurotoxicity, gastrointestinal symptoms, and hematologic toxicities. Therefore, careful monitoring and management of these side effects is necessary during treatment with proteasome inhibitors.

The nuclear envelope is a complex and double-membrane structure that surrounds the eukaryotic cell's nucleus. It consists of two distinct membranes: the outer nuclear membrane, which is continuous with the endoplasmic reticulum (ER) membrane, and the inner nuclear membrane, which is closely associated with the chromatin and nuclear lamina.

The nuclear envelope serves as a selective barrier between the nucleus and the cytoplasm, controlling the exchange of materials and information between these two cellular compartments. Nuclear pore complexes (NPCs) are embedded in the nuclear envelope at sites where the inner and outer membranes fuse, forming aqueous channels that allow for the passive or active transport of molecules, such as ions, metabolites, and RNA-protein complexes.

The nuclear envelope plays essential roles in various cellular processes, including DNA replication, transcription, RNA processing, and chromosome organization. Additionally, it is dynamically regulated during the cell cycle, undergoing disassembly and reformation during mitosis to facilitate equal distribution of genetic material between daughter cells.

Co-repressor proteins are regulatory molecules that bind to DNA-bound transcription factors, forming a complex that prevents the transcription of genes. These proteins function to repress gene expression by inhibiting the recruitment of RNA polymerase or other components required for transcription. They can be recruited directly by transcription factors or through interactions with other corepressor molecules.

Co-repressors often possess enzymatic activity, such as histone deacetylase (HDAC) or methyltransferase activity, which modifies histone proteins and condenses chromatin structure, making it less accessible to the transcription machinery. This results in a decrease in gene expression.

Examples of co-repressor proteins include:

1. Histone deacetylases (HDACs): These enzymes remove acetyl groups from histone proteins, leading to chromatin condensation and transcriptional repression.
2. Nucleosome remodeling and histone deacetylation (NuRD) complex: This multi-protein complex contains HDACs, histone demethylases, and ATP-dependent chromatin remodeling proteins that work together to repress gene expression.
3. Sin3A/Sin3B: These are corepressor proteins that interact with various transcription factors and recruit HDACs to specific genomic loci for transcriptional repression.
4. CoREST (Co-Repressor of RE1 Silencing Transcription factor): This is a complex containing HDACs, LSD1 (lysine-specific demethylase 1), and other proteins that mediate transcriptional repression through histone modifications.
5. CtBP (C-terminal binding protein): These are co-repressors that interact with various transcription factors and recruit HDACs, leading to chromatin condensation and gene silencing.

These co-repressor proteins play crucial roles in various cellular processes, including development, differentiation, and homeostasis, by fine-tuning gene expression patterns. Dysregulation of these proteins has been implicated in several diseases, such as cancer and neurological disorders.

An Electrophoretic Mobility Shift Assay (EMSA) is a laboratory technique used to detect and analyze protein-DNA interactions. In this assay, a mixture of proteins and fluorescently or radioactively labeled DNA probes are loaded onto a native polyacrylamide gel matrix and subjected to an electric field. The negatively charged DNA probe migrates towards the positive electrode, and the rate of migration (mobility) is dependent on the size and charge of the molecule. When a protein binds to the DNA probe, it forms a complex that has a different size and/or charge than the unbound probe, resulting in a shift in its mobility on the gel.

The EMSA can be used to identify specific protein-DNA interactions, determine the binding affinity of proteins for specific DNA sequences, and investigate the effects of mutations or post-translational modifications on protein-DNA interactions. The technique is widely used in molecular biology research, including studies of gene regulation, DNA damage repair, and epigenetic modifications.

In summary, Electrophoretic Mobility Shift Assay (EMSA) is a laboratory technique that detects and analyzes protein-DNA interactions by subjecting a mixture of proteins and labeled DNA probes to an electric field in a native polyacrylamide gel matrix. The binding of proteins to the DNA probe results in a shift in its mobility on the gel, allowing for the detection and analysis of specific protein-DNA interactions.

Deoxyribonucleic acid (DNA) is the genetic material present in the cells of organisms where it is responsible for the storage and transmission of hereditary information. DNA is a long molecule that consists of two strands coiled together to form a double helix. Each strand is made up of a series of four nucleotide bases - adenine (A), guanine (G), cytosine (C), and thymine (T) - that are linked together by phosphate and sugar groups. The sequence of these bases along the length of the molecule encodes genetic information, with A always pairing with T and C always pairing with G. This base-pairing allows for the replication and transcription of DNA, which are essential processes in the functioning and reproduction of all living organisms.

Immediate-early proteins (IEPs) are a class of regulatory proteins that play a crucial role in the early stages of gene expression in viral infection and cellular stress responses. These proteins are synthesized rapidly, without the need for new protein synthesis, after the induction of immediate-early genes (IEGs).

In the context of viral infection, IEPs are often the first proteins produced by the virus upon entry into the host cell. They function as transcription factors that bind to specific DNA sequences and regulate the expression of early and late viral genes required for replication and packaging of the viral genome.

IEPs can also be involved in modulating host cell signaling pathways, altering cell cycle progression, and inducing apoptosis (programmed cell death). Dysregulation of IEPs has been implicated in various diseases, including cancer and neurological disorders.

It is important to note that the term "immediate-early proteins" is primarily used in the context of viral infection, while in other contexts such as cellular stress responses or oncogene activation, these proteins may be referred to by different names, such as "early response genes" or "transcription factors."

Nuclear export signals (NES) are short, specific amino acid sequences that target proteins for transport from the nucleus to the cytoplasm through the nuclear pore complex. They are recognized by members of the karyopherin-Ī² family, such as CRM1 (chromosome region maintenance 1), which bind to the NES and facilitate the translocation of the protein across the nuclear envelope. The NES typically consists of a leucine-rich motif, although other hydrophobic amino acids may also be present. Proteins containing NES are often involved in various cellular processes, including signal transduction, gene expression regulation, and cell cycle control.

Septins are a group of GTP-binding proteins that play a crucial role in the organization of cell membranes and cytoskeleton. They are involved in various cellular processes, including cell division, polarity establishment, and regulation of the actin cytoskeleton. In mammalian cells, there are 13 different septin proteins that can assemble into hetero-oligomeric complexes to form higher-order structures such as filaments and rings. Septins have been implicated in several human diseases, including cancer, neurodegenerative disorders, and infectious diseases.

Matrix Attachment Regions (MARs) are specific DNA sequences that are involved in the attachment of chromatin to the nuclear matrix. The nuclear matrix is a protein structure within the nucleus of a cell, which provides a framework for the organization and function of genetic material. MARs are believed to play a role in the spatial organization of chromosomes within the nucleus, as well as in the regulation of gene expression. They can serve as binding sites for various proteins and enzymes that are involved in DNA replication, transcription, and repair. The precise mechanisms by which MARs function are still being studied and elucidated.

Biocatalysis is the use of living organisms or their components, such as enzymes, to accelerate chemical reactions. In other words, it is the process by which biological systems, including cells, tissues, and organs, catalyze chemical transformations. Biocatalysts, such as enzymes, can increase the rate of a reaction by lowering the activation energy required for the reaction to occur. They are highly specific and efficient, making them valuable tools in various industries, including pharmaceuticals, food and beverage, and biofuels.

In medicine, biocatalysis is used in the production of drugs, such as antibiotics and hormones, as well as in diagnostic tests. Enzymes are also used in medical treatments, such as enzyme replacement therapy for genetic disorders that affect enzyme function. Overall, biocatalysis plays a critical role in many areas of medicine and healthcare.

Prophase is the first phase of mitosis, the process by which eukaryotic cells divide and reproduce. During prophase, the chromosomes condense and become visible. The nuclear envelope breaks down, allowing the spindle fibers to attach to the centromeres of each chromatid in the chromosome. This is a critical step in preparing for the separation of genetic material during cell division. Prophase is also marked by the movement of the centrosomes to opposite poles of the cell, forming the mitotic spindle.

Heterochromatin is a type of chromatin (the complex of DNA, RNA, and proteins that make up chromosomes) that is characterized by its tightly packed structure and reduced genetic activity. It is often densely stained with certain dyes due to its high concentration of histone proteins and other chromatin-associated proteins. Heterochromatin can be further divided into two subtypes: constitutive heterochromatin, which is consistently highly condensed and transcriptionally inactive throughout the cell cycle, and facultative heterochromatin, which can switch between a condensed, inactive state and a more relaxed, active state depending on the needs of the cell. Heterochromatin plays important roles in maintaining the stability and integrity of the genome by preventing the transcription of repetitive DNA sequences and protecting against the spread of transposable elements.

Luciferases are a class of enzymes that catalyze the oxidation of their substrates, leading to the emission of light. This bioluminescent process is often associated with certain species of bacteria, insects, and fish. The term "luciferase" comes from the Latin word "lucifer," which means "light bearer."

The most well-known example of luciferase is probably that found in fireflies, where the enzyme reacts with a compound called luciferin to produce light. This reaction requires the presence of oxygen and ATP (adenosine triphosphate), which provides the energy needed for the reaction to occur.

Luciferases have important applications in scientific research, particularly in the development of sensitive assays for detecting gene expression and protein-protein interactions. By labeling a protein or gene of interest with luciferase, researchers can measure its activity by detecting the light emitted during the enzymatic reaction. This allows for highly sensitive and specific measurements, making luciferases valuable tools in molecular biology and biochemistry.

Genetic recombination is the process by which genetic material is exchanged between two similar or identical molecules of DNA during meiosis, resulting in new combinations of genes on each chromosome. This exchange occurs during crossover, where segments of DNA are swapped between non-sister homologous chromatids, creating genetic diversity among the offspring. It is a crucial mechanism for generating genetic variability and facilitating evolutionary change within populations. Additionally, recombination also plays an essential role in DNA repair processes through mechanisms such as homologous recombinational repair (HRR) and non-homologous end joining (NHEJ).

Hep G2 cells are a type of human liver cancer cell line that were isolated from a well-differentiated hepatocellular carcinoma (HCC) in a patient with hepatitis C virus (HCV) infection. These cells have the ability to grow and divide indefinitely in culture, making them useful for research purposes. Hep G2 cells express many of the same markers and functions as normal human hepatocytes, including the ability to take up and process lipids and produce bile. They are often used in studies related to hepatitis viruses, liver metabolism, drug toxicity, and cancer biology. It is important to note that Hep G2 cells are tumorigenic and should be handled with care in a laboratory setting.

Gene knockdown techniques are methods used to reduce the expression or function of specific genes in order to study their role in biological processes. These techniques typically involve the use of small RNA molecules, such as siRNAs (small interfering RNAs) or shRNAs (short hairpin RNAs), which bind to and promote the degradation of complementary mRNA transcripts. This results in a decrease in the production of the protein encoded by the targeted gene.

Gene knockdown techniques are often used as an alternative to traditional gene knockout methods, which involve completely removing or disrupting the function of a gene. Knockdown techniques allow for more subtle and reversible manipulation of gene expression, making them useful for studying genes that are essential for cell survival or have redundant functions.

These techniques are widely used in molecular biology research to investigate gene function, genetic interactions, and disease mechanisms. However, it is important to note that gene knockdown can have off-target effects and may not completely eliminate the expression of the targeted gene, so results should be interpreted with caution.

SOX (SRY-related HMG box) transcription factors are a family of proteins that regulate gene expression during embryonic development and in adult tissues. They contain a highly conserved DNA-binding domain, the HMG box, which allows them to bind to specific DNA sequences and influence the transcription of nearby genes. SOX proteins play critical roles in various biological processes such as cell fate determination, differentiation, proliferation, and survival.

SOX transcription factors are classified into several groups (A-H) based on their sequence similarities and functional redundancies. Some well-known members of this family include SOX1, SOX2, SOX3, SOX4, SOX9, SOX10, and SOX17. These proteins often form complexes with other transcription factors or cofactors to modulate their target genes' expression.

Dysregulation of SOX transcription factors has been implicated in several human diseases, including cancer, developmental disorders, and degenerative conditions. For example, SOX2 overexpression is associated with certain types of tumors, while mutations in the SOX9 gene can cause campomelic dysplasia, a severe skeletal disorder.

A gene fusion, also known as a chromosomal translocation or fusion gene, is an abnormal genetic event where parts of two different genes combine to create a single, hybrid gene. This can occur due to various mechanisms such as chromosomal rearrangements, deletions, or inversions, leading to the formation of a chimeric gene with new and often altered functions.

Gene fusions can result in the production of abnormal fusion proteins that may contribute to cancer development and progression by promoting cell growth, inhibiting apoptosis (programmed cell death), or activating oncogenic signaling pathways. In some cases, gene fusions are specific to certain types of cancer and serve as valuable diagnostic markers and therapeutic targets for personalized medicine.

The Heat-Shock Response is a complex and highly conserved stress response mechanism present in virtually all living organisms. It is activated when the cell encounters elevated temperatures or other forms of proteotoxic stress, such as exposure to toxins, radiation, or infectious agents. This response is primarily mediated by a group of proteins known as heat-shock proteins (HSPs) or chaperones, which play crucial roles in protein folding, assembly, transport, and degradation.

The primary function of the Heat-Shock Response is to protect the cell from damage caused by misfolded or aggregated proteins that can accumulate under stress conditions. The activation of this response leads to the rapid transcription and translation of HSP genes, resulting in a significant increase in the intracellular levels of these chaperone proteins. These chaperones then assist in the refolding of denatured proteins or target damaged proteins for degradation via the proteasome or autophagy pathways.

The Heat-Shock Response is critical for maintaining cellular homeostasis and ensuring proper protein function under stress conditions. Dysregulation of this response has been implicated in various diseases, including neurodegenerative disorders, cancer, and cardiovascular diseases.

Fungal proteins are a type of protein that is specifically produced and present in fungi, which are a group of eukaryotic organisms that include microorganisms such as yeasts and molds. These proteins play various roles in the growth, development, and survival of fungi. They can be involved in the structure and function of fungal cells, metabolism, pathogenesis, and other cellular processes. Some fungal proteins can also have important implications for human health, both in terms of their potential use as therapeutic targets and as allergens or toxins that can cause disease.

Fungal proteins can be classified into different categories based on their functions, such as enzymes, structural proteins, signaling proteins, and toxins. Enzymes are proteins that catalyze chemical reactions in fungal cells, while structural proteins provide support and protection for the cell. Signaling proteins are involved in communication between cells and regulation of various cellular processes, and toxins are proteins that can cause harm to other organisms, including humans.

Understanding the structure and function of fungal proteins is important for developing new treatments for fungal infections, as well as for understanding the basic biology of fungi. Research on fungal proteins has led to the development of several antifungal drugs that target specific fungal enzymes or other proteins, providing effective treatment options for a range of fungal diseases. Additionally, further study of fungal proteins may reveal new targets for drug development and help improve our ability to diagnose and treat fungal infections.

Cysteine is a semi-essential amino acid, which means that it can be produced by the human body under normal circumstances, but may need to be obtained from external sources in certain conditions such as illness or stress. Its chemical formula is HO2CCH(NH2)CH2SH, and it contains a sulfhydryl group (-SH), which allows it to act as a powerful antioxidant and participate in various cellular processes.

Cysteine plays important roles in protein structure and function, detoxification, and the synthesis of other molecules such as glutathione, taurine, and coenzyme A. It is also involved in wound healing, immune response, and the maintenance of healthy skin, hair, and nails.

Cysteine can be found in a variety of foods, including meat, poultry, fish, dairy products, eggs, legumes, nuts, seeds, and some grains. It is also available as a dietary supplement and can be used in the treatment of various medical conditions such as liver disease, bronchitis, and heavy metal toxicity. However, excessive intake of cysteine may have adverse effects on health, including gastrointestinal disturbances, nausea, vomiting, and headaches.

RNA interference (RNAi) is a biological process in which RNA molecules inhibit the expression of specific genes. This process is mediated by small RNA molecules, including microRNAs (miRNAs) and small interfering RNAs (siRNAs), that bind to complementary sequences on messenger RNA (mRNA) molecules, leading to their degradation or translation inhibition.

RNAi plays a crucial role in regulating gene expression and defending against foreign genetic elements, such as viruses and transposons. It has also emerged as an important tool for studying gene function and developing therapeutic strategies for various diseases, including cancer and viral infections.

The Fluorescent Antibody Technique (FAT) is a type of immunofluorescence assay used in laboratory medicine and pathology for the detection and localization of specific antigens or antibodies in tissues, cells, or microorganisms. In this technique, a fluorescein-labeled antibody is used to selectively bind to the target antigen or antibody, forming an immune complex. When excited by light of a specific wavelength, the fluorescein label emits light at a longer wavelength, typically visualized as green fluorescence under a fluorescence microscope.

The FAT is widely used in diagnostic microbiology for the identification and characterization of various bacteria, viruses, fungi, and parasites. It has also been applied in the diagnosis of autoimmune diseases and certain cancers by detecting specific antibodies or antigens in patient samples. The main advantage of FAT is its high sensitivity and specificity, allowing for accurate detection and differentiation of various pathogens and disease markers. However, it requires specialized equipment and trained personnel to perform and interpret the results.

Zinc fingers are a type of protein structural motif involved in specific DNA binding and, by extension, in the regulation of gene expression. They are so named because of their characteristic "finger-like" shape that is formed when a zinc ion binds to the amino acids within the protein. This structure allows the protein to interact with and recognize specific DNA sequences, thereby playing a crucial role in various biological processes such as transcription, repair, and recombination of genetic material.

Molecular cloning is a laboratory technique used to create multiple copies of a specific DNA sequence. This process involves several steps:

1. Isolation: The first step in molecular cloning is to isolate the DNA sequence of interest from the rest of the genomic DNA. This can be done using various methods such as PCR (polymerase chain reaction), restriction enzymes, or hybridization.
2. Vector construction: Once the DNA sequence of interest has been isolated, it must be inserted into a vector, which is a small circular DNA molecule that can replicate independently in a host cell. Common vectors used in molecular cloning include plasmids and phages.
3. Transformation: The constructed vector is then introduced into a host cell, usually a bacterial or yeast cell, through a process called transformation. This can be done using various methods such as electroporation or chemical transformation.
4. Selection: After transformation, the host cells are grown in selective media that allow only those cells containing the vector to grow. This ensures that the DNA sequence of interest has been successfully cloned into the vector.
5. Amplification: Once the host cells have been selected, they can be grown in large quantities to amplify the number of copies of the cloned DNA sequence.

Molecular cloning is a powerful tool in molecular biology and has numerous applications, including the production of recombinant proteins, gene therapy, functional analysis of genes, and genetic engineering.

Recombinational DNA repair is a biological process that takes place in cells to correct damage to the DNA molecule. This type of repair is particularly important in maintaining the stability and integrity of the genetic code, especially in response to double-strand breaks (DSBs) in the DNA.

In recombinational DNA repair, the cell uses a template from a homologous DNA sequence, typically a sister chromatid, to restore the damaged region. The process involves several steps:

1. Resection: The broken ends of the DNA molecule are processed by enzymes that remove nucleotides and create 3' single-stranded overhangs.
2. Recombination: The single-stranded overhangs invade a homologous DNA sequence, forming a displacement loop (D-loop) structure. This invasion is facilitated by recombinase proteins such as Rad51 and Dmc1.
3. Strand exchange: The invading 3' end of the single strand pairs with the complementary sequence in the template DNA, and DNA synthesis occurs using the template to restore the missing genetic information.
4. Resolution: The recombination intermediate is resolved, and the repaired DNA molecule is ligated together. This step can result in different outcomes, including crossover or non-crossover events, depending on the specific mechanisms involved.

Recombinational DNA repair plays a crucial role in maintaining genome stability and preventing mutations that could lead to diseases such as cancer. Additionally, this process is exploited in genetic engineering techniques like homologous recombination-mediated gene targeting and CRISPR-Cas9 genome editing.

NCOR1 (Nuclear Receptor Co-Repressor 1) is a corepressor protein that interacts with nuclear receptors and other transcription factors to regulate gene expression. It functions as a part of large multiprotein complexes, which also include histone deacetylases (HDACs), to mediate the repression of gene transcription. NCOR1 is involved in various cellular processes, including development, differentiation, and metabolism. Mutations in the NCOR1 gene have been associated with certain genetic disorders, such as Rubinstein-Taybi syndrome.

Gene expression regulation in fungi refers to the complex cellular processes that control the production of proteins and other functional gene products in response to various internal and external stimuli. This regulation is crucial for normal growth, development, and adaptation of fungal cells to changing environmental conditions.

In fungi, gene expression is regulated at multiple levels, including transcriptional, post-transcriptional, translational, and post-translational modifications. Key regulatory mechanisms include:

1. Transcription factors (TFs): These proteins bind to specific DNA sequences in the promoter regions of target genes and either activate or repress their transcription. Fungi have a diverse array of TFs that respond to various signals, such as nutrient availability, stress, developmental cues, and quorum sensing.
2. Chromatin remodeling: The organization and compaction of DNA into chromatin can influence gene expression. Fungi utilize ATP-dependent chromatin remodeling complexes and histone modifying enzymes to alter chromatin structure, thereby facilitating or inhibiting the access of transcriptional machinery to genes.
3. Non-coding RNAs: Small non-coding RNAs (sncRNAs) play a role in post-transcriptional regulation of gene expression in fungi. These sncRNAs can guide RNA-induced transcriptional silencing (RITS) complexes to specific target loci, leading to the repression of gene expression through histone modifications and DNA methylation.
4. Alternative splicing: Fungi employ alternative splicing mechanisms to generate multiple mRNA isoforms from a single gene, thereby increasing proteome diversity. This process can be regulated by RNA-binding proteins that recognize specific sequence motifs in pre-mRNAs and promote or inhibit splicing events.
5. Protein stability and activity: Post-translational modifications (PTMs) of proteins, such as phosphorylation, ubiquitination, and sumoylation, can influence their stability, localization, and activity. These PTMs play a crucial role in regulating various cellular processes, including signal transduction, stress response, and cell cycle progression.

Understanding the complex interplay between these regulatory mechanisms is essential for elucidating the molecular basis of fungal development, pathogenesis, and drug resistance. This knowledge can be harnessed to develop novel strategies for combating fungal infections and improving agricultural productivity.

Signal Transducer and Activator of Transcription 1 (STAT1) is a transcription factor that plays a crucial role in the regulation of gene expression in response to cytokines and interferons. It is activated through phosphorylation by Janus kinases (JAKs) upon binding of cytokines to their respective receptors. Once activated, STAT1 forms homodimers or heterodimers with other STAT family members, translocates to the nucleus, and binds to specific DNA sequences called gamma-activated sites (GAS) in the promoter regions of target genes. This results in the modulation of gene expression involved in various cellular processes such as immune responses, differentiation, apoptosis, and cell cycle control. STAT1 also plays a critical role in the antiviral response by mediating the transcription of interferon-stimulated genes (ISGs).

Leupeptins are a type of protease inhibitors, which are substances that can inhibit the activity of enzymes called proteases. Proteases play a crucial role in breaking down proteins into smaller peptides or individual amino acids. Leupeptins are naturally occurring compounds found in some types of bacteria and are often used in laboratory research to study various cellular processes that involve protease activity.

Leupeptins can inhibit several different types of proteases, including serine proteases, cysteine proteases, and some metalloproteinases. They work by binding to the active site of these enzymes and preventing them from cleaving their protein substrates. Leupeptins have been used in various research applications, such as studying protein degradation, signal transduction pathways, and cell death mechanisms.

It is important to note that leupeptins are not typically used as therapeutic agents in clinical medicine due to their potential toxicity and lack of specificity for individual proteases. Instead, they are primarily used as research tools in basic science investigations.

'Escherichia coli' (E. coli) is a type of gram-negative, facultatively anaerobic, rod-shaped bacterium that commonly inhabits the intestinal tract of humans and warm-blooded animals. It is a member of the family Enterobacteriaceae and one of the most well-studied prokaryotic model organisms in molecular biology.

While most E. coli strains are harmless and even beneficial to their hosts, some serotypes can cause various forms of gastrointestinal and extraintestinal illnesses in humans and animals. These pathogenic strains possess virulence factors that enable them to colonize and damage host tissues, leading to diseases such as diarrhea, urinary tract infections, pneumonia, and sepsis.

E. coli is a versatile organism with remarkable genetic diversity, which allows it to adapt to various environmental niches. It can be found in water, soil, food, and various man-made environments, making it an essential indicator of fecal contamination and a common cause of foodborne illnesses. The study of E. coli has contributed significantly to our understanding of fundamental biological processes, including DNA replication, gene regulation, and protein synthesis.

Acute Promyelocytic Leukemia (APL) is a specific subtype of acute myeloid leukemia (AML), a cancer of the blood and bone marrow. It is characterized by the accumulation of abnormal promyelocytes, which are immature white blood cells, in the bone marrow and blood. These abnormal cells are produced due to a genetic mutation that involves the retinoic acid receptor alpha (RARA) gene on chromosome 17, often as a result of a translocation with the promyelocytic leukemia (PML) gene on chromosome 15 [t(15;17)]. This genetic alteration disrupts the normal differentiation and maturation process of the promyelocytes, leading to their uncontrolled proliferation and impaired function.

APL typically presents with symptoms related to decreased blood cell production, such as anemia (fatigue, weakness, shortness of breath), thrombocytopenia (easy bruising, bleeding, or petechiae), and neutropenia (increased susceptibility to infections). Additionally, APL is often associated with a high risk of disseminated intravascular coagulation (DIC), a serious complication characterized by abnormal blood clotting and bleeding.

The treatment for Acute Promyelocytic Leukemia typically involves a combination of chemotherapy and all-trans retinoic acid (ATRA) or arsenic trioxide (ATO) therapy, which target the specific genetic alteration in APL cells. This approach has significantly improved the prognosis for patients with this disease, with many achieving long-term remission and even cures.

Karyopherins are a group of proteins involved in the nuclear transport of molecules across the nuclear envelope. They are responsible for recognizing and binding to specific signal sequences, known as nuclear localization signals (NLS) or nuclear export signals (NES), on cargo proteins. This interaction allows the karyopherin-cargo complex to be translocated through the nuclear pore complex (NPC) by either importin-Ī² or exportin-Ī² karyopherins, respectively. After the transport is complete, the cargo is released and the karyopherin is recycled back to the cytoplasm. This process plays a crucial role in regulating various cellular activities such as gene expression, DNA replication, and signal transduction.

Down-regulation is a process that occurs in response to various stimuli, where the number or sensitivity of cell surface receptors or the expression of specific genes is decreased. This process helps maintain homeostasis within cells and tissues by reducing the ability of cells to respond to certain signals or molecules.

In the context of cell surface receptors, down-regulation can occur through several mechanisms:

1. Receptor internalization: After binding to their ligands, receptors can be internalized into the cell through endocytosis. Once inside the cell, these receptors may be degraded or recycled back to the cell surface in smaller numbers.
2. Reduced receptor synthesis: Down-regulation can also occur at the transcriptional level, where the expression of genes encoding for specific receptors is decreased, leading to fewer receptors being produced.
3. Receptor desensitization: Prolonged exposure to a ligand can lead to a decrease in receptor sensitivity or affinity, making it more difficult for the cell to respond to the signal.

In the context of gene expression, down-regulation refers to the decreased transcription and/or stability of specific mRNAs, leading to reduced protein levels. This process can be induced by various factors, including microRNA (miRNA)-mediated regulation, histone modification, or DNA methylation.

Down-regulation is an essential mechanism in many physiological processes and can also contribute to the development of several diseases, such as cancer and neurodegenerative disorders.

Hydroxyurea is an antimetabolite drug that is primarily used in the treatment of myeloproliferative disorders such as chronic myelogenous leukemia (CML), essential thrombocythemia, and polycythemia vera. It works by interfering with the synthesis of DNA, which inhibits the growth of cancer cells.

In addition to its use in cancer therapy, hydroxyurea is also used off-label for the management of sickle cell disease. In this context, it helps to reduce the frequency and severity of painful vaso-occlusive crises by increasing the production of fetal hemoglobin (HbF), which decreases the formation of sickled red blood cells.

The medical definition of hydroxyurea is:

A hydantoin derivative and antimetabolite that inhibits ribonucleoside diphosphate reductase, thereby interfering with DNA synthesis. It has been used as an antineoplastic agent, particularly in the treatment of myeloproliferative disorders, and more recently for the management of sickle cell disease to reduce the frequency and severity of painful vaso-occlusive crises by increasing fetal hemoglobin production.

"Drosophila" is a genus of small flies, also known as fruit flies. The most common species used in scientific research is "Drosophila melanogaster," which has been a valuable model organism for many areas of biological and medical research, including genetics, developmental biology, neurobiology, and aging.

The use of Drosophila as a model organism has led to numerous important discoveries in genetics and molecular biology, such as the identification of genes that are associated with human diseases like cancer, Parkinson's disease, and obesity. The short reproductive cycle, large number of offspring, and ease of genetic manipulation make Drosophila a powerful tool for studying complex biological processes.

... centrosomal protein 76), and APP (Amyloid-beta precursor protein). There are no paralogs for KIAA1143 KIAA1143 has homologs in ... "GPS SUMO for KIAA1143". Retrieved 16 December 2022. "YinOYang Analysis". Retrieved 16 December 2022. "Myhits Motif scan". ... The KIAA1143 protein belongs to the uncharacterized protein KIAA1143-like Family, and contains DUF4604 domain of unknown ... KIAA1143 is an uncharacterized protein in humans that is encoded by the KIAA1143 gene. it may play a role in cell growth ...
"The Human Protein Atlas". www.proteinatlas.org. Retrieved 2017-05-07. "STRING: functional protein association networks". string ... "GPS-SUMO 2.0 Online Service". sumosp.biocuckoo.org/online.php. Retrieved May 5, 2017. la Cour T, Kiemer L, MĆølgaard A, Gupta R ... "C21orf62 Gene - GeneCards , CU062 Protein , CU062 Antibody". www.genecards.org. Retrieved 2017-05-07. "Home - Protein - NCBI". ... C21orf62 is a protein that, in humans, is encoded by the C21orf62 gene. C21orf62 is found on human chromosome 21, and it is ...
... maltose-binding protein) to increase the protein's solubility. SUMO can later be cleaved from the protein of interest using a ... one of a small number of E3 ligating proteins attaches it to the protein. In yeast, there are four SUMO E3 proteins, Cst9, ... SUMO-2, SUMO-3 and SUMO-4. At the amino acid level, SUMO1 is about 50% identical to SUMO2.[citation needed] SUMO-2/3 show a ... SUMO protein has a unique N-terminal extension of 10-25 amino acids which other ubiquitin-like proteins do not have. This N- ...
E3 SUMO-protein ligase PIAS2 is an enzyme that in humans is encoded by the PIAS2 gene. Protein inhibitor of activated STAT2 has ... androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability ... Tussie-Luna MI, Michel B, Hakre S, Roy AL (2003). "The SUMO ubiquitin-protein isopeptide ligase family member Miz1/PIASxbeta / ... protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional ...
E3 SUMO-protein ligase PIAS1 is an enzyme that in humans is encoded by the PIAS1 gene. This gene encodes a member of the ... "PIAS proteins promote SUMO-1 conjugation to STAT1". Blood. 102 (9): 3311-3313. doi:10.1182/blood-2002-12-3816. PMID 12855578. ... and glycine-rich protein 2 (CRP2) is a novel marker of hepatic stellate cells and binding partner of the protein inhibitor of ... protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional ...
2004). "A proteomic study of SUMO-2 target proteins". J. Biol. Chem. 279 (32): 33791-8. doi:10.1074/jbc.M404201200. PMID ... The two encoded proteins are thought to be involved in the regulation of proliferation. Both proteins have tumor-rejection ... This gene encodes two proteins, the SART1(800) protein expressed in the nucleus of the majority of proliferating cells, and the ... The SART1(259) protein is found to be essential for the recruitment of the tri-snRNP to the pre-spliceosome in the spliceosome ...
"A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957-68. doi:10.1016/j.cell ... Minty A, Dumont X, Kaghad M, Caput D (Nov 2000). "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 ... This protein is one of the components of a histone deacetylase complex referred to as the Mi-2/NuRD complex which participates ... Chromodomain-helicase-DNA-binding protein 3 is an enzyme that in humans is encoded by the CHD3 gene. This gene encodes a member ...
Homeodomain-interacting protein kinase 3 is an enzyme that in humans is encoded by the HIPK3 gene. GRCh38: Ensembl release 89: ... Minty A, Dumont X, Kaghad M, Caput D (2000). "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 ... Kim YH, Choi CY, Lee SJ, Conti MA, Kim Y (Nov 1998). "Homeodomain-interacting protein kinases, a novel family of co-repressors ... Nupponen NN, Visakorpi T (2000). "Assignment of the protein kinase homolog of YAK1 (HIPK3) to human chromosome band 11p13 by in ...
... or transformation-related protein 53 (TRP53) is a regulatory protein that is often mutated in human cancers. The p53 proteins ( ... Minty A, Dumont X, Kaghad M, Caput D (November 2000). "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with ... All these p53 proteins are called the p53 isoforms. These proteins range in size from 3.5 to 43.7 kDa. Several isoforms were ... Mutant p53 proteins often fail to induce MDM2, causing p53 to accumulate at very high levels. Moreover, the mutant p53 protein ...
Several bacterial proteins have strong sequence homology with this protein. The protein encoded by this gene belongs to the TDG ... Minty A, Dumont X, Kaghad M, Caput D (November 2000). "Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with ... 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins ... Shimizu Y, Iwai S, Hanaoka F, Sugasawa K (2003). "Xeroderma pigmentosum group C protein interacts physically and functionally ...
CCDC166 is predicted to be regulated by SUMO protein. It has a conserved IKAD sequence at amino acid 220-223. This combined ... The pI of the protein is 10.537. The protein has several amino acid repeat structures including; EREA, VQSL and (T)QLLH, all of ... The composition of the protein reveals that it is high in serine, lysine, and arginine. The protein contains three conserved ... The function of the protein is currently unknown. The gene has been found to interact with FAT3, a tumor suppressor gene, as ...
... proteins can bind to modify the protein's function. SUMO proteins may modify proteins to perform many functions, including ... including zinc-finger proteins. C8orf34 protein undergoes few modifications following translation. C8orf34 protein is not ... The nearest protein-encoding gene to C8orf34 is PREX2, a guanine-nucleotide exchange factor for the Rac family of G proteins. ... Proteins with this domain are subunits of a multimer protein kinase. The negatively-charged region within the middle of the ...
... is a protein that in humans is encoded by the NIN gene. Ninein, together with its paralog Ninein-like protein is one of ... 2006). "SUMO-1 modification of centrosomal protein hNinein promotes hNinein nuclear localization". Life Sci. 78 (10): 1114-20. ... 2004). "NIN, a gene encoding a CEP110-like centrosomal protein, is fused to PDGFRB in a patient with a t(5;14)(q33;q24) and an ... Localization of this protein to the centrosome requires three leucine zippers in the central coiled-coil domain. Multiple ...
"Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". J. Biol. Chem. 276 (38): ... Lois LM, Lima CD (2005). "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1 ... "Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1". J. Biol. Chem. 274 (15): ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/ ...
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It is a ubiquitin-like ... "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". The Journal of Biological ... "In vitro modification of human centromere protein CENP-C fragments by small ubiquitin-like modifier (SUMO) protein: definitive ... SUMO) family members, SUMO-2 and SUMO-3". The Journal of Biological Chemistry. 278 (35): 33416-21. doi:10.1074/jbc.M305680200. ...
... transfer of SUMO protein to other proteins). The Small Ubiquitin-related Modifier, SUMO-1, is a ubiquitin-like family member ... SUMO pathway modifies hundreds of proteins that participate in diverse cellular processes. SUMO pathway is the most studied ... Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382 (2004) Melchior, F. SUMO-nonclassical ubiquitin. Annu. Rev. Cell ... Protein modification by SUMO. Annu Rev Biochem 2004;73:355-82 O. Kerscher, R. Felberbaum and M. Hochstrasser, Modification of ...
"Quantitative analysis of multiā€protein interactions using FRET: Application to the SUMO pathway." Protein Science 17.4 (2008): ... Protein-protein docking, the prediction of protein-protein interactions based only on the three-dimensional protein structures ... Bio-layer interferometry (BLI) is a label-free technology for measuring biomolecular interactions (protein:protein or protein: ... Fluorescence polarization/anisotropy can be used to measure protein-protein or protein-ligand interactions. Typically one ...
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It is a ubiquitin-like ... a human ubiquitin-like protein associating with human RAD51/RAD52 proteins". Genomics. 36 (2): 271-9. doi:10.1006/geno. ... "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi: ... SUMO 1 may be an important therapeutic target to help improve cardiac performance in patients with heart failure. In a mouse ...
Small ubiquitin-related modifier 3 is a protein that in humans is encoded by the SUMO3 gene. SUMO proteins, such as SUMO3, and ... "Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9". The Journal of Biological ... SUMO) family members, SUMO-2 and SUMO-3". The Journal of Biological Chemistry. 278 (35): 33416-21. doi:10.1074/jbc.M305680200. ... Su HL, Li SS (August 2002). "Molecular features of human ubiquitin-like SUMO genes and their encoded proteins". Gene. 296 (1-2 ...
"Nucleolar protein B23/nucleophosmin regulates the vertebrate SUMO pathway through SENP3 and SENP5 proteases". The Journal of ... Haindl M, Harasim T, Eick D, Muller S (March 2008). "The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of ... "Identification of the nuclear and nucleolar localization signals of the protein p120. Interaction with translocation protein ... It is involved in the biogenesis of ribosomes and may assist small basic proteins in their transport to the nucleolus. Its ...
The SUMO protein is a small ubiquitin-like modifier, which is added to lysly Īµ-amino groups. This process involves a three- ... The mitochondrial matrix protein p32 stabilizes smARF. This protein binds various cellular and viral proteins, but its exact ... In addition to the INK4a protein, the unrelated protein, ARF, is transcribed from an alternate reading frame at the INK4a/ARF ... ARF associates with UBC9, the only SUMO E2 known, suggesting ARF facilitates SUMO conjugation. The importance of this role is ...
"Identification of the enzyme required for activation of the small ubiquitin-like protein SUMO-1". J. Biol. Chem. 274 (15): ... The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins ... 2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ...
... and the UBA1 for the ubiquitin-like protein (Ubls) NEDD8 and SUMO are heterodimeric complexes with similar molecular weights. ... Lois LM, Lima CD (February 2005). "Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 ... a small RWD-containing protein, enhances SUMO conjugation and stabilizes HIF-1alpha during hypoxia". Cell. 131 (2): 309-23. doi ... "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell. 125 (4): ...
Sumoylation sites allow for the binding of SUMO (small ubiquitin-like modifier protein) which are known to alter different ... Putative uncharacterized protein C6orf52 (C6orf52) is a protein in humans that is encoded by the gene "C6orf52" and has six ... "NPS@: Network Protein Sequence Analysis - SOPMA". Retrieved 2019-05-05. "I-TASSER server for protein structure and function ... Two proteins in cattle that have been linked to fat or energy metabolism were predicted to be similar to C6orf52, however there ...
SENP proteases can remove SUMO from sumoylated proteins, freeing it to be used in further sumoylation reactions. The protein ... In a second step, an E1 activating complex binds to SUMO at its di-glycine and passes it on to the E2 protein Ubc9, where it ... When SUMO protein precursors are first expressed, they first undergo a maturation step in which the four C-terminal amino acids ... Sumoylation is a process in which a Small Ubiquitin-like MOdifier (SUMO) is covalently attached to other proteins in order to ...
The encoded protein contains 11 conserved cysteine residues and is phosphorylated by protein kinase C exclusively on its serine ... The protein may play a role in the regulation of renal and intestinal calcium and phosphate transport, cell metabolism, or ... However, STC1 interacts with many proteins in the cytoplasm, mitochondria, endoplasmatic reticulum, and in dot-like fashion in ... 285 (1): H442-8. doi:10.1152/ajpheart.01071.2002. PMID 12663264. Zlot C, Ingle G, Hongo J, Yang S, Sheng Z, Schwall R, Paoni N ...
Other proteins containing this domain include the human pias family (protein inhibitor of activated STAT protein). The name MIZ ... The crystal structure of S. cerevisiae sumo e3 ligase siz1 containing this domain has been solved. Wu L, Wu H, Ma L, Sangiorgi ... In molecular biology the MIZ-type zinc finger domain is a zinc finger-containing protein with homology to the yeast protein, ... Miz1 binds to the homeobox protein Msx2, enhancing the specific DNA-binding ability of Msx2. ...
E3 SUMO-protein ligase PIAS4 is one of several protein inhibitor of activated STAT (PIAS) proteins. It is also known as protein ... "Entrez Gene: PIAS4 Protein inhibitor of activated STAT, 4". Imoto, Seiyu; Sugiyama Kenji; Muromoto Ryuta; Sato Noriko; Yamamoto ... Sachdev, S; Bruhn L; Sieber H; Pichler A; Melchior F; Grosschedl R (Dec 2001). "PIASy, a nuclear matrix-associated SUMO E3 ... 2002). "Protein inhibitors of activated STAT resemble scaffold attachment factors and function as interacting nuclear receptor ...
SUMO proteins have the widest variety of cellular protein targets after ubiquitin and are involved in processes including ... Ubiquitin-like proteins (UBLs) are a family of small proteins involved in post-translational modification of other proteins in ... SUMO, NEDD8, ATG8, ATG12, URM1, UFM1, FAT10, and ISG15. One additional protein, known as FUBI, is encoded as a fusion protein ... "The dual role of ubiquitin-like protein Urm1 as a protein modifier and sulfur carrier". Protein & Cell. 2 (8): 612-9. doi: ...
NDP55 and 53kDa protein associated with the nuclear matrix. Other proteins, such as PIC1/SUMO-1, which are associated with ... "Evidence for covalent modification of the nuclear dot-associated proteins PML and Sp100 by PIC1/SUMO-1". The Journal of Cell ... The SUMO-1 ubiquitin like protein is responsible for modifying PML protein such that it is targeted to dots. whereas ... The proteins can reorganize in the nucleus, by increasing number of dispersion in response to different stress (stimulation or ...
We identify the SUMO ligase Protein Inhibitor of Activated STAT1 (PIAS1) as a constituent PML-NB protein. We show that PIAS1 ... The SUMO Ligase Protein Inhibitor of Activated STAT 1 (PIAS1) is a constituent PML-NB protein that contributes to the intrinsic ... The SUMO Ligase Protein Inhibitor of Activated STAT 1 (PIAS1) is a constituent PML-NB protein that contributes to the intrinsic ... constituent proteins. During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains ...
Among these, histone H1, histone H3, and p160 Myb-binding protein 1A were further characterized as novel SUMO-1 substrates. The ... Among these, histone H1, histone H3, and p160 Myb-binding protein 1A were further characterized as novel SUMO-1 substrates. The ... ribosomal proteins, histones, RNA-binding proteins, and transcription factor regulators. ... ribosomal proteins, histones, RNA-binding proteins, and transcription factor regulators. ...
Plasmid pSUMO His6 SUMO AMPKa (11-281) from Dr. Karsten Melchers lab contains the insert AMPK a1 and is published in Cell Res ... 2015 Jan;25(1):50-66. doi: 10.1038/cr.2014.150. Epub 2014 Nov 21. This plasmid is available through Addgene. ... Tag / Fusion Protein *6xHis-SUMO (N terminal on insert). Cloning Information * Cloning method Restriction Enzyme ... 2015 Jan;25(1):50-66. doi: 10.1038/cr.2014.150. Epub 2014 Nov 21. 10.1038/cr.2014.150 PubMed 25412657 ...
SUMO-2 and SUMO-3 are conjugated to a wide, but poorly defined range of target proteins and play important roles in many ... While SUMO-2 and SUMO-3 are 98 % identical, they are only 50 % identical to SUMO-1. Preliminary data indicate that SUMO-2 and ... SUMO is attached only to a specific lysine residue in the target protein. In higher eukaryotes, the SUMOylation targets ... and protein modification by SUMO does not have a common functional consequence.. Employment of most modern proteomic and ...
... centrosomal protein 76), and APP (Amyloid-beta precursor protein). There are no paralogs for KIAA1143 KIAA1143 has homologs in ... "GPS SUMO for KIAA1143". Retrieved 16 December 2022. "YinOYang Analysis". Retrieved 16 December 2022. "Myhits Motif scan". ... The KIAA1143 protein belongs to the uncharacterized protein KIAA1143-like Family, and contains DUF4604 domain of unknown ... KIAA1143 is an uncharacterized protein in humans that is encoded by the KIAA1143 gene. it may play a role in cell growth ...
Transgenic, knock-out, congenic and inbread strains are known for C57BL/6, A/J, BALB/c, SCID while the CD-1 is outbred as ... Recombinant Mouse DEFB1/ Beta-defensin 1 Protein, His-SUMO, E.coli-50ug. ...
Human SUMO E1~SUMO1-AMP tetrahedral intermediate mimic ... 3D Structures in the Protein Data Bank *Computed Structure ... Here we report crystal structures for human SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues at ... SUMO-activating enzyme subunit 2. B. 551. Homo sapiens. Mutation(s): 1 Gene Names: HRIHFB2115, SAE2, UBA2, UBLE1B. EC: 6.3.2 ( ... Active site remodelling accompanies thioester bond formation in the SUMO E1.. Olsen, S.K., Capili, A.D., Lu, X., Tan, D.S., ...
His-SUMO-tagged from Creative Biomart. Recombinant Human WDR77 Protein, His-SUMO-tagged can be used for research. ... Recombinant Human WDR77 Protein, His-SUMO-tagged. Cat.No. : WDR77-1049H. Product Overview :. Recombinant Human WDR77 Protein (1 ... Recombinant Human WDR77 Protein, GST-tagged. +Inquiry. WDR77-6232R. Recombinant Rat WDR77 Protein, His (Fc)-Avi-tagged. + ... Recombinant Mouse WDR77 Protein, His (Fc)-Avi-tagged. +Inquiry. WDR77-5018R. Recombinant Rhesus Macaque WDR77 Protein, His (Fc ...
Non-covalent Interaction With SUMO Enhances the Activity of Human Cytomegalovirus Protein IE1. Title. Non-covalent Interaction ... It is a multifunctional and conditionally essential protein for HCMV infection. SUMO signaling regulates several cellular ... Consequently, IE1 exploits SUMO signaling to regulate these pathways. The covalent interaction of IE1 and SUMO (IE1-SUMOylation ... Non-covalent Interaction With SUMO Enhances the Activity of Human Cytomegalovirus Protein IE1. ...
Enables SUMO activating enzyme activity. Predicted to be involved in positive regulation of protein sumoylation and protein ... General protein information Go to the top of the page Help Preferred Names. SUMO-activating enzyme subunit 2. Names. SUMO1 ... Protein Expr Purif, 2003 Jul. PMID 12821332 * SUMO conjugation and deconjugation. Schwienhorst I, et al. Mol Gen Genet, 2000 ... mRNA and Protein(s) * XM_017322348.3 ā†’ XP_017177837.1 SUMO-activating enzyme subunit 2 isoform X1 ...
... is an Escherichia coli Protein fragment 366 to 802 aa range, , 90% purity and validated in SDS-PAGE. ... Important regulator of CDKN1A/p21(CIP1). Has E3 SUMO-protein ligase activity toward itself via its PHD-type zinc finger. ... Proteins and Peptides. Proteomics tools. Agonists, activators, antagonists and inhibitors. Cell lines and Lysates. Multiplex ... Epigenetics and Nuclear Signaling Chromatin Binding Proteins Methylated DNA Share by email ...
An emerging theme is that TonEBP is a stress protein that mediates the cellular response to a range of pathological insults, ... Numerous studies since then have revealed that TonEBP is a pleiotropic stress protein that is involved in a range of ... TonEBP is a DNA-binding protein with multiple roles, via transcription regulation and other mechanisms, in both protective and ... Tonicity-responsive enhancer-binding protein (TonEBP), which is also known as nuclear factor of activated T cells 5 (NFAT5), ...
PDB Description: solution structure of human sumo-2 (smt3b), a ubiquitin-like protein ... PDB Compounds: (A:) Ubiquitin-like protein SMT3B. SCOPe Domain Sequences for d1wz0a1:. Sequence; same for both SEQRES and ATOM ... Class d: Alpha and beta proteins (a+b) [53931] (396 folds). *. Fold d.15: beta-Grasp (ubiquitin-like) [54235] (15 superfamilies ... SCOPe: Structural Classification of Proteins - extended. Release 2.08 (updated 2023-01-06, stable release September 2021) ...
H1 Cell division protein FtsZ (ftsZ) from Cusabio. Cat Number: CSB-EP359270EGX. USA, UK & Europe Distribution. ... N-terminal 10xHis-SUMO-tagged Recombinant * N-terminal 10XHis-tag & C-terminal Myc-tag Rec ... Recombinant Escherichia coli O6:H1 Cell division protein FtsZ (ftsZ) , CSB-EP359270EGX. (No reviews yet) Write a Review Write a ... Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of ...
In this study, we found that RING finger protein 4 (RNF4), a RING finger E3 ubiquitin ligase, is required for the RIPK1 ... Receptor-interacting protein kinase 1 (RIPK1) is a key component of the tumor necrosis factor (TNF) receptor signaling complex ... through downregulation of transforming growth factor Ī²-activated kinase 1 (TAK1) activity, indicating the possibility that RNF4 ... SUMO)-targeted ubiquitin ligase (STUbL) [12,13]. RNF4 recognizes and ubiquitinates polysumoylated proteins via its SUMO- ...
Recombinant Human SENP3 Protein expressed from Insect Cells. Conjugated to His tag. Order Protein ABIN3095425 online. ... smt3ip1 Protein, fa03d07 Protein, wu:fa03d07 Protein, senp3 Protein, SUMO1/sentrin/SMT3 specific peptidase 3 Protein, SUMO/ ... SMT3IP1 Protein, SSP3 Protein, Ulp1 Protein, AA408656 Protein, Smt3ip Protein, Smt3ip1 Protein, ssp3 Protein, ... SENP3 Protein, Senp3 Protein, senp3 Protein, senp3b Protein, senp3.L Protein Background Protease that releases SUMO2 and SUMO3 ...
... but involve functionally relevant host-pathogen interactions associated with tandem and ankyrin repeat effector proteins. In ... but involve functionally relevant host-pathogen interactions associated with tandem and ankyrin repeat effector proteins. In ... This PTM is required for multiple interactions with SUMO-binding domain containing host proteins such as PCGF-5 and GGA1. ... outer membrane proteins, actin polymerization proteins, and a group of poly(G-C) tract containing proteins, which may be ...
pA104R is a highly conserved HU/IHF-like DNA-packaging protein identified in the ASFV nucleoid that appears to be profoundly ... The involvement of viral DNA-binding proteins in the regulation of virulence genes, transcription, DNA replication, and repair ... Molecular interaction between human SUMO-I and histone like DNA binding protein of Helicobacter pylori (Hup) investigated by ... ASFV Structural Proteins and Proteins Involved in Assembly. Up to 70 structural proteins have been identified from the ASFV ...
Therefore, we herein established a SARS-CoV-2 spike (S) protein-mediated cell-cell fusion assay and found that SARS-CoV-2 ... core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in ... series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein- ... The fusion proteins were isolated by Ni-affinity chromatography, and the SUMO tag was removed by Ulp1 enzyme (1:100 w/w) ...
Order PAK1 Proteins from many different species. Find the right product on antibodies-online.com. ... His-SUMO Tag). Reactivity Human Source Escherichia coli (E. coli) ... PAK1 Proteins by Protein Type. Find PAK1 Proteins with a specific Protein Type. The Protein Type listed below are among those ... Proteins. AW045634 Proteins. pak Proteins. pak-1 Proteins. PAK-1 Proteins. Paka Proteins. pakalpha Proteins. PAKalpha Proteins ...
Antibodies, ELISA kits, proteins, reagents. Order quickly and easily at antikoerper-online.de ... Fc fragment of IgG binding protein (FCGBP), Fc fragment of IgG binding protein (Fcgbp), A430096B05Rik, FC(GAMMA)BP Bezeichner ... His-SUMO Tag). ReaktivitƤt Staphylococcus aureus Source Escherichia coli (E. coli) ... "The Goblet Cell Protein Clca1 (Alias mClca3 or Gob-5) Is Not Required for Intestinal Mucus Synthesis, Structure and Barrier ...
Difficult-to-Express Proteins Market reached a valuation of US$ 3,8 Billion in 2021 and is expected to reach US$ 12.37 Billion ... Cell-free Protein Synthesis 7.3.2. Prokaryotic Expression Systems 7.3.3. SUMO Fusion System 7.3.4. Gene Fusion Systems 7.3.5. ... Disulfide-bonded Protein Expression 6.3.2. Membrane Protein Expression 6.3.3. Toxic Protein Expression 6.3.4. Target Protein ... Difficult-to-Express Proteins Market. Difficult-to-Express Proteins Market by Protein, Technology Type, Application & Region , ...
Locate proteins, assay kits, reagents, custom services. Get complete supplier details here. ... Need SARS-CoV-2 Envelope Protein for research? Find and compare commercial and governmental sources for immunological and ... SARS-CoV-2 Envelope Protein is a recombinant protein expressed in E. coli. Met1-Val75. N-terminal His and SUMO tags. Purity > ... COVID-19 protein, Protein COVID-19, Virus COVID-19 Protein, Virus COVID-19, Virus protein COVID-19, 2019-nCoV protein, Protein ...
Post-translational protein modification (Homo sapiens) * SUMOylation (Homo sapiens) * Processing and activation of SUMO (Homo ... SUMO is proteolytically processed (Homo sapiens) * SENP1,2,5 proteolytically process SUMO2 (Homo sapiens) * SUMO2(1-95) [ ...
SUMO2/3 Monoclonal Antibody recognizes proteins post-translational modifications SUMO2 and SUMO3. Tested in WB, IF, and IP ... Anti-SUMO-2/3 mouse monoclonal antibody was raised against full-length recombinant SUMO-2 protein (Uniprot: P61956) combined ... The antibody has been shown to recognize a wide range of SUMO-2/3-targeted proteins in HeLa cell lysate (Fig. 1B) and to detect ... Multiple bands indicate that TFII-I is SUMOylated by several SUMO-2/3 proteins. TFII-I has previously been reported to be a ...
The COOH-terminal A168-170 region of the giant sarcomeric protein titin interacts with muscle-specific RING finger-1 (MURF-1). ... These data, together with the observations that MURF-1s RING domain binds to the nuclear protein SUMO-3 (Dai and Liew, 2001) ... Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. ... Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J. Biol. Chem. ...
... anti-nuclear matrix protein 2 (NXP2), and anti-SUMO-1 activating enzyme (SAE) autoantibodies. [42] ... Patients with antimelanoma differentiation-associated protein 5 antibodies had a significantly lower probability of achieving ... Increased plasma thrombospondin-1 (TSP-1) levels are associated with the TNF alpha-308A allele in children with juvenile ... 1, 2] Dystrophic calcinosis may complicate dermatomyositis and is most often observed in children and adolescents. ...
SARS-CoV-2 Spike Protein RBD (Delta B1.617.2 Variant), His-SUMO tag, HEK293 ... Youre reviewing:SARS-CoV-2 Spike Protein RBD (Delta B1.617.2 Variant), His-SUMO tag, HEK293 - orb1178864. Your Rating. 1 star ... SARS-CoV-2 Spike Protein RBD (Delta B1.617.2 Variant), His-SUMO tag, HEK293 ... SARS-CoV-2 Spike Protein RBD (Delta B1.617.2 Variant), His-SUMO tag, HEK293 ...
Protein ubiquitination patterns are an important component of cellular signaling. The WD-repeat protein WDR48 (USP1-associated ... In addition, WDR48 has a novel ancillary domain and a C-terminal SUMO-like domain encircling the USP46-bound ubiquitin. ... Protein ubiquitination patterns are an important component of cellular signaling. The WD-repeat protein WDR48 (USP1-associated ... Department of Structural Biology, Genentech, Inc., 1 DNA Way, South San Francisco, CA 94080, USA. Electronic address: harris. ...
  • We show that PIAS1 localizes at PML-NBs in a SUMO interaction motif (SIM)-dependent manner that requires SUMOylated or SUMOylation competent PML. (gla.ac.uk)
  • In higher eukaryotes, the SUMOylation targets identified thus far cannot be broadly categorized, and protein modification by SUMO does not have a common functional consequence. (europa.eu)
  • The covalent interaction of IE1 and SUMO (IE1-SUMOylation) is well studied. (ncbs.res.in)
  • Two critical functions of IE1 are inhibition of SUMOylation of Promyelocytic leukemia protein (PML) and transactivation of viral promoters. (ncbs.res.in)
  • Although the non-covalent interaction of IE1 and SUMO is not involved in the inhibition of PML SUMOylation, it contributes to the transactivation activity. (ncbs.res.in)
  • Predicted to be involved in positive regulation of protein sumoylation and protein sumoylation. (nih.gov)
  • Figure 1B: Induction of SUMOylation by heat shock and reduction of SUMOylation by SUMO-2 shRNA knockdown. (cytoskeleton.com)
  • Slm-1 is a sumo ligase, suggesting that sumoylation of a certain protein or protein(s) is essential for tolerance of DNA damage. (harvard.edu)
  • I'm looking at this information in several ways, including the use of transgenic worms harboring an affinity tagged Sumo, in order to identify the target of slm-1 sumoylation during the DNA damage response. (harvard.edu)
  • RanGAP1 acts as a very good control substrate for use in SUMOylation assays producing a product with a single SUMO modification. (enzolifesciences.com)
  • Upon SUMOylation, RanGAP1 and SUMO-1 behave as "beads-on-a-string" joined by a flexible isopeptide tether and their structures and local dynamic features do not change significantly beyond the site of this covalent linkage. (enzolifesciences.com)
  • SUMOylation is a post-translational modification of proteins that has been found to play a major role in the Wnt/Ī²-catenin signaling pathway. (frontiersin.org)
  • Post-translational modifications (PTMs) of proteins, including phosphorylation, acetylation, ubiquitination, and SUMOylation, can regulate the function of proteins, determine the active state and subcellular location of proteins, and dynamically interact with other proteins related to carcinogenesis and progression ( 17 - 20 ). (frontiersin.org)
  • SUMOylation of proteins is an important mechanism in cellular responses to environmental stress ( 21 , 22 ). (frontiersin.org)
  • Proteins associated with the Wnt/Ī²-catenin pathway have been identified as SUMOylated substrates, and evidences suggested that the initiation and progression of cancers depended on the function of the SUMOylation ( 23 ). (frontiersin.org)
  • We further found that SET domain bifurcated 1 (Setdb1) was a SUMOylated protein and that SUMOylation promoted Setdb1 occupancy on the promoter locus of Pparg and Cebpa genes to suppress their expressions by H3K9me3. (deepdyve.com)
  • SUMO Protease (ULP1, Ubiquitin-like-specific protease 1) is a highly active cysteine protease derived from Saccharomyces cerevisiae. (leadgenebio.com)
  • ULP1 protease specifically recognizes the tertiary structure of SUMO rather than an amino acid sequence. (leadgenebio.com)
  • SUMO Protease (ULP1) protease: target protein ratio of 1U:2 Āµg is used for most fusion protein cleavage. (leadgenebio.com)
  • SUMO Protease (ULP1) reactions can be performed in a buffer containing 2M urea. (leadgenebio.com)
  • SUMO Protease (ULP1) reactions can be performed in a buffer which is optimal for the target protein. (leadgenebio.com)
  • SUMO Protease (ULP1) cleavage of control protein. (leadgenebio.com)
  • In this study, we observed the overexpression of SUMO-speciļ«æc protease 2 (Senp2) in adipose tissues during obesity. (deepdyve.com)
  • Accepted December 19, studies have shown that SUMO-speciļ«æc protease 2 (Senp2)is involved in myogenesis (Qi et al. (deepdyve.com)
  • Distinct roles for Arabidopsis SUMO protease ESD4 and its closest homolog ELS1. (mpg.de)
  • Central to the execution of this particular antiviral response is the small ubiquitin-like modifier (SUMO) signalling pathway. (gla.ac.uk)
  • Small Ubiquitin-Like Modifier Conjugating Enzyme with Active Site Mutation Acts as Dominant Negative Inhibitor of SUMO Conjugation in Arabidopsis. (mpg.de)
  • METHODS: In this study, we used a small-ubiquitin-like modifier (SUMO*) cloning vector to express a SUMO*-DENV-4 rNS1 fusion protein to develop NS1 DENV-4 specific monoclonal antibodies (MAbs). (cdc.gov)
  • SUMO signaling regulates several cellular pathways that are also targets of IE1. (ncbs.res.in)
  • Receptor-interacting protein kinase 1 (RIPK1) is a key component of the tumor necrosis factor (TNF) receptor signaling complex that regulates both pro- and anti-apoptotic signaling. (mdpi.com)
  • It has been reported that RNF4 negatively regulates TNF-Ī±-induced activation of the nuclear factor-ĪŗB (NF-ĪŗB) through downregulation of transforming growth factor Ī²-activated kinase 1 (TAK1) activity, indicating the possibility that RNF4-mediated TAK1 suppression results in enhanced sensitivity to cell death. (mdpi.com)
  • L ike protein phosphorylation by kinases, protein ubiquitylation regulates many aspects of cell function and provides a wealth of drug target opportunities across many therapeutic areas including cancer, cardiovascular, metabolism, inflammation, neurodegeneration and infectious diseases. (ddw-online.com)
  • The Ubl SUMO regulates a growing number of recognized proteins involved in the cell cycle, DNA repair, the stress response, nuclear transport, transcription, and signal transduction. (enzolifesciences.com)
  • The tiny ubiqwitin-like modifier protein (SUMO) regulates transcriptional activity and the translocation of proteins across the nuclear membrane1. (cell-signaling-pathways.com)
  • The small ubiquitin-like modifiers, SUMO-1, SUMO-2 and SUMO-3 are conjugated to a wide, but poorly defined range of target proteins and play important roles in many cellular processes. (europa.eu)
  • Employment of most modern proteomic and bioinformatic techniques and tools allowed us to undertake the large-scale identification of SUMO-1 and SUMO-2 putative target proteins. (europa.eu)
  • Extensive analysis of obtained results resulted in much deeper understanding of how poly-SUMO-2 chains are being assembled into longer forms, with preference for extending of already existing chains on target proteins rather than recruitment of large amounts of new substrates. (europa.eu)
  • The result is a 3-D model that allows them to visualize the interaction of potential drug compounds with target proteins (see accompanying video). (medicalxpress.com)
  • In human cells infected with herpes simplex virus 1 the double-stranded RNA-dependent protein kinase (PKR) is activated but phosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2) and total shutoff of protein synthesis is observed only in cells infected with gamma(1)z34.5- mutants. (scienceopen.com)
  • BTK, a TEC-family tyrosine kinase activated by the B-cell antigen receptor, contains a variety of regulatory domains and it is subject to complex regulation by membrane phospholipids, protein ligands, phosphorylation, and dimerization. (elifesciences.org)
  • Coloring is similar to alphafold confidence graphing KIAA1143 is experimentally determined to have interactions with EAPP (E2F-associated phosphoprotein), ECD (Ecdysoneless Cell Cycle Regulator), GPATCH1 (Evolutionarily Conserved G-Patch Domain-Containing Protein), PRPF8 (Pre-MRNA-Processing-Splicing Factor 8), WDR83 (Mitogen-Activated Protein Kinase Organizer 1), CEP76 (centrosomal protein 76), and APP (Amyloid-beta precursor protein). (wikipedia.org)
  • Mitotic kinase Aurora-B is regulated by SUMO-2/3 conjugation/deconjugation during mitosis. (nih.gov)
  • The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-activated protein kinase. (scienceopen.com)
  • However, over the same period protein kinases have rapidly become one of the most significant classes of drug targets for the pharmaceutical industry, with the global market for kinase therapies being about US$15 billion per annum in 2010 and this value is predicted to double by 2020 (3). (ddw-online.com)
  • Enhances transcriptional repression by coordinating the increase in H3K9me, the decrease in histone H3 'Lys-9 and 'Lys-14' acetylation (H3K9ac and H3K14ac, respectively) and the disposition of HP1 proteins to silence gene expression. (abcam.com)
  • Tonicity-responsive enhancer-binding protein (TonEBP), which is also known as nuclear factor of activated T cells 5 (NFAT5), was discovered 20 years ago as a transcriptional regulator of the cellular response to hypertonic (hyperosmotic salinity) stress in the renal medulla. (nature.com)
  • MURF-1 also binds to ubiquitin-conjugating enzyme-9 and isopeptidase T-3, enzymes involved in small ubiquitin-related modifier-mediated nuclear import, and with glucocorticoid modulatory element binding protein-1 (GMEB-1), a transcriptional regulator. (rupress.org)
  • The ICE1-CBF-COR transcriptional cascade (inducer of CBF expression 1 and C-repeat binding factor transcriptional cascade) is the best characterized pathway for gene regulation under cold conditions in many species [ 8 ]. (biomedcentral.com)
  • Of the 31 genes, the 21 upregulated genes were primarily associated with cell paracrine and intracellular signaling, transcription regulation and cell adhesion and migration, and their transcriptional products included transforming growth factor-Ī²2 (TGF-Ī²2), insulin-like growth factor-binding protein 2 and transcriptional factor AP-2Ī±/Ī³ ( 11 ). (spandidos-publications.com)
  • KIAA1143 is an uncharacterized protein in humans that is encoded by the KIAA1143 gene. (wikipedia.org)
  • This gene is located on chromosome 3 on the minus strand This protein has a function that is not yet objectively understood. (wikipedia.org)
  • Gene ontology analysis showed some apparent differences in relation to increased or decreased modification status of certain functionally-related groups of proteins responding to heat shock, mainly by increased modification. (europa.eu)
  • This gene encodes a family member of serine/threonine p21-activating kinases, known as PAK proteins. (antibodies-online.com)
  • In response to low temperature, many biochemical and physiological processes change in plants through regulation of cold responsive (COR) gene expression as well as through posttranslational protein modifications. (biomedcentral.com)
  • 1997), a protein whose gene (SYN, aka PARK 1) has been linked to familial PD (Athanassiadou et al. (ukessays.com)
  • Animal models of the disease, created using neurotoxins such as rotenone or 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), or transgenic mice that overexpress human SYN gene (for ĆÆ Ā”-synuclein) mutations, do not faithfully replicate the structure and antigenicity of the Lewy bodies found in PD (Dickson 2001). (ukessays.com)
  • She explains, "I began this project by characterizing mus-101, a known DNA damage response gene, and found that worms partially depleted of the protein by RNAi are healthy but sensitive to stresses such as drugs that damage DNA or inhibit replication. (harvard.edu)
  • Huntington's disease is a genetic neurological disorder caused by a repeated expansion of the CAG trinucleotide, causing instability in the N-terminal of the gene coding for the Huntingtin protein. (benthamscience.com)
  • The gene Protein phosphatase 1 at 87B is referred to in FlyBase by the symbol Dmel\Pp1-87B (CG5650, FBgn0004103). (yeastrc.org)
  • It is a protein_coding_gene from Drosophila melanogaster. (yeastrc.org)
  • The carboxyl-terminal 64 aa of gamma(1)34.5 protein are homologous to the corresponding domain of MyD116, the murine growth arrest and DNA damage gene 34 (GADD34) protein and the two domains are functionally interchangeable in infected cells. (scienceopen.com)
  • Recombinant Human WDR77 Protein (1-312aa) was expressed in E. coli with N-terminal His-SUMO tag. (creativebiomart.net)
  • Biotin-ubiquitin tagging of mammalian proteins in Escherichia coli. (nih.gov)
  • SARS-CoV-2 Envelope Protein is a recombinant protein expressed in E. coli. (linscottsdirectory.com)
  • Catalase Protein, Human is an approximately 60.0 kDa human catalase protein expressed in E.coli . (medchemexpress.com)
  • Find PAK1 Proteins for a variety of species such as anti-Human PAK1, anti-Mouse PAK1, anti-Rat PAK1. (antibodies-online.com)
  • Our results suggest that cold temperature significantly affects genes related to protein translation and cellular metabolism in this chilling sensitive species. (biomedcentral.com)
  • The conjugation of SUMO adducts to substrates requires the activity of three different SUMO-specific E1, E2 and E3 enzymes that act in a sequential manner. (europa.eu)
  • SUMO conjugation and deconjugation. (nih.gov)
  • SUMO conjugation in plants. (mpg.de)
  • Nuclear corepressor for KRAB domain-containing zinc finger proteins (KRAB-ZFPs). (abcam.com)
  • We identify the SUMO ligase Protein Inhibitor of Activated STAT1 (PIAS1) as a constituent PML-NB protein. (gla.ac.uk)
  • Here we generated a series of lipopeptides derived from EK1 and found that EK1C4 was the most potent fusion inhibitor against SARS-CoV-2 S protein-mediated membrane fusion and pseudovirus infection with IC50s of 1.3 and 15.8 nM, about 241- and 149-fold more potent than the original EK1 peptide, respectively. (nature.com)
  • COH000 was chosen for this study because of its specificity for inhibiting SUMO enzymes, but how the inhibitor works and where it binds to the enzyme were completely unknown. (medicalxpress.com)
  • We also identified a number of branched peptides (between SUMO-2 and its substrate) as one of validation steps. (europa.eu)
  • Anti-SUMO-2/3 mouse monoclonal antibody was raised against full-length recombinant SUMO-2 protein (Uniprot: P61956) combined with a proprietary mix of peptides that include CQIRFRFDGQPINE. (cytoskeleton.com)
  • Results from the first part of this study strongly implicate SUMO-1 modification of the metabolic enzyme GAPDH metabolism in the switch from aerobic to anaerobic metabolism. (europa.eu)
  • Enables SUMO activating enzyme activity. (nih.gov)
  • Predicted to be part of SUMO activating enzyme complex. (nih.gov)
  • Expression and regulation of the mammalian SUMO-1 E1 enzyme. (nih.gov)
  • Selected structural elements are labeled and regions of the enzyme that become disordered in the SUMO E1/COH000 complex transition from solid to transparent representations. (medicalxpress.com)
  • Oxidoreductases (EC 1.x.x.x) are the first enzyme class in the Enzyme Commission Nomenclature. (medchemexpress.com)
  • The ubiquitylation process involves three sequential steps, each of which is controlled by a different class of enzyme (Figure 1). (ddw-online.com)
  • Cleavage efficiency may differ based on structure and properties of each target protein, we recommend testing several enzyme-to-substrate ratios, temperatures, and incubation times. (leadgenebio.com)
  • Prokaryotic expression systems will continue to play an essential role as a cost-effective, customizable, and simple-to-run source of recombinant protein as the number of authorized therapeutic proteins grows, encouraging the sales of difficult-to-express proteins. (futuremarketinsights.com)
  • To achieve results of highest possible quality we employed SILAC (Stable Isotope Labeling of Amino acids in Cell culture) to allow quantification, TAP (Tandem Affinity Purification) for recovery, high accuracy Orbitrap mass spectrometry for identification and MaxQuant software for quantification and analysis of SUMO-2 substrate proteins. (europa.eu)
  • In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization). (antibodies-online.com)
  • In a first purification step, the protein is purified from the cleared cell lysate using three different His-tag capture materials: high yield, EDTA resistant, or DTT resistant. (antibodies-online.com)
  • Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. (antibodies-online.com)
  • Increasing toolbox to approach the production and purification of difficult-to-express proteins to fulfill the demand for difficult-to-express proteins, which include different expression systems, promoters that have different strengths, cultivation media, and conditions. (futuremarketinsights.com)
  • It has often been used as a biotechnological tool for cleavage affinity purification tags such as ubiquitinlike (UBL) protein, and SUMO from fusion proteins. (leadgenebio.com)
  • Anti-SUMO2/3 antibody is a SUMO-2/3 mouse monoclonal antibody that is part of the Signal-Seekerā„¢ product line. (cytoskeleton.com)
  • To exclude the possibility of antibody cross-reaction (genotype 2) was found in plasma of all but 1 of the 6 case- between PARV4 and B19V, we tested plasma samples patients. (cdc.gov)
  • Anti-SUMO-2/3 Monoclonal Antibody from Cytoskeleton, Inc. (cytoskeleton.com)
  • The antibody has been shown to recognize a wide range of SUMO-2/3-targeted proteins in HeLa cell lysate (Fig. 1B) and to detect sub-nanogram amounts of recombinant SUMO-2 (Fig. 1A). (cytoskeleton.com)
  • Western blots of immunoprecipitated proteins were developed using 12F3 (A) or anti-TFII-I antibody (B). (A) Star (*) and circle (o) indicate heavy and light chains of antibodies. (cytoskeleton.com)
  • After washing proteins were eluted from the streptavidin beads separated on SDS-PAGE and immunoblotted with anti-GluR6/7 antibody (1/2 0 as previously described9. (cell-signaling-pathways.com)
  • Therefore, we herein established a SARS-CoV-2 spike (S) protein-mediated cell-cell fusion assay and found that SARS-CoV-2 showed a superior plasma membrane fusion capacity compared to that of SARS-CoV. (nature.com)
  • For example, a protein with several membrane-spanning domains that may or may not enter into the heterologous host's membrane bilayers or a protein that cannot be produced in a soluble form. (futuremarketinsights.com)
  • By contrast, the 10 downregulated genes were primarily associated with epithelial membrane proteins ( 11 ). (spandidos-publications.com)
  • Ubiquitin itself can direct its targets to a number of different fates, including proteasomal degradation and membrane protein transport. (enzolifesciences.com)
  • Signaling is initiated when the Wnt ligand binds to the Frizzled receptor on the cell membrane and the LDL receptor-associated protein 5/6 (LRP5/6) co-receptor. (frontiersin.org)
  • Reactions were incubated for 2 h at 30 Ā°C. Proteins were subjected to SDS-polyacrylamide gel electrophoresis (PAGE) and electrotransfer onto PVDF-membrane. (cell-signaling-pathways.com)
  • The control protein was ribosomal P2 protein fused to SUMO. (cdc.gov)
  • Your body, from protein chief, Drug and activity of chicken ovalbumin upstream promoter transcription factor I (COUP-TF1), which itself is coactivated by the small ubiquitin-related modifier-1 (SUMO-1) conjugase and ligase Ubc9 and PIAS1 (79). (sideload.com)
  • Additionally, our in-depth analysis resulted in the evaluation of the global changes of modification status of SUMO-1 and SUMO-2 sub-proteomes in response to stress conditions such as heat shock and hypoxia. (europa.eu)
  • For this project, we identified and quantified about a thousand of SUMO-2 substrates and divided them into sub-classes of those not responsive to heat shock as well as those, where SUMO-2 modification status was significantly increased or decreased. (europa.eu)
  • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein. (nih.gov)
  • Post-translational modification by ubiquitin and ubiquitin-like proteins (Ubls) is an essential cellular regulatory mechanism, allowing rapid and reversible control of a target protein's function by altering its half-life, sub-cellular localization, enzymatic activity, protein-protein interactions, or other properties. (enzolifesciences.com)
  • Post-translational modification of proteins by SUMO in Arabidopsis thaliana. (mpg.de)
  • Research on protein kinases is now reported to account for approximately 30% of the drug discovery programmes in the pharmaceutical industry and more than 50% of cancer research and development (3). (ddw-online.com)
  • The TEC kinases are the second largest sub-family of non-receptor tyrosine kinases in the human genome after the SRC family [ 1 - 3 ]. (elifesciences.org)
  • To investigate the functional significance of this interaction, we expressed green fluorescent protein fusion constructs encoding defined fragments of titin's M-line region and MURF-1 in cardiac myocytes. (rupress.org)
  • These data suggest that the interaction of titin with MURF-1 is important for the stability of the sarcomeric M-line region. (rupress.org)
  • Using EBNA3C amino acids 365-545 in a yeast two hybrid screen, we found an interaction with the Growth Arrest and DNA-damage protein, Gadd34. (scienceopen.com)
  • Amino acids 483-610 of Gadd34, including the two PP1a interaction, and the HSV-1 ICPĪ³34.5 homology domains, are required for the interaction. (scienceopen.com)
  • Furthermore, interaction is lost with a mutant of EBNA3C ( 509 DVIEVID 515 ā†’AVIAVIA), that abolishes EBNA3C coactivation ability as well as SUMO interaction[ 1 ]. (scienceopen.com)
  • Cell lysates were prepared from HeLa cells: Lane 2: Heat Shock treated (43Ā°C for 10min), Lane 3: untreated, Lane 4: shRNA SUMO-2 knock down. (cytoskeleton.com)
  • Lane 1: parental HeLa cell lysates, Lane 2: SUMO-2 shRNA control lysates, Lane 3: SUMO-1 shRNA knock-down cell lysates, Lane 4: SUMO-2 shRNA knock-down cell lysates. (cytoskeleton.com)
  • We solved the X-ray crystal structure of six-helical bundle (6-HB) core of the HR1 and HR2 domains in the SARS-CoV-2 S protein S2 subunit, revealing that several mutated amino acid residues in the HR1 domain may be associated with enhanced interactions with the HR2 domain. (nature.com)
  • and (iii) the alpha subunit in purified eIF-2 phosphorylated in vitro is specifically dephosphorylated by S10 fractions of wild-type infected cells at a rate 3000 times that of mock-infected cells, whereas the eIF-2alpha-P phosphatase activity of gamma(1)34.5- virus infected cells is lower than that of mock-infected cells. (scienceopen.com)
  • Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. (scienceopen.com)
  • An emerging theme is that TonEBP is a stress protein that mediates the cellular response to a range of pathological insults, including excess caloric intake, inflammation and oxidative stress. (nature.com)
  • Tonicity-responsive enhancer-binding protein (TonEBP) is a stress protein involved in the cellular response to hypertonicity, autoimmune reactions, inflammation and metabolic and genotoxic stress. (nature.com)
  • Despite its small genome and limited number of effector proteins, Ehrlichia efficiently establishes an intracellular infection and avoids immune defenses in vertebrate and invertebrate hosts through complex molecular and cellular reprogramming strategies. (frontiersin.org)
  • Protein ubiquitination patterns are an important component of cellular signaling. (rcsb.org)
  • During herpesvirus infection, these antiviral proteins are independently recruited to nuclear domains that contain infecting viral genomes to cooperatively promote viral genome silencing. (gla.ac.uk)
  • Following infection with herpes simplex virus 1 (HSV-1), PIAS1 is recruited to nuclear sites associated with viral genome entry in a SIM-dependent manner, consistent with the SIM-dependent recruitment mechanisms of other well characterized PML-NB proteins. (gla.ac.uk)
  • The Human Cytomegalovirus (HCMV) Immediate-Early protein 1 (IE1) is the first viral protein to express during infection. (ncbs.res.in)
  • They were named viral protein (VP) 2 and in Taiwan, we detected DNA in plasma of 3 mothers and their newborns with hydrops. (cdc.gov)
  • The involvement of viral DNA-binding proteins in the regulation of virulence genes, transcription, DNA replication, and repair make them significant targets. (mdpi.com)
  • However, the non-covalent interactions between SUMO and IE1 are unknown. (ncbs.res.in)
  • Mechanisms by which E. chaffeensis establishes intracellular infection, and avoids host defenses are not well understood, but involve functionally relevant host-pathogen interactions associated with tandem and ankyrin repeat effector proteins. (frontiersin.org)
  • Olsen and his team use these protein structures to model interactions with other molecules, including potential new drugs. (medicalxpress.com)
  • KRT17 has direct interactions with proteins and molecules. (creativebiomart.net)
  • No yeast two-hybrid interactions found for this protein. (yeastrc.org)
  • E1 enzymes activate ubiquitin (Ub) and ubiquitin-like (Ubl) proteins in two steps by carboxy-terminal adenylation and thioester bond formation to a conserved catalytic cysteine in the E1 Cys domain. (rcsb.org)
  • The antiviral mechanisms of PIAS1 are counteracted by ICP0, the HSV-1 SUMO-targeted ubiquitin ligase, which disrupts the recruitment of PIAS1 to nuclear domains that contain infecting HSV-1 genomes through mechanisms that do not directly result in PIAS1 degradation. (gla.ac.uk)
  • In this study, we found that RING finger protein 4 (RNF4), a RING finger E3 ubiquitin ligase, is required for the RIPK1 autophosphorylation and subsequent cell death. (mdpi.com)
  • In the article, Olsen and his team report that they have discovered a new site on a protein, SUMO E1, which is a target for E1 inhibitors. (medicalxpress.com)
  • Big-1 proteins are surface-expressed proteins that mediate mammalian host cell invasion or attachment. (wikipedia.org)
  • I conducted a screen to co-deplete mus-101 and most of the genes on Chromosome 1 then identified a small number of genes that displayed increased lethality when co-depleted with mus-101. (harvard.edu)
  • Currently, Holway is focusing on one of these genes called slm-1. (harvard.edu)
  • Consequently, IE1 exploits SUMO signaling to regulate these pathways. (ncbs.res.in)
  • Antibodies to ribosomal P2 protein were rarely detected, ransmission routes of human parvovirus 4 (PARV4), except in patients with systemic lupus erythematosus ( 5 ). (cdc.gov)
  • After many washes in extraction buffer proteins were eluted from the streptavidin beads by boiling in reducing sample buffer and then resolved by SDS-PAGE and immunoblotted using rabbit polyclonal antibodies against GluR1 (1/2 0 Upstate Biotechnology) and/or GluR6/7 (1/2 0 Upstate Biotechnology). (cell-signaling-pathways.com)
  • ASM23 is purified by Protein G affinity chromatography and is supplied as a lyophilized white powder. (cytoskeleton.com)
  • Rescued plasmids were digested with for 20 moments at 4 Ā°C. His6-tagged proteins were purified with TALON Co2+ affinity resin (Clontech) and GST fusion proteins were purified by using glutathione Sepharose 4B (Amersham Biosciences) according to the manufacturer's protocols. (cell-signaling-pathways.com)
  • Creative BioMart supplied nearly all the proteins listed, you can search them on our site. (creativebiomart.net)
  • 85% of 2 Ī¼g control substrate at 30Ā°C for 1 h. (leadgenebio.com)
  • After obstructing ADL5859 HCl undamaged and cleaved bands were recognized by HRP-conjugated S-protein (Novagen) and chemiluminescence substrate. (cell-signaling-pathways.com)
  • Aspects of intrinsic antiviral immunity are mediated by promyelocytic leukaemia (PML)-nuclear body (PML-NB) constituent proteins. (gla.ac.uk)
  • These proteins are critical effectors that link RhoGTPases to cytoskeleton reorganization and nuclear signaling, and they serve as targets for the small GTP binding proteins Cdc42 and Rac. (antibodies-online.com)
  • When you develop a drug, you want it to be highly specific for your protein of interest with no cross-reactivity with other targets or proteins, because that can cause negative side effects," Olsen explains. (medicalxpress.com)
  • Preliminary data indicate that SUMO-2 and SUMO-3 perform functionally distinct roles from SUMO-1. (europa.eu)
  • KIAA1143 has another transcript variant called KIAA1143 variant 2, which contains an alternate 3' terminal exon, resulting in a distinct 3' coding region and 3' UTR, compared to variant 1. (wikipedia.org)
  • The encoded isoform 2 has a distinct C-terminus and is shorter than isoform 1. (wikipedia.org)
  • This technique requires a high-energy source that produces intense X-ray beams that hit the crystallized protein and create a distinct diffraction pattern used to determine the 3-D structure of the protein. (medicalxpress.com)
  • BACKGROUND: Dengue, caused by one of the four serologically distinct dengue viruses (DENV-1 to - 4), is a mosquito-borne disease of serious global health significance. (cdc.gov)
  • CONCLUSION: This ELISA was sensitive and specific to DENV-4 with no cross-reactivity to other three DENV (1-3) serotypes and other heterologous flaviviruses. (cdc.gov)
  • On the second day the media was changed to Neurobasal medium supplemented with B27 only and the neurons were then fed weekly with this glutamine-free medium until use (21-25 days for 20 min at 4 Ā°C) supernatants containing equal amount of protein were incubated with streptavidin ADL5859 HCl beads to immunoprecipitate the surface-biotinylated proteins. (cell-signaling-pathways.com)
  • The remaining surface biotin was removed with GSH buffer (pH 9 2 min) then lysed and incubated with streptavidin beads to isolate internalized biotinylated proteins. (cell-signaling-pathways.com)
  • First part of the project aimed at the assessment of the changes of SUMO-2 sub-proteome in response to heat shock in cultured human HeLa cells. (europa.eu)
  • Second part of the project aimed at evaluation of the changes of SUMO-1 sub-proteome in HeLa cells cultured in hypoxic conditions. (europa.eu)
  • The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. (joplink.net)
  • Many proteins require post-translational modifications that may or may not be present in each host, influencing the difficult-to-express proteins market. (futuremarketinsights.com)
  • To solve protein structures, Olsen's lab uses a powerful technique called X-ray crystallography. (medicalxpress.com)
  • PIAS1 promotes the stable accumulation of SUMO1 at nuclear sites associated with HSV-1 genome entry, whereas the accumulation of other evaluated PML-NB proteins occurs independently of PIAS1. (gla.ac.uk)
  • EBNA3C is an EBV-encoded nuclear protein, essential for proliferation of EBV infected B-lymphocytes. (scienceopen.com)
  • When both proteins are overexpressed, Gadd34 can interact with EBNA3C in both nuclear and cytoplasmic compartments. (scienceopen.com)
  • The mature mRNA transcript is 5079 Base pairs long while the length of the KIAA1143 protein is 154 amino acids. (wikipedia.org)
  • These ELM domains are LIG_BIR_II_1 from amino acids 1-5 and LIG_WRC_WIRS_1 from amino acids 144-149. (wikipedia.org)
  • During the process, we found in only 1 mother (Figure, A), who also had IgM against regions of higher similarity in amino acid sequence PARV4. (cdc.gov)
  • Ubiquitylation describes the covalent attachment of a small 76-amino acid protein, ubiquitin, to other proteins. (ddw-online.com)
  • One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. (joplink.net)
  • Human SENP3 Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade. (antibodies-online.com)
  • Low protein yields have important industrial ramifications, especially as the need for recombinant proteins in cells grows. (futuremarketinsights.com)
  • Development of innovative cell-free protein synthesis platforms based on the industrial workhorse CHO cells that address the difficulties that continue to drive the demand for difficult-to-express proteins. (futuremarketinsights.com)
  • It is widely recognized that the accumulation of various harmful genetic alterations in normal cells may induce malignant cancer cells ( 1 ). (spandidos-publications.com)
  • These results indicate that in infected cells, gamma(1)34.5 interacts with and redirects phosphatase to dephosphorylate eIF-2alpha to enable continued protein synthesis despite the presence of activated PKR. (scienceopen.com)
  • The GADD34 protein may have a similar function in eukaryotic cells. (scienceopen.com)
  • Most of the cells in your body have specialized proteins on their surfaces called androgen receptors. (sideload.com)
  • 1mg of lysate was used for the immunoprecipitation of SUMO-2/3 conjugates. (cytoskeleton.com)
  • The difficult-to-express proteins market is likely to register a CAGR of 11.33% during the forecast period and is anticipated to reach a market share of US$ 12.37 Billion in 2032, from US$ 3.8 Billion in 2021, due to the development of new tools and significantly boost the overall revenue. (futuremarketinsights.com)
  • Here we report crystal structures for human SUMO E1 in complex with SUMO adenylate and tetrahedral intermediate analogues at 2.45 and 2.6 A, respectively. (rcsb.org)