Chromosomal proteins non histone. Medical search

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.

Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.

A family of low-molecular weight, non-histone proteins found in chromatin.

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.

An evolutionarily-conserved 10-kDa nuclear protein that binds NUCLEOSOMES and may be involved in the process of CHROMATIN unfolding.

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.

In a prokaryotic cell or in the nucleus of a eukaryotic cell, a structure consisting of or containing DNA which carries the genetic information essential to the cell. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)

Proteins conjugated with nucleic acids.

A 24-kDa HMGB protein that binds to and distorts the minor grove of DNA.

Compounds that inhibit HISTONE DEACETYLASES. This class of drugs may influence gene expression by increasing the level of acetylated HISTONES in specific CHROMATIN domains.

Formation of an acetyl derivative. (Stedman, 25th ed)

The repeating structural units of chromatin, each consisting of approximately 200 base pairs of DNA wound around a protein core. This core is composed of the histones H2A, H2B, H3, and H4.

Enzymes that catalyze acyl group transfer from ACETYL-CoA to HISTONES forming CoA and acetyl-histones.

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 conjugated with deoxyribonucleic acids (DNA) or specific DNA.

The portion of chromosome material that remains condensed and is transcriptionally inactive during INTERPHASE.

Chromosome regions that are loosely packaged and more accessible to RNA polymerases than HETEROCHROMATIN. These regions also stain differentially in CHROMOSOME BANDING preparations.

The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.

A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 2; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.

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)

A 23-kDa HMG-box protein that binds to and distorts the minor grove of DNA.

An enzyme that catalyzes the endonucleolytic cleavage to 3'-phosphomononucleotide and 3'-phospholigonucleotide end-products. It can cause hydrolysis of double- or single-stranded DNA or RNA. (From Enzyme Nomenclature, 1992) EC 3.1.31.1.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

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.

5-Bromo-2,4(1H,3H)-pyrimidinedione. Brominated derivative of uracil that acts as an antimetabolite, substituting for thymine in DNA. It is used mainly as an experimental mutagen, but its deoxyriboside (BROMODEOXYURIDINE) is used to treat neoplasms.

The specific patterns of changes made to HISTONES, that are involved in assembly, maintenance, and alteration of chromatin structural states (such as EUCHROMATIN and HETEROCHROMATIN). The changes are made by various HISTONE MODIFICATION PROCESSES that include ACETYLATION; METHYLATION; PHOSPHORYLATION; and UBIQUITINATION.

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.

A histone deacetylase subtype that is found along with HISTONE DEACETYLASE 1; RETINOBLASTOMA-BINDING PROTEIN 4; and RETINOBLASTOMA-BINDING PROTEIN 7 as core components of histone deacetylase complexes.

Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.

Enzymes that catalyse the removal of methyl groups from LYSINE or ARGININE residues found on HISTONES. Many histone demethylases generally function through an oxidoreductive mechanism.

Proteins involved in the assembly and disassembly of HISTONES into NUCLEOSOMES.

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.

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.

Addition of methyl groups. In histo-chemistry methylation is used to esterify carboxyl groups and remove sulfate groups by treating tissue sections with hot methanol in the presence of hydrochloric acid. (From Stedman, 25th ed)

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.

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 class of weak acids with the general formula R-CONHOH.

A single, unpaired primary lymphoid organ situated in the MEDIASTINUM, extending superiorly into the neck to the lower edge of the THYROID GLAND and inferiorly to the fourth costal cartilage. It is necessary for normal development of immunologic function early in life. By puberty, it begins to involute and much of the tissue is replaced by fat.

An enzyme that catalyzes the methylation of the epsilon-amino group of lysine residues in proteins to yield epsilon mono-, di-, and trimethyllysine. EC 2.1.1.43.

An 11-kDa AT-hook motif-containing (AT-HOOK MOTIFS) protein that binds to the minor grove of AT-rich regions of DNA. It is the full-length product of the alternatively-spliced HMGA1 gene and may function as an architectural chromatin binding protein that is involved in transcriptional regulation.

Various fish of the family SALMONIDAE, usually smaller than salmon. They are mostly restricted to cool clear freshwater. Some are anadromous. They are highly regarded for their handsome colors, rich well-flavored flesh, and gameness as an angling fish. The genera Salvelinus, Salmo, and ONCORHYNCHUS have been introduced virtually throughout the world.

Ducts that serve exclusively for the passage of eggs from the ovaries to the exterior of the body. In non-mammals, they are termed oviducts. In mammals, they are highly specialized and known as FALLOPIAN TUBES.

Proteins containing AT-HOOK MOTIFS that are rich in arginine and glycine residues. They bind to the minor grove of AT-rich regions of DNA.

A species of fruit fly much used in genetics because of the large size of its chromosomes.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.

A group of simple proteins that yield basic amino acids on hydrolysis and that occur combined with nucleic acid in the sperm of fish. Protamines contain very few kinds of amino acids. Protamine sulfate combines with heparin to form a stable inactive complex; it is used to neutralize the anticoagulant action of heparin in the treatment of heparin overdose. (From Merck Index, 11th ed; Martindale, The Extra Pharmacopoeia, 30th ed, p692)

The short, submetacentric human chromosomes, called group E in the human chromosome classification. This group consists of chromosome pairs 16, 17, and 18.

Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.

A family of HIGH MOBILITY GROUP PROTEINS that bind to NUCLEOSOMES.

The sum of the weight of all the atoms in a molecule.

Established cell cultures that have the potential to propagate indefinitely.

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.

Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.

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.

Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.

The phase of cell nucleus division following PROMETAPHASE, in which the CHROMOSOMES line up across the equatorial plane of the SPINDLE APPARATUS prior to separation.

A genus of anaerobic, irregular spheroid-shaped METHANOSARCINALES whose organisms are nonmotile. Endospores are not formed. These archaea derive energy via formation of methane from acetate, methanol, mono-, di-, and trimethylamine, and possibly, carbon monoxide. Organisms are isolated from freshwater and marine environments.

A genetic process by which the adult organism is realized via mechanisms that lead to the restriction in the possible fates of cells, eventually leading to their differentiated state. Mechanisms involved cause heritable changes to cells without changes to DNA sequence such as DNA METHYLATION; HISTONE modification; DNA REPLICATION TIMING; NUCLEOSOME positioning; and heterochromatization which result in selective gene expression or repression.

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.

Proteins found in any species of archaeon.

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.

RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.

Serologic tests based on inactivation of complement by the antigen-antibody complex (stage 1). Binding of free complement can be visualized by addition of a second antigen-antibody system such as red cells and appropriate red cell antibody (hemolysin) requiring complement for its completion (stage 2). Failure of the red cells to lyse indicates that a specific antigen-antibody reaction has taken place in stage 1. If red cells lyse, free complement is present indicating no antigen-antibody reaction occurred in stage 1.

The mechanisms effecting establishment, maintenance, and modification of that specific physical conformation of CHROMATIN determining the transcriptional accessibility or inaccessibility of the DNA.

A family of histone demethylases that share a conserved Jumonji C domain. The enzymes function via an iron-dependent dioxygenase mechanism that couples the conversion of 2-oxoglutarate to succinate to the hydroxylation of N-methyl groups.

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.

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.

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.

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.

Enzymes which catalyze the hydrolases of ester bonds within DNA. EC 3.1.-.

Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503)

Very long DNA molecules and associated proteins, HISTONES, and non-histone chromosomal proteins (CHROMOSOMAL PROTEINS, NON-HISTONE). Normally 46 chromosomes, including two sex chromosomes are found in the nucleus of human cells. They carry the hereditary information of the individual.

The rate dynamics in chemical or physical systems.

Red blood cells. Mature erythrocytes are non-nucleated, biconcave disks containing HEMOGLOBIN whose function is to transport OXYGEN.

Enzymes catalyzing the transfer of an acetyl group, usually from acetyl coenzyme A, to another compound. EC 2.3.1.

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.

A technique for identifying specific DNA sequences that are bound, in vivo, to proteins of interest. It involves formaldehyde fixation of CHROMATIN to crosslink the DNA-BINDING PROTEINS to the DNA. After shearing the DNA into small fragments, specific DNA-protein complexes are isolated by immunoprecipitation with protein-specific ANTIBODIES. Then, the DNA isolated from the complex can be identified by PCR amplification and sequencing.

Tritium is a radioactive isotope of hydrogen used in medical applications such as radiation therapy and as a tracer in diagnostic imaging.

Enzymes that catalyze the methylation of amino acids after their incorporation into a polypeptide chain. S-Adenosyl-L-methionine acts as the methylating agent. EC 2.1.1.

The spatial arrangement of the atoms of a nucleic acid or polynucleotide that results in its characteristic 3-dimensional shape.

A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.

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.

The male gonad containing two functional parts: the SEMINIFEROUS TUBULES for the production and transport of male germ cells (SPERMATOGENESIS) and the interstitial compartment containing LEYDIG CELLS that produce ANDROGENS.

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.

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.

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.

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.

The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.

The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.

Macromolecular molds for the synthesis of complementary macromolecules, as in DNA REPLICATION; GENETIC TRANSCRIPTION of DNA to RNA, and GENETIC TRANSLATION of RNA into POLYPEPTIDES.

A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms.

The process by which a DNA molecule is duplicated.

The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.

A family of histone acetyltransferases that is structurally-related to CREB-BINDING PROTEIN and to E1A-ASSOCIATED P300 PROTEIN. They function as transcriptional coactivators by bridging between DNA-binding TRANSCRIPTION FACTORS and the basal transcription machinery. They also modify transcription factors and CHROMATIN through ACETYLATION.

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.

Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.

Interruption or suppression of the expression of a gene at transcriptional or translational levels.

Structures within the nucleus of fungal cells consisting of or containing DNA, which carry genetic information essential to the cell.

Disruption of the secondary structure of nucleic acids by heat, extreme pH or chemical treatment. Double strand DNA is "melted" by dissociation of the non-covalent hydrogen bonds and hydrophobic interactions. Denatured DNA appears to be a single-stranded flexible structure. The effects of denaturation on RNA are similar though less pronounced and largely reversible.

Female germ cells derived from OOGONIA and termed OOCYTES when they enter MEIOSIS. The primary oocytes begin meiosis but are arrested at the diplotene state until OVULATION at PUBERTY to give rise to haploid secondary oocytes or ova (OVUM).

Proteins found in any species of fungus.

The functional hereditary units of INSECTS.

Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.

An enzyme capable of hydrolyzing highly polymerized DNA by splitting phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide. This catalyzes endonucleolytic cleavage of DNA yielding 5'-phosphodi- and oligonucleotide end-products. The enzyme has a preference for double-stranded DNA.

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.

Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes.

The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.

The commonest and widest ranging species of the clawed "frog" (Xenopus) in Africa. This species is used extensively in research. There is now a significant population in California derived from escaped laboratory animals.

A polynucleotide consisting essentially of chains with a repeating backbone of phosphate and ribose units to which nitrogenous bases are attached. RNA is unique among biological macromolecules in that it can encode genetic information, serve as an abundant structural component of cells, and also possesses catalytic activity. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)

Addition of methyl groups to DNA. DNA methyltransferases (DNA methylases) perform this reaction using S-ADENOSYLMETHIONINE as the methyl group donor.

The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.

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.

The restriction of a characteristic behavior, anatomical structure or physical system, such as immune response; metabolic response, or gene or gene variant to the members of one species. It refers to that property which differentiates one species from another but it is also used for phylogenetic levels higher or lower than the species.

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.

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.

Proteins prepared by recombinant DNA technology.

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.

Derivatives of BUTYRIC ACID. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain the carboxypropane structure.

Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.

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.

Elements of limited time intervals, contributing to particular results or situations.

Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.

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.

A multisubunit enzyme complex that regulates GENETIC TRANSCRIPTION by deacetylating the HISTONE residues of NUCLEOSOMES.

An aspect of protein kinase (EC 2.7.1.37) in which serine residues in protamines and histones are phosphorylated in the presence of ATP.

Electrophoresis in which a pH gradient is established in a gel medium and proteins migrate until they reach the site (or focus) at which the pH is equal to their isoelectric point.

A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

An essential amino acid. It is often added to animal feed.

A histone chaperone that facilitates nucleosome assembly by mediating the formation of the histone octamer and its transfer to DNA.

A cell line derived from cultured tumor cells.

Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.

Phosphoproteins are proteins that have been modified by the attachment of a phosphate group, which can regulate their activity and function in various cellular processes.

A fatty acid with anticonvulsant properties used in the treatment of epilepsy. The mechanisms of its therapeutic actions are not well understood. It may act by increasing GAMMA-AMINOBUTYRIC ACID levels in the brain or by altering the properties of voltage dependent sodium channels.

A subclass of enzymes of the transferase class that catalyze the transfer of a methyl group from one compound to another. (Dorland, 28th ed) EC 2.1.1.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in fungi.

Oxidoreductases, N-Demethylating are enzymes that catalyze the removal of methyl groups from nitrogen-containing compounds in the body.

Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.

A multisubunit polycomb protein complex that catalyzes the METHYLATION of chromosomal HISTONE H3. It works in conjunction with POLYCOMB REPRESSIVE COMPLEX 1 to effect EPIGENETIC REPRESSION.

A retinoblastoma-binding protein that is involved in CHROMATIN REMODELING, histone deacetylation, and repression of GENETIC TRANSCRIPTION. Although initially discovered as a retinoblastoma binding protein it has an affinity for core HISTONES and is a subunit of chromatin assembly factor-1 and polycomb repressive complex 2.

The systematic study of the global gene expression changes due to EPIGENETIC PROCESSES and not due to DNA base sequence changes.

A member of the p300-CBP transcription factor family that was initially identified as a binding partner for CAMP RESPONSE ELEMENT-BINDING PROTEIN. Mutations in CREB-binding protein are associated with RUBINSTEIN-TAYBI SYNDROME.

A four carbon acid, CH3CH2CH2COOH, with an unpleasant odor that occurs in butter and animal fat as the glycerol ester.

A DNA-dependent RNA polymerase present in bacterial, plant, and animal cells. It functions in the nucleoplasmic structure and transcribes DNA into RNA. It has different requirements for cations and salt than RNA polymerase I and is strongly inhibited by alpha-amanitin. EC 2.7.7.6.

A homologous family of regulatory enzymes that are structurally related to the protein silent mating type information regulator 2 (Sir2) found in Saccharomyces cerevisiae. Sirtuins contain a central catalytic core region which binds NAD. Several of the sirtuins utilize NAD to deacetylate proteins such as HISTONES and are categorized as GROUP III HISTONE DEACETYLASES. Several other sirtuin members utilize NAD to transfer ADP-RIBOSE to proteins and are categorized as MONO ADP-RIBOSE TRANSFERASES, while a third group of sirtuins appears to have both deacetylase and ADP ribose transferase activities.

Compounds consisting of chains of AMINO ACIDS alternating with CARBOXYLIC ACIDS via ester and amide linkages. They are commonly cyclized.

A sirtuin family member found primarily in the CYTOPLASM. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.

A family of histone molecular chaperones that play roles in sperm CHROMATIN decondensation and CHROMATIN ASSEMBLY in fertilized eggs. They were originally discovered in XENOPUS egg extracts as histone-binding factors that mediate nucleosome formation in vitro.

Enzymes that catalyze the methylation of arginine residues of proteins to yield N-mono- and N,N-dimethylarginine. This enzyme is found in many organs, primarily brain and spleen.

A member of the p300-CBP transcription factors that was originally identified as a binding partner for ADENOVIRUS E1A PROTEINS.

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.

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.

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 characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.

Somewhat flattened, globular echinoderms, having thin, brittle shells of calcareous plates. They are useful models for studying FERTILIZATION and EMBRYO DEVELOPMENT.

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.

Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.

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.

A histone chaperone protein that plays a role in the deposition of NUCLEOSOMES on newly synthesized DNA. It is comprised of three different subunits of 48, 60, and 150 kDa molecular size. The 48 kDa subunit, RETINOBLASTOMA-BINDING PROTEIN 4, is also a component of several other protein complexes involved in chromatin remodeling.

Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.

A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.

This ribonucleoprotein particle, composed of U7 snRNA, Sm core protein, and U7 snRNP-specific proteins, is involved in the 3'end processing of histone premessenger RNAs.

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.

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.

Macromolecular complexes formed from the association of defined protein subunits.

A pyrimidine analogue that inhibits DNA methyltransferase, impairing DNA methylation. It is also an antimetabolite of cytidine, incorporated primarily into RNA. Azacytidine has been used as an antineoplastic agent.

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.

An enzyme that catalyzes the transfer of a methyl group from S-ADENOSYLMETHIONINE to the 5-position of CYTOSINE residues in DNA.

Factors that are involved in directing the cleavage and POLYADENYLATION of the of MESSENGER RNA near the site of the RNA 3' POLYADENYLATION SIGNALS.

A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.

One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.

Phase of the CELL CYCLE following G1 and preceding G2 when the entire DNA content of the nucleus is replicated. It is achieved by bidirectional replication at multiple sites along each chromosome.

A retinoblastoma-binding protein that has an affinity for core HISTONES. It is found as a subunit of protein complexes that are in involved in the enzymatic modification of histones including the Mi2 and Sin3 histone deacetylase complexes and the polycomb repressive complex 2.

All of the processes involved in increasing CELL NUMBER including CELL DIVISION.

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.

Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in neoplastic tissue.

Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.

Areas of increased density of the dinucleotide sequence cytosine--phosphate diester--guanine. They form stretches of DNA several hundred to several thousand base pairs long. In humans there are about 45,000 CpG islands, mostly found at the 5' ends of genes. They are unmethylated except for those on the inactive X chromosome and some associated with imprinted genes.

A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.

The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.

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.

Theoretical representations that simulate the behavior or activity of genetic processes or phenomena. They include the use of mathematical equations, computers, and other electronic equipment.

A group of 6-alkyl SALICYLIC ACIDS that are found in ANACARDIUM and known for causing CONTACT DERMATITIS.

Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

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.

Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.

A retinoblastoma binding protein that is also a member of the Jumonji-domain histone demethylases. It has demethylation activity towards specific LYSINE residues found on HISTONE H3.

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.

A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.

A sirtuin family member found primarily in the CELL NUCLEUS. It is an NAD-dependent deacetylase with specificity towards HISTONES and a variety of proteins involved in gene regulation.

A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.

The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.

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 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.

A set of nuclear proteins in SACCHAROMYCES CEREVISIAE that are required for the transcriptional repression of the silent mating type loci. They mediate the formation of silenced CHROMATIN and repress both transcription and recombination at other loci as well. They are comprised of 4 non-homologous, interacting proteins, Sir1p, Sir2p, Sir3p, and Sir4p. Sir2p, an NAD-dependent HISTONE DEACETYLASE, is the founding member of the family of SIRTUINS.

The steps that generate the 3' ends of mature RNA molecules. For most mRNAs (RNA, MESSENGER), 3' end processing referred to as POLYADENYLATION includes the addition of POLY A.

Cells derived from the BLASTOCYST INNER CELL MASS which forms before implantation in the uterine wall. They retain the ability to divide, proliferate and provide progenitor cells that can differentiate into specialized cells.

Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.

A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.

Basic homopolyamino acids, histones and protamines are potent antagonists of angiogenin binding to ribonuclease inhibitor. (1/4598)

A radio-ribonuclease inhibitor assay based on the interaction of 125I-angiogenin with ribonuclease inhibitor (RI) was used to detect pancreatic-type ribonucleases and potential modulators of their action. We show that highly basic proteins including the homopolypeptides poly-arginine, poly-lysine and poly-ornithine, core histones, spermatid-specific S1 protein and the protamines HP3 and Z3 were strong inhibitors of angiogenin binding to RI. A minimum size of poly-arginine and poly-lysine was required for efficient inhibition. The inhibition likely resulted from direct association of the basic proteins with the acidic inhibitor, as RI bound to poly-lysine and protamines while 125I-angiogenin did not. Antagonists of the angiogenin-RI interaction are potential regulators of either angiogenin-triggered angiogenesis and/or intracellular RI function, depending on their preferential target. (+info)

Onset of nucleolar and extranucleolar transcription and expression of fibrillarin in macaque embryos developing in vitro. (2/4598)

Specific aims were to characterize the onset of nucleolar and extranucleolar transcription and expression of the nucleolar protein fibrillarin during preimplantation development in vitro in macaque embryos using autoradiographic and immunocytochemical techniques. Autoradiography was performed on whole embryos cultured with [3H]uridine for assessment of nucleolar (rRNA) and extranucleolar (mRNA) transcription. Expression of fibrillarin was immunocytochemically assessed in whole embryos using a primary antibody against fibrillarin and a fluorescein isothiocyanate-conjugated secondary antibody. Extranucleolar incorporation of [3H]uridine was first detected in 2-cell embryos cultured 6-10 h with [3H]uridine. Culture with alpha-amanitin prevented incorporation of label in 2-cell embryos, and treatment with ribonuclease reduced the signal to background levels, indicating that [3H]uridine was incorporated into mRNA and not rRNA or DNA. Nucleolar incorporation of [3H]uridine was not evident in pronucleate-stage or 2- to 5-cell embryos, but it was detected in one 6-cell embryo and in all 8-cell to blastocyst-stage embryos. Fibrillarin was first expressed in some 6- to 7-cell embryos, but it was consistently expressed in all 8-cell embryos. Fibrillarin was localized to the perimeter of the nucleolar precursor bodies, forming a ring that completely encapsulated these structures. Fibrillarin was not expressed in 8- to 16-cell embryos cultured with alpha-amanitin, indicating that it is transcribed, rather than recruited, at the 8-cell stage. In conclusion, in in vitro-fertilized macaque embryos developing in vitro, extranucleolar synthesis of mRNA is initiated at the 2-cell stage while the onset of nucleolar transcription occurs at the 6- to 8-cell stage, coincident with expression of fibrillarin. (+info)

MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. (3/4598)

Terminal cell differentiation is correlated with the extensive sequestering of previously active genes into compact transcriptionally inert heterochromatin. In vertebrate blood cells, these changes can be traced to the accumulation of a developmentally regulated heterochromatin protein, MENT. Cryoelectron microscopy of chicken granulocyte chromatin, which is highly enriched with MENT, reveals exceptionally compact polynucleosomes, which maintain a level of higher order folding above that imposed by linker histones. The amino acid sequence of MENT reveals a close structural relationship with serpins, a large family of proteins known for their ability to undergo dramatic conformational transitions. Conservation of the "hinge region" consensus in MENT indicates that this ability is retained by the protein. MENT is distinguished from the other serpins by being a basic protein, containing several positively charged surface clusters, which are likely to be involved in ionic interactions with DNA. One of the positively charged domains bears a significant similarity to the chromatin binding region of nuclear lamina proteins and with the A.T-rich DNA-binding motif, which may account for the targeting of MENT to peripheral heterochromatin. MENT ectopically expressed in a mammalian cell line is transported into nuclei and is associated with intranuclear foci of condensed chromatin. (+info)

Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin. (4/4598)

Chromatin assembly factor 1 (CAF-1) is required for inheritance of epigenetically determined chromosomal states in vivo and promotes assembly of chromatin during DNA replication in vitro. Herein, we demonstrate that after DNA replication, replicated, but not unreplicated, DNA is also competent for CAF-1-dependent chromatin assembly. The proliferating cell nuclear antigen (PCNA), a DNA polymerase clamp, is a component of the replication-dependent marking of DNA for chromatin assembly. The clamp loader, replication factor C (RFC), can reverse this mark by unloading PCNA from the replicated DNA. PCNA binds directly to p150, the largest subunit of CAF-1, and the two proteins colocalize at sites of DNA replication in cells. We suggest that PCNA and CAF-1 connect DNA replication to chromatin assembly and the inheritance of epigenetic chromosome states. (+info)

The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin. (5/4598)

Camptothecin is an antitumor agent that kills cells by converting DNA topoisomerase I into a DNA-damaging poison. Although camptothecin derivatives are now being used to treat tumors in a variety of clinical protocols, the cellular factors that influence sensitivity to the drug are only beginning to be understood. We report here that two genes required for sister chromatid cohesion, TRF4 and MCD1/SCC1, are also required to repair camptothecin-mediated damage to DNA. The hypersensitivity to camptothecin in the trf4 mutant does not result from elevated expression of DNA topoisomerase I. We show that Trf4 is a nuclear protein whose expression is cell cycle-regulated at a post-transcriptional level. Suppression of camptothecin hypersensitivity in the trf4 mutant by gene overexpression resulted in the isolation of three genes: another member of the TRF4 gene family, TRF5, and two genes that may influence higher order chromosome structure, ZDS1 and ZDS2. We have isolated and sequenced two human TRF4 family members, hTRF4-1 and hTRF4-2. The hTRF4-1 gene maps to chromosome 5p15, a region of frequent copy number alteration in several tumor types. The evolutionary conservation of TRF4 suggests that it may also influence mammalian cell sensitivity to camptothecin. (+info)

The RLF-B component of the replication licensing system is distinct from Cdc6 and functions after Cdc6 binds to chromatin. (6/4598)

Replication licensing factor (RLF) is an essential initiation factor that can prevent re-replication of DNA in a single cell cycle [1] [2]. It is required for the initiation of DNA replication, binds to chromatin early in the cell cycle, is removed from chromatin as DNA replicates and is unable to re-bind replicated chromatin until the following mitosis. Chromatography of RLF from Xenopus extracts has shown that it consists of two components termed RLF-B and RLF-M [3]. The RLF-M component consists of complexes of all six Xenopus minichromosome maintenance (MCM/P1) proteins (XMcm2-7), which bind to chromatin in late mitosis and are removed as replication occurs [3] [4] [5] [6] [7]. The identity of RLF-B is currently unknown. At least two factors must be present on chromatin before licensing can occur: the Xenopus origin recognition complex (XORC) [8] [9] and Xenopus Cdc6 (XCdc6) [10]. XORC saturates Xenopus sperm chromatin at approximately one copy per replication origin whereas XCdc6 binds to chromatin only if XORC is bound first [9] [10] [11]. Although XORC has been shown to be a distinct activity from RLF-B [9], the relationship between XCdc6 and RLF-B is currently unclear. Here, we show that active XCdc6 is loaded onto chromatin in extracts with defective RLF, and that both RLF-M and RLF-B are still required for the licensing of XCdc6-containing chromatin. Furthermore, RLF-B can be separated from XCdc6 by immunoprecipitation and standard chromatography. These experiments demonstrate that RLF-B is both functionally and physically distinct from XCdc6, and that XCdc6 is loaded onto chromatin before RLF-B function is executed. (+info)

Retardation of cell proliferation after expression of p202 accompanies an increase in p21(WAF1/CIP1). (7/4598)

p202 is an IFN-inducible, primarily nuclear, phosphoprotein (52-kDa) whose constitutive overexpression in transfected cells inhibits colony formation. To investigate the molecular mechanism(s) by which expression of p202 protein impairs colony formation, we established stable cell lines that inducibly express p202. Using this cell model, we demonstrate that the induced expression of p202 in asynchronous cultures of these cells was accompanied by: (a) an increase in steady-state levels of p21(WAF1/CIP1/SDI1) (p21) mRNA and protein; (b) a decrease in Cdk2 protein kinase activity; and (c) an increase in the functional form of retinoblastoma protein (pRb). Transient transfection of a p202-encoding plasmid in Saos-2 cells, which do not harbor a wild-type p53 protein, resulted in an increase in p21 protein, which indicated that p202 could regulate expression of p21 protein independent of p53 protein. Moreover, we demonstrate that expression of p202 in these cells increased cell doubling time without accumulation of cells in a particular phase of the cell cycle. Taken together, these results are consistent with the possibility that p202 protein contributes to the cell growth retardation activity of the IFNs, at least in part, by modulating p21 protein levels. (+info)

Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. (8/4598)

Examination of cells at the early stages of herpes simplex virus type 1 infection revealed that the viral immediate-early protein Vmw110 (also known as ICP0) formed discrete punctate accumulations associated with centromeres in both mitotic and interphase cells. The RING finger domain of Vmw110 (but not the C-terminal region) was essential for its localization at centromeres, thus distinguishing the Vmw110 sequences required for centromere association from those required for its localization at other discrete nuclear structures known as ND10, promyelocytic leukaemia (PML) bodies or PODs. We have shown recently that Vmw110 can induce the proteasome-dependent loss of several cellular proteins, including a number of probable SUMO-1-conjugated isoforms of PML, and this results in the disruption of ND10. In this study, we found some striking similarities between the interactions of Vmw110 with ND10 and centromeres. Specifically, centromeric protein CENP-C was lost from centromeres during virus infection in a Vmw110- and proteasome-dependent manner, causing substantial ultrastructural changes in the kinetochore. In consequence, dividing cells either became stalled in mitosis or underwent an unusual cytokinesis resulting in daughter cells with many micronuclei. These results emphasize the importance of CENP-C for mitotic progression and suggest that Vmw110 may be interfering with biochemical mechanisms which are relevant to both centromeres and ND10. (+info)

Chromosomal proteins, non-histone, are proteins that are not directly involved in the structure of chromatin but play important roles in various cellular processes related to chromosomes. These proteins are typically associated with specific regions of the chromosome and are involved in regulating gene expression, DNA replication, and DNA repair. Examples of non-histone chromosomal proteins include transcription factors, coactivators, and chromatin remodeling factors. Abnormalities in the expression or function of non-histone chromosomal proteins have been implicated in various diseases, including cancer and genetic disorders.

Histones are proteins that play a crucial role in the structure and function of DNA in cells. They are small, positively charged proteins that help to package and organize DNA into a compact structure called chromatin. Histones are found in the nucleus of eukaryotic cells and are essential for the proper functioning of genes. There are five main types of histones: H1, H2A, H2B, H3, and H4. Each type of histone has a specific role in the packaging and organization of DNA. For example, H3 and H4 are the most abundant histones and are responsible for the formation of nucleosomes, which are the basic unit of chromatin. H1 is a linker histone that helps to compact chromatin into a more condensed structure. In the medical field, histones have been studied in relation to various diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. For example, changes in the levels or modifications of histones have been linked to the development of certain types of cancer, such as breast cancer and prostate cancer. Additionally, histones have been shown to play a role in the regulation of gene expression, which is important for the proper functioning of cells.

High Mobility Group Proteins (HMG proteins) are a family of non-histone proteins that are involved in DNA packaging and regulation of gene expression. They are characterized by their ability to bind to DNA and move along it, hence their name. HMG proteins are found in all eukaryotic cells and play important roles in various cellular processes, including DNA replication, transcription, and repair. In the medical field, HMG proteins have been studied for their potential roles in various diseases, including cancer, neurological disorders, and cardiovascular disease. Some HMG proteins have also been developed as therapeutic targets for the treatment of these diseases.

Chromatin is a complex of DNA, RNA, and proteins that makes up the chromosomes in the nucleus of a cell. It plays a crucial role in regulating gene expression and maintaining the structure of the genome. In the medical field, chromatin is studied in relation to various diseases, including cancer, genetic disorders, and neurological conditions. For example, chromatin remodeling is a process that can alter the structure of chromatin and affect gene expression, and it has been implicated in the development of certain types of cancer. Additionally, chromatin-based therapies are being explored as potential treatments for diseases such as Alzheimer's and Parkinson's.

HMGN1 protein, also known as high mobility group protein 1, is a non-histone protein that plays a role in chromatin structure and gene regulation. It is a member of the high mobility group (HMG) family of proteins, which are characterized by their ability to bind to DNA and facilitate the opening of chromatin structure. HMGN1 protein is found in the nucleus of cells and is involved in a variety of cellular processes, including DNA replication, transcription, and repair. It is also involved in the regulation of gene expression, as it can bind to specific DNA sequences and affect the accessibility of DNA to transcription factors and other regulatory proteins. HMGN1 protein has been implicated in a number of diseases, including cancer, where it has been shown to be overexpressed in some tumor cells. It is also involved in the development of certain autoimmune diseases, such as systemic lupus erythematosus, and has been shown to play a role in the pathogenesis of some viral infections. Overall, HMGN1 protein is an important regulator of gene expression and chromatin structure, and its function is being studied in a variety of fields, including genetics, epigenetics, and cancer biology.

Histone deacetylases (HDACs) are a family of enzymes that remove acetyl groups from the lysine residues of histone proteins. Histones are proteins that help package and organize DNA into chromatin, which is the complex structure that makes up chromosomes. The addition or removal of acetyl groups to histones can affect the accessibility of DNA to the enzymes that read and write genetic information, and thus play a role in regulating gene expression. In the medical field, HDACs have been implicated in a variety of diseases, including cancer, neurodegenerative disorders, and inflammatory conditions. Some HDAC inhibitors have been developed as potential therapeutic agents for these diseases, as they can alter gene expression in ways that may be beneficial for treating the disease. For example, HDAC inhibitors have been shown to have anti-cancer effects by blocking the growth and proliferation of cancer cells, and to have anti-inflammatory effects by reducing the production of pro-inflammatory molecules.

Nucleoproteins are complex molecules that consist of a protein and a nucleic acid, either DNA or RNA. In the medical field, nucleoproteins play important roles in various biological processes, including gene expression, DNA replication, and DNA repair. One example of a nucleoprotein is histone, which is a protein that helps package DNA into a compact structure called chromatin. Histones are important for regulating gene expression, as they can affect the accessibility of DNA to transcription factors and other regulatory proteins. Another example of a nucleoprotein is ribonucleoprotein (RNP), which is a complex molecule that consists of RNA and one or more proteins. RNPs play important roles in various cellular processes, including mRNA processing, translation, and RNA interference. In the context of viral infections, nucleoproteins are often found in viral particles and play important roles in viral replication and pathogenesis. For example, the nucleoprotein of influenza virus is involved in the packaging of viral RNA into viral particles, while the nucleoprotein of HIV is involved in the regulation of viral gene expression. Overall, nucleoproteins are important molecules in the medical field, and their study can provide insights into various biological processes and diseases.

HMGB1 protein, also known as high mobility group box 1 protein, is a protein that is found in the nuclei of most cells in the human body. It is a member of a family of proteins called high mobility group (HMG) proteins, which are involved in the regulation of gene expression and the maintenance of chromatin structure. HMGB1 protein is normally located in the nucleus of cells, where it helps to regulate the activity of genes by binding to specific DNA sequences. However, under certain conditions, such as inflammation or tissue damage, HMGB1 can be released from the nucleus and enter the bloodstream. This can have a number of effects on the body, including the activation of immune cells and the promotion of tissue repair. In the medical field, HMGB1 protein is being studied as a potential biomarker for a variety of diseases, including cancer, cardiovascular disease, and neurodegenerative disorders. It is also being investigated as a potential therapeutic target for the treatment of these conditions.

In the medical field, nucleosomes are subunits of chromatin, which is the complex of DNA and proteins that makes up the chromosomes in the nucleus of a cell. Each nucleosome is composed of a segment of DNA wrapped around a core of eight histone proteins, which are positively charged and help to compact the DNA. The DNA in nucleosomes is typically about 146 base pairs long, and the histone proteins are arranged in a specific way to form a repeating unit that is about 11 nm in diameter. Nucleosomes play an important role in regulating gene expression by controlling access to the DNA by other proteins.

Histone Acetyltransferases (HATs) are enzymes that add acetyl groups to the lysine residues of histone proteins. Histones are proteins that help package and organize DNA into chromatin, which is the complex structure that makes up chromosomes. By adding acetyl groups to histones, HATs can modify the structure of chromatin, making it more open and accessible to the enzymes that read and write DNA. This modification is thought to play a role in regulating gene expression, as it can affect the ability of transcription factors to bind to DNA and activate or repress genes. HATs are important regulators of many cellular processes, including cell growth, differentiation, and metabolism. In the medical field, HATs are being studied as potential targets for the treatment of a variety of diseases, including cancer, neurological disorders, and inflammatory diseases.

DNA, or deoxyribonucleic acid, is a molecule that carries genetic information in living organisms. It is composed of four types of nitrogen-containing molecules called nucleotides, which are arranged in a specific sequence to form the genetic code. In the medical field, DNA is often studied as a tool for understanding and diagnosing genetic disorders. Genetic disorders are caused by changes in the DNA sequence that can affect the function of genes, leading to a variety of health problems. By analyzing DNA, doctors and researchers can identify specific genetic mutations that may be responsible for a particular disorder, and develop targeted treatments or therapies to address the underlying cause of the condition. DNA is also used in forensic science to identify individuals based on their unique genetic fingerprint. This is because each person's DNA sequence is unique, and can be used to distinguish one individual from another. DNA analysis is also used in criminal investigations to help solve crimes by linking DNA evidence to suspects or victims.

Deoxyribonucleoproteins (DNPs) are complexes of DNA and proteins that play important roles in the storage, replication, and expression of genetic information in cells. In the medical field, DNPs are often studied in the context of diseases such as cancer, where changes in the structure or function of DNPs can lead to the development or progression of the disease. DNPs are also important in the development of new treatments, such as gene therapies, which aim to correct or replace faulty DNA in order to treat or prevent disease.

Heterochromatin is a type of chromatin that is characterized by a darker staining intensity due to the presence of higher levels of the protein histone H3 that is methylated on lysine 9 (H3K9me). Heterochromatin is typically found in the centromeres and telomeres of chromosomes, as well as in regions of the genome that are not actively transcribed. In the medical field, heterochromatin is important because it plays a role in the regulation of gene expression and the maintenance of genomic stability. Abnormalities in heterochromatin structure or function have been linked to a number of diseases, including cancer, developmental disorders, and neurological disorders. For example, mutations in genes that are involved in the regulation of heterochromatin formation have been implicated in the development of certain types of cancer, such as breast cancer and prostate cancer. Additionally, changes in the structure or composition of heterochromatin have been observed in a number of neurological disorders, including Alzheimer's disease and Parkinson's disease.

Euchromatin is a type of chromatin, which is the complex of DNA and proteins that make up the chromosomes in the nucleus of a cell. Euchromatin is characterized by its loose, open structure, which allows for easy access to the DNA by transcription factors and other regulatory proteins. This makes euchromatin more active and transcriptionally permissive than heterochromatin, which is a more condensed and tightly packed form of chromatin that is generally transcriptionally inactive. Euchromatin is typically found in the intergenic regions of the genome, as well as in the promoters and enhancers of active genes. It plays an important role in regulating gene expression and is involved in a variety of cellular processes, including cell division, differentiation, and development.

Histone Deacetylase 1 (HDAC1) is an enzyme that plays a role in regulating gene expression by removing acetyl groups from histone proteins, which are the protein components of chromatin, the complex of DNA and proteins that makes up chromosomes. HDAC1 is a member of the histone deacetylase family of enzymes, which are involved in a variety of cellular processes, including cell growth, differentiation, and apoptosis. In the medical field, HDAC1 has been implicated in a number of diseases and conditions, including cancer, neurodegenerative disorders, and inflammatory diseases. For example, HDAC1 has been shown to be overexpressed in certain types of cancer, and its inhibition has been shown to have anti-cancer effects in preclinical studies. In addition, HDAC1 has been implicated in the development of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, and in the pathogenesis of inflammatory diseases such as rheumatoid arthritis and inflammatory bowel disease. Overall, HDAC1 is an important enzyme that plays a role in regulating gene expression and has been implicated in a number of diseases and conditions. Understanding the function of HDAC1 and developing inhibitors of this enzyme may have therapeutic potential for the treatment of these diseases.

HMGB2 protein is a type of non-histone chromosomal protein that is found in the nuclei of cells. It is a member of the high mobility group box (HMGB) family of proteins, which are involved in the regulation of gene expression and the maintenance of chromatin structure. HMGB2 protein is known to play a role in a variety of cellular processes, including cell growth, differentiation, and apoptosis. It has also been implicated in the development and progression of certain diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. In the medical field, HMGB2 protein is the subject of ongoing research as a potential therapeutic target for the treatment of these and other diseases.

Micrococcal nuclease (MNase) is a type of enzyme that is commonly used in molecular biology research to study the structure and function of DNA. It is derived from the bacterium Staphylococcus aureus and is a member of the DNase family of enzymes. MNase is a highly specific enzyme that cleaves DNA at the phosphodiester bond between the phosphate group and the sugar-phosphate backbone, leaving a 3' hydroxyl group and a 5' phosphate group. This enzyme is particularly useful for studying the structure of DNA, as it can be used to generate single-stranded DNA fragments that can be analyzed using a variety of molecular biology techniques. In the medical field, MNase is used in a variety of applications, including the study of chromatin structure, the analysis of DNA-protein interactions, and the development of new DNA-based therapies. It is also used in diagnostic tests to detect and identify bacterial infections, as well as in the treatment of certain types of cancer.

Bromouracil is a medication that is used to treat certain types of cancer, including leukemia and lymphoma. It works by interfering with the production of DNA and RNA, which are essential for the growth and reproduction of cancer cells. Bromouracil is usually given as a pill or a liquid, and it is usually taken in combination with other medications. It can cause side effects such as nausea, vomiting, and a decrease in the number of white blood cells.

Histone Deacetylase 2 (HDAC2) is an enzyme that plays a role in regulating gene expression by removing acetyl groups from histone proteins, which are the protein components of chromatin, the complex that makes up DNA in the nucleus of cells. HDAC2 is a member of the class IIa histone deacetylases, which are involved in a variety of cellular processes, including cell cycle regulation, differentiation, and apoptosis. In the medical field, HDAC2 has been implicated in a number of diseases and conditions, including cancer, neurodegenerative disorders, and cardiovascular disease. For example, HDAC2 has been shown to be overexpressed in certain types of cancer, and its inhibition has been shown to have anti-cancer effects in preclinical studies. In addition, HDAC2 has been implicated in the development of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease, and in the pathogenesis of cardiovascular disease. Overall, HDAC2 is an important enzyme that plays a role in regulating gene expression and is involved in a variety of cellular processes and diseases.

Histone demethylases are enzymes that remove methyl groups from the N-terminal tails of histone proteins. Histones are proteins that help package and organize DNA into chromatin, which is the complex structure that makes up chromosomes. Methylation of histones is an important mechanism for regulating gene expression, and histone demethylases play a key role in this process by reversing the effects of histone methylation. There are several different types of histone demethylases, including lysine-specific demethylases (KDMs) and arginine-specific demethylases (RDMs). These enzymes can remove methyl groups from different lysine and arginine residues on the histone proteins, and they can have different effects on gene expression. In the medical field, histone demethylases are being studied as potential therapeutic targets for a variety of diseases, including cancer, neurological disorders, and inflammatory diseases. For example, some researchers are investigating the use of histone demethylase inhibitors as cancer treatments, as these enzymes are often overactive in cancer cells and contribute to the development and progression of the disease. Other researchers are studying the role of histone demethylases in neurological disorders such as Alzheimer's disease and Parkinson's disease, as well as in inflammatory diseases such as rheumatoid arthritis.

Histone chaperones are proteins that assist in the assembly and disassembly of nucleosomes, which are the fundamental units of chromatin. They play a crucial role in regulating gene expression by facilitating the movement of histones, which are proteins that package DNA into a compact structure, onto and off of DNA. Histone chaperones also help to maintain the proper structure and stability of chromatin, which is essential for the proper functioning of DNA. In the medical field, histone chaperones are of interest because they have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Understanding the function of histone chaperones may lead to the development of new therapeutic strategies for these diseases.

Nuclear proteins are proteins that are found within the nucleus of a cell. The nucleus is the control center of the cell, where genetic material is stored and regulated. Nuclear proteins play a crucial role in many cellular processes, including DNA replication, transcription, and gene regulation. There are many different types of nuclear proteins, each with its own specific function. Some nuclear proteins are involved in the structure and organization of the nucleus itself, while others are involved in the regulation of gene expression. Nuclear proteins can also interact with other proteins, DNA, and RNA molecules to carry out their functions. In the medical field, nuclear proteins are often studied in the context of diseases such as cancer, where changes in the expression or function of nuclear proteins can contribute to the development and progression of the disease. Additionally, nuclear proteins are important targets for drug development, as they can be targeted to treat a variety of diseases.

DNA-binding proteins are a class of proteins that interact with DNA molecules to regulate gene expression. These proteins recognize specific DNA sequences and bind to them, thereby affecting the transcription of genes into messenger RNA (mRNA) and ultimately the production of proteins. DNA-binding proteins play a crucial role in many biological processes, including cell division, differentiation, and development. They can act as activators or repressors of gene expression, depending on the specific DNA sequence they bind to and the cellular context in which they are expressed. Examples of DNA-binding proteins include transcription factors, histones, and non-histone chromosomal proteins. Transcription factors are proteins that bind to specific DNA sequences and regulate the transcription of genes by recruiting RNA polymerase and other factors to the promoter region of a gene. Histones are proteins that package DNA into chromatin, and non-histone chromosomal proteins help to organize and regulate chromatin structure. DNA-binding proteins are important targets for drug discovery and development, as they play a central role in many diseases, including cancer, genetic disorders, and infectious diseases.

Hydroxamic acids are a class of organic compounds that contain a hydroxyl group (-OH) and an amine group (-NH2) attached to a carbonyl group (-CO-). They are commonly used in the medical field as chelating agents, which means they can bind to metal ions and help remove them from the body. One example of a hydroxamic acid used in medicine is ethylenediaminetetraacetic acid (EDTA), which is used to treat heavy metal poisoning. EDTA is a strong chelating agent that can bind to and remove toxic metal ions such as lead, mercury, and cadmium from the body. Hydroxamic acids are also used in the treatment of certain types of cancer, such as multiple myeloma. One example of a hydroxamic acid used in cancer treatment is hydroxycarbamide, which is used to treat myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML). In addition to their use as chelating agents and cancer treatments, hydroxamic acids have also been studied for their potential use in the treatment of other conditions, such as diabetes and Alzheimer's disease.

Histone-Lysine N-Methyltransferase (HKMT) is an enzyme that transfers a methyl group from S-adenosylmethionine (SAM) to the ε-amino group of a lysine residue on a histone protein. Histones are small proteins that package and organize DNA into chromatin, which is the basic unit of chromosomal structure in eukaryotic cells. HKMTs play a critical role in regulating gene expression by modifying the chromatin structure around specific genes. Specifically, they can add or remove methyl groups to histone tails, which can either promote or repress gene expression. For example, the addition of a methyl group to a lysine residue on the N-terminal tail of histone H3 (H3K4me3) is associated with active gene expression, while the addition of a methyl group to a lysine residue on the H3 tail (H3K9me3) is associated with gene repression. HKMTs are involved in many biological processes, including cell division, differentiation, and development. Dysregulation of HKMT activity has been implicated in various diseases, including cancer, neurological disorders, and cardiovascular disease. Therefore, understanding the function and regulation of HKMTs is an important area of research in the medical field.

HMGA1a protein is a high mobility group A1 protein that is encoded by the HMGA1A gene in humans. It is a non-histone chromosomal protein that plays a role in the regulation of gene expression and chromatin structure. HMGA1a protein is involved in various cellular processes, including cell proliferation, differentiation, and apoptosis. It has been implicated in the development and progression of several types of cancer, including breast, prostate, and lung cancer. In addition, HMGA1a protein has been shown to play a role in the regulation of immune responses and the development of autoimmune diseases.

HMGA proteins, also known as high mobility group A proteins, are a family of non-histone chromosomal proteins that play important roles in the regulation of gene expression and chromatin structure. They are highly conserved across different species and are found in both eukaryotic and prokaryotic cells. HMGA proteins are characterized by their ability to bind to DNA and alter its conformation, which can affect the accessibility of DNA to transcription factors and other regulatory proteins. They can also interact with other chromatin proteins, such as histones, to modulate chromatin structure and accessibility. In the medical field, HMGA proteins have been implicated in a variety of diseases, including cancer, developmental disorders, and neurological diseases. For example, overexpression of certain HMGA proteins has been associated with the development of certain types of cancer, such as breast, prostate, and lung cancer. In addition, mutations in HMGA genes have been linked to developmental disorders such as achondroplasia, a form of dwarfism. Overall, HMGA proteins play important roles in regulating gene expression and chromatin structure, and their dysregulation has been implicated in a variety of diseases.

Protamines are basic proteins that are derived from the amino acid arginine. They are primarily found in the sperm of many animals, including humans, and play a crucial role in the fertilization process. In the male reproductive system, protamines bind to DNA and help to condense it into a more compact structure that can be transported through the female reproductive tract. This process is essential for the survival and function of sperm cells. In addition to their role in fertilization, protamines have also been studied for their potential therapeutic applications. For example, they have been shown to have anti-inflammatory and anti-cancer properties, and are being investigated as potential treatments for a variety of diseases.

Transcription factors are proteins that regulate gene expression by binding to specific DNA sequences and controlling the transcription of genetic information from DNA to RNA. They play a crucial role in the development and function of cells and tissues in the body. In the medical field, transcription factors are often studied as potential targets for the treatment of diseases such as cancer, where their activity is often dysregulated. For example, some transcription factors are overexpressed in certain types of cancer cells, and inhibiting their activity may help to slow or stop the growth of these cells. Transcription factors are also important in the development of stem cells, which have the ability to differentiate into a wide variety of cell types. By understanding how transcription factors regulate gene expression in stem cells, researchers may be able to develop new therapies for diseases such as diabetes and heart disease. Overall, transcription factors are a critical component of gene regulation and have important implications for the development and treatment of many diseases.

HMGN proteins, also known as high-mobility group nucleosome-binding proteins, are a family of non-histone proteins that bind to DNA and regulate chromatin structure. They are involved in a variety of cellular processes, including transcription, DNA replication, and repair. HMGN proteins are characterized by their ability to bind to DNA in a non-sequence-specific manner and to increase the accessibility of DNA to other proteins. They are found in all eukaryotic cells and are encoded by multiple genes.

Amino acids are organic compounds that are the building blocks of proteins. They are composed of an amino group (-NH2), a carboxyl group (-COOH), and a side chain (R group) that varies in size and structure. There are 20 different amino acids that are commonly found in proteins, each with a unique side chain that gives it distinct chemical and physical properties. In the medical field, amino acids are important for a variety of functions, including the synthesis of proteins, enzymes, and hormones. They are also involved in energy metabolism and the maintenance of healthy tissues. Deficiencies in certain amino acids can lead to a range of health problems, including muscle wasting, anemia, and neurological disorders. In some cases, amino acids may be prescribed as supplements to help treat these conditions or to support overall health and wellness.

Saccharomyces cerevisiae proteins are proteins that are produced by the yeast species Saccharomyces cerevisiae. This yeast is commonly used in the production of bread, beer, and wine, as well as in scientific research. In the medical field, S. cerevisiae proteins have been studied for their potential use in the treatment of various diseases, including cancer, diabetes, and neurodegenerative disorders. Some S. cerevisiae proteins have also been shown to have anti-inflammatory and immunomodulatory effects, making them of interest for the development of new therapies.

Repressor proteins are a class of proteins that regulate gene expression by binding to specific DNA sequences and preventing the transcription of the associated gene. They are often involved in controlling the expression of genes that are involved in cellular processes such as metabolism, growth, and differentiation. Repressor proteins can be classified into two main types: transcriptional repressors and post-transcriptional repressors. Transcriptional repressors bind to specific DNA sequences near the promoter region of a gene, which prevents the binding of RNA polymerase and other transcription factors, thereby inhibiting the transcription of the gene. Post-transcriptional repressors, on the other hand, bind to the mRNA of a gene, which prevents its translation into protein or causes its degradation, thereby reducing the amount of protein produced. Repressor proteins play important roles in many biological processes, including development, differentiation, and cellular response to environmental stimuli. They are also involved in the regulation of many diseases, including cancer, neurological disorders, and metabolic disorders.

Archaeal proteins are proteins that are encoded by the genes of archaea, a group of single-celled microorganisms that are distinct from bacteria and eukaryotes. Archaeal proteins are characterized by their unique amino acid sequences and structures, which have been the subject of extensive research in the field of biochemistry and molecular biology. In the medical field, archaeal proteins have been studied for their potential applications in various areas, including drug discovery, biotechnology, and medical diagnostics. For example, archaeal enzymes have been used as biocatalysts in the production of biofuels and other valuable chemicals, and archaeal proteins have been explored as potential targets for the development of new antibiotics and other therapeutic agents. In addition, archaeal proteins have been used as diagnostic markers for various diseases, including cancer and infectious diseases. For example, certain archaeal proteins have been found to be overexpressed in certain types of cancer cells, and they have been proposed as potential biomarkers for the early detection and diagnosis of these diseases. Overall, archaeal proteins represent a rich source of novel biological molecules with potential applications in a wide range of fields, including medicine.

In the medical field, RNA, Messenger (mRNA) refers to a type of RNA molecule that carries genetic information from DNA in the nucleus of a cell to the ribosomes, where proteins are synthesized. During the process of transcription, the DNA sequence of a gene is copied into a complementary RNA sequence called messenger RNA (mRNA). This mRNA molecule then leaves the nucleus and travels to the cytoplasm of the cell, where it binds to ribosomes and serves as a template for the synthesis of a specific protein. The sequence of nucleotides in the mRNA molecule determines the sequence of amino acids in the protein that is synthesized. Therefore, changes in the sequence of nucleotides in the mRNA molecule can result in changes in the amino acid sequence of the protein, which can affect the function of the protein and potentially lead to disease. mRNA molecules are often used in medical research and therapy as a way to introduce new genetic information into cells. For example, mRNA vaccines work by introducing a small piece of mRNA that encodes for a specific protein, which triggers an immune response in the body.

Jumonji domain-containing histone demethylases (JHDMs) are a family of enzymes that remove methyl groups from histone proteins, which are the proteins that make up the "packaging" of DNA in cells. Histone methylation is an important mechanism for regulating gene expression, and changes in histone methylation patterns have been implicated in a variety of diseases, including cancer. JHDMs are thought to play a role in regulating gene expression by removing methyl groups from specific sites on histone proteins, which can lead to changes in the accessibility of DNA to the machinery that reads and transcribes genes. There are several different types of JHDMs, and they are classified based on the specific domain that they contain and their substrate specificity.

Drosophila proteins are proteins that are found in the fruit fly Drosophila melanogaster, which is a widely used model organism in genetics and molecular biology research. These proteins have been studied extensively because they share many similarities with human proteins, making them useful for understanding the function and regulation of human genes and proteins. In the medical field, Drosophila proteins are often used as a model for studying human diseases, particularly those that are caused by genetic mutations. By studying the effects of these mutations on Drosophila proteins, researchers can gain insights into the underlying mechanisms of these diseases and potentially identify new therapeutic targets. Drosophila proteins have also been used to study a wide range of biological processes, including development, aging, and neurobiology. For example, researchers have used Drosophila to study the role of specific genes and proteins in the development of the nervous system, as well as the mechanisms underlying age-related diseases such as Alzheimer's and Parkinson's.

Deoxyribonucleases (DNases) are enzymes that break down DNA molecules into smaller fragments. In the medical field, DNases are used to treat a variety of conditions, including: 1. Pulmonary fibrosis: DNases are used to break down excess DNA in the lungs, which can accumulate in people with pulmonary fibrosis and contribute to the scarring of lung tissue. 2. Cystic fibrosis: DNases are used to break down excess DNA in the airways of people with cystic fibrosis, which can help to reduce the buildup of mucus and improve lung function. 3. Inflammatory bowel disease: DNases are used to break down DNA in the gut, which can help to reduce inflammation and improve symptoms in people with inflammatory bowel disease. 4. Cancer: DNases are being studied as a potential treatment for cancer, as they may be able to help to break down DNA in cancer cells and kill them. DNases are typically administered as a medication, either by inhalation or injection. They are generally considered safe and well-tolerated, although they can cause side effects such as fever, chills, and nausea.

Acetyltransferases are a group of enzymes that transfer an acetyl group from acetyl-CoA to other molecules, such as amino acids, lipids, and nucleotides. These enzymes play important roles in various biological processes, including energy metabolism, biosynthesis of fatty acids and cholesterol, and regulation of gene expression. In the medical field, acetyltransferases are of particular interest because they are involved in the metabolism of drugs and toxins. For example, some drugs are metabolized by acetyltransferases, which can affect their efficacy and toxicity. Additionally, certain toxins can be activated by acetyltransferases, leading to toxic effects on the body. There are several types of acetyltransferases, including N-acetyltransferases (NATs), acetyl-CoA carboxylase (ACC), and acetylcholinesterase (AChE). NATs are involved in the metabolism of drugs and toxins, while ACC is involved in the biosynthesis of fatty acids and cholesterol. AChE is an enzyme that breaks down the neurotransmitter acetylcholine, and is important for proper functioning of the nervous system.

Cell cycle proteins are a group of proteins that play a crucial role in regulating the progression of the cell cycle. The cell cycle is a series of events that a cell goes through in order to divide and produce two daughter cells. It consists of four main phases: G1 (Gap 1), S (Synthesis), G2 (Gap 2), and M (Mitosis). Cell cycle proteins are involved in regulating the progression of each phase of the cell cycle, ensuring that the cell divides correctly and that the daughter cells have the correct number of chromosomes. Some of the key cell cycle proteins include cyclins, cyclin-dependent kinases (CDKs), and checkpoint proteins. Cyclins are proteins that are synthesized and degraded in a cyclic manner throughout the cell cycle. They bind to CDKs, which are enzymes that regulate cell cycle progression by phosphorylating target proteins. The activity of CDKs is tightly regulated by cyclins, ensuring that the cell cycle progresses in a controlled manner. Checkpoint proteins are proteins that monitor the cell cycle and ensure that the cell does not proceed to the next phase until all the necessary conditions are met. If any errors are detected, checkpoint proteins can halt the cell cycle and activate repair mechanisms to correct the problem. Overall, cell cycle proteins play a critical role in maintaining the integrity of the cell cycle and ensuring that cells divide correctly. Disruptions in the regulation of cell cycle proteins can lead to a variety of diseases, including cancer.

Tritium is a radioactive isotope of hydrogen with the atomic number 3 and the symbol T. It is a beta emitter with a half-life of approximately 12.3 years. In the medical field, tritium is used in a variety of applications, including: 1. Medical imaging: Tritium is used in nuclear medicine to label molecules and track their movement within the body. For example, tritium can be used to label antibodies, which can then be injected into the body to track the movement of specific cells or tissues. 2. Radiation therapy: Tritium is used in radiation therapy to treat certain types of cancer. It is typically combined with other isotopes, such as carbon-14 or phosphorus-32, to create a radioactive tracer that can be injected into the body and targeted to specific areas of cancerous tissue. 3. Research: Tritium is also used in research to study the behavior of molecules and cells. For example, tritium can be used to label DNA, which can then be used to study the process of DNA replication and repair. It is important to note that tritium is a highly radioactive isotope and requires careful handling to minimize the risk of exposure to radiation.

Protein methyltransferases (PMTs) are enzymes that transfer a methyl group (a carbon atom bonded to three hydrogen atoms) from a methyl donor molecule (such as S-adenosylmethionine) to a specific amino acid residue on a protein molecule. This process is known as protein methylation and can have a variety of effects on the structure, function, and regulation of the protein. In the medical field, PMTs are of interest because they play a role in many biological processes, including gene expression, signal transduction, and cell division. Abnormal activity of PMTs has been implicated in a number of diseases, including cancer, neurological disorders, and cardiovascular disease. As such, PMTs are the subject of ongoing research in the field of medicine, with the goal of developing new therapeutic strategies based on their role in disease pathogenesis.

P300-CBP transcription factors are a group of proteins that play a crucial role in regulating gene expression in the human body. They are composed of two subunits, p300 and CREB-binding protein (CBP), which work together to modulate the activity of other transcription factors and regulate the expression of specific genes. P300 and CBP are both large, multi-domain proteins that are involved in a wide range of cellular processes, including cell growth, differentiation, and apoptosis. They are also involved in the regulation of gene expression by interacting with other transcription factors and chromatin-modifying enzymes. In the medical field, p300-CBP transcription factors are of particular interest because they have been implicated in a number of diseases, including cancer, neurodegenerative disorders, and inflammatory diseases. For example, mutations in the genes encoding p300 and CBP have been linked to several forms of cancer, including acute myeloid leukemia and colorectal cancer. Additionally, dysregulation of p300-CBP transcription factors has been implicated in the development of neurodegenerative disorders such as Alzheimer's disease and Parkinson's disease. Overall, p300-CBP transcription factors are important regulators of gene expression that play a critical role in maintaining cellular homeostasis. Understanding the function and regulation of these proteins may provide new insights into the pathogenesis of various diseases and lead to the development of novel therapeutic strategies.

In the medical field, a peptide fragment refers to a short chain of amino acids that are derived from a larger peptide or protein molecule. Peptide fragments can be generated through various techniques, such as enzymatic digestion or chemical cleavage, and are often used in diagnostic and therapeutic applications. Peptide fragments can be used as biomarkers for various diseases, as they may be present in the body at elevated levels in response to specific conditions. For example, certain peptide fragments have been identified as potential biomarkers for cancer, neurodegenerative diseases, and cardiovascular disease. In addition, peptide fragments can be used as therapeutic agents themselves. For example, some peptide fragments have been shown to have anti-inflammatory or anti-cancer properties, and are being investigated as potential treatments for various diseases. Overall, peptide fragments play an important role in the medical field, both as diagnostic tools and as potential therapeutic agents.

Fungal proteins are proteins that are produced by fungi. They can be found in various forms, including extracellular proteins, secreted proteins, and intracellular proteins. Fungal proteins have a wide range of functions, including roles in metabolism, cell wall synthesis, and virulence. In the medical field, fungal proteins are of interest because some of them have potential therapeutic applications, such as in the treatment of fungal infections or as vaccines against fungal diseases. Additionally, some fungal proteins have been shown to have anti-cancer properties, making them potential targets for the development of new cancer treatments.

Deoxyribonuclease I (DNase I) is an enzyme that breaks down DNA molecules into smaller fragments. It is commonly used in molecular biology research to digest DNA samples for various applications such as DNA sequencing, Southern blotting, and restriction enzyme digestion. In the medical field, DNase I is used to treat certain lung diseases such as cystic fibrosis and acute respiratory distress syndrome (ARDS), where the lungs become inflamed and produce excess mucus that can obstruct airways. DNase I can help break down the excess mucus, making it easier to clear from the lungs. It is also used in some laboratory tests to detect the presence of DNA in biological samples.

Cyanogen bromide is a highly toxic chemical compound that is not commonly used in the medical field. It is a colorless gas that is highly reactive and can cause severe respiratory and cardiovascular problems if inhaled or ingested. In the past, cyanogen bromide was used as a pesticide and in the production of certain chemicals, but its use has been largely discontinued due to its toxicity. In the medical field, cyanogen bromide is not used for any therapeutic or diagnostic purposes. It is important to note that exposure to cyanogen bromide can be extremely dangerous and should be avoided at all costs.

RNA, or ribonucleic acid, is a type of nucleic acid that is involved in the process of protein synthesis in cells. It is composed of a chain of nucleotides, which are made up of a sugar molecule, a phosphate group, and a nitrogenous base. There are three types of RNA: messenger RNA (mRNA), transfer RNA (tRNA), and ribosomal RNA (rRNA). In the medical field, RNA is often studied as a potential target for the development of new drugs and therapies. For example, some researchers are exploring the use of RNA interference (RNAi) to silence specific genes and treat diseases such as cancer and viral infections. Additionally, RNA is being studied as a potential biomarker for various diseases, as changes in the levels or structure of certain RNA molecules can indicate the presence of a particular condition.

Proteins are complex biomolecules made up of amino acids that play a crucial role in many biological processes in the human body. In the medical field, proteins are studied extensively as they are involved in a wide range of functions, including: 1. Enzymes: Proteins that catalyze chemical reactions in the body, such as digestion, metabolism, and energy production. 2. Hormones: Proteins that regulate various bodily functions, such as growth, development, and reproduction. 3. Antibodies: Proteins that help the immune system recognize and neutralize foreign substances, such as viruses and bacteria. 4. Transport proteins: Proteins that facilitate the movement of molecules across cell membranes, such as oxygen and nutrients. 5. Structural proteins: Proteins that provide support and shape to cells and tissues, such as collagen and elastin. Protein abnormalities can lead to various medical conditions, such as genetic disorders, autoimmune diseases, and cancer. Therefore, understanding the structure and function of proteins is essential for developing effective treatments and therapies for these conditions.

Recombinant proteins are proteins that are produced by genetically engineering bacteria, yeast, or other organisms to express a specific gene. These proteins are typically used in medical research and drug development because they can be produced in large quantities and are often more pure and consistent than proteins that are extracted from natural sources. Recombinant proteins can be used for a variety of purposes in medicine, including as diagnostic tools, therapeutic agents, and research tools. For example, recombinant versions of human proteins such as insulin, growth hormones, and clotting factors are used to treat a variety of medical conditions. Recombinant proteins can also be used to study the function of specific genes and proteins, which can help researchers understand the underlying causes of diseases and develop new treatments.

Recombinant fusion proteins are proteins that are produced by combining two or more genes in a single molecule. These proteins are typically created using genetic engineering techniques, such as recombinant DNA technology, to insert one or more genes into a host organism, such as bacteria or yeast, which then produces the fusion protein. Fusion proteins are often used in medical research and drug development because they can have unique properties that are not present in the individual proteins that make up the fusion. For example, a fusion protein might be designed to have increased stability, improved solubility, or enhanced targeting to specific cells or tissues. Recombinant fusion proteins have a wide range of applications in medicine, including as therapeutic agents, diagnostic tools, and research reagents. Some examples of recombinant fusion proteins used in medicine include antibodies, growth factors, and cytokines.

Butyrates are a group of fatty acids that are derived from butyric acid. They are commonly used in the medical field as a source of energy for the body, particularly for patients who are unable to digest other types of fats. Butyrates are also used in the treatment of certain medical conditions, such as inflammatory bowel disease and liver disease. They have been shown to have anti-inflammatory and immunomodulatory effects, and may help to improve gut health and reduce symptoms of these conditions.

The Sin3 Histone Deacetylase and Corepressor Complex is a protein complex that plays a role in regulating gene expression in cells. It is composed of several proteins, including the Sin3A and Sin3B proteins, which are histone deacetylases (HDACs), and other corepressor proteins. HDACs are enzymes that remove acetyl groups from histone proteins, which are proteins that help package DNA into chromatin. By removing these acetyl groups, HDACs can compact chromatin and make it more difficult for genes to be expressed. The Sin3 Histone Deacetylase and Corepressor Complex helps to regulate gene expression by recruiting other proteins that can further compact chromatin and prevent genes from being expressed. This complex is involved in a variety of cellular processes, including cell growth and differentiation, and is dysregulated in several diseases, including cancer.

Protamine kinase is an enzyme that is involved in the regulation of blood clotting. It is responsible for converting protamine sulfate, a substance that is used to neutralize the anticoagulant effects of heparin, into protamine. Protamine sulfate is often used in conjunction with heparin during medical procedures, such as surgery or catheterization, to prevent excessive bleeding. Protamine kinase helps to ensure that the appropriate amount of protamine is present to neutralize the heparin, preventing the formation of blood clots.

Lysine is an essential amino acid that is required for the growth and maintenance of tissues in the human body. It is one of the nine essential amino acids that cannot be synthesized by the body and must be obtained through the diet. Lysine plays a crucial role in the production of proteins, including enzymes, hormones, and antibodies. It is also involved in the absorption of calcium and the production of niacin, a B vitamin that is important for energy metabolism and the prevention of pellagra. In the medical field, lysine is used to treat and prevent various conditions, including: 1. Herpes simplex virus (HSV): Lysine supplements have been shown to reduce the frequency and severity of outbreaks of HSV-1 and HSV-2, which cause cold sores and genital herpes, respectively. 2. Cold sores: Lysine supplements can help reduce the frequency and severity of cold sore outbreaks by inhibiting the replication of the herpes simplex virus. 3. Depression: Lysine has been shown to increase levels of serotonin, a neurotransmitter that regulates mood, in the brain. 4. Hair loss: Lysine is important for the production of hair, and deficiency in lysine has been linked to hair loss. 5. Wound healing: Lysine is involved in the production of collagen, a protein that is important for wound healing. Overall, lysine is an important nutrient that plays a crucial role in many aspects of human health and is used in the treatment and prevention of various medical conditions.

Nucleosome Assembly Protein 1 (NAP1) is a protein that plays a crucial role in the assembly of nucleosomes, which are the basic unit of chromatin. Nucleosomes consist of DNA wrapped around a core of eight histone proteins, and NAP1 helps to organize and compact the DNA by facilitating the binding of histones to the DNA. In the medical field, NAP1 has been implicated in various diseases, including cancer. For example, mutations in the NAP1 gene have been associated with a rare form of childhood leukemia called acute myeloid leukemia (AML). Additionally, NAP1 has been shown to play a role in the development of other types of cancer, such as breast cancer and colon cancer. NAP1 has also been studied in the context of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. In these conditions, NAP1 has been found to be involved in the regulation of protein aggregation and the clearance of misfolded proteins from cells. Overall, NAP1 is an important protein in the regulation of chromatin structure and function, and its role in various diseases is an active area of research.

Phosphoproteins are proteins that have been modified by the addition of a phosphate group to one or more of their amino acid residues. This modification is known as phosphorylation, and it is a common post-translational modification that plays a critical role in regulating many cellular processes, including signal transduction, metabolism, and gene expression. Phosphoproteins are involved in a wide range of biological functions, including cell growth and division, cell migration and differentiation, and the regulation of gene expression. They are also involved in many diseases, including cancer, diabetes, and cardiovascular disease. Phosphoproteins can be detected and studied using a variety of techniques, including mass spectrometry, Western blotting, and immunoprecipitation. These techniques allow researchers to identify and quantify the phosphorylation status of specific proteins in cells and tissues, and to study the effects of changes in phosphorylation on protein function and cellular processes.

Valproic acid is a medication that is primarily used to treat epilepsy and bipolar disorder. It is also sometimes used to treat migraines and other types of seizures. Valproic acid works by increasing the levels of certain chemicals in the brain that help to regulate mood and prevent seizures. It is usually taken in the form of a pill or liquid and is usually taken once or twice a day. Valproic acid can cause side effects such as dizziness, drowsiness, nausea, and stomach pain. It can also cause more serious side effects such as liver damage and blood disorders, so it is important to take it only as directed by a doctor.

Methyltransferases are a group of enzymes that transfer a methyl group (a carbon atom bonded to three hydrogen atoms) from one molecule to another. In the medical field, methyltransferases play important roles in various biological processes, including DNA methylation, RNA methylation, and protein methylation. DNA methylation is a process in which a methyl group is added to the cytosine base of DNA, which can affect gene expression. Methyltransferases that are involved in DNA methylation are called DNA methyltransferases (DNMTs). Abnormalities in DNA methylation have been linked to various diseases, including cancer, neurological disorders, and developmental disorders. RNA methylation is a process in which a methyl group is added to the ribose sugar or the nitrogenous base of RNA. Methyltransferases that are involved in RNA methylation are called RNA methyltransferases (RNMTs). RNA methylation can affect the stability, localization, and translation of RNA molecules. Protein methylation is a process in which a methyl group is added to the amino acid residues of proteins. Methyltransferases that are involved in protein methylation are called protein methyltransferases (PMTs). Protein methylation can affect protein-protein interactions, protein stability, and protein function. Overall, methyltransferases play important roles in regulating gene expression, RNA stability, and protein function, and their dysfunction can contribute to the development of various diseases.

Oxidoreductases, N-demethylating are a group of enzymes that catalyze the removal of a methyl group from a nitrogen atom in a molecule. These enzymes are important in the metabolism of many drugs and other compounds, as the removal of a methyl group can alter the chemical properties of the molecule and affect its activity. In the medical field, these enzymes are often studied in the context of drug metabolism and the development of new drugs. They may also be targeted for therapeutic purposes, for example in the treatment of certain types of cancer.

Polycomb Repressive Complex 2 (PRC2) is a protein complex that plays a crucial role in regulating gene expression in the epigenetic landscape of cells. It is composed of several subunits, including EZH2, EED, and SUZ12, and is responsible for adding a chemical modification called trimethylated lysine 27 on histone H3 (H3K27me3) at specific regions of the genome. This modification is associated with gene silencing and is involved in various biological processes, including embryonic development, cell differentiation, and cancer. PRC2 is also involved in the maintenance of stable epigenetic states during cell division and differentiation. In the medical field, PRC2 has been implicated in several diseases, including cancer. Abnormal activity of PRC2 has been observed in various types of cancer, including breast, prostate, and lung cancer, and is associated with poor prognosis. Targeting PRC2 has been proposed as a potential therapeutic strategy for cancer treatment.

Retinoblastoma-Binding Protein 4 (RBBP4) is a protein that plays a role in the regulation of gene expression. It is encoded by the RBBP4 gene and is found in the nucleus of cells. RBBP4 is a component of the Retinoblastoma protein (pRb) pathway, which is involved in the regulation of cell cycle progression and the prevention of uncontrolled cell growth. In the context of retinoblastoma, a type of eye cancer that occurs in children, RBBP4 has been shown to play a role in the development and progression of the disease. It is thought to do this by interacting with and regulating the activity of the pRb protein.

CREB-Binding Protein (CREB) is a transcriptional coactivator that plays a critical role in regulating gene expression in response to various stimuli, including hormones, growth factors, and stress. In the medical field, CREB is often studied in the context of various diseases and disorders, including cancer, neurodegenerative diseases, and psychiatric disorders. CREB is a member of the CREB/ATF family of transcription factors, which are activated by phosphorylation in response to extracellular signals. Once activated, CREB binds to specific DNA sequences called cAMP response elements (CREs) in the promoter regions of target genes, leading to their transcription and subsequent protein production. In cancer, CREB has been shown to play a role in regulating the expression of genes involved in cell proliferation, survival, and invasion. In neurodegenerative diseases such as Alzheimer's and Parkinson's disease, CREB has been implicated in regulating the expression of genes involved in synaptic plasticity and memory formation. In psychiatric disorders such as depression and anxiety, CREB has been shown to play a role in regulating the expression of genes involved in mood regulation and stress response. Overall, the regulation of CREB activity is a critical mechanism for controlling gene expression in response to various stimuli, and dysregulation of CREB activity has been implicated in a wide range of diseases and disorders.

Butyric acid is a short-chain fatty acid that is produced by the breakdown of dietary fiber in the large intestine by gut bacteria. It is a major constituent of the gut microbiota and plays an important role in maintaining gut health. In the medical field, butyric acid has been studied for its potential therapeutic effects in a variety of conditions, including inflammatory bowel disease, obesity, diabetes, and cancer. It has been shown to have anti-inflammatory, anti-cancer, and anti-diabetic properties, and may help to regulate the immune system and improve gut barrier function. Butyric acid is also used as a food additive and is found in a variety of foods, including cheese, butter, and yogurt. It has a distinctive sour or rancid smell and taste, and is often used to add flavor to foods.

RNA Polymerase II (Pol II) is an enzyme that plays a crucial role in the process of transcription, which is the first step in gene expression. It is responsible for synthesizing messenger RNA (mRNA) from a DNA template, which is then used by ribosomes to produce proteins. In the medical field, RNA Polymerase II is of great interest because it is involved in the expression of many genes that are important for normal cellular function. Mutations or defects in the genes that encode RNA Polymerase II or its associated proteins can lead to a variety of diseases, including some forms of cancer, neurological disorders, and developmental disorders. RNA Polymerase II is also a target for drugs that are designed to treat these diseases. For example, some drugs work by inhibiting the activity of RNA Polymerase II, while others work by modulating the expression of genes that are regulated by this enzyme.

Sirtuins are a family of proteins that play a role in regulating cellular processes such as metabolism, stress resistance, and aging. They are named after the yeast protein Sir2, which was the first sirtuin to be discovered. There are seven sirtuin proteins in humans, which are encoded by different genes and are found in various tissues throughout the body. These proteins are involved in a wide range of cellular processes, including DNA repair, transcriptional regulation, and the metabolism of carbohydrates, lipids, and proteins. Research has suggested that sirtuins may have potential therapeutic applications in a variety of diseases, including diabetes, obesity, cancer, and neurodegenerative disorders. Some studies have also suggested that sirtuin activators, which are compounds that stimulate the activity of sirtuins, may have anti-aging effects and help to protect against age-related diseases. However, more research is needed to fully understand the role of sirtuins in health and disease and to determine the potential therapeutic benefits of sirtuin activators.

Depsipeptides are a class of biomolecules that are composed of both amino acids and hydroxy acids. They are also known as depsomino acids or depsomino peptides. Depsipeptides are formed by the condensation of an amino acid with a hydroxy acid, typically serine or threonine, through a peptide bond. They are structurally similar to peptides, but with an additional hydroxyl group on the side chain of the amino acid. Depsipeptides have a wide range of biological activities and are found in various natural products, including antibiotics, antifungal agents, and cytotoxic compounds. They have also been used in the development of new drugs for the treatment of various diseases, including cancer, viral infections, and neurological disorders.

Sirtuin 2 (SIRT2) is a protein that belongs to the sirtuin family of enzymes. It is a NAD+-dependent deacetylase that is involved in a variety of cellular processes, including DNA repair, metabolism, and stress response. In the medical field, SIRT2 has been implicated in a number of diseases, including cancer, neurodegenerative disorders, and cardiovascular disease. Research has suggested that SIRT2 may play a role in the development and progression of these diseases by regulating the activity of various cellular pathways. For example, SIRT2 has been shown to regulate the activity of the p53 tumor suppressor protein, which plays a key role in preventing the development of cancer. Additionally, SIRT2 has been shown to regulate the activity of the FOXO transcription factors, which are involved in regulating metabolism and stress response. Overall, SIRT2 is an important protein that is being studied in the medical field for its potential role in the development and treatment of various diseases.

Nucleoplasmins are a family of highly conserved, acidic, and highly charged proteins that are found in the nuclei of eukaryotic cells. They are involved in a variety of nuclear processes, including chromatin remodeling, DNA replication, and transcription. Nucleoplasmins are also involved in the transport of DNA and RNA between the nucleus and the cytoplasm. They are composed of a central acidic domain and a basic domain, which allows them to bind to both DNA and RNA. Nucleoplasmins are important for the proper functioning of the nucleus and are involved in many diseases, including cancer and neurological disorders.

Protein-Arginine N-Methyltransferases (PRMTs) are a family of enzymes that catalyze the transfer of a methyl group from S-adenosylmethionine (SAM) to the amino group of arginine residues in proteins. This post-translational modification, known as arginine methylation, can regulate protein function, localization, and stability, and plays important roles in various biological processes, including gene expression, signal transduction, and chromatin remodeling. PRMTs are divided into three classes based on their substrate specificity and mechanism of action: type I PRMTs, type II PRMTs, and type III PRMTs. Dysregulation of PRMT activity has been implicated in various diseases, including cancer, neurological disorders, and autoimmune diseases.

E1A-Associated p300 Protein is a protein that is involved in the regulation of gene expression. It is a component of a complex that is involved in the transcriptional activation of certain genes by the E1A protein, which is encoded by the adenovirus. The p300 protein is a histone acetyltransferase, which means that it adds acetyl groups to histone proteins, a type of protein that helps to package DNA into chromatin. This modification of histones can affect the accessibility of the DNA to the transcription machinery, and therefore can influence gene expression. The E1A-Associated p300 Protein has been implicated in a number of cellular processes, including cell proliferation, differentiation, and transformation. It is also involved in the development of certain types of cancer.

Polycomb-group proteins (PcG) are a family of transcriptional regulators that play a crucial role in the epigenetic regulation of gene expression. They are involved in the maintenance of gene repression and are often associated with the formation of repressive chromatin structures, such as heterochromatin. In the medical field, PcG proteins have been implicated in a variety of diseases, including cancer, developmental disorders, and neurological disorders. For example, mutations in PcG genes have been linked to several types of cancer, including acute myeloid leukemia and breast cancer. In addition, PcG proteins have been shown to play a role in the development of neurological disorders such as autism and schizophrenia. Overall, PcG proteins are an important area of research in the medical field, as they have the potential to provide new insights into the mechanisms underlying a wide range of diseases and may lead to the development of new therapeutic strategies.

Molecular chaperones are a class of proteins that assist in the folding, assembly, and transport of other proteins within cells. They play a crucial role in maintaining cellular homeostasis and preventing the accumulation of misfolded or aggregated proteins, which can lead to various diseases such as neurodegenerative disorders, cancer, and certain types of infections. Molecular chaperones function by binding to nascent or partially folded proteins, preventing them from aggregating and promoting their proper folding. They also assist in the assembly of multi-subunit proteins, such as enzymes and ion channels, by ensuring that the individual subunits are correctly folded and assembled into a functional complex. There are several types of molecular chaperones, including heat shock proteins (HSPs), chaperonins, and small heat shock proteins (sHSPs). HSPs are induced in response to cellular stress, such as heat shock or oxidative stress, and are involved in the refolding of misfolded proteins. Chaperonins, on the other hand, are found in the cytosol and the endoplasmic reticulum and are involved in the folding of large, complex proteins. sHSPs are found in the cytosol and are involved in the stabilization of unfolded proteins and preventing their aggregation. Overall, molecular chaperones play a critical role in maintaining protein homeostasis within cells and are an important target for the development of new therapeutic strategies for various diseases.

Chromatin Assembly Factor-1 (CAF-1) is a protein complex that plays a crucial role in chromatin assembly and maintenance in the cell nucleus. It is responsible for the deposition of histones onto DNA, which helps to package and organize the genetic material into a compact structure called chromatin. CAF-1 is composed of three subunits: CAF-1p150, CAF-1p60, and CAF-1p105. These subunits work together to deposit new histones onto DNA, replacing the old ones that have been removed during DNA replication. This process is essential for maintaining the integrity of the genome and ensuring that the genetic information is accurately transmitted from one generation of cells to the next. Disruptions in the function of CAF-1 have been linked to various diseases, including cancer, neurodegenerative disorders, and developmental abnormalities. Therefore, understanding the role of CAF-1 in chromatin assembly and maintenance is important for developing new therapeutic strategies for these diseases.

In the medical field, "trans-activators" refer to proteins or molecules that activate the transcription of a gene, which is the process by which the information in a gene is used to produce a functional product, such as a protein. Trans-activators can bind to specific DNA sequences near a gene and recruit other proteins, such as RNA polymerase, to initiate transcription. They can also modify the chromatin structure around a gene to make it more accessible to transcription machinery. Trans-activators play important roles in regulating gene expression and are involved in many biological processes, including development, differentiation, and disease.

Ribonucleoprotein, U7 Small Nuclear (RNP) is a complex molecule that plays a crucial role in the process of splicing pre-mRNA transcripts. It is composed of a small nuclear RNA (snRNA) called U7 and a variety of proteins, including U7-28, U7-30, and U7-39. The U7 snRNA is a small RNA molecule that is approximately 70 nucleotides in length. It is transcribed from a gene located in the intron of the U7 pre-mRNA, which is itself transcribed from a gene located on chromosome 19. The U7 snRNA is then processed and packaged into a small nuclear ribonucleoprotein particle (snRNP) along with the other proteins. The U7 snRNP is involved in the splicing of a specific subset of pre-mRNA transcripts that contain a specific type of intron called a U7-type intron. These introns are typically found in the 3' untranslated region (UTR) of certain mRNAs, and they are removed during the splicing process by the U7 snRNP. The U7 snRNP recognizes a specific sequence of nucleotides within the U7-type intron, and it then recruits other splicing factors to the site of the intron. These factors help to remove the intron and join the two exons together, resulting in a mature mRNA transcript. Disruptions in the function of the U7 snRNP or its associated proteins have been implicated in a number of human diseases, including certain types of cancer and neurological disorders.

Multiprotein complexes are groups of two or more proteins that interact with each other to form a functional unit in the cell. These complexes can be involved in a wide range of cellular processes, including signal transduction, gene expression, metabolism, and protein synthesis. Multiprotein complexes can be transient, meaning they assemble and disassemble rapidly in response to changes in the cellular environment, or they can be stable and persist for longer periods of time. Some examples of well-known multiprotein complexes include the proteasome, the ribosome, and the spliceosome. In the medical field, understanding the structure and function of multiprotein complexes is important for understanding how cells work and how diseases can arise. For example, mutations in genes encoding proteins that make up multiprotein complexes can lead to the formation of dysfunctional complexes that contribute to the development of diseases such as cancer, neurodegenerative disorders, and metabolic disorders. Additionally, drugs that target specific components of multiprotein complexes are being developed as potential treatments for these diseases.

Azacitidine is a medication used to treat certain types of blood cancer, including myelodysplastic syndromes (MDS) and acute myeloid leukemia (AML). It works by slowing or stopping the growth of cancer cells in the bone marrow and bloodstream. Azacitidine is usually given by injection into a vein or under the skin, and is typically administered once a day for a period of several days, followed by a break of several days before the next cycle of treatment. It is important to note that azacitidine can cause side effects, including fatigue, nausea, and low blood cell counts, and should only be used under the supervision of a qualified healthcare professional.

RNA, Small Interfering (siRNA) is a type of non-coding RNA molecule that plays a role in gene regulation. siRNA is approximately 21-25 nucleotides in length and is derived from double-stranded RNA (dsRNA) molecules. In the medical field, siRNA is used as a tool for gene silencing, which involves inhibiting the expression of specific genes. This is achieved by introducing siRNA molecules that are complementary to the target mRNA sequence, leading to the degradation of the mRNA and subsequent inhibition of protein synthesis. siRNA has potential applications in the treatment of various diseases, including cancer, viral infections, and genetic disorders. It is also used in research to study gene function and regulation. However, the use of siRNA in medicine is still in its early stages, and there are several challenges that need to be addressed before it can be widely used in clinical practice.

mRNA Cleavage and Polyadenylation Factors are a group of proteins involved in the process of mRNA maturation in eukaryotic cells. This process involves the addition of a poly(A) tail to the 3' end of the mRNA molecule, which is necessary for its stability, export from the nucleus, and translation into protein. The cleavage and polyadenylation factors are responsible for recognizing and binding to specific sequences in the pre-mRNA molecule, and for recruiting the enzymes necessary for cleavage and polyadenylation. These factors include the cleavage and polyadenylation specificity factor (CPSF), the cleavage stimulation factor (CstF), and the poly(A) polymerase (PAP). Disruptions in the function of these factors can lead to defects in mRNA maturation, which can result in a variety of diseases, including certain types of cancer, neurological disorders, and developmental disorders.

Protein kinases are enzymes that catalyze the transfer of a phosphate group from ATP (adenosine triphosphate) to specific amino acid residues on proteins. This process, known as phosphorylation, can alter the activity, localization, or stability of the target protein, and is a key mechanism for regulating many cellular processes, including cell growth, differentiation, metabolism, and signaling pathways. Protein kinases are classified into different families based on their sequence, structure, and substrate specificity. Some of the major families of protein kinases include serine/threonine kinases, tyrosine kinases, and dual-specificity kinases. Each family has its own unique functions and roles in cellular signaling. In the medical field, protein kinases are important targets for the development of drugs for the treatment of various diseases, including cancer, diabetes, and cardiovascular disease. Many cancer drugs target specific protein kinases that are overactive in cancer cells, while drugs for diabetes and cardiovascular disease often target kinases involved in glucose metabolism and blood vessel function, respectively.

Retinoblastoma-Binding Protein 7 (RBBP7) is a protein that plays a role in the regulation of gene expression. It is a component of the Retinoblastoma protein (pRb) pathway, which is involved in cell cycle regulation and the prevention of uncontrolled cell growth. RBBP7 is thought to function as a co-repressor of transcription factors, helping to regulate the expression of genes involved in cell cycle progression and differentiation. It has been implicated in a number of cellular processes, including cell proliferation, apoptosis, and differentiation. In the medical field, RBBP7 has been studied in the context of cancer, particularly in retinoblastoma, a type of eye cancer that occurs in children. Research has suggested that alterations in RBBP7 expression may contribute to the development and progression of retinoblastoma.

The Mi-2 Nucleosome Remodeling and Deacetylase Complex (Mi-2/NuRD) is a multi-protein complex that plays a crucial role in regulating gene expression and maintaining chromatin structure in the nucleus of cells. It is composed of several subunits, including the ATPase subunit Mi-2, the histone deacetylase (HDAC) subunit RbAp46, and several other regulatory and accessory subunits. The Mi-2/NuRD complex is involved in a variety of cellular processes, including DNA repair, transcriptional regulation, and cell cycle control. It is also implicated in the development and progression of several diseases, including cancer, autoimmune disorders, and neurological disorders. In the context of gene expression, the Mi-2/NuRD complex can either activate or repress gene transcription by altering the chromatin structure around specific genes. It can do this by using its ATPase activity to remodel nucleosomes, which are the basic units of chromatin, and by using its HDAC activity to remove acetyl groups from histone proteins, which can make chromatin more condensed and less accessible to transcription factors. Overall, the Mi-2/NuRD complex is a key regulator of gene expression and chromatin structure, and its dysfunction can have significant consequences for cellular function and disease.

Anacardic acids are a group of organic compounds that are found in the shell of cashew nuts (Anacardium occidentale). They are also found in the shells of other nuts, such as mango and pistachio, as well as in the leaves and bark of certain trees, such as the mango and cashew trees. Anacardic acids are known for their anti-inflammatory and antioxidant properties, and they have been studied for their potential therapeutic effects in a variety of conditions, including skin disorders, respiratory infections, and cancer. Some anacardic acids have also been shown to have antimicrobial and antifungal properties. In the medical field, anacardic acids are sometimes used as ingredients in topical creams and ointments to help treat skin conditions such as eczema and psoriasis. They may also be used in the development of new drugs for the treatment of other conditions. However, more research is needed to fully understand the potential therapeutic effects of anacardic acids and to determine the safest and most effective ways to use them.

In the medical field, macromolecular substances refer to large molecules that are composed of repeating units, such as proteins, carbohydrates, lipids, and nucleic acids. These molecules are essential for many biological processes, including cell signaling, metabolism, and structural support. Macromolecular substances are typically composed of thousands or even millions of atoms, and they can range in size from a few nanometers to several micrometers. They are often found in the form of fibers, sheets, or other complex structures, and they can be found in a variety of biological tissues and fluids. Examples of macromolecular substances in the medical field include: - Proteins: These are large molecules composed of amino acids that are involved in a wide range of biological functions, including enzyme catalysis, structural support, and immune response. - Carbohydrates: These are molecules composed of carbon, hydrogen, and oxygen atoms that are involved in energy storage, cell signaling, and structural support. - Lipids: These are molecules composed of fatty acids and glycerol that are involved in energy storage, cell membrane structure, and signaling. - Nucleic acids: These are molecules composed of nucleotides that are involved in genetic information storage and transfer. Macromolecular substances are important for many medical applications, including drug delivery, tissue engineering, and gene therapy. Understanding the structure and function of these molecules is essential for developing new treatments and therapies for a wide range of diseases and conditions.

DNA primers are short, single-stranded DNA molecules that are used in a variety of molecular biology techniques, including polymerase chain reaction (PCR) and DNA sequencing. They are designed to bind to specific regions of a DNA molecule, and are used to initiate the synthesis of new DNA strands. In PCR, DNA primers are used to amplify specific regions of DNA by providing a starting point for the polymerase enzyme to begin synthesizing new DNA strands. The primers are complementary to the target DNA sequence, and are added to the reaction mixture along with the DNA template, nucleotides, and polymerase enzyme. The polymerase enzyme uses the primers as a template to synthesize new DNA strands, which are then extended by the addition of more nucleotides. This process is repeated multiple times, resulting in the amplification of the target DNA sequence. DNA primers are also used in DNA sequencing to identify the order of nucleotides in a DNA molecule. In this application, the primers are designed to bind to specific regions of the DNA molecule, and are used to initiate the synthesis of short DNA fragments. The fragments are then sequenced using a variety of techniques, such as Sanger sequencing or next-generation sequencing. Overall, DNA primers are an important tool in molecular biology, and are used in a wide range of applications to study and manipulate DNA.

Retinoblastoma-Binding Protein 2 (RBBP2) is a protein that plays a role in the regulation of gene expression. It is encoded by the RBBP2 gene and is found in the nucleus of cells. RBBP2 is a component of the Retinoblastoma protein (pRb) pathway, which is involved in the regulation of cell cycle progression and the prevention of uncontrolled cell growth. Mutations in the RBBP2 gene have been associated with an increased risk of developing certain types of cancer, including retinoblastoma, a type of eye cancer that primarily affects children.

Protein-Serine-Threonine Kinases (PSTKs) are a family of enzymes that play a crucial role in regulating various cellular processes, including cell growth, differentiation, metabolism, and apoptosis. These enzymes phosphorylate specific amino acids, such as serine and threonine, on target proteins, thereby altering their activity, stability, or localization within the cell. PSTKs are involved in a wide range of diseases, including cancer, diabetes, cardiovascular disease, and neurodegenerative disorders. Therefore, understanding the function and regulation of PSTKs is important for developing new therapeutic strategies for these diseases.

Sirtuin 1, also known as SIRT1, is a protein that belongs to the sirtuin family of enzymes. It is a NAD+-dependent deacetylase that plays a crucial role in regulating various cellular processes, including DNA repair, metabolism, inflammation, and aging. In the medical field, SIRT1 has been studied for its potential therapeutic applications in various diseases, including cancer, diabetes, cardiovascular disease, and neurodegenerative disorders. Research has shown that SIRT1 activation can improve insulin sensitivity, reduce inflammation, and protect against oxidative stress, which are all important factors in the development of these diseases. SIRT1 has also been shown to have anti-aging effects, as it can promote cellular longevity and delay the onset of age-related diseases. However, more research is needed to fully understand the role of SIRT1 in aging and to develop effective therapies that target this protein. Overall, SIRT1 is a promising target for the development of new treatments for a wide range of diseases, and ongoing research is exploring its potential therapeutic applications in various fields of medicine.

Polyadenosine diphosphate ribose (PAR) is a complex molecule that is involved in various cellular processes, including energy metabolism, gene expression, and cell signaling. It is composed of multiple units of adenosine diphosphate (ADP) linked together by ribose sugars, with the number of ADP units ranging from two to several hundred. In the medical field, PAR is known to play a role in a number of diseases and conditions, including cancer, neurodegenerative disorders, and cardiovascular disease. For example, PAR has been shown to regulate the activity of certain enzymes involved in energy metabolism, and changes in PAR levels have been associated with altered metabolism in cancer cells. PAR has also been implicated in the regulation of gene expression and the development of neurodegenerative diseases such as Alzheimer's and Parkinson's disease. Additionally, PAR has been shown to play a role in the regulation of blood vessel function and the development of cardiovascular disease.

Silent Information Regulator Proteins (Sir Proteins) in Saccharomyces cerevisiae are a family of proteins that play a crucial role in regulating gene expression in yeast cells. These proteins are involved in the maintenance of chromatin structure and the regulation of transcriptional silencing at specific genomic loci. In yeast cells, Sir Proteins form a complex that binds to specific DNA sequences and recruits other proteins to silence the transcription of nearby genes. This process is important for the proper functioning of the yeast genome, as it helps to prevent the expression of genes that are not needed under certain conditions. Mutations in Sir Proteins can lead to a variety of phenotypes in yeast cells, including changes in gene expression, increased sensitivity to DNA damage, and defects in chromosome segregation. Sir Proteins have also been studied in the context of human diseases, as they are homologous to proteins that play a role in regulating gene expression in human cells.

Homeodomain proteins are a class of transcription factors that play a crucial role in the development and differentiation of cells and tissues in animals. They are characterized by a highly conserved DNA-binding domain called the homeodomain, which allows them to recognize and bind to specific DNA sequences. Homeodomain proteins are involved in a wide range of biological processes, including embryonic development, tissue differentiation, and organogenesis. They regulate the expression of genes that are essential for these processes by binding to specific DNA sequences and either activating or repressing the transcription of target genes. There are many different types of homeodomain proteins, each with its own unique function and target genes. Some examples of homeodomain proteins include the Hox genes, which are involved in the development of the body plan in animals, and the Pax genes, which are involved in the development of the nervous system. Mutations in homeodomain proteins can lead to a variety of developmental disorders, including congenital malformations and intellectual disabilities. Understanding the function and regulation of homeodomain proteins is therefore important for the development of new treatments for these conditions.

Schizosaccharomyces pombe is a type of yeast that is commonly used in research to study basic cellular processes and genetics. Proteins produced by this yeast can be important tools in the medical field, as they can be used to study the function of specific genes and to develop new treatments for diseases. One example of a Schizosaccharomyces pombe protein that is of interest in the medical field is the protein called CDC48. This protein is involved in a variety of cellular processes, including the assembly and disassembly of cellular structures, and it has been implicated in the development of several diseases, including cancer. Researchers are studying CDC48 in order to better understand its role in these diseases and to develop new treatments based on this knowledge. Other Schizosaccharomyces pombe proteins that are of interest in the medical field include those involved in DNA repair, cell division, and signal transduction. These proteins can be used as tools to study the function of specific genes and to develop new treatments for diseases that are caused by defects in these genes.

Myeloid-Lymphoid Leukemia Protein (MLL) is a type of protein that plays a crucial role in the development and function of blood cells. It is also known as Mixed Lineage Leukemia (MLL) protein. MLL is a member of a family of proteins called histone methyltransferases, which are enzymes that add methyl groups to the tails of histone proteins. Histones are proteins that help package DNA into a compact structure called chromatin. By adding methyl groups to histones, MLL can affect the accessibility of DNA to the machinery that reads and writes genetic information, which in turn can influence gene expression. In the context of leukemia, mutations in the MLL gene can lead to the production of abnormal versions of the MLL protein that are not properly regulated. This can result in the uncontrolled growth and proliferation of blood cells, leading to the development of leukemia. MLL is a type of acute leukemia that affects both myeloid and lymphoid cells, hence the name "myeloid-lymphoid leukemia." It is a rare type of leukemia, accounting for only about 1-2% of all cases of acute leukemia. Treatment for MLL leukemia typically involves chemotherapy, stem cell transplantation, and targeted therapies that specifically target the abnormal MLL protein.

Phenylbutyrates are a class of drugs that are used to treat certain metabolic disorders. They are synthetic derivatives of the amino acid leucine and are classified as branched-chain amino acid (BCAA) analogs. Phenylbutyrates are primarily used to treat urea cycle disorders, such as ornithine transcarbamylase deficiency (OTCD) and argininosuccinic aciduria (ASA), which are genetic disorders that affect the body's ability to break down certain amino acids. In these disorders, the accumulation of toxic levels of ammonia in the blood can lead to serious health problems, including brain damage and death. Phenylbutyrates help to reduce the levels of ammonia in the blood by providing an alternative pathway for the breakdown of certain amino acids. Phenylbutyrates are also being studied for their potential use in treating other conditions, such as autism spectrum disorder, Alzheimer's disease, and Huntington's disease. However, more research is needed to determine their effectiveness and safety in these conditions.

Serine is an amino acid that is a building block of proteins. It is a non-essential amino acid, meaning that it can be synthesized by the body from other compounds. In the medical field, serine is known to play a role in various physiological processes, including the production of neurotransmitters, the regulation of blood sugar levels, and the maintenance of healthy skin and hair. It is also used as a dietary supplement to support these functions and to promote overall health. In some cases, serine may be prescribed by a healthcare provider to treat certain medical conditions, such as liver disease or depression.

Nuclear receptor co-repressor 1 (NCoR1) is a protein that plays a role in regulating gene expression in the cell nucleus. It is a member of the nuclear receptor co-repressor family of proteins, which are involved in the regulation of various cellular processes, including metabolism, cell growth, and differentiation. NCoR1 is a transcriptional corepressor that binds to specific nuclear receptors, such as the thyroid hormone receptor and the retinoid X receptor, and inhibits their ability to activate gene transcription. It does this by recruiting other corepressor proteins, such as histone deacetylases, to the promoter region of target genes, leading to the repression of gene expression. NCoR1 has been implicated in a number of diseases, including cancer, metabolic disorders, and neurological disorders. For example, mutations in the NCoR1 gene have been associated with an increased risk of breast cancer, and NCoR1 has been shown to play a role in the development of type 2 diabetes and obesity. Additionally, NCoR1 has been implicated in the pathogenesis of neurological disorders such as Alzheimer's disease and Parkinson's disease.

Polycomb Repressive Complex 1 (PRC1) is a protein complex that plays a crucial role in the regulation of gene expression in the epigenetic modification of chromatin. It is involved in the repression of gene expression by modifying histones, which are proteins that help package DNA into a compact structure within the nucleus of a cell. PRC1 is composed of several subunits, including the core components Ring1B and BMI1, as well as other associated proteins. The complex recognizes and binds to specific DNA sequences, and then modifies histones by adding a chemical modification called ubiquitination. This modification leads to the recruitment of other proteins that further repress gene expression. In the medical field, PRC1 has been implicated in a number of diseases, including cancer. Abnormal activity of PRC1 has been observed in various types of cancer, and it has been suggested that targeting PRC1 may be a potential therapeutic strategy for treating these diseases. Additionally, PRC1 has been studied in the context of stem cell biology, as it plays a role in maintaining the undifferentiated state of stem cells.

Group III Histone Deacetylases (HDACs) are a family of enzymes that remove acetyl groups from the lysine residues of histone proteins. Histones are proteins that help package and organize DNA into chromatin, which is the complex structure that makes up chromosomes. The acetylation of histones is an important regulatory mechanism that affects gene expression by altering the accessibility of DNA to transcription factors and other regulatory proteins. Group III HDACs are a subclass of HDACs that are primarily found in the nucleus of cells and are involved in the regulation of gene expression. They are also known as class III HDACs or sirtuins, and are named after the silent information regulator 2 (SIRT2) protein, which is the first member of this family to be discovered. Group III HDACs play a role in a variety of cellular processes, including aging, metabolism, and stress response. They have been implicated in the development of several diseases, including cancer, neurodegenerative disorders, and diabetes. Inhibitors of Group III HDACs are being investigated as potential therapeutic agents for these diseases.

Biotinidase is an enzyme that is responsible for the cleavage of biotin from biotinylated compounds. Biotin is a water-soluble B-vitamin that is essential for the metabolism of fatty acids, amino acids, and glucose. Biotinidase is primarily found in the liver, kidneys, and small intestine, and it plays a crucial role in the absorption and utilization of biotin. In the medical field, biotinidase deficiency is a rare genetic disorder that results from a deficiency of the biotinidase enzyme. This deficiency can lead to a buildup of biotinylated compounds in the body, which can cause a range of symptoms, including hair loss, skin rash, and neurological problems. Treatment for biotinidase deficiency typically involves oral supplementation with biotin, which can help to normalize the levels of biotinylated compounds in the body and alleviate symptoms.

Nucleoside diphosphate sugars are a type of sugar molecule that serves as the backbone of nucleic acids, such as DNA and RNA. They are composed of a pentose sugar (ribose or deoxyribose) linked to a nitrogenous base and a phosphate group. The nitrogenous base can be either a purine (adenine or guanine) or a pyrimidine (cytosine, thymine, or uracil). In the medical field, nucleoside diphosphate sugars are important components of nucleic acid metabolism and are involved in various cellular processes, including DNA replication, RNA transcription, and protein synthesis. They are also used as precursors for the synthesis of nucleotides, which are the building blocks of nucleic acids. In addition, nucleoside diphosphate sugars are used in the development of antiviral drugs, as many viruses rely on the host cell's nucleic acid metabolism to replicate. By inhibiting the synthesis of nucleoside diphosphate sugars, these drugs can prevent the replication of the virus and treat viral infections.

Cyclin-dependent kinase inhibitor p21 (p21) is a protein that plays a role in regulating the cell cycle, which is the process by which cells divide and grow. It is encoded by the CDKN1A gene and is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. In the cell cycle, the progression from one phase to the next is controlled by a series of checkpoints that ensure that the cell is ready to proceed. One of the key regulators of these checkpoints is the cyclin-dependent kinase (CDK) family of enzymes. CDKs are activated by binding to cyclins, which are proteins that are synthesized and degraded in a cyclic manner throughout the cell cycle. p21 acts as a CDK inhibitor by binding to and inhibiting the activity of cyclin-CDK complexes. This prevents the complexes from phosphorylating target proteins that are required for the progression of the cell cycle. As a result, p21 helps to prevent the cell from dividing when it is not ready, and it plays a role in preventing the development of cancer. In addition to its role in regulating the cell cycle, p21 has been implicated in a number of other cellular processes, including DNA repair, senescence, and apoptosis (programmed cell death). It is also involved in the response of cells to various stressors, such as DNA damage, oxidative stress, and hypoxia.

In the medical field, neoplasms refer to abnormal growths or tumors of cells that can occur in any part of the body. These growths can be either benign (non-cancerous) or malignant (cancerous). Benign neoplasms are usually slow-growing and do not spread to other parts of the body. They can cause symptoms such as pain, swelling, or difficulty moving the affected area. Examples of benign neoplasms include lipomas (fatty tumors), hemangiomas (vascular tumors), and fibromas (fibrous tumors). Malignant neoplasms, on the other hand, are cancerous and can spread to other parts of the body through the bloodstream or lymphatic system. They can cause a wide range of symptoms, depending on the location and stage of the cancer. Examples of malignant neoplasms include carcinomas (cancers that start in epithelial cells), sarcomas (cancers that start in connective tissue), and leukemias (cancers that start in blood cells). The diagnosis of neoplasms typically involves a combination of physical examination, imaging tests (such as X-rays, CT scans, or MRI scans), and biopsy (the removal of a small sample of tissue for examination under a microscope). Treatment options for neoplasms depend on the type, stage, and location of the cancer, as well as the patient's overall health and preferences.

Transcriptional elongation factors are proteins that play a crucial role in the process of transcription, which is the first step in gene expression. During transcription, the DNA sequence of a gene is copied into a complementary RNA sequence, known as messenger RNA (mRNA). Transcriptional elongation factors help to facilitate the movement of the RNA polymerase enzyme along the DNA template, allowing it to synthesize the RNA molecule. There are several different types of transcriptional elongation factors, each with its own specific function. Some of the most well-known include the elongation factor A (EF-A), which helps to unwind the DNA double helix ahead of the RNA polymerase, and the elongation factor B (EF-B), which helps to stabilize the RNA polymerase on the DNA template. Disruptions in the function of transcriptional elongation factors can lead to a variety of genetic disorders, including some forms of cancer. For example, mutations in the gene that encodes for the elongation factor A protein have been linked to certain types of leukemia and lymphoma.

RNA, Ribosomal, 5S is a type of ribosomal RNA (rRNA) that is found in the ribosomes of cells. Ribosomes are the cellular structures responsible for protein synthesis, and rRNA is a key component of the ribosome. The 5S rRNA is one of the smaller subunits of the ribosome and is involved in the initiation of protein synthesis. It is encoded by a specific gene and is transcribed from DNA into RNA. In the medical field, the 5S rRNA is often studied as a target for the development of new drugs to treat various diseases, including cancer.

In the medical field, carrier proteins are proteins that transport molecules across cell membranes or within cells. These proteins bind to specific molecules, such as hormones, nutrients, or waste products, and facilitate their movement across the membrane or within the cell. Carrier proteins play a crucial role in maintaining the proper balance of molecules within cells and between cells. They are involved in a wide range of physiological processes, including nutrient absorption, hormone regulation, and waste elimination. There are several types of carrier proteins, including facilitated diffusion carriers, active transport carriers, and ion channels. Each type of carrier protein has a specific function and mechanism of action. Understanding the role of carrier proteins in the body is important for diagnosing and treating various medical conditions, such as genetic disorders, metabolic disorders, and neurological disorders.

In the medical field, peptides are short chains of amino acids that are linked together by peptide bonds. They are typically composed of 2-50 amino acids and can be found in a variety of biological molecules, including hormones, neurotransmitters, and enzymes. Peptides play important roles in many physiological processes, including growth and development, immune function, and metabolism. They can also be used as therapeutic agents to treat a variety of medical conditions, such as diabetes, cancer, and cardiovascular disease. In the pharmaceutical industry, peptides are often synthesized using chemical methods and are used as drugs or as components of drugs. They can be administered orally, intravenously, or topically, depending on the specific peptide and the condition being treated.

Arabidopsis Proteins refer to proteins that are encoded by genes in the genome of the plant species Arabidopsis thaliana. Arabidopsis is a small flowering plant that is widely used as a model organism in plant biology research due to its small size, short life cycle, and ease of genetic manipulation. Arabidopsis proteins have been extensively studied in the medical field due to their potential applications in drug discovery, disease diagnosis, and treatment. For example, some Arabidopsis proteins have been found to have anti-inflammatory, anti-cancer, and anti-viral properties, making them potential candidates for the development of new drugs. In addition, Arabidopsis proteins have been used as tools for studying human diseases. For instance, researchers have used Arabidopsis to study the molecular mechanisms underlying human diseases such as Alzheimer's, Parkinson's, and Huntington's disease. Overall, Arabidopsis proteins have become an important resource for medical research due to their potential applications in drug discovery and disease research.

Ribosomal Protein S6 Kinases, 90-kDa (RPS6KB1) is a protein that plays a role in the regulation of cell growth and proliferation. It is a member of the ribosomal protein S6 kinase family, which is involved in the translation of messenger RNA into proteins. RPS6KB1 is activated by the mammalian target of rapamycin (mTOR) signaling pathway, which is a key regulator of cell growth and metabolism. Activation of RPS6KB1 leads to the phosphorylation of the ribosomal protein S6, which is involved in the regulation of protein synthesis. Dysregulation of RPS6KB1 has been implicated in a number of diseases, including cancer, diabetes, and neurodegenerative disorders.

Hydroxyurea is a medication that is used to treat certain types of blood disorders, including sickle cell anemia and myelofibrosis. It works by slowing down the production of new blood cells in the bone marrow, which can help to reduce the number of abnormal red blood cells in the body and prevent them from getting stuck in small blood vessels. Hydroxyurea is usually taken by mouth in the form of tablets or capsules, and the dosage and frequency of administration will depend on the specific condition being treated and the individual patient's response to the medication. It is important to follow the instructions provided by your healthcare provider and to report any side effects or concerns to them right away.

DNA, Fungal refers to the genetic material of fungi, which is a type of eukaryotic microorganism that includes yeasts, molds, and mushrooms. Fungal DNA is composed of four types of nucleotides: adenine (A), thymine (T), cytosine (C), and guanine (G), which are arranged in a specific sequence to form the genetic code that determines the characteristics and functions of the fungus. In the medical field, fungal DNA is often studied in the context of infections caused by fungi, such as candidiasis, aspergillosis, and cryptococcosis. Fungal DNA can be detected in clinical samples, such as blood, sputum, or tissue, using molecular diagnostic techniques such as polymerase chain reaction (PCR) or DNA sequencing. These tests can help diagnose fungal infections and guide treatment decisions. Additionally, fungal DNA can be used in research to study the evolution and diversity of fungi, as well as their interactions with other organisms and the environment.

Arginine is an amino acid that plays a crucial role in various physiological processes in the human body. It is an essential amino acid, meaning that it cannot be synthesized by the body and must be obtained through the diet. In the medical field, arginine is used to treat a variety of conditions, including: 1. Erectile dysfunction: Arginine is a precursor to nitric oxide, which helps to relax blood vessels and improve blood flow to the penis, leading to improved sexual function. 2. Cardiovascular disease: Arginine has been shown to improve blood flow and reduce the risk of cardiovascular disease by lowering blood pressure and improving the function of the endothelium, the inner lining of blood vessels. 3. Wound healing: Arginine is involved in the production of collagen, a protein that is essential for wound healing. 4. Immune function: Arginine is involved in the production of antibodies and other immune system components, making it important for maintaining a healthy immune system. 5. Cancer: Arginine has been shown to have anti-cancer properties and may help to slow the growth of tumors. However, it is important to note that the use of arginine as a supplement is not without risks, and it is important to consult with a healthcare provider before taking any supplements.

Tumor suppressor proteins are a group of proteins that play a crucial role in regulating cell growth and preventing the development of cancer. These proteins act as brakes on the cell cycle, preventing cells from dividing and multiplying uncontrollably. They also help to repair damaged DNA and prevent the formation of tumors. Tumor suppressor proteins are encoded by genes that are located on specific chromosomes. When these genes are functioning properly, they produce proteins that help to regulate cell growth and prevent the development of cancer. However, when these genes are mutated or damaged, the proteins they produce may not function properly, leading to uncontrolled cell growth and the development of cancer. There are many different tumor suppressor proteins, each with its own specific function. Some of the most well-known tumor suppressor proteins include p53, BRCA1, and BRCA2. These proteins are involved in regulating cell cycle checkpoints, repairing damaged DNA, and preventing the formation of tumors. In summary, tumor suppressor proteins are a group of proteins that play a critical role in regulating cell growth and preventing the development of cancer. When these proteins are functioning properly, they help to maintain the normal balance of cell growth and division, but when they are mutated or damaged, they can contribute to the development of cancer.

Isobutyrates are a group of organic compounds that contain a carboxyl group (-COOH) and an isobutyl group (-C4H9). They are derivatives of butyric acid, which is a short-chain fatty acid found in the gut and produced by the breakdown of dietary fats. In the medical field, isobutyrates are used as intermediates in the production of various pharmaceuticals and chemicals. They are also used as solvents, plasticizers, and flavoring agents in the food and beverage industry. One specific isobutyrate that has gained attention in recent years is isobutyl acetate, which is a common solvent used in the production of pharmaceuticals and cosmetics. It has been shown to have potential anti-inflammatory and analgesic effects, and is being studied for its potential use in the treatment of various conditions such as arthritis and pain.

Benzamides are a class of organic compounds that contain a benzene ring with an amide functional group (-CONH2) attached to it. They are commonly used in the medical field as analgesics, anti-inflammatory agents, and muscle relaxants. One example of a benzamide used in medicine is acetaminophen (paracetamol), which is a nonsteroidal anti-inflammatory drug (NSAID) used to relieve pain and reduce fever. Another example is benzylamine, which is used as a local anesthetic in dentistry. Benzamides can also be used as anticonvulsants, such as carbamazepine, which is used to treat epilepsy and trigeminal neuralgia. Additionally, some benzamides have been used as antidepressants, such as amitriptyline, which is a tricyclic antidepressant used to treat depression and anxiety disorders. Overall, benzamides have a wide range of medical applications and are an important class of compounds in the field of medicine.

Acetyl Coenzyme A (Acetyl-CoA) is a molecule that plays a central role in metabolism in all living organisms. It is a key intermediate in the breakdown of carbohydrates, fats, and proteins, and is involved in the synthesis of fatty acids, cholesterol, and ketone bodies. In the medical field, Acetyl-CoA is often studied in the context of diseases such as diabetes, obesity, and metabolic disorders. For example, in type 2 diabetes, the body's ability to regulate blood sugar levels is impaired, which can lead to an accumulation of Acetyl-CoA in the liver. This can cause the liver to produce more fatty acids and triglycerides, leading to the development of fatty liver disease. In addition, Acetyl-CoA is also involved in the production of energy in the form of ATP (adenosine triphosphate), which is the primary energy currency of the cell. Therefore, disruptions in Acetyl-CoA metabolism can have significant effects on energy production and overall health.

Ubiquitin-conjugating enzymes, also known as E2 enzymes, are a family of enzymes that play a crucial role in the ubiquitin-proteasome system (UPS) in the medical field. The UPS is a major pathway for the degradation of proteins in cells, and it is involved in a wide range of cellular processes, including cell cycle regulation, signal transduction, and protein quality control. E2 enzymes are responsible for transferring ubiquitin, a small protein that is covalently attached to target proteins, from an E1 enzyme to a target protein. This process is essential for the formation of polyubiquitin chains, which serve as a signal for the degradation of the target protein by the proteasome. In the medical field, the UPS is involved in the regulation of many diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. Dysregulation of the UPS has been implicated in the development and progression of these diseases, and targeting the UPS has become an important strategy for the development of new therapies. E2 enzymes are therefore of great interest in the medical field, as they play a central role in the UPS and are involved in the regulation of many important cellular processes. Understanding the function and regulation of E2 enzymes is essential for developing new therapies for diseases that are associated with dysregulation of the UPS.

Ubiquitin is a small, highly conserved protein that is found in all eukaryotic cells. It plays a crucial role in the regulation of various cellular processes, including protein degradation, cell cycle progression, and signal transduction. In the medical field, ubiquitin is often studied in the context of various diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. For example, mutations in genes encoding ubiquitin or its regulatory enzymes have been linked to several forms of cancer, including breast, ovarian, and prostate cancer. Additionally, the accumulation of ubiquitinated proteins has been observed in several neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Overall, understanding the role of ubiquitin in cellular processes and its involvement in various diseases is an active area of research in the medical field.

"Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24". Proceedings of the ... Later work on modification of histones led to the identification of an unexpected covalent modification of the histone protein ... These proteins are ubiquitinated by SCFTIR1, or SCF in complex with the auxin receptor TIR1. Degradation of Aux/IAA proteins ... Proteins are tagged for degradation with a small protein called ubiquitin. The tagging reaction is catalyzed by enzymes called ...

https://en.wikipedia.org/wiki/Proteasome

Shirakawa H, Tsuda K, Yoshida M (May 1990). "Primary structure of non-histone chromosomal protein HMG2 revealed by the ... High-mobility group protein B3 is a protein that in humans is encoded by the HMGB3 gene. GRCh38: Ensembl release 89: ... HMGB3+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH) PDBe-KB provides an overview of ... all the structure information available in the PDB for Human High mobility group protein B3 (HMGB3) v t e (Articles with short ...

https://en.wikipedia.org/wiki/HMGB3

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... Histone H1.3 is a protein that in humans is encoded by the HIST1H1D gene. ... "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940-8. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H1D

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... 1988). "Two target sites for protein binding in the promoter region of a cell cycle regulated human H1 histone gene". Nucleic ... Histone H1.5 is a protein that in humans is encoded by the HIST1H1B gene. ... Chadwick BP, Willard HF (2001). "A Novel Chromatin Protein, Distantly Related to Histone H2a, Is Largely Excluded from the ...

https://en.wikipedia.org/wiki/HIST1H1B

Nagaki S, Yamamoto M, Yumoto Y, Shirakawa H, Yoshida M, Teraoka H (May 1998). "Non-histone chromosomal proteins HMG1 and 2 ... High mobility group box 1 protein, also known as high-mobility group protein 1 (HMG-1) and amphoterin, is a protein that in ... Like the histones, HMGB1 is among the most important chromatin proteins. In the nucleus HMGB1 interacts with nucleosomes, ... transcription factors, and histones. This nuclear protein organizes the DNA and regulates transcription. After binding, HMGB1 ...

https://en.wikipedia.org/wiki/HMGB1

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... Histone H1t is a protein that in humans is encoded by the HIST1H1T gene. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ... "Entrez Gene: HIST1H1T histone cluster 1, H1t". Drabent B, Kardalinou E, Doenecke D (1991). "Structure and expression of the ...

https://en.wikipedia.org/wiki/HIST1H1T

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... 2000). "Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein". J. Biol. Chem. ... "Entrez Gene: HIST1H1A histone cluster 1, H1a". Du Clos TW, Zlock LT, Marnell L (1991). "Definition of a C-reactive protein ... 1995). "Expression and chromosomal mapping of the gene encoding the human histone H1.1". Hum. Genet. 94 (6): 633-9. doi:10.1007 ...

https://en.wikipedia.org/wiki/HIST1H1A

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... 2000). "Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein". J. Biol. Chem. ... Histone H1.2 is a protein that in humans is encoded by the HIST1H1C gene. ... "Entrez Gene: HIST1H1C histone cluster 1, H1c". Ohe Y, Hayashi H, Iwai K (1990). "Human spleen histone H1. Isolation and amino ...

https://en.wikipedia.org/wiki/HIST1H1C

Histones are basic nuclear proteins responsible for nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules ... Histone H1.4 is a protein that in humans is encoded by the HIST1H1E gene. ... "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): 940-8. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H1E

This gene encodes a member of the non-histone chromosomal high-mobility group protein family. The proteins of this family are ... Nagaki S, Yamamoto M, Yumoto Y, Shirakawa H, Yoshida M, Teraoka H (May 1998). "Non-histone chromosomal proteins HMG1 and 2 ... High-mobility group protein B2 also known as high-mobility group protein 2 (HMG-2) is a protein that in humans is encoded by ... "High mobility group proteins 1 and 2 can function as DNA-binding regulatory components for DNA-dependent protein kinase in ...

https://en.wikipedia.org/wiki/HMGB2

"Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases". Cell. 125 (3): 467-81. doi:10.1016/j. ... This gene is a member of the Jumonji domain 2 (JMJD2) family and encodes a protein with one JmjC domain, one JmjN domain, two ... Chromosomal aberrations and increased transcriptional expression of this gene are associated with esophageal squamous cell ... This nuclear protein belongs to the alpha-ketoglutarate-dependent hydroxylase superfamily. It functions as a trimethylation- ...

https://en.wikipedia.org/wiki/KDM4C

... binds to the WDR5 protein, which forms a complex with the histone methyltransferase protein MLL. This targets the WDR5- ... The non-coding RNA is brought into close proximity with the HOXA genes by chromosomal looping. ...

https://en.wikipedia.org/wiki/HOTTIP

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Popescu N, Zimonjic D, Hatch C, Bonner W (1994). "Chromosomal mapping of the human histone gene H2AZ to 4q24 by fluorescence in ... Histone H2A.Z is a protein that in humans is encoded by the H2AZ1 gene. ... Histone H2AZ is a variant of histone H2A, and is used to mediate the thermosensory response, and is essential to perceive the ...

https://en.wikipedia.org/wiki/Histone_H2A.Z

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2A type 1-D is a protein that in humans is encoded by the HIST1H2AD gene. ... "Entrez Gene: HIST1H2AD histone cluster 1, H2ad". Albig W, Doenecke D (1998). "The human histone gene cluster at the D6S105 ... This gene is intronless and encodes a member of the histone H2A family. Transcripts from this gene lack polyA tails; instead, ...

https://en.wikipedia.org/wiki/HIST1H2AD

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2B type 1-A is a protein that in humans is encoded by the HIST1H2BA gene. ... "Entrez Gene: HIST1H2BA histone cluster 1, H2ba". El Kharroubi A, Piras G, Zensen R, Martin MA (1998). "Transcriptional ... Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core ...

https://en.wikipedia.org/wiki/HIST1H2BA

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H4 is a protein that in humans is encoded by the HIST2H4A gene. ... "Entrez Gene: HIST2H4A histone cluster 2, H4a". Green L, Van Antwerpen R, Stein J, et al. (1984). "A major human histone gene ... 1997). "Functional characterization of human nucleosome assembly protein-2 (NAP1L4) suggests a role as a histone chaperone". ...

https://en.wikipedia.org/wiki/HIST2H4A

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... "Entrez Gene: HIST1H4D histone cluster 1, H4d". Pauli U, Chrysogelos S, Stein G, et al. (1987). "Protein-DNA interactions in ... Histone H4 is a protein that in humans is encoded by the HIST1H4D gene. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H4D

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2A type 1 is a protein that in humans is encoded by the HIST1H2AK gene. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ... Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of ...

https://en.wikipedia.org/wiki/HIST1H2AK

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... 1987). "Protein-DNA interactions in vivo upstream of a cell cycle-regulated human H4 histone gene". Science. 236 (4806): 1308- ... Histone H4 is a protein that, in humans, is encoded by the HIST1H4I gene. ... 1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): ...

https://en.wikipedia.org/wiki/HIST1H4I

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H4 is a protein that in humans is encoded by the HIST1H4B gene. ... 1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H4B

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone cluster 1, H4j is a protein that in humans is encoded by the HIST1H4J gene. ... "Entrez Gene: Histone cluster 1, H4j". Retrieved 2012-03-12. Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H4J

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2B type 1-N is a protein that in humans is encoded by the HIST1H2BN gene. ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-8. Bibcode: ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H2BN

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... 2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116-20. Bibcode: ... Histone H3.1 is a protein in humans that is encoded by the H3C1 gene. ... 2004). "Np95 is a histone-binding protein endowed with ubiquitin ligase activity". Mol. Cell. Biol. 24 (6): 2526-35. doi: ...

https://en.wikipedia.org/wiki/Histone_H3.1

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2A type 1-C is a protein that in humans is encoded by the HIST1H2AC gene. ... "Entrez Gene: HIST1H2AC histone cluster 1, H2ac". Rotondo JC, Bosi S, Bassi C, Ferracin M, Lanza G, Gafà R, Magri E, Selvatici R ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H2AC

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H3.1 is a protein that in humans is encoded by the HIST1H3H gene. ... 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173-1178. Bibcode: ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ...

https://en.wikipedia.org/wiki/HIST1H3H

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... The protein is divergent at the C-terminus compared to the consensus H2A histone family member. GRCh38: Ensembl release 89: ... Histone H2A.J is a protein that in humans is encoded by the H2AFJ gene. ... Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core ...

https://en.wikipedia.org/wiki/H2AFJ

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... 2001). "Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins". Nature. 410 (6824): 116-20. Bibcode: ... Histone H3.1 is a protein that in humans is encoded by the HIST1H3F gene. ... 1991). "Isolation and characterization of two human H1 histone genes within clusters of core histone genes". Genomics. 10 (4): ...

https://en.wikipedia.org/wiki/HIST1H3F

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2B type 1-L is a protein that in humans is encoded by the HIST1H2BL gene. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ... Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of ...

https://en.wikipedia.org/wiki/HIST1H2BL

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... 1998). "Core Histones and HIRIP3, a Novel Histone-Binding Protein, Directly Interact with WD Repeat Protein HIRA". Mol. Cell. ... "Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T ... Histone H2B type 2-E is a protein that in humans is encoded by the HIST2H2BE gene. ...

https://en.wikipedia.org/wiki/HIST2H2BE

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... Histone H2B type 1-M is a protein that in humans is encoded by the HIST1H2BM gene. ... The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher ... Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of ...

https://en.wikipedia.org/wiki/HIST1H2BM

Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind ... Health Conditions Related to Chromosomal Changes. The following chromosomal conditions are associated with changes in the ... By adding a molecule called a methyl group to histones, histone methyltransferases can turn off (suppress) the activity of ... Chromosome 9 likely contains 800 to 900 genes that provide instructions for making proteins. These proteins perform a variety ...

https://medlineplus.gov/genetics/chromosome/9/

... which modify both PARP itself and chromosomal proteins and DNA repair factors [67]. Histones and HMGB (High mobility group box ... Epigenetic regulation is mainly driven by modifications of chromosomal DNAs and histone proteins [98]. The biological relevance ... ADP-ribosylation of chromosomal proteins and mouse mammary tumor virus gene expression. The Journal of Biological Chemistry. ... The activation of HDACs in cancer cells might be the response to the aberrant hyper-acetylation of histone proteins that could ...

https://www.intechopen.com/chapters/57487

Rabbit Polyclonal Antibody Shop Histone H4K8ac Polyclonal Antibody, Active Motif™ at Fishersci.com ... Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. ... histone 1, H4b; histone 1, H4e; histone 1, H4i; histone 2, H4; histone 2, H4a; Histone 4; Histone 4 family, member M; histone 4 ... H4 histone family, member A; H4 histone family, member I; H4 histone family, member J; H4 histone family, member M; H4 histone ...

https://www.fishersci.com/shop/products/histone-h4k8ac-polyclonal-antibody-active-motif-1/p-7188617

Non-histone chromosomal proteins HMG1 and 2 enhance ligation reaction of DNA double-strand breaks. Biochem. Biophys. Res. ... DNA lesion-recognizing proteins and the p53 connection. Anticancer Res. 16:225-242.. Bucher, E. A., Dhoot, G. K., Emerson, M.M ... HMG-domain proteins specifically inhibit the repair of the major DNA adduct of the anticancer drug cisplatin by human excision ... High mobility group proteins 1 and 2 recognize chromium-damaged DNA. Carcinogenesis. 18:371-375.. Wood, R.D. 1996. DNA repair ...

https://ndltd.ncl.edu.tw/cgi-bin/gs32/gsweb.cgi/login?o=dnclcdr&s=id=%22090NTOU0613002%22.&searchmode=basic

5] Parafibromin is thought to act as a tumor suppressor gene but may have several other effects, including histone modification ... Accuracy of combined protein gene product 9.5 and parafibromin markers for immunohistochemical diagnosis of parathyroid ... but carcinomas more frequently exhibit alterations in gene copy number and have large-scale chromosomal deletions. [6] ... Allelic loss of the retinoblastoma protein has been shown to be associated with parathyroid carcinoma. [9] ...

https://emedicine.medscape.com/article/280908-overview

Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 1998. 391:597-601. View this article via: ... Chromosomal translocations cause deregulated BCL-6 expression by promoter substitution in B-cell lymphoma. EMBO J 1995. 14:6209 ... Acetylated histones were detected utilizing the aforementioned anti-acetylated histone H3 and histone H4 antibodies and were ... Fusion proteins of the retinoic acid receptor-alpha recruit histone deacetylase in promyelocytic leukaemia. Nature 1998. 391: ...

https://www.jci.org/articles/view/11537

... approximately half of these DNMs disrupt gene function and the remainder result in altered protein function. We estimate that ... CDC2 Protein Kinase. , Casein Kinase II. , Child. , Chromosomal Proteins, Non-Histone. , Cohort Studies. , DEAD-box RNA ... Myeloid-Lymphoid Leukemia Protein. , Nerve Tissue Proteins. , Parents. , Phenotype. , Prevalence. , Protein Phosphatase 2C. , ... DNA-Binding Proteins. , Developmental Disabilities. , Exome. , Female. , Heredity. , Histone-Lysine N-Methyltransferase. , ...

https://www.repository.cam.ac.uk/items/01526b7a-5c8e-44de-8ae3-2fd0719b59c7

Cell Cycle Proteins * Cell Division / genetics* * Chromosomal Proteins, Non-Histone / genetics * Chromosomal Proteins, Non- ...

https://pubmed.ncbi.nlm.nih.gov/19838048/

It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a ... It is a complex of DNA; HISTONES; and nonhistone proteins (CHROMOSOMAL PROTEINS, NON-HISTONE) found within the nucleus of a ...

https://decs.bvsalud.org/en/ths/resource/?id=23194

Histones, Related Proteins, and Modifying Enzymes. Nonhistone Chromosomal Proteins (includes protamines, transition proteins, ... LIM Domain Proteins. PDZ Domain. WD Repeat Proteins. Ring Finger Proteins. Tripartite Motif Family. Zinc Finger Proteins. ... G-Protein-coupled Receptors. Peptide and Protein G-coupled Signals. G Proteins. Inositol Pathways (includes protein kinase C). ... 8. Structural Proteins. Origins of Structural Proteins. Actin and Related Proteins. Myosin. Tubulin and Microtubules. Kinesins ...

https://cshlpress.com/default.tpl?action=full&cart=1606051323497714024&--eqskudatarq=886&typ=ps&newtitle=Guide%20to%20the%20Human%20Genome

... may bind acetylated histones), and 1 plant homeodomain; these domains may be involved in protein-protein interaction; a FYRN ... Result of the Chromosomal Anomaly. Description. Fusion between MLL intron 9 and EEFSEC intron 1, but with no maintenance of an ... Protein description. A major transcript of 14982 bp produces a 3969 amino acids protein from 36 of the 37 exons. Contains from ... MLL is cleaved by taspase 1 into 2 proteins before entering the nucleus: a p300/320 N-term protein called MLL-N, and a p180 C- ...

https://atlasgeneticsoncology.org/haematological/1407/t

... histone) protein of which the chromosomes are composed] and methylated regions of DNA sequence. This interaction should be ... These chromosomal regions might be good candidates for redesigning chromosomal circuits. Accordingly, I expect that studies in ... DNA methylomes, histone codes and miRNAs: Tying it all together. Int. J. Biochem. Cell Biol., 41: 87-95.. PubMed ... Methylated and non methylated DNA sequences are involved in gene expression of RNA and proteins, beside their role in the ...

https://scialert.net/fulltext/?doi=ajaps.2012.67.73#ref

It is a functional homolog of histone-like nucleoid-structuring protein (H-NS); it acts as a DNA-bridging protein that plays a ... The Lsr2 and MSMEG_1060 proteins exhibit different DNA binding specificities and chromosomal localizations. Our results suggest ... in Mycobacterium tuberculosis via Protein-Protein Interactions. Plocinska, Renata; Wasik, Karolina; Plocinski, Przemyslaw; ... membrane proteins as mycobacterial effectors responsible for the pathogen-host protein interplay. SAA1-opsonization of Mtb ...

https://pesquisa.bvsalud.org/brasil/?lang=pt&q=au:Plocinski,+Przemyslaw

Class II members include non-histone chromosomal .... pfam00505. Location:50 → 117. HMG_box; HMG (high mobility group) box. ... HMG-box; High Mobility Group (HMG)-box is found in a variety of eukaryotic chromosomal proteins and transcription factors. HMGs ... DNA-protein cross-links between abasic DNA damage and mitochondrial transcription factor A (TFAM). Title: DNA-protein cross- ... HMGB-UBF_HMG-box; class II and III members of the HMG-box superfamily of DNA-binding proteins. These proteins bind the minor ...

https://https.ncbi.nlm.nih.gov/gene/7019

Ke, Q.; Ellen, T.P.; Costa, M. Nickel compounds induce histone ubiquitination by inhibiting histone deubiquitinating enzyme ... Chromosomal alterations. a Mixed results [23,96,97,98]. a Mixed results [99,100,101]. a Mixed results [102,103,104,105,106,107] ... Nickel ions have a weak interaction with DNA but a preferentially stronger interaction with proteins. For example, Ni2+ has ... and decrease histone acetylation (H4) through decreased histone acetyltransferase activity (Table 1). Nickel compounds can ...

https://www.mdpi.com/2304-6740/7/7/89

The current concepts of sperm biochemical markers and the central role of the HspA2 chaperone protein, a measure of sperm ... Because HspA2 is a component of the synaptonemal complex, low HspA2 levels and increased frequency of chromosomal aneuploidies ... Hyaluronic acid binding also excludes immature sperm with cytoplasmic extrusion, persistent histones, and DNA chain breaks. ... The frequencies of sperm with chromosomal disomy are reduced approximately fourfold to fivefold in hyaluronic acid selected ...

http://www2a.cdc.gov/nioshtic-2/BuildQyr.asp?s1=20060913&PageNo=1&RecNo=10&View=f&

... histone assembly into nucleosomes, or chromatin remodeling by linker histones, polycomb group proteins, nuclear scaffold ... Chromatin proteins regulate access of transcription factors to chromosomal DNA and expression patterns for individual genes. ... Linker histone H1 and somatic cell histone H1 are important regulators of gene expression. Their expression changes from absent ... Expression of genes in higher organisms is regulated by histones H2A, H2B, H3, and H4, as well as histone H1 and other ...

https://nap.nationalacademies.org/read/10977/chapter/13

This turned out to be the case, and Liz was able to show that the histone proteins associated with the frataxin gene had all ... Since I had a background in studying how chromosomal proteins affect gene expression, my feeling was that DNA structure was not ... We believed that modifications of the histone proteins that bind DNA might be responsible for turning off the frataxin gene in ... This led to our hypothesis that small molecules that act on these histone signals might reverse silencing. Indeed, we found ...

https://www.curefa.org/featured-scientists/?limit=5&limitstart=0

Description: Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in ... Description: This recombinant Histone H2A antibody reacts to the Histone H2A protein, independent of post-translational ... Description: This recombinant Histone H2A antibody reacts to the Histone H2A protein, independent of post-translational ... Human H2A(Histone H2A) ELISA Kit. Human H2A(Histone H2A) ELISA Kit ...

https://unicoupi.com/human-h2ahistone-h2a-elisa-kit/

Histone proteins that surround that region lack the acetylation modification that is present when the genes are expressed in ... When these modifications occur, the gene present in that chromosomal region is silenced. Increasingly, scientists understand ... The c-Flip protein, a protein involved in mediating the cell death pathway, comes in two forms: long (c-FLIPL) and short (c- ... There are characteristic modifications to histone proteins and DNA that are associated with silenced genes. In cancer cells, ...

https://bio.libretexts.org/Courses/Reedley_College/Biology_for_Science_Majors_I/15%3A_Gene_Expression/15.08%3A_Cancer_and_Gene_Regulation

... which includes a gene encoding a binding protein for cyclic adenosine monophosphate-response element binding protein (CBP) ( ... Disruption of the human CBP gene, either by gross chromosomal rearrangements or by point mutations, leads to Rubinstein-Taybi ... serving as histone acetyltransferases that open the chromatin structure, a process essential for gene expression. [10] During ... The EP300 gene on band 22q13 encodes a protein, p300, that is highly similar to CREBBP. At present, the cause of Rubinstein- ...

https://reference.medscape.com/article/1115352-overview

Crystal structure of the Histone Methyltransferase SET7/9. 1ml9. Structure of the Neurospora SET domain protein DIM-5, a ... In addition to these chromosomal proteins modulating gene activities and/or chromatin structure, the SET domain is found in ... GLP (G9a-like protein) SET domain in complex with Dnmt3aK44me0 peptide. 3swc. GLP (G9a-like protein) SET domain in complex with ... Structure and Catalytic Mechanism of a SET Domain Protein Methyltransferase. 1mt6. Structure of histone H3 K4-specific ...

https://smart.embl.de/smart/do_annotation.pl?DOMAIN=SET&START=3823&END=3945&E_VALUE=6.09e-45&TYPE=SMART&BLAST=EAVGVYRSPIHGRGLFCKRNIDAGEMVIEYAGNVIRSIQTDKREKYYDSKGIGCYMFRIDDSEVVDATMHGNAARFINHSCEPNCYSRVINIDGQKHIVIFAMRKIYRGEELTYDYKFPIEDA

However, over 80% of chromosomal proteins are structural proteins, including core and linker histones, topoisomerase II, ... particularly the chromosomal proteins, for there is still so much more to be discovered for application in molecular ... It is not clear how the protein scaffold replicates during the cell cycle. The nature and number of proteins that make up the ... Chromosomal localisation of a single copy gene by in situ hybridisation : human beta-globin genes on the short arm of ...

https://molecularcytogenetics.biomedcentral.com/articles/10.1186/s13039-015-0125-8

Any tendency of Smc proteins with weakened hinges to dissociate will be suppressed by interconnection of their NBDs by Scc1. We ... Amino Acid Sequence, Cell Cycle Proteins, Chromatids, Chromatography, Gel, Chromosomal Proteins, Non-Histone, Crystallization, ... Any tendency of Smc proteins with weakened hinges to dissociate will be suppressed by interconnection of their NBDs by Scc1. We ... Both interaction surfaces within cohesins hinge domain are essential for its stable chromosomal association. ...

https://www.neuroscience.ox.ac.uk/publications/98495

... to talk about his work on the role of non-histone proteins in chromosome structure and function during mitosis. ... how the chromosomal passenger complex was discovered, how condensin I and II work together in chromatin loop formation, and ... The Role of Non-Histone Proteins in Chromosome Structure and Function During Mitosis (Bill Earnshaw). Episode 26 ... to talk about his work on the role of non-histone proteins in chromosome structure and function during mitosis. ...

https://www.activemotif.jp/podcasts-bill-earnshaw

... to probe proteinDNA interactions within specific genes and to determine the genomic location of specific chromosomal proteins. ... Solomon MJ, Larsen PL, Varshavsky A. Mapping proteinDNA interactions in vivo with formaldehyde: Evidence that histone H4 is ... Mapping proteinDNA interactions in vivo with formaldehyde: Evidence that histone H4 is retained on a highly transcribed gene. ... Mapping proteinDNA interactions in vivo with formaldehyde : Evidence that histone H4 is retained on a highly transcribed gene. ...

https://scholars.uthscsa.edu/en/publications/mapping-proteindna-interactions-in-vivo-with-formaldehyde-evidenc

The Mre11/Rad50/Nbs1 protein complex plays central enzymatic and signaling roles in the DNA-damage response. Nuclease (Mre11) ... Amino Acid Sequence, Cell Cycle Proteins, Chromosomal Proteins, Non-Histone, Crystallography, X-Ray, DNA Damage, DNA Repair, ... DNA-Binding Proteins, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Nuclear Proteins, Phosphorylation, Protein ... The Mre11/Rad50/Nbs1 protein complex plays central enzymatic and signaling roles in the DNA-damage response. Nuclease (Mre11) ...

https://www.rdm.ox.ac.uk/publications/418057

... are protein deacetylases dependent on nicotine adenine dinucleotide (NAD) and are found in organisms ranging from bacteria to ... García-Salcedo JA, Gijon P, Nolan DP, Tebabi P, Pays E: A chromosomal SIR2 homologue with both histone NAD-dependent ADP- ... protein-protein interactions, and protein stability (reviewed in [1]). Post-translational modification of proteins at lysine ... Although Sirt3 shows robust histone deacetylase activity on a histone H4 peptide in vitro, the absence of histones in ...

https://genomebiology.biomedcentral.com/articles/10.1186/gb-2004-5-5-224

... which is bound to a complex mixture of proteins (histone and non-histone) to form chromatin. • Eukaryotes have closed, circular ... Plasmid DNA carries genetic information, and undergoes replication that may or may not be synchronized to chromosomal division ... Each prokaryotic chromosome is associated with non-histone proteins that can condense the DNA to form a nucleoid. ... The flow of information from DNA to RNA to protein is termed the "central dogma" of molecular biology and is descriptive of all ...

https://de.slideshare.net/AnamTariq3/structure-of-dna-232669048

... histone modifications, scaffolding proteins, and transcription factors (iii) three-dimensional spatial organization, bringing ... My team will explore the multiple ways in which nuclear organization and chromosomal interactions are important for regulation ... Chromatin is organized at various levels as (i) a linear genome comprising the DNA sequence of protein-coding and non-coding ...

https://www.iisertvm.ac.in/faculty/nishana

Chemical modification of these histones is one way that the cell regulates the packing and unpacking of the DNA and its associated proteins (collectively called chromatin), which in turn helps to determine whether a given gene is activated or repressed. (mdanderson.org)
The Bedford lab studies one such modification, the methylation of arginine amino acids in histones and other chromatin-associated proteins. (mdanderson.org)
The researchers studied the two proteins in breast cancer cell lines, where they discovered that TDRD3 recruits TOP3B to active chromatin (where genes are turned on) that is marked by arginine methylation. (mdanderson.org)
The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. (fishersci.com)
methylates H3, including histones in the HOX area for allowing chromatin to be open to transcription. (atlasgeneticsoncology.org)
The chromatin fiber is further compacted through the interaction of a linker histone, H1, with the DNA between the nucleosomes to form higher order chromatin structures. (epigentek.com)
Independent Mechanisms Target SMCHD1 to Trimethylated Histone H3 Lysine 9-Modified Chromatin and the Inactive X Chromosome. (ox.ac.uk)
We further show that the principal mechanism for chromatin loading of SMCHD1 involves an LRIF1-mediated interaction with HP1γ at trimethylated histone H3 lysine 9 (H3K9me3)-modified chromatin sites on the chromosome arms. (ox.ac.uk)
Both genes are highly conserved, and their proteins are thought to have 2 functions: (1) formation of a bridge or scaffold between the DNA-binding transcription factors and the RNA polymerase II complex and (2) serving as histone acetyltransferases that open the chromatin structure, a process essential for gene expression. (medscape.com)
They bind to structural components (emerin, nesprin), chromatin components (histone), signal transduction molecules (protein kinase C), and several gene regulatory molecules. (medscape.com)

DNA is tightly packaged into chromosomes along with histone proteins. (mdanderson.org)
Preface Eukaryotic chromosomes are complex structures containing very long DNA molecules, histones, and nonhistone proteins. (pdfroom.com)
The impact of nonhistone proteins on the structure of chromosomes is still a mystery. (pdfroom.com)

A new study by Mark Bedford, Ph.D. , professor of Molecular Carcinogenesis , and colleagues published in Molecular Cell sheds light on the mechanism by which TDRD3 - a protein that 'reads' epigenetic marks on chromosomal proteins - turns on certain genes. (mdanderson.org)
Several types of chemical modifications of the five major histone protein families give rise to a complex 'histone code' that signals the transcriptional machinery to turn genes on or off. (mdanderson.org)
Analyzing 5′-upstream non-protein-encoding regions of the human mitochondrial function-associated genes, we speculate that mitochondrial functions could be recovered or improved at a transcriptional level. (intechopen.com)
Chromosome 9 likely contains 800 to 900 genes that provide instructions for making proteins. (medlineplus.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)
In the online version, these sections contain links to more information about proteins encoded by over 17,000 known or predicted human genes. (cshlpress.com)
Furthermore, Omics.org indicated that the main focus of omics is on 1) mapping information objects such as genes, proteins and ligands, 2) finding interaction relationships among the objects, 3) engineering the networks and objects to understand and manipulate the regulatory mechanisms and 4) integrating various omes and omics subfields. (scialert.net)
The chromosomal protein SMCHD1 plays an important role in epigenetic silencing at diverse loci, including the inactive X chromosome, imprinted genes, and the facioscapulohumeral muscular dystrophy locus. (ox.ac.uk)

and nonhistone proteins ( chromosomal proteins, non-histone) found within the nucleus of a cell. (usda.gov)

This gene is intronless and encodes a member of the histone H4 family. (fishersci.com)
This gene encodes a replication-independent member of the histone H2A family that is distinct from other members of the family. (epigentek.com)

This gene is found in the large histone gene cluster on chromosome 6. (fishersci.com)
The following chromosomal conditions are associated with changes in the structure or number of copies of chromosome 9. (medlineplus.gov)
9q22.3 microdeletion is a chromosomal change in which a small piece of the long (q) arm of chromosome 9 is deleted in each cell. (medlineplus.gov)
Methylated and non methylated DNA sequences are involved in gene expression of RNA and proteins, beside their role in the structural organization of the DNA sequence and the chromosome. (scialert.net)
The following topics are discussed: chromosome structure, repair of genetic dam- age and chromosomal aberrations (Chaps. (pdfroom.com)
Although homology with canonical SMC family proteins suggests a role in chromosome organization, the mechanisms underlying SMCHD1 function and target site selection remain poorly understood. (ox.ac.uk)
EDMD1 is caused by mutations in the EMD gene on the X chromosome that codes for the nuclear envelope protein emerin. (medscape.com)

Over 10 years ago, arginine methylation of histone tails was identified as an epigenetic mark that was linked to gene activation. (mdanderson.org)

A 2005 BMC Cancer paper on combining RNAi and protein kinase inhibitors has achieved the designation of highly accessed on BioMed Central. (hstalks.com)
Anaplastic lymphoma kinase (ALK) protein may be detected in most cases (60-70%) of systemic ALCL by immunohistochemistry. (medscape.com)

DDB, a putative DNA repair protein, can function as a transcriptional partner of E2F1. (ncl.edu.tw)
CBP and EP300 are ubiquitously expressed homologous proteins that act as transcriptional co-activators. (medscape.com)

Western blot analysis of extracts of various cell lines, using Histone H2A.Z Polyclonal Antibody at 1:1000 dilution. (epigentek.com)

The present volume deals mainly with chromosomal aberrations. (pdfroom.com)
18-22), and chromosomal aberrations as indicators of mutagenic activities of environmental chemicals and life-style fac- tors (Chaps. (pdfroom.com)
22 DNA Lesions, DNA Repair, and Chromosomal Aberrations (With 6 Figures) A.T. NATARAJAN, R.c. (pdfroom.com)

This is accomplished by a class of enzymes called protein arginine methyltransferases (PRMTs). (mdanderson.org)

Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. (fishersci.com)

The research team observed that in mice lacking the TDRD3 gene there was an increase in both R-loop formation and chromosomal translocations. (mdanderson.org)
Studies in mice have shown that this particular histone is required for embryonic development and indicate that lack of functional histone H2A leads to embryonic lethality. (epigentek.com)

Nucleosomes consist of approximately 146 bp of DNA wrapped around a histone octamer composed of pairs of each of the four core histones (H2A, H2B, H3, and H4). (epigentek.com)

d) Helicases and single-strand binding proteins that work at the 5' end. (brainkart.com)

In 5 of 6 gene mutations that have been shown to cause EDMD, the affected protein is present in the LINC (linker of nucleoskeleton and cytoskeleton) complex. (medscape.com)

HRPT2 encodes a protein called parafibromin. (medscape.com)
The EP300 gene on band 22q13 encodes a protein, p300, that is highly similar to CREBBP. (medscape.com)

A major transcript of 14982 bp produces a 3969 amino acids protein from 36 of the 37 exons. (atlasgeneticsoncology.org)
Recombinant fusion protein containing a sequence corresponding to amino acids 1-128 of human H2AFZ (NP_002097.1). (epigentek.com)

Rett syndrome (RTT) is a severe neurodevelopmental disorder caused, in most classic cases, by mutations in the X-linked methyl-CpG-binding protein 2 gene (MECP2). (nih.gov)
[ 6 ] HRPT2 mutations can also be seen in benign parathyroid adenomas, but carcinomas more frequently exhibit alterations in gene copy number and have large-scale chromosomal deletions. (medscape.com)
Disruption of the human CBP gene, either by gross chromosomal rearrangements or by point mutations, leads to Rubinstein-Taybi syndrome. (medscape.com)
New mutations have been found in the synaptic nuclear envelope protein 1 ( SYNE1 ) gene and in the synaptic nuclear envelope protein 2 ( SYNE2 ) gene in a few families, also termed Nesprin-1 and Nesprin-2, respectively. (medscape.com)
Lastly, mutations in the transmembrane protein 43 (TMEM43), also termed LUMA, which binds to emerin and SUN2, has also been reported to cause an EDMD phenotype in a few families. (medscape.com)
Whatever the true mechanism, the discovery of mutations in several different nuclear membrane proteins that cause similar diseases will likely eventually lead to a better understanding of nuclear membrane physiology and the pathophysiology of diseases caused by mutations in these proteins. (medscape.com)

Lysates/proteins: 25ug per lane. (epigentek.com)
Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Multi-species Histone H2A (H2A) in tissue homogenates, cell lysates and other biological fluids. (unicoupi.com)
Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Multi-species Histone H2A (H2A) in samples from tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (unicoupi.com)
Description: A sandwich quantitative ELISA assay kit for detection of Human H2A Histone Family, Member V (H2AFV) in samples from tissue homogenates, cell lysates or other biological fluids. (unicoupi.com)

The structural features of the association of DNA with histones are relatively well understood. (pdfroom.com)

14-17), the use of chromosomal ab- erration frequencies as biological dosimeters of radiation exposure (Chaps. (pdfroom.com)
The frequencies of sperm with chromosomal disomy are reduced approximately fourfold to fivefold in hyaluronic acid selected sperm compared with semen sperm, comparable to the increase in such abnormalities in intracytoplasmic sperm injection offspring. (cdc.gov)

As part of its charge, the committee was asked to prepare a subreport evaluating methods for detecting potential unintended compositional changes across the spectrum of messenger ribonucleic acid (mRNA), proteins, metabolites and nutrients that may occur in food derived from cloned animals that have not been genetically modified via genetic engineering methods. (nationalacademies.org)

A few years ago the lab identified TDRD3, a protein that 'reads' methyl-arginine marks on histone tails. (mdanderson.org)

These chromosomal changes are seen only in cancer cells. (medlineplus.gov)
The protein produced from the BCR-ABL1 gene signals cells to continue dividing abnormally and prevents them from self-destructing, which leads to overproduction of the abnormal cells. (medlineplus.gov)
They hypothesized that sticky DNA prevents the enzyme RNA polymerase from copying the frataxin gene into messenger RNA, thereby reducing the amount of frataxin protein in patient cells. (curefa.org)

The entire text of the Guide is searchable, and tools are available for identifying human protein sequences using those from other species. (cshlpress.com)

[ 1 ] Even though these proteins are ubiquitously expressed, disease manifestations are tissue specific for as yet unclear reasons. (medscape.com)

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. (fishersci.com)
This complex includes nuclear membrane integral and associated proteins including emerin, lamin A/C, SUN1, SUN2, nesprin-1, and nesprin-2 that are proposed to form a mechanical link between the nucleoskeleton and cytoskeleton. (medscape.com)
Emerin is a ubiquitous inner nuclear membraneprotein, presentin nearly all cell types, although its highest expression is in skeletal and cardiacmuscle.Emerin binds to many nuclear proteins, including several gene-regulatory proteins (eg, barrier-to-autointegration factor, germ cell-less, Btf), nesprins (proteins that act as molecular scaffolds), F-actin, and lamins. (medscape.com)

The study establishes a link between TDRD3 and an enzyme that unwinds DNA at regions of active gene expression, and provides evidence that this partnership can prevent DNA breakage and chromosomal translocations - two of the hallmarks of cancer. (mdanderson.org)

[ 5 ] Parafibromin is thought to act as a tumor suppressor gene but may have several other effects, including histone modification and activation of signaling pathways. (medscape.com)

The functional response of MDMs to hSAA-1 and/or tubercle bacilli was also evaluated for selected cytokines at the protein level by applying the Milliplex system. (bvsalud.org)
A gene, the basic unit of heredity, is a segment of DNA containing all the information necessary to synthesize a polypeptide (protein) or a functional RNA molecule. (msdmanuals.com)

They found that TDRD3 forms a complex with a protein called topoisomerase 3B (TOP3B), an enzyme that unwinds DNA and, in so doing, prevents DNA structures from forming that impede gene transcription. (mdanderson.org)
Because HspA2 is a component of the synaptonemal complex, low HspA2 levels and increased frequency of chromosomal aneuploidies are related in diminished maturity sperm. (cdc.gov)

The encoded protein also functions in mitochondrial DNA replication and repair. (nih.gov)

Identification and isolation of damage-recognition protein complexes from zebrafish(Danio rerio) early embryos. (ncl.edu.tw)

For each protein, basic characteristics about its composition and length, its human relatives and relatedness to proteins in other species, and direct links to resources at NCBI are included. (cshlpress.com)
Additional links to NCBI resources are provided for human noncoding RNAs and repeated DNA elements and for proteins of interest from other species. (cshlpress.com)

Protein synthesis, folding, and tertiary and quaternary structure ultimately determine much of the body's structure and function. (msdmanuals.com)

This Histone H4 acetyl Lys8 antibody was raised against a peptide containing acetyl Lys8 of human Histone H4. (fishersci.com)
The binding activity expressed in embryos was apparently unrelated to human DNA repair damage-recognition proteins XPA、RPA-70 and RPA-32, since those polypeptides recognized by an anti-human XPA、RPA-70 and RPA-32 antibody were detected only in 84-h-old zebrafish extracts. (ncl.edu.tw)
The DNA damage-recognition problem in human and other eukaryotic cell: the XPA damage binding protein. (ncl.edu.tw)
Characterization of DNA recognition by the human UV-damaged DNA-binding protein. (ncl.edu.tw)
10-12), human disorders with chromosomal instabilities (Chap. 13), the phenomenon of adaptive response (Chaps. (pdfroom.com)

Hyaluronic acid binding also excludes immature sperm with cytoplasmic extrusion, persistent histones, and DNA chain breaks. (cdc.gov)

Proto-Oncogene Proteins c-mdm2" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)

He collaborated with the Gunter Reuter laboratory at the Martin Luther Universitat, Germany, on the identification of novel proteins involved in heterochromatin formation later identified as histone deacetylases. (hstalks.com)

This graph shows the total number of publications written about "Proto-Oncogene Proteins c-mdm2" by people in this website by year, and whether "Proto-Oncogene Proteins c-mdm2" was a major or minor topic of these publications. (umassmed.edu)

The current concepts of sperm biochemical markers and the central role of the HspA2 chaperone protein, a measure of sperm cellular maturity and fertilizing potential, are reviewed. (cdc.gov)

The binding of 12-hr-old and 84-hr-old extracts to CPD- and 6-4PPs under various concentration of NaCl supported the possibility that different damage-recognition protein were expressed in zebrafish according to their developmental condition. (ncl.edu.tw)

read more non-histone chromosomal proteins in Tom Grigliatti's laboratory at the University of British Columbia. (hstalks.com)

Anatomy28

Organisms16

Diseases1

Chemicals and Drugs116

Analytical, Diagnostic and Therapeutic Techniques and Equipment24

Phenomena and Processes81

Disciplines and Occupations1

Information Science3

Basic homopolyamino acids, histones and protamines are potent antagonists of angiogenin binding to ribonuclease inhibitor. (1/4598)

Onset of nucleolar and extranucleolar transcription and expression of fibrillarin in macaque embryos developing in vitro. (2/4598)

MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. (3/4598)

Replication-dependent marking of DNA by PCNA facilitates CAF-1-coupled inheritance of chromatin. (4/4598)

The topoisomerase-related function gene TRF4 affects cellular sensitivity to the antitumor agent camptothecin. (5/4598)

The RLF-B component of the replication licensing system is distinct from Cdc6 and functions after Cdc6 binds to chromatin. (6/4598)

Retardation of cell proliferation after expression of p202 accompanies an increase in p21(WAF1/CIP1). (7/4598)

Specific destruction of kinetochore protein CENP-C and disruption of cell division by herpes simplex virus immediate-early protein Vmw110. (8/4598)

Chromosomal Proteins, Non-Histone

Histones

High Mobility Group Proteins

Chromatin

HMGN1 Protein

Histone Deacetylases

Chromosomes

Nucleoproteins

HMGB1 Protein

Histone Deacetylase Inhibitors

Acetylation

Nucleosomes

Histone Acetyltransferases

DNA

Deoxyribonucleoproteins

Heterochromatin

Euchromatin

Transcription, Genetic

Histone Deacetylase 1

Cell Nucleus

HMGB2 Protein

Micrococcal Nuclease

Electrophoresis, Polyacrylamide Gel

Molecular Sequence Data

Bromouracil

Histone Code

Amino Acid Sequence

Histone Deacetylase 2

Chickens

Histone Demethylases

Histone Chaperones

HeLa Cells

Protein Binding

Methylation

Nuclear Proteins

DNA-Binding Proteins

Hydroxamic Acids

Thymus Gland

Histone-Lysine N-Methyltransferase

HMGA1a Protein

Trout

Oviducts

HMGA Proteins

Drosophila melanogaster

Binding Sites

Base Sequence

Protamines

Chromosomes, Human, 16-18

Transcription Factors

HMGN Proteins

Molecular Weight

Cell Line

Mitosis

Amino Acids

Saccharomyces cerevisiae Proteins

Cattle

Metaphase

Methanosarcina

Epigenesis, Genetic

Repressor Proteins

Archaeal Proteins

Gene Expression Regulation

RNA, Messenger

Complement Fixation Tests

Chromatin Assembly and Disassembly

Jumonji Domain-Containing Histone Demethylases

Centromere

Drosophila Proteins

Mutation

Saccharomyces cerevisiae

Deoxyribonucleases

Nucleic Acid Hybridization

Chromosomes, Human

Kinetics

Erythrocytes

Acetyltransferases

Cell Cycle Proteins

Chromatin Immunoprecipitation

Tritium

Protein Methyltransferases