A minichromosome maintenance protein that is a key component of the six member MCM protein complex. It contains a NUCLEAR LOCALIZATION SIGNAL which may provide targeting of the protein complex and an extended N-terminus which is rich in SERINE residues.
A minichromosome maintenance protein that is a key component of the six member MCM protein complex. It is also found in tightly-bound trimeric complex with MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 4 and MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 6.
A minichromosome maintenance protein that is a key component of the six member MCM protein complex. It is also found in tightly-bound trimeric complex with MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 4 and MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 7.
A minichromosome maintenance protein that is a key component of the six member MCM protein complex. It contains a NUCLEAR LOCALIZATION SIGNAL, which provide targeting of the protein complex. In addition, acetylation of this protein may play a role in regulating of DNA replication and cell cycle progression.
A minichromosome maintenance protein that is a key component of the six member MCM protein complex. It is also found in tightly-bound trimeric complex with MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 6 and MINICHROMOSOME MAINTENANCE COMPLEX COMPONENT 7.
Structures within the nucleus of archaeal cells consisting of or containing DNA, which carry genetic information essential to the cell.
A family of proteins that were originally identified in SACCHAROMYCES CEREVISIAE as being essential for maintaining the structure of minichromosomes00. They form into a protein complex that has helicase activity and is involved in a variety of DNA-related functions including replication elongation, RNA transcription, chromatin remodeling, and genome stability.
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 sequence-specific DNA-binding protein that plays an essential role as a global regulator of yeast cell cycle control. It contains a 56 amino acid MADS-box domain within the N-terminal of the protein and is one of the four founder proteins that structurally define the superfamily of MADS DOMAIN PROTEINS.
A family of anaerobic, coccoid to rod-shaped METHANOBACTERIALES. Cell membranes are composed mainly of polyisoprenoid hydrocarbons ether-linked to glycerol. Its organisms are found in anaerobic habitats throughout nature.
The process by which a DNA molecule is duplicated.
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.
A minichromosome maintenance protein that is a key component of the six member MCM protein complex. In addition, interaction of this protein with cyclin A results in its recruitment to CENTROSOMES where it may play a role in controlling centrosome reduplication.
A minichromosome maintenance protein that forms a hexameric complex with MINICHROMSOME MAINTENANCE COMPLEX COMPONENT 9. The MCM8-MCM9 helicase complex is involved in HOMOLOGOUS RECOMBINATION REPAIR following the formation of DNA interstrand cross-links.
A minichromosome maintenance protein that forms a hexameric complex with MINICHROMSOME MAINTENANCE COMPLEX COMPONENT 8. The MCM8-MCM9 helicase complex is involved in HOMOLOGOUS RECOMBINATION REPAIR following the formation of DNA interstrand cross-links.
Proteins that catalyze the unwinding of duplex DNA during replication by binding cooperatively to single-stranded regions of DNA or to short regions of duplex DNA that are undergoing transient opening. In addition DNA helicases are DNA-dependent ATPases that harness the free energy of ATP hydrolysis to translocate DNA strands.
Proteins found in any species of archaeon.
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 CELL CYCLE and tumor growth marker which can be readily detected using IMMUNOCYTOCHEMISTRY methods. Ki-67 is a nuclear antigen present only in the nuclei of cycling cells.
The origin recognition complex is a multi-subunit DNA-binding protein that initiates DNA REPLICATION in eukaryotes.
Geminin inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex. It is absent during G1 phase of the CELL CYCLE and accumulates through S, G2,and M phases. It is degraded at the metaphase-anaphase transition by the ANAPHASE-PROMOTING COMPLEX-CYCLOSOME.
A unique DNA sequence of a replicon at which DNA REPLICATION is initiated and proceeds bidirectionally or unidirectionally. It contains the sites where the first separation of the complementary strands occurs, a primer RNA is synthesized, and the switch from primer RNA to DNA synthesis takes place. (Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
Proteins obtained from the species Schizosaccharomyces pombe. The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes.
A genus of anaerobic, rod-shaped METHANOBACTERIACEAE. Its organisms are nonmotile and use ammonia as the sole source of nitrogen. These methanogens are found in aquatic sediments, soil, sewage, and the gastrointestinal tract of animals.
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.
Deoxyribonucleic acid that makes up the genetic material of archaea.
Structures within the nucleus of fungal cells consisting of or containing DNA, which carry genetic information essential to the cell.
The use of fluorescence spectrometry to obtain quantitative results for the FLUORESCENT ANTIBODY TECHNIQUE. One advantage over the other methods (e.g., radioimmunoassay) is its extreme sensitivity, with a detection limit on the order of tenths of microgram/liter.
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.
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 genus of ascomycetous fungi of the family Schizosaccharomycetaceae, order Schizosaccharomycetales.
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.
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.
Molecular products metabolized and secreted by neoplastic tissue and characterized biochemically in cells or body fluids. They are indicators of tumor stage and grade as well as useful for monitoring responses to treatment and predicting recurrence. Many chemical groups are represented including hormones, antigens, amino and nucleic acids, enzymes, polyamines, and specific cell membrane proteins and lipids.
Deoxyribonucleic acid that makes up the genetic material of fungi.
Proteins found in any species of fungus.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The period of the CELL CYCLE preceding DNA REPLICATION in S PHASE. Subphases of G1 include "competence" (to respond to growth factors), G1a (entry into G1), G1b (progression), and G1c (assembly). Progression through the G1 subphases is effected by limiting growth factors, nutrients, or inhibitors.
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.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Macromolecular complexes formed from the association of defined protein subunits.
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)
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.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
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.
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.
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.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
The 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.
Nuclear antigen with a role in DNA synthesis, DNA repair, and cell cycle progression. PCNA is required for the coordinated synthesis of both leading and lagging strands at the replication fork during DNA replication. PCNA expression correlates with the proliferation activity of several malignant and non-malignant cell types.
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).
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
A species of ciliate protozoa used in genetic and cytological research.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
An order of insects comprising the sucking lice, which are blood-sucking ectoparasites of mammals. Recognized families include: Echinphthiriidae, Haematopinidae, and Pediculidae. The latter contains the medically important genera affecting humans: PEDICULUS and PHTHIRUS.
Immunologic techniques based on the use of: (1) enzyme-antibody conjugates; (2) enzyme-antigen conjugates; (3) antienzyme antibody followed by its homologous enzyme; or (4) enzyme-antienzyme complexes. These are used histologically for visualizing or labeling tissue specimens.
Protein kinases that control cell cycle progression in all eukaryotes and require physical association with CYCLINS to achieve full enzymatic activity. Cyclin-dependent kinases are regulated by phosphorylation and dephosphorylation events.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
DNA constructs that are composed of, at least, elements such as a REPLICATION ORIGIN; TELOMERE; and CENTROMERE, that are required for successful replication, propagation to and maintenance in progeny cells. In addition, they are constructed to carry other sequences for analysis or gene transfer.
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.
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.
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.
Established cell cultures that have the potential to propagate indefinitely.
Proteins conjugated with deoxyribonucleic acids (DNA) or specific DNA.
A prediction of the probable outcome of a disease based on a individual's condition and the usual course of the disease as seen in similar situations.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Proteins prepared by recombinant DNA technology.
A species of POLYOMAVIRUS originally isolated from Rhesus monkey kidney tissue. It produces malignancy in human and newborn hamster kidney cell cultures.
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.
Structures within the nucleus of bacterial cells consisting of or containing DNA, which carry genetic information essential to the cell.
A terminal section of a chromosome which has a specialized structure and which is involved in chromosomal replication and stability. Its length is believed to be a few hundred base pairs.
Interruptions in one of the strands of the sugar-phosphate backbone of double-stranded DNA.
The upkeep of property or equipment.

Identification of target sites of the alpha2-Mcm1 repressor complex in the yeast genome. (1/117)

The alpha2 and Mcm1 proteins bind DNA as a heterotetramer to repress transcription of cell-type-specific genes in the yeast Saccharomyces cerevisiae. Based on the DNA sequence requirements for binding by the alpha2-Mcm1 complex, we have searched the yeast genome for all potential alpha2-Mcm1 binding sites. Genes adjacent to the sites were examined for expression in the different cell mating types. These sites were further analyzed by cloning the sequences into a heterologous promoter and assaying for alpha2-Mcm1-dependent repression in vivo and DNA-binding affinity in vitro. Fifty-nine potential binding sites were identified in the search. Thirty-seven sites are located within or downstream of coding region of the gene. None of the sites assayed from this group are functional repressor sites in vivo or bound by the alpha2-Mcm1 complex in vitro. Among the remaining 22 sites, six are in the promoters of known alpha-specific genes and two other sites have an alpha2-Mcm1-dependent role in determining the direction of mating type switching. Among the remaining sequences, we have identified a functional site located in the promoter region of a previously uncharacterized gene, SCYJL170C. This site functions to repress transcription of a heterologous promoter and the alpha2-Mcm1 complex binds to the site in vitro. SCYJL170C is repressed by alpha2-Mcm1 in vivo and therefore using this method we have identified a new a-specific gene, which we call ASG7.  (+info)

Scanning mutagenesis of Mcm1: residues required for DNA binding, DNA bending, and transcriptional activation by a MADS-box protein. (2/117)

MCM1 is an essential gene in the yeast Saccharomyces cerevisiae and is a member of the MADS-box family of transcriptional regulatory factors. To understand the nature of the protein-DNA interactions of this class of proteins, we have made a series of alanine substitutions in the DNA-binding domain of Mcm1 and examined the effects of these mutations in vivo and in vitro. Our results indicate which residues of Mcm1 are important for viability, transcriptional activation, and DNA binding and bending. Substitution of residues in Mcm1 which are highly conserved among the MADS-box proteins are lethal to the cell and abolish DNA binding in vitro. These positions have almost identical interactions with DNA in both the serum response factor-DNA and alpha2-Mcm1-DNA crystal structures, suggesting that these residues make up a conserved core of protein-DNA interactions responsible for docking MADS-box proteins to DNA. Substitution of residues which are not as well conserved among members of the MADS-box family play important roles in contributing to the specificity of DNA binding. These results suggest a general model of how MADS-box proteins recognize and bind DNA. We also provide evidence that the N-terminal extension of Mcm1 may have considerable conformational freedom, possibly to allow binding to different DNA sites. Finally, we have identified two mutants at positions which are critical for Mcm1-mediated DNA bending that have a slow-growth phenotype. This finding is consistent with our earlier results, indicating that DNA bending may have a role in Mcm1 function in the cell.  (+info)

The replication capacity of intact mammalian nuclei in Xenopus egg extracts declines with quiescence, but the residual DNA synthesis is independent of Xenopus MCM proteins. (3/117)

In eukaryotes, the initiation of DNA synthesis requires the assembly of a pre-replicative complex (pre-RC) at origins of replication. This involves the sequential binding of ORC (origin-recognition-complex), Cdc6 and MCM proteins, a process referred to as licensing. After origin firing, the Cdc6 and MCM proteins dissociate from the chromatin, and do not rebind until after the completion of mitosis, thereby restricting replication to a single round in each cell cycle. Although nuclei normally become licensed for replication as they enter G(1), the extent to which the license is retained when cells enter the quiescent state (G(0)) is controversial. Here we show that the replication capacity of nuclei from Swiss 3T3 cells, in Xenopus egg extracts, is not lost abruptly with the onset of quiescence, but instead declines gradually. The decline in replication capacity, which affects both the number of nuclei induced to replicate and their subsequent rate of DNA synthesis, is accompanied by a fall in the level of chromatin-bound MCM2. When quiescent nuclei are incubated in egg extracts, they do not bind further MCMs unless the nuclei are first permeabilized. The residual replication capacity of intact nuclei must therefore be dependent on the remaining endogenous MCMs. Although high levels of Cdk activity are known to block MCM binding, we show that the failure of intact nuclei in egg extracts to increase their bound MCMs is not due to their uptake and accumulation of Cdk complexes. Instead, the failure of binding must be due to exclusion of some other binding factor from the nucleus, or to the presence within nuclei of an inhibitor of binding other than Cdk activity. In contrast to the situation in Xenopus egg extracts, following serum stimulation of intact quiescent cells, the level of bound MCMs does increase before the cells reach S phase, without any disruption of the nuclear envelope.  (+info)

ArgRII, a component of the ArgR-Mcm1 complex involved in the control of arginine metabolism in Saccharomyces cerevisiae, is the sensor of arginine. (4/117)

Repression of arginine anabolic genes and induction of arginine catabolic genes are mediated by a three-component protein complex, interacting with specific DNA sequences in the presence of arginine. Although ArgRI and Mcm1, two MADS-box proteins, and ArgRII, a zinc cluster protein, contain putative DNA binding domains, alone they are unable to bind the arginine boxes in vitro. Using purified glutathione S-transferase fusion proteins, we demonstrate that ArgRI and ArgRII1-180 or Mcm1 and ArgRII1-180 are able to reconstitute an arginine-dependent binding activity in mobility shift analysis. Binding efficiency is enhanced when the three recombinant proteins are present simultaneously. At physiological concentration, the full-length ArgRII is required to fulfill its functions; however, when ArgRII is overexpressed, the first 180 amino acids are sufficient to interact with ArgRI, Mcm1, and arginine, leading to the formation of an ArgR-Mcm1-DNA complex. Several lines of evidence indicate that ArgRII is the sensor of the effector arginine and that the binding site of arginine would be the region downstream from the zinc cluster, sharing some identity with the arginine binding domain of bacterial arginine repressors.  (+info)

A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control. (5/117)

Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP6). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae, designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP6, was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.  (+info)

In Saccharomyces cerevisiae, expression of arginine catabolic genes CAR1 and CAR2 in response to exogenous nitrogen availability is mediated by the Ume6 (CargRI)-Sin3 (CargRII)-Rpd3 (CargRIII) complex. (6/117)

The products of three genes named CARGRI, CARGRII, and CARGRIII were shown to repress the expression of CAR1 and CAR2 genes, involved in arginine catabolism. CARGRI is identical to UME6 and encodes a regulator of early meiotic genes. In this work we identify CARGRII as SIN3 and CARGRIII as RPD3. The associated gene products are components of a high-molecular-weight complex with histone deacetylase activity and are recruited by Ume6 to promoters containing a URS1 sequence. Sap30, another component of this complex, is also required to repress CAR1 expression. This histone deacetylase complex prevents the synthesis of the two arginine catabolic enzymes, arginase (CAR1) and ornithine transaminase (CAR2), as long as exogenous nitrogen is available. Upon nitrogen depletion, repression at URS1 is released and Ume6 interacts with ArgRI and ArgRII, two proteins involved in arginine-dependent activation of CAR1 and CAR2, leading to high levels of the two catabolic enzymes despite a low cytosolic arginine pool. Our data also show that the deletion of the UME6 gene impairs cell growth more strongly than the deletion of the SIN3 or RPD3 gene, especially in the Sigma1278b background.  (+info)

Solution structure of the MEF2A-DNA complex: structural basis for the modulation of DNA bending and specificity by MADS-box transcription factors. (7/117)

The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1-85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)(4)TAG has been solved by NMR. The protein comprises two domains: a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73). Recognition and specificity are achieved by interactions between the MADS-box and both the major and minor grooves of the DNA. A number of critical differences in protein-DNA contacts observed in the MEF2A-DNA complex and the DNA complexes of the related MADS-box transcription factors SRF and MCM1 provide a molecular explanation for modulation of sequence specificity and extent of DNA bending ( approximately 15 versus approximately 70 degrees ). The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors.  (+info)

The forkhead protein Fkh2 is a component of the yeast cell cycle transcription factor SFF. (8/117)

In the yeast Saccharomyces cerevisiae, the MADS-box protein Mcm1, which is highly related to mammalian SRF (serum response factor), forms a ternary complex with SFF (Swi five factor) to regulate the cell cycle expression of genes such as SWI5, CLB2 and ACE2. Here we show that the forkhead protein Fkh2 is a component of SFF and is essential for ternary complex formation on the SWI5 and ACE2 promoters. Fkh2 is essential for the correct cell cycle periodicity of SWI5 and CLB2 gene expression and is phosphorylated with a timing that is consistent with a role in this expression. Furthermore, investigation of the relationship between Fkh2 and a related forkhead protein Fkh1 demonstrates that these proteins act in overlapping pathways to regulate cell morphology and cell separation. This is the first example of a eukaryotic transcription factor complex containing both a MADS-box and a forkhead protein, and it has important implications for the regulation of mammalian gene expression.  (+info)

Minichromosome Maintenance Complex Component 2 (MCM2) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is involved in the initiation and regulation of DNA replication. MCM2 is specifically a helicase that helps to unwind the DNA double helix during replication. It is essential for the proper duplication of genetic material and cell division. Abnormalities in MCM2 function have been implicated in various diseases, including cancer.

Minichromosome Maintenance Complex Component 7 (MCM7) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is involved in the initiation and regulation of DNA replication. The MCM complex is made up of several different proteins, including MCM2-7, and plays a crucial role in the cell cycle by ensuring that DNA replication occurs only once per cell cycle. MCM7 has helicase activity, which helps to unwind the DNA double helix during replication. Defects in MCM7 have been associated with certain types of cancer.

Minichromosome Maintenance Complex Component 6 (MCM6) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is essential for the initiation and regulation of eukaryotic DNA replication. The MCM complex is composed of six related proteins (MCM2-7) that form a helicase responsible for unwinding DNA at the replication fork.

MCM6 plays a crucial role in the formation of the pre-replicative complex, which assembles at the origins of replication during the G1 phase of the cell cycle. MCM6, along with other MCM proteins, is loaded onto the origin of replication in an inactive form. Upon entry into the S phase, CDK (cyclin-dependent kinase) and DDK (DBF4-dependent kinase) phosphorylate MCM6 and other MCM components, activating the helicase activity and promoting DNA replication.

Mutations in MCM6 have been associated with certain genetic disorders, such as primordial dwarfism and Meier-Gorlin syndrome, which are characterized by growth retardation, developmental delays, and skeletal abnormalities.

Minichromosome Maintenance Complex Component 3 (MCM3) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is involved in the initiation and regulation of DNA replication. The MCM complex is made up of several different proteins, including MCM2-7, and helps to ensure that DNA replication occurs only once per cell cycle. MCM3 specifically plays a role in the loading and unloading of the MCM helicase onto DNA, helping to regulate the initiation of DNA replication. It is also involved in the cellular response to DNA damage and is considered a marker for actively proliferating cells.

Minichromosome Maintenance Complex Component 4 (MCM4) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is involved in the initiation and regulation of DNA replication. The MCM complex is made up of several different proteins, including MCM2-7, and helps to ensure that DNA replication occurs only once per cell cycle. MCM4 has helicase activity, which means it can unwind double-stranded DNA during the replication process. It also plays a role in the regulation of the cell cycle and is essential for cell survival. Defects in MCM4 have been associated with certain types of cancer.

Archaeal chromosomes refer to the genetic material present in Archaea, a domain of single-celled microorganisms. Like bacteria and eukaryotes, Archaea have their genetic material organized into a single circular chromosome, which is typically smaller than bacterial chromosomes. The archaeal chromosome contains all the genetic information necessary for the organism's survival, including genes coding for proteins, RNA molecules, and regulatory elements that control gene expression.

Archaeal chromosomes are structurally similar to bacterial chromosomes, with a histone-like protein called histone-like protein A (HLP) that helps compact the DNA into a more condensed form. However, archaeal chromosomes also share some features with eukaryotic chromosomes, such as the presence of nucleosome-like structures and the use of similar mechanisms for DNA replication and repair.

Overall, archaeal chromosomes are an important area of study in molecular biology, as they provide insights into the evolution and diversity of life on Earth.

Minichromosome Maintenance (MCM) proteins are a group of highly conserved helicase proteins that play essential roles in the initiation and regulation of eukaryotic DNA replication. They are named after the discovery that they are associated with the minichromosomes of budding yeast.

In humans, there are six main MCM proteins (MCM2-7) that form a hexameric complex, which is loaded onto origins of replication during the G1 phase of the cell cycle. This complex functions as a helicase, unwinding double-stranded DNA to create single-stranded templates for the replication machinery.

MCMs are also involved in the regulation of the DNA replication process, ensuring that it is initiated only once per cell cycle and that it proceeds in a controlled and efficient manner. Dysregulation of MCM proteins has been implicated in various diseases, including cancer, where overexpression of these proteins can lead to genomic instability and increased rates of cell division.

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

The major groups of cell cycle proteins include:

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

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

Minichromosome Maintenance 1 Protein (MCM1) is a protein that belongs to the minichromosome maintenance proteins complex, which is essential for the initiation and regulation of eukaryotic DNA replication. MCM1 is a crucial component of this complex, and it functions as a transcription factor that regulates the expression of genes involved in various cellular processes such as cell cycle progression, DNA repair, and development. In addition to its role in DNA replication and gene regulation, MCM1 has also been implicated in the development of certain types of cancer, making it an important area of research in cancer biology.

Methanobacteriaceae is a family of archaea within the order Methanobacteriales. These are obligate anaerobes that obtain energy for growth by reducing carbon dioxide to methane, a process called methanogenesis. They are commonly found in anaerobic environments such as wetlands, digestive tracts of animals, and sewage sludge. Some species are thermophilic, meaning they prefer higher temperatures, while others are mesophilic, growing best at moderate temperatures. Methanobacteriaceae are important contributors to the global carbon cycle and have potential applications in bioremediation and bioenergy production.

DNA replication is the biological process by which DNA makes an identical copy of itself during cell division. It is a fundamental mechanism that allows genetic information to be passed down from one generation of cells to the next. During DNA replication, each strand of the double helix serves as a template for the synthesis of a new complementary strand. This results in the creation of two identical DNA molecules. The enzymes responsible for DNA replication include helicase, which unwinds the double helix, and polymerase, which adds nucleotides to the growing strands.

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

Minichromosome Maintenance Complex Component 5 (MCM5) is a protein that is a part of the minichromosome maintenance (MCM) complex, which is involved in the initiation and regulation of DNA replication. MCM5 is specifically a helicase that unwinds double-stranded DNA into single strands, allowing for the replication process to begin. It is highly expressed in proliferating cells and is often used as a marker for cellular proliferation. Abnormal expression of MCM5 has been implicated in various human cancers, making it a potential target for cancer diagnosis and therapy.

Minichromosome Maintenance Complex Component 8 (MCM8) is a protein that is part of the minichromosome maintenance (MCM) complex, which is involved in the regulation of DNA replication. The MCM complex is a helicase that unwinds double-stranded DNA into single strands, allowing for the duplication of genetic material during the S phase of the cell cycle.

MCM8 forms a heterohexameric complex with MCM9 and functions as an ATPase to facilitate the unwinding of DNA. Mutations in the MCM8 gene have been associated with certain genetic disorders, including Meier-Gorlin syndrome, which is characterized by short stature, small ears, and patella aplasia or hypoplasia.

Defects in MCM8 function can lead to problems with DNA replication and cell division, resulting in the development of clinical features associated with this syndrome.

Minichromosome Maintenance Complex Component 9 (MCM9) is a protein that is involved in the regulation of DNA replication. It is a component of the minichromosome maintenance (MCM) complex, which is a group of proteins that play an essential role in the initiation and elongation phases of DNA replication.

The MCM complex is responsible for unwinding the double-stranded DNA at the replication origin, forming a replication bubble, and recruiting other replication factors to facilitate the synthesis of new DNA strands. MCM9 is specifically involved in the regulation of the MCM2-7 helicase activity, which is critical for the initiation of DNA replication.

Mutations in the gene encoding MCM9 have been associated with certain genetic disorders, such as primordial dwarfism and microcephaly, suggesting that this protein plays a crucial role in normal growth and development.

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

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

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

Archaeal proteins are proteins that are encoded by the genes found in archaea, a domain of single-celled microorganisms. These proteins are crucial for various cellular functions and structures in archaea, which are adapted to survive in extreme environments such as high temperatures, high salt concentrations, and low pH levels.

Archaeal proteins share similarities with both bacterial and eukaryotic proteins, but they also have unique features that distinguish them from each other. For example, many archaeal proteins contain unusual amino acids or modifications that are not commonly found in other organisms. Additionally, the three-dimensional structures of some archaeal proteins are distinct from their bacterial and eukaryotic counterparts.

Studying archaeal proteins is important for understanding the biology of these unique organisms and for gaining insights into the evolution of life on Earth. Furthermore, because some archaea can survive in extreme environments, their proteins may have properties that make them useful in industrial and medical applications.

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

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

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

The Ki-67 antigen is a cellular protein that is expressed in all active phases of the cell cycle (G1, S, G2, and M), but not in the resting phase (G0). It is often used as a marker for cell proliferation and can be found in high concentrations in rapidly dividing cells. Immunohistochemical staining for Ki-67 can help to determine the growth fraction of a group of cells, which can be useful in the diagnosis and prognosis of various malignancies, including cancer. The level of Ki-67 expression is often associated with the aggressiveness of the tumor and its response to treatment.

The Origin Recognition Complex (ORC) is a protein complex in eukaryotic cells that plays a crucial role in the initiation of DNA replication. It specifically recognizes and binds to the origins of replication, which are specific sequences on the DNA molecule where replication begins. The ORC serves as a platform for the assembly of additional proteins required for the initiation of DNA replication, including the minichromosome maintenance (MCM) complex. This whole process is highly regulated and essential for the accurate duplication of genetic material during cell division.

Geminin is a protein that plays a crucial role in the regulation of the cell cycle, specifically in the process of DNA replication. It functions as a regulatory protein that helps ensure the proper timing and completion of DNA replication before cell division occurs.

In more detail, Geminin binds to and inhibits the activity of several proteins involved in initiating DNA replication, such as CDT1 and CDC6. By doing so, it prevents the premature re-replication of DNA during the same cell cycle, which is essential for maintaining genomic stability.

Geminin is expressed in a cell cycle-dependent manner, with its levels peaking during the S and G2 phases, when DNA replication occurs, and declining during mitosis. This precise regulation of Geminin expression and activity helps coordinate the various stages of the cell cycle and ensures that DNA replication and cell division occur in a controlled and orderly fashion.

It's worth noting that deregulation of Geminin expression or function has been implicated in several human diseases, including cancer, where abnormal cell cycle control can contribute to uncontrolled cell growth and proliferation.

A replication origin is a specific location in a DNA molecule where the process of DNA replication is initiated. It serves as the starting point for the synthesis of new strands of DNA during cell division. The origin of replication contains regulatory elements and sequences that are recognized by proteins, which then recruit and assemble the necessary enzymes to start the replication process. In eukaryotic cells, replication origins are often found in clusters, with multiple origins scattered throughout each chromosome.

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

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

Methanobacterium is a genus of archaea belonging to the order Methanobacteriales and the family Methanobacteriaceae. They are commonly known as methanogenic bacteria, but they are not true bacteria; instead, they belong to the domain Archaea. These organisms are characterized by their ability to produce methane as a metabolic end-product in anaerobic conditions. They are typically found in environments like swamps, wetlands, digestive tracts of animals, and sewage sludge. The cells of Methanobacterium are usually rod-shaped and may appear gram-positive or gram-variable. Some species are capable of forming endospores.

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

Archaeal DNA refers to the genetic material present in archaea, a domain of single-celled microorganisms lacking a nucleus. Like bacteria, archaea have a single circular chromosome that contains their genetic information. However, archaeal DNA is significantly different from bacterial and eukaryotic DNA in terms of its structure and composition.

Archaeal DNA is characterized by the presence of unique modifications such as methylation patterns, which help distinguish it from other types of DNA. Additionally, archaea have a distinct set of genes involved in DNA replication, repair, and recombination, many of which are more similar to those found in eukaryotes than bacteria.

One notable feature of archaeal DNA is its resistance to environmental stressors such as extreme temperatures, pH levels, and salt concentrations. This allows archaea to thrive in some of the most inhospitable environments on Earth, including hydrothermal vents, acidic hot springs, and highly saline lakes.

Overall, the study of archaeal DNA has provided valuable insights into the evolutionary history of life on Earth and the unique adaptations that allow these organisms to survive in extreme conditions.

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

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

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

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

A fluoroimmunoassay (FIA) is a type of biochemical test that uses fluorescence to detect and measure the presence or concentration of a specific component, such as a protein or hormone, in a sample. In a FIA, the sample is mixed with a reagent that contains a fluorescent label, which binds to the target component. When the mixture is exposed to light of a specific wavelength, the labeled component emits light at a different wavelength, allowing it to be detected and measured.

FIAs are often used in clinical laboratories to diagnose and monitor various medical conditions, as they can provide sensitive and accurate measurements of specific components in biological samples. They are also used in research settings to study the interactions between biomolecules and to develop new diagnostic tests.

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

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

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

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

In the context of cell biology, "S phase" refers to the part of the cell cycle during which DNA replication occurs. The "S" stands for synthesis, reflecting the active DNA synthesis that takes place during this phase. It is preceded by G1 phase (gap 1) and followed by G2 phase (gap 2), with mitosis (M phase) being the final stage of the cell cycle.

During S phase, the cell's DNA content effectively doubles as each chromosome is replicated to ensure that the two resulting daughter cells will have the same genetic material as the parent cell. This process is carefully regulated and coordinated with other events in the cell cycle to maintain genomic stability.

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

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

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

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

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

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

Tumor markers are substances that can be found in the body and their presence can indicate the presence of certain types of cancer or other conditions. Biological tumor markers refer to those substances that are produced by cancer cells or by other cells in response to cancer or certain benign (non-cancerous) conditions. These markers can be found in various bodily fluids such as blood, urine, or tissue samples.

Examples of biological tumor markers include:

1. Proteins: Some tumor markers are proteins that are produced by cancer cells or by other cells in response to the presence of cancer. For example, prostate-specific antigen (PSA) is a protein produced by normal prostate cells and in higher amounts by prostate cancer cells.
2. Genetic material: Tumor markers can also include genetic material such as DNA, RNA, or microRNA that are shed by cancer cells into bodily fluids. For example, circulating tumor DNA (ctDNA) is genetic material from cancer cells that can be found in the bloodstream.
3. Metabolites: Tumor markers can also include metabolic products produced by cancer cells or by other cells in response to cancer. For example, lactate dehydrogenase (LDH) is an enzyme that is released into the bloodstream when cancer cells break down glucose for energy.

It's important to note that tumor markers are not specific to cancer and can be elevated in non-cancerous conditions as well. Therefore, they should not be used alone to diagnose cancer but rather as a tool in conjunction with other diagnostic tests and clinical evaluations.

Fungal DNA refers to the genetic material present in fungi, which are a group of eukaryotic organisms that include microorganisms such as yeasts and molds, as well as larger organisms like mushrooms. The DNA of fungi, like that of all living organisms, is made up of nucleotides that are arranged in a double helix structure.

Fungal DNA contains the genetic information necessary for the growth, development, and reproduction of fungi. This includes the instructions for making proteins, which are essential for the structure and function of cells, as well as other important molecules such as enzymes and nucleic acids.

Studying fungal DNA can provide valuable insights into the biology and evolution of fungi, as well as their potential uses in medicine, agriculture, and industry. For example, researchers have used genetic engineering techniques to modify the DNA of fungi to produce drugs, biofuels, and other useful products. Additionally, understanding the genetic makeup of pathogenic fungi can help scientists develop new strategies for preventing and treating fungal infections.

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

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

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

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

The G1 phase, or Gap 1 phase, is the first phase of the cell cycle, during which the cell grows in size and synthesizes mRNA and proteins in preparation for subsequent steps leading to mitosis. During this phase, the cell also checks its growth and makes sure that it is large enough to proceed through the cell cycle. If the cell is not large enough, it will arrest in the G1 phase until it has grown sufficiently. The G1 phase is followed by the S phase, during which DNA replication occurs.

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

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

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

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

Medical Definition of "Multiprotein Complexes" :

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

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

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

Chromosomes are thread-like structures that exist in the nucleus of cells, carrying genetic information in the form of genes. They are composed of DNA and proteins, and are typically present in pairs in the nucleus, with one set inherited from each parent. In humans, there are 23 pairs of chromosomes for a total of 46 chromosomes. Chromosomes come in different shapes and forms, including sex chromosomes (X and Y) that determine the biological sex of an individual. Changes or abnormalities in the number or structure of chromosomes can lead to genetic disorders and diseases.

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

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

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

Cell proliferation is the process by which cells increase in number, typically through the process of cell division. In the context of biology and medicine, it refers to the reproduction of cells that makes up living tissue, allowing growth, maintenance, and repair. It involves several stages including the transition from a phase of quiescence (G0 phase) to an active phase (G1 phase), DNA replication in the S phase, and mitosis or M phase, where the cell divides into two daughter cells.

Abnormal or uncontrolled cell proliferation is a characteristic feature of many diseases, including cancer, where deregulated cell cycle control leads to excessive and unregulated growth of cells, forming tumors that can invade surrounding tissues and metastasize to distant sites in the body.

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

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

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

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

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

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

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

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

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

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

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

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

Adenosine triphosphatases (ATPases) are a group of enzymes that catalyze the conversion of adenosine triphosphate (ATP) into adenosine diphosphate (ADP) and inorganic phosphate. This reaction releases energy, which is used to drive various cellular processes such as muscle contraction, transport of ions across membranes, and synthesis of proteins and nucleic acids.

ATPases are classified into several types based on their structure, function, and mechanism of action. Some examples include:

1. P-type ATPases: These ATPases form a phosphorylated intermediate during the reaction cycle and are involved in the transport of ions across membranes, such as the sodium-potassium pump and calcium pumps.
2. F-type ATPases: These ATPases are found in mitochondria, chloroplasts, and bacteria, and are responsible for generating a proton gradient across the membrane, which is used to synthesize ATP.
3. V-type ATPases: These ATPases are found in vacuolar membranes and endomembranes, and are involved in acidification of intracellular compartments.
4. A-type ATPases: These ATPases are found in the plasma membrane and are involved in various functions such as cell signaling and ion transport.

Overall, ATPases play a crucial role in maintaining the energy balance of cells and regulating various physiological processes.

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

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

A base sequence in the context of molecular biology refers to the specific order of nucleotides in a DNA or RNA molecule. In DNA, these nucleotides are adenine (A), guanine (G), cytosine (C), and thymine (T). In RNA, uracil (U) takes the place of thymine. The base sequence contains genetic information that is transcribed into RNA and ultimately translated into proteins. It is the exact order of these bases that determines the genetic code and thus the function of the DNA or RNA molecule.

Tetrahymena thermophila is not a medical term, but rather it refers to a species of ciliated protozoan that is commonly used in scientific research, including biomedical research. Here's a brief biological definition:

Tetrahymena thermophila is a free-living, freshwater ciliate protozoan found in various aquatic environments. It has a complex cell structure with two types of nuclei (a macronucleus and a micronucleus) and numerous cilia for movement. This organism is known for its ability to reproduce both sexually and asexually, making it a valuable model for studying genetic processes. Its genome has been fully sequenced, and it is widely used in research fields such as molecular biology, cell biology, and genetics due to its ease of cultivation and manipulation.

While not directly related to medical terminology, Tetrahymena thermophila has contributed significantly to our understanding of various biological processes with potential implications for medical research, including gene regulation, protein function, and DNA repair mechanisms.

Protein-Serine-Threonine Kinases (PSTKs) are a type of protein kinase that catalyzes the transfer of a phosphate group from ATP to the hydroxyl side chains of serine or threonine residues on target proteins. This phosphorylation process plays a crucial role in various cellular signaling pathways, including regulation of metabolism, gene expression, cell cycle progression, and apoptosis. PSTKs are involved in many physiological and pathological processes, and their dysregulation has been implicated in several diseases, such as cancer, diabetes, and neurodegenerative disorders.

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

Anoplura is an order of insects that are external parasites, specifically known as sucking lice. They are ectoparasites that live on the skin and hair of mammals, including humans, and feed on their blood. Anoplura species have a specialized mouthpart called a fascicle, which consists of several parts working together to pierce the host's skin and suck blood.

The most common and medically significant example of Anoplura is Pediculus humanus, which includes two subspecies: P. h. capitis (head louse) and P. h. corporis (body louse). These species are obligate parasites that can only survive on human hosts. Infestations with these lice can cause skin irritation, itching, and the transmission of diseases such as typhus and trench fever.

It is important to note that Anoplura species are not to be confused with other types of lice, such as chewing lice (Mallophaga), which primarily feed on dead skin scales and hair rather than blood.

Immunoenzyme techniques are a group of laboratory methods used in immunology and clinical chemistry that combine the specificity of antibody-antigen reactions with the sensitivity and amplification capabilities of enzyme reactions. These techniques are primarily used for the detection, quantitation, or identification of various analytes (such as proteins, hormones, drugs, viruses, or bacteria) in biological samples.

In immunoenzyme techniques, an enzyme is linked to an antibody or antigen, creating a conjugate. This conjugate then interacts with the target analyte in the sample, forming an immune complex. The presence and amount of this immune complex can be visualized or measured by detecting the enzymatic activity associated with it.

There are several types of immunoenzyme techniques, including:

1. Enzyme-linked Immunosorbent Assay (ELISA): A widely used method for detecting and quantifying various analytes in a sample. In ELISA, an enzyme is attached to either the capture antibody or the detection antibody. After the immune complex formation, a substrate is added that reacts with the enzyme, producing a colored product that can be measured spectrophotometrically.
2. Immunoblotting (Western blot): A method used for detecting specific proteins in a complex mixture, such as a protein extract from cells or tissues. In this technique, proteins are separated by gel electrophoresis and transferred to a membrane, where they are probed with an enzyme-conjugated antibody directed against the target protein.
3. Immunohistochemistry (IHC): A method used for detecting specific antigens in tissue sections or cells. In IHC, an enzyme-conjugated primary or secondary antibody is applied to the sample, and the presence of the antigen is visualized using a chromogenic substrate that produces a colored product at the site of the antigen-antibody interaction.
4. Immunofluorescence (IF): A method used for detecting specific antigens in cells or tissues by employing fluorophore-conjugated antibodies. The presence of the antigen is visualized using a fluorescence microscope.
5. Enzyme-linked immunosorbent assay (ELISA): A method used for detecting and quantifying specific antigens or antibodies in liquid samples, such as serum or culture supernatants. In ELISA, an enzyme-conjugated detection antibody is added after the immune complex formation, and a substrate is added that reacts with the enzyme to produce a colored product that can be measured spectrophotometrically.

These techniques are widely used in research and diagnostic laboratories for various applications, including protein characterization, disease diagnosis, and monitoring treatment responses.

Cyclin-dependent kinases (CDKs) are a family of serine/threonine protein kinases that play crucial roles in regulating the cell cycle, transcription, and other cellular processes. They are activated by binding to cyclin proteins, which accumulate and degrade at specific stages of the cell cycle. The activation of CDKs leads to phosphorylation of various downstream target proteins, resulting in the promotion or inhibition of different cell cycle events. Dysregulation of CDKs has been implicated in several human diseases, including cancer, and they are considered important targets for drug development.

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

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

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

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

Artificial chromosomes are human-made DNA structures that contain genetic material and can behave like natural chromosomes in cells. They are created in a laboratory and can be used for various research purposes, including studying gene function and developing new gene therapy techniques. Artificial chromosomes are typically constructed by combining specific DNA sequences that are necessary for replication, segregation, and stability within the cell. These synthetic chromosomes do not exist in nature and are not naturally occurring in humans or any other organisms.

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

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

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

Micrococcal Nuclease is a type of extracellular endonuclease enzyme that is produced by certain species of bacteria, including Micrococcus and Staphylococcus. This enzyme is capable of cleaving double-stranded DNA into smaller fragments, particularly at sites with exposed phosphate groups on the sugar-phosphate backbone.

Micrococcal Nuclease has a preference for cleaving DNA at regions rich in adenine and thymine (A-T) bases, and it can also degrade RNA. It is often used in molecular biology research as a tool to digest and remove unwanted nucleic acids from samples, such as during the preparation of plasmid DNA or chromatin for further analysis.

The enzyme has an optimum temperature of around 37°C and requires calcium ions for its activity. It is also relatively resistant to denaturation by heat, detergents, and organic solvents, making it a useful reagent in various biochemical and molecular biology applications.

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

The Western blotting procedure involves several steps:

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

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

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

Deoxyribonucleoproteins are complexes formed by the association of DNA (deoxyribonucleic acid) with proteins. These complexes play a crucial role in various cellular processes, including the packaging and protection of DNA within the cell, as well as the regulation of gene expression.

In particular, deoxyribonucleoproteins are important components of chromatin, which is the material that makes up chromosomes. Histone proteins are among the most abundant proteins found in chromatin, and they play a key role in compacting DNA into a more condensed form. Other non-histone proteins also associate with DNA to regulate various cellular processes, such as transcription, replication, and repair.

Deoxyribonucleoproteins can also be found in viruses, where they are often referred to as nucleocapsids. In these cases, the deoxyribonucleoprotein complex serves to protect the viral genome and facilitate its replication and transmission between host cells.

Prognosis is a medical term that refers to the prediction of the likely outcome or course of a disease, including the chances of recovery or recurrence, based on the patient's symptoms, medical history, physical examination, and diagnostic tests. It is an important aspect of clinical decision-making and patient communication, as it helps doctors and patients make informed decisions about treatment options, set realistic expectations, and plan for future care.

Prognosis can be expressed in various ways, such as percentages, categories (e.g., good, fair, poor), or survival rates, depending on the nature of the disease and the available evidence. However, it is important to note that prognosis is not an exact science and may vary depending on individual factors, such as age, overall health status, and response to treatment. Therefore, it should be used as a guide rather than a definitive forecast.

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

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

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

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

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

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

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

Simian Virus 40 (SV40) is a polyomavirus that is found in both monkeys and humans. It is a DNA virus that has been extensively studied in laboratory settings due to its ability to transform cells and cause tumors in animals. In fact, SV40 was discovered as a contaminant of poliovirus vaccines that were prepared using rhesus monkey kidney cells in the 1950s and 1960s.

SV40 is not typically associated with human disease, but there has been some concern that exposure to the virus through contaminated vaccines or other means could increase the risk of certain types of cancer, such as mesothelioma and brain tumors. However, most studies have failed to find a consistent link between SV40 infection and cancer in humans.

The medical community generally agrees that SV40 is not a significant public health threat, but researchers continue to study the virus to better understand its biology and potential impact on human health.

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

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

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

Bacterial chromosomes are typically circular, double-stranded DNA molecules that contain the genetic material of bacteria. Unlike eukaryotic cells, which have their DNA housed within a nucleus, bacterial chromosomes are located in the cytoplasm of the cell, often associated with the bacterial nucleoid.

Bacterial chromosomes can vary in size and structure among different species, but they typically contain all of the genetic information necessary for the survival and reproduction of the organism. They may also contain plasmids, which are smaller circular DNA molecules that can carry additional genes and can be transferred between bacteria through a process called conjugation.

One important feature of bacterial chromosomes is their ability to replicate rapidly, allowing bacteria to divide quickly and reproduce in large numbers. The replication of the bacterial chromosome begins at a specific origin point and proceeds in opposite directions until the entire chromosome has been copied. This process is tightly regulated and coordinated with cell division to ensure that each daughter cell receives a complete copy of the genetic material.

Overall, the study of bacterial chromosomes is an important area of research in microbiology, as understanding their structure and function can provide insights into bacterial genetics, evolution, and pathogenesis.

A telomere is a region of repetitive DNA sequences found at the end of chromosomes, which protects the genetic data from damage and degradation during cell division. Telomeres naturally shorten as cells divide, and when they become too short, the cell can no longer divide and becomes senescent or dies. This natural process is associated with aging and various age-related diseases. The length of telomeres can also be influenced by various genetic and environmental factors, including stress, diet, and lifestyle.

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

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

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

In the context of medicine, "maintenance" generally refers to the ongoing care or support required to maintain or prevent the deterioration of a person's health, particularly in chronic conditions or disabilities. This may include:

1. Medical treatment: Regular administration of medications, therapies, or procedures to manage a medical condition and prevent complications.
2. Rehabilitation: Continuous support and guidance to help individuals with disabilities or injuries regain their functional abilities and maintain their independence.
3. Preventive care: Routine check-ups, screenings, and immunizations to detect potential health issues early and prevent them from becoming more severe.
4. Lifestyle modifications: Encouragement and support for maintaining healthy habits such as regular exercise, balanced diet, stress management, and smoking cessation.
5. Psychological support: Counseling, therapy, or support groups to help patients cope with their medical conditions and maintain their emotional well-being.
6. Case management: Coordination of various healthcare services and resources to ensure that the patient receives comprehensive and continuous care.
7. Home care or residential care: Provision of assistance with activities of daily living (ADLs) and instrumental activities of daily living (IADLs) in the patient's home or a specialized care facility to support their independence and quality of life.

The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (Sep 1996). "Binding of human minichromosome maintenance proteins with histone ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... and Replication protein A1. Mini Chromosome Maintenance GRCh38: Ensembl release 89: ENSG00000073111 - Ensembl, May 2017 GRCm38 ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis". Mol. Cell ... MCM3 has been shown to interact with: CDC45-related protein, CDC6, DBF4, MCM2 MCM3AP, MCM5, MCM7, ORC4L, and ORC5L. Mini ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential ... Kukimoto I, Igaki H, Kanda T (1999). "Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 subunit of ... Kukimoto I, Igaki H, Kanda T (November 1999). "Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 ... Replication protein A1, Retinoblastoma protein, and UBE3A. Mini Chromosome Maintenance GRCh38: Ensembl release 89: ...
... is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (September 1996). "Binding of human minichromosome maintenance proteins with ... Lee JK, Hurwitz J (2001). "Processive DNA helicase activity of the minichromosome maintenance proteins 4, 6, and 7 complex ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential ... Mini Chromosome Maintenance MCM4 has been shown to interact with: Cell division cycle 7-related protein kinase, MCM2, MCM6, ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (September 1996). "Binding of human minichromosome maintenance proteins with ...
Maine, G. T., Sinha, P. & Tye, B. K. Mutants of S. cerevisiae defective in the maintenance of minichromosomes. Genetics 106, ... "MCM Proteins > PombeNet Forsburg Lab > USC Dana and David Dornsife College of Letters, Arts and Sciences". dornsife.usc.edu. ... Tye's pioneering work on eukaryotic DNA replication led to the discovery of the minichromosome maintenance (MCM) genes in 1984 ... Cerevisiae Defective in the Maintenance of Minichromosomes". Genetics. 106 (3): 365-385. doi:10.1093/genetics/106.3.365. ISSN ...
Mini Chromosome Maintenance MCM5 has been shown to interact with: Cell division cycle 7-related protein kinase, MCM2, MCM3, ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... The protein encoded by this gene is structurally very similar to the CDC46 protein from S. cerevisiae, a protein involved in ... "Aberrant expression of minichromosome maintenance proteins 2 and 5, and Ki-67 in dysplastic squamous oesophageal epithelium and ...
These minichromosomes were constructed using the de novo approach. Minichromosome maintenance proteins Microchromosome Y ... Minichromosomes may be created by natural processes as chromosomal aberrations or by genetic engineering. Minichromosomes can ... Minichromosome technology allows for the stacking of genes side-by-side on the same chromosome thus reducing likelihood of ... The use of minichromosomes as a means for generating more desirable crop traits is actively being explored. Major advantages ...
The minichromosome maintenance proteins were named after a yeast genetics screen for mutants defective in the regulation of DNA ... The minichromosome maintenance protein complex (MCM) is a DNA helicase essential for genomic DNA replication. Eukaryotic MCM ... Passmore S, Elble R, Tye BK (July 1989). "A protein involved in minichromosome maintenance in yeast binds a transcriptional ... Neves H, Kwok HF (August 2017). "In sickness and in health: The many roles of the minichromosome maintenance proteins". ...
Kukimoto I, Igaki H, Kanda T (1999). "Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 subunit of ... Kukimoto I, Igaki H, Kanda T (Nov 1999). "Human CDC45 protein binds to minichromosome maintenance 7 protein and the p70 subunit ... Cdc45 is a member of the highly conserved multiprotein complex including Cdc6/Cdc18, the minichromosome maintenance proteins ( ... CDC45 is a protein that in humans is encoded by the CDC45L gene. The protein encoded by this gene was identified by its strong ...
"Human minichromosome maintenance proteins and human origin recognition complex 2 protein on chromatin". J. Biol. Chem. 273 (38 ... and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis". Mol. Cell ... The protein encoded by this gene is a subunit of the ORC complex. This protein forms a core complex with ORC3, ORC4, and ORC5. ... an origin-specific binding protein that associates with replication proteins, is required for mammalian DNA replication". ...
... and Minichromosome Maintenance Proteins during the Cell Cycle: Assembly of Prereplication Complexes in Late Mitosis". Mol. Cell ... Cell division control protein 6 homolog is a protein that in humans is encoded by the CDC6 gene. The protein encoded by this ... and Minichromosome Maintenance Proteins during the Cell Cycle: Assembly of Prereplication Complexes in Late Mitosis". Mol. Cell ... "Protein Phosphatase 2A Is Targeted to Cell Division Control Protein 6 by a Calcium-binding Regulatory Subunit". J. Biol. Chem. ...
The Cdc7/Dbf4 complex adds a phosphate group to the minichromosome maintenance (MCM) protein complex allowing for the ... "CDC7 kinase phosphorylates serine residues adjacent to acidic amino acids in the minichromosome maintenance 2 protein". Proc. ... The protein is expressed at constant levels throughout the cell cycle. The gene coding for the Dbf4 or ASK protein is regulated ... Because the two proteins, Cdc7 and Dbf4, must form a complex before activating the MCM complex, the regulation of one protein ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential ... This protein contains the central domain that is conserved among the MCM proteins. This protein has been shown to co- ... The hexameric protein complex formed by the MCM proteins is a key component of the pre-replication complex (pre_RC) and may be ... Mini Chromosome Maintenance GRCh38: Ensembl release 89: ENSG00000125885 - Ensembl, May 2017 GRCm38: Ensembl release 89: ...
Holland L, Gauthier L, Bell-Rogers P, Yankulov K (2002). "Distinct parts of minichromosome maintenance protein 2 associate with ... 2004). "Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins ... 2000). "Human pre-mRNA cleavage factor IIm contains homologs of yeast proteins and bridges two other cleavage factors". EMBO J ... Takagaki Y, Manley JL (2000). "Complex Protein Interactions within the Human Polyadenylation Machinery Identify a Novel ...
Cdc6 protein, Cdt1 protein, and minichromosome maintenance proteins (Mcm2-7). Once the pre-RC is formed, activation of the ... Minichromosome maintenance proteins are required for DNA helicase activity. Inactivation of any of the six Mcm proteins during ... The nuclear localization of the minichromosome maintenance proteins is regulated in budding yeast cells. The Mcm proteins are ... which indicates that the proteins are released by different mechanisms. The six minichromosome maintenance proteins and Cdc45 ...
CDT1, along with the protein CDC6, are then recruited to the forming pre-RC, followed by minichromosome maintenance complexes ( ... Cook JG, Chasse DA, Nevins JR (2004). "The regulated association of Cdt1 with minichromosome maintenance proteins and Cdc6 in ... The protein encoded by this gene is a key licensing factor in the assembly of pre-replication complexes (pre-RC), which occurs ... Nishitani H, Lygerou Z, Nishimoto T, Nurse P (2000). "The Cdt1 protein is required to license DNA for replication in fission ...
"In vivo interactions of archaeal Cdc6/Orc1 and minichromosome maintenance proteins with the replication origin". Proceedings of ... Once recruited to origins, ORC and its co-factors Cdc6 and Cdt1 drive the deposition of the minichromosome maintenance 2-7 ( ... Since both regions of Orc1/Cdc6 associate with a minichromosome maintenance (MCM) replicative helicase, this specific ... Bell SD (2012). "Archaeal Orc1/Cdc6 Proteins". The Eukaryotic Replisome: A Guide to Protein Structure and Function. Subcellular ...
The minichromosome maintenance protein 3 (MCM3) is one of the MCM proteins essential for the initiation of DNA replication. The ... "Entrez Gene: MCM3AP MCM3 minichromosome maintenance deficient 3 (S. cerevisiae) associated protein". Takei Y, Assenberg M, ... Nakayama M, Kikuno R, Ohara O (2002). "Protein-protein interactions between large proteins: two-hybrid screening using a ... 80 kDa MCM3-associated protein is a protein that in humans is encoded by the MCM3AP gene. ...
1996). "Binding of human minichromosome maintenance proteins with histone H3". J. Biol. Chem. 271 (39): 24115-22. doi:10.1074/ ... Histone H3.1t is a protein that in humans is encoded by the HIST3H3 gene. Histones are basic nuclear proteins that are ... 1998). "Core histones and HIRIP3, a novel histone-binding protein, directly interact with WD repeat protein HIRA". Mol. Cell. ... 1998). "SAP30, a novel protein conserved between human and yeast, is a component of a histone deacetylase complex". Mol. Cell. ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in ... The protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and it may be involved in ... Protein MCM10 homolog is a protein that in humans is encoded by the MCM10 gene. It is essential for activation of the Cdc45: ... This protein can interact with MCM2 and MCM6, as well as with the origin recognition protein ORC2. It is regulated by ...
... and a homohexamer of the minichromosome maintenance (MCM) protein. Sulfolobus islandicus also uses a Cdt1 homologue to ... In most eukaryotes it is composed of six ORC proteins (ORC1-6), Cdc6, Cdt1, and a heterohexamer of the six MCM proteins (MCM2-7 ... There is a stoichiometric excess of the MCM proteins over the ORC and Cdc6 proteins, indicating that there may be multiple MCM ... The ORC4 protein is known to bind the AT-rich portion of the origin of replication in S. pombe using AT hook motifs. The ...
... and the GINs complex to the origin of replication which has been pre-loaded with the minichromosome maintenance (MCM) complex. ... Nakayama M, Kikuno R, Ohara O (November 2002). "Protein-protein interactions between large proteins: two-hybrid screening using ... TOPBP1 was first identified as a DNA damage protein through its association with BRCA1, which is a protein heavily implicated ... The TOPBP1 gene encodes a scaffold protein which facilitates interactions between different proteins at specific times and ...
Su TT; O'Farrell PH (1998). "Chromosome Association of Minichromosome Maintenance Proteins in Drosophila Endoreplication Cycles ... It has been suggested that increased gene copy number might allow for the mass production of proteins required to meet the ... Recent work suggests that observed oscillations in E2F and cyclin E protein levels result from a negative-feedback loop ... This result suggests that endoreplication and polyploidy may be required for the maintenance of cell identity. Endoreplication ...
In methanogenic archaea of the order Methanococcales, the cellular minichromosome maintenance (MCM) helicase has apparently ... For most archaeal virus families, however, a significant minority of viral proteins are homologous to proteins found in archaea ... Archaeal viruses also encode many proteins that modulate specific stages of virus-host interaction, including proteins that ... of encoded proteins are homologous to proteins found in cellular life or other viruses. In total, the functions of about 85% of ...
In eukaryotes, helicase function is provided by the MCM (Minichromosome maintenance) complex. The DnaB helicase is the product ... The DnaC protein, another AAA+ ATPase, then loads the DnaB protein onto the separated DNA strands in the denatured region. A ... The crucial component in the initiation process is the DnaA protein, a member of the AAA+ ATPase protein family (ATPases ... Eight DnaA protein molecules, all in the ATP-bound state, assemble to form a helical complex encompassing the R and I sites in ...
... also interacts with MCM7 (mini chromosome maintenance complex component 7), part of a protein complex that functions in ... proteins can bind to modify the protein's function. SUMO proteins may modify proteins to perform many functions, including ... including zinc-finger proteins. C8orf34 protein undergoes few modifications following translation. C8orf34 protein is not ... The nearest protein-encoding gene to C8orf34 is PREX2, a guanine-nucleotide exchange factor for the Rac family of G proteins. ...
... is able to form a stable minichromosome in the nucleus of cells that are infected with a particular virus associated ... As part of the nucleus, cccDNA is able to interact with histone and non-histone proteins to form structures similar to ... Allweiss, Lena; Dandri, Maura (June 21, 2017). "The Role of cccDNA in HBV Maintenance". Viruses. 9 (6): 156. doi:10.3390/ ... The cccDNA of viruses is also known as episomal DNA or occasionally as a minichromosome. cccDNA was first described in ...
Cdt1 binding and the ATPase activity of ORC and Cdc6 facilitate the loading of the minichromosome maintenance (MCM) proteins 2- ... Replication initiation proteins are overexpressed in tissue samples from several types of human cancers and experimental ... The identification and characterization of the ORC, Cdc6, Cdt1, and the MCM complex proteins as the licensing factor gives ... CDK-dependent phosphorylation of the MCM2-7 proteins results in the complex's export from the nucleus. (Cdt1 which associates ...
General protein information Go to the top of the page Help Preferred Names. DNA helicase MCM8. Names. DNA replication licensing ... Mcm8 minichromosome maintenance 8 homologous recombination repair factor [Mus mu... Mcm8 minichromosome maintenance 8 ... minichromosome maintenance 8 homologous recombination repair factorprovided by MGI. Primary source. MGI:MGI:1913884 See related ... Mcm8 minichromosome maintenance 8 homologous recombination repair factor [ Mus musculus (house mouse) ] Gene ID: 66634, updated ...
The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (Sep 1996). "Binding of human minichromosome maintenance proteins with histone ... Ishimi Y, Ichinose S, Omori A, Sato K, Kimura H (1996). "Binding of human minichromosome maintenance proteins with histone H3 ... and Replication protein A1. Mini Chromosome Maintenance GRCh38: Ensembl release 89: ENSG00000073111 - Ensembl, May 2017 GRCm38 ...
MCM6: minichromosome maintenance complex component 6. *MCOLN1: mucolipin TRP cation channel 1 ... MPV17: mitochondrial inner membrane protein MPV17. *MPZ: myelin protein zero. *MRAP: melanocortin 2 receptor accessory protein ... MPLKIP: M-phase specific PLK1 interacting protein. * ... MKRN3: makorin ring finger protein 3. *MLC1: modulator of VRAC ...
... which increases the maintenance of genomic stability and counteracts … ... MCM2 protein, human * MCM7 protein, human * Minichromosome Maintenance Complex Component 2 * Minichromosome Maintenance Complex ... Proteins involved in the ATM-and-Rad3-related kinase (ATR)-dependent S-phase checkpoint response (Chk1 and Rad17) were also ... Cell cycle progression, phosphorylation, and DNA binding of cell cycle checkpoint proteins were analyzed. ...
Comparative protein profiling reveals minichromosome maintenance (MCM) proteins as novel potential tumor markers for ... 1, 2, 3, 4, 5, 6] From 2004 to 2010, there were 7,148 newly diagnosed cases of spinal meningioma (age adjusted incidence, 0.33/ ... 12] Calcifications are rarely visible on plain radiographs (1-5%) and usually psammomatous in nature. On plain images, the ... and cancerous meningiomas constitute approximately 1% of all primary brain tumors. An estimated 31,990 people will be diagnosed ...
Comparative protein profiling reveals minichromosome maintenance (MCM) proteins as novel potential tumor markers for ... 1, 2, 3, 4, 5, 6] From 2004 to 2010, there were 7,148 newly diagnosed cases of spinal meningioma (age adjusted incidence, 0.33/ ... 12] Calcifications are rarely visible on plain radiographs (1-5%) and usually psammomatous in nature. On plain images, the ... and cancerous meningiomas constitute approximately 1% of all primary brain tumors. An estimated 31,990 people will be diagnosed ...
... in minichromosome maintenance-deficient 4 (MCM4) that was predicted to result in a severely truncated protein (p.Pro24ArgfsX4 ... Human cytomegalovirus protein pUL117 targets the mini-chromosome maintenance complex and suppresses cellular DNA synthesis. ... encoding minichromosome maintenance complex component 4. These reports suggest a critical role for the minichromosome ... These proteins were also detected in control cells, albeit in much smaller amounts than the full-length protein. Stable ...
Triton X-100 to remove cytosolic and nucleosic proteins but retain the chromatin-bound proteins. Then cells were fixed with 4% ... MicroRNA-31 suppresses medulloblastoma cell growth by inhibiting DNA replication through minichromosome maintenance 2. ... Our results indicate that miR-31 also suppresses tumor initiation by targeting minichromosome maintenance complex component 2 ( ... 30 μg proteins were separated by 12% SDS-polyacrylamide gels. Anti-rabbit MCM2 antibody (Epitomics) and anti-GAPDH (Kangchen) ...
Minichromosome Maintenance Complex Component 2), which are also implicated in the regulation of cell cycle, were examined both ... Bcl-2-associated X protein (BAX) (F: 5′- TGC​AGA​GGA​TGA​TTG​CCG​CCG-3′ R: 5′-ACC​CAA​CCA​CCC​TGG​TGT​TGG-3′), Tyrosine-protein ... For example, HCT116 cells express wild-type forms of the BRAF and p53 genes, whereas both genes encode mutant protein forms ... Kale, J., Osterlund, E. J., and Andrews, D. W. (2018). BCL-2 family proteins: Changing partners in the dance towards death. ...
Immunohistochemical expression of minichromosome maintenance complex protein 2 predicts biochemical recurrence in prostate ...
Expression of MCM proteins in human esophageal biopsies. (A) Expression of minichromosome maintenance (MCM) transcripts and ... Minichromosome maintenance (MCM) complex proteins represent the double-strand break repair term (indicated with the blue arrow ... Digestion of proteins. To digest proteins, 20 μg of each sample (protein mass) was resuspended in 100 μL of 6 M urea and 50 mM ... The minichromosome maintenance complex drives esophageal basal zone hyperplasia. Mark Rochman,1 Yrina Rochman,1 Julie M. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
MCM1 Protein. Minichromosome Maintenance 1 Protein. D13 - Nucleic Acids, Nucleotides, and Nucleosides. RNA, Long Untranslated. ...
Vis forfatter(e) (2009). Biochemical characterization of the minichromosome maintenance protein from the archaeon Thermoplasma ... Vis forfatter(e) (2006). Stimulation of MCM helicase activity by a Cdc6 protein in the archaeon Thermoplasma acidophilum. ... Vis forfatter(e) (2008). Functional analysis of the MCM and Cdc6 proteins from the thermoacidophilic euryarchaeon Thermoplasma ... Vis forfatter(e) (2008). Regulation of DNA replication in Archaea; Functional analysis of DNA replication initiation proteins ...
... minichromosome maintenance complex component 2; CDK1: cyclin dependent kinase 1; DDR: DNA damage respire; ATM: ataxia- ... Protein Cell. 2013;4:331-41 28. Malek R, Gajula RP, Williams RD, Nghiem B, Simons BW, Nugent K. et al. TWIST1-WDR5-Hottip ... Polypyrimidine tract binding protein 1 promotes lymphatic metastasis and proliferation of bladder cancer via alternative ... Western blotting showing that knockdown WDR5 (H) or OICR-9429 (I) reduced protein level of IFNγ-induced PD-L1 in DU145 and PC-3 ...
... as an essential protein for proper differentiation, and, unexpectedly, for the maintenance of pluripotency in ESCs. In ... yet the role of the major heterochromatin proteins in pluripotency is unknown. Here we identify Heterochromatin Protein 1β (HP1 ... However, in differentiated cells, loss of HP1β has the opposite effect, perturbing maintenance of the differentiation state and ... Recently, several chromatin-related proteins have been shown to regulate ESC pluripotency and/or differentiation, ...
2002) Distinct parts of minichromosome maintenance protein 2 associate with histone H3/H4 and RNA polymerase II holoenzyme. Eur ... Bell SD and Botchan MR (2013) The minichromosome maintenance replicative helicase. Cold Spring Harb Perspect Biol 5(11):a012807 ... Dalton S and Hopwood B (1997) Characterization of Cdc47p-minichromosome maintenance complexes in Saccharomyces cerevisiae: ... 2012) Interactions of the human MCM-BP protein with MCM complex components and Dbf4. PLoS One 7(4):e35931 PMID: 22540012 *SGD ...
Down-regulation of CK2α correlates with decreased expression levels of DNA replication minichromosome maintenance protein ... DeepCLIP: predicting the effect of mutations on protein-RNA binding with deep learning. Grønning, A. G. B., Doktor, T. K., ... The ETFDH c.158A,G Variation Disrupts the Balanced Interplay of ESE- and ESS-Binding Proteins thereby Causing Missplicing and ... Madelung, M., Kronborg, T., Doktor, T. K., Struve, C., Krogfelt, K. A. & Møller-Jensen, J., 2017, I: BMC Microbiology. 17, 1, ...
DDK: The Outsourced Kinase of Chromosome Maintenance. Gillespie, P. J. & Blow, J. J., 7 Jun 2022, In: Biology. 11, 6, 19 p., ... Xenopus Cdc7 executes its essential function early in S phase and is counteracted by checkpoint-regulated protein phosphatase 1 ... 1, p. 1-11 11 p., 3704.. Research output: Contribution to journal › Article › peer-review ...
... minichromosome maintenance complex component-7) platform that naturally harbors 3 microRNAs (miRNAs). We replaced the ... Finally, anti-HIV RNA decoys that aim to titrate out early essential viral replication proteins Tat and Rev are constructed. We ... Here we explore combinations of different classes of therapeutic anti-HIV-1 RNAs expressed from within the context of an ... Endogenous MCM7 MicroRNA Cluster as a Novel Platform to Multiplex Small Interfering and Nucleolar RNAs for Combinational HIV-1 ...
Diagnosis of bladder cancer by immunocytochemical detection of minichromosome maintenance protein-2 in cells retrieved from ... 2023 May 31;9(1):37. doi: 10.1186/s40900-023-00440-7. Res Involv Engagem. 2023. PMID: 37259130 Free PMC article. Review. ... 2012 Jan-Feb;12(1):8-15. doi: 10.1016/j.pan.2011.12.009. Epub 2011 Dec 31. Pancreatology. 2012. PMID: 22487467 ...
Match: mcm3ap (minichromosome maintenance complex component 3 associated protein [Source:ZFIN;Acc:ZDB-GENE-040715-1]). HSP 1 ... minichromosome maintenance complex component 3 ass... [more]. mcm3ap. 6.592e-9. 24.07. minichromosome maintenance complex ... Match: mcm3ap (minichromosome maintenance complex component 3 associated protein [Source:ZFIN;Acc:ZDB-GENE-040715-1]). HSP 1 ... Match: mcm3ap (minichromosome maintenance complex component 3 associated protein [Source:ZFIN;Acc:ZDB-GENE-040715-1]). HSP 1 ...
Comparative protein profiling reveals minichromosome maintenance (MCM) proteins as novel potential tumor markers for ... 1, 2, 3, 4, 5] From 2004 to 2010, there were 7,148 newly diagnosed cases of spinal meningioma (age adjusted incidence, 0.33/ ... Calcifications are rarely visible on plain radiographs (1-5%) and usually psammomatous in nature. ...
Comparative protein profiling reveals minichromosome maintenance (MCM) proteins as novel potential tumor markers for ... 1, 2, 3, 4, 5] From 2004 to 2010, there were 7,148 newly diagnosed cases of spinal meningioma (age adjusted incidence, 0.33/ ... Calcifications are rarely visible on plain radiographs (1-5%) and usually psammomatous in nature. ...
  • MCM6 , or minichromosome maintenance deficient 6 gene is one of the highly conserved MCMs that are essential for the initiation of eukaryotic genome replication. (bionity.com)
  • Entrez Gene: MCM6 minichromosome maintenance deficient 6 homolog (S. cerevisiae). (bionity.com)
  • 0.6 in both sample sets: claudin 1 (0.75), minichromosome maintenance deficient 5 (0.71) and 7 (0.64), cell division cycle 6 homologue (0.71), antigen identified by monoclonal antibody Ki-67 (0.66), and SHC SH2-domain binding protein 1 (0.61). (nih.gov)
  • The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. (wikipedia.org)
  • mini chromosome maintenance. (nih.gov)
  • The protein encoded by this gene is a member of the mini-chromosome maintenance (MCM) protein family that are essential for the initiation of eukaryotic genome replication. (utsouthwestern.edu)
  • The MCM complex consisting of this protein and MCM2, 4 and 6 proteins possesses DNA helicase activity, and may act as a DNA unwinding enzyme.The protein encoded by this gene is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. (thermofisher.com)
  • Accurate chromosome segregation during mitosis requires the assembly of centromeric DNA and proteins to form the kinetochore, which couples chromosome movement to dynamic spindle microtubules. (rupress.org)
  • MORF4-related gene-binding protein (MRGBP), which is also known as chromosome 20 open reading frame 20 (C20orf20), is commonly highly expressed in several types of malignant tumors and tumor progression. (oncotarget.com)
  • Cyclin D1-dependent kinase, CDK4, is found to associate with this protein, and may regulate the binding of this protein with the tumorsuppressor protein RB1/RB. (thermofisher.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Death Associated Protein Kinase 1 (DAPK1) in Tissue homogenates, cell lysates and other biological fluids. (kits-elisa.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Death Associated Protein Kinase 1 (DAPK1) in samples from Tissue homogenates, cell lysates and other biological fluids with no significant corss-reactivity with analogues from other species. (kits-elisa.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Mouse Death Associated Protein Kinase 1 (DAPK1) in samples from tissue homogenates or other biological fluids. (kits-elisa.com)
  • death associated protein kinase 2 [So. (gsea-msigdb.org)
  • DNA replication licensing factor MCM2 is a protein that in humans is encoded by the MCM2 gene. (wikipedia.org)
  • The minichromosome maintenance (MCM) gene family comprises of ten members with key roles in eukaryotic DNA replication and are associated with the occurrence and progression of many tumors. (nih.gov)
  • What does this gene/protein do? (cancerindex.org)
  • Pollination inaugurates global changes in gene expression pattern that leads to sepal and petal abscission [ 1 ]. (biomedcentral.com)
  • The protein encoded by this gene is secreted and likely acts as an inhibitor of bone formation. (antikoerper-online.de)
  • Characterization of rco-1 of Neurospora crassa, a pleiotropic gene affecting growth and development that encodes a homolog of Tup1 of Saccharomyces cerevisiae. (tamu.edu)
  • Binding to co-regulatory proteins, such as chromatin remodeling and histone modifying enzymes, occurs through one or more transactivation domains (TADs, also called activation domains) present in TFs ( 1 , 2 ). (frontiersin.org)
  • Here, we report that JMJD5, a Jumonji C (JmjC) domain-containing protein, is a Cathepsin L-type protease that mediates histone H3 N-tail proteolytic cleavage under stress conditions that cause a DNA damage response. (cusabio.com)
  • Chromosomal Proteins, Non-Histone" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (umassmed.edu)
  • Below are the most recent publications written about "Chromosomal Proteins, Non-Histone" by people in Profiles. (umassmed.edu)
  • 1997). "HsMCM6: a new member of the human MCM/P1 family encodes a protein homologous to fission yeast Mis5. (bionity.com)
  • This antibody is purified through a protein A column, followed by peptide affinity purification. (antibodies-online.cn)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Hydrogen Voltage Gated Channel Protein 1 (HVCN1) in Tissue homogenates and other biological fluids. (lipidx.org)
  • Then primary antibody (1% BSA) was incubated at 4°C overnight. (cusabio.com)
  • Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Hemoglobin Alpha 1 (HBa1) in samples from serum, plasma, erythrocyte lysates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species. (therabio.org)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Interleukin 1 Receptor Type II (IL1R2) in serum, plasma, tissue homogenates and other biological fluids. (agctsequencing.com)
  • This protein forms a complex with MCM4, 6, and 7, and has been shown to regulate the helicase activity of the complex. (wikipedia.org)
  • The MCM complex consisting of this protein and MCM2, 4 and 7 possesses DNA helicase activity, and may act as a DNA unwinding enzyme . (bionity.com)
  • A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex. (bionity.com)
  • Binding of this protein to chromatin has been shown to be a pre-requisite for recruiting the MCM2-7 helicase to DNA replication origins. (utsouthwestern.edu)
  • MCM6 produces, by alternative splicing, 3 different transcripts, all with introns, putatively encoding 3 different protein isoforms. (bionity.com)
  • 1998). "Human protein MCM6 on HeLa cell chromatin. (bionity.com)
  • This protein can interact with MCM2 and MCM6, as well as with the origin recognition protein ORC2. (utsouthwestern.edu)
  • Proteins obtained from the species SACCHAROMYCES CEREVISIAE. (musc.edu)
  • Below are the most recent publications written about "Saccharomyces cerevisiae Proteins" by people in Profiles. (musc.edu)
  • Several of the Mcm subunit DNA-binding loops, such as the oligosaccharide-oligonucleotide loops, helix 2 insertion loops, and presensor 1 (PS1) loops, are well defined, and many of them interact extensively with the DNA. (nih.gov)
  • Mediator, a large modular protein complex with varying subunit composition, bridges TFs with Pol II and coordinates DNA-loop formation, transcriptional initiation, and post-initiation events ( 3 , 4 ). (frontiersin.org)
  • Proteins were enzymatically digested into peptides which were measured by high-resolution mass spectrometry and analyzed by "all-or-nothing" analysis, Bonferroni, and Benjamini-Hochberg correction for multiple testing. (oncotarget.com)
  • By comparing LCM cell type preparations, 31 proteins were exclusively found in early stage cervical cancer ( n = 11) when compared with healthy epithelium and stroma, based on criteria that address specificity in a restrictive "all-or-nothing" way. (oncotarget.com)
  • It contains a 56 amino acid MADS-box domain within the N-terminal of the protein and is one of the four founder proteins that structurally define the superfamily of MADS DOMAIN PROTEINS . (nih.gov)
  • This protein also binds, and is a positive regulator of, the chromatin licensing and DNA replication factor 1, CDT1. (utsouthwestern.edu)
  • Moreover, we show for the first time that the STAT1 C-terminal TAD is required for an efficient recruitment of components of the core Mediator complex to the IFN regulatory factor ( Irf ) 1 and Irf8 promoters, which both harbor an open chromatin state under basal conditions. (frontiersin.org)
  • Inner nuclear protein Matrin-3 coordinates cell differentiation by stabilizing chromatin architecture. (umassmed.edu)
  • Studies of a similar protein in Xenopus suggest that the chromatin binding of this protein at the onset of DNA replication is after pre-RC assembly and before origin unwinding. (utsouthwestern.edu)
  • 15. Differential expression of microtubule-associated protein 2 in melanocytic skin lesions. (nih.gov)
  • Hepatitis B virus X protein-induced aberrant epigenetic modifications contributing to human hepatocellular carcinoma pathogenesis. (tamu.edu)
  • The hexameric protein complex formed by MCM proteins is a key component of the pre-replication complex (pre-RC) and may be involved in the formation of replication forks and in the recruitment of other DNA replication-related proteins. (wikipedia.org)
  • Mutational analysis of minichromosome maintenance complex component (MCM) family genes in Chinese Han women with polycystic ovarian syndrome. (amedeo.com)
  • Minichromosome Maintenance Complex Component 4" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (uchicago.edu)
  • A minichromosome maintenance protein that is a key component of the six member MCM protein complex. (uchicago.edu)
  • This graph shows the total number of publications written about "Minichromosome Maintenance Complex Component 4" by people in this website by year, and whether "Minichromosome Maintenance Complex Component 4" was a major or minor topic of these publications. (uchicago.edu)
  • Below are the most recent publications written about "Minichromosome Maintenance Complex Component 4" by people in Profiles. (uchicago.edu)
  • DNA repair proteins that include the bacterial MutL protein and its eukaryotic homologs. (nih.gov)
  • Understanding their complex cell architecture and life cycle is challenging because, as with most eukaryotic microbes, ~50% of genome-encoded proteins have completely unknown functions. (nature.com)
  • Moreover, the flagellum is also a widely conserved organelle in eukaryotes and a defining feature of the last eukaryotic common ancestor 9 , but not yet analysed by genome-wide protein localization mapping using microscopy. (nature.com)
  • E.coli-derived human MCM7 recombinant protein (Position: D526-V719). (thermofisher.com)
  • The protein comprises two domains: a MADS-box (residues 1-58) and a MEF2S domain (residues 59-73). (nih.gov)
  • Minichromosome maintenance proteins (Mcm2-7) form a hexameric complex that unwinds DNA ahead of a replicative fork. (nih.gov)
  • The structure of the MEF2S domain is entirely different from that of the equivalent SAM domain in SRF and MCM1, accounting for the absence of cross-reactivity with other proteins that interact with these transcription factors. (nih.gov)
  • These proteins also appear to be simpler versions of those found in eukaryotes. (york.ac.uk)
  • A DNA-binding protein and AAA ATPase that consists of 5 polypeptides and plays an essential role in DNA REPLICATION in eukaryotes. (ucdenver.edu)
  • 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. (musc.edu)
  • A novel human Mcm protein: homology to the yeast replication protein Mis5 and chromosomal location. (bionity.com)
  • A sequence-specific DNA-binding protein that plays an essential role as a global regulator of yeast cell cycle control. (nih.gov)
  • The ceramide activated protein phosphatase Sit4 impairs sphingolipid dynamics, mitochondrial function and lifespan in a yeast model of Niemann-Pick type C1. (musc.edu)
  • Protein tyrosine phosphatase-PEST and 8 integrin regulate spatiotemporal patterns of RhoGDI1 activation in migrating cells. (tamu.edu)
  • Protein tyrosine phosphatase-like A regulates myoblast proliferation and differentiation through MyoG and the cell cycling signaling pathway. (tamu.edu)
  • The solution structure of the 33 kDa complex between the dimeric DNA-binding core domain of the transcription factor MEF2A (residues 1-85) and a 20mer DNA oligonucleotide comprising the consensus sequence CTA(A/T)(4)TAG has been solved by NMR. (nih.gov)
  • adaptor related protein complex 2 subun. (gsea-msigdb.org)
  • Description: A sandwich ELISA kit for detection of Hydrogen Voltage Gated Channel Protein 1 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lipidx.org)
  • Description: A competitive ELISA for quantitative measurement of Human Voltage gated hydrogen channel 1(HVCN1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (lipidx.org)
  • Description: A competitive ELISA for quantitative measurement of Rat Cysteine and glycine rich protein 1(CSRP1) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (jemsec.com)
  • Description: A sandwich quantitative ELISA assay kit for detection of Rat Kallikrein 1 (KLK1) in samples from serum, plasma, tissue homogenates or other biological fluids. (tuberculosistest.net)
  • Description: Quantitativesandwich ELISA kit for measuring Mouse Kallikrein-1 (KLK1) in samples from serum, plasma, tissue homogenates. (tuberculosistest.net)
  • translocated to, 1) as well as HACE1 (HECT Domain And Ankyrin Repeat Containing E3 Ubiquitin Protein Ligase 1), WWP1 (WW Domain Containing E3 Ubiquitin Protein Ligase 1), 14 HMGN1 )High Mobility Group Nucleosome Binding Domain 1), PLAU (plasminogen activator, urokinase), and PSAP (prosaposin). (pharmamodels.net)
  • These complexes function in DNA repair pathways, primarily DNA MISMATCH REPAIR , where MutL/MLH1 and the MUTS DNA MISMATCH-BINDING PROTEIN are targeted to damaged DNA . (nih.gov)
  • Tumor Suppressor p53-Binding Protein 1" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
  • Below are the most recent publications written about "Tumor Suppressor p53-Binding Protein 1" by people in Profiles. (jefferson.edu)
  • complement C1q binding protein [Sourc. (gsea-msigdb.org)
  • However, such localization attributions are limited by the accuracy of organelle purification or fractionation, and sensitivity is limited by protein abundance and characteristics. (nature.com)
  • The expression of TIP30, cell cycle proteins, migration-related proteins, and cell apoptosis-related proteins was assessed by Western blotting. (cancerindex.org)
  • cell cycle progression 1 [Source:HGNC S. (gsea-msigdb.org)
  • It may also function in M PHASE CELL CYCLE CHECKPOINTS and as an enhancer of TUMOR SUPPRESSOR PROTEIN P53-mediated transcriptional activation. (jefferson.edu)
  • Knockdown of MRGBP in the PDAC cell lines ASPC-1 and Mia PaCa-2 by transiently transfected with small interfering RNA (siRNA) drastically attenuated the proliferation, migration, and invasion of those cells, whereas ectopic MRGBP overexpression in BxPC-3 cells produced exactly the opposite effect. (oncotarget.com)
  • Here, using fluorescence microscopy and cell lines expressing endogenously tagged proteins, we mapped the subcellular localization of 89% of the T. brucei proteome, a resource we call TrypTag. (nature.com)
  • Protein localization offers insights into organelle subdomains/dynamics and cell-cycle-dependent localization changes. (nature.com)
  • cell adhesion molecule 1 [Source:HGNC. (gsea-msigdb.org)
  • Ascribing subcellular localization of proteins assists understanding function and has largely been addressed through 'omic' approaches, such as proteomics of purified organelles and hyperplexed organelle localizations by isotope tagging 1 . (nature.com)
  • From proteins to proteomics and beyond. (csie.org)
  • Tat-interacting protein 30 (TIP30), a transcriptional repressor, possesses antitumor effect in different cancer cells. (cancerindex.org)
  • 16. Proto-oncogene c-kit expression in malignant melanoma: protein loss with tumor progression. (nih.gov)
  • 19. Loss of claudin-1 expression in tumor-associated vessels correlates with acquisition of metastatic phenotype in melanocytic neoplasms. (nih.gov)
  • A nuclear and cytoplasmic protein that associates with KINETOCHORES and contains a C-terminal TUDOR DOMAIN. (jefferson.edu)
  • 1 Laboratory of Chemical Physics, Building 5, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0510, USA. (nih.gov)