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Hsp70
The 70 kilodalton heat shock proteins (Hsp70s or DnaK) are a family of conserved ubiquitously expressed heat shock proteins. Proteins with similar structure exist in virtually all living organisms. Intracellularly localized Hsp70s are an important part of the cell's machinery for protein folding, performing chaperoning functions, and helping to protect cells from the adverse effects of physiological stresses. Additionally, membrane-bound Hsp70s have been identified as a potential target for cancer therapies and their extracellularly localized counterparts have been identified as having both membrane-bound and membrane-free structures. Discovery Members of the Hsp70 family are very strongly upregulated by heat stress and toxic chemicals, particularly heavy metals such as arsenic, cadmium, copper, mercury, etc. Heat shock was originally discovered by Ferruccio Ritossa in the 1960s when a lab worker accidentally boosted the incubation temperature of Drosophila (fruit flies). W ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
HSPBP1
Hsp70-binding protein 1 is a protein that in humans is encoded by the ''HSPBP1'' gene. Interactions HSPBP1 has been shown to interact Advocates for Informed Choice, doing business as, dba interACT or interACT Advocates for Intersex Youth, is a 501(c)(3) nonprofit organization using innovative strategies to advocate for the legal and human rights of children with intersex trai ... with HSPA8 and HSPA4. References Further reading * * * * * * * * * * * * * * {{gene-19-stub Armadillo-repeat-containing proteins ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Heat Shock Protein
Heat shock proteins (HSP) are a family of proteins produced by cells in response to exposure to stressful conditions. They were first described in relation to heat shock, but are now known to also be expressed during other stresses including exposure to cold, UV light and during wound healing or tissue remodeling. Many members of this group perform chaperone functions by stabilizing new proteins to ensure correct folding or by helping to refold proteins that were damaged by the cell stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans. Heat-shock proteins are named according to their molecular weight. For example, Hsp60, Hsp70 and Hsp90 (the most widely studied HSPs) refer to families of heat shock proteins on the order of 60, 70 and 90 kilodal ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Hsp40
In molecular biology, chaperone DnaJ, also known as Hsp40 (heat shock protein 40 kD), is a molecular chaperone protein. It is expressed in a wide variety of organisms from bacteria to humans. Function Molecular chaperones are a diverse family of proteins that function to protect proteins from irreversible aggregation during synthesis and in times of cellular stress. The bacterial molecular chaperone DnaK is an enzyme that couples cycles of ATP binding, hydrolysis, and ADP release by an N-terminal ATP-hydrolyzing domain to cycles of sequestration and release of unfolded proteins by a C-terminal substrate binding domain. Dimeric GrpE is the co-chaperone for DnaK, and acts as a nucleotide exchange factor, stimulating the rate of ADP release 5000-fold. DnaK is itself a weak ATPase; ATP hydrolysis by DnaK is stimulated by its interaction with another co-chaperone, DnaJ. Thus the co-chaperones DnaJ and GrpE are capable of tightly regulating the nucleotide-bound and substrate-bound st ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
BAG1
BAG family molecular chaperone regulator 1 is a protein that in humans is encoded by the ''BAG1'' gene. Function The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. At least three protein isoforms are encoded by this mRNA through the use of alternative translation initiation sites, including a non- AUG site. Clinical significance BAG gene has been implicated in age related neurodegenerative diseases as Alzheimer's. It has been demonstrated that BAG1 and BAG 3 regulate the proteasomal and lysosomal protein elimination pathways, respectively. * Interactions BAG1 has been shown to interact with: * Androgen receptor, * C-Raf, * Calcitriol receptor, * Glucocorticoid receptor, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
GrpE
GrpE (''Gro-P'' like protein E) is a bacterial nucleotide exchange factor that is important for regulation of protein folding machinery, as well as the heat shock response. It is a heat-inducible protein and during stress it prevents unfolded proteins from accumulating in the cytoplasm. Accumulation of unfolded proteins in the cytoplasm can lead to cell death. Discovery GrpE is a nucleotide exchange factor that was first discovered by researchers in 1977 as a protein necessary to propagate bacteriophage λ, a virus that infects bacteria by highjacking the bacteria's own replication machinery, in ''Escherichia coli''. By using a genetic screen, researchers knocked out certain genes in E''. coli'' and then tested whether the bacteria was able to replicate, GrpE was found to be crucial to propagation. Since that time, GrpE has been identified in all bacteria and in Archaea where DnaK and DnaJ are present. The crystal structure of GrpE was determined in 1997 at 2.8 Angstrom an ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
C-terminus
The C-terminus (also known as the carboxyl-terminus, carboxy-terminus, C-terminal tail, C-terminal end, or COOH-terminus) is the end of an amino acid chain (protein or polypeptide), terminated by a free carboxyl group (-COOH). When the protein is translated from messenger RNA, it is created from N-terminus to C-terminus. The convention for writing peptide sequences is to put the C-terminal end on the right and write the sequence from N- to C-terminus. Chemistry Each amino acid has a carboxyl group and an amine group. Amino acids link to one another to form a chain by a dehydration reaction which joins the amine group of one amino acid to the carboxyl group of the next. Thus polypeptide chains have an end with an unbound carboxyl group, the C-terminus, and an end with an unbound amine group, the N-terminus. Proteins are naturally synthesized starting from the N-terminus and ending at the C-terminus. Function C-terminal retention signals While the N-terminus of a protein often ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nucleotide Exchange Factor
Nucleotide exchange factors (NEFs) are proteins that stimulate the exchange (replacement) of nucleoside diphosphates for nucleoside triphosphates bound to other proteins. Function Many cellular proteins cleave (hydrolyze) nucleoside triphosphates–adenosine triphosphate (ATP) or guanosine triphosphate (GTP)–to their diphosphate forms (ADP and GDP) as a source of energy and to drive conformational changes. These changes in turn affect the structural, enzymatic, or signalling properties of the protein. Nucleotide exchange factors actively assist in the exchange of depleted nucleoside diphosphates for fresh nucleoside triphosphates. NEFs are specific for the nucleotides they exchange (ADP or GDP, but not both) and are often specific to a single protein or class of proteins with which they interact. See also * Nucleoside-diphosphate kinase Nucleoside-diphosphate kinases (NDPKs, also NDP kinase, (poly)nucleotide kinases and nucleoside diphosphokinases) are enzymes t ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Figure Hsp70 Function Cycle
Figure may refer to: General *A shape, drawing, depiction, or geometric configuration * Figure (wood), wood appearance * Figure (music), distinguished from musical motif * Noise figure, in telecommunication * Dance figure, an elementary dance pattern *A person's figure, human physical appearance Arts *Figurine, a miniature statuette representation of a creature *Action figure, a posable jointed solid plastic character figurine * Figure painting, realistic representation, especially of the human form * Figure drawing * Model figure, a scale model of a creature Writing *figure, in writing, a type of floating block (text, table, or graphic separate from the main text) *Figure of speech, also called a rhetorical figure * Christ figure, a type of character * in typesetting, text figures and lining figures Accounting *Figure, a synonym for number * Significant figures in a decimal number Science *Figure of the Earth, the size and shape of the Earth in geodesy Sports * Figure (ho ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Prokaryotes
A prokaryote () is a single-celled organism that lacks a nucleus and other membrane-bound organelles. The word ''prokaryote'' comes from the Greek πρό (, 'before') and κάρυον (, 'nut' or 'kernel').Campbell, N. "Biology:Concepts & Connections". Pearson Education. San Francisco: 2003. In the two-empire system arising from the work of Édouard Chatton, prokaryotes were classified within the empire Prokaryota. But in the three-domain system, based upon molecular analysis, prokaryotes are divided into two domains: ''Bacteria'' (formerly Eubacteria) and ''Archaea'' (formerly Archaebacteria). Organisms with nuclei are placed in a third domain, Eukaryota. In the study of the origins of life, prokaryotes are thought to have arisen before eukaryotes. Besides the absence of a nucleus, prokaryotes also lack mitochondria, or most of the other membrane-bound organelles that characterize the eukaryotic cell. It was once thought that prokaryotic cellular components within the cy ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryotes
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). Euk ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
ATP Hydrolysis
ATP hydrolysis is the catabolic reaction process by which chemical energy that has been stored in the high-energy phosphoanhydride bonds in adenosine triphosphate (ATP) is released after splitting these bonds, for example in muscles, by producing work in the form of mechanical energy. The product is adenosine diphosphate (ADP) and an inorganic phosphate (Pi). ADP can be further hydrolyzed to give energy, adenosine monophosphate (AMP), and another inorganic phosphate (Pi). ATP hydrolysis is the final link between the energy derived from food or sunlight and useful work such as muscle contraction, the establishment of electrochemical gradients across membranes, and biosynthetic processes necessary to maintain life. The description and typical textbook labels anhydridic bonds as "''high-energy bonds"''. P-O bonds are in fact fairly strong (~30 kJ/mol stronger than C-N bonds) Darwent, B. deB. (1970). "Bond Dissociation Energies in Simple Molecules", Nat. Stand. Ref. Data Ser., Na ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Peptide
Peptides (, ) are short chains of amino acids linked by peptide bonds. Long chains of amino acids are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. A polypeptide is a longer, continuous, unbranched peptide chain. Hence, peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others. A polypeptide that contains more than approximately 50 amino acids is known as a protein. Proteins consist of one or more polypeptides arranged in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule such as DNA or RNA, or to complex macromolecular assemblies. Amino acids that have been incorporated into peptides are termed residues. A water molecule is released during formation of each amide bond.. All peptides except cyc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
