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Topic: Chaperone protein

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Protein data bank

G protein

protein folding

protein biosynthesis

Protein kinases

protein synthesis

protein structure prediction

integral membrane protein

subunit proteins

C reactive protein

protein electrophoresis

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	Protein Targeting-Mitochondria and Chloroplasts
		Somehow the chaperonins peel off as the protein passes through the pore--it takes breakdown of ATP for the chaperonins to unbind, but there are often other chaperonins in the matrix of the mitochondrion that bind to the protein as it comes out the other side.
		In the cytosol, mitochondrial proteins are bound by chaperone proteins, typically hsp70 or else mitochondrial-import stimulating factor (MSF) which prevents their folding up completely, and that hydrolyzes ATP in order to accomplish this.
		On the one hand, they keep proteins from folding up completely; that is, they keep immature proteins or proteins not yet in their final functional location, in a partially extended state.
	www.lclark.edu /~reiness/cellbio/lectures/lect13.htm (1885 words)

	Biogerontology
		Molecular chaperones bind to, and stabilize an otherwise unstable conformer of another protein or RNA and, by controlled binding and release, facilitate its correct fate in vivo: be it folding, oligomeric assembly, transport to a particular subcellular compartment, or disposal by degradation.
		Chaperones usually do not increase the speed of protein folding, just inversely, by binding to folding intermediates, or by their repetitive pulling attempts extend the total folding time and simultaneously increase the final yield of the native protein.
		As another possible involvement of chaperones in the regulation of cellular senescence, the 90 kDa heat shock protein, Hsp90 is required for the correct assembly and function of telomerase, a major enzyme involved in determining the life-span of cells (Holt et al., 1999).
	www.chaperone.sote.hu /bioger1.htm (3264 words)

	Chaperone - Wikipedia, the free encyclopedia
		Many chaperones are heat shock proteins, that is, proteins expressed in response to elevated temperatures or other cellular stresses.
		The reason for this behaviour is that protein folding is severely affected by heat and, therefore, some chaperones act to repair the potential damage caused by misfolding.
		New functions for chaperones continue to be discovered, such as assistance in protein degradation and in responding to diseases linked to protein aggregation (see prion).
	en.wikipedia.org /wiki/Chaperone (778 words)

	InterPro: IPR000185 SecA protein
		Proteins are produced in the cytoplasm as precursors, and require a chaperone subunit to direct them to the translocase component.
		The translocase protein subunits are encoded on the bacterial chromosome.
		The chaperone protein SecB [ 2 ] is a highly acidic homotetrameric protein that exists as a "dimer of dimers" in the bacterial cytoplasm.
	www.ebi.ac.uk /interpro/IEntry?ac=IPR000185 (3227 words)

	Protein targeting - Wikipedia, the free encyclopedia
		Protein targeting or protein sorting is the mechanisms by which a cell transports proteins to the appropriate positions in the cell or outside of it.
		Once folded, the protein is modified as needed (for example, by glycosylation), then transported to the Golgi apparatus for further processing and goes to its target organelles or is retained in the ER by various ER retention mechanisms.
		This occurs for proteins that go to a mitochondrion, a chloroplast, or a peroxisome (proteins that go to the latter have their signal sequence at the C terminus).
	en.wikipedia.org /wiki/Protein_targeting (1340 words)

	Yeast chaperones interact with human prions
		Chaperone-supervised conversion of prion protein to its protease-resistantÝform
		Therefore, the ability of the chaperones to mediate the conversion of PrPC to PrP-res was modestly facilitated by the absence of N-linked sugars or the GPI anchor.
		EMBO J 1996 Jun 17;15(12):3127-3134 Paushkin SV, Kushnirov VV, Smirnov VN, Ter-Avanesyan MD The Sup35p protein of yeast Saccharomyces cerevisiae is a homologue of the polypeptide chain release factor 3 (eRF3) of higher eukaryotes.
	www.mad-cow.org /chaperones.html (6760 words)

	Adhesive pili page
		A periplasmic chaperone protein, FimC, is required for correct folding of the subunits, and for preventing the formation of non-productive, insoluble, complexes between the different components of the pilus by forming stable, discrete, and soluble pre-assembly complexes with the pili proteins in the periplasm.
		Chaperone/ subunit pre-assembly complexes are targeted to the outer membrane usher where the subunits are incorporated into the growing pilus in a defined order.
		Adhesive pili are complex structures composed of several different protein subunits that require specific pilus-assembly machinery for the incorporation of the component subunits into functional pili.
	xray.bmc.uu.se /~stefan/pili.html (1006 words)

	Copper "Chaperone" Escorts Hazardous Heavy Metal In Cells
		A team of scientists has now shown that a special "chaperone" protein encases one of these hazardous materials, copper, to safely escort it through the interior of the cell and deliver it to the specific site where it is needed.
		The human copper chaperones (there are known to be more than one) are required to transport copper, but diseases related to their malfunction have not yet been identified.
		Geneticist Valeria Culotta and her co-workers at Johns Hopkins SuJu Lin and Paul Schmidt cloned the copper chaperone protein gene in yeast and proved that the chaperone actually touches the protein to which it transfers the copper.
	www.eurekalert.org /pub_releases/1997-10/NU-CEHH-301097.php (612 words)

	The chaperone
		We have a rather elaborate "working-cycle" for the 60 kDa molecular chaperones, which possess a cavity, and are called Anfinsen-cage type chaperones to emphasize the fact that they provide a closed, protected environment to help the folding of their substrates.
		In case of Anfinsen-cage type chaperones the "encircling" of the target is especially pronounced, where the oligomeric structure of the chaperone sequesters the target to its inner cavity and allows an undisturbed folding process preventing aggregation.
		The Anfinsen-cage type chaperone machine-mediated entry of water molecules to the interior folding protein is not only a passive consequence of the chaperone-induced pulling/expansion of the target, but may significantly promote the conformational changes required to reach the native state.
	www.chaperone.sote.hu /bioessip.htm (4388 words)

	Cooperative Action of Escherichia coli ClpB Protein and DnaK Chaperone in the Activation of a Replication Initiation ...
		The Escherichia coli protein ClpB is a member of the universally conserved Hsp100/Clp protein family (1, 2).
		The involvement of the chaperone protein ClpX in the activation
		Activation of TrfA Is Specific for Bacterial Chaperone Proteins-- RK2 is a broad-host-range plasmid able to transfer and replicate its DNA in a wide spectrum of Gram-negative bacteria (19).
	www.jbc.org /cgi/content/full/277/21/18483 (4629 words)

	Heavy metal research is music to biologists' ears
		Culotta and O'Halloran reported that this second chaperone protein directly supplies a molecule of copper to SOD and showed how the chaperone is a necessary ingredient for the free radical-destroying protein's activity.
		In this technique, scientists bombard a tiny crystal of protein with high-energy X-rays, then piece together the protein's shape by tracing the directions in which the energy is scattered.
		Apparent in the X-ray crystallographic data is that the copper chaperone occurs "in double," or as a protein dimer consisting of two identical units.
	www.eurekalert.org /pub_releases/1999-07/NIoG-Hmri-280799.php (1013 words)

	Chaperone Technologies (Site not responding. Last check: 2007-10-29)
		Chaperone has identified the residues responsible for DnaK binding in pyrrhocoricin and the pyrrhocoricin binding surface on Escherichia coli DnaK protein.
		When this process is complete Chaperone can design pyrrhocoricin analogs that kill currently non-sensitive bacteria, including the most feared Staphylococcus aureus, as well as Streptococcus pneumoniae, Streptococcus pyogenes, Haemophilus ducreyi, Helicobacter pylori, or Enterococcus feacalis, just to name a few.
		Because higher organisms have multiple copies of the Hsp70 proteins this appears to be a more complex problem, although the Hsp70 sequences in the binding region of a given animal are remarkably similar.
	www.chaperonetechnologies.com /new/tech/tech5.php (271 words)

	The solution structure of the bacterial HSP70 chaperone protein domain DnaK(393-507) in complex with the peptide ...
		The protein was purified using a Ni-chelating column (Qiagen).
		The N-terminal His-tag was not cleaved from the protein.
		Vosine, C., Craig, E.A., Zufall, N., von Ahsen, O., Pfanner, N., and Voos, W. The protein import motor of mitochondria: Unfolding and trapping of preproteins are distinct and separable functions of matrix Hsp70.
	www.proteinscience.org /cgi/content/full/12/11/2588 (4897 words)

	Binding of a Putative and a Known Chaperone Protein Revealed by Immunogold Labeling Transmission Electron Microscopy: A ...
		Binding of a Putative and a Known Chaperone Protein Revealed by Immunogold Labeling Transmission Electron Microscopy: A Suggested Use of Chaperones as Probes for the Distribution of Their Target Proteins -- Thorpe et al.
		protein and the latter for endogenous chaperone protein distribution.
		Kay JE (1996) Structure-function relationships in the FK506-binding protein (FKBP) family of peptidylprolyl cis-trans isomerases.
	www.jhc.org /cgi/content/full/47/12/1633 (3457 words)

	UniProtKB/Swiss-Prot entry P63971 [DNAJ_STAAN] Chaperone protein dnaJ
		Unfolded proteins bind initially to dnaJ; upon interaction with the dnaJ-bound protein, dnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex.
		View cluster of proteins with at least 50% / 90% / 100% identity.
		Chaperone; Complete proteome; DNA replication; Heat shock; Metal-binding; Repeat; Zinc; Zinc-finger.
	www.expasy.org /uniprot/DNAJ_STAAN (319 words)

	InterPro: IPR003095 Heat shock protein DnaJ
		Molecular chaperones are a diverse family of proteins that function to protect proteins in the intracellular milieu 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-hydrolizing 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 [ 1 ].
	www.ebi.ac.uk /interpro/IEntry?ac=IPR003095 (3311 words)

	The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone -- Konieczny ...
		The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone -- Konieczny and Helinski 94 (26): 14378 -- Proceedings of the National Academy of Sciences
		The replication initiation protein of the broad-host-range plasmid RK2 is activated by the ClpX chaperone
		Molecular chaperones have been shown to be involved in both the assembly and the disassembly of DNA replication complexes.
	www.pnas.org /cgi/content/full/94/26/14378 (4178 words)

	Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ran-binding protein 2 -- Ferreira ...
		Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ran-binding protein 2 -- Ferreira et al.
		Interconversion of red opsin isoforms by the cyclophilin-related chaperone protein Ran-binding protein 2
		Ran-binding protein 2 (RanBP2) (type II) is a retinal cyclophilin-related protein that binds Ran-GTPase.
	www.pnas.org /cgi/content/full/94/4/1556 (4351 words)

	{gamma} Synuclein, a Novel Heat-Shock Protein-Associated Chaperone, Stimulates Ligand-Dependent Estrogen Receptor ...
		The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease.
		Evidence that the 90-kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor.
		Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson’s disease.
	cancerres.aacrjournals.org /cgi/content/full/64/13/4539 (5007 words)

	Anti-Oxidant Enzymes: Superoxide Dismutases (SOD1, SOD2, SOD3), Cu-Chaperone protein for SOD (CCS), Glutathione ...
		Anti-Oxidant Enzymes: Superoxide Dismutases (SOD1, SOD2, SOD3), Cu-Chaperone protein for SOD (CCS), Glutathione Peroxidase (GPX1) and Catalase Proteins and Antibodies,
		Highly reactive and potentially dangerous reactive oxygen species (ROS) are normally produced within the cells, primarily from the mitochondrial respiratory chain where in excess electrons are donated to molecular oxygen (o2) to generate peroxide anion (O2-).
		GPX is one of only a few proteins known in higher vertebrates to contain selenocysteine.
	www.4adi.com /flr/sodflr.html (823 words)

	Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from ... (Site not responding. Last check: 2007-10-29)
		Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli
		Hsc20 is a 20-kDa auxiliary protein that functions with the molecular
		Protein Sci., July 1, 2005; 14(7): 1697 - 1709.
	www.proteinscience.org /cgi/content/abstract/6/9/2028 (302 words)

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