Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.
about
Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsAllosteric opening of the polypeptide-binding site when an Hsp70 binds ATPThe function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.Mitochondrial Hsp70 Ssc1: role in protein folding.Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPIonic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics.Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocationSpecies-specific elements in the large T-antigen J domain are required for cellular transformation and DNA replication by simian virus 40Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain.Mutagenesis of a functional chimeric gene in yeast identifies mutations in the simian virus 40 large T antigen J domain.Maturation of steroid receptors: an example of functional cooperation among molecular chaperones and their associated proteinsDobzhansky-Muller incompatibilities in protein evolution.Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum.Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperonesDecipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.ATPase subdomain IA is a mediator of interdomain allostery in Hsp70 molecular chaperones.A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock proteinDependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.Mutations define cross-talk between the N-terminal nucleotide-binding domain and transmembrane helix-2 of the yeast multidrug transporter Pdr5: possible conservation of a signaling interface for coupling ATP hydrolysis to drug transportSurface binding and uptake of heat shock protein 70 by antigen-presenting cells require all 3 domains of the moleculeSmall molecule modulators of endogenous and co-chaperone-stimulated Hsp70 ATPase activity.Understanding the functional interplay between mammalian mitochondrial Hsp70 chaperone machine componentsA disulfide-bonded DnaK dimer is maintained in an ATP-bound stateAn interdomain sector mediating allostery in Hsp70 molecular chaperones.G673 could be a novel mutational hot spot for intragenic suppressors of pheS5 lesion in Escherichia coli.NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae.Analysis of sequence-specific binding of RNA to Hsp70 and its various homologs indicates the involvement of N- and C-terminal interactions.Identification of an inhibitor of hsc70-mediated protein translocation and ATP hydrolysis.Identification and characterization of OsEBS, a gene involved in enhanced plant biomass and spikelet number in rice.The four hydrophobic residues on the Hsp70 inter-domain linker have two distinct roles.Sequence-based prediction of protein interaction sites with an integrative method.Single molecule force spectroscopy reveals the effect of BiP chaperone on protein folding.Prediction of protein--protein interaction sites in heterocomplexes with neural networks.
P2860
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P2860
Intragenic suppressors of Hsp70 mutants: interplay between the ATPase- and peptide-binding domains.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@ast
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@en
type
label
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@ast
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@en
prefLabel
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@ast
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@en
P2093
P2860
P356
P1476
Intragenic suppressors of Hsp7 ...... - and peptide-binding domains.
@en
P2093
P2860
P304
P356
10.1073/PNAS.96.16.9269
P407
P577
1999-08-01T00:00:00Z