Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.
about
Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory proteinS100A1 is a novel molecular chaperone and a member of the Hsp70/Hsp90 multichaperone complexERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stressCHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substratesNot all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsTim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondriaMetazoan Hsp70-based protein disaggregases: emergence and mechanismsNucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pYeast prions are useful for studying protein chaperones and protein quality controlA DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editingHspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factorAllostery in the Hsp70 chaperone proteinsClose and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiPLow resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structuresModeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysisJ domain co-chaperone specificity defines the role of BiP during protein translocationThe lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity.Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation.T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesisThe unfolding story of the Escherichia coli Hsp70 DnaK: is DnaK a holdase or an unfoldase?Analysis of the levels of conservation of the J domain among the various types of DnaJ-like proteins.Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activityHeat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock proteinCytosolic and ER J-domains of mammalian and parasitic origin can functionally interact with DnaK.The structural and functional diversity of Hsp70 proteins from Plasmodium falciparumBiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP.Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural changeThe 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.Curing of yeast [URE3] prion by the Hsp40 cochaperone Ydj1p is mediated by Hsp70.Species- and Strain-Specific Adaptation of the HSP70 Super Family in Pathogenic TrypanosomatidsAntigenic peptides complexed to phylogenically diverse Hsp70s induce differential immune responses.Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK.The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation.A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum.Structural and Biological Interaction of hsc-70 Protein with Phosphatidylserine in Endosomal Microautophagy.The remarkable multivalency of the Hsp70 chaperones.The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondriaMultiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded proteinSegmental isotopic labeling of the Hsp70 molecular chaperone DnaK using expressed protein ligation.
P2860
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P2860
Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ.
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
Structural features required f ...... naK with its cochaperone DnaJ.
@en
type
label
Structural features required f ...... naK with its cochaperone DnaJ.
@en
prefLabel
Structural features required f ...... naK with its cochaperone DnaJ.
@en
P2093
P2860
P356
P1476
Structural features required f ...... naK with its cochaperone DnaJ.
@en
P2093
P2860
P304
30534-30539
P356
10.1074/JBC.274.43.30534
P407
P577
1999-10-01T00:00:00Z