The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
about
In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysisBag6 complex contains a minimal tail-anchor-targeting module and a mock BAG domainBAG-1 modulates the chaperone activity of Hsp70/Hsc70.Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG In vivoGrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1Reversible inhibition of Hsp70 chaperone function by Scythe and ReaperMechanisms for regulation of Hsp70 function by Hsp40Molecular chaperones as HSF1-specific transcriptional repressorsThe p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficaciesAnti-HSP90 autoantibodies in sera of infertile women identify a dominant, conserved epitope EP6 (380-389) of HSP90 beta proteinComplexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsStable transformation of an Arabidopsis cell suspension culture with firefly luciferase providing a cellular system for analysis of chaperone activity in vivoInhibition of Translation and Induction of Apoptosis by Bunyaviral Nonstructural Proteins Bearing Sequence Similarity to ReaperSaccharomyces cerevisiae Rot1 is an essential molecular chaperone in the endoplasmic reticulumFolding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.In vivo analysis of the Hsp90 cochaperone Sti1 (p60)Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependenceIn vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone.Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.Substrate-binding characteristics of proteins in the 90 kDa heat shock protein familyPathophysiological tissue changes associated with repetitive movement: a review of the evidenceA purine analog synergizes with chloroquine (CQ) by targeting Plasmodium falciparum Hsp90 (PfHsp90)A transmembrane guanylyl cyclase (DAF-11) and Hsp90 (DAF-21) regulate a common set of chemosensory behaviors in caenorhabditis elegansProteotoxic stress and inducible chaperone networks in neurodegenerative disease and agingGeranylgeranylacetone selectively binds to the HSP70 of Helicobacter pylori and alters its coccoid morphology.Bacterial proteostasis balances energy and chaperone utilization efficientlyTo fold or not to fold: modulation and consequences of Hsp90 inhibition.Chaperone-supervised conversion of prion protein to its protease-resistant form.Production and purification of human Hsp90β in Escherichia coli.Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids.Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation.ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.Overexpression of yeast Hsp110 homolog Sse1p suppresses ydj1-151 thermosensitivity and restores Hsp90-dependent activityPolypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.Genomic cloning of the Hsc71 gene in the hermaphroditic teleost Rivulus marmoratus and analysis of its expression in skeletal muscle: identification of a novel muscle-preferred regulatory element.Dynamic changes in the localization of thermally unfolded nuclear proteins associated with chaperone-dependent protectionIn vivo chaperone activity of heat shock protein 70 and thermotolerance.Dual role for Hsc70 in the biogenesis and regulation of the heme-regulated kinase of the alpha subunit of eukaryotic translation initiation factor 2Calreticulin recognizes misfolded HLA-A2 heavy chainsCharge-rich regions modulate the anti-aggregation activity of Hsp90.
P2860
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P2860
The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
The human cytosolic molecular ...... protein and protein refolding
@ast
The human cytosolic molecular ...... protein and protein refolding
@en
The human cytosolic molecular ...... protein and protein refolding
@nl
type
label
The human cytosolic molecular ...... protein and protein refolding
@ast
The human cytosolic molecular ...... protein and protein refolding
@en
The human cytosolic molecular ...... protein and protein refolding
@nl
prefLabel
The human cytosolic molecular ...... protein and protein refolding
@ast
The human cytosolic molecular ...... protein and protein refolding
@en
The human cytosolic molecular ...... protein and protein refolding
@nl
P2860
P3181
P1433
P1476
The human cytosolic molecular ...... protein and protein refolding
@en
P2093
Freeman BC
Morimoto RI
P2860
P304
P3181
P356
10.1002/J.1460-2075.1996.TB00660.X
P407
P577
1996-06-01T00:00:00Z