Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
about
Identification of Mrj, a DnaJ/Hsp40 family protein, as a keratin 8/18 filament regulatory proteinMitochondrial enzyme rhodanese is essential for 5 S ribosomal RNA import into human mitochondriaOptimal functional levels of activation-induced deaminase specifically require the Hsp40 DnaJa1ERdj4 and ERdj5 are required for endoplasmic reticulum-associated protein degradation of misfolded surfactant protein CRegulated release of ERdj3 from unfolded proteins by BiPThe Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesisERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesMechanisms for regulation of Hsp70 function by Hsp40Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activityPopulation genetic variation in gene expression is associated with phenotypic variation in Saccharomyces cerevisiaePeptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display libraryMetazoan Hsp70-based protein disaggregases: emergence and mechanismsHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.A functional chaperone triad on the yeast ribosomeThe Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkGenetic analysis reveals that FLO11 upregulation and cell polarization independently regulate invasive growth in Saccharomyces cerevisiae.Sti1 is a novel activator of the Ssa proteins.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pThe function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.Mutations in the yeast Hsp40 chaperone protein Ydj1 cause defects in Axl1 biogenesis and pro-a-factor processing.The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Sue1p is required for degradation of labile forms of altered cytochromes C in yeast mitochondria.The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.The J-protein family: modulating protein assembly, disassembly and translocation.Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.Cns1 is an activator of the Ssa1 ATPase activity.RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein B mRNA editingLow resolution structural study of two human HSP40 chaperones in solution. DJA1 from subfamily A and DJB4 from subfamily B have different quaternary structuresPlasmodium falciparum encodes a single cytosolic type I Hsp40 that functionally interacts with Hsp70 and is upregulated by heat shockA review of multi-domain and flexible molecular chaperones studies by small-angle X-ray scattering.A role for the Hsp40 Ydj1 in repression of basal steroid receptor activity in yeastIn vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae.A targeted analysis of cellular chaperones reveals contrasting roles for heat shock protein 70 in flock house virus RNA replication.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.
P2860
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P2860
Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@ast
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@en
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@nl
type
label
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@ast
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@en
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@nl
prefLabel
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@ast
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@en
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@nl
P2860
P3181
P356
P1476
Protein folding activity of Hs ...... 0 co-chaperones Sis1 and Ydj1.
@en
P2860
P304
P3181
P356
10.1074/JBC.273.43.27824
P407
P577
1998-10-23T00:00:00Z