Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
about
Hsp70 chaperones: cellular functions and molecular mechanismThe nucleotide exchange factors of Hsp70 molecular chaperonesBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsModulation and elimination of yeast prions by protein chaperones and co-chaperonesOrchestration of secretory protein folding by ER chaperonesHsp104, Hsp70 and Hsp40 interplay regulates formation, growth and elimination of Sup35 prions.A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.A Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasisADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.HspBP1, an Hsp70 cochaperone, has two structural domains and is capable of altering the conformation of the Hsp70 ATPase domainHspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factorThe distribution of active RNA polymerase II along the transcribed region is gene-specific and controlled by elongation factorsThe HSP70 chaperone machinery: J proteins as drivers of functional specificityPathways of chaperone-mediated protein folding in the cytosolHsp110 is required for spindle length control.Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities.Global transcript and phenotypic analysis of yeast cells expressing Ssa1, Ssa2, Ssa3 or Ssa4 as sole source of cytosolic Hsp70-Ssa chaperone activityHierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.Coordinated Hsp110 and Hsp104 Activities Power Protein Disaggregation in Saccharomyces cerevisiae.Hsp110 chaperones control client fate determination in the hsp70-Hsp90 chaperone systemExpression of a malarial Hsp70 improves defects in chaperone-dependent activities in ssa1 mutant yeast.The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free systemHsp70- and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila.Metazoan Hsp70 machines use Hsp110 to power protein disaggregationPrimate chaperones Hsc70 (constitutive) and Hsp70 (induced) differ functionally in supporting growth and prion propagation in Saccharomyces cerevisiae.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Importance of the Hsp70 ATPase domain in yeast prion propagationSmall heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation.Keep the traffic moving: mechanism of the Hsp70 motor.Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica.All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.The Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae.Nucleotide exchange factors for Hsp70s are required for [URE3] prion propagation in Saccharomyces cerevisiae.
P2860
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P2860
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@ast
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@en
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p.
@nl
type
label
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@ast
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@en
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p.
@nl
prefLabel
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@ast
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@en
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p.
@nl
P2860
P1476
Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
@en
P2093
Jean-Marie Beckerich
Jeffrey L Brodsky
P2860
P304
P356
10.1128/MCB.22.13.4677-4689.2002
P407
P50
P577
2002-07-01T00:00:00Z