The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.
about
Unfolding the Role of Large Heat Shock Proteins: New Insights and Therapeutic ImplicationsThe nucleotide exchange factors of Hsp70 molecular chaperonesBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsHigh molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapyOrchestration of secretory protein folding by ER chaperonesThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsA bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause diseaseA Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum MembraneMetazoan Hsp70 machines use Hsp110 to power protein disaggregationA chaperone trap contributes to the onset of cystic fibrosis.Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.Unfolded protein response-induced ERdj3 secretion links ER stress to extracellular proteostasis.The nucleotide exchange factors Grp170 and Sil1 induce cholera toxin release from BiP to enable retrotranslocation.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeastThe Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelThe large Hsp70 Grp170 binds to unfolded protein substrates in vivo with a regulation distinct from conventional Hsp70s.The control of spindle length by Hsp70 and Hsp110 molecular chaperones.Chaperone-Driven Degradation of a Misfolded Proinsulin Mutant in Parallel With Restoration of Wild-Type Insulin Secretion.Myopathy in Marinesco-Sjögren syndrome links endoplasmic reticulum chaperone dysfunction to nuclear envelope pathology.The FgSsb-FgZuo-FgSsz complex regulates multiple stress responses and mycotoxin production via folding the soluble SNARE Vam7 and β2-tubulin in Fusarium graminearum.
P2860
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P2860
The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年学术文章
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2010年学术文章
@zh-cn
2010年学术文章
@zh-hans
2010年学术文章
@zh-my
2010年学术文章
@zh-sg
2010年學術文章
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2010年學術文章
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name
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@en
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@nl
type
label
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@en
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@nl
prefLabel
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@en
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@nl
P2860
P50
P356
P1476
The endoplasmic reticulum Grp1 ...... that of the cytosolic Hsp110.
@en
P2093
Claes Andréasson
Heike Rampelt
P2860
P304
12445-12453
P356
10.1074/JBC.M109.096735
P407
P577
2010-02-20T00:00:00Z