The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
about
Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulumOne step at a time: endoplasmic reticulum-associated degradationPosttranslational modifications of proteins in the pathobiology of medically relevant fungiSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationQuality control and fate determination of Hsp90 client proteinsThe Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase networkCytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.The requirements of yeast Hsp70 of SSA family for the ubiquitin-dependent degradation of short-lived and abnormal proteins.Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.The proteome response to amyloid protein expression in vivoHeat shock proteins: cellular and molecular mechanisms in the central nervous system.Ubiquitin conjugation triggers misfolded protein sequestration into quality control foci when Hsp70 chaperone levels are limiting.Novel, gel-free proteomics approach identifies RNF5 and JAMP as modulators of GPCR stability.Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.Methylglyoxal alters the function and stability of critical components of the protein quality control.Ubiquitylation in ERAD: reversing to go forward?A nucleus-based quality control mechanism for cytosolic proteinsUbiquitin proteasome pathway-mediated degradation of proteins: effects due to site-specific substrate deamidationRegulation of inducible nitric-oxide synthase by the SPRY domain- and SOCS box-containing proteins.Hsp70- and Hsp90-mediated proteasomal degradation underlies TPI sugarkill pathogenesis in Drosophila.DSSylation, a novel protein modification targets proteins induced by oxidative stress, and facilitates their degradation in cells.Chaperones in control of protein disaggregation.Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteinsExposed hydrophobicity is a key determinant of nuclear quality control degradation.Protein targeting and degradation are coupled for elimination of mislocalized proteins.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase.Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signalBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.The endoplasmic reticulum-associated degradation pathways of budding yeast.Protein quality control: the who's who, the where's and therapeutic escapes.Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeastThe protective and destructive roles played by molecular chaperones during ERAD (endoplasmic-reticulum-associated degradation).Hsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseTrauma-associated human neutrophil alterations revealed by comparative proteomics profilingThe Hsp110 molecular chaperone stabilizes apolipoprotein B from endoplasmic reticulum-associated degradation (ERAD)
P2860
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P2860
The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system
description
2007 nî lūn-bûn
@nan
2007 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@ast
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@en
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@nl
type
label
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@ast
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@en
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@nl
prefLabel
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@ast
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@en
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@nl
P2093
P2860
P921
P3181
P356
P1476
The cytoplasmic Hsp70 chaperon ...... he ubiquitin-proteasome system
@en
P2093
Dieter H Wolf
Frederik Eisele
Junko Takeuchi
Natalia Bolender
Philip Coffino
Sae-Hun Park
Zlatka Kostova
P2860
P304
P3181
P356
10.1091/MBC.E06-04-0338
P407
P577
2007-01-01T00:00:00Z