about
ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesHsp70 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 functionsOrchestration of secretory protein folding by ER chaperonesInsights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1Structure of the Hsp110:Hsc70 nucleotide exchange machine.Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factorSaccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.Nucleotide binding by Lhs1p is essential for its nucleotide exchange activity and for function in vivo.The Hsp70/90 cochaperone, Sti1, suppresses proteotoxicity by regulating spatial quality control of amyloid-like proteins.The promoter of filamentation (POF1) protein from Saccharomyces cerevisiae is an ATPase involved in the protein quality control process.Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1.The Saccharomyces cerevisiae YFR041C/ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum.Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.Redox signaling via the molecular chaperone BiP protects cells against endoplasmic reticulum-derived oxidative stressThe gene disrupted in Marinesco-Sjögren syndrome encodes SIL1, an HSPA5 cochaperoneA Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum MembraneThe challenge of improved secretory production of active pharmaceutical ingredients in Saccharomyces cerevisiae: a case study on human insulin analogs.Genomic analysis of the secretion stress response in the enzyme-producing cell factory Aspergillus niger.The KM-Algorithm Identifies Regulated Genes in Time Series Expression DataThe BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Superior antitumor response induced by large stress protein chaperoned protein antigen compared with peptide antigen.Genome-scale modeling of the protein secretory machinery in yeastMolecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways.Sil1, a nucleotide exchange factor for BiP, is not required for antibody assembly or secretionCellular thermotolerance is associated with heat shock protein 70.1 genetic polymorphisms in Holstein lactating cowsLocalization of BiP to translating ribosomes increases soluble accumulation of secreted eukaryotic proteins in an Escherichia coli cell-free systemEndoplasmic reticulum retention signal-dependent glycylation of the Hsp70/Grp170-related Pgp1p in Tetrahymena.Blocking Hsp70 enhances the efficiency of amphotericin B treatment against resistant Aspergillus terreus strains.All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.The response to heat shock and oxidative stress in Saccharomyces cerevisiaeBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Enhancing antibody folding and secretion by tailoring the Saccharomyces cerevisiae endoplasmic reticulum.Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.Feature Identification of Compensatory Gene Pairs without Sequence Homology in Yeast.Versatility of the endoplasmic reticulum protein folding factory.Engineering eukaryotic protein factories
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Coordinated activation of Hsp70 chaperones.
@ast
Coordinated activation of Hsp70 chaperones.
@en
Coordinated activation of Hsp70 chaperones.
@nl
type
label
Coordinated activation of Hsp70 chaperones.
@ast
Coordinated activation of Hsp70 chaperones.
@en
Coordinated activation of Hsp70 chaperones.
@nl
prefLabel
Coordinated activation of Hsp70 chaperones.
@ast
Coordinated activation of Hsp70 chaperones.
@en
Coordinated activation of Hsp70 chaperones.
@nl
P2093
P3181
P356
P1433
P1476
Coordinated activation of Hsp70 chaperones.
@en
P2093
Colin J Stirling
Donna M Fullerton
Gregor J Steel
John R Tyson
P304
P3181
P356
10.1126/SCIENCE.1092287
P407
P577
2004-01-02T00:00:00Z