A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors
about
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumGene expression profiling in the human pathogenic dermatophyte Trichophyton rubrum during growth on proteinsBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsHigh molecular weight stress proteins: Identification, cloning and utilisation in cancer immunotherapyThe Endoplasmic Reticulum Chaperone GRP170: From Immunobiology to Cancer TherapeuticsA role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation.Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.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.SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.Remodeling of yeast genome expression in response to environmental changes.Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.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.Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control.A novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesEndoplasmic reticulum: ER stress regulates mitochondrial bioenergetics.Impact of the lectin chaperone calnexin on the stress response, virulence and proteolytic secretome of the fungal pathogen Aspergillus fumigatus.Endoplasmic reticulum stress and fungal pathogenesis.Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.The unfolded protein response supports cellular robustness as a broad-spectrum compensatory pathway.Endoplasmic reticulum retention signal-dependent glycylation of the Hsp70/Grp170-related Pgp1p in Tetrahymena.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.Feature Identification of Compensatory Gene Pairs without Sequence Homology in Yeast.The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiaeThe unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control.Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiaeThe Lhs1/GRP170 chaperones facilitate the endoplasmic reticulum-associated degradation of the epithelial sodium channelProtein aggregation activates erratic stress response in dietary restricted yeast cells.Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Hac1p/Ern4p that activates the unfolded protein responseThe cytoplasmic chaperone hsp104 is required for conformational repair of heat-denatured proteins in the yeast endoplasmic reticulum.Interactions between intersubunit transmembrane domains regulate the chaperone-dependent degradation of an oligomeric membrane protein.The endoplasmic reticulum Grp170 acts as a nucleotide exchange factor of Hsp70 via a mechanism similar to that of the cytosolic Hsp110.A nucleotide exchange factor promotes endoplasmic reticulum-to-cytosol membrane penetration of the nonenveloped virus simian virus 40.A microsomal ATP-binding protein involved in efficient protein transport into the mammalian endoplasmic reticulum.Crosstalk between cellular compartments protects against proteotoxicity and extends lifespan.Spatial localisation of chaperone distribution in the endoplasmic reticulum of yeast.
P2860
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P2860
A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursors
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
A novel Hsp70 of the yeast ER ...... a number of protein precursors
@en
A novel Hsp70 of the yeast ER ...... number of protein precursors.
@nl
type
label
A novel Hsp70 of the yeast ER ...... a number of protein precursors
@en
A novel Hsp70 of the yeast ER ...... number of protein precursors.
@nl
prefLabel
A novel Hsp70 of the yeast ER ...... a number of protein precursors
@en
A novel Hsp70 of the yeast ER ...... number of protein precursors.
@nl
P2093
P2860
P3181
P1433
P1476
A novel Hsp70 of the yeast ER ...... a number of protein precursors
@en
P2093
P2860
P304
P3181
P356
10.1002/J.1460-2075.1996.TB00624.X
P407
P577
1996-06-01T00:00:00Z