BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
about
ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substratesThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemA molecular portrait of the response to unfolded proteinsA 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.Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.Genetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.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.A novel Hsp70 of the yeast ER lumen is required for the efficient translocation of a number of protein precursorsPrm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.The membrane stress response buffers lethal effects of lipid disequilibrium by reprogramming the protein homeostasis network.Involvement of protein N-glycosyl chain glucosylation and processing in the biosynthesis of cell wall beta-1,6-glucan of Saccharomyces cerevisiae.N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast.Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion.The thioredoxin system protects ribosomes against stress-induced aggregationThe coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast.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.Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure.Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.Co- and Post-Translational Protein Folding in the ERBinding of BiP to the processing enzyme lymphoma proprotein convertase prevents aggregation, but slows down maturationEndoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunitThe molecular basis of oculocutaneous albinism type 1 (OCA1): sorting failure and degradation of mutant tyrosinases results in a lack of pigmentationMechanism of the facilitation of PC2 maturation by 7B2: involvement in ProPC2 transport and activation but not foldingCompetition between folding and glycosylation in the endoplasmic reticulum.The BiP molecular chaperone plays multiple roles during the biogenesis of torsinA, an AAA+ ATPase associated with the neurological disease early-onset torsion dystonia.Evasion of endoplasmic reticulum surveillance makes Wsc1p an obligate substrate of Golgi quality controlA misfolded protein conformation is not a sufficient condition for in vivo glucosylation by the UDP-Glc:glycoprotein glucosyltransferase.Sac1p plays a crucial role in microsomal ATP transport, which is distinct from its function in Golgi phospholipid metabolism.Secretory pathway genes assessed by high-throughput microscopy and synthetic genetic array analysis.J domain co-chaperone specificity defines the role of BiP during protein translocationOverexpression of an anti-CD3 immunotoxin increases expression and secretion of molecular chaperone BiP/Kar2p by Pichia pastorisCharacterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradationIdentification and characterization of a novel endoplasmic reticulum (ER) DnaJ homologue, which stimulates ATPase activity of BiP in vitro and is induced by ER stress.Human alpha B-crystallin mutation causes oxido-reductive stress and protein aggregation cardiomyopathy in miceDegradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system.Genome-scale modeling of the protein secretory machinery in yeast
P2860
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P2860
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@ast
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@en
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@nl
type
label
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@ast
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@en
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@nl
prefLabel
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@ast
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@en
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@nl
P2093
P2860
P356
P1476
BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast
@en
P2093
A Helenius
J F Simons
S Ferro-Novick
P2860
P356
10.1083/JCB.130.1.41
P407
P577
1995-07-01T00:00:00Z