Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.
about
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumNot all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactionsThe T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperoneYeast flavin-containing monooxygenase generates oxidizing equivalents that control protein folding in the endoplasmic reticulumOligomerization-dependent folding of the membrane fusion protein of Semliki Forest virusA 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.Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation.Genetic interactions between KAR7/SEC71, KAR8/JEM1, KAR5, and KAR2 during nuclear fusion in Saccharomyces cerevisiaeSec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.Coordination of N-glycosylation and protein translocation across the endoplasmic reticulum membrane by Sss1 protein.SSI1 encodes a novel Hsp70 of the Saccharomyces cerevisiae endoplasmic reticulum.The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosome-nascent chain complex.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Sls1p stimulates Sec63p-mediated activation of Kar2p in a conformation-dependent manner in the yeast endoplasmic reticulum.Molecular characterization of a novel mammalian DnaJ-like Sec63p homologA novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesRegulation of the ribosome-membrane junction at early stages of presecretory protein translocation in the mammalian endoplasmic reticulum.BiP clustering facilitates protein folding in the endoplasmic reticulumPosttranslational protein translocation across the membrane of the endoplasmic reticulum.HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.The brownian ratchet and power stroke models for posttranslational protein translocation into the endoplasmic reticulumCharacterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.Specificity of class II Hsp40 Sis1 in maintenance of yeast prion [RNQ+].Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.Determination of the Plasmodium vivax schizont stage proteome.Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP.The Candida albicans Kar2 protein is essential and functions during the translocation of proteins into the endoplasmic reticulum.Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiaeThe mitochondrial protein import motor: dissociation of mitochondrial hsp70 from its membrane anchor requires ATP binding rather than ATP hydrolysisExport of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.A new role for BiP: closing the aqueous translocon pore during protein integration into the ER membraneMutation of sec63 in zebrafish causes defects in myelinated axons and liver pathologyProtein translocation across the rough endoplasmic reticulum.Interaction between the small GTPase Ran/Gsp1p and Ntf2p is required for nuclear transportSpecific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.Protein O-mannosyltransferases associate with the translocon to modify translocating polypeptide chains.The Sec translocon mediated protein transport in prokaryotes and eukaryotes.
P2860
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P2860
Interaction between BiP and Sec63p is required for the completion of protein translocation into the ER of Saccharomyces cerevisiae.
description
1995 nî lūn-bûn
@nan
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
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@ast
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@en
type
label
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@ast
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@en
prefLabel
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@ast
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@en
P2860
P356
P1476
Interaction between BiP and Se ...... R of Saccharomyces cerevisiae.
@en
P2093
P2860
P304
P356
10.1083/JCB.131.5.1163
P407
P577
1995-12-01T00:00:00Z