BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.
about
Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cellsInteraction of murine BiP/GRP78 with the DnaJ homologue MTJ1Dissecting toxin immunity in virus-infected killer yeast uncovers an intrinsic strategy of self-protectionA molecular portrait of the response to unfolded proteinsThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneSec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo.Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1pGenetic evidence for a role of BiP/Kar2 that regulates Ire1 in response to accumulation of unfolded proteins.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 precursorsFunctional characterization of the trans-membrane domain interactions of the Sec61 protein translocation complex beta-subunit.Prm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.Tom7 modulates the dynamics of the mitochondrial outer membrane translocase and plays a pathway-related role in protein importDifferential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy.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.ATPase activity of a yeast secretory glycoprotein allows ER exit during inactivation of COPII components Sec24p and Sec13p.Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.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.Emerging features of ER resident J-proteins in plants.Reconstitution of the protein insertion machinery of the mitochondrial inner membrane.The membrane-bound DnaJ protein located at the cytosolic site of glyoxysomes specifically binds the cytosolic isoform 1 of Hsp70 but not other Hsp70 species.HEDJ, an Hsp40 co-chaperone localized to the endoplasmic reticulum of human cells.BiP availability distinguishes states of homeostasis and stress in the endoplasmic reticulum of living cells.Archaeal protein translocation crossing membranes in the third domain of life.J domain co-chaperone specificity defines the role of BiP during protein translocationRejection of impassable substrates by Yersinia type III secretion machinesCo-translational targeting and translocation of the amino terminus of opsin across the endoplasmic membrane requires GTP but not ATP.Characterization of pancreatic ERj3p, a homolog of yeast DnaJ-like protein Scj1p.Role of human sec63 in modulating the steady-state levels of multi-spanning membrane proteins.Mutation of the ATP-binding pocket of SSA1 indicates that a functional interaction between Ssa1p and Ydj1p is required for post-translational translocation into the yeast endoplasmic reticulum.Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequenceIn vivo and in vitro interaction of DnaK and a chloroplast transit peptide.Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes.Cotranslational stabilization of Sec62/63 within the ER Sec61 translocon is controlled by distinct substrate-driven translocation events.Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP.
P2860
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P2860
BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.
description
1995 nî lūn-bûn
@nan
1995 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@ast
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@en
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@nl
type
label
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@ast
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@en
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@nl
prefLabel
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@ast
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@en
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@nl
P2860
P356
P1476
BiP and Sec63p are required fo ...... e yeast endoplasmic reticulum.
@en
P2093
J Goeckeler
J L Brodsky
P2860
P304
P356
10.1073/PNAS.92.21.9643
P407
P577
1995-10-10T00:00:00Z