Sec61p and BiP directly facilitate polypeptide translocation into the ER.
about
The signal sequence coding region promotes nuclear export of mRNALHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumThe human oesophageal squamous epithelium exhibits a novel type of heat shock protein responseMapping of residues forming the voltage sensor of the voltage-dependent anion-selective channelEukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteinsThe oligomerization reaction of the Semliki Forest virus membrane protein subunitsOligomerization-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.In vivo action of the HRD ubiquitin ligase complex: mechanisms of endoplasmic reticulum quality control and sterol regulation.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 cerevisiaeThe FKB2 gene of Saccharomyces cerevisiae, encoding the immunosuppressant-binding protein FKBP-13, is regulated in response to accumulation of unfolded proteins in the endoplasmic reticulumSec63p 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 Ssa1pFunctional characterization of Ost3p. Loss of the 34-kD subunit of the Saccharomyces cerevisiae oligosaccharyltransferase results in biased underglycosylation of acceptor substrates.Genetic 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 precursorsPrm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.The cold sensitivity of a mutant of Saccharomyces cerevisiae lacking a mitochondrial heat shock protein 70 is suppressed by loss of mitochondrial DNA.BiP and Sec63p are required for both co- and posttranslational protein translocation into the yeast endoplasmic reticulum.A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70sFunctional interaction of cytosolic hsp70 and a DnaJ-related protein, Ydj1p, in protein translocation in vivo.Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins.A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiaeCer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.Cytosolic Hsp70s are involved in the transport of aminopeptidase 1 from the cytoplasm into the vacuole.All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.PEB1 (PAS7) in Saccharomyces cerevisiae encodes a hydrophilic, intra-peroxisomal protein that is a member of the WD repeat family and is essential for the import of thiolase into peroxisomes.Cell wall 1,6-beta-glucan synthesis in Saccharomyces cerevisiae depends on ER glucosidases I and II, and the molecular chaperone BiP/Kar2p.A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viabilityMolecular characterization of a novel mammalian DnaJ-like Sec63p homologA Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposomeBiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeastA novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesA role for calnexin (IP90) in the assembly of class II MHC moleculesThe complete general secretory pathway in gram-negative bacteriaRegulation of the ribosome-membrane junction at early stages of presecretory protein translocation in the mammalian endoplasmic reticulum.
P2860
Q21092749-A7C00EE5-13A3-4721-86C0-4E2A74E61EA6Q24290571-3FF7EE3F-0D91-4C93-9462-3CEED0B72A3BQ24291808-772E6FA8-8A04-4011-8415-7760F158DD65Q24562735-254D23A6-73E8-40FC-8AC0-78BA2369FEBFQ24622449-B0C0FD26-BDBA-4C2E-8F11-EC2D147DCCC9Q27482650-69A7E1CC-AD2A-4954-8075-1DEC99F46366Q27485868-8C7B8CA0-0587-43E1-8762-321F6D3A4DF3Q27929932-D5D7CDAD-2ADE-404B-A2B6-4D64ECECA02DQ27929958-36FD1DA4-2F49-463E-A330-F679E5A3F863Q27930004-7C9FD472-CAE2-41D0-B772-34CA071F6DA5Q27930550-BF53654B-A483-4AEF-A05A-F2B728003285Q27930560-5C7884BD-3D36-47D5-B7C2-DB37E5C0B900Q27930631-191CE030-C070-4053-831B-7CC069DDE75AQ27930764-9E4C068D-3F1B-45D8-BF9E-750855A3880EQ27931293-2DBBB465-09B5-4783-9391-09150DEC21CBQ27931520-9374CBCD-6FFE-4827-AEF0-3E559BD20672Q27931697-D10317B0-0160-4BD4-9D1D-400E202C34F0Q27932136-A1252201-A2E4-4BBF-973E-BB6A1937C56FQ27932477-A85B050A-F9B5-4363-9808-E29065AC6078Q27933142-9D5D7D81-1805-490A-BDE1-6EAC30428634Q27935128-447C5E5F-E62E-4568-BA6B-52FDC811BF9DQ27935171-CAB19E9D-D752-4469-8076-57241DF62740Q27935309-08BFDFC6-06CD-445C-81F0-DA3A2F7E4692Q27935347-DCB4CB25-0F98-4B98-A180-B327BFA74D1DQ27935523-6BE71C67-40FD-442A-B2A4-B6A8E9CC048EQ27935591-CCD530E0-13F0-4F65-BAD5-4981026E3BE2Q27936368-13371D31-0C99-4253-A6EE-DBC5FF5EBB6BQ27936886-FD693F63-140C-4BF6-AE6E-C76437C35255Q27937279-EC839656-4509-47F7-B150-4A3A9F47E4A3Q27938591-1C474E26-FAE1-4E3C-AD21-67B955B575BAQ27938605-A9D33E58-D986-45DD-9A9A-0E2072A2BC02Q27939632-E22FD69D-1CF9-4B53-B09A-DB73A26A5B36Q27972960-EAB9EA39-F10B-4BB5-9BB9-B28EDCF3BCDEQ28146116-DA827005-D596-4670-A2F3-0A68E3B87B81Q28257113-8D248037-6E1B-4483-AA65-0DA44D2EB4A1Q28303811-8EC1C68D-C32C-43C5-AEEE-94465D095154Q28588605-A54535C6-163D-4AF8-9F8E-D81897683B4CQ28613001-1544C44E-D6DF-4204-A97A-A227B898C70FQ29615298-6F08BC44-5EE5-41A7-A196-31409A724C33Q30442132-90054C1A-15A5-443D-BE9D-8E3BEAAAC01B
P2860
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh
1992年學術文章
@zh-hant
name
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@en
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@nl
type
label
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@en
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@nl
prefLabel
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@en
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@nl
P2093
P1433
P1476
Sec61p and BiP directly facilitate polypeptide translocation into the ER.
@en
P2093
K M Whitfield
S L Sanders
P304
P356
10.1016/0092-8674(92)90415-9
P407
P577
1992-04-01T00:00:00Z