Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex.
about
Mammalian Sec61 is associated with Sec62 and Sec63Translocon-associated protein TRAP delta and a novel TRAP-like protein are coordinately expressed with pro-opiomelanocortin in Xenopus intermediate pituitaryHuman homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neuronsA protein of the endoplasmic reticulum involved early in polypeptide translocationThe yeast RER2 gene, identified by endoplasmic reticulum protein localization mutations, encodes cis-prenyltransferase, a key enzyme in dolichol synthesisAnalysis of mRNA with microsomal fractionation using a SAGE-based DNA microarray system facilitates identification of the genes encoding secretory proteinsEukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteinsOne step at a time: endoplasmic reticulum-associated degradationThe endoplasmic reticulum: structure, function and response to cellular signalingThe Aspergillus nidulans peripheral ER: disorganization by ER stress and persistence during mitosisThe protein translocation channel mediates glycopeptide export across the endoplasmic reticulum membraneX-ray structure of a protein-conducting channelPeriplasmic Bar1 protease of Saccharomyces cerevisiae is active before reaching its extracellular destination.A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.Structural studies and the assembly of the heptameric post-translational translocon complexSec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex.Endoplasmic Reticulum-associated Degradation of Pca1p, a Polytopic Protein, via Interaction with the Proteasome at the MembraneSec61p 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 cerevisiaeSec61p is part of the endoplasmic reticulum-associated degradation machineryExtragenic suppressors of mutations in the cytoplasmic C terminus of SEC63 define five genes in Saccharomyces cerevisiae.The protein translocation channel binds proteasomes to the endoplasmic reticulum membraneTor kinases are in distinct membrane-associated protein complexes in Saccharomyces cerevisiae.Rer1p, a retrieval receptor for endoplasmic reticulum membrane proteins, is dynamically localized to the Golgi apparatus by coatomerFutile protein folding cycles in the ER are terminated by the unfolded protein O-mannosylation pathway.An interaction between the SRP receptor and the translocon is critical during cotranslational protein translocation.An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transportDer3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiaeStructural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum.Protein translocation mutants defective in the insertion of integral membrane proteins into the endoplasmic reticulum.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.Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.The SESA network links duplication of the yeast centrosome with the protein translation machinery.Shr3p mediates specific COPII coatomer-cargo interactions required for the packaging of amino acid permeases into ER-derived transport vesiclesRegulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1bA Sec63p-BiP complex from yeast is required for protein translocation in a reconstituted proteoliposomeA novel type of co-chaperone mediates transmembrane recruitment of DnaK-like chaperones to ribosomesThe complete general secretory pathway in gram-negative bacteria
P2860
Q22254037-E500599A-7047-4462-879F-601448F42CEAQ24303980-29126736-0ACB-4788-932F-CC4B8E4B6FCBQ24306619-2F8037A3-1CE2-4FB0-8201-578CB90A9CCEQ24336350-DBF97865-79B9-4586-A1E1-2010D6194E59Q24554649-3AF3E54C-752B-4F6A-B19D-2FABDB58B490Q24561656-29480172-9AB4-4695-ACBD-48B4B5FF6203Q24622449-01AB0422-97E3-42EF-8C6B-509670E900B3Q24658302-FFE02703-B069-46FF-AB98-83AE2A29BC1AQ26782462-FC2342D0-DA68-4DF1-A48A-C37FA93A3A21Q27312475-29F79652-8309-4D35-A713-DA33E08929FAQ27478172-016FC09E-108E-4502-B061-72260B08CD5DQ27642744-4D3C0345-857A-40CF-8493-F8E4697FAB72Q27929785-040E30B5-58D2-401E-AEBF-C637CFA75173Q27929932-4B10F604-CFF6-43D1-9BF2-FCA07820E3B6Q27930101-76E90C6D-835E-4CC9-A54E-8B02DC58B94DQ27930142-A3A7D4FC-E9F9-4033-90E3-6F88B437044BQ27930456-33CB2793-0C72-4991-B9D4-009F43DACA03Q27930550-4D5C1EEF-B427-4A9B-B28F-B7D7178CD470Q27930560-A340F7B4-1ECC-48BD-8657-7E58242C52B5Q27930621-8881FB2C-5D55-496F-BAA0-74E3A430BFABQ27931215-446B46D8-3474-41CA-ADCF-6E6505260237Q27931542-9EC6BF94-C1BF-4E93-8ABF-D7665022E9E3Q27931595-CA4AE239-8BFA-46F1-A0BA-6149196B5F43Q27931848-2E8DDCE4-4A25-4C6B-B97D-6D6B12E8E4ADQ27932449-AF476534-BDC8-4C5A-8B7A-183B26A9C4A9Q27932958-28CB97F9-E581-487F-B1CA-3BC76E3335E5Q27933526-1C9466FB-8793-42EC-A9ED-D09A07B3EBDAQ27934337-3BA6FA91-54C5-4E60-BABB-FE8D235E8626Q27935591-11EFFF14-5180-48D7-B0F7-09735FDEFE11Q27937407-8CEFF817-8227-4BB6-A1BF-AB130776E365Q27937605-1AC81568-878F-482E-956B-97A825699A36Q27937897-3B70FC99-1999-473D-8B3A-3D93B4DA5172Q27938591-3EC1ECA5-1E52-4423-81B8-469E9A430091Q27939668-43336BBC-4048-414A-89ED-3D9984F94648Q27939958-B503E64F-AA65-4811-880E-8CA75AD269B6Q27940100-1CC311B0-71FB-4205-89EA-5CA9D01E8ED3Q28118467-785CFF6E-9CA6-4460-B8F6-34453B918D29Q28257113-022CBB3F-6548-4196-8F52-723992768E06Q28588605-66C7245C-682F-47D3-BECB-9D4E90A5C238Q29615298-28F3D0BF-0D43-490B-AFFE-41D9D74A37A1
P2860
Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex.
description
1991 nî lūn-bûn
@nan
1991 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@ast
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@en
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@nl
type
label
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@ast
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@en
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@nl
prefLabel
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@ast
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@en
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@nl
P2093
P356
P1433
P1476
Assembly of yeast Sec proteins ...... ne-bound multisubunit complex.
@en
P2093
D A Feldheim
R J Deshaies
S L Sanders
P2888
P356
10.1038/349806A0
P407
P577
1991-02-28T00:00:00Z
P6179
1039650783