A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum.
about
The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulumFolding efficiency is rate-limiting in dopamine D4 receptor biogenesisA membrane protein required for dislocation of misfolded proteins from the ERDownregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteinsCarboxyl-terminal targeting and novel post-translational processing of JAW1, a lymphoid protein of the endoplasmic reticulumCharacterization of a human ubiquitin-conjugating enzyme gene UBE2L3TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitinationPerturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasomeSubpopulations of proteasomes in rat liver nuclei, microsomes and cytosolTransport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membraneFusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified geneQuantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradationOne step at a time: endoplasmic reticulum-associated degradationThe Hedgehog-inducible ubiquitin ligase subunit WSB-1 modulates thyroid hormone activation and PTHrP secretion in the developing growth plateMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlFunctional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteinsThe P5 disulfide switch: taming the aging unfolded protein responseThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyEndoplasmic 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.A regulatory link between ER-associated protein degradation and the unfolded-protein response.A yeast phenomic model for the gene interaction network modulating CFTR-ΔF508 protein biogenesis.SM-protein-controlled ER-associated degradation discriminates between different SNAREs.The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitmentDer3p/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. cerevisiaeINSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteinsComprehensive characterization of genes required for protein folding in the endoplasmic reticulumSec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane.Cue1p is an activator of Ubc7p E2 activity in vitro and in vivo.Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.Recognition of a subset of signal sequences by Ssh1p, a Sec61p-related protein in the membrane of endoplasmic reticulum of yeast Saccharomyces cerevisiae.Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding.HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins.Ubiquitin-mediated proteolysis of a short-lived regulatory protein depends on its cellular localizationInositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)Cleaning up in the endoplasmic reticulum: ubiquitin in chargeERAD: the long road to destructionSec61p-independent degradation of the tail-anchored ER membrane protein Ubc6p
P2860
Q24291942-84EA90C2-01C0-4A93-8C06-CA31CD3994F1Q24297696-4477DDAD-E917-4472-907C-EBADA1AD2C57Q24297703-BBCEE0E1-876C-4568-BEA6-113F6CD2E833Q24304937-7D60A366-13A1-471A-A8EE-0A5869267FE4Q24321857-621D8436-DCC8-46EC-8012-2FA93ED6621DQ24324671-49E95EE9-A58E-4681-A612-D3BAEFC9C4ABQ24529129-7E8746DC-9806-467A-B8AB-28BA251A9290Q24533430-07BAB9F2-37E3-46C6-89CA-9969254A0FDDQ24534300-E954EA54-4730-4A91-83C0-68F1DE1F3B0CQ24568369-961E576E-9AFC-4CF0-A97C-2DD5E463DA6DQ24622966-650748D3-DA66-46CA-A238-6DFF8A631509Q24643067-85F65FA1-7085-496E-96B0-51B2E44846DEQ24658302-16DF5866-54DE-4D43-B2B6-D26532B50795Q24669733-3F8D03E2-7106-4250-BD27-F42443125E62Q24677354-D5B0551F-5B6C-419B-BFBA-A7CF6EF30005Q24802049-4AEB7D93-48F2-4406-80EB-595A7694EF0CQ26861500-10361D0A-347C-4BF2-8800-C10EDC88ADFDQ27015793-6D39C9B2-E08B-4AF9-B6F9-4383725D00CAQ27930456-60BA16BF-6B8C-4678-A898-7EE47CD90E9DQ27930550-6071AC30-9C80-4E67-8F71-5A574CCDF2C4Q27931238-EB7425D1-FD14-42FB-8086-850D02BB5E85Q27931694-712FEFBB-6273-4F32-A45B-9A802C6CC4AAQ27932266-FBD3B0E6-43A7-4D7C-9988-E9BA893E7C01Q27932818-805C6C48-F220-4284-A67A-F2B68979EE39Q27934337-CFCCAFD7-0204-4D2D-AC96-698D5EC41D45Q27935591-FDBB0F3B-EE3F-416F-A31C-DA518053CA59Q27936730-7580AF59-F836-416C-A6B7-0B165209AC67Q27937991-45265441-10CB-4320-88F4-674EA6616E6BQ27938591-29AB606C-9DFD-4DD7-AA8F-8F8DED173078Q27938752-6FE50B4D-CE83-42B9-9299-89F72301164FQ27939649-00A469DC-3A3D-433C-BD52-AA71C39736F9Q27939668-1863E7B7-4D00-4722-8AE4-E203D712EE66Q27939944-D4C0A351-F584-42F6-A08F-69C656DC01A6Q27939971-00351818-99E1-45CA-996B-74CE29B3F1A0Q28138877-DB177407-8C89-413F-AB98-62CAEFAFBA9DQ28187990-042C8DBB-1F17-4DC5-AA20-64C797EBB598Q28207747-BA8542C8-5D5C-4107-B02F-AE82A62E9135Q28237362-F8225345-B46A-4B85-8E84-B00FF3E8F463Q28264823-AF281276-0A92-40B9-87AB-B7CFA2ADDC1CQ28366803-203372A8-D02C-4DC1-8FC7-1A8FFD52F161
P2860
A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum.
description
1993 nî lūn-bûn
@nan
1993 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年学术文章
@wuu
1993年学术文章
@zh-cn
1993年学术文章
@zh-hans
1993年学术文章
@zh-my
1993年学术文章
@zh-sg
1993年學術文章
@yue
name
A protein translocation defect ...... at the endoplasmic reticulum.
@ast
A protein translocation defect ...... at the endoplasmic reticulum.
@en
A protein translocation defect ...... at the endoplasmic reticulum.
@nl
type
label
A protein translocation defect ...... at the endoplasmic reticulum.
@ast
A protein translocation defect ...... at the endoplasmic reticulum.
@en
A protein translocation defect ...... at the endoplasmic reticulum.
@nl
prefLabel
A protein translocation defect ...... at the endoplasmic reticulum.
@ast
A protein translocation defect ...... at the endoplasmic reticulum.
@en
A protein translocation defect ...... at the endoplasmic reticulum.
@nl
P3181
P356
P1433
P1476
A protein translocation defect ...... at the endoplasmic reticulum.
@en
P2093
P2888
P3181
P356
10.1038/365176A0
P407
P577
1993-09-09T00:00:00Z
P6179
1013695938