Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
about
Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting stepsA membrane protein required for dislocation of misfolded proteins from the ERA membrane protein complex mediates retro-translocation from the ER lumen into the cytosolThe RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERADHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumA ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationSGTA recognizes a noncanonical ubiquitin-like domain in the Bag6-Ubl4A-Trc35 complex to promote endoplasmic reticulum-associated degradationFunction of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chainsOS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADNMR characterization of the interaction between the PUB domain of peptide:N-glycanase and ubiquitin-like domain of HR23USP13 antagonizes gp78 to maintain functionality of a chaperone in ER-associated degradationRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERADRecruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneEvidence for distinct functions for human DNA repair factors hHR23A and hHR23BThe tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteinsLocalization of a highly active pool of type II phosphatidylinositol 4-kinase in a p97/valosin-containing-protein-rich fraction of the endoplasmic reticulumMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.SVIP is a novel VCP/p97-interacting protein whose expression causes cell vacuolation.E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemFolding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulumOne step at a time: endoplasmic reticulum-associated degradationVCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivoThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemMisfolded proteins are sorted by a sequential checkpoint mechanism of ER quality controlVCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragmentsAtaxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysisUbiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3Ring of Change: CDC48/p97 Drives Protein Dynamics at ChromatinProtein folding and quality control in the ERRecent technical developments in the study of ER-associated degradationRegulation of Unperturbed DNA Replication by UbiquitylationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyFrom neurodevelopment to neurodegeneration: the interaction of neurofibromin and valosin-containing protein/p97 in regulation of dendritic spine formationKey steps in ERAD of luminal ER proteins reconstituted with purified componentsDissecting the ER-associated degradation of a misfolded polytopic membrane protein.Sec61p is part of the endoplasmic reticulum-associated degradation machineryThe budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7).The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
P2860
Q21131559-3914C92C-7908-42FE-8D10-9ABE5096D065Q24297703-5960E65A-9962-43DD-B5C5-3B929FAB2B07Q24297732-6CC7885D-3591-432E-9C63-A5203AB5135DQ24297892-3F49045F-AD80-419F-8F49-29A464D84042Q24298901-324E41C7-51A3-4E29-AD26-2C70467B1F86Q24305231-BD42B1D2-9DB2-461F-976B-9179822BCE5AQ24306367-2B41CC78-07CF-449A-BCF4-126BF45357B3Q24307429-29E3D190-2C79-4B10-B048-525C1BD974E7Q24312778-A363D804-AD50-4A3A-B05B-CBF87DD5E8D2Q24320023-4E8D281B-989F-42DC-A017-B870A04DCB03Q24320201-F5051577-D913-464F-92D7-0B2F992AAA7AQ24323658-A24CF68B-5744-41C1-8F4A-00465B400253Q24324707-B6E61E1A-97EF-4164-95C3-D41DF678FEA0Q24336904-B4663BDB-C290-4A6D-A8B4-5BAE3E5562BEQ24337432-CE7C4599-7037-42BA-BD50-A0861130CC59Q24338770-41234C3E-F2D1-4E51-8817-AED8CB337A40Q24529995-E531E65F-035E-4757-BEE2-1F5BFD52B6F7Q24530318-E982F616-BC94-44F9-AD45-A3BDB1EF523CQ24539071-747EEB8F-A8F0-4655-9536-A626CC86C23EQ24540390-C9C0F80D-CD68-4DAA-8BC7-ADD88F218D7BQ24554438-544AEF97-5B43-4DE9-9EB2-34DCAA2BC0E9Q24600792-621241E8-8A0E-4F6C-AA75-219990ECB543Q24658302-05F519E6-EECD-4B38-8721-D1FB6F6A8D0BQ24673098-1076B834-4A85-442D-8EBC-B549076F725DQ24676115-FA997ACD-6156-4B88-B5D9-72E846E15E15Q24677354-C4006436-3868-4CEC-BB52-BC66E2EEE183Q24677725-91424427-E228-4F37-AC7C-5F06E7E18306Q24682823-0731CB01-DFEA-4A72-931C-07F64B4A33D2Q24683139-6AB66AB1-5F40-4DAA-B77B-A3CE17037083Q26747328-D9E40B48-3A7B-471E-BAB4-1FB1B53541A2Q26823157-780F3E40-3D86-4988-A291-0953C3A68303Q26823514-DE7B0CA6-75B9-4A64-B713-409F856B405DQ26853389-BFC334EB-53BB-42B7-B4A5-92A468F4869DQ27015793-5F83908F-41B0-4CAD-BE9C-CC1CA22D1C7CQ27015865-60F7D9D7-5162-4E1C-8231-EFB4AFB3FF20Q27929992-262D5E29-313F-41C9-99D5-E99B67A98E91Q27930024-8FC6A29C-C05C-4E5E-A57E-510FA46C588FQ27930621-4BD9CB72-8144-47F1-BCA1-BC2F3B996CB3Q27931138-DFD0361D-98DC-40DD-82D0-E1BE7037A20AQ27931542-CEECD2CA-B3A6-42CC-B54D-8FB9A1162EE2
P2860
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
description
2002 nî lūn-bûn
@nan
2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@ast
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@en
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@nl
type
label
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@ast
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@en
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@nl
altLabel
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
@en
prefLabel
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@ast
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@en
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@nl
P2093
P2860
P3181
P356
P1433
P1476
Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48.
@en
P2093
Christof Taxis
Corinna Volkwein
Daniel Finley
Dieter H Wolf
Ernst Jarosch
Javier Bordallo
Thomas Sommer
P2860
P2888
P3181
P356
10.1038/NCB746
P407
P577
2002-02-01T00:00:00Z
P6179
1034773057