A membrane protein required for dislocation of misfolded proteins from the ER
about
Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting stepsTEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulumA high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradationA membrane protein complex mediates retro-translocation from the ER lumen into the cytosolSEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesSimultaneous induction of the four subunits of the TRAP complex by ER stress accelerates ER degradationDerlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradationA complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteinsSignal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1uRegulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradationMannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ERA functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathwayProtein disulphide isomerase is required for signal peptide peptidase-mediated protein degradationThe otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ERRNF185 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 membraneHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationCaveolin-1 interacts with Derlin-1 and promotes ubiquitination and degradation of cyclooxygenase-2 via collaboration with p97 complexSignal-peptide-mediated translocation is regulated by a p97-AIRAPL complexMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding siteThe retrotranslocation protein Derlin-1 binds peptide:N-glycanase to the endoplasmic reticulumEDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosolInhibition of p97-dependent protein degradation by Eeyarestatin IOne step at a time: endoplasmic reticulum-associated degradationMurine polyomavirus requires the endoplasmic reticulum protein Derlin-2 to initiate infectionUbiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3Ubiquitylation of an ERAD substrate occurs on multiple types of amino acidsIdentifying the ERAD ubiquitin E3 ligases for viral and cellular targeting of MHC class IGlycoprotein Quality Control and Endoplasmic Reticulum StressProtein folding and quality control in the ERRecent technical developments in the study of ER-associated degradationEndoplasmic reticulum-mediated protein quality control in ArabidopsisSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationThe role of ubiquitylation in immune defence and pathogen evasionAlternative Antigen Processing for MHC Class I: Multiple Roads Lead to RomeRoad to ruin: targeting proteins for degradation in the endoplasmic reticulum
P2860
Q21131559-0D8DD9E6-C245-490D-9A7C-B5608BD51064Q24292812-53A79DE6-B527-44E4-B80B-C08687FFDC07Q24297209-B7C19812-F4CF-404D-9D9E-46E82766A20FQ24297732-D4E5098A-91D3-4250-9604-D417957D3F83Q24298501-A3FCB38C-BBB9-4821-8B0B-07A6627D7A75Q24300776-0415AD32-8E7D-43C6-A0DD-5E48495D485BQ24302539-170059E6-5687-47CB-91AB-5038A94FEFE7Q24303569-81458B2C-EB3A-45EC-BE96-53FCD23A4938Q24304271-275D2D36-01B9-497B-82CD-430B97CD463BQ24304415-2C62EC8A-AA8F-4125-AFCA-11CFA952181AQ24305231-6A287590-77E5-4A54-9942-FCFCD149A7CDQ24306408-4B11E1B3-E421-4874-91D9-C8D42FE18C54Q24311488-0CDDD8D6-580F-48E8-96D0-FBE9616EDCFEQ24315993-EB955EE5-39F0-4C9C-848C-0C48B0BFACD0Q24322026-2E379F5A-927C-4BDC-B5B0-A13A46F0234AQ24323509-37B1E374-754B-4F0E-B7E4-739D571E5734Q24323658-781C3BF9-F235-4AEB-A447-A14659EBDE03Q24324707-7A3D1C86-630A-4DC1-8F8C-106D260D8425Q24336904-2C03EA1D-2D5B-498F-9984-D5F8012FC8A8Q24337606-CC934CB4-4623-40C1-9590-2FB8FF10B757Q24337689-74A691A8-8EB1-44FF-81D0-F9E85CFE6838Q24338887-B2DC9CDD-154C-4472-99F0-C6F2B2562A57Q24530318-8791B238-892F-4418-8905-B00C2AB06B0FQ24535990-D6C2779B-95A6-4FBD-B076-BA46D989435AQ24536195-A03A0C0C-947B-4B23-8DCD-A0E7D01AC73BQ24541550-32571EDB-D7D2-4657-9E57-9E4E758808E3Q24648805-2AC604FB-9299-4F2F-A534-09E17DFA9B45Q24658302-70A56967-344F-4EC0-85B4-A9C5B44EFD89Q24674111-61E28A6A-9485-4705-B02C-1CAE0E5DE331Q24683139-E430633E-70E8-48B7-A483-C8B5EF8AEA12Q26781978-D686E687-41B9-402A-9EB4-6F87A0969B8CQ26799569-35F97BF5-189F-4A66-BBF7-784726B58C65Q26801535-3FDFF82F-FEB6-4D22-B379-84EB194D3215Q26823157-29365619-3340-43CA-8F9D-E6AB5DCE8693Q26823514-65366FE5-F291-4406-8849-F9A923336E44Q26824018-D53A0D64-4851-4FB7-BEB9-6F29397B3392Q26824733-54BE572C-6029-45C9-B080-2DF0E97A46E9Q26860775-F387EDA8-9048-4E35-9658-45D5AEB3FAE4Q26864074-6004D1E6-5C92-474E-87E7-6D110A24E293Q26866096-9881FC14-5473-4E59-94E0-BBAF9E8209AF
P2860
A membrane protein required for dislocation of misfolded proteins from the ER
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A membrane protein required for dislocation of misfolded proteins from the ER
@ast
A membrane protein required for dislocation of misfolded proteins from the ER
@en
A membrane protein required for dislocation of misfolded proteins from the ER
@en-gb
A membrane protein required for dislocation of misfolded proteins from the ER
@nl
type
label
A membrane protein required for dislocation of misfolded proteins from the ER
@ast
A membrane protein required for dislocation of misfolded proteins from the ER
@en
A membrane protein required for dislocation of misfolded proteins from the ER
@en-gb
A membrane protein required for dislocation of misfolded proteins from the ER
@nl
prefLabel
A membrane protein required for dislocation of misfolded proteins from the ER
@ast
A membrane protein required for dislocation of misfolded proteins from the ER
@en
A membrane protein required for dislocation of misfolded proteins from the ER
@en-gb
A membrane protein required for dislocation of misfolded proteins from the ER
@nl
P2860
P3181
P356
P1433
P1476
A membrane protein required for dislocation of misfolded proteins from the ER
@en
P2093
Brendan N Lilley
Hidde L Ploegh
P2860
P2888
P304
P3181
P356
10.1038/NATURE02592
P407
P577
2004-06-24T00:00:00Z
P5875
P6179
1051268133