Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.
about
A SEL1L mutation links a canine progressive early-onset cerebellar ataxia to the endoplasmic reticulum-associated protein degradation (ERAD) machineryMultilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting stepsA high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradationDefining human ERAD networks through an integrative mapping strategySEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulum-associated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substratesDerlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradationRegulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsA luminal flavoprotein in endoplasmic reticulum-associated degradationThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the EROS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERADHuman OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycansAn endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptorsHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPProtein 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 ERSEPS1 protects RAW264.7 cells from pharmacological ER stress agent-induced apoptosisEDEM is involved in retrotranslocation of ricin from the endoplasmic reticulum to the cytosolE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemHIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanismsInhibition of p97-dependent protein degradation by Eeyarestatin IMurine 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 mK3Glycoprotein Quality Control and Endoplasmic Reticulum StressSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyThe E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis in miceStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexStructure-function relations, physiological roles, and evolution of mammalian ER-resident selenoproteins.The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitmentThe ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48pA proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates.Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-LSignal peptide peptidase is required for dislocation from the endoplasmic reticulumThe role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradationKaposi's sarcoma-associated herpesvirus K7 induces viral G protein-coupled receptor degradation and reduces its tumorigenicitySecretion of novel SEL1L endogenous variants is promoted by ER stress/UPR via endosomes and shed vesicles in human cancer cellsThe AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptorBruton's Tyrosine Kinase (BTK) and Vav1 contribute to Dectin1-dependent phagocytosis of Candida albicans in macrophages
P2860
Q21092417-F37168F4-DC5E-4710-9F79-6EF68D13AB91Q21131559-AE12B993-1A03-438D-B419-FBEF72F8DDB5Q24297209-9D8FD69C-EA31-4128-A2B7-06BF841F899FQ24298439-7B6F9E37-C277-4B17-B11C-24F18B8FB8BDQ24298501-6C73C6AA-BCC5-4CAD-8A63-F81F37F73505Q24302539-70DAE184-15B0-45C1-91FF-4BA0BC78BF5BQ24304415-FB56093E-8CB2-440E-88D7-07F8167A3C68Q24306408-A61C6F94-2902-46AF-8924-50FD33A01C4AQ24309147-F25C4A27-FEF1-4113-8A17-2A53814096D4Q24311488-EED0B8A9-547B-43F6-BC25-9EFEEC21514FQ24312778-FD4F7A0E-3457-4337-B181-3412180D08C3Q24313146-7E050781-45EE-4254-B3A9-C7321DF12DF5Q24314540-5C8E6B81-9DED-4E17-A681-5C1B51B303E6Q24316328-C541D159-B903-4FBD-95E8-DD3704112427Q24322026-D74F6EA5-9251-4124-B565-7F1392F55D6DQ24323509-768FB853-E26E-4796-A578-17766EBE435EQ24338858-11049094-DFB8-4DCA-A4C6-224A46AAB769Q24541550-4C6E0530-FD13-4ED8-86C9-23B4CCA40A5AQ24554438-7366B745-2C90-4030-9D0B-3190046D3526Q24619066-3F818167-54AD-4FE9-8A9C-C43E8A362DCDQ24648805-BF6BFDD4-D767-44F2-A923-D2DDA15029F7Q24674111-82AA9D0E-1D33-42A7-AEF3-C288998763A8Q24683139-CD571B42-5139-495C-8E96-0EABBA2AF98DQ26801535-D85AC5E1-493C-4D7C-8288-EF72C3AA3B8EQ26824733-A561C86E-AD35-421D-9BD1-2D2B6EFD2C85Q27015793-7C3B06B7-82AB-4302-9AA5-F189327019BBQ27314641-7EA28495-5599-4F0A-8697-8455287AA772Q27676812-0C242F0B-B659-456C-8B1D-671B1486819DQ27863410-157E63D3-D51C-4000-B6D1-CA3BDED1480BQ27932818-5CE13E95-51F1-41C7-87D8-62761A0B12B5Q27934285-019EE73A-C743-4C96-8593-B89618DA487DQ27934511-9CD94C22-CC62-4AC3-AF13-2CA6ED205A8EQ27938831-4C9C0756-CA8B-49B4-BB66-775B06FC583EQ28119008-0A6F8AB2-171D-456B-8E51-DF5F90048907Q28243253-90A264BB-6027-4158-8EAC-76E41ED9FB54Q28264480-1471BB34-9B94-4C2B-8068-33C2C6400BE1Q28473623-1D5A33D9-8FC8-4703-8576-213DEF183766Q28477193-2D425784-B7CD-40C0-81DF-E176A38AE210Q28507832-6D8052EA-5A87-41C0-9D63-00F0DEC05534Q28534361-BBAE8BA3-5CE8-4C2A-88DF-79B2861D1789
P2860
Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.
description
2005 nî lūn-bûn
@nan
2005 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
name
Multiprotein complexes that li ...... endoplasmic reticulum membrane
@nl
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@ast
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en-gb
type
label
Multiprotein complexes that li ...... endoplasmic reticulum membrane
@nl
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@ast
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en-gb
prefLabel
Multiprotein complexes that li ...... endoplasmic reticulum membrane
@nl
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@ast
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en-gb
P2860
P356
P1476
Multiprotein complexes that li ...... ndoplasmic reticulum membrane.
@en
P2093
Brendan N Lilley
Hidde L Ploegh
P2860
P304
14296-14301
P356
10.1073/PNAS.0505014102
P407
P577
2005-09-26T00:00:00Z