Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
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 degradationThe RBCC gene RFP2 (Leu5) encodes a novel transmembrane E3 ubiquitin ligase involved in ERADDefining 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 substratesMannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsA ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of ParkinA luminal flavoprotein in endoplasmic reticulum-associated degradationCYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor receptor, AMFR) and CHIP E3 ligasesThe TRC8 E3 ligase ubiquitinates MHC class I molecules before dislocation from the ERHuman XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiPUbiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradationRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membraneCytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'A deubiquitinase negatively regulates retro-translocation of nonubiquitinated substratesHRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradationMultiprotein 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 siteE2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell systemHECT and RING finger families of E3 ubiquitin ligases at a glanceHIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanismsStructure of human ubiquitin-conjugating enzyme E2 G2 (UBE2G2/UBC7)One step at a time: endoplasmic reticulum-associated degradationAn amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machineryUbiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3Rheumatoid arthritis as a hyper-endoplasmic-reticulum-associated degradation diseaseTargeting p97 to Disrupt Protein Homeostasis in CancerUbiquitylation of an ERAD substrate occurs on multiple types of amino acidsGlycoprotein Quality Control and Endoplasmic Reticulum StressRecent technical developments in the study of ER-associated degradationSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationMechanisms for quality control of misfolded transmembrane proteinsUbiquitin ligases in cholesterol metabolismThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyUbiquitination-induced fluorescence complementation (UiFC) for detection of K48 ubiquitin chains in vitro and in live cellsAllosteric Activation of E2-RING Finger-Mediated Ubiquitylation by a Structurally Defined Specific E2-Binding Region of gp78Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2Role of endoplasmic reticulum stress in rheumatoid arthritis pathogenesis.
P2860
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P248
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P2860
Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
description
2004 nî lūn-bûn
@nan
2004 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի հունվարին 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
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@ast
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en-gb
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@nl
type
label
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@ast
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en-gb
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@nl
prefLabel
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@ast
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en-gb
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@nl
P2093
P2860
P921
P3181
P356
P1476
Human HRD1 is an E3 ubiquitin ...... from the endoplasmic reticulum
@en
P2093
Emmanuel Wiertz
Gerco Hassink
Joseph Roitelman
Rachel Avner
Ram Doolman
Sjaak van Voorden
Swapna Thanedar
Vincent Chau
P2860
P304
P3181
P356
10.1074/JBC.M307453200
P407
P577
2004-01-30T00:00:00Z