Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
about
TEB4 is a C4HC3 RING finger-containing ubiquitin ligase of the endoplasmic reticulumEndoplasmic reticulum stress and Parkinson's disease: the role of HRD1 in averting apoptosis in neurodegenerative diseaseHuman HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulumLuman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response elementDerlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradationA ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of ParkinA novel protein, Luman/CREB3 recruitment factor, inhibits Luman activation of the unfolded protein responseCytoplasmic destruction of p53 by the endoplasmic reticulum-resident ubiquitin ligase 'Synoviolin'Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Ubiquitination of serine, threonine, or lysine residues on the cytoplasmic tail can induce ERAD of MHC-I by viral E3 ligase mK3Synoviolin/Hrd1, an E3 ubiquitin ligase, as a novel pathogenic factor for arthropathyRheumatoid arthritis as a hyper-endoplasmic-reticulum-associated degradation diseaseMelanoma and the Unfolded Protein ResponseSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationThe delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiologyEndoplasmic Reticulum Stress Is a Determinant of Retrovirus-Induced Spongiform NeurodegenerationDeterminants of RING-E2 fidelity for Hrd1p, a membrane-anchored ubiquitin ligase.Association of the SEL1L protein transmembrane domain with HRD1 ubiquitin ligase regulates ERAD-LInositol 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+AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradationSuppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stressAntiviral activity of a small molecule deubiquitinase inhibitor occurs via induction of the unfolded protein responseWFS1-deficiency increases endoplasmic reticulum stress, impairs cell cycle progression and triggers the apoptotic pathway specifically in pancreatic beta-cellsEssential role of synoviolin in embryogenesisE3 ubiquitin ligase synoviolin is involved in liver fibrogenesisThe E3 ubiquitin ligases Hrd1 and gp78 bind to and promote cholera toxin retro-translocation.Protective unfolded protein response in human pancreatic beta cells transplanted into mice.Role of interleukin 17 in arthritis chronicity through survival of synoviocytes via regulation of synoviolin expression.Transcriptional profiling of Plasmodium falciparum parasites from patients with severe malaria identifies distinct low vs. high parasitemic clusters.Glucocorticoid-induced Leucine zipper 1 stimulates the epithelial sodium channel by regulating serum- and glucocorticoid-induced kinase 1 stability and subcellular localization.Herp regulates Hrd1-mediated ubiquitylation in a ubiquitin-like domain-dependent manner.Exposed hydrophobicity is a key determinant of nuclear quality control degradation.Effects of oxidative stress on the solubility of HRD1, a ubiquitin ligase implicated in Alzheimer's diseaseGefitinib and Erlotinib Lead to Phosphorylation of Eukaryotic Initiation Factor 2 Alpha Independent of Epidermal Growth Factor Receptor in A549 CellsSEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.Experimental study of the protective effects of SYVN1 against diabetic retinopathyFamilial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Microarray based analysis of temperature and oxidative stress induced messenger RNA in Schistosoma mansoni.The ER membrane-anchored ubiquitin ligase Hrd1 is a positive regulator of T-cell immunity.
P2860
Q24292812-CE733C49-6AAA-4591-8DBB-AE31AC8AA25CQ24293694-D561588A-3B30-45B9-BF0F-2752EC16EE40Q24298901-80265A3D-F31D-4ADA-999D-1F5B53C05E08Q24301000-8307C598-D91C-497D-9AE5-FDE830C8FC24Q24302539-D0496A57-4256-49C4-8BBE-03EB2B15491EQ24308676-08A40D17-8BFF-4DAD-9385-747E02A656EFQ24317491-9C5183BA-B6E0-42E8-8295-FCC45AE5E32AQ24336917-7610EDB7-D6D8-4896-8176-07D87D5B9DAAQ24530318-7D2DACCB-3CFC-4110-88DA-AFD9A9D5DB0FQ24683139-ECA8528B-7A5E-49C6-BF55-185BE41E3806Q24684755-6A57A1B0-8820-4A9B-9ED5-0C6839811B37Q24812528-70E14218-BAA8-4414-A98A-54AFBF5DA664Q26765426-8C71D567-F0AC-4831-97BC-46FCD5F84D5FQ26824733-E59586CE-AC43-4CAD-9E81-315EA8A6BAF9Q27015793-9AFA985B-85AF-4FB4-8B2D-B5C95DB669F9Q27487568-BFA7240A-48E2-4124-A34F-618F71DA91DDQ27932421-5D5AA17D-540A-4251-9097-99D293609C52Q28119008-562FA318-F385-4EF6-9680-02F22D3ABFD5Q28187990-F4254112-0C0E-4E13-B797-F7073B0BEF68Q28279098-4AA3BF46-CCC2-4B6A-971F-9344E98B9B71Q28302176-5B0C6E7C-91DC-44C9-A333-91CCA5A03BB5Q28481001-403A6528-D329-4DC9-B891-05CF16C3F4CBQ28508342-D8374D24-150E-471E-BDC0-196370D56020Q28588247-616F4F5C-8237-4B07-807A-310208409D47Q28748731-24898330-5743-4483-9129-6C9956E4A674Q33571592-5EF40964-866B-470D-B12D-A0CE2DB15220Q33618964-C6D5BFAA-B7AF-48B5-A027-440C201738D5Q33728533-569F0AAD-1FEC-4D1C-B38E-CB89C9C95741Q34345090-DDA70CB5-40C1-4EB7-9221-6F27A3081D96Q34400942-A55E7CCE-934D-4C7D-9DB7-37EFECFBF2A7Q34568352-110A6EBC-B7CE-44DC-8C89-F998B1E4ED74Q35083477-88ABA991-56B6-481B-B34C-D90ECF0A6409Q35161700-C205674C-5DBD-4B6D-8F15-89F63D266C48Q35750388-5B06291D-8A2B-4E0B-BFF6-BF18B64C9834Q36119119-05B9FF0C-5AC9-452A-9ABD-B6D60AF18829Q36273653-796455C0-8138-4A24-BCD2-3837AE0F3A57Q36581422-FFD04C8D-3AE1-46E7-AECE-7B38394CEC51Q36647227-2BEA2D35-C09E-457A-9339-7C06B8EB033BQ36990847-CFA37F45-5FF5-4295-A352-17D9D83F0EBEQ37099446-06AABD5B-A0C7-4246-96E7-1FC0F80AD4D3
P2860
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
description
2002 nî lūn-bûn
@nan
2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի դեկտեմբերին 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
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@ast
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en-gb
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@nl
type
label
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@ast
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en-gb
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@nl
prefLabel
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@ast
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en-gb
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@nl
P2093
P2860
P921
P3181
P1433
P1476
Human HRD1 protects against ER stress-induced apoptosis through ER-associated degradation
@en
P2093
Mai Uesugi
Masataro Ishiguro
Yasuyuki Nomura
Yoshifumi Niinuma
P2860
P304
P3181
P356
10.1016/S0014-5793(02)03660-8
P407
P577
2002-12-01T00:00:00Z