Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
about
Recent technical developments in the study of ER-associated degradationHow Polyomaviruses Exploit the ERAD Machinery to Cause InfectionKey steps in ERAD of luminal ER proteins reconstituted with purified componentsThe yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degronAutoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.A Complex of Htm1 and the Oxidoreductase Pdi1 Accelerates Degradation of Misfolded Glycoproteins.A bacterial toxin and a nonenveloped virus hijack ER-to-cytosol membrane translocation pathways to cause diseaseCleaning up in the endoplasmic reticulum: ubiquitin in chargeTMEM129 is a Derlin-1 associated ERAD E3 ligase essential for virus-induced degradation of MHC-I.Apolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.Derlin-1 regulates mutant VCP-linked pathogenesis and endoplasmic reticulum stress-induced apoptosis.The Toxicity of a Novel Antifungal Compound Is Modulated by Endoplasmic Reticulum-Associated Protein Degradation Components.The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.Familial prion protein mutants inhibit Hrd1-mediated retrotranslocation of misfolded proteins by depleting misfolded protein sensor BiP.Direct and essential function for Hrd3 in ER-associated degradation.The non-canonical mitochondrial inner membrane presequence translocase of trypanosomatids contains two essential rhomboid-like proteins.Lipid disequilibrium disrupts ER proteostasis by impairing ERAD substrate glycan trimming and dislocation.Quality control: ER-associated degradation: protein quality control and beyondRegulation of Endoplasmic Reticulum-Associated Protein Degradation (ERAD) by Ubiquitin.Proteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.Glycosylation-directed quality control of protein folding.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.Snapshot: implications for melatonin in endoplasmic reticulum homeostasis.Mitochondrial protein import in trypanosomes: Expect the unexpected.The Biology and Underlying Mechanisms of Cross-Presentation of Exogenous Antigens on MHC-I Molecules.Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3.Transmembrane helix hydrophobicity is an energetic barrier during the retrotranslocation of integral membrane ERAD substratesConserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).Unfolded Protein Response of the Endoplasmic Reticulum in Tumor Progression and Immunogenicity.N-terminal lysines are essential for protein translocation via a modified ERAD system in complex plastids.Mutual interaction between oxidative stress and endoplasmic reticulum stress in the pathogenesis of diseases specifically focusing on non-alcoholic fatty liver disease
P2860
Q26823514-47C7008B-60BD-4969-A343-4B10D3EC184FQ27468807-DD506A07-63E8-442D-8B82-7E2ED3915A98Q27929992-86BCA8A3-ADBF-42D6-BB90-F7CE03D71137Q27933477-B7F9BFEC-1EAB-47E3-818D-A7807E865BA4Q27935283-2D58B50B-92A7-4167-8E35-EC7CDBBDD7F0Q27935416-75187C3B-5C3B-4C56-8169-4E8D0CAFBEBCQ28087358-7FF5FBC2-EA61-4708-93CF-9553DEE18D8BQ28237362-2EB0E354-6A64-4B4C-B317-210C67B97CC8Q29871423-FC516E4B-178F-4068-A472-F042D24036ABQ33858526-4347288C-B133-4F28-B7A3-E6BFB780B550Q34256709-A311E06A-67A7-4827-BF19-CBF6D2116AA4Q34505078-DB7DA659-EADB-4135-86ED-122FAB4CA0DBQ34960632-690B148D-4F4A-462B-8BA5-CE6E06FCA692Q35175501-5D2F5F8B-0C8A-4211-BFF1-7FCBA9B57E7EQ36560259-5EADFCAC-542B-445C-88B6-5D26AEAFFD7FQ36581422-E2C1962A-2D9B-4927-9744-B22CABE684B5Q36957336-D58667CA-E4A8-4352-A76D-3556AF6D0241Q37533229-41010782-3184-4E81-985F-DBF04CC9EDC8Q37583253-5FC6C708-D527-46CF-93C2-47E7C88D4124Q38196654-48839463-2834-4E2B-BFED-22F3CAD1F02CQ38237571-8D931B85-D776-40C1-87D8-7EFE5C8415B7Q38585206-A039EAC5-08B5-4543-A3FB-73F4ADCB80F8Q38606832-0715633D-9F12-43EA-A814-A5505D49F52FQ38979904-ED602F6F-3970-42CB-B9CA-0A0228487D81Q38985173-F0BAEB70-8D84-494C-B46F-AC399CB6ADC5Q39038972-EDF2C3B3-C29D-458D-B4D8-13A457726A70Q39104926-5EC995D0-F781-4EAB-8D6A-A421EFEBEC11Q41597296-23854263-8C3E-419B-A6B0-F84A09D453E3Q41662080-6FA595C3-AF36-4362-9AC9-A24A02EC8C35Q47924713-57F2E914-FDD6-4071-A24F-C677CA9DC825Q50073383-B32EF6E6-1C01-4225-91FF-FB01D3709397Q50452503-C9522CF2-CA6E-49FD-B8C9-3F047B41418CQ58604208-F3653CD1-33AC-49F1-9758-D25F0DFD2F77
P2860
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@ast
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@en
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@nl
type
label
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@ast
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@en
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@nl
prefLabel
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@ast
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@en
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@nl
P2860
P3181
P356
P1433
P1476
Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.
@en
P2093
Martin Mehnert
Thomas Sommer
P2860
P2888
P3181
P356
10.1038/NCB2882
P407
P577
2014-01-01T00:00:00Z
P6179
1024073539