Modularity of the Hrd1 ERAD complex underlies its diverse client range.
about
Endoplasmic reticulum-mediated protein quality control in ArabidopsisMechanisms for quality control of misfolded transmembrane proteinsA Cdc48p-associated factor modulates endoplasmic reticulum-associated degradation, cell stress, and ubiquitinated protein homeostasisYos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumThe expression of a xylanase targeted to ER-protein bodies provides a simple strategy to produce active insoluble enzyme polymers in tobacco plantsQuality and quantity control at the endoplasmic reticulum.Ricin trafficking in cellsA context-independent N-glycan signal targets the misfolded extracellular domain of Arabidopsis STRUBBELIG to endoplasmic-reticulum-associated degradationExposed hydrophobicity is a key determinant of nuclear quality control degradation.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Expression of endoplasmic reticulum stress-related factors in the retinas of diabetic ratsRole of the unfolded protein response in regulating the mucin-dependent filamentous-growth mitogen-activated protein kinase pathway.Routing misfolded proteins through the multivesicular body (MVB) pathway protects against proteotoxicity.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesiRhom1 regulates proteasome activity via PAC1/2 under ER stressAberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.The endoplasmic reticulum-associated degradation pathways of budding yeast.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Vertebrate protein glycosylation: diversity, synthesis and function.Sorting things out through endoplasmic reticulum quality control.ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum.Protein quality control in the ER: balancing the ubiquitin checkbook.Ubiquitin-dependent sorting in endocytosis.The safety dance: biophysics of membrane protein folding and misfolding in a cellular contextGlycosylation-directed quality control of protein folding.Endoplasmic reticulum stress-induced degradation of DNAJB12 stimulates BOK accumulation and primes cancer cells for apoptosis.Signalling mucin Msb2 Regulates adaptation to thermal stress in Candida albicans.Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex formation for ER-associated degradation (ERAD).ERAD-dependent control of the Wnt secretory factor Evi.Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.Arabidopsis DOK1 encodes a functional dolichol kinase involved in reproduction.
P2860
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P2860
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
description
2010 nî lūn-bûn
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2010 թուականի Մարտին հրատարակուած գիտական յօդուած
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2010 թվականի մարտին հրատարակված գիտական հոդված
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年學術文章
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name
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@ast
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
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type
label
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@ast
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@en
prefLabel
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@ast
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@en
P2093
P2860
P356
P1476
Modularity of the Hrd1 ERAD complex underlies its diverse client range.
@en
P2093
Davis T W Ng
Kazue Kanehara
P2860
P304
P356
10.1083/JCB.200907055
P407
P577
2010-03-01T00:00:00Z