Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
about
Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation stepsRNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)Recent technical developments in the study of ER-associated degradationEndoplasmic reticulum-mediated protein quality control in ArabidopsisSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationRoad to ruin: targeting proteins for degradation in the endoplasmic reticulumStructural and Biochemical Basis of Yos9 Protein Dimerization and Possible Contribution to Self-association of 3-Hydroxy-3-methylglutaryl-Coenzyme A Reductase Degradation Ubiquitin-Ligase ComplexThe predator becomes the prey: regulating the ubiquitin system by ubiquitylation and degradationRecognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.Autoubiquitination of the Hrd1 Ligase Triggers Protein Retrotranslocation in ERAD.Yos9p assists in the degradation of certain nonglycosylated proteins from the endoplasmic reticulumN-terminal acetylation of the yeast Derlin Der1 is essential for Hrd1 ubiquitin-ligase activity toward luminal ER substrates.Der1 promotes movement of misfolded proteins through the endoplasmic reticulum membrane.Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.Arms Race between Enveloped Viruses and the Host ERAD MachineryCleaning up in the endoplasmic reticulum: ubiquitin in chargeDerlin-1 deficiency is embryonic lethal, Derlin-3 deficiency appears normal, and Herp deficiency is intolerant to glucose load and ischemia in miceModularity of the Hrd1 ERAD complex underlies its diverse client range.Apolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum.Misfolded proteins induce aggregation of the lectin Yos9.How viruses hijack the ERAD tuning machinery.WNP: a novel algorithm for gene products annotation from weighted functional networks.Herp regulates Hrd1-mediated ubiquitylation in a ubiquitin-like domain-dependent manner.The Unfolded Protein Response, Degradation from Endoplasmic Reticulum and CancerThe protein translocation systems in plants - composition and variability on the example of Solanum lycopersicumMolecular chaperones and substrate ubiquitination control the efficiency of endoplasmic reticulum-associated degradation.The virulence of the opportunistic fungal pathogen Aspergillus fumigatus requires cooperation between the endoplasmic reticulum-associated degradation pathway (ERAD) and the unfolded protein response (UPR).The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Ubiquitin-dependent protein degradation at the yeast endoplasmic reticulum and nuclear envelope.Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.Aberrant substrate engagement of the ER translocon triggers degradation by the Hrd1 ubiquitin ligase.The ubiquitin-proteasome system of Saccharomyces cerevisiae.The endoplasmic reticulum-associated degradation pathways of budding yeast.Cleaning up: ER-associated degradation to the rescue.Crystal structure of SEL1L: Insight into the roles of SLR motifs in ERAD pathway.Effects of a defective endoplasmic reticulum-associated degradation pathway on the stress response, virulence, and antifungal drug susceptibility of the mold pathogen Aspergillus fumigatusA stalled retrotranslocation complex reveals physical linkage between substrate recognition and proteasomal degradation during ER-associated degradation
P2860
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P2860
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
description
2009 nî lūn-bûn
@nan
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@ast
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@en
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@nl
type
label
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@ast
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@en
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@nl
prefLabel
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@ast
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@en
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@nl
P2093
P3181
P1433
P1476
Usa1 functions as a scaffold of the HRD-ubiquitin ligase.
@en
P2093
Anja Schütz
Christian Hirsch
Corinna Volkwein
Jennifer Hanna
Sabine C Horn
Thomas Sommer
P304
P3181
P356
10.1016/J.MOLCEL.2009.10.015
P407
P577
2009-12-11T00:00:00Z