The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
about
Rkr1/Ltn1 Ubiquitin Ligase-mediated Degradation of Translationally Stalled Endoplasmic Reticulum Proteins.Subcellular Fractionation Analysis of the Extraction of Ubiquitinated Polytopic Membrane Substrate during ER-Associated DegradationDegradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in YeastTransmembrane domain quality control systems operate at the endoplasmic reticulum and Golgi apparatusA Conserved C-terminal Element in the Yeast Doa10 and Human MARCH6 Ubiquitin Ligases Required for Selective Substrate Degradation.Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiaeProteolytic regulation of metabolic enzymes by E3 ubiquitin ligase complexes: lessons from yeast.Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon.Glycosylation-directed quality control of protein folding.Bioinformatics analysis identifies several intrinsically disordered human E3 ubiquitin-protein ligases.The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.Protein quality and quantity control at the yeast ER.Diminished Ost3-dependent N-glycosylation of the BiP nucleotide exchange factor Sil1 is an adaptive response to reductive ER stress.
P2860
Q35883810-E27BF306-2828-40CE-AF95-963B8831CD4BQ35915784-F842493D-E91B-4AE8-8006-7D53F65E7BD2Q36016016-95878E96-8DDC-4C4A-AD4E-AD4DA645C7B9Q36338280-CA5B1F06-B9F4-42E1-AB40-583DC629D0A5Q37065990-0DC45B11-1DD3-45BE-9EF2-EF0A9D2E8B99Q37087744-E09D1498-702F-4ABA-8E38-966D81627B81Q38585206-952524BE-9C63-481C-B3CD-B66CC921CB96Q38604728-7C898152-7D64-4271-9ED1-C1450975C80BQ38606832-FA2206D8-CA3F-42D0-AE4D-35B7D75918B0Q38842180-939FDD52-A730-47E0-9C53-283B997733BDQ38979904-E82115F1-8411-453B-9285-619C7596955FQ43195465-CF54887D-DDF2-4F96-A275-3E79E90E45C1Q47433965-978AD7D5-CBEA-4F20-A4C3-E18ECE6C5DF7
P2860
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
description
2015 nî lūn-bûn
@nan
2015 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@ast
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@en
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.
@nl
type
label
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@ast
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@en
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.
@nl
prefLabel
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@ast
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@en
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron.
@nl
P2093
P2860
P3181
P356
P1476
The yeast ERAD-C ubiquitin ligase Doa10 recognizes an intramembrane degron
@en
P2093
Felix A Ebner
Hiroko Shimada-Kreft
Stefan G Kreft
P2860
P304
P3181
P356
10.1083/JCB.201408088
P407
P577
2015-04-01T00:00:00Z