A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
about
Identification of a functional docking site in the Rpn1 LRR domain for the UBA-UBL domain protein Ddi1UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnoverUbiquitin receptor proteins hHR23a and hPLIC2 interactThe otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ERMultiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane.Folding-competent and folding-defective forms of ricin A chain have different fates after retrotranslocation from the endoplasmic reticulumUbiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradationOne step at a time: endoplasmic reticulum-associated degradationDimerization of ubiquilin is dependent upon the central region of the protein: evidence that the monomer, but not the dimer, is involved in binding presenilinsThe cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome systemRing of Change: CDC48/p97 Drives Protein Dynamics at ChromatinThe recognition of ubiquitinated proteins by the proteasomeAffinity Makes the Difference: Nonselective Interaction of the UBA Domain of Ubiquilin-1 with Monomeric Ubiquitin and Polyubiquitin ChainsThe Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding DomainDoa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domainSec61p is part of the endoplasmic reticulum-associated degradation machineryGenome-wide analysis identifies MYND-domain protein Mub1 as an essential factor for Rpn4 ubiquitylation.Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.A proteasomal ATPase contributes to dislocation of endoplasmic reticulum-associated degradation (ERAD) substrates.Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domainCentrin/Cdc31 is a novel regulator of protein degradation.Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulumDegradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1.Ubx2 links the Cdc48 complex to ER-associated protein degradation.An evolutionarily conserved pathway controls proteasome homeostasisThe role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradationERAD: the long road to destructionAAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradationEeyarestatin 1 interferes with both retrograde and anterograde intracellular trafficking pathwaysA genome-wide synthetic dosage lethality screen reveals multiple pathways that require the functioning of ubiquitin-binding proteins Rad23 and Dsk2A genome-wide screen identifies Yos9p as essential for ER-associated degradation of glycoproteins.Membrane and soluble substrates of the Doa10 ubiquitin ligase are degraded by distinct pathwaysRNA interference analysis of Legionella in Drosophila cells: exploitation of early secretory apparatus dynamics.Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A.Ubiquitylation in ERAD: reversing to go forward?Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48.The Unfolded Protein Response, Degradation from Endoplasmic Reticulum and CancerGrowth-based determination and biochemical confirmation of genetic requirements for protein degradation in Saccharomyces cerevisiae
P2860
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P2860
A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
A genomic screen identifies Ds ...... s of ER-associated degradation
@ast
A genomic screen identifies Ds ...... s of ER-associated degradation
@en
A genomic screen identifies Ds ...... of ER-associated degradation.
@nl
type
label
A genomic screen identifies Ds ...... s of ER-associated degradation
@ast
A genomic screen identifies Ds ...... s of ER-associated degradation
@en
A genomic screen identifies Ds ...... of ER-associated degradation.
@nl
prefLabel
A genomic screen identifies Ds ...... s of ER-associated degradation
@ast
A genomic screen identifies Ds ...... s of ER-associated degradation
@en
A genomic screen identifies Ds ...... of ER-associated degradation.
@nl
P2093
P2860
P3181
P356
P1433
P1476
A genomic screen identifies Ds ...... s of ER-associated degradation
@en
P2093
Antje Schaefer
Balasubrahmanyam Medicherla
Dieter H Wolf
Zlatka Kostova
P2860
P304
P3181
P356
10.1038/SJ.EMBOR.7400164
P407
P577
2004-05-28T00:00:00Z