Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.
about
HECT and RING finger families of E3 ubiquitin ligases at a glanceSelective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradationMolecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradationQuality control and fate determination of Hsp90 client proteinsProtein homeostasis at the plasma membraneProtein quality control in the nucleusPhenotypes on demand via switchable target protein degradation in multicellular organisms.Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation.Genome-wide functional profiling identifies genes and processes important for zinc-limited growth of Saccharomyces cerevisiae.Prefoldin Promotes Proteasomal Degradation of Cytosolic Proteins with Missense Mutations by Maintaining Substrate Solubility.Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.The yeast ubr1 ubiquitin ligase participates in a prominent pathway that targets cytosolic thermosensitive mutants for degradationRibosomal proteins produced in excess are degraded by the ubiquitin-proteasome systemA nucleus-based quality control mechanism for cytosolic proteinsUbiquitin ligases of the N-end rule pathway: assessment of mutations in UBR1 that cause the Johanson-Blizzard syndromeMicroarray analysis of peripheral blood lymphocytes from ALS patients and the SAFE detection of the KEGG ALS pathway.The N-end rule pathway and regulation by proteolysisSer(120) of Ubc2/Rad6 regulates ubiquitin-dependent N-end rule targeting by E3{alpha}/Ubr1The Type II Hsp40 Sis1 cooperates with Hsp70 and the E3 ligase Ubr1 to promote degradation of terminally misfolded cytosolic protein.The Mub1/Ubr2 ubiquitin ligase complex regulates the conserved Dsn1 kinetochore protein.Cytosolic aggregates perturb the degradation of nontranslocated secretory and membrane proteinsExposed hydrophobicity is a key determinant of nuclear quality control degradation.Protein targeting and degradation are coupled for elimination of mislocalized proteins.UBR1 promotes protein kinase quality control and sensitizes cells to Hsp90 inhibition.Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Absence of the Yeast Hsp31 Chaperones of the DJ-1 Superfamily Perturbs Cytoplasmic Protein Quality Control in Late Growth Phase.Degradation Signals for Ubiquitin-Proteasome Dependent Cytosolic Protein Quality Control (CytoQC) in YeastBiology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.A network of ubiquitin ligases is important for the dynamics of misfolded protein aggregates in yeast.The ubiquitin-proteasome system of Saccharomyces cerevisiae.Pharmacological Modulation of the N-End Rule Pathway and Its Therapeutic Implications.Border Safety: Quality Control at the Nuclear Envelope.Substrate recognition in nuclear protein quality control degradation is governed by exposed hydrophobicity that correlates with aggregation and insolubility.Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeastHsp70 targets a cytoplasmic quality control substrate to the San1p ubiquitin ligaseDegradation of newly synthesized polypeptides by ribosome-associated RACK1/c-Jun N-terminal kinase/eukaryotic elongation factor 1A2 complex.Specificity in the actions of the UBR1 ubiquitin ligase in the degradation of nuclear receptors.Quality control: quality control at the plasma membrane: one mechanism does not fit allProtein Quality Control by Molecular Chaperones in Neurodegeneration.How a disordered ubiquitin ligase maintains order in nuclear protein homeostasis
P2860
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P2860
Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@ast
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@en
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@nl
type
label
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@ast
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@en
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@nl
altLabel
Ubr1 and Ubr2 function in a qu ...... of unfolded cytosolic proteins
@en
prefLabel
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@ast
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@en
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@nl
P2093
P2860
P3181
P356
P1476
Ubr1 and Ubr2 function in a qu ...... f unfolded cytosolic proteins.
@en
P2093
Atin K Mandal
Avrom J Caplan
Douglas M Cyr
Hong Yu Ren
Jill Johnson
Katie J Mayo
Kenneth Wu
Maria A Theodoraki
Nadinath B Nillegoda
Rasheda Sultana
P2860
P304
P3181
P356
10.1091/MBC.E10-02-0098
P407
P577
2010-07-01T00:00:00Z