Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.
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ArPIKfyve regulates Sac3 protein abundance and turnover: disruption of the mechanism by Sac3I41T mutation causing Charcot-Marie-Tooth 4J disorderPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Genome-Wide Survey of Gut Fungi (Harpellales) Reveals the First Horizontally Transferred Ubiquitin Gene from a Mosquito HostParticle-rich cytoplasmic structure (PaCS): identification, natural history, role in cell biology and pathologyThe Proteasome Subunit Rpn8 Interacts with the Small Nucleolar RNA Protein (snoRNP) Assembly Protein Pih1 and Mediates Its Ubiquitin-independent Degradation in Saccharomyces cerevisiae.Mediation of organismal aging and somatic proteostasis by the germlineTargeting proteins for degradationUbiquitin-independent proteasomal degradationRegulation of proteasome activity in health and diseaseDisordered proteinaceous machinesThe intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathwayNucleolar stress induces ubiquitination-independent proteasomal degradation of PICT1 proteinDirect ubiquitin independent recognition and degradation of a folded protein by the eukaryotic proteasomes-origin of intrinsic degradation signals.Understanding the mechanism of proteasome 20S core particle gating.NAD(P)H quinone-oxydoreductase 1 protects eukaryotic translation initiation factor 4GI from degradation by the proteasome.Ubiquitin not only serves as a tag but also assists degradation by inducing protein unfolding.Mcl-1 ubiquitination: unique regulation of an essential survival protein.Analysis of proteasomal proteolysis during the in vitro metacyclogenesis of Trypanosoma cruziAssembly, structure, and function of the 26S proteasome.Plastidial starch phosphorylase in sweet potato roots is proteolytically modified by protein-protein interaction with the 20S proteasomeAltered composition of liver proteasome assemblies contributes to enhanced proteasome activity in the exceptionally long-lived naked mole-ratRegulating the 20S proteasome ubiquitin-independent degradation pathway.Transcriptomic analysis of the salivary glands of an invasive whiteflyParadigms of protein degradation by the proteasome.PaCS is a novel cytoplasmic structure containing functional proteasome and inducible by cytokines/trophic factors.Timely activation of budding yeast APCCdh1 involves degradation of its inhibitor, Acm1, by an unconventional proteolytic mechanism.Cooperation between an intrinsically disordered region and a helical segment is required for ubiquitin-independent degradation by the proteasomeThe 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.Facilitated Tau Degradation by USP14 Aptamers via Enhanced Proteasome Activity.Proteasomes and protein conjugation across domains of life.Compromising the 19S proteasome complex protects cells from reduced flux through the proteasome.Control of Pim2 kinase stability and expression in transformed human haematopoietic cellsDistribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.Subcellular distribution and dynamics of active proteasome complexes unraveled by a workflow combining in vivo complex cross-linking and quantitative proteomics.Degradation of NF-κB, p53 and other regulatory redox-sensitive proteins by thiol-conjugating and -nitrosylating drugs in human tumor cells.Regulation of Proteasomal Degradation by Modulating Proteasomal Initiation RegionsProteasome regulates turnover of toxic human amylin in pancreatic cells.Structural insights into proteasome activation by the 19S regulatory particle.The N-terminal domain of Rpn4 serves as a portable ubiquitin-independent degron and is recognized by specific 19S RP subunits.Prokaryotic proteasomes: nanocompartments of degradation.
P2860
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P248
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P2860
Proteasomes can degrade a significant proportion of cellular proteins independent of ubiquitination.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին 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
Proteasomes can degrade a sign ...... independent of ubiquitination.
@ast
Proteasomes can degrade a sign ...... independent of ubiquitination.
@en
Proteasomes can degrade a sign ...... independent of ubiquitination.
@nl
type
label
Proteasomes can degrade a sign ...... independent of ubiquitination.
@ast
Proteasomes can degrade a sign ...... independent of ubiquitination.
@en
Proteasomes can degrade a sign ...... independent of ubiquitination.
@nl
altLabel
Proteasomes can degrade a sign ...... independent of ubiquitination
@en
prefLabel
Proteasomes can degrade a sign ...... independent of ubiquitination.
@ast
Proteasomes can degrade a sign ...... independent of ubiquitination.
@en
Proteasomes can degrade a sign ...... independent of ubiquitination.
@nl
P2093
P2860
P3181
P1476
Proteasomes can degrade a sign ...... independent of ubiquitination.
@en
P2093
Ekaterina G Viktorova
Evgeny V Pilipenko
James M Baugh
P2860
P304
P3181
P356
10.1016/J.JMB.2008.12.081
P407
P577
2009-01-08T00:00:00Z