Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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Molecular basis for specificity of the Met1-linked polyubiquitin signalStructural Studies of HHARI/UbcH7∼Ub Reveal Unique E2∼Ub Conformational Restriction by RBR RING1.Association between Cullin-3 Single-Nucleotide Polymorphism rs17479770 and Essential Hypertension in the Male Chinese Han Population.Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI.Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase.Parkin-phosphoubiquitin complex reveals cryptic ubiquitin-binding site required for RBR ligase activity.Enzyme-substrate relationships in the ubiquitin system: approaches for identifying substrates of ubiquitin ligases.The Logic of the 26S Proteasome.Dynamic ubiquitin signaling in cell cycle regulation.Cullin-RING E3 Ubiquitin Ligases: Bridges to Destruction.Trade-off and flexibility in the dynamic regulation of the cullin-RING ubiquitin ligase repertoire.Cullin 3-Based Ubiquitin Ligases as Master Regulators of Mammalian Cell Differentiation.Prospect of divergent roles for the CUL3 system in vascular endothelial cell function and angiogenesis.RING-Between-RING E3 Ligases: Emerging Themes amid the Variations.Expanding the host cell ubiquitylation machinery targeting cytosolic Salmonella.Two functionally distinct E2/E3 pairs coordinate sequential ubiquitination of a common substrate in Caenorhabditis elegans development.AcM-UBE2M transfers NEDD8 to CRL1 E3 ubiquitin ligase complexAri-1 Regulates Myonuclear Organization Together with Parkin and Is Associated with Aortic Aneurysms.ECD promotes gastric cancer metastasis by blocking E3 ligase ZFP91-mediated hnRNP F ubiquitination and degradation.MARCH6 and TRC8 facilitate the quality control of cytosolic and tail-anchored proteins.The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation.UBE2G1 governs the destruction of cereblon neomorphic substrates
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P2860
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
description
2016 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2016 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2016
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im August 2016 veröffentlichter wissenschaftlicher Artikel
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scientific journal article
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vedecký článok (publikovaný 2016/08/25)
@sk
vědecký článek publikovaný v roce 2016
@cs
wetenschappelijk artikel (gepubliceerd op 2016/08/25)
@nl
наукова стаття, опублікована в серпні 2016
@uk
مقالة علمية (نشرت في 25-8-2016)
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name
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@en
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
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type
label
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@ast
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@en
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@nl
prefLabel
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@ast
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@en
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@nl
P2093
P2860
P50
P1433
P1476
Two Distinct Types of E3 Ligases Work in Unison to Regulate Substrate Ubiquitylation
@en
P2093
Arno F Alpi
Daniel C Scott
David M Duda
Jennifer L Olszewski
Joao A Paulo
P2860
P304
1198-1214.e24
P356
10.1016/J.CELL.2016.07.027
P407
P577
2016-08-01T00:00:00Z