The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
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Structure of the E6/E6AP/p53 complex required for HPV-mediated degradation of p53.Epigenetic regulation of UBE3A and roles in human neurodevelopmental disorders.Convergent evolution in the assembly of polyubiquitin degradation signals by the Shigella flexneri IpaH9.8 ligaseCatalytically Important Residues of E6AP Ubiquitin Ligase Identified Using Acid-Cleavable Photo-Cross-LinkersAn Autism-Linked Mutation Disables Phosphorylation Control of UBE3A.Role of ubiquitin and the HPV E6 oncoprotein in E6AP-mediated ubiquitinationThe High-Risk Human Papillomavirus E6 Oncogene Exacerbates the Negative Effect of Tryptophan Starvation on the Development of Chlamydia trachomatis.Multiple Weak Linear Motifs Enhance Recruitment and Processivity in SPOP-Mediated Substrate Ubiquitination.Ubiquitylation-dependent oligomerization regulates activity of Nedd4 ligases.Autism gene Ube3a and seizures impair sociability by repressing VTA Cbln1.E6AP/UBE3A catalyzes encephalomyocarditis virus 3C protease polyubiquitylation and promotes its concentration reduction in virus-infected cells.Mechanism of ubiquitin chain synthesis employed by a HECT domain ubiquitin ligase.Structural Insights in Multifunctional Papillomavirus Oncoproteins.In silico modeling of the cryptic E2∼ubiquitin-binding site of E6-associated protein (E6AP)/UBE3A reveals the mechanism of polyubiquitin chain assembly.The mechanism of neural precursor cell expressed developmentally down-regulated 4-2 (Nedd4-2)/NEDD4L-catalyzed polyubiquitin chain assembly.Group-I PAKs-mediated phosphorylation of HACE1 at serine 385 regulates its oligomerization state and Rac1 ubiquitination.Substrate clustering potently regulates activity of WW-HECT domain-containing ubiquitin ligases.A Numerical Approach for Kinetic Analysis of the Nonexponential Thermoinactivation Process of Uricase.Structural dynamics of the E6AP/UBE3A-E6-p53 enzyme-substrate complex
P2860
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P2860
The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
description
2013 nî lūn-bûn
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2013年の論文
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2013年学术文章
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2013年学术文章
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2013年学术文章
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2013年学术文章
@zh-my
2013年学术文章
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2013年學術文章
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2013年學術文章
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2013年學術文章
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name
The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
@en
The active form of E6-associated protein
@nl
type
label
The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
@en
The active form of E6-associated protein
@nl
prefLabel
The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
@en
The active form of E6-associated protein
@nl
P2093
P2860
P356
P1476
The active form of E6-associated protein (E6AP)/UBE3A ubiquitin ligase is an oligomer.
@en
P2093
Arthur L Haas
Daniel J Edwards
Jennifer M Klein
Virginia P Ronchi
P2860
P304
P356
10.1074/JBC.M113.517805
P407
P577
2013-11-22T00:00:00Z