Protein-linked Ubiquitin Chain Structure Restricts Activity of Deubiquitinating Enzymes
出版年份 2011 全文链接
标题
Protein-linked Ubiquitin Chain Structure Restricts Activity of Deubiquitinating Enzymes
作者
关键词
-
出版物
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 286, Issue 52, Pages 45186-45196
出版商
American Society for Biochemistry & Molecular Biology (ASBMB)
发表日期
2011-11-10
DOI
10.1074/jbc.m111.310094
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Biochemical Characterization of a Multidomain Deubiquitinating Enzyme Ubp15 and the Regulatory Role of Its Terminal Domains
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- C-terminal region of USP7/HAUSP is critical for deubiquitination activity and contains a second mdm2/p53 binding site
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- Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
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- Dissection of USP catalytic domains reveals five common insertion points
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- Analysis of Activator-Binding Sites on the APC/C Supports a Cooperative Substrate-Binding Mechanism
- (2009) Mary E. Matyskiela et al. MOLECULAR CELL
- Building ubiquitin chains: E2 enzymes at work
- (2009) Yihong Ye et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- Breaking the chains: structure and function of the deubiquitinases
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- Protein partners of deubiquitinating enzymes
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- The Structure of the CYLD USP Domain Explains Its Specificity for Lys63-Linked Polyubiquitin and Reveals a B Box Module
- (2008) David Komander et al. MOLECULAR CELL
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