Ubiquitin-interacting Motifs Confer Full Catalytic Activity, but Not Ubiquitin Chain Substrate Specificity, to Deubiquitinating Enzyme USP37
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Title
Ubiquitin-interacting Motifs Confer Full Catalytic Activity, but Not Ubiquitin Chain Substrate Specificity, to Deubiquitinating Enzyme USP37
Authors
Keywords
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Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 289, Issue 4, Pages 2415-2423
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Online
2013-12-10
DOI
10.1074/jbc.m113.528372
References
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Related references
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- Atypical ubiquitylation — the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
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- The deubiquitinating enzyme USP37 regulates the oncogenic fusion protein PLZF/RARA stability
- (2012) W-C Yang et al. ONCOGENE
- The deubiquitylase USP37 links REST to the control of p27 stability and cell proliferation
- (2012) C M Das et al. ONCOGENE
- Deubiquitinase USP37 Is Activated by CDK2 to Antagonize APCCDH1 and Promote S Phase Entry
- (2011) XiaoDong Huang et al. MOLECULAR CELL
- Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains
- (2010) Ai-Xin Song et al. PLoS One
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- (2009) Joshua J. Sims et al. MOLECULAR CELL
- Breaking the chains: structure and function of the deubiquitinases
- (2009) David Komander et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- The UBA-UIM Domains of the USP25 Regulate the Enzyme Ubiquitination State and Modulate Substrate Recognition
- (2009) Amanda Denuc et al. PLoS One
- Post-translational regulation of the tumor suppressor p27KIP1
- (2008) J. Vervoorts et al. CELLULAR AND MOLECULAR LIFE SCIENCES
- The Deubiquitinating Enzyme Ataxin-3, a Polyglutamine Disease Protein, Edits Lys63Linkages in Mixed Linkage Ubiquitin Chains
- (2008) Brett J. Winborn et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Recognition of Polyubiquitin Isoforms by the Multiple Ubiquitin Binding Modules of Isopeptidase T
- (2008) Francisca E. Reyes-Turcu et al. JOURNAL OF BIOLOGICAL CHEMISTRY
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- (2008) Yusuke Sato et al. NATURE
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