Crystal Structure of a Josephin-Ubiquitin Complex

Features and development ofCoot

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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Silencing ataxin-3 mitigates degeneration in a rat model of Machado–Joseph disease: no role for wild-type ataxin-3?

(2010) Sandro Alves et al.   HUMAN MOLECULAR GENETICS

Activity and Cellular Functions of the Deubiquitinating Enzyme and Polyglutamine Disease Protein Ataxin-3 Are Regulated by Ubiquitination at Lysine 117

(2010) Sokol V. Todi et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Polyglutamine-induced neurodegeneration in SCA3 is not mitigated by non-expanded ataxin-3: Conclusions from double-transgenic mouse models

(2010) Jeannette Hübener et al.   NEUROBIOLOGY OF DISEASE

Understanding the Role of the Josephin Domain in the PolyUb Binding and Cleavage Properties of Ataxin-3

(2010) Giuseppe Nicastro et al.   PLoS One

Regulation and Cellular Roles of Ubiquitin-Specific Deubiquitinating Enzymes

(2009) Francisca E. Reyes-Turcu et al.   Annual Review of Biochemistry

Josephin domain of ataxin-3 contains two distinct ubiquitin-binding sites

(2009) Giuseppe Nicastro et al.   BIOPOLYMERS

Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3

(2009) Sokol V Todi et al.   EMBO JOURNAL

Breaking the chains: structure and function of the deubiquitinases

(2009) David Komander et al.   NATURE REVIEWS MOLECULAR CELL BIOLOGY

Protein partners of deubiquitinating enzymes

(2008) Karen H. Ventii et al.   BIOCHEMICAL JOURNAL

The Deubiquitinating Enzyme Ataxin-3, a Polyglutamine Disease Protein, Edits Lys63Linkages in Mixed Linkage Ubiquitin Chains

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