The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension-Reference-Cited by-同舟云学术

The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension

Published:2012-08-03 Issue:19 Volume:31 Page:3833-3844
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:

Author:

Smit Judith J¹,Monteferrario Davide²,Noordermeer Sylvie M²,van Dijk Willem J¹,van der Reijden Bert A²,Sixma Titia K¹

Affiliation:

1. Division of Biochemistry, The Netherlands Cancer Institute; Amsterdam The Netherlands

2. Laboratory of Hematology, Department of Laboratory Medicine, Nijmegen Centre of Molecular Life sciences, Radboud University Nijmegen Medical Centre; Nijmegen The Netherlands

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference42 articles.

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2. Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex;Brzovic;Proc Natl Acad Sci USA,2003

3. Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b;Buchwald;EMBO J,2006

4. Structure of the C-terminal RING finger from a RING-IBR-RING/TRIAD motif reveals a novel zinc-binding domain distinct from a RING;Capili;J Mol Biol,2004

5. Autoregulation of Parkin activity through its ubiquitin-like domain;Chaugule;EMBO J,2011

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