2013
DOI: 10.1158/1538-7445.am2013-632
|View full text |Cite
|
Sign up to set email alerts
|

Abstract 632: Characterization of BCCIP as a novel BARD1 interaction partner.

Abstract: BARD1 (BRCA1-Associated Ring Domain 1) was originally identified in a yeast-two-hybrid (Y2H) screen as a binding partner of BRCA1. The functional heterodimer BRCA1/BARD1 is required for several of the cellular and tumor-suppressor functions of BRCA1. Both proteins interact through the N-terminal RING domain to form a heterodimeric E3 ubiquitin ligase that constitutes the major catalytic activity of the BRCA1-BARD1 complex. BARD1 is also associated to p53-mediated apoptosis, in a BRCA1-independent manner. The c… Show more

Help me understand this report

This publication either has no citations yet, or we are still processing them

Set email alert for when this publication receives citations?

See others like this or search for similar articles