An IRBIT homologue lacks binding activity to inositol 1,4,5-trisphosphate receptor due to the unique N-terminal appendage
Author:
Publisher
Wiley
Subject
Cellular and Molecular Neuroscience,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1471-4159.2009.05979.x/fullpdf
Reference23 articles.
1. IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding protein, is released from the IP3 receptor upon IP3 binding to the receptor;Ando;J. Biol. Chem.,2003
2. IRBIT suppresses IP3 receptor activity by competing with IP3 for the common binding site on the IP3 receptor;Ando;Mol. Cell,2006
3. Molecular and functional characterization of inositol trisphosphate receptors during early zebrafish development;Ashworth;J. Biol. Chem.,2007
4. A large-scale RNAi screen in human cells identifies new components of the p53 pathway;Berns;Nature,2004
5. Inositol trisphosphate and calcium signalling;Berridge;Nature,1993
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