David Communi

TL;DR: Rat brain inositol 1,4,5-trisphosphate (InsP3) 3-kinase A was expressed in Escherichia coli to identify the amino acid residues involved in substrate ATP/Mg2+ binding, and results strongly indicated that amino acids residues Lys-197 and Asp-414 are necessary for InsP3 3-Kinase activity and form part of the ATP/ Mg(2+)-binding domain.

TL;DR: These data provide the first biochemical evidence for the existence of a novel InsP3 3-kinase isoenzyme in human platelets, which is distinct from previously reported InsP4 3- Kinase A and InsP2 3-Kinase B.

TL;DR: In this paper, a G-protein coupled receptor and a novel ligand were proposed for the diagnosis and treatment of a disease or disorder related to the dysregulation of Gprotein-coupled receptor signaling.

TL;DR: Immunodetection as well as mass spectrometric peptide mass fingerprinting and post-source decay (PSD) sequence data analysis after immunoprecipitation permitted unambiguous identification of the major native 5-phosphatase isoform hydrolyzing Ins(1,4,5)P3 and Ins( 1,3, 4, 5)P4 as type I inositol polyphosphate 5- phosphatase.

TL;DR: A reactive cysteine residue is directly identified as part of the active site, i.e. the substrate-binding domain, of Ins(1,4,5)P3 5-phosphatase, part of a sequence 10 amino acids long that is well conserved among the primary structures of inositol and phosphatidylinositol polyphosphate 5- phosphatases.