Pietro Ciceri

TL;DR: This work presents interaction maps for 38 kinase inhibitors across a panel of 317 kinases representing >50% of the predicted human protein kinome and introduces the concept of a selectivity score as a general tool to quantify and differentiate the observed interaction patterns.

TL;DR: An efficient way to determine kinase inhibitor specificity by measuring binding of small molecules to the ATP site of kinases is described, which represents a systematic small molecule-protein interaction map for clinical compounds across a large number of related proteins.

TL;DR: In this article, the authors report that several clinical kinase inhibitors also inhibit bromodomains with therapeutically relevant potencies and are best classified as dual kinase-brommodomain inhibitors.

TL;DR: The approach described enables investigation of the complex relationship between kinase activation state and compound binding affinity and should facilitate strategic inhibitor design.

TL;DR: It is reported that several clinical kinase inhibitors also inhibit bromodomains with therapeutically relevant potencies and are best classified as dual kinase/bromidomain inhibitors, a novel strategy for rational single agent polypharmacological targeting.