A road to modulators of the kinase activity and the non-enzymatic functions of Src and IDO1 at once.

A high-throughput comparison of substrate specificities of the Src-family kinases Lck and c-Src against a library of proteome-derived phosphorylation sites reveals that Lck has evolved divergent electrostatic features reflecting its involvement in T-cell signaling.

The functional role of novel regulatory mechanism within prototypic oncogenic kinase c-Src is described with particular emphasis on cancer cell migration, invasiveness, oncogenic transformation, and multilevel regulation of Src itself.

A comprehensive analysis questioned the prevailing views of Src-mediated hPANX1 phosphorylation at Tyr199 and Tyr309.

Light-sensitive allosteric switch module, a broadly applicable protein engineering method, is used for the regulation of protein activity with tight temporal control and spatial precision.

The ubiquitin ligase c-Cbl preferentially targets unique-region phosphorylated LynA for rapid degradation, regulating its expression and differentially tuning signaling responsiveness in macrophages and mast cells.

Slow conformational changes after drug binding rationalize selectivity, affinity and long on-target residence time for kinase inhibitors.

The Netrin-1 and ephrin-B2 proteins act synergistically in the developing nervous system.

A high-throughput method to profile tyrosine kinases and phosphotyrosine recognition domains reveals new rules for sequence specificity and maps the effects of mutations on the recognition of tyrosine phosphorylation sites.

Mechanicals forces and local (Wnt) signaling can synergize to increase β-catenin signaling and produce unique growth phenotypes.