A four-switch long-range allosteric network controls FGF receptor kinase conformational dynamics as well as activity and is applicable to other receptor tyrosine kinases.

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.

The adaptor protein Grb2 is able to enhance the activity of the cytoplasmic tyrosine kinase Btk through a novel mechanism, revealing a new role for Grb2 in B-cell signaling.

Extracellular signals mediated by the EphB2 receptor tyrosine kinase may access the effectors of fundamental cell functions controlled by MYCBP2.

A key B-cell tyrosine kinase that adopts an autoinhibited conformation, and can be activated by either membrane recruitment or soluble inositol hexakisphosphates in solution.

Computational methods based on both sequence and structure show evidence that tyrosine kinases are energetically biased to populate the 'DFG-out' type-II inhibitor binding conformation relative to serine/threonine kinases.

A high-throughput technique to characterize the substrate specificities of tyrosine kinases identifies the key features of kinases and substrates that enforce accurate signaling from T cell receptors.

The recruitment of SH2-containing proteins to Epidermal Growth Factor in cells happens more slowly than predicted by in vitro techniques.

Targeting Abelson kinase can be beneficial for treating disorders characterized by dysregulated Down Syndrome Cell Adhesion Molecule signaling.

The newly characterized activity regulating neuropeptide encoding gene Spar is a transcriptional target of the Jeb/Alk receptor tyrosine kinase signaling pathway in the Drosophila nervous system.