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.

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.

The tyrosine degradation pathway reprogramming connects mitochondrial dysfunction, aging, and production of tyrosine-derived neuromediators that can be targeted with an FDA-approved drug, Tigecycline.

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.

Genetic variation in a biogenic amines receptor underlies a means of gain control for nonassociative learning and hence an important form of attention that is the basis for tradeoffs in foraging in a social collective.

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

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

Phosphorylation of tyrosine 1 in the carboxy-terminal domain (CTD) of the largest subunit of RNA Polymerase (RNAP) II functions to stabilize this domain, and facilitates turnover of upstream antisense RNAs.

Mg²⁺-dependent JAK1-mediated phosphorylation sensitizes TRPV2 activity and thermo-threshold, which is counterbalanced by PTPN1-mediated dephosphorylation, highlighting a role of phosphorylation homeostasis in setting the basal activity of TRPV2.

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.