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

Orthogonal to traditional paradigms that manipulate neuroligin expression level, optogenetic stimulation of tyrosine phosphorylation highlights a role of the intracellular domain of endogenous neuroligin-1 in excitatory synaptic differentiation and potentiation.

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

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.

Two receptor tyrosine phosphatases having overlapping function for the determination of the final axon stabilizing layer is encoded for their cumulative cytoplasmic activity and ligand specificity in the visual system.

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

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.

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.

The first-in-class kinase inhibitor, Ibrutinib, destabilizes its autoinhibited Bruton’s tyrosine kinase (BTK) target, and a remote resistance mutation causes global structural changes that activate BTK catalytic activity.