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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.

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.

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.

Advanced glycation end-products (compounds which make the food appetizing and aromatic) intricately modulate organism’s homeostatic and hedonistic signaling pathways thereby inducing preferential consumption of excess nutrients offering preliminary insights into overconsumption of modern-day processed food.

Loss-of-function variants of human ACK1 and BRK kinase underlie systemic lupus erythematosus in young patients from multiplex families and disrupt the anti-inflammatory response of macrophages to apoptotic cells.

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.

pYtags are novel biosensors that can be used to measure the activity of a receptor tyrosine kinase of interest in live cells with high spatiotemporal resolution and are applied to reveal rapid activity dynamics of EGFR/ErbB2 signaling.

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

Two cancer related proteins, tyrosine phosphatase PTPRK and ubiquitin ligase ZNRF3, interact to downregulate Wnt receptors, thereby regulating Spemann organizer function during Xenopus development.