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

The crystal structure of a mammalian protein kinase G reveals contacts between the regulatory and catalytic domains, indicates how cGMP binding alters domain conformations and thus domain:domain interactions, and informs a model for enzyme auto-inhibition and cooperative activation.

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.

The transcriptional cofactor HPK-1 (homeodomain-interacting protein kinase) functions as a key regulator of multiple proteostatic stress responses, each originating from discrete neuronal subtypes within the Caenorhabditis elegans nervous system to preserve neuronal health and maintain organismal proteostasis during normal aging.

Retrograde signaling activates the Rad53 checkpoint kinase independently of the canonical DNA replication stress response.

Active site migration establishes kinase activity in protein O-mannose kinase.

A combination of NMR, fluorescence, and molecular dynamics simulations reveals the recognition mechanism for the intrinsically disordered regulator of protein kinase A, highlighting the enzyme's nuclear export process.

Host protein kinase C family members regulate influenza virus genome replication by phosphorylating the viral nucleoprotein and controlling assembly of the viral replication machinery.

Structural analysis of an AKAP18-protein kinase A complex reveals that regions of intrinsic disorder impact the phosphorylation of preferred substrates.

High-resolution, large-scale immunohistochemical mouse brain images showing global views of different brain regions, as well as cellular and subcellular details, identified distinct localization of PKA RIβ and RIIβ regulatory subunits that reveal functional differences.