Aurora A kinase, an anti-cancer drug target, can be activated by two independent mechanisms.

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

Genetically-encoded platforms direct kinase inhibitor drugs to organelles to reveal new dimensions of local kinase signaling.

Casein kinase I, a pivotal kinase in the circadian clock encoded by ck-1a, is positively regulated by a novel RNA-binding protein that protects ck-1a transcripts from nonsense-mediated decay.

Closed-ring and open-spiral assembly of the multi-subunit neuronal kinase CaMKII suggest a mechanism for how active subunits shuttle between individual assemblies, propagating stimulatory signals.

A chemical biology approach has identified the kinase DYRK1A as a new regulator of the inflammatory response.

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

The pyruvate kinase contained in the apicoplast organelle of malaria parasites makes the nucleotide triphosphates required for several processes including transcription of the organellar genome.

The major cytosolic yeast peroxiredoxin Tsa1 controls aging and H₂O₂-resistance by inhibiting protein kinase A through a conserved cysteine in the catalytic subunit activation loop and not by scavenging H₂O₂.

The human NimA-related kinases (Neks) recognize divergent substrate motifs, and include Nek10 as a dual-specificity serine/tyrosine kinase, and Nek6, Nek7 and Nek9 as amplifiers of the Plk1 phospho-motif.