Luca Cesaro

TL;DR: The catalytic sites of protein kinases are divergent enough as to allow a competitive inhibitor like staurosporine to be fairly selective, a feature that can be enhanced by suitable modifications designed based on the structure of the catalytic site of the kinase.

TL;DR: A direct correlation between high basal Lyn activity and defects in the induction of apoptosis in leukemic cells is suggested and a critical role for Lyn is supported in B-CLL pathogenesis and this tyrosine kinase is identified as a potential therapeutic target.

TL;DR: It is concluded that indeed the 2275 putative CK2 sites (accounting for 20.9% of the whole phosphoproteome they belong to), or at least the great majority of these are generated by CK2.

TL;DR: The crystal structure of apigenin and luteolin in complex with the catalytic subunit of Zea mays CK2 has been solved, revealing their ability to interact with both the hinge region (Val116) and the positive area near Lys68 and the conserved water W1, the two main polar ligand anchoring points in the CK2 active site.

TL;DR: In this paper, SLS and acidic cluster motifs are shown to be crucial for β-catenin recognition and showed that Pro-44 and Pro-52 are also important for efficient phosphorylation.