Barbara Guerra

TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.

TL;DR: The crystal structure of a fully active form of human protein kinase CK2 (casein kinase 2) consisting of two C‐terminally truncated catalytic and two regulatory subunits has been determined and shows an inter‐domain mobility in the catalytic subunit known to be functionally important in protein kinases and detected here for the first time directly within one crystal structure.

TL;DR: The structure of the catalytic subunit with the fixed positioning of the activation segment in the active conformation through its own aminoterminal region suggests a regulation at the transcriptional level making a regulation by second messengers unlikely.

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: The present review of CK2 may help to further elucidate its aberrant role in many disease states and its peculiar structural features may be advantageous in designing tailor-made compounds with the possibility to specifically target this protein kinase.