Rachel Grimley

TL;DR: X-ray crystal structures of compounds bound into bromodomains of Brd2 and Brd4 elucidate the molecular interactions of binding and explain the precisely defined stereochemistry required for activity.

TL;DR: This study confirms the irreversible covalent binding of the inhibitor to the kinase by x-ray crystallography and enzymology while demonstrating potency, selectivity, and prolonged duration of action in in vitro biological assays.

TL;DR: It is confirmed in cellular assays that SIRT6 can deacetylate acetylated-histone H3 lysine 9 (H3K9Ac), however this de acetylase activity is unusually low in biochemical assays.

TL;DR: The difference in the binding affinity between NADH and NAD indicates that there may be an energy requirement for the transfer of reducing equivalents into this site in the complete enzyme under physiological conditions, and suggests that the loop has closed down to within 0.5 nm of the nucleotide.

TL;DR: A number of interacting partners are reported which strengthen previous findings that SIRT6 functions in base excision repair (BER), and novel interactors which suggest a role in nucleosome and chromatin remodeling, the cell cycle and NFκB biology.