Huizhen Zhao

TL;DR: SIRT1 can be directly activated through an allosteric mechanism common to chemically diverse STACs, and specific hydrophobic motifs found in SIRT1 substrates such as PGC-1α and FOXO3a facilitate Sirtuin-activating compounds (STACs) activation by STacs.

TL;DR: Yuan et al. as mentioned in this paper found that specific hydrophobic motifs found in SIRT1 substrates such as PGC-1α and FOXO3a facilitate SIRT 1 activation by STACs.

TL;DR: It is demonstrated that small molecule activators of SIRT1 (STACs) enhance deacetylation of cellular p65 protein, which results in the suppression of TNF α-induced NF-κB transcriptional activation and reduction of LPS-stimulated TNFα secretion in a SIRT 1-dependent manner.

TL;DR: The crystal structure of the Chk1 kinase domain in complex with UCN-01 was determined and hydrophobic interactions and hydrogen-bonding interactions were observed, consistent with the potency and selectivity of UCn-01.

TL;DR: Crystallographic and biochemical results demonstrated that compounds of this chemical series bind to an allosteric site and lock the enzyme in a catalytically inactive conformation, thereby enabling inhibition of different clinically relevant IDH1 mutants.