Yong Jiang

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: This mutation highlights the interplay between Y641 and A677 residues in the substrate specificity of EZH2 and identifies another lymphoma patient population that harbors an activating mutation of EzH2.

TL;DR: This work has identified highly potent, selective, SAM-competitive, and cell-active EZH2 inhibitors, including GSK926 and GSK343, which are small molecule chemical tools that would be useful to further explore the biology of EZh2.

TL;DR: The design and characterization of an engineered human SIRT1 construct containing the minimal structural elements required for lysine deacetylation and catalytic activation by small molecule sirtuin-activating compounds (STACs) are reported and the STAC-binding site within the N-terminal domain of hSIRT1 is revealed.