SIRT2 has detrimental effects in the heart and plays a role in cardiac response to injury and the progression of cardiac hypertrophy, and targeting SIRT2 may provide a novel avenue for the treatment of cardiac hypertrophy and ischemic disease.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

SIRT1 deacetylates SIRT6 at K33 to facilitate DNA double-strand breaks-recognition, subsequent expansion and local chromatin remodeling.

Hundreds of proteins are involved in the DNA damage response but only three sensors for DSB were known but now SIRT6 is identified as a fourth DSB sensor.

The decrotonylase FoSir5 modulates ATP synthesis that supports conidial germination in Fusarium oxysporum through coordinated lysine decrotonylation in different organelles.

A new post-translational regulatory mechanism of K-Ras is identified, which expands the function of reversible protein lysine fatty acylation and offers new possibility to target the K-Ras oncoprotein.

A series of experiments at the molecular level reveal the underlying mechanism of how a gene activates liver glucose production to regulate the blood glucose metabolism in mice.

Vitamin D bound to its receptor interacts with SIRT1 to induce its auto deacetylation and catalytic activity, which drives anti-proliferative effects in colorrectal cancer and this may lead to new therapeutic approaches for colorrectal and perhaps other cancers.

Mass spectroscopy, molecular modeling and/or molecular dynamics simulations reveal how acetylation regulates the activity of GSK3 isoforms independent of inhibitory phosphorylation.