The dynamics of Sirtuin 6 binding to the nucleosome shed light on how it is able to deacetylate histone H3 lysines close to the core, including K27.

The inhibition of host Sirtuin-2 by AGK2 restricts mycobacterial growth in vivo by modulation of host transcriptome leading to activation of protective immune responses.

Multifaceted properties of the water-soluble derivative of antibiotic heliomycin enable it to offer greater antitumor value than its parent compound by inhibiting the tNOX-NAD⁺-SIRT1 axis to induce apoptosis.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

SIRT1 and SIRT3-mediated immunometabolic shift governs intracellular Salmonella proliferation both in vitro and in vivo and dissemination in mice, thereby influencing the infection outcomes.

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.

Transgenic mice and cell models provide evidence of a pathophysiological mechanism that connects mtDNA damage to cardiac dysfunction via reduced NAD⁺ levels and loss of mitochondrial function and communication.

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.

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.

Sirtuin, Hst4 is a novel DDK kinase target, which is modified and degraded in response to replication stress, increasing H3K56 acetylation, to stabilize DNA replication forks via fork protection complex which maintains genome stability and has potential in cancer therapeutics.