The dramatic extension of lifespan in Sirt6-deficient mice by Trp53 haploinsufficiency suggests that SIRT6 has distinct biological function from SIRT1 in regulating p53 activity and preventing cells from senescence/apoptosis.

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

The ATM-SIRT6 axis integrates the DNA repair machinery to longevity-promoting pathways.

A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.

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.

In addition to its cytoplasmic role for translation, the seryl-tRNA synthetase also antagonizes the c-Myc transcription factor in the nucleus to transcriptionally repress the growth factor VEGFA and ensure proper development of the vasculature in vertebrates.

The small molecule Inauhzin possesses a dual targeting ability, and activates p53 by targeting two enzymes—SIRT1 and IMP dehydrogenase 2 (IMPDH2)—which are highly expressed in human cancers.

Sirt3 functions as decrotonylase to regulate histone crotonylation dynamics.

Metabolic relationships between cells in the retina and retinal pigment epithelium are fundamental to retinal function, retinal disease and age-related vision loss and they may provide strategies for metabolism-based therapies.

The deacetylase Sir2 fine-tunes transcription of PMA1 and other aging related genes in a cAMP-PKA and CK2 signaling dependent manner.