Academic
Publications
Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation

Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation,10.1016/j.phrs.2009.12.006,Pharmacological Res

Protein deacetylation by SIRT1: An emerging key post-translational modification in metabolic regulation   (Citations: 5)
BibTex | RIS | RefWorks Download
The biological function of most proteins relies on reversible post-translational modifications, among which phosphorylation is most prominently studied and well recognized. Recently, a growing amount of evidence indicates that acetylation–deacetylation reactions, when applied to crucial mediators, can also robustly affect the function of target proteins and thereby have wide-ranging physiological impacts. Sirtuin 1 (SIRT1), which functions as a nicotinamide adenine dinucleotide (NAD+)-dependent protein deacetylase, deacetylates a wide variety of metabolic molecules in response to the cellular energy and redox status and as such causes significant changes in metabolic homeostasis. This review surveys the evidence for the emerging role of SIRT1-mediated deacetylation in the control of metabolic homeostasis.
Journal: Pharmacological Research - PHARMACOL RES , vol. 62, no. 1, pp. 35-41, 2010
Cumulative Annual
View Publication
The following links allow you to view full publications. These links are maintained by other sources not affiliated with Microsoft Academic Search.
Sort by: