Send to:

Choose Destination
See comment in PubMed Commons below
Biochim Biophys Acta. 2010 Oct-Dec;1799(10-12):726-39. doi: 10.1016/j.bbagrm.2010.06.003. Epub 2010 Jun 23.

Inhibitors to understand molecular mechanisms of NAD(+)-dependent deacetylases (sirtuins).

Author information

  • 1Department of Pharmaceutical Chemistry, Martin-Luther Universit√§t Halle-Wittenberg, Wolfgang-Langenbeckstr. 4, 06120 Halle/Saale, Germany.


Histone deacetylases (HDACs) are enzymes that cleave acetyl groups from acetyl-lysine residues in histones and various nonhistone proteins. Unlike the other three of the four classes of HDACs that have been identified in humans, which are zinc-dependent amidohydrolases, class III HDACs depend on nicotinamide adenine dinucleotide (NAD(+)) for their catalytic activity. The seven members of the class III HDACs are also named sirtuins for their homology to Sir2p, a yeast histone deacetylase. Sirtuin inhibitors have been critical for the linkage of sirtuin activity to many physiological and pathological processes, and sirtuin activity has been associated with the pathogenesis of cancer, HIV, and metabolic and neurological diseases. Presented here is an overview of the many sirtuin inhibitors that have provided insight into the biological role of sirtuins.

Copyright © 2010 Elsevier B.V. All rights reserved.

[PubMed - indexed for MEDLINE]

LinkOut - more resources

Full Text Sources

Other Literature Sources

Molecular Biology Databases

PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk