Sirtuins inhibitors: The approach to affinity and selectivity-Reference-Cited by-同舟云学术

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Sirtuins inhibitors: The approach to affinity and selectivity

Published:2010-08 Issue:8 Volume:1804 Page:1635-1644
ISSN:1570-9639
Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Cen Yana

Publisher

Elsevier BV

Reference101 articles.

1. The silencing protein SIR2 and its homologs are NAD-dependent protein deacetylases;Landry;Proc. Natl. Acad. Sci. U. S. A.,2000

2. SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates;Sauve;Curr. Med. Chem.,2004

3. Coupling of histone deacetylation to NAD breakdown by the yeast silencing protein Sir2: evidence for acetyl transfer from substrate to an NAD breakdown product;Tanny;Proc. Natl. Acad. Sci. U. S. A.,2001

4. Regulation of insulin secretion by SIRT4, a mitochondrial ADP-ribosyltransferase;Ahuja;J. Biol. Chem.,2007

5. SIRT2, a tubulin deacetylase, acts to block the entry to chromosome condensation in response to mitotic stress;Inoue;Oncogene,2007

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