Literature: Sirtuin, class I (IPR017328)
References used in this entry
The following publications were referred to in the abstract:
Diversity in the Sir2 family of protein deacetylases.
Buck SW, Gallo CM, Smith JS.
J. Leukoc. Biol. 75 939-50 2004
PMID: 14742637 Related citations
Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase.
French JB, Cen Y, Sauve AA.
Biochemistry 47 10227-39 2008
PMID: 18729382 Related citations
The following publications were not referred to in the abstract, but provide useful additional information:
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide.
Zhao K, Chai X, Marmorstein R.
Structure 11 1403-11 2003
PMID: 14604530 Related citations
Structural basis for nicotinamide inhibition and base exchange in Sir2 enzymes.
Sanders BD, Zhao K, Slama JT, Marmorstein R.
Mol. Cell 25 463-72 2007
PMID: 17289592 Related citations
Structure and autoregulation of the yeast Hst2 homolog of Sir2.
Zhao K, Chai X, Clements A, Marmorstein R.
Nat. Struct. Biol. 10 864-71 2003
PMID: 14502267 Related citations
Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases.
Zhao K, Harshaw R, Chai X, Marmorstein R.
Proc. Natl. Acad. Sci. U.S.A. 101 8563-8 2004
PMID: 15150415 Related citations
Structure of the histone deacetylase SIRT2.
Finnin MS, Donigian JR, Pavletich NP.
Nat. Struct. Biol. 8 621-5 2001
PMID: 11427894 Related citations