Format
Items per page
Sort by

Send to:

Choose Destination

Links from PubMed

Items: 1 to 20 of 241

1.

The human Sir2 ortholog, SIRT2, is an NAD+-dependent tubulin deacetylase.

North BJ, Marshall BL, Borra MT, Denu JM, Verdin E.

Mol Cell. 2003 Feb;11(2):437-44.

3.

Substrate specificity and kinetic mechanism of the Sir2 family of NAD+-dependent histone/protein deacetylases.

Borra MT, Langer MR, Slama JT, Denu JM.

Biochemistry. 2004 Aug 3;43(30):9877-87.

PMID:
15274642
4.

Mutations in SIRT2 deacetylase which regulate enzymatic activity but not its interaction with HDAC6 and tubulin.

Nahhas F, Dryden SC, Abrams J, Tainsky MA.

Mol Cell Biochem. 2007 Sep;303(1-2):221-30. Epub 2007 May 22.

PMID:
17516032
5.
7.

Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase.

Imai S, Armstrong CM, Kaeberlein M, Guarente L.

Nature. 2000 Feb 17;403(6771):795-800.

PMID:
10693811
8.

Human Sir2 and the 'silencing' of p53 activity.

Smith J.

Trends Cell Biol. 2002 Sep;12(9):404-6.

PMID:
12220851
9.

Bypassing the catalytic activity of SIR2 for SIR protein spreading in Saccharomyces cerevisiae.

Yang B, Kirchmaier AL.

Mol Biol Cell. 2006 Dec;17(12):5287-97. Epub 2006 Oct 11.

10.

Identification of a class of small molecule inhibitors of the sirtuin family of NAD-dependent deacetylases by phenotypic screening.

Grozinger CM, Chao ED, Blackwell HE, Moazed D, Schreiber SL.

J Biol Chem. 2001 Oct 19;276(42):38837-43. Epub 2001 Aug 1.

11.

Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition.

Sauve AA, Moir RD, Schramm VL, Willis IM.

Mol Cell. 2005 Feb 18;17(4):595-601.

12.

Structure of the histone deacetylase SIRT2.

Finnin MS, Donigian JR, Pavletich NP.

Nat Struct Biol. 2001 Jul;8(7):621-5.

PMID:
11427894
13.

Acetylation of Sirt2 by p300 attenuates its deacetylase activity.

Han Y, Jin YH, Kim YJ, Kang BY, Choi HJ, Kim DW, Yeo CY, Lee KY.

Biochem Biophys Res Commun. 2008 Oct 31;375(4):576-80. doi: 10.1016/j.bbrc.2008.08.042. Epub 2008 Aug 21.

PMID:
18722353
14.

Quantitative assays for characterization of the Sir2 family of NAD(+)-dependent deacetylases.

Borra MT, Denu JM.

Methods Enzymol. 2004;376:171-87. Review. No abstract available.

PMID:
14975305
15.

Sir2 flexes its muscle.

Bedalov A, Simon JA.

Dev Cell. 2003 Aug;5(2):188-9.

16.

Identification of a small molecule inhibitor of Sir2p.

Bedalov A, Gatbonton T, Irvine WP, Gottschling DE, Simon JA.

Proc Natl Acad Sci U S A. 2001 Dec 18;98(26):15113-8.

17.
18.

Human histone deacetylase SIRT2 interacts with the homeobox transcription factor HOXA10.

Bae NS, Swanson MJ, Vassilev A, Howard BH.

J Biochem. 2004 Jun;135(6):695-700.

19.

Nicotinamide clearance by Pnc1 directly regulates Sir2-mediated silencing and longevity.

Gallo CM, Smith DL Jr, Smith JS.

Mol Cell Biol. 2004 Feb;24(3):1301-12.

20.

SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric restriction.

Wang F, Nguyen M, Qin FX, Tong Q.

Aging Cell. 2007 Aug;6(4):505-14. Epub 2007 May 23.

Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Write to the Help Desk