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The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.

Evidence for a Common Mechanism of SIRT1 Regulation by Allosteric Activators

Hubbard, Basil P., Gomes, Ana P., Dai, Han, Li, Jun, Case, April W., Considine, Thomas, Riera, Thomas V., Lee, Jessica E., E, Sook Yen, Lamming, Dudley W., Pentelute, Bradley L., Schuman, Eli R., Stevens, Linda A., Ling, Alvin J. Y., Armour, Sean M., Michan, Shaday, Zhao, Huizhen, Jiang, Yong, Sweitzer, Sharon M., Blum, Charles A., Disch, Jeremy S., Ng, Pui Yee, Howitz, Konrad T., Rolo, Anabela P., Hamuro, Yoshitomo, Moss, Joel, Perni, Robert B., Ellis, James L., Vlasuk, George P., Sinclair, David A.·2013·Science
DOI 10.1126/science.1231097PMC PMC3799917
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Abstract

It's a SIRT: Intense attention has focused on the SIRT1 deacetylase as a possible target for anti-aging drugs. But unexpected complications in assays of SIRT1 activity have made it unclear whether compounds thought to be sirtuin-activating compounds (STACs) are really direct regulators of the enzyme. Further exploration of these effects by Hubbard et al. (p. 1216 ; see the Perspective by Yuan and Marmorstein ) revealed that interaction of SIRT1 with certain substrates allows activation of SIRT1 by STACs and identified critical amino acids in SIRT1 required for these effects. Mouse myoblasts reconstituted with SIRT1 mutated at this amino acid lost their responsiveness to STACs.

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Crossref · 10.1126/science.1231097

Cites

9 of 9 references verified0 citation errors · 0 not checkable

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  • SRT3025 acts by allosteric binding to Sirt1 at the lysine site 230, which is located at its catalytic core.

    “Thus, similar to previously described Sirt1 activators,15 SRT3025 acts by allosteric binding to Sirt1 at the lysine site 230, which is located at its catalytic core.”

    From The Sirt1 activator SRT3025 provides atheroprotection in Apoe−/− mice by reducing hepatic Pcsk9 secretion and enhancing Ldlr expression (2015) · cites this paper as [15]

    The paper supports allosteric activation of SIRT1 by previously described activators, but it identifies residue 230 as glutamate (Glu230), not lysine, and places it immediately N-terminal to the catalytic core, not within it (Abstract section; page unavailable). It reports that replacing Glu230 with lysine attenuated activation. Our copy does not mention SRT3025, so it cannot establish that compound’s binding site. (LLM, conf=0.88)

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Citations

Cites

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Research works printed but not linked: 21

  1. 10.1146/annurev.pathol.4.110807.092250 · DOI · Paper page
  2. 10.1146/annurev.pathol.4.110807.092250 · DOI · Paper page
  3. 10.1038/nrendo.2011.225 · DOI
  4. 10.1038/nature05354 · DOI · Paper page
  5. 10.1074/jbc.M500655200 · DOI · Paper page
  6. 10.1111/j.1747-0285.2009.00901.x · DOI · Paper page
  7. 10.1002/yea.810 · DOI · Paper page
  8. 10.1093/oxfordjournals.jbchem.a133257 · DOI
  9. 10.1146/annurev.biochem.74.082803.133500 · DOI · Paper page
  10. 10.1074/jbc.M110.133892 · DOI
  11. 10.1016/j.molcel.2004.08.031 · DOI · Paper page
  12. 10.1074/jbc.M605904200 · DOI
  13. 10.1074/jbc.M805711200 · DOI · Paper page
  14. 10.1038/nature07861 · DOI
  15. 10.1038/nature05354 · DOI · Paper page
  16. 10.1016/j.molcel.2011.07.038 · DOI
  17. 10.1074/jbc.M111.285031 · DOI
  18. 10.1038/sj.emboj.7601633 · DOI · Paper page
  19. 10.1074/jbc.M110.200311 · DOI
  20. 10.1016/j.cmet.2012.04.003 · DOI · Paper page
  21. 10.1016/j.ab.2009.07.019 · DOI

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Metadata

Authors
Hubbard, B. P., Gomes, A. P., Dai, H., Li, J., Case, A. W., Considine, T., Riera, T. V., Lee, J. E., E, S. Y., Lamming, D. W., Pentelute, B. L., Schuman, E. R., Stevens, L. A., Ling, A. J. Y., Armour, S. M., Michan, S., Zhao, H., Jiang, Y., Sweitzer, S. M., Blum, C. A., Disch, J. S., Ng, P. Y., Howitz, K. T., Rolo, A. P., Hamuro, Y., Moss, J., Perni, R. B., Ellis, J. L., Vlasuk, G. P., & Sinclair, D. A.
Affiliations
  • Department of Genetics, Harvard Medical School, Boston, MA 02115, USA.
  • Sirtris, a GSK Company, Cambridge, MA 02139, USA.
  • ExSAR Corporation, Monmouth Junction, NJ 08852, USA.
  • Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
  • NIH Cardiovascular and Pulmonary Branch/National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA.
  • GlaxoSmithKline, Collegeville, PA 19426, USA.
  • BIOMOL Research Laboratories Inc., Plymouth Meeting, PA 19462, USA.
  • Center for Neurosciences and Cell Biology, Department of Life Sciences, University of Coimbra, Coimbra 3004-517, Portugal.
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2013-03-08
Volume
339
Issue
6124
Pages
1216-1219
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.1231097
PMC
PMC3799917
Cited by
561
References
9
Language
en

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