Evidence map›Paper›PMID 24160699›Full record

ReviewAnnual review of pharmacology and toxicology2014

Small-molecule allosteric activators of sirtuins.

David A Sinclair, Leonard Guarente

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of pharmacology and toxicology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
0.6field-weighted citation impact, top 29% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

125 citing papers in PubMed, 10 citations in OpenAlex.

  1. Trial
  2. Trial
  3. SIRT1: Protean roles at the nexus of health, disease, and therapeutics.Journal of cell communication and signaling · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Histone acylation at a glance.Journal of cell science · 2024
    Review
  14. Review
  15. Review
  16. NADInternational journal of molecular sciences · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Article

65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

David A SinclairGlenn Laboratories for the Biological Mechanisms of Aging, Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115; email: david_sinclair@hms.harvard.edu.
Leonard Guarente
Massachusetts Institute of Technology · USUNSW Sydney · AU

Funding

MOLECULAR STUDY OF YEAST SGS1 AND RDNA CIRCLES IN AGINGR01AG015339 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GUARENTE, LEONARD P · 1999 to 2014
$5.5M
Role of Sgs1 DNA helicase in telomere maintenanceR01AG019719 · NIA · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI SINCLAIR, DAVID A. · 2001 to 2022
$5.3M
SIRT1 as a regulator of health and lifespan of mammalsR37AG028730 · NIA · HARVARD MEDICAL SCHOOL · PI SINCLAIR, DAVID A. · 2012 to 2021
$4.1M
SIRT as a regulator of health and lifespan of mammalsR01AG028730 · NIA · HARVARD MEDICAL SCHOOL · PI SINCLAIR, DAVID A. · 2007 to 2011
$1.7M
Function in Mammalian SIRT1 in AgingR56AG015339 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GUARENTE, LEONARD P · 2016 to 2016
$230k
NIA NIH HHS R01 AG015339NIA NIH HHS R01 AG019719NIA NIH HHS R01 AG028730NIA NIH HHS R37 AG028730NIA NIH HHS R56 AG015339
6 · The paper itself

Abstract

The mammalian sirtuins (SIRT1-7) are NAD(+)-dependent lysine deacylases that play central roles in cell survival, inflammation, energy metabolism, and aging. Members of this family of enzymes are considered promising pharmaceutical targets for the treatment of age-related diseases including cancer, type 2 diabetes, inflammatory disorders, and Alzheimer's disease. SIRT1-activating compounds (STACs), which have been identified from a variety of chemical classes, provide health benefits in animal disease models. Recent data point to a common mechanism of allosteric activation by natural and synthetic STACs that involves the binding of STACs to a conserved N-terminal domain in SIRT1. Compared with polyphenols such as resveratrol, the synthetic STACs show greater potency, solubility, and target selectivity. Although considerable progress has been made regarding SIRT1 allosteric activation, key questions remain, including how the molecular contacts facilitate SIRT1 activation, whether other sirtuin family members will be amenable to activation, and whether STACs will ultimately prove safe and efficacious in humans.

Indexed as

Molecular Targeted TherapyAllosteric RegulationAnimalsBenzimidazolesDisease Models, AnimalHumansInflammationResveratrolSirtuinsStilbenesbenzimidazoleBenzimidazolesResveratrolSirtuinsStilbenes

Identifiers

PMID24160699
PMCPMC4018738
OpenAlexW1480841945

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.