Evidence map›Paper›PMID 23029496›Full record

ArticlePloS one2012

SIRT1 activators suppress inflammatory responses through promotion of p65 deacetylation and inhibition of NF-κB activity.

Hongying Yang, Wei Zhang, Heng Pan, Heidi G Feldser, Elden Lainez, Christine Miller, Stewart Leung, Zhong Zhong, Huizhen Zhao, Sharon Sweitzer and 7 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed, 2 pooled it
7.5field-weighted citation impact, top 2% 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

201 citing papers in PubMed, 2 syntheses or guidelines pooled it, 363 citations in OpenAlex.

  1. Pooled it
  2. Physical exercise and inflammation in Parkinson's disease: a review.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Pooled it
  3. Trial
  4. Trial
  5. Trial
  6. Review
  7. Article
  8. Curcumin (The Journal of clinical and aesthetic dermatology · 2026
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review

141 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

17 authors at 3 institutions in 2 countries.

Hongying YangSirtris, a GSK Company, Cambridge, Massachusetts, United States of America. Hongying.2.yang@gsk.com
Wei Zhang
Heng Pan
Heidi G Feldser
Elden Lainez
Christine Miller
Stewart Leung
Zhong Zhong
Huizhen Zhao
Sharon Sweitzer
Thomas Considine
Thomas Riera
Vipin Suri
Brian White
James L Ellis
George P Vlasuk
Christine Loh
GlaxoSmithKline (China) · CNGlaxoSmithKline (United States) · USTris Pharma (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chronic inflammation is a major contributing factor in the pathogenesis of many age-associated diseases. One central protein that regulates inflammation is NF-κB, the activity of which is modulated by post-translational modifications as well as by association with co-activator and co-repressor proteins. SIRT1, an NAD(+)-dependent protein deacetylase, has been shown to suppress NF-κB signaling through deacetylation of the p65 subunit of NF-κB resulting in the reduction of the inflammatory responses mediated by this transcription factor. The role of SIRT1 in the regulation of NF-κB provides the necessary validation for the development of pharmacological strategies for activating SIRT1 as an approach for the development of a new class of anti-inflammatory therapeutics. We report herein the development of a quantitative assay to assess compound effects on acetylated p65 protein in the cell. We demonstrate that small molecule activators of SIRT1 (STACs) enhance deacetylation of cellular p65 protein, which results in the suppression of TNFα-induced NF-κB transcriptional activation and reduction of LPS-stimulated TNFα secretion in a SIRT1-dependent manner. In an acute mouse model of LPS-induced inflammation, the STAC SRTCX1003 decreased the production of the proinflammatory cytokines TNFα and IL-12. Our studies indicate that increasing SIRT1-mediated NF-κB deacetylation using small molecule activating compounds is a novel approach to the development of a new class of therapeutic anti-inflammatory agents.

Indexed as

Protein Processing, Post-TranslationalAcetylationAnimalsAnti-Inflammatory AgentsBenzimidazolesCell LineHumansInflammationInterleukin-12LipopolysaccharidesMaleMiceMice, Inbred BALB CSignal TransductionSirtuin 1Small Molecule LibrariesAnti-Inflammatory AgentsBenzimidazolesInterleukin-12LipopolysaccharidesSIRT1 protein, humanSirtuin 1Small Molecule LibrariesSRTCX1003ThiazolesTranscription Factor RelATumor Necrosis Factor-alpha

Identifiers

PMID23029496
PMCPMC3460821
OpenAlexW2075877600

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.