Evidence map›Paper›PMID 26607666›Full record

ArticleChembiochem : a European journal of chemical biology2016

N-Acylethanolamines Bind to SIRT6.

Minna Rahnasto-Rilla, Tarja Kokkola, Elina Jarho, Maija Lahtela-Kakkonen, Ruin Moaddel

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

26 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Emerging Therapeutic Potential of SIRT6 Modulators.Journal of medicinal chemistry · 2021
    Review
  11. Review
  12. Review
  13. Review
  14. Nitro-fatty acids as activators of hSIRT6 deacetylase activity.The Journal of biological chemistry · 2020
    Article
  15. Article
  16. Effects of galloflavin and ellagic acid on sirtuin 6 and its anti-tumorigenic activities.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2020
    Article
  17. Review
  18. Article
  19. Article
  20. Sirtuins and SIRT6 in Carcinogenesis and in Diet.International journal of molecular sciences · 2019
    Review
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

5 authors at 2 institutions in 2 countries.

Minna Rahnasto-RillaBioanalytical Chemistry and Drug Screening Centre, Laboratory of Clinical Investigation, National Institute on Aging, National Institutes of Health, Suite 100, Biomedical Research Center, 251 Bayview Boulevard, Baltimore, MD, 21224-6825, USA.
Tarja KokkolaSchool of Pharmacy, University of Eastern Finland, Yliopistonranta 1C, Kuopio, 70210, Finland.
Elina JarhoSchool of Pharmacy, University of Eastern Finland, Yliopistonranta 1C, Kuopio, 70210, Finland.
Maija Lahtela-KakkonenSchool of Pharmacy, University of Eastern Finland, Yliopistonranta 1C, Kuopio, 70210, Finland.
Ruin MoaddelBioanalytical Chemistry and Drug Screening Centre, Laboratory of Clinical Investigation, National Institute on Aging, National Institutes of Health, Suite 100, Biomedical Research Center, 251 Bayview Boulevard, Baltimore, MD, 21224-6825, USA. moaddelru@grc.nia.nih.gov.
University of Eastern Finland · FINational Institutes of Health · US

Funding

Immobilized Receptors In Drug DiscoveryZIAAG000295 · NIA · NATIONAL INSTITUTE ON AGING · PI EGAN, JOSEPHINE · 2009 to 2025
$11.4M
Intramural NIH HHS Z99 AG999999Intramural NIH HHS ZIA AG000295
6 · The paper itself

Abstract

Sirtuin 6 (SIRT6) is an NAD+-dependent histone deacetylase enzyme that is involved in multiple molecular pathways related to aging. Initially, it was reported that SIRT6 selectively deacetylated H3K9Ac and H3K56Ac; however, it has more recently been shown to preferentially hydrolyze long-chain fatty acyl groups over acetyl groups in vitro. Subsequently, fatty acids were demonstrated to increase the catalytic activity of SIRT6. In this study, we investigated whether a series of N-acylethanolamines (NAEs), quercetin, and luteolin could regulate SIRT6 activity. NAEs increased SIRT6 activity, with oleoylethanolamide having the strongest activity (EC50 value of 3.1 μm). Quercetin and luteolin were demonstrated to have dual functionality with respect to SIRT6 activity; namely, they inhibited SIRT6 activity with IC50 values of 24 and 2 μm, respectively, and stimulated SIRT6 activity more than sixfold (EC50 values of 990 and 270 μm, respectively).

Indexed as

EthanolaminesHumansMolecular StructureSirtuinsEthanolaminesN-acylethanolaminesSIRT6 protein, humanSirtuinsenzymesethanolamidesnatural productsquercetinsirtuins

Identifiers

PMID26607666
PMCPMC4813509
OpenAlexW2175544344

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.