Evidence map›Paper›PMID 25163004›Full record

ArticleOrganic & biomolecular chemistry2014

Thiomyristoyl peptides as cell-permeable Sirt6 inhibitors.

Bin He, Jing Hu, Xiaoyu Zhang, Hening Lin

Open access · greenAbstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Continuous Histone Deacylase Activity Assays.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  6. Review
  7. Article
  8. Review
  9. Emerging Therapeutic Potential of SIRT6 Modulators.Journal of medicinal chemistry · 2021
    Review
  10. Review
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Sirtuins and SIRT6 in Carcinogenesis and in Diet.International journal of molecular sciences · 2019
    Review
  17. Updates on the epigenetic roles of sirtuins.Current opinion in chemical biology · 2019
    Review
  18. Article
  19. NRoyal Society open science · 2019
    Article
  20. 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

4 authors at 2 institutions in 1 country.

Bin HeDepartment of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, NY 14853, USA. hl379@cornell.edu.
Jing Hu
Xiaoyu Zhang
Hening Lin
Ithaca College · USCornell University · US

Funding

Chemical/biochemical tools for studying novel protein acyl lysine modificationsR01GM098596 · NIGMS · CORNELL UNIVERSITY · PI LIN, HENING · 2012 to 2015
$1.8M
NIGMS NIH HHS R01 GM098596
6 · The paper itself

Abstract

Sirtuins regulate a variety of biological pathways and inhibitors of sirtuins have been actively pursued as tool compounds to study sirtuin biology and as potential therapeutics. Here we demonstrate that thiomyristoyl peptides are potent and cell-permeable inhibitors of Sirt6, one of the seven human sirtuins, and will serve as the starting point for the development of more specific Sirt6 inhibitors.

Indexed as

Amino Acid SequenceCell-Penetrating PeptidesHistone Deacetylase InhibitorsHumansMolecular Sequence DataSirtuinsCell-Penetrating PeptidesHistone Deacetylase InhibitorsSIRT6 protein, humanSirtuins

Identifiers

PMID25163004
PMCPMC4161628
OpenAlexW1975397970

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.