Evidence map›Paper›PMID 24962284›Full record

ReviewFuture medicinal chemistry2014

Sirtuin inhibitors as anticancer agents.

Jing Hu, Hui Jing, Hening Lin

Abstract readReview
In one paragraph

Review in Future medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.2field-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

83 citing papers in PubMed, 171 citations in OpenAlex.

  1. Review
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  18. Frontiers in medicine · 2023
    Article
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23 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

3 authors at 1 institution in 1 country.

Jing HuDepartment of Chemistry & Chemical Biology, Cornell University, Ithaca, NY 14850, USA.
Hui Jing
Hening Lin
Cornell University · US

Funding

Succinylation and Malonylation as Novel Protein Modifications in CancerR01CA163255 · NCI · CORNELL UNIVERSITY · PI CERIONE, RICHARD A., LIN, HENING · 2011 to 2015
$2.9M
NCI NIH HHS R01 CA163255
6 · The paper itself

Abstract

Sirtuins are a class of enzymes with nicotinamide adenine dinucleotide (NAD)-dependent protein lysine deacylase function. By deacylating various substrate proteins, including histones, transcription factors, and metabolic enzymes, sirtuins regulate various biological processes, such as transcription, cell survival, DNA damage and repair, and longevity. Small molecules that can inhibit sirtuins have been developed and many of them have shown anticancer activity. Here, we summarize the major biological findings that connect sirtuins to cancer and the different types of sirtuin inhibitors developed. Interestingly, biological data suggest that sirtuins have both tumor-suppressing and tumor-promoting roles. However, most pharmacological studies with small-molecule inhibitors suggest that inhibiting sirtuins has anticancer effects. We discuss possible explanations for this discrepancy and suggest possible future directions to further establish sirtuin inhibitors as anticancer agents.

Indexed as

AnimalsAntineoplastic AgentsBenzamidesEnzyme InhibitorsHumansNaphtholsNeoplasmsNiacinamideProtein BindingReactive Oxygen SpeciesSirtuinsAntineoplastic AgentsBenzamidesEnzyme InhibitorsNaphtholsNiacinamideReactive Oxygen SpeciessirtinolSirtuins

Identifiers

PMID24962284
PMCPMC4384657
OpenAlexW2090408565

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.