Evidence map›Paper›PMID 23086947›Full record

ReviewThe Journal of biological chemistry2012

Sirtuin catalysis and regulation.

Jessica L Feldman, Kristin E Dittenhafer-Reed, John M Denu

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 143 papers.

0numbers the graph read from it
0cells of the map it votes in
143citing papers in PubMed
8.7field-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

143 citing papers in PubMed, 243 citations in OpenAlex.

  1. Article
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  6. Evaluation of Molecular Responses and Longevity Markers inInternational journal of molecular sciences · 2026
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83 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 2 institutions in 1 country.

Jessica L FeldmanDepartment of Biomolecular Chemistry and the Wisconsin Institute for Discovery, University of Wisconsin, Madison, Wisconsin 53715, USA. jmdenu@wisc.edu
Kristin E Dittenhafer-Reed
John M Denu
University of Wisconsin–Madison · USWisconsin Institutes for Discovery · US

Funding

Reversible protein acetylation and sirtuin functionR01GM065386 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2003 to 2022
$7.3M
Molecular mechanisms of histone modification - Alzheimer’s supplement NOT-AG-18-008R37GM059785 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI DENU, JOHN M · 2013 to 2022
$3.7M
NIGMS NIH HHS R01 GM065386NIGMS NIH HHS R37 GM059785
6 · The paper itself

Abstract

Sirtuins are a family of NAD(+)-dependent protein deacetylases/deacylases that dynamically regulate transcription, metabolism, and cellular stress response. Their general positive link with improved health span in mammals, potential regulation of pathways mediated by caloric restriction, and growing links to human disease have spurred interest in therapeutics that target their functions. Here, we review the current understanding of the chemistry of catalysis, biological targets, and endogenous regulation of sirtuin activity. We discuss recent efforts to generate small-molecule regulators of sirtuin activity.

Indexed as

BiocatalysisAcylationAnimalsHumansSirtuinsSmall Molecule LibrariesSubstrate SpecificitySirtuinsSmall Molecule Libraries

Identifiers

PMID23086947
PMCPMC3522242
OpenAlexW2066852267

What OpenQuestion holds

Textmetadata
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.