Evidence map›Paper›PMID 26788256›Full record

ReviewOxidative medicine and cellular longevity2016

Potential Modulation of Sirtuins by Oxidative Stress.

Leonardo Santos, Carlos Escande, Ana Denicola

Registry-linked trialOpen access · hybridAbstract readReview
In one paragraph

Review in Oxidative medicine and cellular longevity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05561738 (Nicotinamide Riboside in Ulcerative Colitis), which is not on this map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.8field-weighted citation impact, top 4% 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.

NCT05561738 naterminatednot on this mapstarted 2024, after this paper: background citation

Nicotinamide Riboside in Ulcerative Colitis

TypeinterventionalSponsorUniversity of PittsburghRan2024 to 2026Enrolled19ConditionsUlcerative ColitisArmsNicotinamide Riboside Chloride, Placebo, Standard of Care
3 · Its place in the literature

Who cites it

55 citing papers in PubMed, 109 citations in OpenAlex.

  1. Review
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  13. Protective effects ofJournal of ginseng research · 2023
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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.

Leonardo SantosLaboratorio de Fisicoquímica Biológica, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Iguá 4225, 11400 Montevideo, Uruguay.
Carlos EscandeLaboratorio de Patologías del Metabolismo y Envejecimiento, Institut Pasteur de Montevideo, Mataojo 2020, 11400 Montevideo, Uruguay.
Ana DenicolaLaboratorio de Fisicoquímica Biológica, Instituto de Química Biológica, Facultad de Ciencias, Universidad de la República, Iguá 4225, 11400 Montevideo, Uruguay.
Universidad de la República · UYInstitut Pasteur de Montevideo · UY

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sirtuins are a conserved family of NAD-dependent protein deacylases. Initially proposed as histone deacetylases, it is now known that they act on a variety of proteins including transcription factors and metabolic enzymes, having a key role in the regulation of cellular homeostasis. Seven isoforms are identified in mammals (SIRT1-7), all of them sharing a conserved catalytic core and showing differential subcellular localization and activities. Oxidative stress can affect the activity of sirtuins at different levels: expression, posttranslational modifications, protein-protein interactions, and NAD levels. Mild oxidative stress induces the expression of sirtuins as a compensatory mechanism, while harsh or prolonged oxidant conditions result in dysfunctional modified sirtuins more prone to degradation by the proteasome. Oxidative posttranslational modifications have been identified in vitro and in vivo, in particular cysteine oxidation and tyrosine nitration. In addition, oxidative stress can alter the interaction with other proteins, like SIRT1 with its protein inhibitor DBC1 resulting in a net increase of deacetylase activity. In the same way, manipulation of cellular NAD levels by pharmacological inhibition of other NAD-consuming enzymes results in activation of SIRT1 and protection against obesity-related pathologies. Nevertheless, further research is needed to establish the molecular mechanisms of redox regulation of sirtuins to further design adequate pharmacological interventions.

Indexed as

Oxidative StressAgingAnimalsDiseaseHumansMolecular Targeted TherapyProtein BindingSirtuinsSirtuins

Identifiers

PMID26788256
PMCPMC4691645
OpenAlexW2269031989

What OpenQuestion holds

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Registered trials

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.