Evidence map›Paper›PMID 34456745›Full record

ArticleFrontiers in physiology2021

Regulation of NADPH Oxidase-Mediated Superoxide Production by Acetylation and Deacetylation.

Ning Xia, Stefan Tenzer, Oleg Lunov, Martin Karl, Thomas Simmet, Andreas Daiber, Thomas Münzel, Gisela Reifenberg, Ulrich Förstermann, Huige Li

Open access · goldAbstract read
In one paragraph

Article in Frontiers in physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. 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

10 authors at 3 institutions in 1 country.

Ning XiaDepartment of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany.
Stefan TenzerDepartment of Immunology, Johannes Gutenberg University Medical Center, Mainz, Germany.
Oleg LunovInstitute of Pharmacology of Natural Products and Clinical Pharmacology, University of Ulm, Ulm, Germany.
Martin KarlDepartment of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany.
Thomas SimmetInstitute of Pharmacology of Natural Products and Clinical Pharmacology, University of Ulm, Ulm, Germany.
Andreas DaiberDepartment of Cardiology, Cardiology I, Johannes Gutenberg University Medical Center, Mainz, Germany.
Thomas MünzelDepartment of Cardiology, Cardiology I, Johannes Gutenberg University Medical Center, Mainz, Germany.
Gisela ReifenbergDepartment of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany.
Ulrich FörstermannDepartment of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany.
Huige LiDepartment of Pharmacology, Johannes Gutenberg University Medical Center, Mainz, Germany.
University Medical Center of the Johannes Gutenberg University Mainz · DEJohannes Gutenberg University Mainz · DEUniversität Ulm · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Oral treatment of apolipoprotein E-knockout (ApoE-KO) mice with the putative sirtuin 1 (SIRT1) activator resveratrol led to a reduction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activity in the heart. In contrast, the SIRT1 inhibitor EX527 enhanced the superoxide production in isolated human polymorphonuclear granulocytes. In human monocytic THP-1 cells, phorbol ester-stimulated superoxide production was enhanced by inhibitors of histone deacetylases (HDACs; including quisinostat, trichostatin A (TSA), PCI34051, and tubastatin A) and decreased by inhibitors of histone acetyltransferases [such as garcinol, curcumin, and histone acetyltransferase (HAT) Inhibitor II]. These results indicate that protein acetylation and deacetylation may represent crucial mechanisms regulating NADPH oxidase-mediated superoxide production. In cell-free systems, incubation of recombinant Rac1 with SIRT1 resulted in decreased Rac1 acetylation. Mass spectrometry analyses identified lysine 166 (K166) in Rac1 as a residue targeted by SIRT1. Deacetylation of Rac1 by SIRT1 markedly reduced the interaction of Rac1 with p67phox in

Indexed as

acetylationhistone acetyltransferasehistone deacetylaseNADPH oxidaseRac1resveratrolsirtuin 1

Identifiers

PMID34456745
PMCPMC8387964
OpenAlexW3193527933

What OpenQuestion holds

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Registered trials

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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.