Evidence map›Paper›PMID 22982047›Full record

ArticleFree radical biology & medicine2013

The peroxidase activity of mitochondrial superoxide dismutase.

Kristine Ansenberger-Fricano, Douglas Ganini, Mao Mao, Saurabh Chatterjee, Shannon Dallas, Ronald P Mason, Krisztian Stadler, Janine H Santos, Marcelo G Bonini

Abstract read
In one paragraph

Article in Free radical biology & medicine, 2013. 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
2.6field-weighted citation impact, top 10% 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, 67 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The curious life of human mitochondrial SOD2.International journal of biological macromolecules · 2026
    Review
  5. Article
  6. Article
  7. Integrative medicine (Encinitas, Calif.) · 2022
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. SOD2 acetylation on lysine 68 promotes stem cell reprogramming in breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. SOD2 acetylation and deacetylation: Another tale of Jekyll and Hyde in cancer.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 5 institutions in 1 country.

Kristine Ansenberger-FricanoSection of Cardiology and Department of Pharmacology, College of Medicine, University of Illinois at Chicago, Chicago, IL 60612, USA.
Douglas Ganini
Mao Mao
Saurabh Chatterjee
Shannon Dallas
Ronald P Mason
Krisztian Stadler
Janine H Santos
Marcelo G Bonini
National Institute of Environmental Health Sciences · USUniversity of Illinois Chicago · USNational Institutes of Health · USRutgers, The State University of New Jersey · USUniversity of Pennsylvania · US

Funding

Protein Derived RadicalsZIAES050139 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI MASON, RONALD P · 2009 to 2018
$17.5M
Training in Mechanisms of Cardiovascular DiseasesT32HL072742 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI TOBACMAN, LARRY S · 2003 to 2013
$3.7M
Oxidative stress imbalance n Pulmonary&Cardiovascular disease,Electron paramagnetS10RR027848 · NCRR · UNIVERSITY OF ILLINOIS AT CHICAGO · PI BONINI, MARCELO G. · 2011 to 2011
$251k
Intramural NIH HHSNCRR NIH HHS S10 RR027848NHLBI NIH HHS HL072742-08NHLBI NIH HHS T32 HL072742
6 · The paper itself

Abstract

Manganese superoxide dismutase (MnSOD) is an integral mitochondrial protein known as a first-line antioxidant defense against superoxide radical anions produced as by-products of the electron transport chain. Recent studies have shaped the idea that by regulating the mitochondrial redox status and H(2)O(2) outflow, MnSOD acts as a fundamental regulator of cellular proliferation, metabolism, and apoptosis, thereby assuming roles that extend far beyond its proposed antioxidant functions. Accordingly, allelic variations of MnSOD that have been shown to augment levels of MnSOD in mitochondria result in a 10-fold increase in prostate cancer risk. In addition, epidemiologic studies indicate that reduced glutathione peroxidase activity along with increases in H(2)O(2) further increase cancer risk in the face of MnSOD overexpression. These facts led us to hypothesize that, like its Cu,ZnSOD counterpart, MnSOD may work as a peroxidase, utilizing H(2)O(2) to promote mitochondrial damage, a known cancer risk factor. Here we report that MnSOD indeed possesses peroxidase activity that manifests in mitochondria when the enzyme is overexpressed.

Indexed as

AnimalsGene Expression Regulation, NeoplasticHumansHydrogen PeroxideMCF-7 CellsMiceMicroscopy, ElectronMitochondriaNeoplasmsOxidation-ReductionOxidative StressPeroxidaseRecombinant ProteinsRiskSuperoxide DismutaseSuperoxidesHydrogen PeroxidePeroxidaseRecombinant ProteinsSuperoxide DismutaseSuperoxides

Identifiers

PMID22982047
PMCPMC4155036
OpenAlexW2055369568

What OpenQuestion holds

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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.