Evidence map›Paper›PMID 22079668›Full record

ReviewFEBS letters2012

Superoxide dismutases: ancient enzymes and new insights.

Anne-Frances Miller

Abstract readReview
In one paragraph

Review in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 221 papers.

0numbers the graph read from it
0cells of the map it votes in
221citing papers in PubMed
7.8field-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

221 citing papers in PubMed, 542 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Activation and execution of lipoxygenase catalysis.Redox biochemistry and chemistry · 2026
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Scorpionate Complexes [(κInorganic chemistry · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Genome-Wide Expression Profile ofInternational journal of molecular sciences · 2025
    Article
  18. Review
  19. Article
  20. Review

161 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

1 author at 1 institution in 1 country.

Anne-Frances MillerDepartment of Chemistry, University of Kentucky, Lexington, KY 40506-0055, USA. afm@uky.edu
University of Kentucky · US

Funding

Enzyme Mis-Metallation, Consequences and OpportunitiesR01GM085302 · NIGMS · UNIVERSITY OF KENTUCKY · PI MILLER, ANNE-FRANCES · 2009 to 2010
$512k
NIGMS NIH HHS 1R01GM085302-01ANIGMS NIH HHS R01 GM085302
6 · The paper itself

Abstract

Superoxide dismutases (SODs) catalyze the de toxification of superoxide. SODs therefore acquired great importance as O(2) became prevalent following the evolution of oxygenic photosynthesis. Thus the three forms of SOD provide intriguing insights into the evolution of the organisms and organelles that carry them today. Although ancient organisms employed Fe-dependent SODs, oxidation of the environment made Fe less bio-available, and more dangerous. Indeed, modern lineages make greater use of homologous Mn-dependent SODs. Our studies on the Fe-substituted MnSOD of Escherichia coli, as well as redox tuning in the FeSOD of E. coli shed light on how evolution accommodated differences between Fe and Mn that would affect SOD performance, in SOD proteins whose activity is specific to one or other metal ion.

Indexed as

Models, ChemicalMolecular ConformationAnimalsBiological EvolutionEukaryotic CellsHumansOxidation-ReductionProkaryotic CellsSuperoxide DismutaseSuperoxidesSuperoxide DismutaseSuperoxides

Identifiers

PMID22079668
PMCPMC5443681
OpenAlexW2020887458

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.