Evidence map›Paper›PMID 19914407›Full record

ReviewBiochimica et biophysica acta2010

The structural biochemistry of the superoxide dismutases.

J J P Perry, D S Shin, E D Getzoff, J A Tainer

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
11.0field-weighted citation impact, top 1% 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

203 citing papers in PubMed, 553 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Lower Plasma Antioxidant Defense and Heat Shock Proteins Mark Intra-Amniotic Sludge Ultrasound Finding.Journal of ultrasound in medicine : official journal of the American Institute of Ultrasound in Medicine · 2026
    Article
  9. Copper (CuPharmaceuticals (Basel, Switzerland) · 2026
    Article
  10. Review
  11. Scorpionate Complexes [(κInorganic chemistry · 2026
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Genome-Wide Expression Profile ofInternational journal of molecular sciences · 2025
    Article
  19. Article
  20. Review

143 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

4 authors at 3 institutions in 2 countries.

J J P PerrySkaggs Institute for Chemical Biology and Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
D S Shin
E D Getzoff
J A Tainer
Scripps Research Institute · USAmrita Vishwa Vidyapeetham · INLawrence Berkeley National Laboratory · US

Funding

STRUCTURAL ANALYSIS OF CHROMATICALLY ACTIVE PROTEINSR01GM037684 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D · 1987 to 2009
$3.1M
SUPEROXIDE DISMUTASE STRUCTURES AND LOU GEHRIGS DISEASER01GM039345 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GETZOFF, ELIZABETH D, TAINER, JOHN A. · 1988 to 2013
$1.9M
NIGMS NIH HHS GM37684NIGMS NIH HHS GM39345NIGMS NIH HHS R01 GM037684NIGMS NIH HHS R01 GM039345
6 · The paper itself

Abstract

The discovery of superoxide dismutases (SODs), which convert superoxide radicals to molecular oxygen and hydrogen peroxide, has been termed the most important discovery of modern biology never to win a Nobel Prize. Here, we review the reasons this discovery has been underappreciated, as well as discuss the robust results supporting its premier biological importance and utility for current research. We highlight our understanding of SOD function gained through structural biology analyses, which reveal important hydrogen-bonding schemes and metal-binding motifs. These structural features create remarkable enzymes that promote catalysis at faster than diffusion-limited rates by using electrostatic guidance. These architectures additionally alter the redox potential of the active site metal center to a range suitable for the superoxide disproportionation reaction and protect against inhibition of catalysis by molecules such as phosphate. SOD structures may also control their enzymatic activity through product inhibition; manipulation of these product inhibition levels has the potential to generate therapeutic forms of SOD. Markedly, structural destabilization of the SOD architecture can lead to disease, as mutations in Cu,ZnSOD may result in familial amyotrophic lateral sclerosis, a relatively common, rapidly progressing and fatal neurodegenerative disorder. We describe our current understanding of how these Cu,ZnSOD mutations may lead to aggregation/fibril formation, as a detailed understanding of these mechanisms provides new avenues for the development of therapeutics against this so far untreatable neurodegenerative pathology.

Indexed as

Amino Acid SequenceAnimalsHumansMolecular Sequence DataSequence Homology, Amino AcidSuperoxide DismutaseSuperoxide Dismutase

Identifiers

PMID19914407
PMCPMC3098211
OpenAlexW1975695493

What OpenQuestion holds

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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.