Evidence map›Paper›PMID 29259135›Full record

ReviewThe Journal of biological chemistry2018

Eukaryotic copper-only superoxide dismutases (SODs): A new class of SOD enzymes and SOD-like protein domains.

Natalie G Robinett, Ryan L Peterson, Valeria C Culotta

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed, 1 pooled it
3.7field-weighted citation impact, top 6% 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

63 citing papers in PubMed, 1 synthesis or guideline pooled it, 114 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  7. Article
  8. Review
  9. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
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3 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

3 authors at 1 institution in 1 country.

Natalie G RobinettDepartment of Biochemistry and Molecular Biology, The Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205.
Ryan L PetersonDepartment of Biochemistry and Molecular Biology, The Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205.
Valeria C CulottaDepartment of Biochemistry and Molecular Biology, The Johns Hopkins University Bloomberg School of Public Health, Baltimore, Maryland 21205. Electronic address: vculott1@jhu.edu.
Johns Hopkins University · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Genetic Determinants of Oxygen ToxicityR37GM050016 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 2005 to 2014
$3.6M
GENETIC DETERMINANTS OF OXYGEN TOXICITYR01GM050016 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 1993 to 2018
$3.0M
Copper as a nutrient for Candida albicans at the host-pathogen interfaceR01AI119949 · NIAID · JOHNS HOPKINS UNIVERSITY · PI CULOTTA, VALERIA C · 2015 to 2019
$2.3M
NCI NIH HHS T32 CA009110NIAID NIH HHS R01 AI119949NIGMS NIH HHS R01 GM050016NIGMS NIH HHS R37 GM050016
6 · The paper itself

Abstract

The copper-containing superoxide dismutases (SODs) represent a large family of enzymes that participate in the metabolism of reactive oxygen species by disproportionating superoxide anion radical to oxygen and hydrogen peroxide. Catalysis is driven by the redox-active copper ion, and in most cases, SODs also harbor a zinc at the active site that enhances copper catalysis and stabilizes the protein. Such bimetallic Cu,Zn-SODs are widespread, from the periplasm of bacteria to virtually every organelle in the human cell. However, a new class of copper-containing SODs has recently emerged that function without zinc. These copper-only enzymes serve as extracellular SODs in specific bacteria (

Indexed as

CopperFungal ProteinsMetalloproteinsPeriplasmic ProteinsSuperoxide DismutaseZincFungiMycobacteriumOomycetesCopperFungal ProteinsMetalloproteinsPeriplasmic ProteinsSuperoxide DismutaseZinccoppermetalloproteinredox signalingsuperoxide dismutase (SOD)superoxide ion

Identifiers

PMID29259135
PMCPMC5880121
OpenAlexW2779821636

What OpenQuestion holds

Textmetadata
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.