Evidence map›Paper›PMID 35151099›Full record

ArticleJournal of inorganic biochemistry2022

Old dogs, new tricks: New insights into the iron/manganese superoxide dismutase family.

Katie A Frye, Kacper M Sendra, Kevin J Waldron, Thomas E Kehl-Fie

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

16 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  9. Current research in microbial sciences · 2025
    Article
  10. Review
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  12. Article
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  14. Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023
    Review
  15. Article
  16. 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

4 authors.

Katie A FryeDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, USA.
Kacper M SendraFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK.
Kevin J WaldronFaculty of Medical Sciences, Biosciences Institute, Newcastle University, Newcastle upon Tyne, NE2 4HH, UK. Electronic address: kevin.waldron@newcastle.ac.uk.
Thomas E Kehl-FieDepartment of Microbiology, University of Illinois Urbana-Champaign, Urbana, IL, USA; Carl R. Woese Institute for Genomic Biology, University of Illinois Urbana-Champaign, Urbana, IL, USA. Electronic address: kehlfie@illinois.edu.

Funding

Leveraging host-imposed metal starvation to elucidate the molecular and environmental factors that dictate metal utilization by the iron/manganese superoxide dismutase superfamilyR01AI155611 · NIAID · UNIVERSITY OF IOWA · PI KEHL-FIE, THOMAS EVERETT · 2021 to 2025
$2.8M
Overcoming nutritional immunity: Staphylococcal adaptation to host-imposed manganese and zinc starvationR01AI118880 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI KEHL-FIE, THOMAS EVERETT · 2016 to 2020
$1.9M
Phosphate homeostasis and uptake in Staphylococcus aureusR21AI149115 · NIAID · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI KEHL-FIE, THOMAS EVERETT · 2020 to 2021
$408k
Biotechnology and Biological Sciences Research Council BB/S006818/1NIAID NIH HHS R01 AI118880NIAID NIH HHS R01 AI155611NIAID NIH HHS R21 AI149115
6 · The paper itself

Abstract

Superoxide dismutases (SODs) are ancient enzymes of widespread importance present in all domains of life. Many insights have been gained into these important enzymes over the 50 years since their initial description, but recent studies in the context of microbial pathogenesis have resulted in findings that challenge long established dogmas. The repertoire of SODs that bacterial pathogens encode is diverse both in number and in metal dependencies, including copper, copper and zinc, manganese, iron, and cambialistic enzymes. Other bacteria also possess nickel dependent SODs. Compartmentalization of SODs only partially explains their diversity. The need for pathogens to maintain SOD activity across distinct hostile environments encountered during infection, including those limited for essential metals, is also a driver of repertoire diversity. SOD research using pathogenic microbes has also revealed the apparent biochemical ease with which metal specificity can change within the most common family of SODs. Collectively, these studies are revealing the dynamic nature of SOD evolution, both that of individual SOD enzymes that can change their metal specificity to adapt to fluctuating cellular metal availability, and of a cell's repertoire of SOD isozymes that can be differentially expressed to adapt to fluctuating environmental metal availability in a niche.

Indexed as

IronManganeseCopperIonsSuperoxide DismutaseZincCopperIonsIronManganeseSuperoxide DismutaseZincEvolutionIronManganeseMetalloenzymesMetal specificityPathogenesisSuperoxide dismutase (SOD)

Identifiers

PMID35151099
PMCPMC9112591

What OpenQuestion holds

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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.