Evidence map›Paper›PMID 37725277›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2023

Initial characterization of an iron superoxide dismutase from Thermobifida fusca.

Anne Grethe Hamre, Rim Al-Sadawi, Kirsti Merete Johannesen, Bastien Bisarro, Åsmund Røhr Kjendseth, Hanna-Kirsti S Leiros, Morten Sørlie

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. 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

7 authors at 2 institutions in 1 country.

Anne Grethe HamreDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, 1432, Ås, Norway.
Rim Al-SadawiDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, 1432, Ås, Norway.
Kirsti Merete JohannesenDepartment of Chemistry, Faculty of Science and Technology, UiT The Arctic University of Norway, 9037, Tromsö, Norway.
Bastien BisarroDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, 1432, Ås, Norway.
Åsmund Røhr KjendsethDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, 1432, Ås, Norway.
Hanna-Kirsti S LeirosDepartment of Chemistry, Faculty of Science and Technology, UiT The Arctic University of Norway, 9037, Tromsö, Norway.
Morten SørlieDepartment of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, PO 5003, 1432, Ås, Norway. morten.sorlie@nmbu.no.ORCID 0000-0001-7259-6710
Norwegian University of Life Sciences · NOUiT The Arctic University of Norway · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Superoxide dismutases (SODs) are enzymes that catalyze the dismutation of the superoxide radical anion into O

Indexed as

Superoxide DismutaseSuperoxidesHydrogen PeroxideThermobifidaHydrogen PeroxideSuperoxide DismutaseSuperoxidesCrystal structureEnzyme thermostabilitySuperoxide dismutaseThermobifida fusca

Identifiers

PMID37725277
PMCPMC10520107
OpenAlexW4386851411

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.