Evidence map›Paper›PMID 34825885›Full record

ArticleMicrobiology (Reading, England)2021

Key carboxylate residues for iron transit through the prokaryotic ferritin

Justin M Bradley, Joshua Fair, Andrew M Hemmings, Nick E Le Brun

Open access · hybridAbstract read
In one paragraph

Article in Microbiology (Reading, England), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Cavity acidification limits ferritin iron biomineralization.Journal of inorganic biochemistry · 2026
    Article
  2. Article
  3. Article
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 1 institution in 1 country.

Justin M BradleyCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
Joshua FairCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
Andrew M HemmingsCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
Nick E Le BrunCentre for Molecular and Structural Biochemistry, School of Chemistry, University of East Anglia, Norwich, NR4 7TJ, UK.
University of East Anglia · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R002363/1
6 · The paper itself

Abstract

Ferritins are proteins forming 24meric rhombic dodecahedral cages that play a key role in iron storage and detoxification in all cell types. Their function requires the transport of Fe

Indexed as

FerritinsIronSynechococcusAnimalsCatalytic DomainCeruloplasminMineralsOxidation-ReductionCeruloplasminFerritinsIronMineralsferritinironoxidationstoragetransport

Identifiers

PMID34825885
PMCPMC8743623
OpenAlexW3200056960

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.