Evidence map›Paper›PMID 32587293›Full record

ArticleScientific reports2020

Iron stored in ferritin is chemically reduced in the presence of aggregating Aβ(1-42).

James Everett, Jake Brooks, Frederik Lermyte, Peter B O'Connor, Peter J Sadler, Jon Dobson, Joanna F Collingwood, Neil D Telling

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
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

39 citing papers in PubMed, 50 citations in OpenAlex.

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  20. A novel view of ferritin in cancer.Biochimica et biophysica acta. Reviews on cancer · 2023
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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

8 authors at 3 institutions in 2 countries.

James EverettSchool of Pharmacy and Bioengineering, Keele University, Stoke-on-Trent, Staffordshire, ST4 7QB, United Kingdom. j.everett@keele.ac.uk.
Jake BrooksSchool of Engineering, University of Warwick, Coventry, CV4 7AL, United Kingdom.
Frederik LermyteSchool of Engineering, University of Warwick, Coventry, CV4 7AL, United Kingdom.
Peter B O'ConnorDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, United Kingdom.
Peter J SadlerDepartment of Chemistry, University of Warwick, Coventry, CV4 7AL, United Kingdom.
Jon DobsonJ. Crayton Pruitt Family Department of Biomedical Engineering & Department of Materials Science and Engineering, University of Florida, Gainesville, Florida, 32611, United States.
Joanna F CollingwoodSchool of Engineering, University of Warwick, Coventry, CV4 7AL, United Kingdom.
Neil D TellingSchool of Pharmacy and Bioengineering, Keele University, Stoke-on-Trent, Staffordshire, ST4 7QB, United Kingdom.
University of Warwick · GBKeele University · GBUniversity of Florida · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Atypical low-oxidation-state iron phases in Alzheimer's disease (AD) pathology are implicated in disease pathogenesis, as they may promote elevated redox activity and convey toxicity. However, the origin of low-oxidation-state iron and the pathways responsible for its formation and evolution remain unresolved. Here we investigate the interaction of the AD peptide β-amyloid (Aβ) with the iron storage protein ferritin, to establish whether interactions between these two species are a potential source of low-oxidation-state iron in AD. Using X-ray spectromicroscopy and electron microscopy we found that the co-aggregation of Aβ and ferritin resulted in the conversion of ferritin's inert ferric core into more reactive low-oxidation-states. Such findings strongly implicate Aβ in the altered iron handling and increased oxidative stress observed in AD pathogenesis. These amyloid-associated iron phases have biomarker potential to assist with disease diagnosis and staging, and may act as targets for therapies designed to lower oxidative stress in AD tissue.

Indexed as

Alzheimer DiseaseAmyloid beta-PeptidesBiomarkersFerritinsHumansIronMicroscopy, Electron, Scanning TransmissionOxidation-ReductionOxidative StressPeptide FragmentsProtein AggregatesSpectrometry, X-Ray EmissionAmyloid beta-Peptidesamyloid beta-protein (1-42)BiomarkersFerritinsIronPeptide FragmentsProtein Aggregates

Identifiers

PMID32587293
PMCPMC7316746
OpenAlexW3037208315

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.