Evidence map›Paper›PMID 41945998›Full record

ArticleRedox biology2026

Ferroptosis-related mechanisms in prion diseases provide insights into neurodegeneration and reveal therapeutic implications.

Mohammed Zayed, Hilal Tayara, Byung-Hoon Jeong

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Redox biology, 2026. 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
–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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. 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

3 authors.

Mohammed ZayedKorea Zoonosis Research Institute, Jeonbuk National University, Iksan, 54531, Republic of Korea; Department of Bioactive Material Sciences, Jeonbuk National University, Jeonju, 54896, Republic of Korea; Department of Surgery, College of Veterinary Medicine, Qena University, Qena, 83523, Egypt.
Hilal TayaraSchool of International Engineering and Science, Jeonbuk National University, Jeonju, 54896, Republic of Korea.
Byung-Hoon JeongKorea Zoonosis Research Institute, Jeonbuk National University, Iksan, 54531, Republic of Korea; Department of Bioactive Material Sciences, Jeonbuk National University, Jeonju, 54896, Republic of Korea. Electronic address: bhjeong@jbnu.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prion diseases are a group of fatal neurodegenerative disorders caused by misfolded proteins. Understanding the regulatory networks of ferroptosis in prion diseases could unveil new diagnostic and therapeutic strategies. To explore this, we systematically evaluated ferroptosis-associated alterations across human sporadic Creutzfeldt-Jakob disease (sCJD) brain samples, the ME7-infected mouse model, and in vitro using PrP

Indexed as

Creutzfeldt-Jakob SyndromeFerroptosisPrion DiseasesAmino Acid Transport System y+AnimalsBrainCyclohexylaminesDisease Models, AnimalHumansIronLipid PeroxidationMiceNeurodegenerative DiseasesPeptide FragmentsPhenylenediaminesPhospholipid Hydroperoxide Glutathione PeroxidaseAmino Acid Transport System y+Cyclohexylaminesferrostatin-1IronPeptide FragmentsPhenylenediaminesPhospholipid Hydroperoxide Glutathione Peroxidaseprion protein (106-126)PrionsReactive Oxygen SpeciesSLC7A11 protein, humanCell deathFerroptosisNeurodegenerative diseasesPathogenesisPrion diseaseTherapeutics

Identifiers

PMID41945998
PMCPMC13090729

What OpenQuestion holds

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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.