Evidence map›Paper›PMID 40643475›Full record

ReviewCells2025

The Ac/N-Degron Domain of MARCHF6 E3 Ubiquitin Ligase and Its Role in Regulating Ferroptosis.

Hope Omoniyi, Grace Hohman, Mohamed Eldeeb

Abstract readReview
In one paragraph

Review in Cells, 2025. 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
–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

1 citing paper in PubMed.

  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

3 authors.

Hope OmoniyiDepartment of Chemistry, Illinois State University, Normal, IL 61790, USA.
Grace HohmanDepartment of Chemistry, Illinois State University, Normal, IL 61790, USA.
Mohamed EldeebDepartment of Chemistry, Illinois State University, Normal, IL 61790, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ferroptosis is a form of cell death characterized by iron and reactive oxygen species accumulation. Notably, this mode of cell death has been shown to exhibit significant implications for aging-related disorders including tumorigenesis and neurodegeneration. Nonetheless, the intricate underlying molecular mechanisms of ferroptosis and their differential roles in the molecular etiology of these diseases are still elusive. Elucidating the precise molecular mechanisms underlying ferroptosis is, thus, important for understanding the molecular basis of these diseases and unveiling potential therapeutic targets. MARCHF6 is an E3 ub ligase involved in regulating various cellular processes throughout the cell including ferroptosis. Research findings by Yang et al. identified a novel role of MARCHF6 E3 ub ligase in recognizing Ac/N-degron bearing substrates, which includes pro-ferroptotic and anti-ferroptotic proteins, demonstrating a regulatory role for MARCHF6 in fine-tuning ferroptosis. Herein, we highlight these recent findings and discuss the potential role of MARCHF6 in modulating ferroptosis pointing to the emerging role of MARCHF6 as a potential therapeutic target for treating ferroptosis-related diseases.

Indexed as

FerroptosisMembrane ProteinsUbiquitin-Protein LigasesAnimalsDegronsHumansProtein DomainsReactive Oxygen SpeciesMembrane ProteinsReactive Oxygen SpeciesUbiquitin-Protein LigasesferroptosisN-terminal acetylationproteasomeprotein degradationproteolysisubiquitin

Identifiers

PMID40643475
PMCPMC12248422

What OpenQuestion holds

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Registered trials

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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.