Evidence map›Paper›PMID 39940646›Full record

ReviewInternational journal of molecular sciences2025

The Ferroxidase-Permease System for Transport of Iron Across Membranes: From Yeast to Humans.

Matteo Amadei, Fabio Polticelli, Giovanni Musci, Maria Carmela Bonaccorsi di Patti

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. The different affinity of the two metal-binding sites of human ferroportin drives outward directionality of transport.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2025
    Article
  2. 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.

Matteo AmadeiDepartment of Biochemical Sciences 'A. Rossi Fanelli', Sapienza University of Rome, 00185 Rome, Italy.
Fabio PolticelliDepartment of Sciences, University Roma Tre, 00146 Rome, Italy.ORCID 0000-0002-7657-2019
Giovanni MusciDepartment of Biosciences and Territory, University of Molise, 86090 Pesche, Italy.ORCID 0000-0002-5196-709X
Maria Carmela Bonaccorsi di PattiDepartment of Biochemical Sciences 'A. Rossi Fanelli', Sapienza University of Rome, 00185 Rome, Italy.ORCID 0000-0002-4794-7037

Funding

Project ECS 0000024 Rome Technopole-NRP Mission 4 Component 2 Investment 1.5the European Union-NextGenerationEUthe Grant Departments of Excellence art. 1, comma 314-337 Legge 232/2016
6 · The paper itself

Abstract

Transport of iron across the cell membrane is a tightly controlled process carried out by specific proteins in all living cells. In yeast and in mammals, a system formed by an enzyme with ferroxidase activity coupled to a membrane transporter supports iron uptake or iron efflux, respectively. Ferroxidase belongs to the family of blue multicopper oxidases, enzymes able to couple the one-electron oxidation of substrate(s) to full reduction of molecular oxygen to water. On the other hand, the permeases are widely different and are specific to Fe

Indexed as

Cell MembraneCeruloplasminIronMembrane Transport ProteinsYeastsAnimalsBiological TransportHumansSaccharomyces cerevisiaeCeruloplasminIronMembrane Transport ProteinsceruloplasmincopperferroportinferroxidaseFet3Ftr1hephaestinironmulticopper oxidaseyeast

Identifiers

PMID39940646
PMCPMC11817551

What Socratic 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 Socratic graph.