Evidence map›Paper›PMID 32947891›Full record

ArticleInternational journal of molecular sciences2020

Dynamical Behavior of the Human Ferroportin Homologue from

Valentina Tortosa, Maria Carmela Bonaccorsi di Patti, Federico Iacovelli, Andrea Pasquadibisceglie, Mattia Falconi, Giovanni Musci, Fabio Polticelli

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  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
  3. Review
  4. Article
  5. Iron Availability in Tissue Microenvironment: The Key Role of Ferroportin.International journal of molecular sciences · 2021
    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

7 authors at 4 institutions in 1 country.

Valentina TortosaDepartment of Sciences, Roma Tre University, 00146 Rome, Italy.
Maria Carmela Bonaccorsi di PattiDepartment of Biochemical Sciences, Sapienza University of Roma, 00185 Rome, Italy.ORCID 0000-0002-4794-7037
Federico IacovelliDepartment of Biology, University of Rome Tor Vergata, 00133 Rome, Italy.ORCID 0000-0001-7511-6575
Andrea PasquadibisceglieDepartment of Sciences, Roma Tre University, 00146 Rome, Italy.ORCID 0000-0002-1630-6982
Mattia FalconiDepartment of Biology, University of Rome Tor Vergata, 00133 Rome, Italy.ORCID 0000-0002-3990-4758
Giovanni MusciDepartment Biosciences and Territory, University of Molise, 86090 Pesche, Italy.ORCID 0000-0002-5196-709X
Fabio PolticelliDepartment of Sciences, Roma Tre University, 00146 Rome, Italy.ORCID 0000-0002-7657-2019
Roma Tre University · ITUniversity of Rome Tor Vergata · ITSapienza University of Rome · ITUniversity of Molise · IT

Funding

Ministero dell'Istruzione, dell'Università e della Ricerca 2017483NH8Ministero dell'Istruzione, dell'Università e della Ricerca "Dipartimenti di Eccellenza" (Legge 232/2016, Articolo 1, Comma 314-337)
6 · The paper itself

Abstract

Members of the major facilitator superfamily of transporters (MFS) play an essential role in many physiological processes such as development, neurotransmission, and signaling. Aberrant functions of MFS proteins are associated with several diseases, including cancer, schizophrenia, epilepsy, amyotrophic lateral sclerosis and Alzheimer's disease. MFS transporters are also involved in multidrug resistance in bacteria and fungi. The structures of most MFS members, especially those of members with significant physiological relevance, are yet to be solved. The lack of structural and functional information impedes our detailed understanding, and thus the pharmacological targeting, of these transporters. To improve our knowledge on the mechanistic principles governing the function of MSF members, molecular dynamics (MD) simulations were performed on the inward-facing and outward-facing crystal structures of the human ferroportin homologue from the Gram-negative bacterium

Indexed as

Amino Acid MotifsApoproteinsBacterial ProteinsBdellovibrio bacteriovorusCation Transport ProteinsCrystallography, X-RayFerroportinIronLigandsModels, MolecularMolecular Dynamics SimulationProtein BindingProtein ConformationApoproteinsBacterial ProteinsCation Transport ProteinsFerroportinIronLigandsBdellovibrio bacteriovorusferroportiniron transportermajor facilitator superfamilymolecular dynamics

Identifiers

PMID32947891
PMCPMC7555787
OpenAlexW3086156050

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.