Evidence map›Paper›PMID 37963965›Full record

ArticleScientific reports2023

Ferritin microheterogeneity, subunit composition, functional, and physiological implications.

Ayush K Srivastava, Aliaksandra A Reutovich, Nathan J Hunter, Paolo Arosio, Fadi Bou-Abdallah

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Iron dysregulation in the central nervous system: implications for autism spectrum disorder.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  2. Introducing a novel variant in the FTH1 gene; A closer look at FTH1-related neuroferritinopathy as a neurodegeneration with brain iron accumulation (NBIA) disorder.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Article
  3. Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.Protein science : a publication of the Protein Society · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. IncreasedInternational journal of molecular sciences · 2025
    Article
  10. Observational
  11. Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024
    Article
  12. 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

5 authors at 2 institutions in 2 countries.

Ayush K SrivastavaDepartment of Chemistry, State University of New York, Potsdam, NY, 13676, USA.
Aliaksandra A ReutovichDepartment of Chemistry, State University of New York, Potsdam, NY, 13676, USA.
Nathan J HunterDepartment of Chemistry, State University of New York, Potsdam, NY, 13676, USA.
Paolo ArosioDepartment of Molecular and Translational Medicine, University of Brescia, 25121, Brescia, Italy.
Fadi Bou-AbdallahDepartment of Chemistry, State University of New York, Potsdam, NY, 13676, USA. bouabdf@potsdam.edu.ORCID 0000-0002-8557-1827
State University of New York at Potsdam · USUniversity of Brescia · IT

Funding

Heteropolymer Ferritins Structure-Function StudiesR15GM104879 · NIGMS · STATE UNIVERSITY OF NEW YORK AT POTSDAM · PI BOU-ABDALLAH, FADI · 2015 to 2019
$675k
NIGMS NIH HHS R15 GM104879
6 · The paper itself

Abstract

Ferritin is a ubiquitous intracellular iron storage protein that plays a crucial role in iron homeostasis. Animal tissue ferritins consist of multiple isoforms (or isoferritins) with different proportions of H and L subunits that contribute to their structural and compositional heterogeneity, and thus physiological functions. Using size exclusion and anion exchange chromatography, capillary isoelectric focusing (cIEF), and SDS-capillary gel electrophoresis (SDS-CGE), we reveal for the first time a significant variation in ferritin subunit composition and isoelectric points, in both recombinant and native ferritins extracted from animal organs. Our results indicate that subunits composition is the main determinant of the mean pI of recombinant ferritin heteropolymers, and that ferritin microheterogeneity is a common property of both natural and recombinant proteins and appears to be an intrinsic feature of the cellular machinery during ferritin expression, regulation, post-translational modifications, and post-subunits assembly. The functional significance and physiological implications of ferritin heterogeneity in terms of iron metabolism, response to oxidative stress, tissue-specific functions, and pathological processes are discussed.

Indexed as

FerritinsIronAnimalsElectrophoresis, Polyacrylamide GelIsoelectric FocusingIsoelectric PointFerritinsIron

Identifiers

PMID37963965
PMCPMC10646083
OpenAlexW4388652873

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.