Evidence map›Paper›PMID 34391801›Full record

ArticleJournal of molecular biology2021

A Novel Approach for the Synthesis of Human Heteropolymer Ferritins of Different H to L Subunit Ratios.

Ayush K Srivastava, Paolo Arosio, Maura Poli, Fadi Bou-Abdallah

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 12% 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

14 citing papers in PubMed, 17 citations in OpenAlex.

  1. Multivalent recognition of ferritin by full-length NCOA4 enables robust ferritinophagy.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. The assembly rules guiding hetero-oligomeric bacterioferritin organization and their evolutionary signature.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. A Brief History of Ferritin, an Ancient and Versatile Protein.International journal of molecular sciences · 2024
    Review
  8. Article
  9. Unveiling the stochastic nature of human heteropolymer ferritin self-assembly mechanism.Protein science : a publication of the Protein Society · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. 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 at 2 institutions in 2 countries.

Ayush K SrivastavaDepartment of Chemistry, State University of New York, Potsdam, NY 13676, USA.
Paolo ArosioDepartment of Molecular and Translational Medicine, University of Brescia, 25121 Brescia, Italy.
Maura PoliDepartment 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. Electronic address: bouabdf@potsdam.edu.
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

Mammalian ferritins are predominantly heteropolymeric species consisting of 24 structurally similar, but functionally different subunit types, named H and L, that co-assemble in different proportions. Despite their discovery more than 8 decades ago, recombinant human heteropolymer ferritins have never been synthesized, owing to the lack of a good expression system. Here, we describe for the first time a unique approach that uses a novel plasmid design that enables the synthesis of these complex ferritin nanostructures. Our study reveals an original system that can be easily tuned by altering the concentrations of two inducers, allowing the synthesis of a full spectrum of heteropolymer ferritins, from H-rich to L-rich ferritins and any combinations in-between (isoferritins). The H to L subunit composition of purified ferritin heteropolymers was analyzed by SDS-PAGE and capillary gel electrophoresis, and their iron handling properties characterized by light absorption spectroscopy. Our novel approach allows future investigations of the structural and functional differences of isoferritin populations, which remain largely obscure. This is particularly exciting since a change in the ferritin H- to L-subunit ratio could potentially lead to new iron core morphologies for various applications in bio-nanotechnologies.

Indexed as

ApoferritinsEscherichia coliHumansIronPlasmidsProtein EngineeringRecombinant ProteinsApoferritinsIronRecombinant ProteinsCapillary gel electrophoresisH-rich ferritinIron oxidationIsoferritinL-rich ferritin

Identifiers

PMID34391801
PMCPMC8461589
OpenAlexW3191085603

What OpenQuestion holds

Textmetadata
LicenceTDM
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.