Evidence map›Paper›PMID 24102308›Full record

ReviewInorganic chemistry2013

Ferritin: the protein nanocage and iron biomineral in health and in disease.

Elizabeth C Theil

Abstract readReview
In one paragraph

Review in Inorganic chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
8.8field-weighted citation impact, top 2% 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

110 citing papers in PubMed, 245 citations in OpenAlex.

  1. Article
  2. Chemical reviews · 2026
    Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Observational
  14. Article
  15. Review
  16. Article
  17. Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Article
  18. Article
  19. Review
  20. Article

50 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Elizabeth C TheilChildren's Hospital Oakland Research Institute (CHORI) , 5700 Martin Luther King Jr. Way, Oakland, California 94609, United States , and Department of Molecular and Structural Biochemistry, North Carolina State University , Raleigh, North Carolina 2765-7622, United States.
North Carolina State University · US

Funding

RED CELL FERRITIN: ONTOGENETIC CONTROLR01DK020251 · NIDDK · NORTH CAROLINA STATE UNIVERSITY RALEIGH · PI GOSS, DIXIE J, THEIL, ELIZABETH C · 1986 to 2010
$5.1M
Ferritin: Protein/mRNA/DNA in Fe/O Regulation/MetabolismR56DK020251 · NIDDK · CHILDREN'S HOSPITAL & RES CTR AT OAKLAND · PI GOSS, DIXIE J, THEIL, ELIZABETH C · 2008 to 2008
$120k
NIDDK NIH HHS R01 DK020251NIDDK NIH HHS R01-DK20251NIDDK NIH HHS R56 DK020251
6 · The paper itself

Abstract

At the center of iron and oxidant metabolism is the ferritin superfamily: protein cages with Fe(2+) ion channels and two catalytic Fe/O redox centers that initiate the formation of caged Fe2O3·H2O. Ferritin nanominerals, initiated within the protein cage, grow inside the cage cavity (5 or 8 nm in diameter). Ferritins contribute to normal iron flow, maintenance of iron concentrates for iron cofactor syntheses, sequestration of iron from invading pathogens, oxidant protection, oxidative stress recovery, and, in diseases where iron accumulates excessively, iron chelation strategies. In eukaryotic ferritins, biomineral order/crystallinity is influenced by nucleation channels between active sites and the mineral growth cavity. Animal ferritin cages contain, uniquely, mixtures of catalytically active (H) and inactive (L) polypeptide subunits with varied rates of Fe(2+)/O2 catalysis and mineral crystallinity. The relatively low mineral order in liver ferritin, for example, coincides with a high percentage of L subunits and, thus, a low percentage of catalytic sites and nucleation channels. Low mineral order facilitates rapid iron turnover and the physiological role of liver ferritin as a general iron source for other tissues. Here, current concepts of ferritin structure/function/genetic regulation are discussed and related to possible therapeutic targets such as mini-ferritin/Dps protein active sites (selective pathogen inhibition in infection), nanocage pores (iron chelation in therapeutic hypertransfusion), mRNA noncoding, IRE riboregulator (normalizing the ferritin iron content after therapeutic hypertransfusion), and protein nanovessels to deliver medicinal or sensor cargo.

Indexed as

AnemiaAnimalsCatalytic DomainDrug Delivery SystemsFerritinsHemosiderinHumansIron OverloadMolecular Targeted TherapyNanostructuresRNA, MessengerTransfusion ReactionFerritinsHemosiderinRNA, Messenger

Identifiers

PMID24102308
PMCPMC3882016
OpenAlexW2016151582

What OpenQuestion holds

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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.