Evidence map›Paper›PMID 38780762›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2024

Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/O

Narmada Behera, Gargee Bhattacharyya, Satyabrat Behera, Rabindra K Behera

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Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

4 authors.

Narmada BeheraDepartment of Chemistry, National Institute of Technology, Rourkela, Odisha, 769008, India.
Gargee BhattacharyyaDepartment of Chemistry, National Institute of Technology, Rourkela, Odisha, 769008, India.
Satyabrat BeheraDepartment of Chemistry, National Institute of Technology, Rourkela, Odisha, 769008, India.
Rabindra K BeheraDepartment of Chemistry, National Institute of Technology, Rourkela, Odisha, 769008, India. beherarabi@nitrkl.ac.in.

Funding

Science and Engineering Research Board CRG/2020/005332
6 · The paper itself

Abstract

Ferritins are multimeric nanocage proteins that sequester/concentrate excess of free iron and catalytically synthesize a hydrated ferric oxyhydroxide bio-mineral. Besides functioning as the primary intracellular iron storehouses, these supramolecular assemblies also oversee the controlled release of iron to meet physiologic demands. By virtue of the reducing nature of the cytosol, reductive dissolution of ferritin-iron bio-mineral by physiologic reducing agents might be a probable pathway operating in vivo. Herein, to explore this reductive iron-release pathway, a series of quinone analogs differing in size, position/nature of substituents and redox potentials were employed to relay electrons from physiologic reducing agent, NADH, to the ferritin core. Quinones are well known natural electron/proton mediators capable of facilitating both 1/2 electron transfer processes and have been implicated in iron/nutrient acquisition in plants and energy transduction. Our findings on the structure-reactivity of quinone mediators highlight that iron release from ferritin is dictated by electron-relay capability (dependent on E

Indexed as

FerritinsIronNADOxidation-ReductionQuinonesReactive Oxygen SpeciesMycobacteriumOxygenFerritinsIronNADOxygenQuinonesReactive Oxygen SpeciesElectron transferFerritinIron releaseMediatorProtein-cageQuinones

Identifiers

PMID38780762

What OpenQuestion holds

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Registered trials

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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.