Cavity acidification limits ferritin iron biomineralization.

Zhiheng Wang, Yiwen Wang, Ivan J Dmochowski

Abstract read

In one paragraph

Article in Journal of inorganic biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

3 authors.

Zhiheng WangDepartment of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA 19104-6323, USA.

Yiwen WangDepartment of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA 19104-6323, USA.

Ivan J DmochowskiDepartment of Chemistry, University of Pennsylvania, 231 S. 34th Street, Philadelphia, PA 19104-6323, USA. Electronic address: ivandmo@sas.upenn.edu.

Funding

Designer Molecular Probes for Biomedical ApplicationsR35GM131907 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ivan Julian Dmochowski · 2019 to 2026

$4.7M

NIGMS NIH HHS R35 GM131907

6 · The paper itself

Abstract

Studies of ferritin biomineralization have elucidated iron loading/egress pathways and mechanisms of iron oxidation, while paying less attention to the spatiotemporal details of proton generation during iron hydrolysis. Here, we performed ferroxidase reactions with Archaeoglobus fulgidus ferritin (AfFtn) 24mer cage, which allows site-specific labeling as a dimer at low ionic strength and reassembly into a 24mer at high ionic strength. Cysteines engineered on the ferritin interior surface were covalently labeled with fluorescein-5-maleimide (F5M), which reported the dynamic changes in proton activity during ferroxidase chemistry. F5M labeled at D61C was highly responsive to proton generation and release, without being vulnerable to fluorescence quenching by Fe

Indexed as

Archaeoglobus fulgidusBiomineralizationCeruloplasminFerritinsIronFluoresceinHydrogen-Ion ConcentrationOxidation-ReductionProtonsCeruloplasminFerritinsFluoresceinIronProtonsFerroxidase activityFluoresceinIron hydrolysispH sensingProton transfer

Identifiers

PMID41616735

DOI10.1016/j.jinorgbio.2026.113242

PMCPMC13071896

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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.