Evidence map›Paper›PMID 41659615›Full record

ArticlebioRxiv : the preprint server for biology2026

Structural and functional basis of proton-independent transition metal import by a canonical bacterial Nramp transporter.

Shamayeeta Ray, Samuel P Berry, Rachelle Gaudet

Abstract readPreprint
In one paragraph

Article in bioRxiv : the preprint server for biology, 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

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Shamayeeta RayDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138 USA.ORCID 0000-0001-7906-0572
Samuel P BerryDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138 USA.ORCID 0000-0002-3480-5988
Rachelle GaudetDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138 USA.ORCID 0000-0002-9177-054X

Funding

User Training & OutreachP30GM138396 · NIGMS · UCHICAGO ARGONNE, LLC · PI ROBERT F. FISCHETTI, JANET L. SMITH · 2020 to 2026
$34.3M
Mechanism of Divalent Metal Transport by NRamp-Family TransportersR01GM120996 · NIGMS · HARVARD UNIVERSITY · PI GAUDET, RACHELLE · 2017 to 2024
$3.0M
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
NIGMS NIH HHS P30 GM138396NIGMS NIH HHS R01 GM120996NIH HHS S10 OD012289
6 · The paper itself

Abstract

Natural resistance-associated macrophage proteins (Nramps) are divalent transition metal transporters found in most organisms, typically coupling metal uptake to proton co-transport. How this coupling evolved, however, remains unclear. We present structural, functional, and evolutionary analyses of a clade B Nramp from the gut bacterium

Identifiers

PMID41659615
PMCPMC12873925

What OpenQuestion holds

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LicenceCC BY
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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.