Evidence map›Paper›PMID 30714568›Full record

ArticleeLife2019

Structures in multiple conformations reveal distinct transition metal and proton pathways in an Nramp transporter.

Aaron T Bozzi, Christina M Zimanyi, John M Nicoludis, Brandon K Lee, Casey H Zhang, Rachelle Gaudet

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 72 citations in OpenAlex.

  1. A redox- and proton-coupled inner membrane transporter mediates copper import to the bacterial cytoplasm.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  10. The mntH gene of Burkholderia cenocepacia influences motility and quorum sensing to control virulence.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
  11. Article
  12. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Iron from the gut: the role of divalent metal transporter 1.Journal of clinical biochemistry and nutrition · 2024
    Article
  18. Article
  19. Review
  20. 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

6 authors at 1 institution in 1 country.

Aaron T Bozzi *Department of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0003-4245-8725
Christina M Zimanyi *Department of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-6782-507X
John M NicoludisDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-3755-7844
Brandon K LeeDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.
Casey H ZhangDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.
Rachelle GaudetDepartment of Molecular and Cellular Biology, Harvard University, Cambridge, United States.ORCID 0000-0002-9177-054X
Harvard University · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Mechanism of Divalent Metal Transport by NRamp-Family TransportersR01GM120996 · NIGMS · HARVARD UNIVERSITY · PI GAUDET, RACHELLE · 2017 to 2024
$3.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS 1R01GM120996NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM120996
6 · The paper itself

Abstract

Nramp family transporters-expressed in organisms from bacteria to humans-enable uptake of essential divalent transition metals via an alternating-access mechanism that also involves proton transport. We present high-resolution structures of

Indexed as

Protein ConformationBinding SitesCation Transport ProteinsCrystallography, X-RayDeinococcusIon TransportManganeseMetalsModels, MolecularNatural Resistance-associated Macrophage Protein 1Protein FoldingProtonsSignal TransductionCation Transport ProteinsManganeseMetalsNatural Resistance-associated Macrophage Protein 1Protonsbiochemistrychemical biologyDeinococcus radioduransE. coliLeuT foldMntHmolecular biophysicssecondary transporterSLC11structural biologyx-ray crystallography

Identifiers

PMID30714568
PMCPMC6398981
OpenAlexW2889494942

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.