Evidence map›Paper›PMID 21880957›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Bacterial outer membrane channel for divalent metal ion acquisition.

Thomas H Hohle, William L Franck, Gary Stacey, Mark R O'Brian

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
7.0field-weighted citation impact, top 4% 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

36 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
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  4. Article
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  6. Review
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  8. Live and inactivatedFrontiers in immunology · 2023
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Comparative Phenotypic Analysis ofJournal of microbiology and biotechnology · 2021
    Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Transcriptome and Proteome of Fish-PathogenicFrontiers in microbiology · 2018
    Article
  20. Manganese scavenging and oxidative stress response mediated by type VI secretion system inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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 at 2 institutions in 1 country.

Thomas H HohleDepartment of Biochemistry, State University of New York, Buffalo, NY 14214, USA.
William L Franck
Gary Stacey
Mark R O'Brian
University at Buffalo, State University of New York · USUniversity of Missouri · US

Funding

Regulation of Bacterial Heme MetabolismR01GM067966 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI O'BRIAN, MARK R · 2004 to 2012
$2.2M
NIAID NIH HHS T32AI707614NIGMS NIH HHS R01 GM067966
6 · The paper itself

Abstract

The prevailing model of bacterial membrane function predicts that the outer membrane is permeable to most small solutes because of pores with limited selectivity based primarily on size. Here, we identified mnoP in the Gram-negative bacterium Bradyrhizobium japonicum as a gene coregulated with the inner membrane Mn(2+) transporter gene mntH. MnoP is an outer membrane protein expressed specifically under manganese limitation. MnoP acts as a channel to facilitate the tranlocation of Mn(2+), but not Co(2+) or Cu(2+), into reconstituted proteoliposomes. An mnoP mutant is defective in high-affinity Mn(2+) transport into cells and has a severe growth phenotype under manganese limitation. We suggest that the outer membrane is a barrier to divalent metal ions that requires a selective channel to meet the nutritional needs of the cell.

Indexed as

Bacterial Outer Membrane ProteinsBacterial ProteinsBinding SitesBiological TransportBradyrhizobiumCations, DivalentCation Transport ProteinsGene Expression Regulation, BacterialGenes, BacterialIon ChannelsLiposomesManganeseMetalsPromoter Regions, GeneticProtein BindingProtein Structure, SecondaryBacterial Outer Membrane ProteinsBacterial ProteinsCations, DivalentCation Transport ProteinsIon ChannelsLiposomesManganeseMetalsMntH protein, bacteria

Identifiers

PMID21880957
PMCPMC3174606
OpenAlexW1989117650

What OpenQuestion holds

Textmetadata
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.