Evidence map›Paper›PMID 29953152›Full record

ReviewMetallomics : integrated biometal science2018

Toward a mechanistic understanding of Feo-mediated ferrous iron uptake.

Alexandrea E Sestok, Richard O Linkous, Aaron T Smith

Abstract readReview
In one paragraph

Review in Metallomics : integrated biometal science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
5.4field-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

59 citing papers in PubMed, 95 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Understanding Iron and Oxidative Stress Response inbioRxiv : the preprint server for biology · 2026
    Article
  6. The response regulator BqsR/CarR controls ferrous iron (FebioRxiv : the preprint server for biology · 2025
    Article
  7. The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025
    Article
  8. Methanotroph Methylotuvimicrobium alcaliphilum 20Z-3E as a fumarate producer: transcriptomic analysis and the role of malic enzyme.International microbiology : the official journal of the Spanish Society for Microbiology · 2025
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Structural Determinants ofbioRxiv : the preprint server for biology · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Alexandrea E SestokDepartment of Chemistry and Biochemistry, University of Maryland, Baltimore County, Baltimore, Maryland 21250, USA. smitha@umbc.edu.
Richard O Linkous
Aaron T Smith
University of Baltimore · US

Funding

Graduate Training at The Chemistry Biology InterfaceT32GM066706 · NIGMS · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SELEY-RADTKE, KATHERINE L, SMITH, AARON T · 2004 to 2023
$3.3M
NIGMS NIH HHS T32 GM066706
6 · The paper itself

Abstract

Virtually all organisms require iron and have evolved to obtain this element in free or chelated forms. Under anaerobic or low pH conditions commonly encountered by numerous pathogens, iron predominantly exists in the ferrous (Fe2+) form. The ferrous iron transport (Feo) system is the only widespread mechanism dedicated solely to bacterial ferrous iron import, and this system has been linked to pathogenic virulence, bacterial colonization, and microbial survival. The canonical feo operon encodes for three proteins that comprise the Feo system: FeoA, a small cytoplasmic β-barrel protein; FeoB, a large, polytopic membrane protein with a soluble G-protein domain capable of hydrolyzing GTP; and FeoC, a small, cytoplasmic protein containing a winged-helix motif. While previous studies have revealed insight into soluble and fragmentary domains of the Feo system, the chief membrane-bound component FeoB remains poorly studied. However, recent advances have demonstrated that large quantities of intact FeoB can be overexpressed, purified, and biophysically characterized, revealing glimpses into FeoB function. Two models of full-length FeoB have been published, providing starting points for hypothesis-driven investigations into the mechanism of FeoB-mediated ferrous iron transport. Finally, in vivo studies have begun to shed light on how this system functions as a unique multicomponent complex. In light of these new data, this review will summarize what is known about the Feo system, including recent advancements in FeoB structure and function.

Indexed as

VirulenceCation Transport ProteinsCell MembraneEscherichia coli ProteinsFerrous CompoundsGene Expression Regulation, BacterialIon TransportIronMembrane Transport ProteinsOperonProtein ConformationCation Transport ProteinsEscherichia coli Proteinsfeo protein, E coliFerrous CompoundsIronMembrane Transport Proteins

Identifiers

PMID29953152
PMCPMC6051883
OpenAlexW2809675268

What OpenQuestion holds

Textmetadata
LicenceTDM
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.