Evidence map›Paper›PMID 26055720›Full record

ReviewThe Journal of biological chemistry2015

Microbial Copper-binding Siderophores at the Host-Pathogen Interface.

Eun-Ik Koh, Jeffrey P Henderson

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 72 citations in OpenAlex.

  1. Structural and Functional Siderophore Remodeling by Enzymatic Delipidation.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Comparative metabolomic profiling ofFrontiers in chemistry · 2023
    Article
  13. Review
  14. Oosporein Produced by Root EndophyticPlants (Basel, Switzerland) · 2022
    Article
  15. Article
  16. Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022
    Review
  17. Article
  18. Antimicrobial Activity of Metals and Metalloids.Annual review of microbiology · 2021
    Review
  19. Review
  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

2 authors at 1 institution in 1 country.

Eun-Ik KohFrom the Center for Women's Infectious Diseases Research, Division of Infectious Diseases, and Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Jeffrey P HendersonFrom the Center for Women's Infectious Diseases Research, Division of Infectious Diseases, and Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110 jhenderson@DOM.wustl.edu.
Washington University in St. Louis · US

Funding

EXPRESSION AND IRON-INDEPENDENT FUNCTIONS OF SIDEROPHORES IN URINARY TRACT INFECTR01DK099534 · NIDDK · WASHINGTON UNIVERSITY · PI HENDERSON, JEFFREY P · 2014 to 2018
$1.8M
NIDDK NIH HHS R01 DK099534NIDDK NIH HHS R01DK099534
6 · The paper itself

Abstract

Numerous pathogenic microorganisms secrete small molecule chelators called siderophores defined by their ability to bind extracellular ferric iron, making it bioavailable to microbes. Recently, a siderophore produced by uropathogenic Escherichia coli, yersiniabactin, was found to also bind copper ions during human infections. The ability of yersiniabactin to protect E. coli from copper toxicity and redox-based phagocyte defenses distinguishes it from other E. coli siderophores. Here we compare yersiniabactin to other extracellular copper-binding molecules and review how copper-binding siderophores may confer virulence-associated gains of function during infection pathogenesis.

Indexed as

Host-Pathogen InteractionsAnimalsBacterial InfectionsCoordination ComplexesCopperEscherichia coliHumansImmunity, InnateSiderophoresYersiniaCoordination ComplexesCopperSiderophorescopperhost-pathogen interactionmicrobial pathogenesissiderophoresuperoxide dismutase (SOD)

Identifiers

PMID26055720
PMCPMC4521018
OpenAlexW1611601856

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.