Evidence map›Paper›PMID 20420522›Full record

ReviewAnnual review of microbiology2010

TonB-dependent transporters: regulation, structure, and function.

Nicholas Noinaj, Maude Guillier, Travis J Barnard, Susan K Buchanan

Abstract readReview
In one paragraph

Review in Annual review of microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 528 papers.

0numbers the graph read from it
0cells of the map it votes in
528citing 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

528 citing papers in PubMed.

  1. Article
  2. Zinc Homeostasis inBiology · 2026
    Article
  3. Identification of iron and zinc responsive TonB-dependent transporters in Pseudomonas aeruginosa.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Article
  4. Article
  5. Multiple TonB-dependent transport systems inInfection and immunity · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. TheJournal of bacteriology · 2026
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Deletion ofApplied and environmental microbiology · 2026
    Article

468 more citing papers are in PubMed but not listed here.

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.

Nicholas NoinajLaboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892, USA. noinajn@niddk.nih.gov
Maude Guillier
Travis J Barnard
Susan K Buchanan

Funding

structural characterization of iron uptake from human transferrinZIADK036143 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2009 to 2013
$3.1M
Intramural NIH HHS ZIA DK036143
6 · The paper itself

Abstract

TonB-dependent transporters (TBDTs) are bacterial outer membrane proteins that bind and transport ferric chelates, called siderophores, as well as vitamin B(12), nickel complexes, and carbohydrates. The transport process requires energy in the form of proton motive force and a complex of three inner membrane proteins, TonB-ExbB-ExbD, to transduce this energy to the outer membrane. The siderophore substrates range in complexity from simple small molecules such as citrate to large proteins such as serum transferrin and hemoglobin. Because iron uptake is vital for almost all bacteria, expression of TBDTs is regulated in a number of ways that include metal-dependent regulators, σ/anti-σ factor systems, small RNAs, and even a riboswitch. In recent years, many new structures of TBDTs have been solved in various states, resulting in a more complete understanding of siderophore selectivity and binding, signal transduction across the outer membrane, and interaction with the TonB-ExbB-ExbD complex. However, the transport mechanism is still unclear. In this review, we summarize recent progress in understanding regulation, structure, and function in TBDTs and questions remaining to be answered.

Indexed as

Gene Expression Regulation, BacterialBacteriaBacterial ProteinsBiological TransportCarbohydrate MetabolismEnergy MetabolismIronMembrane ProteinsMembrane Transport ProteinsModels, BiologicalNickelProton-Motive ForceSiderophoresVitamin B 12Bacterial ProteinsIronMembrane ProteinsMembrane Transport ProteinsNickelSiderophorestonB protein, BacteriaVitamin B 12

Identifiers

PMID20420522
PMCPMC3108441

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.