Evidence map›Paper›PMID 39626085›Full record

ReviewMolecular microbiology2024

Substrate Uptake by TonB-Dependent Outer Membrane Transporters.

Volkmar Braun

Abstract readReview
In one paragraph

Review in Molecular microbiology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Structural and Functional Siderophore Remodeling by Enzymatic Delipidation.Angewandte Chemie (International ed. in English) · 2026
    Article
  2. Article
  3. Multiple TonB-dependent transport systems inInfection and immunity · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Advances in understanding Ton and Tol system motor proteins.Biochemical Society transactions · 2026
    Review
  13. Article
  14. Article
  15. Microbial metal physiology: ions to ecosystems.Nature reviews. Microbiology · 2025
    Review
  16. Review
  17. Targeting Siderophore Biosynthesis to Thwart Microbial Growth.International journal of molecular sciences · 2025
    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

1 author.

Volkmar BraunMax-Planck-Institute of Biology, Tübingen, Germany.ORCID 0000-0003-0093-8595

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TonB is an essential component of an energy-generating system that powers active transport across the outer membrane (OM) of compounds that are too large or too scarce to diffuse through porins. The TonB-dependent OM transport proteins (TBDTs) consist of β barrels forming pores that are closed by plugs. The binding of TonB to TBDTs elicits plug movement, which opens the pores and enables nutrient translocation from the cell surface into the periplasm. TonB is also involved in the uptake of certain proteins, particularly toxins, through OM proteins that differ structurally from TBDTs. TonB binds to a sequence of five residues, designated as the TonB box, which is conserved in all TBDTs. Energy from the proton motive force (pmf) of the cytoplasmic membrane is transmitted to TonB by two proteins, ExbB and ExbD. These proteins form an energy-transmitting protein complex consisting of five ExbB proteins, forming a pore that encloses the ExbD dimer. This review discusses the structural changes that occur in TBDTs upon interaction with TonB, as well as the interaction of ExbB-ExbD with TonB, which is required to transmit the energy of the pmf and thereby open TBDT pores. TonB facilitates import of a wide range of substrates.

Indexed as

Bacterial Outer Membrane ProteinsEscherichia coli ProteinsMembrane Transport ProteinsBacterial ProteinsBiological TransportCell MembraneEscherichia coliMembrane ProteinsBacterial Outer Membrane ProteinsBacterial ProteinsEscherichia coli ProteinsExbB protein, E coliexbD protein, E coliMembrane ProteinsMembrane Transport ProteinstonB protein, BacteriatonB protein, E colienergy deliveryTonB proteintransport

Identifiers

PMID39626085
PMCPMC11658791

What Socratic 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 Socratic graph.