Evidence map›Paper›PMID 29479520›Full record

ReviewFrontiers in cellular and infection microbiology2018

Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity.

Leonardo T Rosa, Matheus E Bianconi, Gavin H Thomas, David J Kelly

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in cellular and infection microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
15.6field-weighted citation impact, top 1% 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

63 citing papers in PubMed, 131 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Review
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  6. Review
  7. Article
  8. Article
  9. Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Exploring aggregation genes in aJournal of bacteriology · 2025
    Article
  16. Review
  17. Lipid Trafficking in Diverse Bacteria.Accounts of chemical research · 2025
    Review
  18. Article
  19. Article
  20. Vibrio natriegens: Application of a Fast-Growing Halophilic Bacterium.Advances in biochemical engineering/biotechnology · 2025
    Review

3 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 at 2 institutions in 1 country.

Leonardo T RosaDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.
Matheus E BianconiDepartment of Animal and Plant Sciences, University of Sheffield, Sheffield, United Kingdom.
Gavin H ThomasDepartment of Biology, University of York, York, United Kingdom.
David J KellyDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, United Kingdom.
University of Sheffield · GBUniversity of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability to efficiently scavenge nutrients in the host is essential for the viability of any pathogen. All catabolic pathways must begin with the transport of substrate from the environment through the cytoplasmic membrane, a role executed by membrane transporters. Although several classes of cytoplasmic membrane transporters are described, high-affinity uptake of substrates occurs through Solute Binding-Protein (SBP) dependent systems. Three families of SBP dependant transporters are known; the primary ATP-binding cassette (ABC) transporters, and the secondary Tripartite ATP-independent periplasmic (TRAP) transporters and Tripartite Tricarboxylate Transporters (TTT). Far less well understood than the ABC family, the TRAP transporters are found to be abundant among bacteria from marine environments, and the TTT transporters are the most abundant family of proteins in many species of β-proteobacteria. In this review, recent knowledge about these families is covered, with emphasis on their physiological and structural mechanisms, relating to several examples of relevant uptake systems in pathogenicity and colonization, using the SiaPQM sialic acid uptake system from

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsBiological TransportMembrane Transport ProteinsMultigene FamilyProtein BindingProtein SubunitsStructure-Activity RelationshipVirulenceAdenosine TriphosphateATP-Binding Cassette TransportersBacterial ProteinsMembrane Transport ProteinsProtein Subunitscarboxylic acidshigh-affinityperiplasmic binding-proteinssecondary transportersolute transport

Identifiers

PMID29479520
PMCPMC5812351
OpenAlexW2790373708

What OpenQuestion 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 OpenQuestion graph.