Evidence map›Paper›PMID 20860484›Full record

ReviewFuture microbiology2010

The TonB energy transduction systems in Vibrio species.

Carole J Kuehl, Jorge H Crosa

Open access · greenAbstract readReview
In one paragraph

Review in Future microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

28 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Analysis of SixInfection and immunity · 2022
    Article
  6. Ferric quinate (QPLEX) interacts with the major outer membrane protein (MOMP) ofComputational and structural biotechnology journal · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Fish PathogenMicroorganisms · 2019
    Article
  13. Article
  14. Iron Acquisition Strategies ofFrontiers in cellular and infection microbiology · 2017
    Review
  15. Article
  16. Review
  17. Article
  18. Plasmid- and chromosome-encoded siderophore anguibactin systems found in marine vibrios: biosynthesis, transport and evolution.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2013
    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

2 authors at 1 institution in 1 country.

Carole J KuehlDepartment of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, 97239, USA.
Jorge H Crosa
Oregon Health & Science University · US

Funding

INTERACTIONS AT THE MICROBE/HOST INTERFACET32AI007472 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI LANDFEAR, SCOTT M · 1995 to 2019
$6.7M
IRON UPTAKE AS A VIRULENCE FACTOR IN PATHOGENIC VIBRIOSR01AI019018 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI CROSA, JORGE H · 1985 to 2011
$3.9M
Iron and pathogenesis in infections by Vibrio vulnificusR01AI065981 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI CROSA, JORGE H · 2007 to 2011
$2.1M
Studies of the Influence of Microbial Co-infection on HIV InfectionZ01AI000747 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI MORIUCHI, HIROYUKI · 1998 to 2000
–
NIAID NIH HHS 5R01-AI 019018NIAID NIH HHS 5R01-AI 065981NIAID NIH HHS 5T32-AI 007472‑13NIAID NIH HHS R01 AI019018NIAID NIH HHS R01 AI065981NIAID NIH HHS T32 AI007472
6 · The paper itself

Abstract

Studying the organization and conservation of the TonB systems across the genus Vibrio, we can tease out trends in gene arrangement and function that lead to clues about the evolution and necessity of the proteins in multiple TonB systems. The TonB2 systems, with additional TtpC proteins, are in general more promiscuous regarding their interactions with many different TonB-dependent transporters in the outer membrane. Studies show that the TtpC protein spans the periplasmic space, suggesting that it can be the connection between the energy from the proton motive force and the outer membrane protein receptors, which the shorter TonB2 cannot provide. As an earlier system, the combination of the TtpC protein and a TonB2 system must have been necessary for the function of the smaller TonB2 protein and to transduce energy in a medium that can have osmotic challenges.

Indexed as

Biological TransportAnimalsBacterial ProteinsFish DiseasesHumansIronMembrane ProteinsMiceProton-Motive ForceSiderophoresVibrioVibrio InfectionsVirulenceBacterial ProteinsIronMembrane ProteinsSiderophorestonB protein, Bacteria

Identifiers

PMID20860484
PMCPMC3032567
OpenAlexW2114240493

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.