Evidence map›Paper›PMID 26156628›Full record

ArticleSmall GTPases2015

Dual function of a bacterial protein as an adhesin and extracellular effector of host GTPase signaling.

Daniel Henry Stones, Anne Marie Krachler

Open access · hybridAbstract read
In one paragraph

Article in Small GTPases, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Saudi journal of medicine & medical sciences
    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

2 authors at 2 institutions in 2 countries.

Daniel Henry Stonesa Institute of Microbiology and Infection ; School of Biosciences ; University of Birmingham ; Edgbaston, Birmingham , United Kingdom.
Anne Marie Krachler
Czech Academy of Sciences, Institute of Microbiology · CZUniversity of Birmingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L007916/1Wellcome Trust ISSFPP76
6 · The paper itself

Abstract

Bacterial pathogens often target conserved cellular mechanisms within their hosts to rewire signaling pathways and facilitate infection. Rho GTPases are important nodes within eukaryotic signaling networks and thus constitute a common target of pathogen-mediated manipulation. A diverse array of microbial mechanisms exists to interfere with Rho GTPase signaling. While targeting of GTPases by secreted bacterial effectors is a well-known strategy bacterial pathogens employ to interfere with the host, we have recently described pathogen adhesion as a novel extracellular stimulus that hijacks host GTPase signaling. The Multivalent Adhesion Molecule MAM7 from Vibrio parahaemolyticus directly binds host cell membrane lipids. The ensuing coalescence of phosphatidic acid ligands in the host membrane leads to downstream activation of RhoA and actin rearrangements. Herein, we discuss mechanistic models of lipid-mediated Rho activation and the implications from the infected host's and the pathogen's perspective.

Indexed as

ActinsAdhesins, BacterialBacterial ProteinsGTP PhosphohydrolasesHost-Pathogen InteractionsHumansMembrane LipidsrhoA GTP-Binding ProteinSignal TransductionVibrio InfectionsVibrio parahaemolyticusActinsAdhesins, BacterialBacterial ProteinsGTP PhosphohydrolasesMembrane LipidsrhoA GTP-Binding ProteinRHOA protein, humanactin dynamicsadhesineffectorhost-pathogen interactionlipid signalingphosphatidic acidRhoARho GTPasesVibrio

Identifiers

PMID26156628
PMCPMC4601360
OpenAlexW1935048644

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.