Evidence map›Paper›PMID 25684173›Full record

ArticleProteomics2015

Alteration in abundance of specific membrane proteins of Aggregatibacter actinomycetemcomitans is attributed to deletion of the inner membrane protein MorC.

Kenneth P Smith, Julia G Fields, Richard D Voogt, Bin Deng, Ying-Wai Lam, Keith P Mintz

Open access · greenAbstract read
In one paragraph

Article in Proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

10 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Virulence and Pathogenicity Properties ofPathogens (Basel, Switzerland) · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. 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

6 authors at 2 institutions in 1 country.

Kenneth P SmithDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
Julia G FieldsDepartment of Biology, University of Vermont, Burlington, VT, USA.
Richard D VoogtDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
Bin DengDepartment of Biology, University of Vermont, Burlington, VT, USA.
Ying-Wai LamDepartment of Biology, University of Vermont, Burlington, VT, USA.
Keith P MintzDepartment of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT, USA.
University of Vermont · USVermont Oxford Network · US

Funding

Vermont INBRE Administrative Supplement 2024 AWD 118P20GM103449 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI CHRISTOPHER S FRANCKLYN · 2012 to 2026
$58.4M
Environmental Adaptation and Membrane Physiology of an Oral PathogenR01DE018889 · NIDCR · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI MINTZ, KEITH PETER · 2009 to 2013
$1.8M
NIDCR NIH HHS R01 DE018889NIDCR NIH HHS R01-DE018889NIGMS NIH HHS P20 GM103449NIGMS NIH HHS P20GM103449
6 · The paper itself

Abstract

Aggregatibacter actinomycetemcomitans is an important pathogen in the etiology of human periodontal and systemic diseases. Inactivation of the gene coding for the inner membrane protein, morphogenesis protein C (MorC), results in pleotropic effects pertaining to the membrane structure and function of this bacterium. The role of this protein in membrane biogenesis is unknown. To begin to understand the role of this conserved protein, stable isotope dimethyl labeling in conjunction with MS was used to quantitatively analyze differences in the membrane proteomes of the isogenic mutant and wild-type strain. A total of 613 proteins were quantified and 601 of these proteins were found to be equal in abundance between the two strains. The remaining 12 proteins were found in lesser (10) or greater (2) abundance in the membrane preparation of the mutant strain compared with the wild-type strain. The 12 proteins were ascribed functions associated with protein quality control systems, oxidative stress responses, and protein secretion. The potential relationship between these proteins and the phenotypes of the MorC mutant strain is discussed.

Indexed as

Gene DeletionAggregatibacter actinomycetemcomitansBacterial ProteinsCell MembraneMembrane ProteinsMutationProteomicsBacterial ProteinsMembrane ProteinsChaperone proteinsLeukotoxin secretionMicrobiologyType I secretion

Identifiers

PMID25684173
PMCPMC4456248
OpenAlexW2153258481

What OpenQuestion holds

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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.