Evidence map›Paper›PMID 28876981›Full record

ReviewAnnual review of genetics2017

Genetic and Structural Analyses of RRNPP Intercellular Peptide Signaling of Gram-Positive Bacteria.

Matthew B Neiditch, Glenn C Capodagli, Gerd Prehna, Michael J Federle

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
9.7field-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

96 citing papers in PubMed, 154 citations in OpenAlex.

  1. Review
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  3. Article
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  6. Journal of bacteriology · 2026
    Review
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  8. Review
  9. Review
  10. Article
  11. Article
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  15. Article
  16. Review
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  18. The MutRS quorum-sensing system controls lantibiotic mutacin production in the human pathogenProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Review
  20. Article

36 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.

Matthew B NeiditchDepartment of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, New Jersey 07103, USA; email: matthew.neiditch@rutgers.edu , glenn.capodagli@rutgers.edu.
Glenn C CapodagliDepartment of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, The State University of New Jersey, Newark, New Jersey 07103, USA; email: matthew.neiditch@rutgers.edu , glenn.capodagli@rutgers.edu.
Gerd PrehnaCenter for Structural Biology, Research Resources Center and Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60607, USA; email: prehnag@uic.edu.
Michael J FederleDepartment of Medicinal Chemistry and Pharmacognosy and Center for Biomolecular Sciences, University of Illinois at Chicago, Chicago, Illinois 60607, USA; email: mfederle@uic.edu.
Rutgers, The State University of New Jersey · USUniversity of Illinois Chicago · US

Funding

Mechanistic Dissection of Pheromone-Dependent Regulation of Group A StreptococcalR01AI091779 · NIAID · UNIVERSITY OF ILLINOIS AT CHICAGO · PI FEDERLE, MICHAEL J · 2011 to 2021
$3.9M
Molecular Mechanisms of Rgg Receptor Regulation by Pheromones and InhibitorsR01AI125452 · NIAID · RBHS-NEW JERSEY MEDICAL SCHOOL · PI FEDERLE, MICHAEL J, NEIDITCH, MATTHEW B · 2016 to 2019
$1.9M
NIAID NIH HHS R01 AI091779NIAID NIH HHS R01 AI125452
6 · The paper itself

Abstract

Bacteria use diffusible chemical messengers, termed pheromones, to coordinate gene expression and behavior among cells in a community by a process known as quorum sensing. Pheromones of many gram-positive bacteria, such as Bacillus and Streptococcus, are small, linear peptides secreted from cells and subsequently detected by sensory receptors such as those belonging to the large family of RRNPP proteins. These proteins are cytoplasmic pheromone receptors sharing a structurally similar pheromone-binding domain that functions allosterically to regulate receptor activity. X-ray crystal structures of prototypical RRNPP members have provided atomic-level insights into their mechanism and regulation by pheromones. This review provides an overview of RRNPP prototype signaling; describes the structure-function of this protein family, which is spread widely among gram-positive bacteria; and suggests approaches to target RRNPP systems in order to manipulate beneficial and harmful bacterial behaviors.

Indexed as

Gene Expression Regulation, BacterialBacillusBacterial ProteinsBiological TransportModels, MolecularPeptidesPheromonesPhylogenyQuorum SensingReceptors, PheromoneSignal TransductionStreptococcusStructure-Activity RelationshipTrans-ActivatorsBacterial ProteinsPeptidesPheromonesReceptors, PheromoneTrans-Activatorspeptide pheromonequorum sensingRap phosphataserepeat domainsignal transduction

Identifiers

PMID28876981
PMCPMC6588834
OpenAlexW2623959065

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.