Evidence map›Paper›PMID 29030429›Full record

ArticleThe Journal of biological chemistry2017

Activating mutations in quorum-sensing regulator Rgg2 and its conformational flexibility in the absence of an intermolecular disulfide bond.

Reid V Wilkening, Glenn C Capodagli, Atul Khataokar, Kaitlyn M Tylor, Matthew B Neiditch, Michael J Federle

Open access · hybridAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Structure-function studies of Rgg binding to pheromones and target promoters reveal a model of transcription factor interplay.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  3. 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.

Reid V WilkeningFrom the Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60607.
Glenn C Capodaglithe Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, State University of New Jersey, Newark, New Jersey 07103, and.
Atul Khataokarthe Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, State University of New Jersey, Newark, New Jersey 07103, and.
Kaitlyn M TylorFrom the Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60607.
Matthew B Neiditchthe Department of Microbiology, Biochemistry, and Molecular Genetics, New Jersey Medical School, Rutgers, State University of New Jersey, Newark, New Jersey 07103, and matthew.neiditch@rutgers.edu.
Michael J FederleFrom the Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 60607, mfederle@uic.edu.
Rutgers New Jersey Medical SchoolUniversity 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

Rap/Rgg/NprR/PlcR/PrgX (RRNPP) quorum-sensing systems use extracellular peptide pheromones that are detected by cytoplasmic receptors to regulate gene expression in firmicute bacteria. Rgg-type receptors are allosterically regulated through direct pheromone binding to control transcriptional activity; however, the receptor activation mechanism remains poorly understood. Previous work has identified a disulfide bond between Cys-45 residues within the homodimer interface of Rgg2 from

Indexed as

Models, MolecularPoint MutationAmino Acid SubstitutionBacterial ProteinsBinding SitesCrystallography, X-RayCyclosporineCysteineDimerizationDrug Resistance, BacterialKineticsMutagenesis, Site-DirectedPheromonesProtein ConformationProtein Interaction Domains and MotifsProtein IsoformsBacterial ProteinsCyclosporineCysteinePheromonesProtein IsoformsRecombinant Proteinsrgg protein, StreptococcusTrans-ActivatorsTranscription Factorsbacterial transcriptiondisulfidepheromoneStreptococcus pyogenes (S. pyogenes)X-ray crystallography

Identifiers

PMID29030429
PMCPMC5733591
OpenAlexW2763937263

What OpenQuestion holds

Textmetadata
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.