Evidence map›Paper›PMID 28645224›Full record

ReviewAnnual review of microbiology2017

A Symphony of Cyclases: Specificity in Diguanylate Cyclase Signaling.

Kurt M Dahlstrom, George A O'Toole

Open access · bronzeAbstract readReview
In one paragraph

Review in Annual review of microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 104 citations in OpenAlex.

  1. Article
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  17. Review
  18. ACS synthetic biology · 2023
    Article
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  20. Article

6 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

2 authors at 1 institution in 1 country.

Kurt M DahlstromDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire 03755; email: georgeo@dartmouth.edu.
George A O'TooleDepartment of Microbiology and Immunology, Geisel School of Medicine at Dartmouth, Hanover, New Hampshire 03755; email: georgeo@dartmouth.edu.
Dartmouth College · US

Funding

Molecular and Cellular Biology at DartmouthT32GM008704 · NIGMS · DARTMOUTH COLLEGE · PI COMPTON, DUANE A. · 1998 to 2018
$6.8M
Molecular mechanism regulating periplasmic proteolysis in bacterial pathogenesisR01AI097307 · NIAID · CORNELL UNIVERSITY · PI O'TOOLE, GEORGE A., SONDERMANN, HOLGER · 2012 to 2016
$1.9M
Molecular mechanism regulating periplasmic proteolysis in bacterial pathogenesisR01GM123609 · NIGMS · CORNELL UNIVERSITY · PI O'TOOLE, GEORGE A., SONDERMANN, HOLGER · 2017 to 2020
$1.3M
NIAID NIH HHS R01 AI097307NIGMS NIH HHS R01 GM123609NIGMS NIH HHS T32 GM008704
6 · The paper itself

Abstract

Cyclic diguanylate (c-di-GMP) is a near universal signaling molecule produced by diguanylate cyclases that can direct a variety of bacterial behaviors. A major area of research over the last several years has been aimed at understanding how a cell with dozens of diguanylate cyclases can deploy a given subset of them to produce a desired phenotypic outcome without undesired cross talk between c-di-GMP-dependent systems. Several models have been put forward to address this question, including specificity of cyclase activation, tuned binding constants of effector proteins, and physical interaction between cyclases and effectors. Additionally, recent evidence has suggested that there may be a link between the catalytic state of a cyclase and its physical contact with an effector. This review highlights several key studies, examines the proposed global and local models of c-di-GMP signaling specificity in bacteria, and attempts to identify the most fruitful steps that can be taken to better understand how dynamic networks of sibling cyclases and effector proteins result in sensible outputs that govern cellular behavior.

Indexed as

Gene Expression Regulation, BacterialSignal TransductionBacteriaCyclic GMPEscherichia coli ProteinsModels, BiologicalPhosphorus-Oxygen LyasesProtein BindingSubstrate Specificitybis(3',5')-cyclic diguanylic acidCyclic GMPdiguanylate cyclaseEscherichia coli ProteinsPhosphorus-Oxygen Lyasesbiofilmsc-di-GMPcyclic diguanylatediguanylate cyclasesignaling specificity

Identifiers

PMID28645224
PMCPMC5936083
OpenAlexW2604083163

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.