Evidence map›Paper›PMID 27409636›Full record

ReviewToxins2016

Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways.

Meenakumari Muthuramalingam, John C White, Christina R Bourne

Open access · goldAbstract readReview
In one paragraph

Review in Toxins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
9.6field-weighted citation impact, top 2% 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

55 citing papers in PubMed, 97 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. TheApplied and environmental microbiology · 2024
    Article
  9. The Bro-Xre toxin-antitoxin modules inFrontiers in microbiology · 2024
    Article
  10. Article
  11. Identification of Genes Encoded Toxin-Antitoxin System inInfectious disorders drug targets · 2024
    Article
  12. Review
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Meenakumari MuthuramalingamDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA. meena85@ou.edu.
John C WhiteDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA. John.C.White-1@ou.edu.
Christina R BourneDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019, USA. cbourne@ou.edu.
University of Oklahoma · US

Funding

Structure-Function Studies of MsvR, a Methanogen-Specific Transcriptional RegulaP20GM103640 · NIGMS · UNIVERSITY OF OKLAHOMA · PI THOMAS, LEONARD M · 2012 to 2021
$20.4M
NIGMS NIH HHS P20 GM103640
6 · The paper itself

Abstract

Toxin-antitoxin (TA) modules are bacterial regulatory switches that facilitate conflicting outcomes for cells by promoting a pro-survival phenotypic adaptation and/or by directly mediating cell death, all through the toxin activity upon degradation of antitoxin. Intensive study has revealed specific details of TA module functions, but significant gaps remain about the molecular details of activation via antitoxin degradation used by different bacteria and in different environments. This review summarizes the current state of knowledge about the interaction of antitoxins with cellular proteases Lon and ClpP to mediate TA module activation. An understanding of these processes can answer long-standing questions regarding stochastic versus specific activation of TA modules and provide insight into the potential for manipulation of TA modules to alter bacterial growth.

Indexed as

Signal TransductionAnimalsAnti-Bacterial AgentsAntitoxinsBacteriaBacterial ToxinsEndopeptidase ClpEnzyme ActivationHost-Pathogen InteractionsHumansProtease LaProteolysisAnti-Bacterial AgentsAntitoxinsBacterial ToxinsEndopeptidase ClpProtease Labacterial physiologycellular proteasesenvironmental adaptationpersister cellsphenotypic changespost-segregational killingprotease adaptorstoxin-antitoxin

Identifiers

PMID27409636
PMCPMC4963847
OpenAlexW2474500496

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.