Evidence map›Paper›PMID 35121656›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

A hyperpromiscuous antitoxin protein domain for the neutralization of diverse toxin domains.

Tatsuaki Kurata, Chayan Kumar Saha, Jessica A Buttress, Toomas Mets, Tetiana Brodiazhenko, Kathryn J Turnbull, Ololade F Awoyomi, Sofia Raquel Alves Oliveira, Steffi Jimmy, Karin Ernits and 6 more

Open access · hybridAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
7.1field-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

22 citing papers in PubMed, 39 citations in OpenAlex.

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  9. Microbiology spectrum · 2024
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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

16 authors at 7 institutions in 6 countries.

Tatsuaki KurataDepartment of Experimental Medicine, University of Lund, 221 84 Lund, Sweden.
Chayan Kumar SahaDepartment of Experimental Medicine, University of Lund, 221 84 Lund, Sweden.ORCID 0000-0002-5357-517X
Jessica A ButtressCenter for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, United Kingdom.ORCID 0000-0001-8822-6917
Toomas MetsUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.ORCID 0000-0002-6796-7000
Tetiana BrodiazhenkoUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.
Kathryn J TurnbullDepartment of Clinical Microbiology, Rigshospitalet, 2200 Copenhagen, Denmark.
Ololade F AwoyomiDepartment of Medical Biochemistry and Biophysics, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0002-6263-0142
Sofia Raquel Alves OliveiraUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.ORCID 0000-0001-6090-6742
Steffi JimmyCenter for Structural Systems Biology, Deutsches Elektronen-Synchrotron, 22607 Hamburg, Germany.
Karin ErnitsDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0003-1072-4945
Maxence DelannoyDépartement Génie Biologique, Campus SophiaTech, Université Nice Sophia Antipolis, 06000 Nice, France.
Karina PerssonDepartment of Chemistry, Umeå University, 901 87 Umeå, Sweden.ORCID 0000-0003-0807-0348
Tanel TensonUniversity of Tartu, Institute of Technology, 50411 Tartu, Estonia.ORCID 0000-0002-0260-3601
Henrik StrahlCenter for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne NE2 4AX, United Kingdom.ORCID 0000-0003-4416-2178
Vasili HauryliukDepartment of Experimental Medicine, University of Lund, 221 84 Lund, Sweden; vasili.hauryliuk@med.lu.se gemma.atkinson@med.lu.se.ORCID 0000-0003-2389-5057
Gemma C AtkinsonDepartment of Experimental Medicine, University of Lund, 221 84 Lund, Sweden; vasili.hauryliuk@med.lu.se gemma.atkinson@med.lu.se.ORCID 0000-0002-4861-4584
Lund University · SEUniversity of Tartu · EEUmeå University · SENewcastle University · GBCentre for Structural Systems Biology · DERigshospitalet · DKUniversité Côte d'Azur · FR

Funding

Biotechnology and Biological Sciences Research Council BB/S00257X/1Medical Research Council MR/N013840/1
6 · The paper itself

Abstract

Toxin-antitoxin (TA) gene pairs are ubiquitous in microbial chromosomal genomes and plasmids as well as temperate bacteriophages. They act as regulatory switches, with the toxin limiting the growth of bacteria and archaea by compromising diverse essential cellular targets and the antitoxin counteracting the toxic effect. To uncover previously uncharted TA diversity across microbes and bacteriophages, we analyzed the conservation of genomic neighborhoods using our computational tool FlaGs (for flanking genes), which allows high-throughput detection of TA-like operons. Focusing on the widespread but poorly experimentally characterized antitoxin domain DUF4065, our in silico analyses indicated that DUF4065-containing proteins serve as broadly distributed antitoxin components in putative TA-like operons with dozens of different toxic domains with multiple different folds. Given the versatility of DUF4065, we have named the domain

Indexed as

AntitoxinsBacterial ProteinsBacterial ToxinsBurkholderiaGene Expression Regulation, BacterialGuanosine PentaphosphateOperonProphagesProtein DomainsToxin-Antitoxin SystemsAntitoxinsBacterial ProteinsBacterial ToxinsGuanosine Pentaphosphateantitoxinbacteriophageevolutionpanaceatoxin

Identifiers

PMID35121656
PMCPMC8832971
OpenAlexW4210647992

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.