Disulphide bond-forming enzymes in clostridial species.

Claudia Antonika, Jocelyne Mendoza, Cristina Landeta

Abstract read

In one paragraph

Article in Microbiology (Reading, England), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

1 citing paper in PubMed.

Giant viruses encode vitamin K-based redox modules for lipid modification.Proceedings of the National Academy of Sciences of the United States of America · 2026
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.

Claudia AntonikaDepartment of Biology, Indiana University, Bloomington, USA.

Jocelyne MendozaDepartment of Biology, Indiana University, Bloomington, USA.

Cristina LandetaDepartment of Biology, Indiana University, Bloomington, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disulphide bond formation is critical for the folding and stability of proteins involved in bacterial cell envelope processes yet remains understudied in clostridial pathogens. While a few Clostridia-derived toxins and virulence factors are known to depend on disulphide bonds, the enzymes catalysing their formation are poorly characterized. Here, we performed a bioinformatic search to identify ten putative disulphide bond-forming enzymes in Clostridia. We cloned and codon-optimized these genes, testing their ability to complement

Indexed as

Bacterial ProteinsClostridiumDisulfidesProtein Disulfide-IsomerasesClostridioides difficileClostridium botulinumClostridium tetaniEscherichia coliEscherichia coli ProteinsMembrane ProteinsProtein FoldingBacterial ProteinsDisulfidesdsbA protein, E coliDsbB protein, BacteriaEscherichia coli ProteinsMembrane ProteinsProtein Disulfide-IsomerasesClostridioides difficileClostridium botulinumClostridium tetanicystinedisulphide bondDsbADsbBergothioneineglutathionelow molecular weight thiolVKOR

Identifiers

PMID40938763

DOI10.1099/mic.0.001603

PMCPMC12453122

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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.