ArticleJournal of enzyme inhibition and medicinal chemistry2018
Sulphonamide inhibition studies of the β-carbonic anhydrase from the bacterial pathogen Clostridium perfringens.
Article in Journal of enzyme inhibition and medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Selected gut bacteria promote mosquito larval growth through the regulation of ionic microenvironment and protease expression.iScience · 2025Article
- Carbonic Anhydrase Inhibitors as Novel Antibacterials in the Era of Antibiotic Resistance: Where Are We Now?Antibiotics (Basel, Switzerland) · 2023Review
- An anion and small molecule inhibition study of the β-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Anion inhibition studies of the α-carbonic anhydrases fromJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Microbiota, Bacterial Carbonic Anhydrases, and Modulators of Their Activity: Links to Human Diseases?Mediators of inflammation · 2021Review
- Coumarin carbonic anhydrase inhibitors from natural sources.Journal of enzyme inhibition and medicinal chemistry · 2020Review
- Activation studies with amines and amino acids of the β-carbonic anhydrase encoded by the Rv3273 gene from the pathogenic bacterium Mycobacterium tuberculosis.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Anion inhibition studies of a beta carbonic anhydrase from the malaria mosquito Anopheles gambiae.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- Activation studies of the α- and β-carbonic anhydrases from the pathogenic bacterium Vibrio cholerae with amines and amino acids.Journal of enzyme inhibition and medicinal chemistry · 2018Article
- An Overview of the Bacterial Carbonic Anhydrases.Metabolites · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The β-carbonic anhydrases (CAs, EC 4.2.1.1) from the pathogenic bacterium Clostridium perfringens (CpeCA) was recently characterised kinetically and for its anion inhibition profile. In the search of effective CpeCA inhibitors, possibly useful to inhibit the growth/pathogenicity of this bacterium, we report here an inhibition study of this enzyme with a panel of aromatic, heterocyclic and sugar sulphonamides/sulphamates. Some sulphonamides, such as acetazolamide, ethoxzolamide, dichlorophenamide, dorzolamide, sulthiame and 4-(2-hydroxymethyl-4-nitrophenyl-sulphonamido)ethylbenzenesulphonamide were effective CpeCA inhibitors, with K
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Registered trials
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.