ArticleJournal of enzyme inhibition and medicinal chemistry2020
Novel sulphonamides incorporating triazene moieties show powerful carbonic anhydrase I and II inhibitory properties.
Article in Journal of enzyme inhibition and medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Chromones as Nonclassical Inhibitors of Carbonic Anhydrase IX and XII Isoforms: Probing Chromone-Based Derivatives.Archiv der Pharmazie · 2026Article
- Privileged Scaffold Hybridization in the Design of Carbonic Anhydrase Inhibitors.Molecules (Basel, Switzerland) · 2024Article
- 1,3-Diaryl Triazenes Incorporating Disulfonamides Show Both Antiproliferative Activity and Effective Inhibition of Tumor-associated Carbonic Anhydrases IX and XII.Anti-cancer agents in medicinal chemistry · 2024Article
- 2H-chromene and 7H-furo-chromene derivatives selectively inhibit tumour associated human carbonic anhydrase IX and XII isoforms.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Selective inhibition of carbonic anhydrase IX and XII by coumarin and psoralen derivatives.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Novel Mannich bases with strong carbonic anhydrases and acetylcholinesterase inhibition effects: 3-(aminomethyl)-6-{3-[4-(trifluoromethyl)phenyl]acryloyl}-2(3H)-benzoxazolones.Turkish journal of chemistry · 2021Article
- Bioorganometallic derivatives of 4-hydrazino-benzenesulphonamide as carbonic anhydrase inhibitors: synthesis, characterisation and biological evaluation.Journal of enzyme inhibition and medicinal chemistry · 2020Article
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
A series of compounds incorporating 3-(3-(2/3/4-substituted phenyl)triaz-1-en-1-yl) benzenesulfonamide moieties were synthesised and their chemical structure was confirmed by physico-chemical methods. Carbonic anhydrase (CA, EC 4.2.1.1) inhibitory effects of the compounds were evaluated against human isoforms hCA I and II. K
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