ArticleJournal of enzyme inhibition and medicinal chemistry2018
Investigation of piperazines as human carbonic anhydrase I, II, IV and VII activators.
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 4 papers.
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4 citing papers in PubMed.
- Effect of amino acids and amines on the activity of the recombinant ι-carbonic anhydrase from the Gram-negative bacteriumJournal of enzyme inhibition and medicinal chemistry · 2021Article
- Carbonic anhydrase activation profile of indole-based derivatives.Journal of enzyme inhibition and medicinal chemistry · 2021Article
- Synthesis and Biological Evaluation of Imidazo[2 ,1-Metabolites · 2020Article
- Activation of human α-carbonic anhydrase isoforms I, II, IV and VII with bis-histamine schiff bases and bis-spinaceamine substituted derivatives.Journal of enzyme inhibition and medicinal chemistry · 2019Article
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5 authors.
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Abstract
Four human (h) carbonic anhydrase isoforms (CA, EC 4.2.1.1), hCA I, II, IV, and VII, were investigated for their activation profile with piperazines belonging to various classes, such as N-aryl-, N-alkyl-, N-acyl-piperazines as well as 2,4-disubstituted derivatives. As the activation mechanism involves participation of the activator in the proton shuttling between the zinc-coordinated water molecule and the external milieu, these derivatives possessing diverse basicity and different scaffolds were appropriate for being investigated as CA activators (CAAs). Most of these derivatives showed CA activating properties against hCA I, II, and VII (cytosolic isoforms) but were devoid of activity against the membrane-associated hCA IV. For hCA I, the K
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