A New Series of Amino Alcohol Oxime Ethers as Activators of Human Brain Carbonic Anhydrases: Advances in Selective Activation of Human Carbonic Anhydrase VII

= 72 nM) and selective over other brain isoforms. These results were further supported by in silico studies, which revealed favorable binding interactions at site A due to structural features present in both R and S enantiomers of compound 12.

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Publication Details

Journal
ChemMedChem
Published
2026-04-21
DOI
https://doi.org/10.1002/cmdc.70272
Primary Topic
Enzyme function and inhibition
Type
article
Field-Weighted Citation Impact
0.00

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article

A New Series of Amino Alcohol Oxime Ethers as Activators of Human Brain Carbonic Anhydrases: Advances in Selective Activation of Human Carbonic Anhydrase VII

Sabrina Taliani, Riccardo Di Leo, Alessio Nocentini, Claudiu T. Supuran et al.
ChemMedChem
Enzyme function and inhibition
article

A New Series of Amino Alcohol Oxime Ethers as Activators of Human Brain Carbonic Anhydrases: Advances in Selective Activation of Human Carbonic Anhydrase VII

Sabrina Taliani, Riccardo Di Leo, Alessio Nocentini, Claudiu T. Supuran, Paola Gratteri, Elisa Nuti, Doretta Cuffaro, Armando Rossello, Jacopo Castagnoli, Camilla Mangini
article en

Abstract

= 72 nM) and selective over other brain isoforms. These results were further supported by in silico studies, which revealed favorable binding interactions at site A due to structural features present in both R and S enantiomers of compound 12.

ChemMedChemVol. 21(8)
University of Pisa (IT), Istituto di Fisiologia Clinica (IT), National Research Council (IT), University of Florence (IT)
Università di Pisa
Openalex Percentile: Top 11%
Enzyme function and inhibition
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