title: Carbonic anhydrase inhibitors: X-ray crystallographic studies for the binding of N-substituted benzenesulfonamides to human isoform II.
abstract: N-substituted benzenesulfonamides, incorporating the N-amino-, N-hydroxy- and N-methoxy-moieties at the sulfonamide zinc binding group, have been investigated as CAIs by means of inhibition and structural studies, unraveling interesting aspects related to their inhibition mechanism.
authors.affiliation: Istituto di Biostrutture e Bioimmagini-CNR, via Mezzocannone 16, 80134 Napoli, Italy.
authors.forename: Anna
authors.initials: A
authors.lastname: Di Fiore
authors.forename: Alfonso
authors.initials: A
authors.lastname: Maresca
authors.forename: Vincenzo
authors.initials: V
authors.lastname: Alterio
authors.forename: Claudiu T
authors.initials: CT
authors.lastname: Supuran
authors.forename: Giuseppina
authors.initials: G
authors.lastname: De Simone
mesh_terms: D024402:Carbonic Anhydrase II / Q000378:metabolism*; D002257:Carbonic Anhydrase Inhibitors / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D011485:Protein Binding; D013449:Sulfonamides / Q000737:chemistry / Q000378:metabolism*
chemical_list: D002257:Carbonic Anhydrase Inhibitors; D013449:Sulfonamides; D024402:Carbonic Anhydrase II