A
Arthur H. Robbins
Researcher at University of Florida
Publications - 23
Citations - 900
Arthur H. Robbins is an academic researcher from University of Florida. The author has contributed to research in topics: Carbonic anhydrase & Carbonic anhydrase II. The author has an hindex of 15, co-authored 23 publications receiving 841 citations. Previous affiliations of Arthur H. Robbins include Cornell University & University of Florence.
Papers
More filters
Journal ArticleDOI
Selective hydrophobic pocket binding observed within the carbonic anhydrase II active site accommodate different 4-substituted-ureido-benzenesulfonamides and correlate to inhibitor potency.
Fabio Pacchiano,Mayank Aggarwal,Balendu Sankara Avvaru,Arthur H. Robbins,Andrea Scozzafava,Robert McKenna,Claudiu T. Supuran +6 more
TL;DR: 4-Substituted-ureido benzenesulfonamides showing inhibitory activity against carbonic anhydrase II between 3.3-226 nM were crystallized in complex with the enzyme, explaining the diverse inhibitory range of these derivatives.
Journal ArticleDOI
Sulfonamides incorporating 1,3,5-triazine moieties selectively and potently inhibit carbonic anhydrase transmembrane isoforms IX, XII and XIV over cytosolic isoforms I and II: Solution and X-ray crystallographic studies.
Fabrizio Carta,Vladimír Garaj,Vladimír Garaj,Alfonso Maresca,Jason Wagner,Balendu Sankara Avvaru,Arthur H. Robbins,Andrea Scozzafava,Robert McKenna,Claudiu T. Supuran +9 more
TL;DR: The 1,3,5-triazinyl-substituted benzenesulfonamides constitute thus a class of compounds with great potential for obtaining inhibitors targeting both α-class mammalian, tumor-associated, and β-class from pathogenic organisms CAs.
Journal ArticleDOI
High-resolution structure of human carbonic anhydrase II complexed with acetazolamide reveals insights into inhibitor drug design.
Katherine H. Sippel,Arthur H. Robbins,John F. Domsic,Caroli Genis,Mavis Agbandje-McKenna,Robert McKenna +5 more
TL;DR: The co-binding of AZM and glycerol in the active site demonstrate that given an appropriate ring orientation and substituents, an isozyme-specific CA inhibitor may be developed.
Journal ArticleDOI
Carbonic anhydrase inhibitors. The X-ray crystal structure of human isoform II in adduct with an adamantyl analogue of acetazolamide resides in a less utilized binding pocket than most hydrophobic inhibitors.
Balendu Sankara Avvaru,Jason Wagner,Alfonso Maresca,Andrea Scozzafava,Arthur H. Robbins,Claudiu T. Supuran,Robert McKenna +6 more
TL;DR: The high resolution X-ray crystal structure of hCA II in complex with 5-(1-adamantylcarboxamido)-1,3,4-thiadiazole-2-sulfonamide scaffold showed the adamantyl moiety of the inhibitor residing in a less utilized binding pocket than that of most hydrophobic inhibitors, lined by the amino acid residues Ile91, Val121 and Phe131.
Journal ArticleDOI
Anticonvulsant 4-aminobenzenesulfonamide derivatives with branched-alkylamide moieties: X-ray crystallography and inhibition studies of human carbonic anhydrase isoforms I, II, VII, and XIV.
Naama Hen,Meir Bialer,Boris Yagen,Alfonso Maresca,Mayank Aggarwal,Arthur H. Robbins,Robert McKenna,Andrea Scozzafava,Claudiu T. Supuran +8 more
TL;DR: Aromatic amides comprising branched aliphatic carboxylic acids and 4-aminobenzenesulfonamide andStructural studies suggest that differences in the active sites' hydrophobicity modulate the affinity of the inhibitors.