Purinergic Receptors and their Modulators / Topics in Medicinal Chemistry Bd.41 (PDF)

Vittoria Colotta is an Associate Professor of Medicinal Chemistry at Dipartimento Neurofarba, Universita` degli Studi di Firenze, Sezione di Scienze Farmaceutiche e Nutraceutiche, Italy. She completed her degree in Pharmaceutical Chemistry and Technology in 1985 and her PhD in Medicinal Chemistry in 1988, both at University of Florence. Her past research interest was the synthesis of new biologically active compounds designed as ligands of benzodiazepine and glutamate receptors. Current research is mainly focused on the development of adenosine receptors' ligands and inhibitors of the enzymes 5'-ectonucleotidase (CD73), carbonic anhydrases and casein kinases 1 and 2. The aim of the work is the identification of selective or multitarget-directed ligands as potential therapeutic agents for cancer and neurodegenerative diseases. She is co-author of more than 110 peer-reviewed articles and co-inventor of 2 Patents. She is an Editor of the journal Pharmaceuticals and a Review Editor of Frontiers in Pharmacology (Experimental Pharmacology and Drug Discovery section). She is an active reviewer for high-impact medicinal chemistry journals.


Claudiu T. Supuran is a Full Professor of Medicinal Chemistry at Dipartimento Neurofarba, Universita` degli Studi di Firenze, Sezione di Scienze Farmaceutiche e Nutraceutiche, Florence, Italy. He received his BSc in Chemistry from the Polytechnic University of Bucharest, Romania (1987), and Ph. D. in Chemistry at the same university in 1991. His research interests focus on drug development against Carbonic anhydrases and other enzymes. He has published 2000+ research articles on enzyme inhibitors/activators, being one of the most cited medicinal chemists worldwide. His research is also focused on metalloenzymes cloning, characterization and inhiibtion studies, carbonic anhydrases, proteases, heterocyclic chemistry, chemistry of sulfonamides, sulfamates and sulfamides, X-ray crystallography of metallo-enzymes, biologically