{"product_id":"drug-design-of-zinc-enzyme-inhibitors-isbn-9780470275009","title":"Drug Design of Zinc-Enzyme Inhibitors","description":"\u003cb\u003eBrings together functional and structural informationrelevant to the design of drugs targeting zinc enzymes\u003c\/b\u003e  \u003cp\u003eThe second most abundant transition element in living organisms, zinc spans all areas of metabolism, with zinc-containing proteins offering both established and potential drug targets. \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e brings together functional and structural information relevant to these zinc-containing targets. With up-to-date overviews of the latest developments field, this unique and comprehensive text enables readers to understand zinc enzymes and evaluate them in a drug design context.\u003c\/p\u003e \u003cp\u003eWith contributions from the leaders of today's research, \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e covers such key topics as:\u003c\/p\u003e \u003cul\u003e \u003cli\u003e \u003cp\u003eMajor drug targets like carbonic anhydrases, matrix metalloproteinases, bacterial proteases, angiotensin-converting enzyme, histone deacetylase, and APOBEC3G\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eRoles of recently discovered zinc-containing isozymes in cancer, obesity, epilepsy, pain management, malaria, and other conditions\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eCross reactivity of zinc-enzyme inhibitors and activators\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eThe extensive use of X-ray crystallography and QSAR studies for understanding zinc-containing proteins\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eClinical applications\u003c\/p\u003e \u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eAn essential resource for the discovery and development of new drug molecules, \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e gives researchers, professionals, students, and academics the foundation to understand and work with zinc enzyme inhibitors and activators.\u003c\/p\u003e  PREFACE.  \u003cp\u003eCONTRIBUTORS.\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART I: INTRODUCTION.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e1. Introduction to Zinc Enzymes as Drug Targets (\u003ci\u003eClaudiu T. Supuran and Jean-Yves Winum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART II: DRUG DESIGN OF CARBONIC ANHYDRASE INHIBITORS AND ACTIVATORS.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e2. Carbonic Anhydrases as Drug Targets: General Presentation (\u003ci\u003eClaudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e3. Zinc Binding Functions in the Design of Carbonic Anhydrase Inhibitors (\u003ci\u003eJean-Yves Winum, Jean-Louis Montero, Andrea Scozzafava, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e4. X-Ray Crystallography of Carbonic Anhydrase Inhibitors and Its Importance in Drug Design (\u003ci\u003eVincenzo Alterio, Anna Di Fiore, Katia D’Ambrosio, Claudiu T. Supuran, and Giuseppina De Simone\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e5. Antiglaucoma Carbonic Anhydrase Inhibitors as Ophthalomologic Drugs (\u003ci\u003eFrancesco Mincione, Andrea Scozzafava, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e6. Diuretics with Carbonic Anhydrase Inhibitory Activity: Toward Novel Applications for Sulfonamide Drugs (\u003ci\u003eDaniela Vullo, Alessio Innocenti, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e7. Drug Design of Carbonic Anhydrase Inhibitors as Anticonvulsant Agents (\u003ci\u003eAnne Thiry, Jean-Michel Dogn\u003c\/i\u003e\u003ci\u003ee, Claudiu T. Supuran, and Bernard Masereel\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e8. Carbonic Anhydrase Inhibitors Targeting Cancer: Therapeutic, Immunologic, and Diagnostic Tools Targeting Isoforms IX and XII (\u003ci\u003eSilvia Pastorekova, Monika Barathova, Juraj Kopacek, and Jaromir Pastorek\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e9. Fluorescent- and Spin-Labeled Sulfonamides as Probe for Carbonic Anhydrase IX (\u003ci\u003eAlessandro Cecchi, Laura Ciani, Sandra Ristori, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e10. Drug Design of Antiobesity Carbonic Anhydrase Inhibitors (\u003ci\u003eGiuseppina De Simone and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e11. Dual Carbonic Anhydrase and Cyclooxygenase-2 Inhibition (\u003ci\u003eJean-Michel Dogn\u003c\/i\u003e\u003ci\u003ee, Anne Thiry, Bernard Masereel, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e12. Advances in the Inhibitory and Structural Investigations on Carbonic Anhydrase Isozymes XIII and XV (\u003ci\u003eMika Hilvo, Giuseppina De Simone, Claudiu T. Supuran, and Seppo Parkkila\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e13. Mechanism and Inhibition of the b-Class and c-Class Carbonic Anhydrases (James \u003ci\u003eG. Ferry and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e14. Fungal and Nematode Carbonic Anhydrases: Their Inhibition in Drug Design (\u003ci\u003eRebecca A. Hall and Fritz. A. M€\u003c\/i\u003e\u003ci\u003euhlschlegel\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e15. Crystallographic Studies on Carbonic Anhydrases from Fungal Pathogens for Structure-Assisted Drug Development (\u003ci\u003eUta-Maria Ohndorf, Christine Schlicker, and Clemens Steegborn\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e16. Malaria Parasite Carbonic Anhydrase and Its Inhibition in the Development of Novel Therapies of Malaria (\u003ci\u003eJerapan Krungkrai, Sudaratana R. Krungkrai, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e17. Inhibitors of Helicobacter pylori a- and b-Carbonic Anhydrases as Novel Drugs for Gastroduodenal Diseases (\u003ci\u003eIsao Nishimori, Hiroaki Takeuchi, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e18. QSAR of Carbonic Anhydrase Inhibitors and Their Impact on Drug Design (\u003ci\u003eAdriano Martinelli and Tiziano Tuccinardi\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e19. Selectivity Issues in the Design of CA Inhibitors (\u003ci\u003eClaudiu T. Supuran and Jean-Yves Winum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e20. Bicarbonate Transport Metabolons (\u003ci\u003eDanielle E. Johnson and Joseph R. Casey\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e21. Metal Complexes of Sulfonamides as Dual Carbonic Anhydrase Inhibitors (\u003ci\u003eMarc A. Ilies\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e22. Drug Design Studies of Carbonic Anhydrase Activators (\u003ci\u003eClaudia Temperini, Andrea Scozzafava, and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART III DRUG DESIGN OF MATRIX METALLOPROTEINASE INHIBITORS.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e23. Matrix Metalloproteinases: An Overview (\u003ci\u003eHideaki Nagase and Robert Visse\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e24. MMP Inhibitors Based on Earlier Succinimide Strategies: From Early to New Approaches (\u003ci\u003eM. Amelia Santos\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e25. Drug Design of Sulfonylated MMP Inhibitors (\u003ci\u003eArmando Rossello and Elisa Nuti\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e26. ADAMs and ADAMTs Selective Synthetic Inhibitors (\u003ci\u003eArmando Rossello, Elisa Nuti, and Alfonso Maresca\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e27. QSAR Studies of MMP Inhibitors (\u003ci\u003eTiziano Tuccinardi and Adriano Martinelli\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART IV DRUG DESIGN OF BACTERIAL ZINC PROTEASE INHIBITORS.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e28. Bacterial Zinc Proteases as Orphan Targets (\u003ci\u003eClaudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e29. Botulinus Toxin, Tetanus Toxin, and Anthrax Lethal Factor Inhibitors (\u003ci\u003eAntonio Mastrolorenzo and Claudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e30. Clostridium histolyticum Collagenase Inhibitors in the Drug Design (\u003ci\u003eClaudiu T. Supuran\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e31. Other Bacterial Zinc Peptidases as Potential Drug Targets (\u003ci\u003eKunihiko Watanabe\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePART V DRUG DESIGN STUDIES OF OTHER ZINC-CONTAINING ENZYMES.\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e32. Angiotensin Converting Enzyme (ACE) Inhibitors (\u003ci\u003eAna Camara-Artigas, Vicente Jara-Perez, and Montserrat Andujar-S\u003c\/i\u003e\u003ci\u003eanchez\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e33. P-III Metalloproteinase (Leucurolysin-B) from Bothrops leucurus Venom: Isolation and Possible Inhibition (\u003ci\u003eEladio F. Sanchez and Johannes A. Eble\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e34. CaaX-Protein Prenyltransferase Inhibitors (\u003ci\u003eMartin Schlitzer, Regina Ortmann, and Mirko Altenk\u003c\/i\u003e\u003ci\u003eamper\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e35. Histone Deacetylase Inhibitors (\u003ci\u003ePaul W. Finn\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e36. Recent Development of Diagnostic and Therapeutic Agents Targeting Glutamate Carboxypeptidase II (GCPII) (\u003ci\u003eYoungjoo Byun, Ronnie C. Mease, Shawn E. Lupold, and Martin G. Pomper\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e37. Targeting HIV-1 Integrase Zinc Binding Motif (\u003ci\u003eMario Sechi, Mauro Carcelli, Dominga Rogolino, and Nouri Neamati\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e38. Inhibitors of Histidinol Dehydrogenases as Antibacterial Agents (\u003ci\u003ePascale Joseph, Franc¸ois Turtaut, Stephan K€\u003c\/i\u003e\u003ci\u003eohler, and Jean-Yves Winum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e39. Dihydroorotase Inhibitors (\u003ci\u003eMihwa Lee, Megan J. Maher, Richard I. Christopherson, and J. Mitchell Guss\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e40. APOBEC3G: A Promising Antiviral Target (\u003ci\u003eClaudiu T. Supuran and Jean-Yves Winum\u003c\/i\u003e).\u003c\/p\u003e \u003cp\u003e\u003cb\u003eIndex.\u003c\/b\u003e\u003c\/p\u003e  \u003cb\u003eClaudiu T. Supuran\u003c\/b\u003e is a professor in the Department of Chemistry at the University of Florence, Italy. His main research interests include medicinal chemistry, design of enzyme inhibitors and activators, X-ray crystallography of metallo-enzymes, and metal complexes with biologically active ligands (metal-based drugs). He has published more than 400 original research papers in these fields.  \u003cp\u003e\u003cb\u003eJean-Yves Winum\u003c\/b\u003e is an assistant professor in the Department of Chemistry at the University of Montpellier 2 (Institut des Biomolécules Max Mousseron UMR CNRS 5247), France. His research interests are focused on organic\/medicinal chemistry of metallo-enzyme inhibitors and activators.\u003c\/p\u003e  \u003cb\u003eBrings together functional and structural informationrelevant to the design of drugs targeting zinc enzymes\u003c\/b\u003e  \u003cp\u003eThe second most abundant transition element in living organisms, zinc spans all areas of metabolism, with zinc-containing proteins offering both established and potential drug targets. \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e brings together functional and structural information relevant to these zinc-containing targets. With up-to-date overviews of the latest developments field, this unique and comprehensive text enables readers to understand zinc enzymes and evaluate them in a drug design context.\u003c\/p\u003e \u003cp\u003eWith contributions from the leaders of today's research, \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e covers such key topics as:\u003c\/p\u003e \u003cul\u003e \u003cli\u003e \u003cp\u003eMajor drug targets like carbonic anhydrases, matrix metalloproteinases, bacterial proteases, angiotensin-converting enzyme, histone deacetylase, and APOBEC3G\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eRoles of recently discovered zinc-containing isozymes in cancer, obesity, epilepsy, pain management, malaria, and other conditions\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eCross reactivity of zinc-enzyme inhibitors and activators\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eThe extensive use of X-ray crystallography and QSAR studies for understanding zinc-containing proteins\u003c\/p\u003e \u003c\/li\u003e \u003cli\u003e \u003cp\u003eClinical applications\u003c\/p\u003e \u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eAn essential resource for the discovery and development of new drug molecules, \u003ci\u003eDrug Design of Zinc-Enzyme Inhibitors\u003c\/i\u003e gives researchers, professionals, students, and academics the foundation to understand and work with zinc enzyme inhibitors and activators.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989087437029,"sku":"NP9780470275009","price":277.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9780470275009.jpg?v=1761782743","url":"https:\/\/k12savings.com\/products\/drug-design-of-zinc-enzyme-inhibitors-isbn-9780470275009","provider":"K12savings","version":"1.0","type":"link"}