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Phosphodiesterases in Health and Disease is a modern, comprehensive reference book on cyclic nucleotide phosophodiesterases (PDE) that will appeal to scientists in academia, the pharmaceutical industry, and related clinical disciplines. In the last 15 years, information relating to PDE genetics, physiological functions, roles in disease states, regulation, structure and interaction with pharmacologically active agents has burgeoned. This book covers the current information and its potential for future development. It describes the fundamental biochemical features of each of the known PDE…mehr

Produktbeschreibung
Phosphodiesterases in Health and Disease is a modern, comprehensive reference book on cyclic nucleotide phosophodiesterases (PDE) that will appeal to scientists in academia, the pharmaceutical industry, and related clinical disciplines. In the last 15 years, information relating to PDE genetics, physiological functions, roles in disease states, regulation, structure and interaction with pharmacologically active agents has burgeoned. This book covers the current information and its potential for future development. It describes the fundamental biochemical features of each of the known PDE families and the advances being made in developing selective inhibitors for these various enzymes.

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Autorenporträt
Joseph A. Beavo is a professor of pharmacology at the University of Washington. He obtained a BS from Stetson University in Deland, Florida and then a PhD from Vanderbilt University in Nashville, Tennessee. He has been involved in research concerning cyclic nucleotide phosphodiesterases since his graduate work with Drs. Joel Hardman and Earl Sutherland in the 1960s. He is an active member of the American Society for Pharmacology and Experimental Therapeutics and the National Academy of Sciences, having served on the editorial boards of journals published by both organizations. His current research focuses on the structural mechanisms of regulation of cyclic nucleotide phosphodiesterases and also on the functional roles played by the different phosphodiesterase gene products. Sharron H. Francis is a research professor of molecular physiology and biophysics at Vanderbilt University School of Medicine in Nashville, Tennessee. She obtained her undergraduate degree with emphasis in biology and chemistry from the Western Kentucky State in Bowling Green; studies for her doctoral degree in physiology were performed at Vanderbilt University under the guidance of Jane Park, PhD. She did postdoctoral study with Dr. Herman Eisen at Washington University in St. Louis, Missouri and was a research fellow in the Laboratory of Biochemistry at the National Heart and Lung Institute in Bethesda, Maryland under the guidance of Earl Stadtman, PhD. She is an active member of the American Society for Biochemistry and Molecular Biology, served the Scientific Advisory Board for Cell Pathways, Inc., and also has served as a consultant for numerous pharmaceutical companies. Her research interests focus on mechanisms involved in cGMP signaling, molecular characteristics of cGMP-dependent protein kinase, and phosphodiesterase-5, which are targets of cGMP, and the features that contribute to potent inhibition of phosphodiesterase- 5 by selective inhibitors. Miles D. Houslay is a Gardiner professor of biochemistry at the University of Glasgow, Scotland, UK. He obtained his first degree in biochemistry at the University of Wales in Cardiff and then his PhD from King's College, Cambridge. He has held faculty positions at the Universities of Cambridge and Manchester. He is a fellow of the Royal Society of Edinburgh, Colworth Medal Holder of the British Biochemical Society, has served as member= chair of numerous grant agencies, and has consulted widely in the pharmaceutical industry. He has been involved in cell signaling research since its inception. His current research interest is focused on the role of phosphodiesterase-4 isoforms in underpinning cAMP compartmentalization and cross-talk processes and potential for identifying novel therapeutic opportunities.