The first volume in a new series dedicated to protein degradation, this book explains the fundamentals of targeted protein breakdown via the ubiquitin pathway. Drawing on the combined knowledge of the world's leading protein degradation experts, this handy reference compiles information on the initial steps of the ubiquitin pathway. Starting out with a broad overview of protein degradation and its functions in cellular regulation, it then goes on to discuss the molecular mechanisms of ubiquitin conjugation and recycling in detail. All currently known classes of ubiquitin protein ligases are treated; this includes latest structural data on these enzymes. Further volumes in the series cover the function of the proteasome, the roles of the ubiquitin pathway in regulating key cellular processes, and its pathophysiological disease states. Required reading for molecular biologists, cell biologists and physiologists with an interest in protein degradation.
About the Author
John Mayer obtained his MS and PhD degrees from the University of Birmingham (UK). He is currently serving as Professor of Biochemistry at the School of Biomedical Sciences at Nottingham University. For the past 30 years, he has investigated intracellular proteolysis and particularly the ubiquitin/proteasome system. Presently, he is particularly interested in intracellular proteolysis in relation to neurodegenerative illnesses.
Aaron Ciechanover obtained his MD from the Hebrew University in Jerusalem (Israel), and his PhD from the Technion-Israel Institute of Technology in Haifa, where he is presently serving as Professor of Biochemistry. Professor Ciechanover is known for his discovery of the first ubiquitin system mutant cell, demonstrating the role of the ubiquitin-proteasome proteolytic system in protein degradation in vivo. In 2004, he has received the Nobel Prize in Chemistry for his ground-breaking work on the ubiquitin-proteasome system.
Martin Rechsteiner is Professor of Biochemistry at the University of Utah in Salt Lake City (USA). He is interested in the proteasome component of the ubiquitin-proteasome pathway. He has identified several key regulators of proteasome function and is currently working on their structural and functional elucidation.
