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Protein Degradation Series, 4 Volume Set

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Description
This series of four topical volumes includes more than 50 contributions covering all aspects of the molecular biology and physiology of controlled protein breakdown in higher organisms via the ubiquitin-proteasome pathway. The editors and authors comprise virtually all the top scientists in the field, including the pioneers of protein degradation research and the 2004 Nobel laureate in chemistry.
Each volume highlights a different aspect of the field, namely ubiquitin and the chemistry of life, as well as the cell biology and pathology of the ubiquitin-proteasome system, with the individual volumes featuring their own separate indices. Together, all four volumes provide the most comprehensive reference on protein degradation available.
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.