Cell Biology of the Ubiquitin-Proteasome System. Volume 3. Protein Degradation

  • ID: 2179679
  • Book
  • 252 Pages
  • John Wiley and Sons Ltd
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Protein degradation is a major component in cellular metabolism, regulating numerous cell functions, such as the removal of misfolded proteins, growth and cell division, DNA repair, the immune response and the stress response to emergency conditions.

This third volume in the series discusses the role of ubiquitin–mediated protein breakdown in cellular regulation and physiology.

Drawing on the combined knowledge of the world′s leading protein degradation experts, this handy reference includes information on

∗ deubiquitylating enzymes

∗ tyrosine kinase receptors

∗ the COP9/signalosome complex

∗ regulation of the NFKB system

∗ ubiquitin in transcription, DNA monitoring and repair, and peroxisomes,

∗ endocytosis and membrane trafficking

∗ the ubiquitin–proteasome system in plants and muscle development.

Required reading for molecular biologists, cell biologists and physiologists with an interest in the topic.
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Ubiquitin: a new player in the peroxisome field

The ubiquitin–proteasome system and muscle development

The COP9 signalosome: structural and biochemical conservation and its roles in the regulation of plant development

Ubiquitin and protein sorting to the lysosome

ISG15–Dependent Regulation

The role of the ubiquitin proteasome pathway in the regulation of the cellular hypoxia response

p97 and ubiquitin: A complex story

Cdc48 (p97) and its co–factors

Deubiquitylating enzymes, cell proliferation, and cancer

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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.
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