The Ubiquitin-Proteasome System and Disease. Volume 4. Protein Degradation

  • ID: 2179680
  • Book
  • 258 Pages
  • John Wiley and Sons Ltd
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Protein degradation, the controlled break–up of cellular proteins by intracellular proteolysis, is a major component in cellular metabolism and regulates numerous cell functions, including removal of misfolded proteins, growth and cell division, DNA repair, the immune response and the stress response to emergency conditions.

This final volume in the series focuses on malfunctions of the ubiquitin–proteasome system and their role in human disease. As such, it is the most comprehensive resource on this key topic in molecular cell biology, incorporating the unmatched expertise of the 2004 Chemistry Nobel laureates. The editors and authors comprise virtually all the top scientists in the field, including the pioneers of protein degradation research.

From the contents:

∗ Ubiquitin and cancer

∗ Ubiquitin and liver cancer

∗ Muscle atrophy

∗ Aggresomes and human disease

∗ Parkin and neurodegeneration

∗ Chronic neurodegenerative diseases

∗ Parkinson′s disease

∗ Ubiquitin and viruses

∗ Druggability of the ubiquitin–proteasome system

Required reading for molecular and cell biologists, as well as physiologists with an interest in the topic.
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Ubiquitin signaling and cancer pathogenesis

Regulation of the p53 tumor–suppressor protein by ubiquitin and ubiquitin–like molecules

The ubiquitin–proteasome system in Epstein–Barr virus infection and oncogenesis

HECT ubiquitin–protein ligases in human disease

Ubiquitin–independent mechanisms of substrate recognition and degradation by the proteasome

Endoplasmic reticulum protein quality control and degradation

Interactions between viruses and the ubiquitin–proteasome system

The ubiquitin–proteasome system in Parkinson′s disease

The molecular pathway to neurodegeneration in parkin–related Parkinsonism

Parkin and neurodegeneration
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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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