Protein Degradation
Vol. 2: The Ubiquitin-Proteasome System
Protein Degradation (Band Nr. 2)
1. Auflage Dezember 2005
XIV, 286 Seiten, Hardcover
78 Abbildungen (25 Farbabbildungen)
5 Tabellen
Handbuch/Nachschlagewerk
Kurzbeschreibung
The second volume in a new series, this book discusses the mechanism and cellular functions of targeted protein breakdown via the ubiquitin pathway. Required reading for molecular biologists, cell biologists and physiologists with an interest in protein degradation.
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The second volume in a new series dedicated to protein degradation, this book discusses the mechanism and cellular functions 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 proteasome-mediated degradation steps of the ubiquitin pathway. In addition to proteasomal function and regulation, it also presents the latest results on novel members of the ubiquitin superfamily and their role in cellular regulation.
Further volumes in the series cover the function of ubiquitin-protein ligases, and the roles of the ubiquitin pathway in regulating key cellular processes, as well as its pathophysiological disease states.
Required reading for molecular biologists, cell biologists and physiologists with an interest in protein degradation.
The proteasome portal and regulation of proteolysis
PAN and the proteasome
Ubiquitin domain proteins
MEKK1: dual function as a protein kinase and a ubiquitin protein ligase
HECT domain ubiquitin protein ligases
UCRP: ubiquitin cross-reactive protein
SUMOs and their function in the cell
Functions of the ubiquitin-proteasome pathway
Molecular Chaperones and the ubiquitin/proteasome system
Dissecting intracellular proteolysis using small molecule inhibitors and molecular probes
Electron microscopy of compartmentalised proteases
Molecular dissection of autophagy in yeast
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Nachrichten aus der Chemie
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.
