Ubiquitin and the Chemistry of LifeR. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner John Wiley & Sons, 6 mars 2006 - 393 pages The first volume in a new series dedicated to protein degradation, this book lays the foundations of targeted protein breakdown via the ubiquitin pathway. The outstanding importance of the ubiquitin pathway has been recognized with the 2004 Nobel Prize in Chemistry for Aaaron Chiechanover, Avram Hershko, and Irwin Rose. Aaron Ciechanover is one of the editors of this series, and Avram Hershko has contributed to the opening chapter of the present volume. Drawing on the the expertise of two Nobel prize winners, this handy reference compiles information on the initial steps of the ubiquitin pathway. Starting out with a broad view of protein degradation and its functions in cellular regulation, it then goes on to examine the molecular mechanisms of ubiquitin conjugation and recycling in detail. All currently known classes of ubiquitin protein ligases are treated here, including latest structural data on these enzymes. Further volumes in the series cover the function of the proteasome, 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. |
Table des matières
| 1 | |
2 Nterminal Ubiquitination No Longer Such a Rare Modification | 10 |
3 Evolutionary Origin of the Activation Step During Ubiquitindependent Protein Degradation | 21 |
4 RING Fingers and Relatives Determinators of Protein Fate | 44 |
5 Ubiquitinconjugating Enzymes | 102 |
6 The SCF Ubiquitin E3 Ligase | 135 |
7 The Structural Biology of UbiquitinProtein Ligases | 156 |
8 The Deubiquitinating Enzymes | 190 |
9 The 26S Proteasome | 220 |
10 Molecular Machines for Protein Degradation | 248 |
11 Proteasome Regulator PA700 19S Regulatory Particle | 288 |
12 Bioinformatics of Ubiquitin Domains and Their Binding Partners | 318 |
13 The COP9 Signalosome Its Possible Role in the Ubiquitin System | 348 |
| 370 | |
Autres éditions - Tout afficher
Protein Degradation: Ubiquitin and the Chemistry of Life R. John Mayer,Aaron J. Ciechanover,Martin Rechsteiner Aucun aperçu disponible - 2006 |
Ubiquitin and the Chemistry of Life R. John Mayer,Aaron J. Ciechanover,Martin Rechsteiner Aucun aperçu disponible - 2006 |
Expressions et termes fréquents
26S proteasome Acad Sci USA active-site cysteine amino acids ATP-dependent ATPase b-catenin binding Biochem Biol Chem Brca1 c-Cbl catalytic Cdc4 cellular components conjugation conserved COP9 signalosome crystal structure Cul1 cullin cyclin cysteine deubiquitinating enzyme DNA repair Drosophila DUBs E2 enzyme E3 activity E3 ligase E6AP Embo eukaryotic F-box proteins factor function gene HECT domain homolog HslU HslV human inhibition inhibitor interaction kinase loop lysine lysine residue mammalian Mdm2 MdmX mechanism mediated MoaD modification MoeB Mol Cell Biol molecular mono-ubiquitin motif mutations MyoD N-terminal Natl Acad Sci NEDD8 NF-kB ofthe Parkin pathway peptide phosphorylation Pickart polyubiquitin chains Proc Natl Acad protease protein degradation proteolysis proteolytic Rbx1 receptor regulation regulatory RING domain RING finger role SCF complex sequence signal Skp1 Skp2 specific substrate subunits target teins tion transcription tumor UBA domains UbcH7 ubiquitin ligase ubiquitin system ubiquitin-dependent ubiquitin-like protein ubiquitylation uitin vitro yeast