By R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner
This ultimate quantity within the sequence makes a speciality of malfunctions of the ubiquitin-proteasome method and their function in human affliction.
The editors and authors characterize unrivaled services, comprising nearly all of the best scientists within the box, together with the pioneers of protein degradation research.
From the contents:
* Ubiquitin and melanoma
* Ubiquitin and liver cancer
* Muscle atrophy
* Aggresomes and human disease
* Parkin and neurodegeneration
* power neurodegenerative diseases
* Parkinson's disease
* Ubiquitin and viruses
* Druggability of the ubiquitin-proteasome system
Required studying for molecular and telephone biologists, in addition to physiologists with an curiosity within the subject.
Read or Download Protein Degradation: The Ubiquitin-Proteasome System and Disease PDF
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Additional info for Protein Degradation: The Ubiquitin-Proteasome System and Disease
D. R. F. Stancato, P. B. Pratt, Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90based chaperone machinery. hsp70, J. Biol. Chem. 272 (1997) 21213–21220. S. Chen, V. A. Rimerman, B. F. Smith, Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70. Mol. Endocrinol. 10 (1996) 682–693. H. Kosano, B. C. Charlesworth, N. McMahon, D. Toft, The assembly of progesterone receptor-hsp90 complexes using puriﬁed proteins, J. Biol.
K. Y. Q. M. M. Bonini, Chaperone suppression of asynuclein toxicity in a Drosophila model for Parkinson’s disease, Science 295 (2002) 865–868. U. Hartl, M. Hayer-Hartl, 26 27 28 29 30 31 32 33 34 35 Molecular chaperones in the cytosol: from nascent chain to folded protein, Science 295 (2002) 1852–1858. J. Frydman, Folding of newly translated proteins in vivo: the role of molecular chaperones, Annu. Rev. Biochem. 70 (2001) 603–647. J. Frydman, J. Ho¨hfeld, Chaperones get in touch: the Hip-Hop connection, Trends Biochem.
C. Reed, p53inducible homologue of Drosophila seven in absentia (Siah) inhibits cell growth: suppression by BAG-1, EMBO J. 17 (1998) 2736–2747. 164 C. Soti, P. Csermely, Aging and 165 166 167 168 169 170 171 molecular chaperones, Exp. Gerontol. 38 (2003) 1037–1040. J. Fargnoli, T. J. Jr. L. J. Holbrook, Decreased expression of heat shock protein 70 mRNA and protein after heat tretament in cells of aged rats, Proc. Natl. Acad. Sci. USA 87 (1990) 846–850. K. G. Klopp, R. A. Prolla, Gene expression proﬁle of aging and its retardation by caloric restriction, Science 285 (1999) 1390– 1393.