Prions and Diseases
Volume 1, Physiology and Pathophysiology
Gebonden Engels 2012 2013e druk 9781461453048Samenvatting
Volume I highlights the association of the cellular prion protein (PrPC) with copper and zinc, the potential roles of PrPC in Alzheimer’s disease and cancers, insoluble PrPC, PMCA, molecular and cellular mechanisms of PrPSc formation and clearance, possible co-factors involved in the conversion of PrPC into PrPSc, infectious and pathogenic forms of PrP, cell biology of prions, prion strains and their interference, as well as yeast prions and their inheritable and structural traits. This unique volume will take you through the fascinating chronicle of prions in mammals, yeast, and fungi.
Specificaties
Lezersrecensies
Inhoudsopgave
Paul Brown
Chapter 2 The Rich Chemistry of the Copper and Zinc Sites in Cellular Prion Protein
Glenn L. Millhauser
Chapter 3 Role of Cellular Prion Protein in the Amyloid-ß Oligomer Pathophysiology of Alzheimer’s Disease
Adam C. Kaufman, Stephen M. Strittmatter
Chapter 4 Cellular Prion Protein and Cancers
Wei Xin, Man-sun Sy, Chaoyang Li
Chapter 5 Insoluble Cellular Prion Protein
Wen-Quan Zou
Chapter 6 Protein Misfolding Cyclic Amplification
Fabio Moda, Sandra Pritzkow, Claudio Soto
Chapter 7 Cofactor Involvement in Prion Propagation
Surachai Supattapone, Michael B. Miller
Chapter 8 Prion Protein Conversion and Lipids
Jiyan Ma
Chapter 9 New Perspectives on Prion Conversion: Introducing a Mechanism of Deformed Templating
Ilia V. Baskakov
Chapter 10 Infectious and Pathogenic Forms of Prion Protein
Emiliano Biasini, David A. Harris
Chapter 11 Cellular Mechanisms of Propagation and Clearance
Hermann M. Schatzl
Chapter 12 Molecular Mechanisms Encoding Quantitative and Qualitative Traits of Prion Strains
Jiri G. Safar
Chapter 13 Modeling the Cell Biology of Prions
Richard Rubenstein, Robert B. Petersen
Chapter 14 Prion Strain Interference
Charles R. Schutt, Ronald A. Shikiya, Jason C. Bartz
Chapter 15 Introduction to Yeast and Fungal Prions
Reed B. Wickner
Chapter 16 Yeast Prions are Pathogenic, in-register Parallel Amyloids
Reed B. Wickner, Herman K. Edskes, David A. Bateman, Amy C. Kelly, Anton Gorkovskiy
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