Internationally recognized investigators review the latest developments in, and novel approaches to, understanding the prion protein and prion diseases at the molecular level. Utilizing a variety of cutting-edge techniques, these distinguished scientists seek to define the normal function of a prion protein, to detect and measure the early immune response to prion disease, and to discover possible therapeutic targets. They also use transgenic mice and new electrophysiological investigations to elucidate the pathogenetic mechanisms involved in prion diseases. State-of-the-art and richly insightful, Molecular Pathology of the Prions captures for basic and clinical neuropathologists the latest developments and approaches to understanding the pathogenesis of prion diseases, and by analogy suggests possible research techniques for the more common proteinopthies, such as Alzheimer's and Parkinson's diseases.
Reihe
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Sprache
Verlagsort
Zielgruppe
Für höhere Schule und Studium
Für Beruf und Forschung
Professional/practitioner
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Maße
Höhe: 241 mm
Breite: 160 mm
Dicke: 23 mm
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ISBN-13
978-0-89603-924-7 (9780896039247)
DOI
Schweitzer Klassifikation
What Would Thomas Henry Huxley Have Made of Prion Diseases?.- Prion Protein as Copper-Binding Protein at the Synapse.- A Function for the Prion Protein?.- Prion Protein Peptide.- Characterization of Bovine Spongiform Encephalopathy and Scrapie Strains/Isolates by Immunochemical Analysis of PrPSc.- Differential Targeting of Neurons by Prion Strains.- Transgenic Studies of Prion Diseases.- Prions: From Neurografts to Neuroinvasion.- Cellular and Transgenic Models of Familial Prion Diseases.- Central Nervous System Inflammation and Prion Disease Pathogenesis.- The Electroneuropathology of Prion Disease.- Transmissible Spongiform Encephalopathy Neurobiology and Ultrastructure Suggests Extracellular PrPSc Conversion Consistent with Classical Amyloidosis.- Conformation as Therapeutic Target in the Prionoses and Other Neurodegenerative Conditions.- Prions of Yeast From Cytoplasmic Genes to Heritable Amyloidosis.
