Molecular Pathology of the PrionsHarry F. Baker Springer Science & Business Media, 2 feb 2008 - 279 páginas 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. |
Índice
Prion Protein as CopperBinding Protein at the Synapse | 17 |
A Function for the Prion Protein? | 31 |
Agents of Death for Neurons | 51 |
Characterization of Bovine Spongiform Encephalopathy | 71 |
Differential Targeting of Neurons by Prion Strains | 85 |
MARIELISE MADDELEIN Laboratory of Biochemistry and Genetics National | 105 |
Transgenic Studies of Prion Diseases | 111 |
From Neurografts to Neuroinvasion | 129 |
Cellular and Transgenic Models of Familial Prion Diseases | 149 |
Central Nervous System Inflammation and Prion | 163 |
The Electroneuropathology of Prion Disease | 181 |
Transmissible Spongiform Encephalopathy Neurobiology | 199 |
Conformation as Therapeutic Target in the Prionoses and Other | 223 |
From Cytoplasmic Genes to Heritable Amyloidosis | 237 |
269 | |
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Términos y frases comunes
abnormal Acad activity aggregated Alzheimer's disease amino acid amyloid antibodies astrocytes Biochem Biol brain codon conformation Creutzfeldt-Jakob disease culture cytokines DeArmond deletion dendritic extracellular fibrils formation Fraser function genetic glutamate glycosylation H. F. Baker hamsters Het-s hippocampus incubation infection inhibit inoculation isoform knockout Kretzschmar ME7 mice membrane microglia Molecular molecule mouse murine mutant mutant PrPs N-terminal Natl Neurobiol neurodegeneration neuronal loss neurons Neuropathol Neurosci neurotoxicity normal overexpressing oxidative stress pathogenesis pathology peptide phenotype plaques prion disease prion domain prion protein prion replication prion strain Prnp Prnp0/0 mice Proc propagation protease-resistant PrP accumulation PrP gene PrPC PrPC expression PrPC-deficient PrPSc Prpse Prusiner PSI+ Purkinje cells receptor region residues role scrapie scrapie agent scrapie prion scrapie-infected sequence SHaPrPC spongiform encephalopathy ẞ-sheet structure studies synaptic tion tissue toxicity transmission TSES URE2 Ure2p URE3 Virol vitro wild-type yeast
Referencias a este libro
How the Cows Turned Mad: Unlocking the Mysteries of Mad Cow Disease Maxime Schwartz Vista previa restringida - 2004 |