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- Sofort-KaufenNeurodegeneration and Prion Disease by David R. Brown (English) Hardcover Book
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eBay-Artikelnr.:226222258847
Artikelmerkmale
- Artikelzustand
- Neuwertig
- Hinweise des Verkäufers
- ISBN-13
- 9780387239224
- Book Title
- Neurodegeneration and Prion Disease
- ISBN
- 9780387239224
Über dieses Produkt
Product Identifiers
Publisher
Springer
ISBN-10
0387239227
ISBN-13
9780387239224
eBay Product ID (ePID)
44123718
Product Key Features
Number of Pages
Xv, 473 Pages
Publication Name
Neurodegeneration and Prion Disease
Language
English
Publication Year
2005
Subject
Neurology, Neuroscience, Life Sciences / Neuroscience, Life Sciences / Cell Biology, Infectious Diseases, Applied
Type
Textbook
Subject Area
Mathematics, Science, Medical
Format
Hardcover
Dimensions
Item Height
0.5 in
Item Weight
34.9 Oz
Item Length
9.3 in
Item Width
6.1 in
Additional Product Features
Intended Audience
Scholarly & Professional
LCCN
2004-062570
Dewey Edition
22
Number of Volumes
1 vol.
Illustrated
Yes
Dewey Decimal
616.8/3
Table Of Content
Neuropathology of Transmissible Spongiform Encephalopathies (Prion Diseases).- Central Pathogenesis of Prion Diseases.- Hereditary Prion Protein Amyloidoses.- Mouse Behavioural Studies and What They Can Teach Us about Prion Diseases.- Electrophysiological Approaches to the Study of Prion Diseases.- Prion Protein, Prion Protein-Like Protein, and Neurodegeneration.- Oxidative Stress and Mitochondrial Dysfunction in Neurodegeneration of Transmissible Spongiform Encephalopathies (TSEs).- Mechanisms of Prion Toxicity and Their Relationship to Prion Infectivity.- A Stone Guest on the Brain: Death as a Prion.- Molecular Mechanisms Mediating Neuronal Cell Death in Experimental Models of Prion Diseases, in vitro.- Processing and Mis-Processing of the Prion Protein: Insights into the Pathogenesis of Familial Prion Disorders.- Signaling Pathways Controling Prion Neurotoxicity: Role of Endoplasmic Reticulum Stress-Mediated Apoptosis.- Cell Culture Models to Unravel Prion Protein Function and Aberrancies in TSE.- Insights into the Cellular Trafficking of Prion Proteins.- The Molecular Basis of Prion Protein-Mediated Neuronal Damage.- Conclusion: Intervention, the Final Frontier.
Synopsis
David R. Brown Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK In 1982 Stanley Prusiner and colleagues puri'ed an abnormal protein from the brains of mice experimentally infected with a rare sheep dis- 1 ease called scrapie . This protein was called the prion protein. Earlier work had suggested that this diseases and others, loosely collected - gether as transmissible spongiform encephalopathies (TSEs), were not transmitted by conventional infectious agents. Prusiner suggested that 2 this new protein was the infectious agent in these diseases . Such a contentious suggestion lead to ferocious debate. Many researchers still maintained that there was no such thing as an infectious protein. - spite this, by 1990 most people accepted that the cause of the TSEs was the abnormal isoform of the prion protein his research group had id- ti'ed. The most convincing evidence for this had come from the work of Charles Weissmann, whose prion protein knockout mice could not be infected because they lacked expression of the protein that was now 3,4 forever linked to these disease . Since then it has become more widely accepted for these diseases to be termed prion diseases. In 1997 when 5 Stanley Prusiner won the Nobel Prize for his work on prion diseases . Even then, there was still an element of resistance in the scienti'c c- munity. It was considered that, in order the transmissible agent to truly be a protein only, the protein would have to be generated from a rec- binant source., This is the first and only book on the subject of prions to cover the cause of cell death in the disease. It covers the full range of competing theories on the subject, from broad description and basic points up to the final details of the basic science., This volume provides an in-depth overview from world experts on prion disease. These fatal diseases include Creutzfeldt-Jakob disease, chronic wasting disease in deer, scrapie of sheep, bovine spongiform encephalopathy (mad cow?'s disease) of cattle and related diseases. Understanding what causes neuronal death in these diseases is essential to both preventing and curing them. The most recent advances in understanding neuronal death in prion diseases are presented. Prion diseases serve as an experimental model for all neurodegenerative conditions. This book will provide understanding of neurodegeneration and provide an up-to-date record of the state of the art for other specialists and non-specialists in related fields., David R. Brown Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, UK In 1982 Stanley Prusiner and colleagues puri?ed an abnormal protein from the brains of mice experimentally infected with a rare sheep dis- 1 ease called scrapie . This protein was called the prion protein. Earlier work had suggested that this diseases and others, loosely collected - gether as transmissible spongiform encephalopathies (TSEs), were not transmitted by conventional infectious agents. Prusiner suggested that 2 this new protein was the infectious agent in these diseases . Such a contentious suggestion lead to ferocious debate. Many researchers still maintained that there was no such thing as an infectious protein. - spite this, by 1990 most people accepted that the cause of the TSEs was the abnormal isoform of the prion protein his research group had id- ti?ed. The most convincing evidence for this had come from the work of Charles Weissmann, whose prion protein knockout mice could not be infected because they lacked expression of the protein that was now 3,4 forever linked to these disease . Since then it has become more widely accepted for these diseases to be termed prion diseases. In 1997 when 5 Stanley Prusiner won the Nobel Prize for his work on prion diseases . Even then, there was still an element of resistance in the scienti?c c- munity. It was considered that, in order the transmissible agent to truly be a protein only, the protein would have to be generated from a rec- binant source.
LC Classification Number
RC321-580
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