Title Molecular pathology of the prions / edited by Harry F. Baker

Published Totowa, N.J. : Humana Press, ©2001

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Description 1 online resource (xii, 279 pages) : illustrations Series Methods in molecular medicine ; 59 Methods in molecular medicine ; 59. Contents What would Thomas Henry Huxley have made of prion diseases? / R.M. Ridley -- Prion protein as copper-binding protein at the synapse / H.A. Kretzschmar [and others] -- A function for the prion protein? / D.R. Brown and I.M. Jones -- Prion protein peptide / D.R. Brown -- Characterization of bovine spongiform encephalopathy and scrapie strains/isolates by immunochemical analysis of PRPSC / M.H. Groschup [and others] -- Differential targeting of neurons by prion strains / S.J. DeArmond -- Transgenic studies of prion diseases / G.C. Telling -- Prions: From neurografts to neuroinvasion / M. Glatzel [and others] -- Cellular and transgenic models of familial prion diseases / D.A. Harris [and others] -- Central nervous system inflammation and prion disease pathogenesis / S. Betmouni and V. Hugh Perry -- The electroneuropathology of prion disease / J. Richard Greene -- Transmissible spongiform encephalopathy neurobiology and ultrastructure suggests extracellular PRPSC conversion consistent with classical amyloidosis / M. Jeffrey and J.R. Fraser -- Conformation as therapeutic target in the prionoses and other neurodegenerative conditions / T. Wisniewski [and others] -- Prions of yeast from cytoplasmic genes to heritable amyloidosis / R.B. Wickner [and others] Summary It is now widely agreed that the prion protein plays a key role in the molecular pathogenesis of prion diseases-diseases that involve the misfolding of proteins-in both humans and animals. In Molecular Pathology of the Prions, noted prion researcher Harry Baker has asked internationally recognized investigators to 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. Other topics addressed include the neuronal death that occurs in prion disease, the different strains of prion disease agents, and the accumulation of protein deposits within brain parenchyma. 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, including research techniques now likely to enjoy broader application for the more common proteinopathies, such as Alzheimer's and Parkinson's diseases Bibliography Includes bibliographical references and index Notes Master and use copy. Digital master created according to Benchmark for Faithful Digital Reproductions of Monographs and Serials, Version 1. Digital Library Federation, December 2002. http://purl.oclc.org/DLF/benchrepro0212 MiAaHDL English Print version record digitized 2010 HathiTrust Digital Library committed to preserve pda MiAaHDL In Springer Protocols Subject Prion diseases -- Research -- Methodology Proteins. Central nervous system -- Infections. Central nervous system -- Diseases. Nervous system -- Diseases. Diseases. Proteins Neurodegenerative Diseases Central Nervous System Infections Central Nervous System Diseases Nervous System Diseases Amino Acids, Peptides, and Proteins Disease Chemicals and Drugs Prion Diseases Prions protein. HEALTH & FITNESS -- Diseases -- Alzheimer's & Dementia. MEDICAL -- Neurology. Medicine Pathology Prionen. Wetenschappelijke technieken. Genre/Form Laboratory manuals. Manuels de laboratoire. Form Electronic book Author Baker, Harry F. LC no. 2001026395 ISBN 9781592591343 0896039242 9780896039247 1592591345 1280821019 9781280821011 9786610821013 6610821011

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