Prion-related diseases, known as transmissible spongiform encephalopathies (TSEs), are infectious, fatal neurodegenerative disorders for which there is no cure, treatment, nor even a means for early diagnosis. The horrific advent of Mad Cow Disease -- transmitted to humans through eating meat from steers sickened by bovine spongiform encephalopathy

Human Prion Diseases, Volume 153 is designed to update the reader on the latest advances and clinical aspects of prion diseases. The book is organized into five sections, including the pathophysiology of prions and a description of animal and human diseases. This is followed by detailed reports on recent advances in diagnosis strategies for the development of novel anti-prion molecules and possible designs of clinical trials in such a rare disease. An introductory chapter gives an extensive historical background of prion research, with a final chapter highlighting recent progress, and more importantly, unsolved problems. - Offers an authoritative overview of prion diseases in humans, detailing the pathogenesis of the disease, clinical investigations, and the diagnosis of both the genetic and acquired forms - Provides clarity and context by presenting prion diseases in relation to other neurodegenerative diseases in humans - Emphasizes the unique properties of prion diseases and consequent problems they can cause, both clinically and in public health terms

Prions are infectious proteins responsible for diseases such as Creutzfeldt-Jakob disease and "mad cow" disease. They are misfolded versions of normal proteins that replicate by converting their normal cellular counterparts into abnormal prion proteins that disrupt cell function and can be transmitted to other cells and individuals. This book examines our under-standing of their structure, biochemistry, and pathophysiology.

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.

In Advancing Prion Science, the Institute of Medicine's Committee on Transmissible Spongiform Encephalopathies Assessment of Relevant Science recommends priorities for research and investment to the Department of Defense's National Prion Research Program (NPRP). Transmissible spongiform encephalopathies (TSEs), also called prion diseases, are invariably fatal neurodegenerative infectious diseases that include bovine spongiform encephalopathy (commonly called mad cow disease), chronic wasting disease, scrapie, and Creutzfeldt-Jakob disease. To develop antemortem diagnostics or therapies for TSEs, the committee concludes that NPRP should invest in basic research specifically to elucidate the structural features of prions, the molecular mechanisms of prion replication, the mechanisms of TSE pathogenesis, and the physiological function of prions' normal cellular isoform. Advancing Prion Science provides the first comprehensive reference on present knowledge about all aspects of TSEs' from basic science to the U.S. research infrastructure, from diagnostics to surveillance, and from prevention to treatment. This report summarizes the progress thus far.

Neurogenetics, Part II, Volume 148, the latest release in the Handbook of Clinical Neurology, provides the latest information on the genetic methodologies that are having a significant impact on the study of neurological and psychiatric disorders. Using genetic science, researchers have identified over 200 genes that cause or contribute to neurological disorders. Still an evolving field of study, defining the relationship between genes and neurological and psychiatric disorders is expected to dramatically grow in scope. Part II builds on the foundation of Part I, expanding the coverage to dementias, paroxysmal disorders, neuromuscular disorders, white matter and demyelination diseases, cerebrovascular diseases, adult psychiatric disorders and cancer and phacomatoses. - Contains comprehensive coverage of neurogenetics - Details the latest science and its impact on our understanding of neurological, psychiatric disorders - Presents a focused reference for clinical practitioners and the neuroscience/neurogenetics research community

A conformational transition of the cellular prion protein (PrPC) into an aberrantly folded isoform designated scrapie prion protein (PrPSc) is the hallmark of a variety of neurodegenerative disorders collectively called prion diseases. They include Creutzfeldt-Jakob disease and Gerstmann-Stäussler-Scheinker syndrome in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle and chronic wasting disease (CWD) in free-ranging deer. In contrast to the deadly properties of misfolded PrP, PrPC seems to possess a neuroprotective activity. More-over, animal models indicated that the stress-protective activity of PrPC and the neurotoxic effects of PrPSc are somehow interconnected. In this timely book, leading scientists in the field have come together to highlight the apparently incongruous activities of different PrP conformers. The articles outline current research on celluar pathways implicated in the formation and signaling of neurotoxic and physiological PrP isoforms and delineate future research direction. Topics covered include the physiologcial activity of PrPC and its possible role as a neurotrophic factor, the finding that aberrant PrP conformers can cause neurodegeneration in the absence of infectious prion propagation, the requirement of the GPI anchor of PrPC for the neurotoxic effects of scrapie prions, the pathways implicated in the formation and neurotoxic properties of cytosolically localized PrP, the impact of metal ions on the processing of PrP, and the role of autophagy in the propagation and clearance of PrPSc. The book is fully illustrated and chapters include comprehensive reference sections. Essential reading for scientists involved in prion research.

The author, a 1997 recipient of the Noble Prize in medicine, describes the years he spent researching and demonstrating how the infectious proteins known as prions were responsible for brain diseases and how his theory has now become widely accepted in the science establishment.

DIVThe story of the revolutionary science that is unraveling the mysteries of mad cow and other fatal brain diseases/div