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The Nature and Origin of Amyloid Fibrils

CIBA Foundation Staff

ISBN 10: 0471963615 / ISBN 13: 9780471963615
Verlag: John Wiley & Sons, U.K., 1996
Gebraucht Zustand: Good Hardcover
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Ciba Foundation symposium 112. Cover clean, bright and shiny. Pages white and tight. Buchnummer des Verkäufers 175507

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Bibliografische Details

Titel: The Nature and Origin of Amyloid Fibrils

Verlag: John Wiley & Sons, U.K.

Erscheinungsdatum: 1996

Einband: hardcover

Zustand:Good

Zustand des Schutzumschlags: No Dust Jacket

Art des Buches: Used

Über diesen Titel

Inhaltsangabe:

Amyloid fibrils are associated with a range of pathological disorders including Alzheimer's Disease, Down's syndrome, diabetes, cardiomyopathies, and transmissible spongiform encephalopathies. This volume is a comprehensive account of recent developments in the understanding of the process of amyloid fibrils. Contains up-to-date data on all of the clinical problems which, despite their pathological significance, are still largely unsolved.

From the Back Cover:

The term ?amyloid fibril? refers to a protein that has self-assembled into an insoluble antiparallel β-pleated sheet quaternary structure. This process is known as amyloidogenesis, and in combination with other non-protein components these fibrils give rise to the amyloid plaques that are seen in a number of pathological processes. As recently as 25 years ago, amyloid fibrils were thought to represent a single protein entity on the basis of their unique morphological and protein-organizational characteristics. Subsequently it has been shown that a number of different amyloid proteins exist?so far almost 20 have been identified, each associated with a particular disorder. Among these, β-amyloid forms plaques in the brains of individuals with Alzheimer?s disease and Down?s syndrome, transthyretin is responsible for familial amyloid polyneuropathies and cardiomyopathies, and prion protein is implicated in transmissible spongiform encephalopathies. Despite their pathological significance, the fundamental questions of how amyloid fibrils form and why they are not degraded are still largely unsolved. This book brings together scientists working on different amyloidoses to discuss these questions and to examine how an understanding of amyloidogenesis might contribute to the development of therapeutic interventions.

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