Amyloid Proteins

Beschreibung

There is increasing evidence that a significant number of clinical disorders involve changes in protein folding. The hallmark of these diseases is the formation of intracellular protein aggregates, the so-called amyloid plaques or fibrils. Progress in amyloid research has now finally provided the link between biochemical cause and pathological effect, opening up new ways of diagnosis and treatment of these severe disorders. This is the first book to present a systematic overview of all known fibril-forming proteins, including their biochemical characteristics and pathophysiology. It considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders, dealing with their common structural and thermodynamic features that lead to amyloid fibril formation and disease. Emphasis is on the thermodynamics of protein folding, the structure and physiologic effects of common oligomeric and subfibrillar intermediates and the influence of the extracellular matrix and cellular trafficking and metabolism on the genesis and catabolism of beta pleated sheet proteins. From the contents: * Overview of Amyloidosis and Amyloid Proteins * Protein Structure and the Beta Pleated Sheet Conformation * Protein Folding, Unfolding and Refolding * Pathway to Amyloid Fibril Formation * Pathophysiology of Amyloid Fibril Formation * Amyloid Proteins -- Brain, Systemic, Hormone The chapters on specific amyloid proteins all follow a common structure, allowing quick access to the desired biochemical and medical data, making this a first-stop reference for clinicians and researchers alike.
A first-stop reference on proteins associated with amyloidosis. This book is the first to present a systematic overview of all known fibril-forming proteins, including their biochemical characteristics and pathophysiology. It considers the clinically recognized amyloid proteins that are known to be associated with the amyloid protein folding disorders, dealing with their common structural and thermodynamic features that lead to amyloid fibril formation and disease. Emphasis is on the thermodynamics of protein folding, the structure and physiologic effects of common oligomeric and subfibrillar intermediates and the influence of the extracellular matrix and cellular trafficking and metabolism on the genesis and catabolism of beta pleated sheet proteins. The chapters on specific amyloid proteins all follow a common structure, allowing quick access to the desired biochemical and medical data, making this an invaluable tool for clinicians and researchers alike.

Autor*in

Jean D. Sipe

Themen in »Amyloid Proteins«

Biochemie Biowissenschaften Cellular & Molecular Medicine Chemie Chemistry Life Sciences Medical Science Medizin Molekularbiologie Neurologie Neuroscience Neurowissenschaften Protein Science Proteine Structural Biology

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