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Amyloid Proteins, 2 Volume Set (Hardback)  | Released: 12 Sep 2005

By: Jean D Sipe (Author)   Publisher: Wiley-vch

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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... Read More

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Author:

Jean D Sipe

Publisher Name:

Wiley-vch

Language:

English

Binding:

(Hardback)

About The Book
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.About the Author: Jean D. Sipe earned her Ph.D. in Chemistry from the University of Maryland in 1971. She held various positions at the NIH before moving to Boston University in 1980, where she became full professor in 1991. Since 1997 she is also Scientific Review Administrator at the NIH's Center for Scientific Review.Dr. Sipe is a founding editor of the Journal "Amyloid" and was instrumental in establishing a new Gordon Conference on Serum Amyloid A and Amyloidosis.

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