By Jean D. Sipe
A first-stop reference on proteins linked to amyloidosis. This booklet is the 1st to give a scientific review of all recognized fibril-forming proteins, together with their biochemical features and pathophysiology. It considers the clinically well-known amyloid proteins which are recognized to be linked to the amyloid protein folding issues, facing their universal structural and thermodynamic positive factors that bring about amyloid fibril formation and illness. Emphasis is at the thermodynamics of protein folding, the constitution and physiologic results of universal oligomeric and subfibrillar intermediates and the effect of the extracellular matrix and mobile trafficking and metabolism at the genesis and catabolism of beta pleated sheet proteins. The chapters on particular amyloid proteins all persist with a standard constitution, permitting easy access to the specified biochemical and scientific facts, making this a useful software for clinicians and researchers alike.
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Extra resources for Amyloid Proteins: The Beta Sheet Conformation and Disease
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E. Dwulet, J. Liepnieks and M. D. Benson. Variant apolipoprotein AI as a major constituent of a human hereditary amyloid. Biochem Biophys Res Commun 1988, 156, 762– 768. Benson, M. , J. Liepnieks, M. Yazaki, T. Yamashita, K. Hamidi Asl, B. Guenther and B. Kluve-Beckerman. A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene. Genomics 2001, 72, 272–277. 23 24 1 Amyloidosis and Amyloid Proteins: Brief History and Definitions 129 Benson, M. , J. Liepnieks, T.
Amyloid Proteins: The Beta Sheet Conformation and Disease by Jean D. Sipe