By Jean D. Sipe
A first-stop reference on proteins linked to amyloidosis. This booklet is the 1st to give a scientific evaluation of all identified fibril-forming proteins, together with their biochemical features and pathophysiology. It considers the clinically well-known amyloid proteins which are identified to be linked to the amyloid protein folding issues, facing their universal structural and thermodynamic good points 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 stick to a typical constitution, permitting easy accessibility to the specified biochemical and scientific information, making this a useful software for clinicians and researchers alike.
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Additional info for Amyloid Proteins: The Beta Sheet Conformation and Disease
Rérat. 8 Å. J Mol Biol 1978, 121, 339–356. Benson, M. D. Partial amino acid sequence homology between a heredofamilial amyloid protein and human plasma prealbumin. J Clin Invest 1981, 67, 1035–1041. Skinner, M. and A. S. Cohen. The prealbumin nature of the amyloid protein in familial amyloidotic polyneuropathy (FAP) – Swedish variety. Biochem Biophys Res Commun 1981, 99, 1326–1332. , S. Araki, K. Toshimori, H. K. Nakagawa and S. Ohtaki. Amyloid fibril protein in type I familial amyloidotic polyneuropathy in Japanese.
The SAP protein binds non-covalently and calcium dependently to ligands  such as b-pleated sheet fibrils. SAP is a normal constituent of the glomerular basement membrane  and elastic microfibrils . The nature of the amyloid fibril was long an enigma. Methods to concentrate amyloid fibrils and to make good, representative fibrillar extracts of systemic 7 8 1 Amyloidosis and Amyloid Proteins: Brief History and Definitions amyloid deposits were developed by Cohen et al.  and Pras et al.
N. J. Reeke. Threedimensional structure of b2-microglobulin. Proc Natl Acad Sci USA 1985, 82, 4225–4229. , T. Yamada, S. Odani, Y. Nakagawa, M. Arakawa, T. Kunitomo, H. Kataoka, M. Suzuki, Y. Hirasawa, T. Shirahama, A. S. Cohen and K. Schmid. A new form of amyloid protein associated with chronic hemodialysis was identified as b2-microglobulin. Biochem Biophys Res Commun 1985, 129, 701–706. 137 Gorevic, P. , T. T. Casey, W. J. Stone, 138 139 140 141 142 143 144 145 146 C. R. DiRaimondo, F. Prelli and B.
Amyloid Proteins: The Beta Sheet Conformation and Disease by Jean D. Sipe