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By Jean D. Sipe

A first-stop reference on proteins linked to amyloidosis. This ebook is the 1st to provide a scientific review of all identified fibril-forming proteins, together with their biochemical features and pathophysiology. It considers the clinically famous amyloid proteins which are identified to be linked to the amyloid protein folding problems, facing their universal structural and thermodynamic gains that result in amyloid fibril formation and affliction. 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 keep on with a typical constitution, permitting easy access to the specified biochemical and clinical information, making this a useful software for clinicians and researchers alike.

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G. Glenner. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 1983, 35, 349– 358. Opie, E. L. On relation of chronic interstitial pancreatitis to the islands of Langerhans and to diabetes mellitus. J Exp Med 1901, 5, 397–428. Weichselbaum, A. and E. Stangl. Zur Kenntnis der feineren Veränderungen des Pankreas bei Diabetes mellitus. Wien Klin Wochenschr 1901, 14, 968– 972. Ehrlich, J. C. and I. M. Ratner. Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and nondiabetic individuals.

The blood plasma protein SAA was shown to be about 40% larger than the 76amino-acid residue AA protein that was first described. This larger size apparently depended on a C-terminal extension in the SAA molecule [84]. Subsequently, it was established that human SAA is a 104-amino-acid molecule of which amyloid protein A corresponds to the major N-terminal part [85]. The acute-phase SAA is produced by the liver, but extrahepatic expression of SAA was demonstrated. Thus, it was not immediately accepted that the circulating SAA is the precursor of the amyloid protein.

3 Classification of Missmahl et al. A third classification is that of Missmahl et al. This was also suggested before the biochemical era of amyloidosis and was based on polarization findings with Congo red. These researchers noted that amyloid infiltration occurs either in association with collagen fibrils or with reticulin fibrils and based a differentiation of types on this difference [179, 180]. The classification into the pericollagen form, now known to include AL amyloidosis, and the perireticulin form, particularly including AA amyloidosis, did not survive for long.

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Amyloid Proteins: The Beta Sheet Conformation and Disease by Jean D. Sipe

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