Download Amyloid and Amyloidosis by Gilles Grateau (Editor), Robert A. Kyle (Editor), Martha PDF

By Gilles Grateau (Editor), Robert A. Kyle (Editor), Martha Skinner (Editor)

This authoritative quantity includes 179 chapters via foreign specialists on fresh advancements in our realizing of amyloid proteins, protein folding problems, and new and proposed scientific trials in amyloidosis. themes comprise detection and characterization concepts; organic services; genetics; problems, analysis, and coverings, together with organ transplants and drug cures; effects from wide medical experiences; and epidemiology. this can be a helpful source for clinicians who take care of sufferers with systemic and localized sorts of amyloidosis, and for researchers in biochemistry, neurobiology, and cellphone biology.

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Extra info for Amyloid and Amyloidosis

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Biochim Biophys Acta 1594, 1-5. 4. , 2002. Amyloid fibril formation by human stefin B: influence of the initial pH-induced intermediate state. Biochem Soc Trans. 30, 543-547. Review. 5. , 2002. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511. 6. , 1999. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. J. Biol. Chem. 274, 25945-25952. 7. , 2002. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo.

Chem. , 35, 413. Aszodi A. R. (1996), Fold. , 1, 325. M. J. , 10, 905. , Ptak M. and Vovelle F. (1997), Fold. , 2, 183. Godzik A. , 44, 525. Skolnick J. and Kihara D. (2000), Proteins: Struct. Funct. , 42, 319. , Marchler-Bauer A. H. (2000), J. Mol. , 296, 1319. V. and Luthey-Schulten Z. (2002), Curr. Opin. Struct. , 12, 176. Tramontano A. and Morea V. (2003), Proteins: Struct. Funct. , 53, 352. , Cheng H. V. (2003), Proteins: Struct. Funct. , 53, 395. , Hadley C. B. (2003), Proteins: Struct. Funct.

N. (2003). Novel pharmacological strategies in amyloidosis. Nephron Clin Pract 94, c85-8. si In several cases of single point mutations inverse correlation between stability and propensity to form amyloidlike fibrils has been demonstrated (1). Previously, chimeric mutants of human stefins A and B have been studied. , submitted) have shown that there is no correlation between stability and the propensity to fibrillise. The apparent contradiction may be understood if we compare proteins of the same structural class : all stefin B-like and all stefin A-like.

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