By Gilles Grateau, Robert A. Kyle, Martha Skinner
This authoritative quantity includes 179 chapters by way of foreign specialists on contemporary advancements in our knowing of amyloid proteins, protein folding issues, and new and proposed scientific trials in amyloidosis. subject matters comprise detection and characterization recommendations; organic services; genetics; issues, prognosis, and coverings, together with organ transplants and drug cures; effects from huge scientific reviews; and epidemiology. it is a worthy source for clinicians who take care of sufferers with systemic and localized varieties of amyloidosis, and for researchers in biochemistry, neurobiology, and phone biology.
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Additional info for Amyloid and amyloidosis
Modler and K. Gast 1. Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, D-13125 Berlin, Germany. 2. Potsdam University, Physical Biochemistry, Karl-Liebknecht-Str. 24-25 Haus 25, D-14476 Golm b. Potsdam, Germany. We investigated the amyloid formation of phosphoglycerate kinase (PGK) (1), a pseudo wild-type of barstar (C40A/C82A/P27A) (2) and the Syrian hamster prion protein SHaPrP 90-232 (3) in vitro. The first two proteins are not related to any known disease or change of metabolic state of organisms.
Diekmann, T. R. Appel 1 Institut für Molekulare Biotechnologie (IMB), Beutenbergstraße 11, D-07745 Jena, Germany; ): Heller Institute of Medical Research, Tel Aviv, Israel 2 ): Max-Planck-Institut of Biochemistry, Martinsried, Germany. com The formation of amyloid fibrils from soluble polypeptide chains represents a fundamental biochemical process in the initiation and progression of the various amyloid diseases. These fibrils occur in tissues in association with a range of chemically heterogeneous substances that includes glycosaminoglycans, proteins, such as SAP, and lipids .
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. Nature 416, 535-539. 8. , 2000. Acceleration of oligomerization, not fibrillization, is a shared property of both alpha-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy.