By Gilles Grateau, Robert A. Kyle, Martha Skinner
This authoritative quantity includes 179 chapters by means of foreign specialists on fresh advancements in our realizing of amyloid proteins, protein folding problems, and new and proposed medical trials in amyloidosis. subject matters comprise detection and characterization suggestions; organic features; genetics; problems, prognosis, and coverings, together with organ transplants and drug cures; effects from large scientific reviews; and epidemiology. this can be a necessary source for clinicians who deal with sufferers with systemic and localized types of amyloidosis, and for researchers in biochemistry, neurobiology, and telephone biology.
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Extra resources for Amyloid and amyloidosis
1998), Arch. Biochem. , 356, 296. , Dehouck Y. and Rooman M. (2002), Bioinformatics, 18, 1701. , Rooman M. P. (2003), J. Mol. , 325, 581. AMYLOIDOSIS IN VIVO: FROM MOLECULAR INTERACTIONS TO THERAPEUTIC TARGETS R. Kisilevsky Department of Pathology and Molecular Medicine, Queen’s University, and The Syl and Molly Apps Research Centre, Kingston General Hospital, Kingston Ontario CANADA, K7L 3N6 INTRODUCTION Over the last 15-20 years, based on in vitro studies, major progress has been made in understanding the mechanism of amyloid fibrillogenesis.
1; Table 1). The most exposed part in lipids are unsaturated fatty acids. Since fatty acid double bonds are highly unstable , their loss reflects the Amyloid Fibrillogenesis 17 extent of degradation. This points out against a strong oxidative or hydrolytic damage of the lipid classes that could have occurred while purifying the amyloid deposits or during lipid analysis. CONCLUSION: The method is suitable for analysis of small quantities of lipids present in purified amyloid deposits. The lipids possess a typical pattern that is rich in sphingolipids and cholesterol.
The constitution and genesis of amyloid. Int Rev Exp Pathol 4:159-243, 1965. 2. Wolman, M. Amyloid, its nature and molecular structure. Lab Invest 25:104-110, 1971. 3. Inoue, S. and R. Kisilevsky. 4. G. A. Bladen. Purification and reconstution of periodic fibril and unit structure of A high resolution ultrastructural study of experimental murine AA amyloid. Lab Invest 74:670-683, 1996. human amyloid. Science 154:271-272, 1966. 5. , Deák, Gy. and J. Fischer. Aldehyde-bisulfite-toluidine blue (ABT) staining as a topooptical reaction for demonstration of linear order of vicinal OH groups in biological structures.
Amyloid and amyloidosis by Gilles Grateau, Robert A. Kyle, Martha Skinner