By Gilles Grateau, Robert A. Kyle, Martha Skinner
This authoritative quantity comprises 179 chapters by means of foreign specialists on contemporary advancements in our realizing of amyloid proteins, protein folding issues, and new and proposed medical trials in amyloidosis. subject matters contain detection and characterization strategies; organic capabilities; genetics; issues, analysis, and coverings, together with organ transplants and drug treatments; effects from wide scientific stories; and epidemiology. it is a beneficial source for clinicians who deal with sufferers with systemic and localized kinds of amyloidosis, and for researchers in biochemistry, neurobiology, and mobilephone biology.
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Extra resources for Amyloid and amyloidosis
53, 436. J. W. (2000), Nature, 407, 923. , Dafforn T. , Gettins P. G. A. (2000), J. Biol. , 275, 33663. James E. L. and Bottomley S. P. (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.
P. & Hawkins, P. N. (2002). Targeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis. Nature 417, 254-9. 3. Lachmann, H. J. & Hawkins, P. 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.
Fig. 4. ABT-reaction on isolated fibrils, light microscopical picture (80x) polarization optical picture (80x) Fig. 5. The sialic acid specific reaction on isolated fibrils, light microscopical picture (80x) and polarization optical picture (80x) REFERENCES 1. S. 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.
Amyloid and amyloidosis by Gilles Grateau, Robert A. Kyle, Martha Skinner