References
- Sipe J D. Amyloidosis. Crit Rev Clin Lab Sci 1994; 31: 325–54
- Mattson M P, Goodman Y. Different amyloidogenic peptides share a similar mechanism of neurotoxicity involving reactive oxygen species and calcium. Brain Res 1995; 679: 219–24
- Hsiao K, Chapman P, Nilsen S, Eckman C, Harigaya Y, Yang Younkin S, Cole G. Correlative memory defects, A beta elevation, and amyloid plaques in transgenic mice. Science 1996; 274: 99–102
- Westermark P, Wilander E. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Diabetologia 1978; 15: 417–421
- Clark A, Lewis C E, Willis A C, Cooper G JC, Morris J F, Reid K BM. Islet amyloid formed from diabetes associated peptide may be pathogenic in type II diabetes. Lancet 1987; ii: 231–234
- Cooper G JS, Willis A C, Clare A, Turner R C, Sim R B, Reid K BM. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 1987; 84: 8628–8632
- de Konig E JP, Morris E R, Hofhuis F MA, Posthuma G, Hoppener J WM, Morris J F, Capel P A, Clark A, Verbeek J S. Intra- and extra-cellular amyloid fibrils are formed in cultured pancreatic islets of transgenic mice expressing human islet amyloid polypeptide. Proc Natl Acad Sci USA 1994; 91: 8467–8471
- Lorenzo A, Razzaboni B, Weir G C, Yankner B A. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes melletus. Nature 1994; 368: 756–760
- Forloni G, Angeretti N, Chiesa R, Monzani E, Salmona M, Bugiani O, Tagliavini F. Neurotoxicity of a prion protein fragment. Nature 1993; 362: 543–546
- Hegde R S, Mastrianni J A, Scott M R, De Fea K A, Trenblay P, Torchia M, De Armond S J, Prusiner S B, Lingappa V R. A transmembrane form of the prion protein in neurodegenerative disease. Science 1998; 279: 827–34
- Prusiner S B, Scott M R, DeArmond S J, Cohen F E. Prion Protein Biology Cell 1998; 93: 337–348
- Arispe N, Rojas E, Pollard H D. Alzheimer's disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl Acad Sci USA 1993; 89: 10940–10944
- Arispe N, Pollard H D, Rojas E. Zn2+ interaction with Alzheimer amyloid b protein calcium channels. Proc Natl Acad Sci USA 1996; 93: 1710–5
- Mirzabekov T, Lin M-C, Kagan B L. Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem 1996; 270: 1988–1992
- Lin M, Mirzabekov T, Kagan B L. Channel formation by a neurotoxic fragment of the prion protein. J Biol Chem 1997; 272: 44–47
- Hirakura Y, Lin M C, Kagan B L. Alzheimer amyloid Aβ 1–42 channels: Effects of solvent, pH, and Congo red. J Neurosci Res 1999; 57: 458–66
- Mirzabekov T, Lin M-C, Yuan W L, Marshall P, Carman M, Lieberburg I, Kagan B L. Channel formation in planar lipid bilayers by a neurotoxic fragment of the beta-amyloid peptide. Biochem Biophys Res Commun 1994; 202: 1142–1148
- Hirakura Y, Kagan B L. The role of amyloid peptide channels in Alzheimer's and other amyloidoses. Einstein QJ Biol Med 2000, in press
- Rhee S K, Quist A P, Lal R. Amyloid p Protein-(1–42) Forms Calcium-permeable, Zn2+-sensitive Channel. J Biol Chem 1998; 273: 13379–13382
- Caspi S, Halimi M, Yanai A, Sasson S B, Taraboulous A, Gabizon R. The antiprion activity of Congo Red:putative mechanism. J Biol Chem 1998; 273: 3484–9
- Lorenzo A, Yankner B A. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proc Natl Acad Sci USA 1994; 91: 12243–7
- Mirzabekov T, Silberstein A, Kagan B L. The use of planar lipid bilayer membranes for rapid screening of membrane active compounds. Meth Enz 1998; 294: 67–74
- Kawahara M, Arispe N, Kuroda Y, Rojas E. Alzheimer's disease amyloid-beta protein forms Zu(2+)- sensitive, cation selective channels across excised membrane patches from hypothalamic neurons. Biophys J 1997; 73: 67–75
- Prasad A S. Zinc: The biology and therapeutics of an ion. Ann Int Med 1996; 125: 142–4
- Mossad S B, Macknin M L, Medendorp S V, Mason P. Zinc gluconate lozenges for treating the common cold: A randomized, double-blind, placebo-controlled study. Ann Int Med 1996; 125: 81–8