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197. Guo, Q., Manolopoulou, M., Bian, Y. et al. (2010) Molecular basis for the recognition and
cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme. J. Mol.
Biol. , 395 , 430-443.
198. Zirah, S., Kozin, S.A., Mazur, A.K. et al. (2005) Structural changes of region 1-16 of the
Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging. J. Biol. Chem. ,
281 , 2151-2161.
199. da Silva, G.F.Z., Tay, W.M., and Ming, L.-J. (2005) Catechol oxidase-like oxidation chemistry
of the 1-20 and 1-16 fragments of Alzheimer's disease-related b-Amyloid peptide: their struc-
ture-activity correlation and the fate of hydrogen peroxide. J. Biol. Chem. , 280 , 16601-16609.
200. (a) Some recent publications: Mirzabekov, T., Lin, M.C., Yuan, W.L. et al. (2004) Channel
formation in planar lipid bilayers by a neurotoxic fragment of the b-amyloid peptide. Biochim.
Biophys. Res. Commun. , 202 , 1142-1148; (b) Terzi, E. Holzemann, G., and Seeling, J. (1995)
Self-association of b-amyloid peptide (1-40) in solution and binding to lipid membrane. J. Mol.
Biol. , 252 , 633-642; (c) Muller, W.E., Koch, S., Eckert, A. et al. (1995) b-amyloid peptide
decrease membrane fluidity. Brain Res. , 674 , 133-136; (d) Allen, D.D., Galdzicki, Z., Brining,
S.K. et al. (1997) Beta-amyloid induced increase in choline flux across PC12 cell membranes.
Neurosci. Lett. , 234 , 71-73; (e) Inoue, S. Kuroiwa, M., and Kisilevsky, R. (1999) Basement
membranes, microfibrils and b amyloid fibrillogenesis in Alzheimer' disease: high resolution
ultrastructural findings. Brain Res. Rev. , 29 , 218-231; (f) Rodrigues, C.M.P., Sola, S., Brito, M.
A. et al. (2001) Amyloid b-peptide disrupts mitochondrial membrane lipid and protein struc-
ture: Protective role of tauroursodeoxycholate. Biochem. Biophys. Res. Commun. , 281 ,468-
474; (g) Butterfield, D.A. and Lauderback, C.M. (2002) Lipid peroxidation and protein oxida-
tion in Alzheimer's disease brain: Potential causes and consequences involving amyloid b-pep-
tide-associated free radical oxidative stress. Free Radical Biol. Med. , 32 , 1050-1060; (h) Kiuchi,
Y., Isobe, Y., Fukushima, K., and Kimura, M. (2002) Disassembly of amyloid b-protein fibril by
basement membrane components. Life Sci. , 70 , 2421-2431; (i) Mremer, J.J. and Murphy, R.M.
(2003) Kinetics of adsorption of b-amyloid peptide Ab(1-40) to lipid bilayers. J. Biochem. Bio-
phys. Met. , 57 , 159-169; (j) Mingeot-Leclercq, M.P., Lins, L., Bensliman, M. et al. (2003)
Piracetam inhibits the lipid-destabilising effect of the amyloid peptide Ab C-terminal fragment.
Biochim. Biophys. Acta , 1609 , 28-38; (k) Wood, W.G., Eckert, G.P., Igbavboa, U., and Muller,
W.E. (2003) Amyloid beta-protein interactions with membranes and cholesterol: causes or casu-
alties of Alzheimer's disease. Biochim. Biophys. Acta , 1610 , 281-290.
201. (a) Prusiner, S.B. (1998) Prions. Proc. Natl Acad. Sci. USA , 95 , 13363-13383; (b) Brown, D.
R., Qin, K.F., Herms, J.W. et al. (1997) The cellular prion protein binds copper in vivo .
Nature , 390 , 684-687.
202. Wadsworth, J.D., Hill, A.F., Joiner, S. et al. (1999) Strain-specific prion-protein conformation
determined by metal ions. Nat. Cell Biol. , 1 , 55-59.
203. (a) Riek, R., Hornemann, S., Wider, G. et al. (1996) NMR structure of the mouse prion protein
domain PrP(121-321). Nature , 382 , 180-182; (b) Zahn, R., Liu, A., Luhrs, T. et al. (2000)
NMR solution structure of the human prion protein. Proc. Natl Acad. Sci. USA , 97 , 145-150.
204. Haire, L.F., Whyte, S.M., Vasisht, N. et al. (2004) The crystal structure of the globular domain
of sheep prion protein. J. Mol. Biol. , 336 , 1175-1183.
205. Donne, D.G., Viles, J.H., Groth, D. et al. (1997) Structure of the recombinant full-length ham-
ster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl Acad. Sci. USA ,
94 , 13452-13457.
206. Zahn, R. (2003) The octapeptide repeats in mammalian prion protein constitute a pH-depen-
dent folding and aggregation site. J. Mol. Biol. , 334 , 477-88.
207. (a) Dyson, H.J. and Wright, P.E. (2005) Intrinsically unstructured protein and their functions.
Nat. Rev. Mol. Cell Biol. , 6 , 197-208; (b) Schlessinger, A., Schaefer, C., Vicedo, E. et al.
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