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By Moerder D., Pamadi B.

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2,926-928. P. (1997a). Cellular actions of P-amyloid precursor protein, and its soluble and fibrillogenic peptide derivatives. Physiol. Rev. 77, 1081-1 132. P. (1997b). Mother’s legacy: Mitochondria1 DNA mutations and Alzheimer’s disease. Trends Neurosci. 20,373-375. P. (1998). Modification of ion homeostasis by lipid peroxidation: roles in neuronal degeneration and adaptive plasticity. Trends Neurosci. 53-57. P. G. (1996). Amyloid 0-peptide alters thrombin-induced calcium responses in cultured human neural cells.

Summary . . . . . . . . . . . . . . . . . . . . 65 66 INTRODUCTION The identification of a novel class of mutation, referred to as dynamic mutations (Richards and Sutherland, 1992) or tandem repeat expansions (Tables 1 and 2), has revolutionized our understanding of how genetic diseases can arise in humans. Dynamic mutations arise from genetic instability of short tandem DNA repeat sequences that are generally polymorphic. Instability generally favors the tendency toward expansion, though on some occasions, contractions in repeat lengths have been observed.

J. Biol. Chem. 272,14505-14508. G. (1994). Estrogen replacement therapy in older women. Comparisons between Alzheimer’s disease cases and nondemented control subjects. Arch. Neurol. 51,896-900. , Floyd, R. A. (1994). A model for 0-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer’s disease. Proc. Natl. Acad. Sci. A. 91,3270-3274. E. (1991). Apolipoprotein Epolymorphisms affect atherosclerosisin young males. Arterioscler. Thromb. 11, 1237-1244.

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Constrained Minimization of smooth function using a genetic algoritm by Moerder D., Pamadi B.


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