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By Takaomi Comings Saido

Beta-secretase M. Citron Alpha-secretases S. Ishiura ADAM 10/alpha secretase and presenilins/gamma secretase in APP processing and notch signaling D. Hartmann Gamma-secretase and presenilin M. Wolfe Biochemistry of gamma-secretase (tentative name) S. Sinha Presenilin and intracellular protein delivery Degradation of Abeta by means of neprilysin T.C. Saido Degradation of Abeta by means of endothelin-converting enzyme C. Eckman Degradation of Abeta by way of insulin-degrading enzyme Lipid raft and Abeta metabolism T. Golde Lipid raft and Abeta accumulation M. Morishima-Kawashima and Y. Ihara Transport-dependent clearance of Abeta B. Zlokovic Abeta vaccination C. Lemere

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A-Beta Metabolism and Alzheimer's Disease (Neuroscience Intelligence Unit 7)

Beta-secretase M. Citron Alpha-secretases S. Ishiura ADAM 10/alpha secretase and presenilins/gamma secretase in APP processing and notch signaling D. Hartmann Gamma-secretase and presenilin M. Wolfe Biochemistry of gamma-secretase (tentative identify) S. Sinha Presenilin and intracellular protein shipping Degradation of Abeta via neprilysin T.

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Saitoh T, Sundsmo M, Roch JM et al. Secreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts. Cell 1989; 58(4):615-622. 23. Mattson MP, Cheng B, Culwell AR et al. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein. Neuron 1993; 10(2):243-254. 24. Kang J, Lemaire HG, Unterbeck A et al. The precursor of Alzheimer’s disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987; 325(6106):733-736.

Dual protease inhibitor therapy in HIV-infected patients: pharmacologic rationale and clinical benefits. Annu Rev Pharmacol Toxicol 2000; 40:649-674. 30. Götz J, Chen F, van Dorpe J et al. Formation of neurofibrillary tangles in P301L tau transgenic mice induced by Aβ42 fibrils. Science 2001; 293:1491-1495. 31. Lewis J, Dickson DW, Lin WL et al. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 2001; 293:1487-1491. 32. Campion D, Dumanchin C, Hannequin D et al.

BACE1 contains two active site motifs at amino acids 93 to 96 and 289 to 292 in the lumenal domain, each containing the highly conserved signature sequence of aspartic proteases D T/S G T/S. Based on the amino acid sequence, BACE1 is predicted to be a type I transmembrane protein with the active site on the lumenal side of the membrane where β-secretase cleaves APP. At the amino acid level, BACE1 shows less than 30% sequence identity with human pepsin family members. 3, not associated with AD. We have thoroughly demonstrated that BACE1 exhibits all the known properties of β-secretase7 and subsequent publications from other groups have confirmed this analysis.

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