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References
Iwata, N. et al. Identification of the major Aβ1–42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition. Nature Med. 6, 143–150 (2000).
Mackic, J.B. et al. Human blood–brain barrier receptors for Alzheimer's amyloid β 1–40. Asymmetrical binding, endocytosis, and transcytosis at the apical side of brain microvascular endothelial cell monolayer. J. Clin. Invest. 102, 734–743 (1998).
Zlokovic, B.V. et al. Glycoprotein 330/megalin: probable role in receptormediated transport of apolipoprotein J alone and in a complex with Alzheimer disease amyloid β at the blood-brain and blood-cerebrospinal fluid barriers. Proc. Natl. Acad. Sci. USA 93, 4229–4234 (1996).
Blanc, E.M., Toborek, M., Mark, R.J., Hennig, B. & Mattson, M.P. Amyloid β-peptide induces cell monolayer albumin permeability, impairs glucose transport, and induces apoptosis in vascular endothelial cells. J. Neurochem. 68, 1870–1881 (1997).
Thomas, T., Thomas, G., McLendon, C. & Sutton, T & Mullan, M. β-amyloid-mediated vasoactivity and vascular endothelial damage. Nature. 380, 168–171 (1996).
Hersh, L.B. & Morihara, K. Comparison of subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin. J. Biol. Chem. 261, 6433–6437 (1986).
Hsiao K. et al. Correlative memory deficits, Aβ elevation, and amyloid plaques in transgenic mice. Science 274, 99–102 (1996).
Yan, SD, et al. RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease. Nature 382, 685–691 (1996).
Narita, M., Holtzman, D.M., Schwartz, A.L. & Bu, G. α2-macroglobulin complexes with and mediates the endocytosis of β-amyloid peptide via cell surface low-density lipoprotein receptor-related protein. J. Neurochem. 69, 1904–1011 (1997).
Permanne, B. et al. Aβ40 and Aβ42 clearance in a transgenic mouse model expressing human ApoE3 and ApoE4. Soc. Neurosci. Abstr. 25, 1058 (1999).
Jarret, J.T. & Lansbury, P.T. Jr. Seeding “one-dimensional crystallization” of amyloid: a pathogenic mechanism of Alzheimer's disease and scrapie? Cell 73, 1055–1058 (1993).
Hardy, J. Amyloid, the presenilins and Alzheimer's disease. Trends Neurosci. 20, 154–159 (1997).
Selkoe, D.J. The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447–453 (1998).
Price, D.L., Tanzi, R.E., Borchelt, D.R. & Sisodia, S.S. Alzheimer's disease: genetic studies and transgenic models. Annu. Rev. Genet. 32, 461–493 (1998).
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Iwata, N., Tsubuki, S., Hama, E. et al. Reply to: 'Clearance of amyloid β-peptide from brain: transport or metabolism?'. Nat Med 6, 718–719 (2000). https://doi.org/10.1038/77399
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DOI: https://doi.org/10.1038/77399
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