Alzheimer's Disease: From Pathology to Therapeutic Approaches

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123

Alzheimer's disease: the amyloid cascade hypothesis

Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484

Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide

Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744

Inflammation and Alzheimer’s disease

Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514

Imaging brain amyloid in Alzheimer's disease with Pittsburgh Compound‐B

Klunk, W. E., Engler, H., Nordberg, A., Wang, Y., Blomqvist, G., Holt, D. P., Bergström, M., Savitcheva, I., Huang, G., Estrada, S., et al. (2004) · Annals of Neurology · doi:10.1002/ana.20009 · Cited by 4,496

Alzheimer's Disease Is a Synaptic Failure

Selkoe, D. J. (2002) · Science · doi:10.1126/science.1074069 · Cited by 4,420

Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo

Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291

Mild cognitive impairment

Gauthier, S. G., Reisberg, ‌., Zaudig, M., Petersen, R. C., Ritchie, K. A., Broich, K., Belleville, S., Brodaty, H., Bennett, D. A., Chertkow, H. M., et al. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68542-5 · Cited by 4,094

β-Secretase Cleavage of Alzheimer's Amyloid Precursor Protein by the Transmembrane Aspartic Protease BACE

Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685

Phases of Aβ-deposition in the human brain and its relevance for the development of AD

Thal, D. R., Rüb, U., Orantes, M., & Braak, H. (2002) · Neurology · doi:10.1212/wnl.58.12.1791 · Cited by 3,490

Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse

Schenk, D., Barbour, R., Dunn, W., Gordon, G., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., Khan, K., et al. (1999) · Nature · doi:10.1038/22124 · Cited by 3,160

The molecular pathology of Alzheimer's disease

Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708

Curcumin Inhibits Formation of Amyloid β Oligomers and Fibrils, Binds Plaques, and Reduces Amyloid in Vivo

Yang, F., Lim, G. P., Begum, A. N., Ubeda, O. J., Simmons, M. R., Ambegaokar, S. S., Chen, P. P., Kayed, R., Glabe, C. G., Frautschy, S. A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m404751200 · Cited by 2,336

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174

Copper, iron and zinc in Alzheimer's disease senile plaques

Lovell, M. A., Robertson, J. D., Teesdale, W. J., Campbell, J. L., & Markesbery, W. R. (1998) · Journal of the Neurological Sciences · doi:10.1016/s0022-510x(98)00092-6 · Cited by 2,120

Peripherally administered antibodies against amyloid β-peptide enter the central nervous system and reduce pathology in a mouse model of Alzheimer disease

Bard, F., Cannon, C., Barbour, R., Burke, R.-L., Games, D., Grajeda, H., Guido, T., Hu, K., Huang, J., Johnson-Wood, K., et al. (2000) · Nature Medicine · doi:10.1038/78682 · Cited by 2,012

3D structure of Alzheimer's amyloid-β(1–42) fibrils

Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D. A., & Riek, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506723102 · Cited by 2,001

Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity

Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,959

Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective

Tanzi, R. E., & Bertram, L. (2005) · Cell · doi:10.1016/j.cell.2005.02.008 · Cited by 1,849

Purification and cloning of amyloid precursor protein β-secretase from human brain

Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612

Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588

Regulation of NMDA receptor trafficking by amyloid-β

Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561

Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease

Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530

Aβ peptide vaccination prevents memory loss in an animal model of Alzheimer's disease

Morgan, D., Diamond, D. M., Gottschall, P. E., Ugen, K. E., Dickey, C. A., Hardy, J., Duff, K., Jantzen, P. T., DiCarlo, G., Wilcock, D. M., et al. (2000) · Nature · doi:10.1038/35050116 · Cited by 1,506

An english translation of alzheimer’s 1907 paper, “über eine eigenartige erkankung der hirnrinde”

Stelzmann, R. A., Norman Schnitzlein, H., & Reed Murtagh, F. (1995) · Clinical Anatomy · doi:10.1002/ca.980080612 · Cited by 1,455

Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447

Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity

Yan, R., Bienkowski, M. J., Shuck, M. E., Miao, H., Tory, M. C., Pauley, A. M., Brashler, J. R., Stratman, N. C., Mathews, W. R., Buhl, A. E., et al. (1999) · Nature · doi:10.1038/990107 · Cited by 1,438

Aβ peptide immunization reduces behavioural impairment and plaques in a model of Alzheimer's disease

Janus, C., Pearson, J., McLaurin, J., Mathews, P. M., Jiang, Y., Schmidt, S. D., Chishti, M. A., Horne, P., Heslin, D., French, J., et al. (2000) · Nature · doi:10.1038/35050110 · Cited by 1,431

Mitochondrial abnormalities in Alzheimer's disease

Hirai, K., Aliev, G., Nunomura, A., Fujioka, H., Russell, R. L., Atwood, C. S., Johnson, A. B., Kress, Y., Vinters, H. V., Tabaton, M., et al. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-09-03017.2001 · Cited by 1,367

Alzheimer’s disease β-amyloid peptides are released in association with exosomes

Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., & Simons, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603838103 · Cited by 1,343

Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways

Bitan, G., Kirkitadze, M. D., Lomakin, A., Vollers, S. S., Benedek, G. B., & Teplow, D. B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222681699 · Cited by 1,316

The metallobiology of Alzheimer's disease

Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315

ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease

Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303

Peripheral anti-Aβ antibody alters CNS and plasma Aβ clearance and decreases brain Aβ burden in a mouse model of Alzheimer's disease

DeMattos, R. B., Bales, K. R., Cummins, D. J., Dodart, J.-C., Paul, S. M., & Holtzman, D. M. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.151261398 · Cited by 1,298

Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid β-protein in both transfected cells and transgenic mice

Citron, M., Westaway, D., Xia, W., Carlson, G., Diehl, T., Levesque, G., Johnson-wood, K., Lee, M., Seubert, P., Davis, A., et al. (1997) · Nature Medicine · doi:10.1038/nm0197-67 · Cited by 1,271

Correlation Between Elevated Levels of Amyloid β-Peptide in the Brain and Cognitive Decline

Näslund, J. (2000) · JAMA · doi:10.1001/jama.283.12.1571 · Cited by 1,268

Recovery of learning and memory is associated with chromatin remodelling

Fischer, A., Sananbenesi, F., Wang, X., Dobbin, M., & Tsai, L.-H. (2007) · Nature · doi:10.1038/nature05772 · Cited by 1,227

Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease

Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214

Deciphering the Molecular Basis of Memory Failure in Alzheimer's Disease

Walsh, D. M., & Selkoe, D. J. (2004) · Neuron · doi:10.1016/j.neuron.2004.09.010 · Cited by 1,207

Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease

Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118

Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide

Butterfield, D. A., Drake, J., Pocernich, C., & Castegna, A. (2001) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02173-6 · Cited by 1,114

Imaging β-amyloid burden in aging and dementia

Rowe, C. C., Ng, S., Ackermann, U., Gong, S. J., Pike, K., Savage, G., Cowie, T. F., Dickinson, K. L., Maruff, P., Darby, D., et al. (2007) · Neurology · doi:10.1212/01.wnl.0000261919.22630.ea · Cited by 1,104

Identification of a Novel Aspartic Protease (Asp 2) as β-Secretase

Hussain, I., Powell, D., Howlett, D. R., Tew, D. G., Meek, T. D., Chapman, C., Gloger, I. S., Murphy, K. E., Southan, C. D., Ryan, D. M., et al. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0811 · Cited by 1,080

Alzheimer's disease-affected brain: Presence of oligomeric Aβ ligands (ADDLs) suggests a molecular basis for reversible memory loss

Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061

Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦

Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,057

Dramatic Aggregation of Alzheimer Aβ by Cu(II) Is Induced by Conditions Representing Physiological Acidosis

Atwood, C. S., Moir, R. D., Huang, X., Scarpa, R. C., Bacarra, N. M. E., Romano, D. M., Hartshorn, M. A., Tanzi, R. E., & Bush, A. I. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.12817 · Cited by 1,009

Targeting small Aβ oligomers: the solution to an Alzheimer's disease conundrum?

Klein, W. (2001) · Trends in Neurosciences · doi:10.1016/s0166-2236(00)01749-5 · Cited by 989

Metal-Protein Attenuation With Iodochlorhydroxyquin (Clioquinol) Targeting Aβ Amyloid Deposition and Toxicity in Alzheimer Disease: A Pilot Phase 2 Clinical Trial

Ritchie, C. W., Bush, A. I., Mackinnon, A., Macfarlane, S., Mastwyk, M., MacGregor, L., Kiers, L., Cherny, R., Li, Q.-X., Tammer, A., et al. (2003) · Archives of Neurology · doi:10.1001/archneur.60.12.1685 · Cited by 988

Metabolic Regulation of Brain Aβ by Neprilysin

Iwata, N., Tsubuki, S., Takaki, Y., Shirotani, K., Lu, B., Gerard, N. P., Gerard, C. J., Hama, E., Lee, H.-J., & Saido, T. C. (2001) · Science · doi:10.1126/science.1059946 · Cited by 982

Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease

Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967

Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor

Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 952

Reconstitution of γ-secretase activity

Edbauer, D., Winkler, E., Regula, J. T., Pesold, B., Steiner, H., & Haass, C. (2003) · Nature Cell Biology · doi:10.1038/ncb960 · Cited by 914

Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress

Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885

Environmental Enrichment Reduces Aβ Levels and Amyloid Deposition in Transgenic Mice

Lazarov, O., Robinson, J., Tang, Y.-P., Hairston, I. S., Korade-Mirnics, Z., Lee, V. M.-Y., Hersh, L. B., Sapolsky, R. M., Mirnics, K., & Sisodia, S. S. (2005) · Cell · doi:10.1016/j.cell.2005.01.015 · Cited by 885

Functional gamma‐secretase inhibitors reduce beta‐amyloid peptide levels in brain

Dovey, H. F., John, V., Anderson, J. P., Chen, L. Z., Andrieu, P. D. S. I., Fang, L. Y., Freedman, S. B., Folmer, B., Goldbach, E. G., Holsztynska, E. J., et al. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00012.x · Cited by 870

Potential therapeutic applications of autophagy

Rubinsztein, D. C., Gestwicki, J. E., Murphy, L. O., & Klionsky, D. J. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2272 · Cited by 862

Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model

Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858

Staging of Alzheimer-Related Cortical Destruction

Braak, H., Braak, E., & Bohl, J. (2008) · European Neurology · doi:10.1159/000116984 · Cited by 836

Microglia and cytokines in neurological disease, with special reference to AIDS and Alzheimer's disease

Dickson, D. W., Lee, S. C., Mattiace, L. A., Yen, S.-H. C., & Brosnan, C. F. (1993) · Glia · doi:10.1002/glia.440070113 · Cited by 830

Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory

Turner, P. R., O’Connor, K., Tate, W. P., & Abraham, W. C. (2003) · Progress in Neurobiology · doi:10.1016/s0301-0082(03)00089-3 · Cited by 796

-amyloid imaging and memory in non-demented individuals: evidence for preclinical Alzheimer's disease

Pike, K. E., Savage, G., Villemagne, V. L., Ng, S., Moss, S. A., Maruff, P., Mathis, C. A., Klunk, W. E., Masters, C. L., & Rowe, C. C. (2007) · Brain · doi:10.1093/brain/awm238 · Cited by 789

Antibodies against β-Amyloid Slow Cognitive Decline in Alzheimer's Disease

Höck, C., Konietzko, U., Streffer, J. R., Tracy, J., Signorell, A., Müller-Tillmanns, B., Lemke, U., Henke, K., Moritz, E., Garcia, E., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00294-0 · Cited by 786

Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein

Lin, X., Koelsch, G., Wu, S., Downs, D., Dashti, A., & Tang, J. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.4.1456 · Cited by 769

Cu(II) Potentiation of Alzheimer Aβ Neurotoxicity

Huang, X., Cuajungco, M. P., Atwood, C. S., Hartshorn, M. A., Tyndall, J. D. A., Hanson, G. R., Stokes, K. C., Leopold, M., Multhaup, G., Goldstein, L. E., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.52.37111 · Cited by 762

Cell Biology of the Amyloid beta-Protein Precursor and the Mechanism of Alzheimer's Disease

Selkoe, D. J. (1994) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.10.110194.002105 · Cited by 748

Enhanced Proteolysis of β-Amyloid in APP Transgenic Mice Prevents Plaque Formation, Secondary Pathology, and Premature Death

Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 725

Chronic Treatment with the γ-Secretase Inhibitor LY-411,575 Inhibits β-Amyloid Peptide Production and Alters Lymphopoiesis and Intestinal Cell Differentiation

Wong, G. T., Manfra, D. J., Poulet, F. M., Zhang, Q., Josien, H. B., Bara, T. A., Engstrom, L., Pinzon-Ortiz, M. C., Fine, J. S., Lee, H.-J. J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311652200 · Cited by 723

Green tea Epigallocatechin-3-Gallate (EGCG) Modulates Amyloid Precursor Protein Cleavage and Reduces Cerebral Amyloidosis in Alzheimer Transgenic Mice

Rezai-Zadeh, K., Shytle, D., Sun, N., Mori, T., Hou, H., Jeanniton, D., Ehrhart, J., Townsend, K., Zeng, J., Morgan, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1521-05.2005 · Cited by 713

Control of Peripheral Nerve Myelination by the ß-Secretase BACE1

Willem, M., Garratt, A. N., Novak, B., Citron, M., Kaufmann, S., Rittger, A., DeStrooper, B., Saftig, P., Birchmeier, C., & Haass, C. (2006) · Science · doi:10.1126/science.1132341 · Cited by 703

Apolipoprotein E and Alzheimer disease.

Strittmatter, W. J., & Roses, A. D. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.11.4725 · Cited by 701

Efficacy of rosiglitazone in a genetically defined population with mild-to-moderate Alzheimer’s disease

Risner, M. E., Saunders, A. M., Altman, J. F. B., Ormandy, G. C., Craft, S., Foley, I. M., Zvartau-Hind, M. E., Hosford, D. A., Roses, A. D., & for the Rosiglitazone in Alzheimer's Disease Study Group (2006) · The Pharmacogenomics Journal · doi:10.1038/sj.tpj.6500369 · Cited by 686

The genetic epidemiology of neurodegenerative disease

Bertram, L. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24761 · Cited by 680

P-glycoprotein deficiency at the blood-brain barrier increases amyloid- deposition in an Alzheimer disease mouse model

Cirrito, J. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25247 · Cited by 660

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 658

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641

NSAIDs and enantiomers of flurbiprofen target γ-secretase and lower Aβ42 in vivo

Eriksen, J. L., Sagi, S. A., Smith, T. E., Weggen, S., Das, P., McLendon, D. C., Ozols, V. V., Jessing, K. W., Zavitz, K. H., Koo, E. H., et al. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18162 · Cited by 634

A quantitative morphometric analysis of the neuronal and synaptic content of the frontal and temporal cortex in patients with Alzheimer's disease

Davies, C. A., Mann, D. M. A., Sumpter, P. Q., & Yates, P. O. (1987) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(87)90057-8 · Cited by 628

Human amyloid-β synthesis and clearance rates as measured in cerebrospinal fluid in vivo

Bateman, R. J., Munsell, L. Y., Morris, J. C., Swarm, R., Yarasheski, K. E., & Holtzman, D. M. (2006) · Nature Medicine · doi:10.1038/nm1438 · Cited by 599

Widespread activation of calcium-activated neutral proteinase (calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration.

Saito, K., Elce, J. S., Hamos, J. E., & Nixon, R. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.7.2628 · Cited by 591

Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP

Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A., & Goldstein, L. S. B. (2001) · Nature · doi:10.1038/414643a · Cited by 583

Modulation of Notch Processing by γ-Secretase Inhibitors Causes Intestinal Goblet Cell Metaplasia and Induction of Genes Known to Specify Gut Secretory Lineage Differentiation

Milano, J., McKay, J., Dagenais, C., Foster-Brown, L., Pognan, F., Gadient, R. A., Jacobs, R. T., Zacco, A., Greenberg, B., & Ciaccio, P. J. (2004) · Toxicological Sciences · doi:10.1093/toxsci/kfh254 · Cited by 575

The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging

Wang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567

Brain to Plasma Amyloid-β Efflux: a Measure of Brain Amyloid Burden in a Mouse Model of Alzheimer's Disease

DeMattos, R. B., Bales, K. R., Cummins, D. J., Paul, S. M., & Holtzman, D. M. (2002) · Science · doi:10.1126/science.1067568 · Cited by 563

Cerebral amyloid angiopathy in the brains of patients with Alzheimer's disease: The CERAD experience, part XV

Ellis, R. J., Olichney, J. M., Thal, L. J., Mirra, S. S., Morris, J. C., Beekly, D., & Heyman, A. (1996) · Neurology · doi:10.1212/wnl.46.6.1592 · Cited by 561

Vitamin E and its function in membranes

Wang, X. (1999) · Progress in Lipid Research · doi:10.1016/s0163-7827(99)00008-9 · Cited by 560

Alzheimer's brains harbor somatic mtDNA control-region mutations that suppress mitochondrial transcription and replication

Coskun, P. E., Beal, M. F., & Wallace, D. C. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403649101 · Cited by 556

The Alzheimer's disease Beta-secretase enzyme, BACE1

Cole, S. L., & Vassar, R. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-22 · Cited by 550

Alcohol consumption and risk of dementia: the Rotterdam Study

Ruitenberg, A., Swieten, J. C. V., Witteman, J. C. M., Mehta, K. M., van Duijn, C. M., Albert Hofman, D., & Breteler, M. M. B. (2002) · The Lancet · doi:10.1016/s0140-6736(02)07493-7 · Cited by 549

Take five—BACE and the γ‐secretase quartet conduct Alzheimer's amyloid β‐peptide generation

Haass, C. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600061 · Cited by 547

Notch regulation of lymphocyte development and function

Radtke, F., Wilson, A., Mancini, S. J. C., & MacDonald, H. R. (2004) · Nature Immunology · doi:10.1038/ni1045 · Cited by 539

E PIDEMIOLOGY OF N EURODEGENERATION

Mayeux, R. P. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.043002.094919 · Cited by 531

Contribution of glial cells to the development of amyloid plaques in Alzheimer’s disease

Nagele, R. G., Węgiel, J., Venkataraman, V., Imaki, H., Wang, K.-C., & Wegiel, J. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.01.007 · Cited by 522

Amyloid-β oligomers: their production, toxicity and therapeutic inhibition

Walsh, D. M., Klyubin, I. V., Fadeeva, J. V., Rowan, M. J., & Selkoe, D. J. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300552 · Cited by 507

NSAIDs and Alzheimer disease: Epidemiological, animal model and clinical studies

McGeer, P. L., & McGeer, E. G. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.03.013 · Cited by 498

Electron transport chain defects in Alzheimer's disease brain

Parker, W. D., Parks, J. K., Filley, C. M., & Kleinschmidt-DeMasters, B. K. (1994) · Neurology · doi:10.1212/wnl.44.6.1090 · Cited by 495

The presenilin hypothesis of Alzheimer’s disease: Evidence for a loss-of-function pathogenic mechanism.

Shen, J., & Kelleher, R. J. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608332104 · Cited by 485

Notch–RBP-J signaling is involved in cell fate determination of marginal zone B cells

Tanigaki, K., Han, H., Yamamoto, N., Tashiro, K., Ikegawa, M., Kuroda, K., Suzuki, A., Nakano, T., & Honjo, T. (2002) · Nature Immunology · doi:10.1038/ni793 · Cited by 478

Nicastrin Functions as a γ-Secretase-Substrate Receptor

Shah, S., Lee, S.-F., Tabuchi, K., Hao, Y.-H., Yu, C., LaPlant, Q. C., Ball, H. L., Dann, C. E., Südhof, T. C., & Yu, G. (2005) · Cell · doi:10.1016/j.cell.2005.05.022 · Cited by 470

Intracellular accumulation of β-amyloid1–42 in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer’s disease

Nagele, R. G., D’Andrea, M. R., Anderson, W. J., & Wang, H.-Y. (2002) · Neuroscience · doi:10.1016/s0306-4522(01)00460-2 · Cited by 468

Chaperones increase association of tau protein with microtubules

Dou, F., Netzer, W. J., Tanemura, K., Li, F., Hartl, F. U., Takashima, A., Gouras, G. K., Greengard, P., & Xu, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242720499 · Cited by 462

Neuronal and glial calcium signaling in Alzheimer’s disease

Mattson, M. P., & Chan, S. L. (2003) · Cell Calcium · doi:10.1016/s0143-4160(03)00128-3 · Cited by 459

Effect of dimebon on cognition, activities of daily living, behaviour, and global function in patients with mild-to-moderate Alzheimer's disease: a randomised, double-blind, placebo-controlled study

Doody, R. S., Si, G., Sano, M. C., Thomas, R. G., Aisen, P. S. S., Бачурин, С. О., Seely, L., & Hung, D. S.-Y. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61074-0 · Cited by 458

H. M.’s Medial Temporal Lobe Lesion: Findings from Magnetic Resonance Imaging

Corkin, S., Amaral, D. G., González, R., Johnson, K. A., & Hyman, B. T. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-10-03964.1997 · Cited by 451

Neuroplasticity Failure in Alzheimer's Disease

Mesulam, M.-M. (1999) · Neuron · doi:10.1016/s0896-6273(00)81109-5 · Cited by 449

Clearance of Alzheimer's Aβ Peptide

Tanzi, R. E., Moir, R. D., & Wagner, S. L. (2004) · Neuron · doi:10.1016/j.neuron.2004.08.024 · Cited by 446

Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis

Tennent, G. A., Lovat, L. B., & Pepys, M. B. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4299 · Cited by 438

Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice

Lee, J., Cole, T. B., Palmiter, R. D., Suh, S. W., & Koh, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092034699 · Cited by 432

Alzheimer's disease: the two-hit hypothesis

Zhu, X., Raina, A. K., Perry, G. L., & Smith, M. A. (2004) · The Lancet Neurology · doi:10.1016/s1474-4422(04)00707-0 · Cited by 431

Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses

Mandelkow�, E. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.007 · Cited by 412

The role of cerebral amyloid accumulation in common forms of Alzheimer disease

Gandy, S. (2005) · Journal of Clinical Investigation · doi:10.1172/jci25100 · Cited by 407

CREB and the formation of long-term memory

Yin, J. C. P., & Tully, T. P. (1996) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(96)80082-1 · Cited by 399

Interplay between brain-derived neurotrophic factor and signal transduction modulators in the regulation of the effects of exercise on synaptic-plasticity

Vaynman, S., Ying, Z., & Gomez-Pinilla, F. (2003) · Neuroscience · doi:10.1016/j.neuroscience.2003.08.001 · Cited by 396

In Vivo Assessment of Brain Interstitial Fluid with Microdialysis Reveals Plaque-Associated Changes in Amyloid-β Metabolism and Half-Life

Cirrito, J. R., May, P. C., O'Dell, M. A., Taylor, J. W., Parsadanian, M., Cramer, J. W., Audia, J. E., Nissen, J. S., Bales, K. R., Paul, S. M., et al. (2003) · The Journal of Neuroscience · doi:10.1523/jneurosci.23-26-08844.2003 · Cited by 394

Evidence that the β-Amyloid Plaques of Alzheimer's Disease Represent the Redox-silencing and Entombment of Aβ by Zinc

Cuajungco, M. P., Goldstein, L. E., Nunomura, A., Smith, M. A., Lim, J. T., Atwood, C., Huang, X., Farrag, Y. W., Perry, G. L., & Bush, A. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000165200 · Cited by 392

Longer Forms of Amyloid β Protein: Implications for the Mechanism of Intramembrane Cleavage by γ-Secretase

Qi-Takahara, Y., Morishima-Kawashima, M., Tanimura, Y., Dolios, G., Hirotani, N., Horikoshi, Y., Kametani, F., Maeda, M., Saido, T. C., Wang, R., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1575-04.2005 · Cited by 391

Evidence that neurones accumulating amyloid can undergo lysis to form amyloid plaques in Alzheimer’s disease

D'Andrea, M. R., Nagele, R. G., Wang, H., Peterson, P. A., & Lee, D. H. S. (2001) · Histopathology · doi:10.1046/j.1365-2559.2001.01082.x · Cited by 390

Amyloid Deposition Begins in the Striatum of Presenilin-1 Mutation Carriers from Two Unrelated Pedigrees

Klunk, W. E., Price, J. C., Mathis, C. A., Tsopelas, N. D., Lopresti, B. J., Ziolko, S. K., Bi, W., Hoge, J. A., Cohen, A. D., Ikonomovic, M. D., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0730-07.2007 · Cited by 389

Presenilin: Running with Scissors in the Membrane

Selkoe, D. J., & Wolfe, M. S. (2007) · Cell · doi:10.1016/j.cell.2007.10.012 · Cited by 379

Sequence of Aβ-protein deposition in the human medial temporal lobe

Thal, D. R., Rüb, U., Schultz, C., Sassin, I., Ghebremedhin, E., Del Tredici, K., Braak, E., & Braak, H. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.8.733 · Cited by 370

“Preclinical” AD revisited: Neuropathology of cognitively normal older adults

Schmitt, F. A., Davis, D. G., Wekstein, D. R., Smith, C. D., Ashford, J. W., & Markesbery, W. R. (2000) · Neurology · doi:10.1212/wnl.55.3.370 · Cited by 369

Interferon-γ and Tumor Necrosis Factor-α Regulate Amyloid-β Plaque Deposition and β-Secretase Expression in Swedish Mutant APP Transgenic Mice

Yamamoto, M., Kiyota, T., Horiba, M., Buescher, J. L., Walsh, S. M., Gendelman, H. E., & Ikezu, T. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.060378 · Cited by 367

Aging and Alzheimer's Disease: Lessons From the Nun Study

Snowdon, D. A. (1997) · The Gerontologist · doi:10.1093/geront/37.2.150 · Cited by 367

Role of the Blood-Brain Barrier in the Pathogenesis of Alzheimers Disease

Deane, R., & Zloković, B. V. (2007) · Current Alzheimer Research · doi:10.2174/156720507780362245 · Cited by 365

Somatostatin regulates brain amyloid β peptide Aβ42 through modulation of proteolytic degradation

Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S.-M., Suemoto, T., Higuchi, M., & Saido, T. C. (2005) · Nature Medicine · doi:10.1038/nm1206 · Cited by 364

Cognitive functions of the basal forebrain

Baxter, M. G., & Chiba, A. A. (1999) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(99)80024-5 · Cited by 351

Abnormalities of mitochondrial enzymes in Alzheimer disease

Gibson, G. E., Sheu, K.-F. R., & Blass, J. P. (1998) · Journal of Neural Transmission · doi:10.1007/s007020050099 · Cited by 345

Adipsin, a Biomarker of Gastrointestinal Toxicity Mediated by a Functional γ-Secretase Inhibitor

Searfoss, G. H., Jordan, W. H., Calligaro, D. O., Galbreath, E. J., Schirtzinger, L., Berridge, B. R., Gao, H. T., Higgins, M. A., May, P. C., & Ryan, T. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307757200 · Cited by 336

Clearing amyloid through the blood-brain barrier

Zlokovic, B. V. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02385.x · Cited by 336

Microglia and Alzheimer's disease pathogenesis

Streit, W. J. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20093 · Cited by 335

The neuroscience of remote memory

Squire, L. R., & Bayley, P. J. (2007) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2007.02.006 · Cited by 329

Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice

Bayer, T. A., Schäfer, S., Simons, A., Kemmling, A., Kamer, T., Tepest, R., Eckert, A., Schüssel, K., Eikenberg, O., Sturchler, C., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332818100 · Cited by 329

Sorting through the Cell Biology of Alzheimer's Disease: Intracellular Pathways to Pathogenesis

Small, S. A., & Gandy, S. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.001 · Cited by 328

Dissection of Amyloid-β Precursor Protein-dependent Transcriptional Transactivation

Cao, X., & Südhof, T. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402248200 · Cited by 316

Neprilysin Degrades Both Amyloid β Peptides 1–40 and 1–42 Most Rapidly and Efficiently among Thiorphan- and Phosphoramidon-sensitive Endopeptidases

Shirotani, K., Tsubuki, S., Iwata, N., Takaki, Y., Yamao‐Harigaya, W., Maruyama, K., Kiryu‐Seo, S., Kiyama, H., Iwata, H., Tomita, T., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008511200 · Cited by 312

TMP21 is a presenilin complex component that modulates γ-secretase but not ɛ-secretase activity

Chen, F., Hasegawa, H., Schmitt‐Ulms, G., Kawarai, T., Böhm, C., Katayama, T., Gu, Y., Sanjo, N., Glista, M. J., Rogaeva, E. A., et al. (2006) · Nature · doi:10.1038/nature04667 · Cited by 311

Human neurons generate C-reactive protein and amyloid P: upregulation in Alzheimer’s disease

Yasojima, K., Schwab, C., McGeer, E. G., & McGeer, P. L. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02970-x · Cited by 307

A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage

Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305

Brain Levels of Microtubule‐Associated Protein τ Are Elevated in Alzheimer's Disease: A Radioimmuno‐Slot‐Blot Assay for Nanograms of the Protein

Khatoon, S., Grundke, I., & Iqbal, K. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb09432.x · Cited by 304

Axonal Transport and Alzheimer's Disease

Stokin, G. B., & Goldstein, L. S. B. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142637 · Cited by 296

NOBEL LECTURE: The Molecular Biology of Memory Storage: A Dialog Between Genes and Synapses

Kandel, E. R. (2001) · Bioscience Reports · doi:10.1023/a:1014775008533 · Cited by 292

Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease

Siemers, E., Quinn, J. F., Kaye, J. A., Farlow, M. R., Porsteinsson, A. P., Tariot, P. N., Zoulnouni, P., Galvin, J. E., Holtzman, D. M., Knopman, D. S., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000198762.41312.e1 · Cited by 291

Elucidation of Primary Structure Elements Controlling Early Amyloid β-Protein Oligomerization

Bitan, G., Vollers, S. S., & Teplow, D. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300825200 · Cited by 291

Application of the National Institute on Aging (NIA)-Reagan Institute Criteria for the Neuropathological Diagnosis of Alzheimer Disease

Newell, K. L., Hyman, B. T., Growdon, J. H., & Hedley-Whyte, E. T. (1999) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199911000-00004 · Cited by 289

Amyloid β-induced Changes in Nitric Oxide Production and Mitochondrial Activity Lead to Apoptosis

Keil, U., Bonert, A., Marques, C. A., Scherping, I., Weyermann, J., Strosznajder, J. B., Müller-Spahn, F., Haass, C., Czech, C., Pradier, L., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405600200 · Cited by 287

Ribosomal RNA in Alzheimer Disease Is Oxidized by Bound Redox-active Iron

Honda, K., Smith, M. A., Zhu, X., Baus, D., Merrick, W. C., Tartakoff, A. M., Hattier, T., Harris, P. L., Siedlak, S. L., Fujioka, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500526200 · Cited by 280

Amyloid β42Activates a G-Protein-Coupled Chemoattractant Receptor, FPR-Like-1

Le, Y., Gong, W., Tiffany, H. L., Tumanov, A. V., Nedospasov, S. A., Shen, W., Dunlop, N. M., Gao, J., Murphy, P. M., Oppenheim, J. J., et al. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-02-j0003.2001 · Cited by 278

Ultrastructure of the microglia that phagocytose amyloid and the microglia that produce ?-amyloid fibrils

Frackowiak, J., Wisniewski, H. M., Wegiel, J., Merz, G. S., Iqbal, K., & Wang, K. C. (1992) · Acta Neuropathologica · doi:10.1007/bf00227813 · Cited by 276

Cholesterol and the Biology of Alzheimer's Disease

Wolozin, B. (2004) · Neuron · doi:10.1016/s0896-6273(03)00840-7 · Cited by 275

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies

Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., Moulick, K., Aguirre, J., Wu, N. F., Greengard, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701055104 · Cited by 274

Synaptotrophic effects of human amyloid β protein precursors in the cortex of transgenic mice

Mucke, L., Masliah, E., Johnson, W. B., Ruppe, M. D., Alford, M. F., Rockenstein, E. M., Forss‐Petter, S., Pietropaolo, M., Mallory, M. E., & Abraham, C. R. (1994) · Brain Research · doi:10.1016/0006-8993(94)90767-6 · Cited by 270

Axonal Membrane Proteins Are Transported in Distinct Carriers: A Two-Color Video Microscopy Study in Cultured Hippocampal Neurons

Kaether, C., Skehel, P., & Dotti, C. G. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.4.1213 · Cited by 270

The significance of neuroinflammation in understanding Alzheimer’s disease

Eikelenboom, P., Veerhuis, R., Scheper, W., Rozemüller, A. J. M., van Gool, W. A., & Hoozemans, J. J. M. (2006) · Journal of Neural Transmission · doi:10.1007/s00702-006-0575-6 · Cited by 268

Aβ Species Removal After Aβ 42 Immunization

Nicoll, J. A. R., Barton, E., Boche, D., Neal, J. W., Ferrer, I., Thompson, P., Vlachouli, C., Wilkinson, D., Bayer, A., Games, D., et al. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000240466.10758.ce · Cited by 265

Clinical phenotypic heterogeneity of Alzheimer's disease associated with mutations of the presenilin–1 gene

Larner, A. J., & Doran, M. (2005) · Journal of Neurology · doi:10.1007/s00415-005-0019-5 · Cited by 264

Astrocytes Regulate Microglial Phagocytosis of Senile Plaque Cores of Alzheimer's Disease

DeWitt, D. A., Perry, G., Cohen, M., Doller, C., & Silver, J. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6738 · Cited by 261

Down regulation of trk but not p75NTR gene expression in single cholinergic basal forebrain neurons mark the progression of Alzheimer's disease

Ginsberg, S. D., Che, S., Wuu, J., Counts, S., & Mufson, E. J. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03764.x · Cited by 253

Ferritin is a component of the neuritic (senile) plaque in Alzheimer dementia

Grundke, I., Fleming, J. T., Tung, Y. C., Lassmann, H., Iqbal, K., & Joshi, J. G. (1990) · Acta Neuropathologica · doi:10.1007/bf00334497 · Cited by 253

Calcium homeostasis and reactive oxygen species production in cells transformed by mitochondria from individuals with sporadic Alzheimer's disease

Sheehan, J. P., Swerdlow, R. H., Miller, S. W., Davis, R. E., Parks, J. K., Parker, W. D., & Tuttle, J. B. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-12-04612.1997 · Cited by 249

β-Amyloid-induced Dynamin 1 Degradation Is Mediated by N-Methyl-D-Aspartate Receptors in Hippocampal Neurons

Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 244

Elevation of serum copper levels in Alzheimer’s disease

Squitti, R., Lupoi, D., Pasqualetti, P., Forno, G. D., Vernieri, F., Chiovenda, P., Rossi, L. C., Cortesi, M., Cassetta, E., & Rossini, P. M. (2002) · Neurology · doi:10.1212/wnl.59.8.1153 · Cited by 237

High-resolution Atomic Force Microscopy of Soluble Aβ42 Oligomers

Mastrangelo, I. A., Ahmed, M., Sato, T., Liu, W., Wang, C., Hough, P. V. C., & Smith, S. O. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.01.042 · Cited by 236

Soluble Amyloid Oligomers Increase Bilayer Conductance by Altering Dielectric Structure

Sokolov, Y., Kozak, J. A., Kayed, R., Chanturiya, A., Glabe, C. G., & Hall, J. E. (2006) · The Journal of General Physiology · doi:10.1085/jgp.200609533 · Cited by 232

Common molecular mechanisms in explicit and implicit memory

Barco, Á., Bailey, C. H., & Kandel, E. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03870.x · Cited by 228

Purification and Characterization of the Human γ-Secretase Complex

Fraering, P. C., Ye, W., Strub, J., Dolios, G., LaVoie, M. J., Ostaszewski, B. L., DORSSELAER, A. V., Wang, R., Selkoe, D. J., & Wolfe, M. S. (2004) · Biochemistry · doi:10.1021/bi0494976 · Cited by 227

Structure of a Site-2 Protease Family Intramembrane Metalloprotease

Feng, L., Yan, H., Wu, Z., Yan, N., Wang, Z., Jeffrey, P. D., & Shi, Y. (2007) · Science · doi:10.1126/science.1150755 · Cited by 224

Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease

Nixon, R. A., & Cataldo, A. M. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s331 · Cited by 222

Nerve growth factor in Alzheimer's disease: defective retrograde transport to nucleus basalis

Mufson, E., Conner, J., & Kordower, J. (1995) · NeuroReport · doi:10.1097/00001756-199505090-00028 · Cited by 221

Identification of oxidized histidine generated at the active site of Cu,Zn-superoxide dismutase exposed to H2O2. Selective generation of 2-oxo-histidine at the histidine 118.

Uchida, K., & Kawakishi, S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41960-0 · Cited by 218

Safety, Tolerability, and Changes in Amyloid β Concentrations After Administration of a γ-Secretase Inhibitor in Volunteers

Siemers, E., Skinner, M., Dean, R. A., Gonzales, C., Satterwhite, J. H., Farlow, M. R., NESS, D. K., & May, P. C. (2005) · Clinical Neuropharmacology · doi:10.1097/01.wnf.0000167360.27670.29 · Cited by 215

Rapidly progressing atrophy of medial temporal lobe in Alzheimer's disease

Jobst, K. A., Smith, A. D., Szatmari, M., Esiri, M. M., Jaskowski, A., Hindley, N., McDonald, B., & Molyneux, A. J. (1994) · The Lancet · doi:10.1016/s0140-6736(94)92028-1 · Cited by 215

The Non-Amyloidogenic Pathway: Structure and Function of α-Secretases

Kojro, E., & Fahrenholz, F. (2006) · Springer eBooks · doi:10.1007/0-387-23226-5_5 · Cited by 211

The Cell Adhesion Protein P-selectin Glycoprotein Ligand-1 Is a Substrate for the Aspartyl Protease BACE1

Lichtenthaler, S. F., Dominguez, D.-I., Westmeyer, G. G., Reiss, K., Haass, C., Saftig, P., De Strooper, B., & Seed, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303861200 · Cited by 206

Redox Reactions of Copper Complexes Formed with Different β-Amyloid Peptides and Their Neuropathalogical Relevance

Jiang, D., Men, L., Wang, J., Zhang, Y., Chickenyen, S., Wang, Y., & Zhou, F. (2007) · Biochemistry · doi:10.1021/bi700508n · Cited by 204

Clearance of amyloid-beta in Alzheimer's disease: progress, problems and perspectives

Wang, Y., Zhou, H., & Zhou, X. (2006) · Drug Discovery Today · doi:10.1016/j.drudis.2006.08.004 · Cited by 204

Imaging the progression of Alzheimer pathology through the brain

Smith, A. D. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082107399 · Cited by 202

Amyloid β Protein Starting Pyroglutamate at Position 3 Is a Major Component of the Amyloid Deposits in the Alzheimer's Disease Brain

Harigaya, Y., Saido, T. C., Eckman, C. B., Prada, C.-M., Shoji, M., & Younkin, S. G. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3490 · Cited by 202

Relation between smoking and risk of dementia and Alzheimer disease

Reitz, C., den Heijer, T., van Duijn, C. M., Albert Hofman, D., & Breteler, M. M. B. (2007) · Neurology · doi:10.1212/01.wnl.0000271395.29695.9a · Cited by 200

Nonsteroidal anti-inflammatory drugs lower Aβ42 and change presenilin 1 conformation

Lleó, A., Berezovska, O., Herl, L. D., Raju, S., Deng, A., Bacskai, B. J., Frosch, M. P., Irizarry, M. C., & Hyman, B. T. (2004) · Nature Medicine · doi:10.1038/nm1112 · Cited by 198

Aβ ion channels. Prospects for treating Alzheimer's disease with Aβ channel blockers

Arispe, N. J., Díaz, J. C., & Šimáková, O. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.03.014 · Cited by 196

β-Amyloid Is Different in Normal Aging and in Alzheimer Disease

Piccini, A., Russo, C., Gliozzi, A., Relini, A., Vitali, A., Borghi, R., Giliberto, L., Armirotti, A., D’Arrigo, C., Bachi, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501694200 · Cited by 192

Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study.

Yamaguchi, H., Yamazaki, T., Lemere, C. A., Frosch, M. P., & Selkoe, D. J. (1992) · PubMed Central · Cited by 191

Amyloid-β and τ serve antioxidant functions in the aging and Alzheimer brain

Smith, M. A., Casadesús, G., Joseph, J. A., & Perry, G. L. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01021-3 · Cited by 189

Role of gangliosides in Alzheimer’s disease

Yanagisawa, K. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.01.018 · Cited by 185

Presenilin 2 familial Alzheimer's disease mutations result in partial loss of function and dramatic changes in Aβ 42/40 ratios

Walker, E. S., Martínez, M., Brunkan, A. L., & Goate, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02858.x · Cited by 184

Regulation of Amyloid Protein Precursor (APP) Binding to Collagen and Mapping of the Binding Sites on APP and Collagen Type I

Beher, D., Hesse, L., Masters, C. L., & Multhaup, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1613 · Cited by 183

Rosiglitazone Induces Mitochondrial Biogenesis in Mouse Brain

Strum, J. C., Shehee, R., Virley, D. J., Richardson, J. C., Mattie, M. D., Selley, P., Ghosh, S., Nock, C. M., Saunders, A. M., & Roses, A. D. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11108 · Cited by 183

Transglutaminase activity is increased in Alzheimer's disease brain

Johnson, G. V. W., Cox, T. M., Lockhart, J., ZINNERMAN, M., Miller, M. L., & Powers, R. E. (1997) · Brain Research · doi:10.1016/s0006-8993(96)01431-x · Cited by 182

A Cell Biological Perspective on Alzheimer's Disease

Annaert, W., & De Strooper, B. (2002) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.18.020402.142302 · Cited by 182

Cleavage of Amyloid-β Precursor Protein and Amyloid-β Precursor-like Protein by BACE 1

Li, Q., & Südhof, T. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310001200 · Cited by 180

Amyloid β protein (Aβ) removal by neuroglial cells in culture

Shaffer, L. M., Dority, M. D., Gupta‐Bansal, R., Frederickson, R. C. A., Younkin, S. G., & Brunden, K. R. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00055-j · Cited by 180

Selected Non-steroidal Anti-inflammatory Drugs and Their Derivatives Target γ-Secretase at a Novel Site

Beher, D., Clarke, E. E., Wrigley, J. D. J., Martin, A. C. L., Nadin, A. J., Churcher, I., & Shearman, M. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404937200 · Cited by 179

Therapeutic actions of insulin-like growth factor I on APP/PS2 mice with severe brain amyloidosis

Carro, E., Trejo, J. L., Gerber, A., Loetscher, H., Torrado, J. J., Metzger, F., & Torres‐Alemán, I. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.06.015 · Cited by 179

Isolation, Chemical Characterization, and Quantitation of Aβ 3-Pyroglutamyl Peptide from Neuritic Plaques and Vascular Amyloid Deposits

Kuo, Y.-M., Emmerling, M. R., Woods, A. S., Cotter, R. J., & Roher, A. E. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7083 · Cited by 178

Neuronal and microglial involvement in beta-amyloid protein deposition in Alzheimer's disease.

Cras, P. P., Kawai, M., Siedlak, S. L., Mulvihill, P., Gambetti, P. L., Lowery, D. E., Gonzalez‐DeWhitt, P. A., Greenberg, B., & Perry, G. L. (1990) · Europe PMC (PubMed Central) · Cited by 174

Peroxisome Proliferator-Activated Receptor γ Induces a Clearance Mechanism for the Amyloid-β Peptide

Espuny-Camacho, I., Serneels, L., Spittaels, K., Merchiers, P., Dominguez, D. I., & Strooper, B. D. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3987-04.2004 · Cited by 171

Ultrastructural morphology of amyloid fibrils from neuritic and amyloid plaques

MERZ, P. A., Wı́sniewski, H. M., Somerville, R. A., Bobin, S. A., Masters, C. L., & Iqbal, K. (1983) · Acta Neuropathologica · doi:10.1007/bf00685355 · Cited by 171

Exercise intensity influences the temporal profile of growth factors involved in neuronal plasticity following focal ischemia.

Ploughman, M., Granter-Button, S., Chernenko, G., Attwood, Z., Tucker, B. A., Mearow, K. M., & Corbett, D. (2007) · Brain Research · doi:10.1016/j.brainres.2007.02.065 · Cited by 170

Orally available compound prevents deficits in memory caused by the Alzheimer amyloid‐β oligomers

Townsend, M., Cleary, J. P., Mehta, T., Hofmeister, J. J., Lesné, S., O‘Hare, E., Walsh, D. M., & Selkoe, D. J. (2006) · Annals of Neurology · doi:10.1002/ana.21051 · Cited by 169

Oxidative stress and the amyloid beta peptide in Alzheimer’s disease

Cheignon, C., Tomas, M., Bonnefont-Rousselot, D., Faller, P., Hureau, C., & Collin, F. (2018) · Redox Biology · doi:10.1016/j.redox.2017.10.014 · Cited by 2,185

Compromised MAPK signaling in human diseases: an update

Kim, E., & Choi, E. (2015) · Archives of Toxicology · doi:10.1007/s00204-015-1472-2 · Cited by 1,033

Bioinorganic Chemistry of Alzheimer’s Disease

Kepp, K. P. (2012) · Chemical Reviews · doi:10.1021/cr300009x · Cited by 683

Mitochondria-Targeting Ceria Nanoparticles as Antioxidants for Alzheimer’s Disease

Kwon, H. J., Cha, M.-Y., Kim, D., Kim, D., Soh, M., Shin, K., Hyeon, T., & Mook‐Jung, I. (2016) · ACS Nano · doi:10.1021/acsnano.5b08045 · Cited by 667

New Horizons for Diagnostics and Therapeutic Applications of Graphene and Graphene Oxide

Feng, L., Wu, L. J., & Qu, X. (2012) · Advanced Materials · doi:10.1002/adma.201203229 · Cited by 634

Die Alzheimer‐Demenz: von der Pathologie zu therapeutischen Ansätzen

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie · doi:10.1002/ange.200802808 · Cited by 41

The Role and Therapeutic Targeting of α-, β- and γ-Secretase in Alzheimer's Disease

MacLeod, R., Hillert, E., Cameron, R. T., & Baillie, G. S. (2015) · Future Science OA · doi:10.4155/fso.15.9 · Cited by 136

Progress towards testing the amyloid hypothesis: inhibitors of APP processing.

Olson, R. E., Copeland, R. A., & Seiffert, D. (2001) · PubMed · Cited by 20

β-Amyloid therapies in Alzheimer’s disease

Jhee, S. S., Shiovitz, T. M., Crawford, A. W., & Cutler, N. R. (2001) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.10.4.593 · Cited by 25

Views on Amyloid Hypothesis and Secretase Inhibitors for Treating Alzheimers Disease: Progress and Problems

Nguyen, J., Yamani, A., & Kiso, Y. (2006) · Current Pharmaceutical Design · doi:10.2174/138161206778792976 · Cited by 36