Intracellular amyloid-β in Alzheimer's disease

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404

Amyloid plaque core protein in Alzheimer disease and Down syndrome.

Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431

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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

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

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676

Selective impairment of learning and blockade of long-term potentiation by an N-methyl-D-aspartate receptor antagonist, AP5

Morris, R. G. M., Anderson, E., Lynch, G. S., & Baudry, M. (1986) · Nature · doi:10.1038/319774a0 · Cited by 3,640

Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation

Oakley, H., Cole, S. L., Logan, S., Maus, E., Shao, P., Craft, J., Guillozet-Bongaarts, A., Ohno, M., Disterhoft, J., Van Eldik, L., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1202-06.2006 · Cited by 3,530

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

Oxidative stress hypothesis in Alzheimer’s disease

Markesbery, W. R. (1997) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(96)00629-6 · Cited by 2,383

Memantine in Moderate-to-Severe Alzheimer's Disease

Reisberg, B., Doody, R., Stöffler, A., Schmitt, F., Ferris, S., & Möbius, H. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa013128 · Cited by 2,043

The carboxy terminus of the .beta. amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease

Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022

RAGE and amyloid-β peptide neurotoxicity in Alzheimer's disease

Yan, S. D., Chen, X., Fu, J., Chen, M., Zhu, H., Roher, A., Slattery, T., Zhao, L., Nagashima, M., Morser, J., et al. (1996) · Nature · doi:10.1038/382685a0 · Cited by 2,012

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

An Immunohistochemical Study

Isaacson, P. G., Doǧan, A., Price, S. K., & Spencer, J. (1989) · The American Journal of Surgical Pathology · doi:10.1097/00000478-198912000-00004 · Cited by 1,913

Natural oligomers of the amyloid-β protein specifically disrupt cognitive function

Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722

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

Mutant presenilins specifically elevate the levels of the 42 residue β-amyloid peptide in vivo: evidence for augmentation of a 42-specific γ secretase

Jankowsky, J. L., Fadale, D. J., Anderson, J., Xu, G. M., Gonzales, V., Jenkins, N. A., Copeland, N. G., Lee, M. K., Younkin, L. H., Wagner, S. L., et al. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh019 · Cited by 1,575

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

Uber eine eigenartige Erkrankung der Hirnrinde

Alzheimer, A. (1907) · Medical Entomology and Zoology · Cited by 1,503

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,491

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

RAGE mediates amyloid-β peptide transport across the blood-brain barrier and accumulation in brain

Deane, R., Du Yan, S., Submamaryan, R. K., LaRue, B., Jovanovic, S., Hogg, E., Welch, D., Manness, L., Lin, C., Yu, J., et al. (2003) · Nature Medicine · doi:10.1038/nm890 · Cited by 1,426

Intraneuronal Aβ Causes the Onset of Early Alzheimer’s Disease-Related Cognitive Deficits in Transgenic Mice

Billings, L. M., Oddo, S., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.01.040 · Cited by 1,294

Untitled work

Wyss-Coray (2006) · doi:10.1038/nm1484 · Cited by 1,284

APP locus duplication causes autosomal dominant early-onset Alzheimer disease with cerebral amyloid angiopathy

Rovelet‐Lecrux, A., Hannequin, D., Raux, G., Meur, N. L., Laquerrière, A., Vital, A., Dumanchin‐Njock, C., Feuillette, S., Brice, A., Vercelletto, M., et al. (2005) · Nature Genetics · doi:10.1038/ng1718 · Cited by 1,284

The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation

Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209

The neuronal sortilin-related receptor SORL1 is genetically associated with Alzheimer disease

Rogaeva, E., Meng, Y., Lee, J. H., Gu, Y., Kawarai, T., Zou, F., Katayama, T., Baldwin, C. T., Cheng, R., Hasegawa, H., et al. (2007) · Nature Genetics · doi:10.1038/ng1943 · Cited by 1,167

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134

Mitochondria are a direct site of Aβ accumulation in Alzheimer's disease neurons: implications for free radical generation and oxidative damage in disease progression

Manczak, M., Anekonda, T. S., Henson, E., Park, B. S., Quinn, J., & Reddy, P. H. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl066 · 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

Intraneuronal Aβ42 Accumulation in Human Brain

Gouras, G. K., Tsai, J., Naslund, J., Vincent, B., Edgar, M., Checler, F., Greenfield, J. P., Haroutunian, V., Buxbaum, J. D., Xu, H., et al. (2000) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64700-1 · Cited by 991

Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing

Yu, G., Nishimura, M., Arawaka, S., Levitan, D. J., Zhang, L., Tandon, A., Song, Y., Rogaeva, E. A., Chen, F., Kawarai, T., et al. (2000) · Nature · doi:10.1038/35024009 · Cited by 929

Evidence that production and release of amyloid beta-protein involves the endocytic pathway

Koo, E. H., & Squazzo, S. L. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32449-3 · Cited by 829

β-Amyloid1–42 Binds to α7 Nicotinic Acetylcholine Receptor with High Affinity

Wang, H.-Y., Lee, D. H. S., D’Andrea, M. R., Peterson, P. A., Shank, R. P., & Reitz, A. B. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.8.5626 · Cited by 818

aph-1 and pen-2 Are Required for Notch Pathway Signaling, γ-Secretase Cleavage of βAPP, and Presenilin Protein Accumulation

Francis, R., McGrath, G., Zhang, J., Ruddy, D. A., Sym, M., Apfeld, J., Nicoll, M., Maxwell, M., Hai, B., Ellis, M. C., et al. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00189-2 · Cited by 805

Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.003 · Cited by 780

Mitochondrial Aβ: a potential focal point for neuronal metabolic dysfunction in Alzheimer's disease

Caspersen, C., Wang, N., Yao, J., Sosunov, A., Chen, X., Lustbader, J. W., Xu, H. W., Stern, D., McKhann, G., & Du Yan, S. (2005) · The FASEB Journal · doi:10.1096/fj.05-3735fje · Cited by 738

Processing of the Amyloid Protein Precursor to Potentially Amyloidogenic Derivatives

Golde, T. E., Estus, S., Younkin, L. H., Selkoe, D. J., & Younkin, S. G. (1992) · Science · doi:10.1126/science.1738847 · Cited by 737

Distinct sites of intracellular production for Alzheimer's disease Aβ40/42 amyloid peptides

Hartmann, T., Bieger, S. C., Brühl, B., Tienari, P. J., Ida, N., Allsop, D., Roberts, G. W., Masters, C. L., Dotti, C. G., Unsicker, K., et al. (1997) · Nature Medicine · doi:10.1038/nm0997-1016 · Cited by 719

Intraneuronal Alzheimer Aβ42 Accumulates in Multivesicular Bodies and Is Associated with Synaptic Pathology

Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706

A Diet Enriched with the Omega-3 Fatty Acid Docosahexaenoic Acid Reduces Amyloid Burden in an Aged Alzheimer Mouse Model

Lim, G. P., Calon, F., Morihara, T., Yang, F., Teter, B., Ubeda, O. J., Salem, N., Frautschy, S. A., & Cole, G. M. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4225-04.2005 · Cited by 697

Glucocorticoids increase amyloid-β and tau pathology in a mouse model of alzheimer’s disease

Green, K. N., Billings, L. M., Roozendaal, B., McGaugh, J. L., & LaFerla, F. M. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.2797-06.2006 · Cited by 623

The Swedish mutation causes early-onset Alzheimer's disease by β-secretase cleavage within the secretory pathway

Haass, C., Lemere, C. A., Capell, A., Citron, M., Seubert, P., Schenk, D., Lannfelt, L., & Selkoe, D. J. (1995) · Nature Medicine · doi:10.1038/nm1295-1291 · Cited by 592

Generation of beta-amyloid in the secretory pathway in neuronal and nonneuronal cells.

Busciglio, J., Gabuzda, D. H., Matsudaira, P., & Yankner, B. A. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.2092 · Cited by 569

Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1

Ihara, Y., Nukina, N., Miura, R., & OGAWARA, M. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135662 · Cited by 527

Stimulation of β-Amyloid Precursor Protein Trafficking by Insulin Reduces Intraneuronal β-Amyloid and Requires Mitogen-Activated Protein Kinase Signaling

Gasparini, L., Gouras, G. K., Wang, R., Gross, R. S., Beal, M. F., Greengard, P., & Xu, H. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-08-02561.2001 · Cited by 492

Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice

Guo, Q., Fu, W., Sopher, B. L., Miller, M. W., Ware, C. B., Martin, G. M., & Mattson, M. P. (1999) · Nature Medicine · doi:10.1038/4789 · Cited by 489

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

beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms.

Haass, C., Hung, A. Y., Schlossmacher, M. G., Teplow, D. B., & Selkoe, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53650-4 · Cited by 465

Oligomerization of Alzheimer's β-Amyloid within Processes and Synapses of Cultured Neurons and Brain

Takahashi, R. H., Almeida, C. G., Kearney, P. F., Yu, F., Lin, M. T., Milner, T. A., & Gouras, G. K. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5167-03.2004 · Cited by 445

Alzheimer's Aβ(1–42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells

Cook, D. G., Forman, M. S., Sung, J. C., Leight, S., Kolson, D. L., Iwatsubo, T., Lee, V. M.-Y., & Doms, R. W. (1997) · Nature Medicine · doi:10.1038/nm0997-1021 · Cited by 444

Induction of Alzheimer-like β-Amyloid Immunoreactivity in the Brains of Rabbits with Dietary Cholesterol

Sparks, D. L., Scheff, S. W., Hunsaker, J. C., Liu, H., Landers, T., & Gross, D. R. (1994) · Experimental Neurology · doi:10.1006/exnr.1994.1044 · Cited by 443

ADAMs family members as amyloid precursor protein α‐secretases

Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10737 · Cited by 441

Amyloid-β peptide–Receptor for Advanced Glycation Endproduct interaction elicits neuronal expression of macrophage-colony stimulating factor: A proinflammatory pathway in Alzheimer disease

Yan, S. D., Zhu, H., Fu, J., Yan, S. F., Roher, A. E., Tourtellotte, W. W., Rajavashisth, T. B., Chen, X., Godman, G. C., Stern, D. M., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.10.5296 · Cited by 429

Ubiquitin Hydrolase Uch-L1 Rescues β-Amyloid-Induced Decreases in Synaptic Function and Contextual Memory

Gong, B., Cao, Z., Zheng, P., Vitolo, O. V., Liu, S., Staniszewski, A., Moolman, D. L., Zhang, H., Shelanski, M. L., & Arancio, O. (2006) · Cell · doi:10.1016/j.cell.2006.06.046 · Cited by 425

Abnormal phosphorylation of the microtubule-associated protein? (tau) in Alzheimer cytoskeletal pathology

Grundke, I., Iqbal, K., Tung, Y.-C., Quinlan, M., Wisniewski, H., & Binder, L. (1987) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198701030-00020 · Cited by 410

The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain

Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 401

Massive CA1/2 Neuronal Loss with Intraneuronal and N-Terminal Truncated Aβ42 Accumulation in a Novel Alzheimer Transgenic Model

Casas, C., Sergeant, N., Itier, J.-M., Blanchard, V., Wirths, O., van der Kolk, N., Vingtdeux, V., van de Steeg, E., Ret, G., Canton, T., et al. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63388-3 · Cited by 400

A detergent-insoluble membrance compartment contains Aβ in vivo

Lee, S., Liyanage, U. K., Bickel, P. E., Xia, W., Lansbury, P. T., & Kosik, K. S. (1998) · Nature Medicine · doi:10.1038/nm0698-730 · Cited by 395

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

Mutagenesis Identifies New Signals for β-Amyloid Precursor Protein Endocytosis, Turnover, and the Generation of Secreted Fragments, Including Aβ42

Perez, R. G., Soriano, S., Hayes, J. D., Ostaszewski, B. L., Xia, W., Selkoe, D. J., Chen, X., Stokin, G. B., & Koo, E. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.27.18851 · Cited by 387

Aβ inhibits the proteasome and enhances amyloid and tau accumulation

Tseng, B. P., Green, K. N., Chan, J. L., Blurton-Jones, M., & LaFerla, F. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.014 · Cited by 384

Temporal Profile of Amyloid-β (Aβ) Oligomerization in an in Vivo Model of Alzheimer Disease

Oddo, S., Caccamo, A., Tran, L., Lambert, M. P., Glabe, C. G., Klein, W. L., & LaFerla, F. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m507892200 · Cited by 379

Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation

Chui, D.-H., Tanahashi, H., Ozawa, K., Ikeda, S., Checler, F., Ueda, O., Suzuki, H., Araki, W., Inoue, H., Shirotani, K., et al. (1999) · Nature Medicine · doi:10.1038/8438 · Cited by 364

Phenotype associated with APP duplication in five families

Cabrejo, L., Guyant‐Maréchal, L., Laquerrière, A., Vercelletto, M., Fournière, F. D. L., Thomas-Antérion, C., Verny, C., Letournel, F., Pasquier, F., Vital, A., et al. (2006) · Brain · doi:10.1093/brain/awl237 · Cited by 351

Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease

Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338

Intraneuronal Aβ accumulation precedes plaque formation in β-amyloid precursor protein and presenilin-1 double-transgenic mice

Wirths, O., Multhaup, G., Czech, C., Blanchard, V., Moussaoui, S., Tremp, G., Pradier, L., Beyreuther, K., & Bayer, T. A. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)01876-6 · Cited by 336

Dietary Docosahexaenoic Acid and Docosapentaenoic Acid Ameliorate Amyloid-β and Tau Pathology via a Mechanism Involving Presenilin 1 Levels

Green, K. N., Martínez‐Coria, H., Khashwji, H., Hall, E. B., Yurko‐Mauro, K., Ellis, L., & LaFerla, F. M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0055-07.2007 · Cited by 336

Dimeric Amyloid β Protein Rapidly Accumulates in Lipid Rafts followed by Apolipoprotein E and Phosphorylated Tau Accumulation in the Tg2576 Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Shoji, M., Younkin, L. H., Wen-Lang, L., Dickson, D. W., Murakami, T., Matsubara, E., Abe, K., Ashe, K. H., & Younkin, S. G. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.5543-03.2004 · Cited by 320

β-Amyloid Accumulation Impairs Multivesicular Body Sorting by Inhibiting the Ubiquitin-Proteasome System

Almeida, C. G., Takahashi, R. H., & Gouras, G. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5078-05.2006 · Cited by 316

Oxidative Stress Induces Intracellular Accumulation of Amyloid β-Protein (Aβ) in Human Neuroblastoma Cells

Misonou, H., Morishima-Kawashima, M., & Ihara, Y. (2000) · Biochemistry · doi:10.1021/bi000169p · Cited by 304

Intracellular Generation and Accumulation of Amyloid β-Peptide Terminating at Amino Acid 42

Wild-Bode, C., Yamazaki, T., Capell, A., Leimer, U., Steiner, H., Ihara, Y., & Haass, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16085 · Cited by 303

Detection of a Novel Intraneuronal Pool of Insoluble Amyloid β Protein that Accumulates with Time in Culture

Skovronsky, D. M., Doms, R. W., & Lee, V. M.-Y. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1031 · Cited by 290

Chronic Administration of Docosahexaenoic Acid Ameliorates the Impairment of Spatial Cognition Learning Ability in Amyloid β–Infused Rats

Hashimoto, M., Tanabe, Y., Fujii, Y., Kikuta, T., Shibata, H., & Shido, O. (2005) · The Journal of Nutrition · doi:10.1093/jn/135.3.549 · Cited by 288

Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes

Kinoshita, A., Fukumoto, H., Shah, T., Whelan, C. M., Irizarry, M. C., & Hyman, B. T. (2003) · Journal of Cell Science · doi:10.1242/jcs.00643 · Cited by 284

The role of Aβ42 in Alzheimer's disease

Younkin, S. G. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80035-1 · Cited by 282

PEN-2 Is an Integral Component of the γ-Secretase Complex Required for Coordinated Expression of Presenilin and Nicastrin

Steiner, H., Winkler, E., Edbauer, D., Prokop, S., Basset, G., Yamasaki, A., Kostka, M., & Haass, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200469200 · Cited by 281

A Dynamic Relationship between Intracellular and Extracellular Pools of Aβ

Oddo, S., Caccamo, A., Smith, I. F., Green, K. N., & LaFerla, F. M. (2006) · The American Journal of Pathology · doi:10.2353/ajpath.2006.050593 · Cited by 261

The Arctic Alzheimer mutation facilitates early intraneuronal Aβ aggregation and senile plaque formation in transgenic mice

Lord, A., Kalimo, H., Eckman, C., Zhang, X.-Q., Lannfelt, L., & Nilsson, L. N. G. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.12.007 · Cited by 260

Intracellular Aβ and cognitive deficits precede β-amyloid deposition in transgenic arcAβ mice

Knobloch, M., Konietzko, U., Krebs, D. C., & Nitsch, R. M. (2007) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.06.019 · Cited by 259

Nicastrin, Presenilin, APH-1, and PEN-2 Form Active γ-Secretase Complexes in Mitochondria

Hansson, C. A., Frykman, S., Farmery, M. R., Tjernberg, L. O., Nilsberth, C., Pursglove, S. E., Ito, A., Winblad, B., Cowburn, R. F., Thyberg, J., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404500200 · Cited by 256

Intraneuronal Aβ42 accumulation in Down syndrome brain: Original Articles

Mori, C., Spooner, E. T., Wisniewski, K. E., Wisniewski, T. M., Yamaguchi, H., Saido, T. C., Tolan, D. R., Selkoe, D. J., & Lemere, C. A. (2002) · Amyloid · doi:10.3109/13506120208995241 · Cited by 255

Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer’s disease

Sasaki, N., Toki, S., Chowei, H., Saito, T., Nakano, N., Hayashi, Y., Takeuchi, M., & Makita, Z. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03075-4 · Cited by 253

Beta amyloid precursor protein mediates neuronal cell‐cell and cell‐surface adhesion

Breen, K. C., Bruce, M. T., & Anderton, B. H. (1991) · Journal of Neuroscience Research · doi:10.1002/jnr.490280109 · Cited by 249

Intraneuronal Aβ-Amyloid Precedes Development of Amyloid Plaques in Down Syndrome

Gyure, K. A., Durham, R., Stewart, W. F., Smialek, J. E., & Troncoso, J. C. (2001) · Archives of Pathology & Laboratory Medicine · doi:10.5858/2001-125-0489-iaapdo · Cited by 248

Amyloid β-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro

Gregori, L. L., Fuchs, C., Figueiredo‐Pereira, M. E., Nostrand, W. E. V., & Goldgaber, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19702 · Cited by 239

The Alzheimer Amyloid Precursor Protein (APP) and Fe65, an APP-Binding Protein, Regulate Cell Movement

Sabo, S. L., Ikin, A. F., Buxbaum, J. D., & Greengard, P. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.7.1403 · Cited by 237

Human neurons derived from a teratocarcinoma cell line express solely the 695-amino acid amyloid precursor protein and produce intracellular beta-amyloid or A4 peptides.

Wertkin, A. M., Turner, R. S., Pleasure, S. J., Golde, T. E., Younkin, S. G., Trojanowski, J. Q., & Lee, V. M. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9513 · Cited by 231

Inflammation, anti-inflammatory agents and Alzheimer disease: The last 12 years

McGeer, P. L., Rogers, J., & McGeer, E. G. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s330 · Cited by 222

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

Chronic nicotine administration exacerbates tau pathology in a transgenic model of Alzheimer's disease

Oddo, S., Caccamo, A., Green, K. N., Liang, K., Tran, L., Chen, Y., Leslie, F. M., & LaFerla, F. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408500102 · Cited by 211

Molecular biology and genetics of Alzheimer's disease

George‐Hyslop, P. S., & Petit-Paitel, A. (2005) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2004.10.013 · Cited by 208

Amyloid Filaments in Inclusion Body Myositis

Mendell, J. R. (1991) · Archives of Neurology · doi:10.1001/archneur.1991.00530240033013 · Cited by 206

p25/Cyclin-Dependent Kinase 5 Induces Production and Intraneuronal Accumulation of Amyloid βIn Vivo

Cruz, J. C., Kim, D., Moy, L. Y., Dobbin, M. M., Sun, X., Bronson, R. T., & Tsai, L. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.3133-06.2006 · Cited by 197

Pathways by Which Aβ Facilitates Tau Pathology

Blurton-Jones, M. M., & LaFerla, F. M. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025242 · Cited by 195

β-Amyloid accumulation in aged canine brain: A model of early plaque formation in Alzheimer's disease

Cummings, B. J., Su, J. H., Cotman, C. W., White, R. G., & Russell, M. J. (1993) · Neurobiology of Aging · doi:10.1016/0197-4580(93)90038-d · Cited by 193

Memantine Improves Spatial Learning in a Transgenic Mouse Model of Alzheimer’s Disease

Minkeviciene, R., Banerjee, P., & Tanila, H. (2004) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.071027 · Cited by 187

Synaptic pathology and glial responses to neuronal injury precede the formation of senile plaques and amyloid deposits in the aging cerebral cortex.

(1994) · PubMed Central · Cited by 169

Untitled work

Askanas (2006) · doi:10.1212/01.wnl.0000192128.13875.1e · Cited by 168

Regulated Formation of Golgi Secretory Vesicles Containing Alzheimer β-Amyloid Precursor Protein

Xu, H., Greengard, P., & Gandy, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.40.23243 · Cited by 168

Amyloid peptide attenuates the proteasome activity in neuronal cells

Oh, S., Hong, H., Hwang, E., Sim, H. J., Lee, W., Shin, S. J., & Mook‐Jung, I. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.07.006 · Cited by 166

Neuronal cell death in Alzheimer's disease correlates with apoE uptake and intracellular Abeta stabilization.

LaFerla, F. M., Troncoso, J. C., Strickland, D. K., Kawas, C. H., & Jay, G. D. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119536 · Cited by 165

Subcellular Topography of Neuronal Aβ Peptide in APPxPS1 Transgenic Mice

Langui, D., Girardot, N., El Hachimi, K. H., Allinquant, B., Blanchard, V., Pradier, L., & Duyckaerts, C. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63405-0 · Cited by 165

Learning Decreases Aβ*56 and Tau Pathology and Ameliorates Behavioral Decline in 3xTg-AD Mice

Billings, L. M., Green, K. N., McGaugh, J. L., & LaFerla, F. M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.4800-06.2007 · Cited by 145

Amyloid protein and neurofibrillary tangles coexist in the same neuron in Alzheimer disease.

Grundke, I., Iqbal, K., George, L., Tung, Y. C., Kim, K. S., & Wisniewski, H. M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.8.2853 · Cited by 142

LRP in Amyloid‐β Production and Metabolism

Bu, G., Cam, J. A., & Zerbinatti, C. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1377.005 · Cited by 141

Aβ peptides can enter the brain through a defective blood–brain barrier and bind selectively to neurons

Clifford, P. M., Zarrabi, S., Siu, G., Kinsler, K., Kosciuk, M. C., Venkataraman, V., D’Andrea, M. R., Dinsmore, S. T., & Nagele, R. G. (2007) · Brain Research · doi:10.1016/j.brainres.2007.01.070 · Cited by 136

Apolipoprotein E and Low Density Lipoprotein Receptor-related Protein Facilitate Intraneuronal Aβ42 Accumulation in Amyloid Model Mice

Zerbinatti, C. V., Wahrle, S. E., Kim, H., Cam, J. A., Bales, K., Paul, S. M., Holtzman, D. M., & Bu, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m604436200 · Cited by 129

GM1 ganglioside-mediated accumulation of amyloid β-protein on cell membranes

Wakabayashi, M., Okada, T., Kozutsumi, Y., & Matsuzaki, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.060 · Cited by 125

Amyloid β oligomerization is induced by brain lipid rafts

Kim, S., Yi, J.-S., & Ko, Y. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20978 · Cited by 121

Amyloid beta protein is internalized selectively by hippocampal field CA1 and causes neurons to accumulate amyloidogenic carboxyterminal fragments of the amyloid precursor protein.

Bahr, B. A., Hoffman, K. B., Yang, A. J., Hess, U. S., Glabe, C. G., & LYNCH, G. S. (1998) · PubMed · Cited by 116

Intraneuronal β-Amyloid Expression Downregulates the Akt Survival Pathway and Blunts the Stress Response

Magrané, J., Rosen, K. M., Smith, R. C., Walsh, K. X., Gouras, G. K., & Querfurth, H. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.1723-05.2005 · Cited by 115

Enhanced detection of Congo‐red‐positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique

Askanas, V., Engel, W. K., & Alvarez, R. B. (1993) · Neurology · doi:10.1212/wnl.43.6.1265-a · Cited by 112

Role of Formyl Peptide Receptor–Like 1 (FPRL1/FPR2) in Mononuclear Phagocyte Responses in Alzheimer Disease

Iribarren, P., Zhou, Y., Hu, J., Le, Y., & Wang, J. M. (2005) · Immunologic Research · doi:10.1385/ir:31:3:165 · Cited by 108

β Amyloid peptide (Aβ 42 ) is internalized via the G‐protein‐coupled receptor FPRL1 and forms fibrillar aggregates in macrophages 1

YAZAWA, H., YU, Z.-X., TAKEDA, K., LE, Y., GONG, W., FERRANS, V. J., OPPENHEIM, J. J., LI, C. C. H., & WANG, J. M. (2001) · The FASEB Journal · doi:10.1096/fj.01-0251com · Cited by 105

Altered mitogen-activated protein kinase signaling, tau hyperphosphorylation and mild spatial learning dysfunction in transgenic rats expressing the β-amyloid peptide intracellularly in hippocampal and cortical neurons

Echeverrı́a, V., Ducatenzeiler, A., Dowd, E., Jänne, J., Grant, S. M., Szyf, M., Wandosell, F. G., Ávila, J., Grimm, H. S., Dunnett, S. B., et al. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2004.07.036 · Cited by 104

Intracellular Accumulation of β-Amyloid in Cells Expressing the Swedish Mutant Amyloid Precursor Protein

Martin, B. L., Schrader‐Fischer, G., Busciglio, J. A., Duke, M., Paganetti, P., & Yankner, B. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.45.26727 · Cited by 104

Inclusion body myositis-like phenotype induced by transgenic overexpression of βAPP in skeletal muscle

Sugarman, M. C., Yamasaki, T. R., Oddo, S., Echegoyen, J. C., Murphy, M. P., Golde, T. E., Jannatipour, M., Leissring, M. A., & LaFerla, F. M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082545599 · Cited by 104

Microtubule-associated protein tau (? ) is a major antigenic component of paired helical filaments in Alzheimer disease

Kosik, K. S., Joachim, C., & Selkoe, D. J. (1987) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-198701030-00022 · Cited by 100

Cellular Membrane Composition Defines Aβ-Lipid Interactions

Waschuk, S. A., Elton, E. A., Darabie, A. A., Fraser, P. E., & McLaurin, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103598200 · Cited by 98

Uptake and pathogenic effects of amyloid beta peptide 1–42 are enhanced by integrin antagonists and blocked by NMDA receptor antagonists

Bi, X., Gall, C. M., Zhou, J., & Lynch, G. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00132-x · Cited by 92

The Evolution of Aβ Peptide Burden in the APP23 Transgenic Mice: Implications for Aβ Deposition in Alzheimer Disease

Kuo, Y.-M., Beach, T. G., Sue, L. I., Scott, S., Layne, K. J., Kokjohn, T. A., Kalback, W. M., Luehrs, D. C., Vishnivetskaya, T. A., Abramowski, D., et al. (2001) · Molecular Medicine · doi:10.1007/bf03401867 · Cited by 90

The Low Density Lipoprotein Receptor-related Protein 1B Retains β-Amyloid Precursor Protein at the Cell Surface and Reduces Amyloid-β Peptide Production

Cam, J. A., Zerbinatti, C. V., Knisely, J. M., Hecimovic, S., Li, Y., & Bu, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313893200 · Cited by 89

Intraneuronal Aβ immunoreactivity is not a predictor of brain amyloidosis-β or neurofibrillary degeneration

Węgiel, J., Kuchna, I., Nowicki, K., Frackowiak, J., Mazur‐Kolecka, B., Imaki, H., Wegiel, J., Mehta, P. D., Silverman, W. P., Reisberg, ‌., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-006-0191-4 · Cited by 89

Aβ42-positive non-pyramidal neurons around amyloid plaques in Alzheimer's disease

Mochizuki, A., Tamaoka, A., Shimohata, A., Komatsuzaki, Y., & Shoji, S. (2000) · The Lancet · doi:10.1016/s0140-6736(99)04937-5 · Cited by 85

β-amyloid precursor protein mRNA is increased in inclusion-body myositis muscle

Sarkozi, E., Askanas, V., Johnson, S. A., Engel, W. K., & Alvarez, R. B. (1993) · Neuroreport · doi:10.1097/00001756-199306000-00055 · Cited by 85

PS1 N- and C-terminal fragments form a complex that functions in APP processing and Notch signaling

Levitan, D. J., Lee, J., Song, L., Manning, R., Wong, G., Parker, E. M., & Zhang, L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211321898 · Cited by 85

Inhibitors of amyloid β-protein aggregation mediated by GM1-containing raft-like membranes

Matsuzaki, K., Noguch, T., Wakabayashi, M., Ikeda, K., Okada, T., Ohashi, Y., Hoshino, M., & Naiki, H. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.09.014 · Cited by 82

Accelerated Aβ aggregation in the presence of GM1‐ganglioside‐accumulated synaptosomes of aged apoE4‐knock‐in mouse brain

Yamamoto, N., Igbabvoa, U., Shimada, Y., Ohno‐Iwashita, Y., Kobayashi, M., Wood, W. G., Fujita, S. C., & Yanagisawa, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.05.037 · Cited by 79

GRK5 deficiency leads to early Alzheimer-like pathology and working memory impairment

Suo, Z., Cox, A., Bartelli, N. L., Rasul, I., Festoff, B. W., Premont, R. T., & Arendash, G. W. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.08.013 · Cited by 75

Homocysteic acid induces intraneuronal accumulation of neurotoxic Aβ42: Implications for the pathogenesis of Alzheimer's disease

Hasegawa, T., Ukai, W., Jo, D., Xu, X. Z. S., Mattson, M. P., Nakagawa, M., Araki, W., Saito, T., & Yamada, T. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20514 · Cited by 73

Intracellular Accumulation of Detergent‐Soluble Amyloidogenic Aβ Fragment of Alzheimer's Disease Precursor Protein in the Hippocampus of Aged Transgenic Mice

Li, Q., Maynard, C. J., Cappai, R., McLean, C., Cherny, R. A., Lynch, T., Culvenor, J. G., Trevaskis, J., Tanner, J. E., Bailey, K. A., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722479.x · Cited by 73

Genetically Augmenting Aβ42 Levels in Skeletal Muscle Exacerbates Inclusion Body Myositis-Like Pathology and Motor Deficits in Transgenic Mice

Kitazawa, M., Green, K. N., Caccamo, A., & LaFerla, F. M. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051232 · Cited by 73

Amyloid β-Peptide: The Inside Story

Tseng, B., Kitazawa, M., & LaFerla, F. (2004) · Current Alzheimer Research · doi:10.2174/1567205043332045 · Cited by 72

Role of microglia in plaque formation in senile dementia of the Alzheimer type

Rozemüller, A. J. M., Eikelenboom, P., & Stam, F. C. (1986) · Virchows Archiv B Cell Pathology Including Molecular Pathology · doi:10.1007/bf02899034 · Cited by 72

Early intraneuronal Aβ deposition in the hippocampus of APP transgenic mice

Shie, F.-S., LeBoeur, R. C., & Jin, L.-W. (2003) · NeuroReport · doi:10.1097/00001756-200301200-00023 · Cited by 70

Inclusion body myositis

Rose, M. R., & Griggs, R. C. (2007) · Handbook of clinical neurology · doi:10.1016/s0072-9752(07)86013-1 · Cited by 66

Consistent immunohistochemical detection of intracellular β-amyloid42 in pyramidal neurons of Alzheimer's disease entorhinal cortex

D'Andrea, M. R., Nagele, R. G., Wang, H.-Y., & Lee, D. H. S. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(02)00875-3 · Cited by 64

Ultrastructural evidence of fibrillar β-amyloid associated with neuronal membranes in behaviorally characterized aged dog brains

Torp, R., Head, E., Milgram, N. W., Hahn, F. F., Ottersen, O. P., & Cotman, C. W. (2000) · Neuroscience · doi:10.1016/s0306-4522(99)00568-0 · Cited by 61

Inclusion body myositis

Tawil, R., & Griggs, R. C. (2002) · Current Opinion in Rheumatology · doi:10.1097/00002281-200211000-00004 · Cited by 61

Intraneuronal amyloid β and reduced brain volume in a novel APP T714I mouse model for Alzheimer's disease

Van Broeck, B., Vanhoutte, G., Pirici, D., Van Dam, D., Wils, H., Cuijt, I., Vennekens, K., Zabielski, M., Michalik, A., Theuns, J., et al. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.016 · Cited by 60

Lipofuscin and Aβ42 exhibit distinct distribution patterns in normal and Alzheimer's disease brains

D’Andrea, M. R., Nagele, R. G., Gumula, N. A., Reiser, P. A., Polkovitch, D. A., Hertzog, B. M., & Andrade‐Gordon, P. (2002) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02444-2 · Cited by 52

The use of formic acid to embellish amyloid plaque detection in Alzheimer's disease tissues misguides key observations

D'Andrea, M. R., Reiser, P. A., Polkovitch, D. A., Gumula, N. A., Branchide, B., Hertzog, B. M., Schmidheiser, D., Belkowski, S., Gastard, M. C., & Andrade-Gordon, P. (2003) · Neuroscience Letters · doi:10.1016/s0304-3940(03)00252-0 · Cited by 50

Age‐related changes of intracellular Aβ in cynomolgus monkey brains

Kimura, N., Yanagisawa, K., Terao, K., Ono, F., Sakakibara, I., Ishii, Y., Kyuwa, S., & Yoshikawa, Y. (2005) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00624.x · Cited by 44

Differential distribution of cellular forms of β-amyloid precursor protein in murine glial cell cultures

Mizuguchi, M., Ikeda, K., & Kim, S. U. (1992) · Brain Research · doi:10.1016/0006-8993(92)90898-j · Cited by 43

Transgenic expression of B‐APP in fast‐twitch skeletal muscle leads to calcium dyshomeostasis and IBM‐like pathology

Moussa, C., Fu, Q., Kumar, P., Shtifman, A., Lopez, J. R., Allen, P. D., LaFerla, F. M., Weinberg, D., Magrané, J., Aprahamian, T. R., et al. (2006) · The FASEB Journal · doi:10.1096/fj.06-5763fje · Cited by 38

Mitochondrial dysfunction induced by disease relevant AβPP and tau protein mutations

Keil, U., Hauptmann, S., Bonert, A., Scherping, I., Eckert, A., & Müller, W. E. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9206 · Cited by 36

Intraneuronal amyloid β42 enhanced by heating but counteracted by formic acid

Ohyagi, Y., Tsuruta, Y., Motomura, K., Miyoshi, K., Kikuchi, H., Iwaki, T., Taniwaki, T., & Kira, J. (2006) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2006.06.010 · Cited by 36

Untitled work

Salin (1998) · doi:10.1002/(sici)1096-9861(19980720)397:1

Pathological roles of MAPK signaling pathways in human diseases

Kim, E. K., & Choi, E.-J. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.12.009 · Cited by 2,472

Amyloid Precursor Protein Processing and Alzheimer's Disease

O'Brien, R. J., & Wong, P. C. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113613 · Cited by 2,061

The Amyloid-β Pathway in Alzheimer’s Disease

Hampel, H., Hardy, J., Blennow, K., Chen, C., Perry, G., Kim, S. H., Villemagne, V. L., Aisen, P., Vendruscolo, M., Iwatsubo, T., et al. (2021) · Molecular Psychiatry · doi:10.1038/s41380-021-01249-0 · Cited by 1,952

Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease

Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750

Amyloid-β and tau--a toxic pas de deux in Alzheimer’s disease

Ittner, L. M., & Götz, J. (2011) · Nature Reviews Neuroscience · doi:10.1038/nrn2967 · Cited by 1,269

Intracellular A-Beta Amyloid, A Sign for Worse Things to Come?

Echeverría, V., & Cuello, A. C. (2002) · Molecular Neurobiology · doi:10.1385/mn:26:2-3:299 · Cited by 81

Intraneuronal β-amyloid accumulation and synapse pathology in Alzheimer’s disease

Gouras, G. K., Tampellini, D., Takahashi, R. H., & Capetillo-Zarate, E. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0679-9 · Cited by 372

The impact of extracellular amyloid-β (Αβ) peptides on cortical neurotransmitters and of intracellular Aβ accumulation on protein expression AC Cuello, KFS Bell, V Echeverria, E Lopez, A Ribeiro-da-Silva, M Szyf

(2005) · CRC Press eBooks · doi:10.1201/b14441-47

Intracellular A? and its Pathological Role in Alzheimer's Disease: Lessons from Cellular to Animal Models

Ji, L., Zhao, X., Lu, W., Zhang, Q. H., & Hua, Z. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160322142226 · Cited by 23

Intraneuronal Aβ accumulation and origin of plaques in Alzheimer's disease

Gouras, G. K., Almeida, C. G., & Takahashi, R. H. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.022 · Cited by 338