A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease

McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915 · see citing works

Alzheimer's disease: the amyloid cascade hypothesis

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

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 · see citing works

Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease

Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659 · see citing works

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 · see citing works

The molecular pathology of Alzheimer's disease

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

Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor

Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403 · see citing works

Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type

Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,380 · see citing works

Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene

Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214 · see citing works

A mutation in the Amyloid Precursor Protein Associated with Hereditary Alzheimer's Disease

Murrell, J. R., Farlow, M. R., Ghetti, B. F., & Benson, M. D. (1991) · Science · doi:10.1126/science.1925564 · Cited by 1,122 · see citing works

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 · see citing works

Presenile dementia and cerebral haemorrhage linked to a mutation at codon 692 of the β–amyloid precursor protein gene

Hendriks, L., van Duijn, C. M., Cras, P. P., Cruts, M., Hul, W. V., van Harskamp, F., Warren, A., McInnis, M. G., Antonarakis, S. E., Martin, J., et al. (1992) · Nature Genetics · doi:10.1038/ng0692-218 · Cited by 735 · see citing works

Amyloid β Protein Precursor Gene and Hereditary Cerebral Hemorrhage with Amyloidosis (Dutch)

Broeckhoven, C. V., Haan, J., Bakker, E., Hardy, J., Hul, W. V., Wehnert, A., der Vlis, M. V.-V., & Roos, R. A. C. (1990) · Science · doi:10.1126/science.1971458 · Cited by 471 · see citing works

Neuritic plaques and cerebrovascular amyloid in Alzheimer disease are antigenically related.

Wong, C. W., Quaranta, V., & Glenner, G. G. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.24.8729 · Cited by 438 · see citing works

Potentially Amyloidogenic, Carboxyl-Terminal Derivatives of the Amyloid Protein Precursor

Estus, S., Golde, T. E., Kunishita, T., Blades, D. A., Lowery, D. E., Eisen, M., Usiak, M., QU, X., Tabira, T., Greenberg, B., et al. (1992) · Science · doi:10.1126/science.1738846 · Cited by 431 · see citing works

Mis-sense mutation Val→Ile in exon 17 of amyloid precursor protein gene in Japanese familial Alzheimer's disease

Naruse, S., Igarashi, S., Aoki, K., Kaneko, K., Iihara, K., Miyatake, T., Kobayashi, H., Inuzuka, T., Shimizu, T., Kojima, T., et al. (1991) · The Lancet · doi:10.1016/0140-6736(91)91612-x · Cited by 282 · see citing works

Genomic organization of the human amyloid beta-protein precursor gene

Yoshikai, S.-I., Sasaki, H., Doh‐ura, K., Furuya, H., & Sakaki, Y. (1990) · Gene · doi:10.1016/0378-1119(90)90310-n · Cited by 259 · see citing works

Exact cleavage site of Alzheimer amyloid precursor in neuronal PC-12 cells

Anderson, J. P., Esch, F. S., Keim, P. S., Sambamurti, K., Lieberburg, I. M., & Robakis, N. K. R. K. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90775-o · Cited by 212 · see citing works

The 717Val→Ile substitution in amyloid precursor protein is associated with familial Alzheimer's disease regardless of ethnic groups

Yoshioka, K., Miki, T., Katsuya, T., Ogihara, T., & Sakaki, Y. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91011-z · Cited by 130 · see citing works

Hereditary cerebral haemorrhage caused by cortical amyloid angiopathy

Luyendijk, W., Bots, G. T. A. M., der Vlis, M. V.-V., Went, L. N., & Frangione, B. (1988) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(88)90186-4 · Cited by 115 · see citing works

Alzheimer's mutation

Tanzi, R. E., & Hyman, B. T. (1991) · Nature · doi:10.1038/350564a0 · Cited by 99 · see citing works

Coca chewing and cholera

Feldmeier, H., & Krantz, I. (1991) · The Lancet · doi:10.1016/0140-6736(91)93010-7 · Cited by 82 · see citing works

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Secreted amyloid β–protein similar to that in the senile plaques of Alzheimer's disease is increased in vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease

Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599 · see citing works

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 · see citing works

High-Level Neuronal Expression of Aβ_1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation

Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856 · see citing works

Visualization of Aβ42(43) and Aβ40 in senile plaques with end-specific Aβ monoclonals: Evidence that an initially deposited species is Aβ42(43)

Iwatsubo, T., Odaka, A., Suzuki, N., Mizusawa, H., Nukina, N., & Ihara, Y. (1994) · Neuron · doi:10.1016/0896-6273(94)90458-8 · Cited by 1,774 · see citing works

Mutation of the β-amyloid precursor protein in familial Alzheimer's disease increases β-protein production

Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757 · see citing works

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611 · see citing works

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 · see citing works

Increased amyloid beta-peptide deposition in cerebral cortex as a consequence of apolipoprotein E genotype in late-onset Alzheimer disease.

Schmechel, D. E., Saunders, A. M., Strittmatter, W. J., Crain, B. J., Hulette, C. M., Joo, S. H., Pericak-Vance, M. A., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.20.9649 · Cited by 1,525 · see citing works

Two amyloid precursor protein transgenic mouse models with Alzheimer disease-like pathology

Sturchler-Pierrat, C., Abramowski, D., Duke, M., Wiederhold, K.-H., Mistl, C., Rothacher, S., Ledermann, B., Bürki, K., Frey, P., Paganetti, P. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.24.13287 · Cited by 1,507 · see citing works

Rapid induction of Alzheimer A beta amyloid formation by zinc

Bush, A., Pettingell, W., Multhaup, G., d Paradis, M., Vonsattel, J., Gusella, J., Beyreuther, K., Masters, C., & Tanzi, R. (1994) · Science · doi:10.1126/science.8073293 · Cited by 1,522 · see citing works

Familial Alzheimer's Disease–Linked Presenilin 1 Variants Elevate Aβ1–42/1–40 Ratio In Vitro and In Vivo

Borchelt, D. R., Thinakaran, G., Eckman, C. B., Lee, M. K., Davenport, F., Ratovitsky, T., Prada, C.-M., Kim, G., Seekins, S., Yager, D., et al. (1996) · Neuron · doi:10.1016/s0896-6273(00)80230-5 · Cited by 1,478 · see citing works

Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability

Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452 · see citing works

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 · see citing works

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 · see citing works

Plaque-independent disruption of neural circuits in Alzheimer’s disease mouse models

Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123 · see citing works

Trafficking and Proteolytic Processing of APP

Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works

Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease

Kawarabayashi, T., Younkin, L. H., Saido, T. C., Shoji, M., Ashe, K. H., & Younkin, S. G. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-02-00372.2001 · Cited by 1,053 · see citing works

Amyloid β-Protein Fibrillogenesis

Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046 · see citing works

Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins

Borchelt, D. R., Ratovitski, T., van Lare, J., Lee, M. K., Gonzales, V., Jenkins, N. A., Copeland, N. G., Price, D. L., & Sisodia, S. S. (1997) · Neuron · doi:10.1016/s0896-6273(00)80974-5 · Cited by 1,023 · see citing works

Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice

Chapman, P. F., White, G. L., Jones, M. W., Cooper-Blacketer, D., Marshall, V. J., Irizarry, M., Younkin, L., Good, M. A., Bliss, T. V. P., Hyman, B. T., et al. (1999) · Nature Neuroscience · doi:10.1038/6374 · Cited by 946 · see citing works

Cerebral amyloid angiopathy and Alzheimer disease — one peptide, two pathways

Greenberg, S. M., Bacskai, B. J., Hernandez-Guillamon, M., Pruzin, J., Sperling, R., & van Veluw, S. J. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-019-0281-2 · Cited by 947 · see citing works

Advanced glycation end products contribute to amyloidosis in Alzheimer disease

Vitek, M. P., Bhattacharya, K., Glendening, J. M., Stopa, E., Vlassara, H., Bucala, R., Manogue, K., & Cerami, A. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.11.4766 · Cited by 806 · see citing works

History and progress of hypotheses and clinical trials for Alzheimer’s disease

Liu, P.-P., Xie, Y., Meng, X.-Y., & Kang, J.-S. (2019) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-019-0063-8 · Cited by 723 · see citing works

The β-Secretase BACE1 in Alzheimer’s Disease

Hampel, H., Vassar, R., De Strooper, B., Hardy, J., Willem, M., Singh, N., Zhou, J., Yan, R., Vanmechelen, E., De Vos, A., et al. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2020.02.001 · Cited by 694 · see citing works

The role of microglia in amyloid clearance from the AD brain

Lee, C. Y. D., & Landreth, G. E. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0433-4 · Cited by 701 · see citing works

Early Phenotypic Changes in Transgenic Mice That Overexpress Different Mutants of Amyloid Precursor Protein in Brain

Moechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668 · see citing works

Aβ Deposition Is Associated with Neuropil Changes, but not with Overt Neuronal Loss in the Human Amyloid Precursor Protein V717F (PDAPP) Transgenic Mouse

Irizarry, M. C., Soriano, F., McNamara, M., Page, K. J., Schenk, D., Games, D., & Hyman, B. T. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-18-07053.1997 · Cited by 497 · see citing works

Alzheimer’s Disease Genetics: From the Bench to the Clinic

Karch, C. M., Cruchaga, C., & Goate, A. M. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.041 · Cited by 473 · see citing works

Relative Abundance of Alzheimer A Beta Amyloid Peptide Variants in Alzheimer Disease and normal Aging

Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468 · see citing works

REVIEW: Curcumin and Alzheimer’s disease

Hamaguchi, T., Ono, K., & Yamada, M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00147.x · Cited by 450 · see citing works

Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation

Eimer, W. A., & Vassar, R. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-2 · Cited by 425 · see citing works

Tau Aggregation and Its Interplay with Amyloid-β

Nisbet, R. M., Polanco, J.-C., Ittner, L. M., & Götz, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1371-2 · Cited by 359 · see citing works

Early-onset and Robust Cerebral Microvascular Accumulation of Amyloid β-Protein in Transgenic Mice Expressing Low Levels of a Vasculotropic Dutch/Iowa Mutant Form of Amyloid β-Protein Precursor

Davis, J., Xu, F., Deane, R., Romanov, G., Previti, M. L., Zeigler, K., Zlokovic, B. V., & Van Nostrand, W. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312946200 · Cited by 373 · see citing works

A Critical Function for β-Amyloid Precursor Protein in Neuronal Migration Revealed by <i>In Utero</i> RNA Interference

Young-Pearse, T. L., Bai, J., Chang, R., Zheng, J. B., LoTurco, J. J., & Selkoe, D. J. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4701-07.2007 · Cited by 369 · see citing works

β-Site Amyloid Precursor Protein Cleaving Enzyme 1 Levels Become Elevated in Neurons around Amyloid Plaques: Implications for Alzheimer's Disease Pathogenesis

Zhao, J., Fu, Y., Yasvoina, M., Shao, P., Hitt, B., O'Connor, T., Logan, S., Maus, E., Citron, M., Berry, R., et al. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4396-06.2007 · Cited by 365 · see citing works

A Genome-wide Gene-Expression Analysis and Database in Transgenic Mice during Development of Amyloid or Tau Pathology

Matarin, M., Salih, D. A., Yasvoina, M., Cummings, D. M., Guelfi, S., Liu, W., Nahaboo Solim, M. A., Moens, T. G., Paublete, R. M., Ali, S. S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2014.12.041 · Cited by 290 · see citing works

Genes associated with Alzheimer&amp;#39;s disease: an overview and current status

Giri, M., Lü, Y., & Zhang, M. (2016) · Clinical Interventions in Aging · doi:10.2147/cia.s105769 · Cited by 311 · see citing works

Sensitive ELISA detection of amyloid‐β protofibrils in biological samples

Englund, H., Sehlin, D., Johansson, A., Nilsson, L. N. G., Gellerfors, P., Paulie, S., Lannfelt, L., & Pettersson, F. E. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04759.x · Cited by 292 · see citing works

Presynaptic dystrophic neurites surrounding amyloid plaques are sites of microtubule disruption, BACE1 elevation, and increased Aβ generation in Alzheimer’s disease

Sadleir, K. R., Kandalepas, P. C., Buggia-Prévot, V., Nicholson, D. A., Thinakaran, G., & Vassar, R. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1558-9 · Cited by 294 · see citing works

The cerebrospinal-fluid soluble form of Alzheimer's amyloid β is complexed to SP-40,40 (apolipoprotein J), an inhibitor of the complement membrane-attack complex

Ghiso, J., Matsubara, E., Koudinov, A., Choi-Miura, N. H., Tomita, M., Wisniewski, T., & Frangione, B. (1993) · Biochemical Journal · doi:10.1042/bj2930027 · Cited by 304 · see citing works

BACE1 gene deletion prevents neuron loss and memory deficits in 5XFAD APP/PS1 transgenic mice

Ohno, M., Cole, S. L., Yasvoina, M., Zhao, J., Citron, M., Berry, R., Disterhoft, J. F., & Vassar, R. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.12.008 · Cited by 290 · see citing works

Amyloid β-protein oligomers and Alzheimer’s disease

Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research &amp; Therapy · doi:10.1186/alzrt226 · Cited by 276 · see citing works

Augmented Senile Plaque Load in Aged Female β-Amyloid Precursor Protein-Transgenic Mice

Callahan, M. J., Lipinski, W. J., Bian, F., Durham, R. A., Pack, A., & Walker, L. C. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64064-3 · Cited by 274 · see citing works

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 · see citing works

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 · see citing works

Genetics of β-Amyloid Precursor Protein in Alzheimer's Disease

TCW, J., & Goate, A. M. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a024539 · Cited by 242 · see citing works

Untangling Genetic Risk for Alzheimer’s Disease

Pimenova, A. A., Raj, T., & Goate, A. M. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.05.014 · Cited by 223 · see citing works

Dendritic spine loss in the hippocampus of young PDAPP and Tg2576 mice and its prevention by the ApoE2 genotype

Lanz, T. A., Carter, D. B., & Merchant, K. M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00079-2 · Cited by 227 · see citing works

Pathogenic APP mutations near the gamma-secretase cleavage site differentially affect Abeta secretion and APP C-terminal fragment stability

De Jonghe, C. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.16.1665 · Cited by 223 · see citing works

Alterations in cerebral blood flow and glucose utilization in mice overexpressing the amyloid precursor protein

Niwa, K., Kazama, K., Younkin, S. G., Carlson, G. A., & Iadecola, C. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0460 · Cited by 218 · see citing works

Somatic APP gene recombination in Alzheimer’s disease and normal neurons

Lee, M.-H., Siddoway, B., Kaeser, G. E., Segota, I., Rivera, R., Romanow, W. J., Liu, C. S., Park, C., Kennedy, G., Long, T., et al. (2018) · Nature · doi:10.1038/s41586-018-0718-6 · Cited by 210 · see citing works

The Potent BACE1 Inhibitor LY2886721 Elicits Robust Central Aβ Pharmacodynamic Responses in Mice, Dogs, and Humans

May, P. C., Willis, B. A., Lowe, S. L., Dean, R. A., Monk, S. A., Cocke, P. J., Audia, J. E., Boggs, L. N., Borders, A. R., Brier, R. A., et al. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.4129-14.2015 · Cited by 206 · see citing works

Inhibition of Calcineurin-mediated Endocytosis and α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors Prevents Amyloid β Oligomer-induced Synaptic Disruption

Zhao, W.-Q., Santini, F., Breese, R., Ross, D., Zhang, X. D., Stone, D. J., Ferrer, M., Townsend, M., Wolfe, A. L., Seager, M. A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.057182 · Cited by 188 · see citing works

Transgenic mouse models of alzheimer disease: Developing a better model as a tool for therapeutic interventions.

Kitazawa, M., Medeiros, R., & M. LaFerla, F. (2012) · Current Pharmaceutical Design · doi:10.2174/138161212799315786 · Cited by 178 · see citing works

Correlating familial Alzheimer’s disease gene mutations with clinical phenotype

Ryan, N. S., & Rossor, M. N. (2010) · Biomarkers in Medicine · doi:10.2217/bmm.09.92 · Cited by 176 · see citing works

Lipopolysaccharide-Induced Memory Impairment in Rats: a Model of Alzheimer’s Disease

ZAKARIA, R., WAN YAACOB, W. M. H., OTHMAN, Z., LONG, I., AHMAD, A. H., & AL-RAHBI, B. (2017) · Physiological Research · doi:10.33549/physiolres.933480 · Cited by 167 · see citing works

The Role of Cathepsin D in the Pathogenesis of Human Neurodegenerative Disorders

Vidoni, C., Follo, C., Savino, M., Melone, M. A. B., & Isidoro, C. (2016) · Medicinal Research Reviews · doi:10.1002/med.21394 · Cited by 164 · see citing works

Amyloids and Are Generated Intracellularly in Cultured Human Neurons and Their Secretion Increases with Maturation

Turner, R. S., Suzuki, N., Chyung, A. S. C., Younkin, S. G., & Lee, V. M.-Y. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.15.8966 · Cited by 161 · see citing works

Genetic Modification of the Phenotypes Produced by Amyloid Precursor Protein Overexpression in Transgenic Mice

Carlson, G. A., Borchelt, D. R., Dake, A., Turner, S., Danielson, V., Coffin, J. D., Eckman, C., Meiners, J., Nilsen, S. P., Younkin, S. G., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.11.1951 · Cited by 158 · see citing works

Nonfibrillar diffuse amyloid deposition due to a gamma42-secretase site mutation points to an essential role for N-truncated Abeta42 in Alzheimer's disease

Kumar-Singh, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2589 · Cited by 158 · see citing works

Recent advances in the modeling of Alzheimer’s disease

Sasaguri, H., Hashimoto, S., Watamura, N., Sato, K., Takamura, R., Nagata, K., Tsubuki, S., Ohshima, T., Yoshiki, A., Sato, K., et al. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.807473 · Cited by 157 · see citing works

New roles for Fc receptors in neurodegeneration-the impact on Immunotherapy for Alzheimer's Disease

Fuller, J. P., Stavenhagen, J. B., & Teeling, J. L. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00235 · Cited by 154 · see citing works

Histone deacetylases (HDACs) and brain function

Volmar, C.-H., & Wahlestedt, C. (2015) · Neuroepigenetics · doi:10.1016/j.nepig.2014.10.002 · Cited by 151 · see citing works

Enhanced Amyloidogenic Processing of the β-Amyloid Precursor Protein in Gene-targeted Mice Bearing the Swedish Familial Alzheimer's Disease Mutations and a “Humanized” Aβ Sequence

Reaume, A. G., Howland, D. S., Trusko, S. P., Savage, M. J., Lang, D. M., Greenberg, B. D., Siman, R., & Scott, R. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23380 · Cited by 150 · see citing works

If amyloid drives Alzheimer disease, why have anti-amyloid therapies not yet slowed cognitive decline?

Haass, C., & Selkoe, D. (2022) · PLOS Biology · doi:10.1371/journal.pbio.3001694 · Cited by 145 · see citing works

Making the final cut: Pathogenic amyloid-β peptide generation by γ-secretase

Steiner, H., Fukumori, A., Tagami, S., & Okochi, M. (2018) · Cell Stress · doi:10.15698/cst2018.11.162 · Cited by 133 · see citing works

Neuropathology after active Aβ42 immunotherapy: implications for Alzheimer’s disease pathogenesis

Boche, D., Denham, N., Holmes, C., & Nicoll, J. A. R. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0719-5 · Cited by 135 · see citing works

Animal models of Alzheimer disease: historical pitfalls and a path forward

Cavanaugh, S. E. (2014) · ALTEX · doi:10.14573/altex.1310071 · Cited by 132 · see citing works

Altered metabolism of familial Alzheimer's disease-linked amyloid precursor protein variants in yeast artificial chromosome transgenic mice

Lamb, B. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.9.1535 · Cited by 128 · see citing works

Intraneuronal APP/Aβ Trafficking and Plaque Formation in β‐Amyloid Precursor Protein and Presenilin‐1 Transgenic Mice

Wirths, O., Multhaup, G., Czech, C., Feldmann, N., Blanchard, V., Tremp, G., Beyreuther, K., Pradier, L., & Bayer, T. A. (2002) · Brain Pathology · doi:10.1111/j.1750-3639.2002.tb00442.x · Cited by 125 · see citing works

Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion

Barbero-Camps, E., Roca-Agujetas, V., Bartolessis, I., de Dios, C., Fernández-Checa, J. C., Marí, M., Morales, A., Hartmann, T., & Colell, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1438807 · Cited by 125 · see citing works

Increased plasma beta-secretase 1 may predict conversion to Alzheimer’s disease dementia in individuals with mild cognitive impairment

Shen, Y., Wang, H., Sun, Q., Yao, H., Keegan, A. P., Mullan, M., Wilson, J., Lista, S., Leyhe, T., Laske, C., et al. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.02.007 · Cited by 123 · see citing works

Phosphodiesterase-4 (PDE4) Molecular Pharmacology and Alzheimer's Disease

Gurney, M. E., D'Amato, E. C., & Burgin, A. B. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0309-7 · Cited by 121 · see citing works

Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau

Rayaprolu, S., Higginbotham, L., Bagchi, P., Watson, C. M., Zhang, T., Levey, A. I., Rangaraju, S., & Seyfried, N. T. (2021) · Neuropsychopharmacology · doi:10.1038/s41386-020-00840-3 · Cited by 118 · see citing works

Clinical and Neuropathological Features of the Arctic APP Gene Mutation Causing Early-Onset Alzheimer Disease

Basun, H., Bogdanovic, N., Ingelsson, M., Almkvist, O., Näslund, J., Axelman, K., Bird, T. D., Nochlin, D., Schellenberg, G. D., Wahlund, L.-O., et al. (2008) · Archives of Neurology · doi:10.1001/archneur.65.4.499 · Cited by 115 · see citing works

Amyloid‐β protein (Aβ) Glu11 is the major β‐secretase site of β‐site amyloid‐β precursor protein‐cleaving enzyme 1(BACE1), and shifting the cleavage site to Aβ Asp1 contributes to Alzheimer pathogenesis

Deng, Y., Wang, Z., Wang, R., Zhang, X., Zhang, S., Wu, Y., Staufenbiel, M., Cai, F., & Song, W. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12235 · Cited by 108 · see citing works

Amyloid‐β oligomers are inefficiently measured by enzyme‐linked immunosorbent assay

Stenh, C., Englund, H., Lord, A., Johansson, A., Almeida, C. G., Gellerfors, P., Greengard, P., Gouras, G. K., Lannfelt, L., & Nilsson, L. N. G. (2005) · Annals of Neurology · doi:10.1002/ana.20524 · Cited by 99 · see citing works

Altered cleavage and secretion of a recombinant β–APP bearing the Swedish familial Alzheimer's disease mutation

Felsenstein, K. M., Hunihan, L. W., & Roberts, S. B. (1994) · Nature Genetics · doi:10.1038/ng0394-251 · Cited by 90 · see citing works

Sex‐biased hippocampal pathology in the 5XFAD mouse model of Alzheimer's disease: A multi‐omic analysis

Bundy, J. L., Vied, C., Badger, C., & Nowakowski, R. S. (2019) · Journal of Comparative Neurology · doi:10.1002/cne.24551 · Cited by 90 · see citing works

Cerebral Amyloid Angiopathy

(2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00006-0 · Cited by 84 · see citing works

Shifting paradigms: The central role of microglia in Alzheimer’s disease

Schwabe, T., Srinivasan, K., & Rhinn, H. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104962 · Cited by 84 · see citing works

Apolipoprotein E4 allele and Alzheimer disease: Examination of Allelic association and effect on age at onset in both early‐and late‐onset cases

Locke, P. A., Conneally, P. M., Tanzi, R. E., Gusella, J. F., & Haines, J. L. (1995) · Genetic Epidemiology · doi:10.1002/gepi.1370120108 · Cited by 75 · see citing works

Behavioral and neural network abnormalities in human APP transgenic mice resemble those of App knock-in mice and are modulated by familial Alzheimer's disease mutations but not by inhibition of BACE1

Johnson, E. C. B., Ho, K., Yu, G.-Q., Das, M., Sanchez, P. E., Djukic, B., Lopez, I., Yu, X., Gill, M., Zhang, W., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00393-5 · Cited by 73 · see citing works

Evidence that the APOE locus influences rate of disease progression in late onset familial Alzheimer's Disease but is not causative

Bennett, C., Crawford, F., Osborne, A., Diaz, P., Hoyne, J., Lopez, R., Roques, P., Duara, R., Rossor, M., & Mullan, M. (1995) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320600102 · Cited by 67 · see citing works

N-truncated Abeta starting with position four: Early intraneuronal accumulation and rescue of toxicity using NT4X-167, a novel monoclonal antibody

Antonios, G., Saiepour, N., Bouter, Y., Richard, B. C., Paetau, A., Verkkoniemi-Ahola, A., Lannfelt, L., Ingelsson, M., Kovacs, G. G., Pillot, T., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-56 · Cited by 53 · see citing works

β-amyloid: The known unknowns

Ayton, S., & Bush, A. I. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101212 · Cited by 45 · see citing works

Insights on the Use of Transgenic Mice Models in Alzheimer’s Disease Research

Pádua, M. S., Guil-Guerrero, J. L., Prates, J. A. M., & Lopes, P. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052805 · Cited by 46 · see citing works

Amyloid β-peptide in cerebrospinal fluid in individuals with the Swedish Alzheimer amyloid precursor protein mutation

Lannfelt, L., Basun, H., Vigo-Pelfrey, C., Wahlund, L.-O., Winblad, B., Lieberburg, I., & Schenk, D. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12059-d · Cited by 39 · see citing works

Dietary intervention with edible medicinal plants and derived products for prevention of Alzheimer's disease: A compendium of time-tested strategy

Peng, Y., Tao, H., Wang, S., Xiao, J., Wang, Y., & Su, H. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104463 · Cited by 31 · see citing works

Translating Alzheimer’s disease-associated polymorphisms into functional candidates: a survey of IGAP genes and SNPs

Katsumata, Y., Nelson, P. T., Estus, S., & Fardo, D. W. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.10.017 · Cited by 30 · see citing works

Genetic Variation in N-Methyl-D-Aspartate Receptor Subunit NR3A but Not NR3B Influences Susceptibility to Alzheimer’s Disease

Liu, H.-P., Lin, W.-Y., Liu, S.-H., Wang, W.-F., Tsai, C.-H., Wu, B.-T., Wang, C.-K., & Tsai, F.-J. (2009) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000254757 · Cited by 29 · see citing works

Is It the Twilight of BACE1 Inhibitors?

Hrabinova, M., Pejchal, J., Kucera, T., Jun, D., Schmidt, M., & Soukup, O. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200503023323 · Cited by 28 · see citing works

Systemic LPS-induced Aβ-solubilization and clearance in AβPP-transgenic mice is diminished by heparanase overexpression

Jendresen, C., Digre, A., Cui, H., Zhang, X., Vlodavsky, I., Li, J.-P., & Nilsson, L. N. G. (2019) · Scientific Reports · doi:10.1038/s41598-019-40999-4 · Cited by 19 · see citing works

Apolipoprotein E, Aβ‐Amyloid, and the Molecular Pathology of Alzheimer's Disease Therapeutic Implicationsa

KAPLITT, M., GOURAS, G. K., MAKIMURA, H., JOVANOVIC, J., SWEENEY, D., GREENGARD, P., RELKIN, N. R., & GANDY, S. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb32597.x · Cited by 12 · see citing works

Aβ43 levels determine the onset of pathological amyloid deposition

Tambini, M. D., Yin, T., Yesiltepe, M., Breuillaud, L., Zehntner, S. P., d'Abramo, C., Giliberto, L., & D'Adamio, L. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104868 · Cited by 8 · see citing works

Initial assessment of the spatial learning, reversal, and sequencing task capabilities of knock-in rats with humanizing mutations in the Aβ-coding region of App

Pham, H., Yin, T., & D’Adamio, L. (2022) · PLOS ONE · doi:10.1371/journal.pone.0263546 · Cited by 6 · see citing works

[Detection of alterations of the DPC4 gene in paraffin-embedded tissues of pancreatic carcinomas].

Gu, L., Cui, Q.-C., Chen, J., et al. (2000) · PubMed

Characterization of a novel alternatively-spliced 5′ exon in the human insulin-like growth factor I (IGF-I) gene, expressed in liver and some cancers

Wallis, M. (2019) · Growth Hormone & IGF Research · doi:10.1016/j.ghir.2019.06.002 · Cited by 4 · see citing works

Nitric oxide synthase 1 mRNA: tissue-specific variants from rat with alternative first exons.

Oberbäumer, I., Moser, D., & Bachmann, S. (1998) · PubMed · Cited by 36 · see citing works

Structure of the glucocorticoid receptor (NR3C1) gene 5′ untranslated region: identification, and tissue distribution of multiple new human exon 1

Turner, J. D., & Muller, C. P. (2005) · Journal of Molecular Endocrinology · doi:10.1677/jme.1.01822 · Cited by 256 · see citing works

(606)

Lecybył, R., Acosta‐Guillen, J., & Hanna, M. G. (2006) · Journal of Pain · doi:10.1016/j.jpain.2006.01.008 · Cited by 1 · see citing works