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Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Abstract
Alzheimer's disease (AD) is the most common cause of progressive intellectual failure in aged humans. AD brains contain numerous amyloid plaques surrounded by dystrophic neurites, and show profound synaptic loss, neurofibrillary tangle formation and gliosis. The amyloid plaques are composed of amyloid beta-peptide (A beta), a 40-42-amino-acid fragment of the beta-amyloid precursor protein (APP). A primary pathogenic role for APP/A beta is suggested by missense mutations in APP that are tightly linked to autosomal dominant forms of AD. A major obstacle to elucidating and treating AD has been the lack of an animal model. Animals transgenic for APP have previously failed to show extensive AD-type neuropathology, but we now report the production of transgenic mice that express high levels of human mutant APP (with valine at residue 717 substituted by phenylalanine) and which progressively develop many of the pathological hallmarks of AD, including numerous extracellular thioflavin S-positive A beta deposits, neuritic plaques, synaptic loss, astrocytosis and microgliosis. These mice support a primary role for APP/A beta in the genesis of AD and could provide a preclinical model for testing therapeutic drugs.
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In the citing paper
“Mouse models that overexpress amyloid precursor protein (APP) develop plaques remarkably similar to those observed in AD but do not recapitulate neurofibrillary pathology or widespread neuronal loss (Games et al., 1995;Hsiao et al., 1996;Irizarry et al., 1997a;Urbanc et al., 2002), allowing interpretation of results in the context of amyloid-related pathologies.”
From Dendritic Spine Abnormalities in Amyloid Precursor Protein Transgenic Mice Demonstrated by Gene Transfer and Intravital Multiphoton Microscopy (2005) · cites this paper as Games et al., 1995
In the citing paper
“Similar to AD, APP transgenic mouse models have elevated inflammation markers and gliosis associated with amyloid deposits (Games et al., 1995; Hsiao et al., 1996; Sturchler-Pierrat et al., 1997).”
From Intraneuronal β-Amyloid Aggregates, Neurodegeneration, and Neuron Loss in Transgenic Mice with Five Familial Alzheimer's Disease Mutations: Potential Factors in Amyloid Plaque Formation (2006) · cites this paper as Games et al., 1995
In the citing paper
“The first successful mouse models reproducing Aβ pathologies overexpressed human APP with either a single Swedish [25, 26] or Indiana [27] mutation.”
From Amyloid-β plaque formation and reactive gliosis are required for induction of cognitive deficits in App knock-in mouse models of Alzheimer’s disease (2019) · cites this paper as [27]
In the citing paper
“The hAPP tg line J9 selected for this study expresses an alternatively spliced minigene, hA PP, bearing the amyloidogenic V717F and K670M / N671L mutations that have been linked to familial AD (Games et al., 1995).”
From Increased Extracellular Amyloid Deposition and Neurodegeneration in Human Amyloid Precursor Protein Transgenic Mice Deficient in Receptor-Associated Protein (2002) · cites this paper as Games et al., 1995
In the citing paper
“The J9 model utilizes a mini-APP gene that can produce all three isoforms of APP: APP695, APP751 and APP770 [41].”
From Receptor-Associated Protein (RAP) Plays a Central Role in Modulating Aβ Deposition in APP/PS1 Transgenic Mice (2008) · cites this paper as [41]
In the citing paper
“These genetic findings led to several transgenic mouse models that successfully recapitulated Aβ plaque formation, increasing support for the hypothesis (Table 1) [23–29].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [25]
Citations
Cites
Single-Step Method of RNA Isolation by Acid Guanidinium Thiocyanate–Phenol–Chloroform Extraction
Chomczynski, P., & Sacchi, N. (1987) · Analytical Biochemistry · doi:10.1006/abio.1987.9999 · Cited by 65,515
Manipulating the mouse embryo: A laboratory manual
Hogan, B. L. M., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,460
Manipulating the mouse embryo: A laboratory manual
Johnson, M. (1986) · Trends in Genetics · doi:10.1016/0168-9525(86)90275-1 · Cited by 2,259
Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Self-citationQuantitation of mRNA by the polymerase chain reaction.
Wang, A. M., DOYLE, M. V., & Mark, D. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.24.9717 · Cited by 1,630
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
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 1,142
Normal and Abnormal Biology of the Beta-Amyloid Precursor Protein
Selkoe, D. J. (1994) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.17.030194.002421 · Cited by 834
Roher, A. E., Lowenson, J. D., Clarke, S., Wolkow, C., Wang, R., Cotter, R. J., Reardon, I. M., Zürcher-Neely, H. A., Heinrikson, R. L., & Ball, M. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53661-9 · Cited by 799
Sasahara, M., Fries, J. W. U., Raines, E. W., Gown, A. M., Westrum, L. E., Frosch, M. P., Bonthron, D. T., Ross, R., & Collins, T. (1991) · Cell · doi:10.1016/0092-8674(91)90223-l · Cited by 411
Research works printed but not linked: 4
- Mann, D. M. A. et al. Neurodegeneration 1, 201–215 (1992).
- McConlogue, L. et al. Neurobiol. Aging 15, S12 (1994).
- Masliah, E. et al. Am. J. Path. 138, 235–246 (1991).
- Chomazynski, P. & Sacchi, N. Analyt. Biochem. 162, 156–159 (1987).
Cited by
Sorted by citations
Items 201–300 of 1,029
Monoclonal antibodies inhibit in vitro fibrillar aggregation of the Alzheimer beta-amyloid peptide.
Solomon, B., Koppel, R., Hanan, E., & Katzav-Gozansky, T. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.1.452 · Cited by 314
Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade
Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313
Lipids revert inert Aβ amyloid fibrils to neurotoxic protofibrils that affect learning in mice
Martins, I. C., Kuperstein, I., Wilkinson, H. R., Maes, E., Vanbrabant, M., Jonckheere, W., Gelder, P. V., Hartmann, D., D’Hooge, R., Strooper, B. D., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601953 · Cited by 318
Czarny, P., Wigner, P., Galecki, P., & Sliwinski, T. (2018) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2017.06.036 · Cited by 310
TRANSFORMING GROWTH FACTOR-βS IN NEURODEGENERATIVE DISEASE
FLANDERS, K. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(97)00066-x · Cited by 364
Role of complement in neurodegeneration and neuroinflammation
Bonifati, D. M., & Kishore, U. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.03.007 · Cited by 314
Targeting soluble Aβ peptide with Tramiprosate for the treatment of brain amyloidosis
Gervais, F., Paquette, J., Morissette, C., Krzywkowski, P., Yu, M. W. N., Azzi, M., Lacombe, D., Kong, X., Aman, A. M., Laurin, J., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.02.015 · Cited by 313
Neurodegenerative disorders and ischemic brain diseases
Mattson, M. P., Duan, W., Pedersen, W. A., & Culmsee, C. (2001) · APOPTOSIS · doi:10.1023/a:1009676112184 · Cited by 307
Cummings, B. J., Pike, C. J., Shankle, R., & Cotman, C. W. (1996) · Neurobiology of Aging · doi:10.1016/s0197-4580(96)00170-4 · Cited by 305
Synaptic changes in Alzheimer’s disease and its models
Pozueta, J., Lefort, R., & Shelanski, M. L. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2012.05.050 · Cited by 319
Amyloid-β Deposits Lead to Retinal Degeneration in a Mouse Model of Alzheimer Disease
Ning, A., Cui, J., To, E., Ashe, K. H., & Matsubara, J. (2008) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.08-1849 · Cited by 303
Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment.
Lombardo, S., & Maskos, U. (2015) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.11.018 · Cited by 281
Alzheimer's disease: synapses gone cold
Koffie, R. M., Hyman, B. T., & Spires‐Jones, T. L. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-63 · Cited by 316
Ferrer, I., Gómez‐Isla, T., Puig, B., Freixes, M., Ribé, E. M., Dalfó, E., & Ávila, J. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772713 · Cited by 309
McConlogue, L., Buttini, M., Anderson, J. P., Brigham, E. F., Chen, K. S., Freedman, S. B., Games, D., Johnson-Wood, K., Lee, M., Zeller, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611687200 · Cited by 300
Self-citationGolde, T. E., Eckman, C. B., & Younkin, S. G. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00043-0 · Cited by 244
Evidence for glial-mediated inflammation in aged APPSW transgenic mice
Benzing, W. C., Wujek, J. R., Ward, E. K., Shaffer, D. J., Ashe, K. H., Younkin, S. G., & Brunden, K. R. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00065-2 · Cited by 303
Yuan, S., Ryder, J. W., Li, B., Wu, X., Fox, N. W., Solenberg, P., Brune, K. A., Paul, S. M., Zhou, Y., Liu, F., et al. (2004) · Biochemistry · doi:10.1021/bi035627j · Cited by 298
β-Secretase Activity Increases with Aging in Human, Monkey, and Mouse Brain
Fukumoto, H., Rosene, D. L., Moss, M. B., Raju, S., Hyman, B. T., & Irizarry, M. C. (2004) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63159-8 · Cited by 294
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
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290
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
Rogers, J. T., Leiter, L. M., McPhee, J., Cahill, C. M., Zhan, S.-S., Potter, H., & Nilsson, L. N. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6421 · Cited by 290
Inducible nitric oxide synthase in tangle-bearing neurons of patients with Alzheimer's disease.
Yoram Vodovotz, B., Lucia, M. S., Flanders, K. C., Chesler, L., Xie, Q. W., Smith, T. W., Weidner, J. R., Mumford, R. A., Webber, R., Nathan, C., et al. (1996) · The Journal of Experimental Medicine · doi:10.1084/jem.184.4.1425 · Cited by 292
Mouse models of Alzheimer’s disease
Esquerda-Canals, G., Montoliu-Gaya, L., Güell-Bosch, J., & Villegas, S. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170045 · Cited by 288
A decade of modeling Alzheimer's disease in transgenic mice
MCGOWAN, E., ERIKSEN, J., & HUTTON, M. (2006) · Trends in Genetics · doi:10.1016/j.tig.2006.03.007 · Cited by 287
Mattson, M. P., Duan, W., & Guo, Z. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01586.x · Cited by 289
Females exhibit more extensive amyloid, but not tau, pathology in an Alzheimer transgenic model
Hirata-Fukae, C., Li, H.-F., Hoe, H.-S., Gray, A. J., Minami, S. S., Hamada, K., Niikura, T., Hua, F., Tsukagoshi-Nagai, H., Horikoshi-Sakuraba, Y., et al. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.079 · Cited by 284
Blanchard, V., Moussaoui, S., Czech, C., Touchet, N., Bonici, B., Planche, M., Canton, T., Jedidi, I., Gohin, M., Wirths, O., et al. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00252-8 · Cited by 283
Han, H., Weinreb, P. H., & Lansbury, P. T. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90071-3 · Cited by 287
The canine as an animal model of human aging and dementia
Cummings, B. J., Head, E., Ruehl, W. W., Milgram, N. W., & Cotman, C. W. (1996) · Neurobiology of Aging · doi:10.1016/0197-4580(95)02060-8 · Cited by 291
Verchere, C. B., D'Alessio, D. A., Palmiter, R. D., Weir, G. C., Bonner-Weir, S., Baskin, D. G., & Kahn, S. E. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.8.3492 · Cited by 278
Hoshi, M. M., Takashima, A., Noguchi, K., Murayama, M., Sato, M., Kondo, S., Saitoh, Y., Ishiguro, K., Hoshino, T., & Imahori, K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.7.2719 · Cited by 277
Solvent effects on self-assembly of beta-amyloid peptide
Shen, C. L., & Murphy, R. M. (1995) · Biophysical Journal · doi:10.1016/s0006-3495(95)79940-4 · Cited by 281
Karran, E. H., & Hardy, J. (2014) · Annals of Neurology · doi:10.1002/ana.24188 · Cited by 279
Cortical Degeneration in the Absence of Neurotrophin Signaling
Xu, B., Zang, K., Ruff, N. L., Zhang, Y. A., McConnell, S. K., Stryker, M. P., & Reichardt, L. F. (2000) · Neuron · doi:10.1016/s0896-6273(00)81153-8 · Cited by 275
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
Larson, J., LYNCH, G. S., Games, D., & Seubert, P. A. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01698-4 · Cited by 291
Self-citationGötz, J., Streffer, J. R., David, D. C., Schild, A., Hoerndli, F. J., Pennanen, L., Kurosinski, P., & Chen, F. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001508 · Cited by 284
Exploring the Etiology of Alzheimer Disease Using Molecular Genetics
Lendon, C. L. (1997) · JAMA · doi:10.1001/jama.1997.03540340059034 · Cited by 274
γ-Secretase inhibitors and modulators
Golde, T. E., Koo, E. H., Felsenstein, K. M., Osborne, B. A., & Miele, L. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.06.005 · Cited by 275
Subramaniam, R., Roediger, F., Jordan, B., Mattson, M. P., Keller, J. N., Waeg, G., & Butterfield, D. A. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.69031161.x · Cited by 270
Slow Degradation of Aggregates of the Alzheimer's Disease Amyloid β-Protein by Microglial Cells
Paresce, D. M., Chung, H., & Maxfield, F. R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.46.29390 · Cited by 275
The Glutamatergic System and Alzheimer???s Disease
Butterfield, D. A., & Pocernich, C. B. (2003) · CNS Drugs · doi:10.2165/00023210-200317090-00004 · Cited by 274
Learning and memory in the SAMP8 mouse
Flood, J. F., & Morley, J. E. (1997) · Neuroscience & Biobehavioral Reviews · doi:10.1016/s0149-7634(96)00063-2 · Cited by 267
Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
Botto, M., Hawkins, P. N., Bickerstaff, M. C. M., Herbert, J., Bygrave, A. E., Mcbride, A., Hutchinson, W. L., Tennent, G. A., Walportz, M. J., & Pepys, M. B. (1997) · Nature Medicine · doi:10.1038/nm0897-855 · Cited by 266
Neuronal hyperactivity--A key defect in Alzheimer’s disease?
Busche, M. A., & Konnerth, A. (2015) · BioEssays · doi:10.1002/bies.201500004 · Cited by 266
Neuroprotection by memantine against neurodegeneration induced by β-amyloid(1–40)
Miguel-Hidalgo, J. J., Alvarez, X. A., Cacabelos, R., & Quack, G. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03731-9 · Cited by 265
Barger, S. W., & Basile, A. S. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00075.x · Cited by 264
Seizures accelerate anoxia-induced neuronal death in the neonatal rat hippocampus
Dzhala, V. I., Ben‐Ari, Y., & Khazipov, R. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200010)48:4 · Cited by 82
Alzheimer's disease: a re-examination of the amyloid hypothesis
Neve, R. L., & Robakis, N. K. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(97)01168-5 · Cited by 255
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
Image analysis of β-amyloid load in Alzheimer's disease and relation to dementia severity
Cummings, B. J., & Cotman, C. W. (1995) · The Lancet · doi:10.1016/s0140-6736(95)92053-6 · Cited by 262
APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.407957 · Cited by 268
“For example, crossing apoE-targeted replacement mice (apoE-TR) (9) with PDAPP mice (10) delays plaque deposition from 10 to 18 months, although once detected, plaque levels are greater with APOE4 than APOE3 (3).”
BackgroundA Mathematical Model of the Kinetics of β-Amyloid Fibril Growth from the Denatured State
Pallitto, M. M., & Murphy, R. M. (2001) · Biophysical Journal · doi:10.1016/s0006-3495(01)75831-6 · Cited by 261
Genetic Neurodegenerative Diseases: The Human Illness and Transgenic Models
Price, D. L., Sisodia, S. S., & Borchelt, D. (1998) · Science · doi:10.1126/science.282.5391.1079 · Cited by 258
Search for natural products related to regeneration of the neuronal network
Tohda, C., Kuboyama, T., & Komatsu, K. (2005) · Neurosignals · doi:10.1159/000085384 · Cited by 257
Seabrook, G. R., Smith, D. W., Bowery, B. J., Easter, A., Reynolds, T., Fitzjohn, S. M., Morton, R. A., Zheng, H., Dawson, G. R., SIRINATHSINGHJI, D. J. S., et al. (1999) · Neuropharmacology · doi:10.1016/s0028-3908(98)00204-4 · Cited by 281
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256
Vellas, B. J., Black, R. S., Thal, L. J., Fox, N. C., Daniels, M., McLennan, G., Tompkins, C., Leibman, C. W., Pomfret, M., & Grundman, M. (2009) · Current Alzheimer Research · doi:10.2174/156720509787602852 · Cited by 261
Estus, S., Tucker, H. M., van Rooyen, C., Wright, S., Brigham, E. F., Wogulis, M. D., & Rydel, R. E. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-20-07736.1997 · Cited by 255
Tran, H. T., LaFerla, F. M., Holtzman, D. M., & Brody, D. L. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0858-11.2011 · Cited by 255
Esposito, L., Raber, J., Kekonius, L., Yan, F., Yu, G.-Q., Bien-Ly, N., Puoliväli, J., Scearce-Levie, K., Masliah, E., & Mucke, L. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0482-06.2006 · Cited by 254
Self-citationGordon, D. J., Sciarretta, K. L., & Meredith, S. C. (2001) · Biochemistry · doi:10.1021/bi002416v · Cited by 254
Demattos, R. B., Bales, K. R., Parsadanian, M., O'Dell, M. A., Foss, E. M., Paul, S. M., & Holtzman, D. M. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00889.x · Cited by 254
Bacskai, B. J., Hickey, G. A., Skoch, J. M., Kajdasz, S. T., Wang, Y., Huang, G.-F., Mathis, C. A., Klunk, W. E., & Hyman, B. T. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2034101100 · Cited by 253
Antioxidants as treatment for neurodegenerative disorders
Moosmann, B., & Behl, C. (2002) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.11.10.1407 · Cited by 255
Rockenstein, E. M., McConlogue, L., Tan, H. T., Power, M., Masliah, E., & Mucke, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28257 · Cited by 255
Self-citationActive and passive immunotherapy for neurodegenerative disorders
Brody, D. L., & Holtzman, D. M. (2008) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.31.060407.125529 · Cited by 250
Kubo, T., Nishimura, S., Kumagae, Y., & Kaneko, I. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10391 · Cited by 255
Iwatsubo, T., Saido, T. C., Mann, D. M. A., Lee, V. M.-Y., & Trojanowski, J. Q. (1996) · Europe PMC (PubMed Central) · Cited by 248
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Gordon, M. N., Holcomb, L. A., Jantzen, P. T., DiCarlo, G., Wilcock, D., Boyett, K. W., Connor, K., Melachrino, J., O'Callaghan, J. P., & Morgan, D. (2002) · Experimental Neurology · doi:10.1006/exnr.2001.7754 · Cited by 247
Fiala, M., Zhang, L., Gan, X.-H., Sherry, B. A., Taub, D. D., Graves, M. C., Hama, S., Way, D., Weinand, M. E., Witte, M. H., et al. (1998) · Molecular Medicine · doi:10.1007/bf03401753 · Cited by 250
Kuo, Y., Kokjohn, T. A., Beach, T. G., Sue, L. I., Brune, D. C., Lopez, J. C., Kalback, W. M., Abramowski, D., Sturchler, C., Staufenbiel, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007859200 · Cited by 247
Mechanisms of Aβ mediated neurodegeneration in Alzheimer's disease
Crouch, P. J., Harding, S.-M. E., White, A. R., Camakaris, J., Bush, A. I., & Masters, C. L. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.07.013 · Cited by 254
Cellular signaling roles of TGFβ, TNFα and βAPP in brain injury responses and Alzheimer's disease
Mattson, M. P., Barger, S. W., Furukawa, K., Bruce‐Keller, A. J., Wyss‐Coray, T., Mark, R. J., & Mucke, L. (1997) · Brain Research Reviews · doi:10.1016/s0165-0173(96)00014-8 · Cited by 243
Self-citationGenetics 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
Senile plaques stimulate microglia to release a neurotoxin found in Alzheimer brain
Giulian, D., Haverkamp, L. J., Li, J., Karshin, W. L., Yu, J., Tom, D., Li, X., & Kirkpatrick, J. B. (1995) · Neurochemistry International · doi:10.1016/0197-0186(95)00067-i · Cited by 242
Behavioral characterization of the Tg2576 transgenic model of Alzheimer's disease through 19 months
King, D. L., & Arendash, G. W. (2002) · Physiology & Behavior · doi:10.1016/s0031-9384(02)00639-x · Cited by 250
Pierce, J., Trojanowski, J., Graham, D., Smith, D., & McIntosh, T. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-03-01083.1996 · Cited by 239
“One such transgenic mouse expressing human APP developed spontaneous deposits of A/3 that form amyloid fibrils (Games et al., 1995).”
BackgroundTesseur, I. C., Dorpe, J. V., Spittaels, K., den Haute, C. V., Moechars, D., & LEUVEN, F. V. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64963-2 · Cited by 239
Yamada, K., Tanaka, T., Han, D., Senzaki, K., Kameyama, T., & Nabeshima, T. (1999) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.1999.00408.x · Cited by 238
Mattson, M. P. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02790-6 · Cited by 239
Molecular mechanisms for Alzheimer's disease: implications for neuroimaging and therapeutics
Masters, C. L., Cappai, R., Barnham, K. J., & Villemagne, V. L. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03989.x · Cited by 242
Dewachter, I., Reversé, D., Caluwaerts, N., Ris, L., Kuipéri, C., den Haute, C. V., Spittaels, K., Umans, L., Serneels, L., Thiry, E., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03445.2002 · Cited by 238
JNK3 Perpetuates Metabolic Stress Induced by Aβ Peptides
Yoon, S. O., Park, D. J., Ryu, J. C., Özer, H. G., Tep, C., Shin, Y. J., Lim, T. H., Pastorino, L., Kunwar, A. J., Walton, J. C., et al. (2012) · Neuron · doi:10.1016/j.neuron.2012.06.024 · Cited by 243
Rivastigmine, a New‐Generation Cholinesterase Inhibitor for the Treatment of Alzheimer's Disease
Jann, M. W. (2000) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1592/phco.20.1.1.34664 · Cited by 241
Detection of neuritic plaques in Alzheimer’s disease by magnetic resonance microscopy
Benveniste, H., Einstein, G., Kim, K. R., Hulette, C., & Johnson, G. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.14079 · Cited by 235
Reduced levels of amyloid β-peptide antibody in Alzheimer disease
Du, Y., Dodel, R. C., Hampel, H. J., Büerger, K., Lin, S., Eastwood, B. J., Bales, K. R., Gao, F., Moeller, H. –., Oertel, W. H., et al. (2001) · Neurology · doi:10.1212/wnl.57.5.801 · Cited by 236
Mastrangelo, M. A., & Bowers, W. J. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-81 · Cited by 242
4 Primate Embryonic Stem Cells
Thomson, J. A., & Marshall, V. S. (1997) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(08)60246-x · Cited by 242
Controlling Amyloid β-Peptide Fibril Formation with Protease-stable Ligands
Tjernberg, L. O., Lilliehöök, C., Callaway, D. J. E., Näslund, J., Hahne, S., Thyberg, J., Terenius, L. Y., & Nordstedt, C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.19.12601 · Cited by 233
Estradiol protects against β-amyloid (25–35)-induced toxicity in SK-N-SH human neuroblastoma cells
Green, P. S., Gridley, K. E., & Simpkins, J. W. (1996) · Neuroscience Letters · doi:10.1016/s0304-3940(96)13148-7 · Cited by 231
Reversal of long-term dendritic spine alterations in Alzheimer disease models
Smith, D. L., Pozueta, J., Gong, B., Arancio, O., & Shelanski, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908706106 · Cited by 229
Inflammation in the nervous system
Perry, V. H., Bell, M. D., Brown, H. C., & Matyszak, M. K. (1995) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(95)80069-7 · Cited by 229
Animal models in the drug discovery pipeline for Alzheimer's disease
Dam, D. V., & Deyn, P. P. D. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01299.x · Cited by 239
Lanz, T. A., Carter, D. B., & Merchant, K. M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00079-2 · Cited by 227
King, D. L., Arendash, G. W., Crawford, F., Sterk, T., Menendez, J., & MULLAN, M. J. (1999) · Behavioural Brain Research · doi:10.1016/s0166-4328(99)00037-6 · Cited by 230
Raymond, S. B., Treat, L. H., Dewey, J. D., McDannold, N. J., Hynynen, K., & Bacskai, B. J. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002175 · Cited by 235
Presenilin-1 Knockin Mice Reveal Loss-of-Function Mechanism for Familial Alzheimer’s Disease
Xia, D., Watanabe, H., Wu, B., Lee, S. H., Li, Y., Tsvetkov, E., Bolshakov, V. Y., Shen, J., & Kelleher, R. J. (2015) · Neuron · doi:10.1016/j.neuron.2015.02.010 · Cited by 234
Metadata
- Authors
- Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., Guido, T., Hagopian, S., Johnson-Wood, K., Khan, K., Lee, M., Leibowitz, P., Lieberburg, I., Little, S., Masliah, E., McConlogue, L., Montoya-Zavala, M., Mucke, L., Paganini, L., Penniman, E., Power, M., Schenk, D., Seubert, P., Snyder, B., Soriano, F., Tan, H., Vitale, J., Wadsworth, S., Wolozin, B., & Zhao, J.
- Affiliations
- Worcester Polytechnic Institute (US)
- University of Massachusetts Chan Medical School (US)
- Eli Lilly (United States) (US)
- Boston Children's Hospital (US)
- University of California San Diego (US)
- Scripps Research Institute (US)
- ORCID
- Venue
- Nature
- Published
- 1995-02
- Volume
- 373
- Issue
- 6514
- Pages
- 523-527
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2126800086
- Cited by
- 2,516
- References
- 28
- Citations by year
- 2026: 17 · 2025: 34 · 2024: 55 · 2023: 38 · 2022: 42 · 2021: 52 · 2020: 55 · 2019: 42 · 2018: 35 · 2017: 54 · 2016: 69 · 2015: 64 · 2014: 58 · 2013: 75 · 2012: 73
- FWCI
- 101.17
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- Alzheimer's disease, amyloid precursor protein, transgenic mice, amyloid-beta, amyloid plaques, neuritic plaques, synaptic loss, astrocyte activation, microglial activation, animal models of Alzheimer's disease, thioflavin S staining
- MeSH terms
- Alzheimer Disease, Animals, Base Sequence, Brain, Humans, Immunoenzyme Techniques, Mice, Transgenic, Molecular Sequence Data, Mutation, Platelet-Derived Growth Factor, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, DNA Primers, Microscopy, Confocal, Mice
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