The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Accelerated Amyloid Deposition in the Brains of Transgenic Mice Coexpressing Mutant Presenilin 1 and Amyloid Precursor Proteins
Open accessAbstract
Missense mutations in two related genes, termed presenilin 1 (PS1) and presenilin 2 (PS2), cause dementia in a subset of early-onset familial Alzheimer's disease (FAD) pedigrees. In a variety of experimental in vitro and in vivo settings, FAD-linked presenilin variants influence the processing of the amyloid precursor protein (APP), leading to elevated levels of the highly fibrillogenic Abeta1-42 peptides that are preferentially deposited in the brains of Alzheimer Disease (AD) patients. In this report, we demonstrate that transgenic animals that coexpress a FAD-linked human PS1 variant (A246E) and a chimeric mouse/human APP harboring mutations linked to Swedish FAD kindreds (APP swe) develop numerous amyloid deposits much earlier than age-matched mice expressing APP swe and wild-type Hu PS1 or APP swe alone. These results provide evidence for the view that one pathogenic mechanism by which FAD-linked mutant PS1 causes AD is to accelerate the rate of beta-amyloid deposition in brain.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“However, APP mice develop dystrophic neurites immediately around plaques (50), suggesting that this neuronal pathology is independent of cell death.”
From Attenuating astrocyte activation accelerates plaque pathogenesis in APP/PS1 mice (2013) · cites this paper as [50]
In the citing paper
“However, such studies have not definitively identified which Aβ species are responsible for seeding amyloid deposition in either the parenchyma or vasculature.”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Borchelt et al., 1997
In the citing paper
“Increasing relative Aβ42 levels lowers the age when deposition first occurs, increases the amount of diffuse Aβ, and promotes parenchymal versus cerebrovascular deposition.”
From Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice (2005) · cites this paper as Borchelt et al., 1997
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 [24]
Citations
Cites
1 retracted
Familial Alzheimer's disease associated with S182 codon 286 mutation
Chapman, J., Asherov, A., Wang, N., Treves, T. A., Korczyn, A. D., & Goldfarb, L. G. (1995) · The Lancet · doi:10.1016/s0140-6736(95)91723-3 · Cited by 25
RetractedMcKhann, 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
Self-citationGoate, 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
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease
Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., et al. (1995) · Nature · doi:10.1038/375754a0 · Cited by 4,051
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
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
Self-citationRogaev, E. I., Sherrington, R., Rogaeva, E. A., Levesque, G., Ikeda, M., Liang, Y., Chi, H., Lin, C., Holman, K., Tsuda, T., et al. (1995) · Nature · doi:10.1038/376775a0 · Cited by 2,052
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Research works printed but not linked: 2
- Barelli, 1997, Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid β peptides, Mol. Med, in press
- Kim, 1990, Detection and quantitation of amyloid β-peptide with 2 monoclonal antibodies, Neurosci. Res. Commun, 7, 113
Cited by
Sorted by citations
Items 301–400 of 1,000
Kwan, A. C., Duff, K., Gouras, G. K., & Webb, W. W. (2009) · Optics Express · doi:10.1364/oe.17.003679 · Cited by 90
Boutajangout, A., Authelet, M., Blanchard, V., Touchet, N., Tremp, G. L., Pradier, L., & Brion, J. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.09.007 · Cited by 90
Age-Dependent and Tissue-Related Glutathione Redox Status in a Mouse Model of Alzheimer's Disease
Zhang, C., Rodríguez, C., Spaulding, J., Aw, T. Y., & Feng, J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111244 · Cited by 89
Kurt, M. A., Davies, D. C., Kidd, M., Duff, K., Rolph, S. C., JENNINGS, K. H., & Howlett, D. R. (2001) · Experimental Neurology · doi:10.1006/exnr.2001.7717 · Cited by 89
Huang, Q., Aluise, C. D., Gururaj Joshi, A., Rukhsana Sultana, A., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22422 · Cited by 89
Thomas, P., Wang, Y., Zhong, J., Kosaraju, S. L., O’Callaghan, N. J., Zhou, X., & Fenech, M. F. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.10.016 · Cited by 89
Puig, B., Gómez‐Isla, T., Ribé, E. M., Cuadrado‐Tejedor, M., Torrejón-Escribano, B., Dalfó, E., & Ferrer, I. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00569.x · Cited by 88
Esmaeili, M. A., Panahi, M., Yadav, S., Hennings, L. J., & Kiaei, M. (2013) · International Journal of Experimental Pathology · doi:10.1111/iep.12006 · Cited by 87
Park, K. H. J., Hallows, J. L., Chakrabarty, P., Davies, P., & Vincent, I. J. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0186-07.2007 · Cited by 87
Tran, H. T., Sanchez, L., Esparza, T. J., & Brody, D. L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025475 · Cited by 86
Nigrostriatal Dysfunction in Familial Alzheimer's Disease-Linked APPswe/PS1ΔE9 Transgenic Mice
Perez, S. E., Lazarov, O., Koprich, J. B., Chen, E., Rodriguez‐Menendez, V., Lipton, J. W., Sisodia, S. S., & Mufson, E. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2773-05.2005 · Cited by 86
Self-citationRole of Synucleins in Alzheimer’s Disease
Crews, L. A., Tsigelny, I. F., Hashimoto, M., & Masliah, E. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9073-6 · Cited by 85
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
Transgenic mouse models of Alzheimer's disease
Hock, B. J., & Lamb, B. T. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02449-0 · Cited by 85
Lehman, E. J. H. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg322 · Cited by 85
(2012) · Progress in Molecular Biology and Translational Science · doi:10.1016/b978-0-12-385883-2.00006-0 · Cited by 84
Filali, M., Lalonde, R., & Rivest, S. (2011) · Physiology & Behavior · doi:10.1016/j.physbeh.2011.05.023 · Cited by 85
Murine models of Alzheimer's disease and their use in developing immunotherapies
Wısnıewskı, T., & Sigurdsson, E. M. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.05.004 · Cited by 84
Mody, N., Agouni, A., Mcilroy, G. D., Platt, B., & Delibegović, M. (2011) · Diabetologia · doi:10.1007/s00125-011-2160-2 · Cited by 84
Alzheimers Disease: Interactions Between Cholinergic Functions and β- amyloid
Yan, Z., & Feng, J. (2004) · Current Alzheimer Research · doi:10.2174/1567205043331992 · Cited by 84
Mifflin, M. A., Winslow, W., Surendra, L., Tallino, S., Vural, A. S., & Velázquez, R. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.01.018 · Cited by 84
Hölscher, C. (2005) · Reviews in the Neurosciences · doi:10.1515/revneuro.2005.16.3.181 · Cited by 83
Lee, J., Lau, K., Perkinton, M. S., Standen, C. L., Shemilt, S. J. A., Mercken, L., Cooper, J. D., McLoughlin, D. M., & Miller, C. C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300503200 · Cited by 83
Modeling Alzheimer's disease with non-transgenic rat models
Lecanu, L., & Papadopoulos, V. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt171 · Cited by 83
Silva-Abreu, M., Calpena, A. C., Andrés‐Benito, P., Aso, E., Romero, I. A., Roig-Carles, D., Gromnicova, R., Espina, M., Ferrer, I., García, M. L., et al. (2018) · International Journal of Nanomedicine · doi:10.2147/ijn.s171490 · Cited by 83
Alzheimer's Disease and Amyloid: Culprit or Coincidence?
Skaper, S. D. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00011-9 · Cited by 82
Savonenko, A. V., Xu, G. M., Price, D. L., Borchelt, D. R., & Markowska, A. L. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(02)00012-8 · Cited by 63
Self-citationRofina, J., Singh, K., Skoumalova-Vesela, A., van Ederen, A. M., van Asten, A. J., Wilhelm, J., & Gruys, E. (2004) · Amyloid · doi:10.1080/13506120412331285779 · Cited by 82
Mckean, N. E., Handley, R. R., & Snell, R. G. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222313168 · Cited by 81
ROCKENSTEIN, E., CREWS, L., & MASLIAH, E. (2007) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2007.08.013 · Cited by 65
Oxidative damage in brain from human mutant APP/PS-1 double knock-in mice as a function of age
Abdul, H. M., Rukhsana Sultana, A., Clair, D. K. S., Markesbery, W. R., & Butterfield, D. A. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.08.012 · Cited by 81
Hickman, S. E., Allison, E. K., Coleman, U., Kingery-Gallagher, N. D., & El Khoury, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02780 · Cited by 80
Lee, S., Choi, B., Kim, J., LaFerla, F. M., Park, J. H. Y., Han, J., Lee, K. W., & Kim, J. (2018) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201800240 · Cited by 80
Ho, A., Liu, X., & Südhof, T. C. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2481-08.2008 · Cited by 80
Knafo, S., Venero, C., Merino‐Serrais, P., Fernaud-Espinosa, I., González‐Soriano, J., Ferrer, I., Santpere, G., & DeFelipe, J. (2009) · The Journal of Pathology · doi:10.1002/path.2565 · Cited by 80
Gene Vaccination to Bias the Immune Response to Amyloid-β Peptide as Therapy for Alzheimer Disease
Qu, B. (2004) · Archives of Neurology · doi:10.1001/archneur.61.12.1859 · Cited by 80
Ingram, D. K., & Jucker, M. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00033-0 · Cited by 80
APP transgenic mice: their use and limitations
Balducci, C., & Forloni, G. (2011) · NeuroMolecular Medicine · doi:10.1007/s12017-010-8141-7 · Cited by 79
Agca, C., Fritz, J. J., Walker, L. C., Levey, A. I., Chan, A. W. S., Lah, J. J., & Ağca, Y. (2008) · BMC Neuroscience · doi:10.1186/1471-2202-9-28 · Cited by 79
Watanabe, T., Yamagata, N., Takasaki, K., Sano, K., Hayakawa, K., Katsurabayashi, S., Egashira, N., 三島, 健., Iwasaki, K., & Fujiwara, M. (2008) · Brain Research · doi:10.1016/j.brainres.2008.10.029 · Cited by 79
Redundant Gs-coupled serotonin receptors regulate amyloid-β metabolism in vivo
Fisher, J. R., Wallace, C. E., Tripoli, D. L., Sheline, Y. I., & Cirrito, J. R. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0112-5 · Cited by 79
Heikkinen, T., Kalesnykas, G., Rissanen, A., Tapiola, T., Iivonen, S., Wang, J., Chaudhuri, J. D., Tanila, H., Miettinen, R. A., & Puoliväli, J. T. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.01.015 · Cited by 79
Hori, Y., Takeda, S., Cho, H., Wegmann, S., Shoup, T. M., Takahashi, K., Irimia, D., Elmaleh, D. R., Hyman, B. T., & Hudry, E. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.586602 · Cited by 78
“cursor protein gene containing the Swedish mutation K594N/ M595L as well as the Presenilin 1 gene deleted for exon 9, both under the control of the prion promoter (35).”
BackgroundSt‐Pierre, M., Carrier, M., Ibáñez, F. G., Šimončičová, E., Wallman, M., Vallières, L., Parent, M., & Tremblay, M. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02595-8 · Cited by 80
Frye, C. A., & Walf, A. A. (2007) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2007.09.008 · Cited by 78
Dewachter, I., Dorpe, J. V., Spittaels, K., Tesseur, I. C., den Haute, C. V., Moechars, D., & LEUVEN, F. V. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00149-2 · Cited by 78
Aso, E., Andrés‐Benito, P., & Ferrer, I. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160533 · Cited by 77
Discovery and development of biomarkers of neurological disease
Dunckley, T. L., Coon, K. D., & Stephan, D. A. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(04)03353-7 · Cited by 77
Preclinical validation of a potent γ-secretase modulator for Alzheimer’s disease prevention
Rynearson, K. D., Ponnusamy, M., Prikhodko, O., Xie, Y., Zhang, C., Nguyen, P., Hug, B., Sawa, M., Becker, A., Spencer, B., et al. (2021) · Journal of Experimental Medicine · doi:10.1084/jem.20202560 · Cited by 76
Function and Dysfunction of the Presenilins
Sisodia, S. S., Kim, S. H., & Thinakaran, G. (1999) · The American Journal of Human Genetics · doi:10.1086/302475 · Cited by 76
Self-citationPoon, C. H., Wang, Y., Fung, M., Zhang, C., & Lim, L. W. (2020) · Aging and Disease · doi:10.14336/ad.2019.1026 · Cited by 76
Presenilin transgenic mice as models of Alzheimer’s disease
Elder, G. A., Sosa, M. A. G., Gasperi, R. D., Dickstein, D. L., & Hof, P. R. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0227-3 · Cited by 76
Alzheimer's disease, the nematode Caenorhabditis elegans, and ginkgo biloba leaf extract
Luo, Y. (2006) · Life Sciences · doi:10.1016/j.lfs.2005.12.004 · Cited by 76
Capsoni, S., Marinelli, S., Ceci, M., Vignone, D., Amato, G., Malerba, F., Paoletti, F., Meli, G., Viegi, A., Pavone, F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0037555 · Cited by 76
Therapeutic potential of nuclear receptor agonists in Alzheimer's disease
Moutinho, M., & Landreth, G. E. (2017) · Journal of Lipid Research · doi:10.1194/jlr.r075556 · Cited by 76
Presenilin 1 Suppresses the Function of C-Jun Homodimers via Interaction with Qm/Jif-1
Imafuku, I., Masaki, T., Waragai, M., Takeuchi, S., Kawabata, M., Hirai, S., Ohno, S., Nee, L. E., Lippa, C. F., Kanazawa, I., et al. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.1.121 · Cited by 76
Neuron Loss in Alzheimer’s Disease: Translation in Transgenic Mouse Models
Wirths, O., & Zampar, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21218144 · Cited by 75
“, 5XFAD [46], APPswe/PS1dE9 [72], APP/PS1 [49], PS2APP [73], APP/PS1KI [52]), APP and Tau (such as APP/Tau [55]), or triple transgenic mice expressing APP, PS1/2, and Tau (e.”
Baruch, K., Kertser, A., Porat, Z., & Schwartz, M. (2015) · The EMBO Journal · doi:10.15252/embj.201591468 · Cited by 75
Wild-type Presenilin 1 Protects against Alzheimer Disease Mutation-induced Amyloid Pathology
Wang, R., Wang, B., He, W., & Zheng, H. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512574200 · Cited by 75
Implication of APP Secretases in Notch Signaling
Hartmann, D., Tournoy, J., Säftig, P., Annaert, W. G., & Strooper, B. D. (2001) · Journal of Molecular Neuroscience · doi:10.1385/jmn:17:2:171 · Cited by 75
Gd-nanoparticles functionalization with specific peptides for ß-amyloid plaques targeting
Plissonneau, M., Pansieri, J., Heinrich, L., Morfin, J., Stransky-Heilkron, N., Rivory, P., Mowat, P., Dumoulin, M., Cohen, R., Allémann, É., et al. (2016) · Journal of Nanobiotechnology · doi:10.1186/s12951-016-0212-y · Cited by 74
Mondragón‐Rodríguez, S., Perry, G. L., Zhu, X., & Boehm, J. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/630182 · Cited by 74
Involvement of Prostaglandin E2 in Production of Amyloid-β Peptides Both in Vitro and in Vivo
Hoshino, T., Nakaya, T., Homan, T., Tanaka, K., Sugimoto, Y., Araki, W., Narita, M., Narumiya, S., Suzuki, T., & Mizushima, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703087200 · Cited by 74
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
Aso, E., Andrés‐Benito, P., Carmona, M., Maldonado, R. J., & Ferrer, I. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150913 · Cited by 73
Reddy, P. H., & McWeeney, S. K. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.04.014 · Cited by 73
Li, W., Hoffman, P. N., Stirling, W. L. H., Price, D. L., & Lee, M. K. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02166.x · Cited by 73
Self-citationAmyloid precursor protein-induced axonopathies are independent of amyloid-β peptides
Stokin, G. B., Almenar-Queralt, A., Gunawardena, S., Rodrigues, E. M., Falzone, T., Kim, J., Lillo, C., Mount, S. L., Roberts, E. A., McGowan, E., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn240 · Cited by 72
Intravenous Delivery of Targeted Liposomes to Amyloid-β Pathology in APP/PSEN1 Transgenic Mice
Tanifum, E. A., Dasgupta, I., Srivastava, M., Bhavane, R. C., Sun, L., Berridge, J., Pourgarzham, H., Kamath, R., Espinosa, G., Cook, S. C., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048515 · Cited by 72
Hong, X., Liu, J., Zhu, G., Zhuang, Y., Suo, H., Wang, P., Huang, D., Xu, J., Huang, Y., Yu, M., et al. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt501 · Cited by 73
Smit, T., Deshayes, N. A. C., Borchelt, D. R., Kamphuis, W., Middeldorp, J., & Hol, E. M. (2021) · Glia · doi:10.1002/glia.23981 · Cited by 71
Self-citationZheng, Y. M., Deng, Y., Gao, J.-M., Lv, C., Lang, L.-H., Shi, J., Yu, C., & Gong, Q. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0300-2 · Cited by 71
Olive Biophenols Reduces Alzheimer’s Pathology in SH-SY5Y Cells and APPswe Mice
Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010125 · Cited by 71
Pardon, M., & Rattray, I. (2008) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2008.03.005 · Cited by 70
Watt, G., Shang, K., Zieba, J., Olaya, J. C., Li, H., Garner, B., & Karl, T. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191242 · Cited by 70
Novel behavioural characteristics of the APPSwe/PS1ΔE9 transgenic mouse model of Alzheimer's disease
Cheng, D., Logge, W., Low, J. K., Garner, B., & Karl, T. (2013) · Behavioural Brain Research · doi:10.1016/j.bbr.2013.02.008 · Cited by 69
Paulson, J. B., Ramsden, M., Forster, C. L., Sherman, M. A., McGowan, E. M., & Ashe, K. H. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080175 · Cited by 69
Zhu, M., Allard, J. S., Zhang, Y., Perez, E., Spangler, E. L., Becker, K. G., & Rapp, P. R. (2014) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000060 · Cited by 69
Lee, J., Lau, K., Perkinton, M. S., Standen, C. L., Rogelj, B., Falinska, A. M., McLoughlin, D. M., & Miller, C. C. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405602200 · Cited by 69
β-Site APP Cleaving Enzyme mRNA Expression in APP Transgenic Mice
Irizarry, M. C., Locascio, J. J., & Hyman, B. T. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63955-7 · Cited by 69
Go, J., Chang, D., Ryu, Y., Park, H., Lee, I.-B., Noh, J., Hwang, D. Y., Kim, B., Kim, K., & Lee, C. (2020) · Nutrition Research · doi:10.1016/j.nutres.2020.12.010 · Cited by 69
Williamson, R., van Aalten, L., Mann, D. M. A., Platt, B., Plattner, F., Bedford, L., Mayer, J., Howlett, D. R., Usardi, A., Sutherland, C. D., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110617 · Cited by 68
Untargeted lipidomics reveals progression of early Alzheimer’s disease in APP/PS1 transgenic mice
Zhang, X., Liu, W., Zan, J., Wu, C., & Tan, W. (2020) · Scientific Reports · doi:10.1038/s41598-020-71510-z · Cited by 69
Catecholaminergic neuronal loss in locus coeruleus of aged female dtg APP/PS1 mice
O’Neil, J. N., Mouton, P. R., Tizabi, Y., Ottinger, M. A., Lei, D.-L., Ingram, D. K., & Manaye, K. F. (2007) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2007.05.008 · Cited by 68
Lawlor, P. A., Bland, R. J., Das, P., Price, R. W., Holloway, V., Smithson, L., Dicker, B. L., During, M. J., Young, D., & Golde, T. E. (2007) · Molecular Neurodegeneration · doi:10.1186/1750-1326-2-11 · Cited by 67
Astrocyte‐neuronal network interplay is disrupted in Alzheimer's disease mice
Lines, J., Baraibar, A. M., Fang, C. C., Martín, E. D., Aguilar, J., Lee, M. K., Araque, A., & Kofuji, P. (2021) · Glia · doi:10.1002/glia.24112 · Cited by 67
Self-citationAβ42 gene vaccination reduces brain amyloid plaque burden in transgenic mice
Qu, B., Boyer, P. J., Johnston, S. A., Hynan, L. S., & Rosenberg, R. N. (2006) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2006.02.006 · Cited by 67
Impact of RTN3 Deficiency on Expression of BACE1 and Amyloid Deposition
Shi, Q., Ge, Y., Sharoar, M. G., He, W., Xiang, R., Zhang, Z., Hu, X., & Yan, R. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.1588-14.2014 · Cited by 67
Stanley, M., Macauley, S. L., Caesar, E. E., Koscal, L. J., Moritz, W., Robinson, G. O., Roh, J., Keyser, J., Jiang, H., & Holtzman, D. M. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2119-16.2016 · Cited by 67
Li, Q., Navakkode, S., Rothkegel, M., Soong, T. W., Sajikumar, S., & Körte, M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1613700114 · Cited by 67
Zaman, S. H., Parent, A., Laskey, A., Lee, M. K., Borchelt, D., Sisodia, S. S., & Malinow, R. (2000) · Neurobiology of Disease · doi:10.1006/nbdi.1999.0271 · Cited by 67
Self-citationProgress toward valid transgenic mouse models for Alzheimer’s disease
Guénette, S. Y., & Tanzi, R. E. (1999) · Neurobiology of Aging · doi:10.1016/s0197-4580(99)00042-1 · Cited by 67
Lee, G. D., Aruna, J. H., Barrett, P. M., Lei, D.-L., Ingram, D. K., & Mouton, P. R. (2005) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2004.11.024 · Cited by 67
Pinning down phosphorylated tau and tauopathies
Lim, J., & Lu, K. P. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.10.003 · Cited by 67
Roberson, E. D., & Kao, A. W. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511581410.010 · Cited by 67
APP transgenic mice for modelling behavioural and psychological symptoms of dementia (BPSD)
Lalonde, R., Fukuchi, K., & Strazielle, C. (2012) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2012.02.011 · Cited by 66
Sola, I., Aso, E., Frattini, D., López‐González, I., Espargaró, A., Sabaté, R., Pietro, O. D., Luque, F. J., Clos, M. V., Ferrer, I., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b00624 · Cited by 66
Hoeijmakers, L., Lesuis, S. L., Krugers, H. J., Lucassen, P. J., & Kőrösi, A. (2018) · Neurobiology of Stress · doi:10.1016/j.ynstr.2018.02.003 · Cited by 66
Nie, J., Jiang, L.-S., Zhang, Y., Tian, Y., Li, L., Lu, Y.-L., Yang, W.-J., & Shi, J. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.01479 · Cited by 66
Howlett (2008) · PubMed · doi:10.14670/hh-23.67 · Cited by 65
Metadata
- Authors
- 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.
- Affiliations
- Johns Hopkins University (US)
- Frederick National Laboratory for Cancer Research (US)
- Corresponding author
- Borchelt, David R
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 1997-10
- Volume
- 19
- Issue
- 4
- Pages
- 939-945
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2062214806
- Cited by
- 1,023
- References
- 52
- Citations by year
- 2026: 9 · 2025: 13 · 2024: 16 · 2023: 17 · 2022: 18 · 2021: 36 · 2020: 35 · 2019: 25 · 2018: 30 · 2017: 38 · 2016: 29 · 2015: 38 · 2014: 33 · 2013: 44 · 2012: 46
- FWCI
- 17.54
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuron (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- National Institute on Aging (AG 14248, P50AG005146, P01AG014248, AG 05146)
- National Institute of Neurological Disorders and Stroke (NS-20471)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- presenilin 1, presenilin 2, amyloid precursor protein, familial Alzheimer's disease, amyloid-beta deposition, transgenic mice, amyloid-beta 42, amyloidosis, Alzheimer's disease pathogenesis
- MeSH terms
- Aging, Alzheimer Disease, Amyloid, Animals, Brain, Family, Humans, Membrane Proteins, Mice, Transgenic, Pedigree, Recombinant Fusion Proteins, Sweden, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Mice, Presenilin-1
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review