The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Abstract
A locus segregating with familial Alzheimer's disease (AD) has been mapped to chromosome 21, close to the amyloid precursor protein (APP) gene. Recombinants between the APP gene and the AD locus have been reported which seemed to exclude it as the site of the mutation causing familial AD. But recent genetic analysis of a large number of AD families has demonstrated that the disease is heterogeneous. Families with late-onset AD do not show linkage to chromosome 21 markers. Some families with early-onset AD show linkage to chromosome 21 markers, but some do not. This has led to the suggestion that there is non-allelic genetic heterogeneity even within early onset familial AD. To avoid the problems that heterogeneity poses for genetic analysis, we have examined the cosegregation of AD and markers along the long arm of chromosome 21 in a single family with AD confirmed by autopsy. Here we demonstrate that in this kindred, which shows linkage to chromosome 21 markers, there is a point mutation in the APP gene. This mutation causes an amino-acid substitution (Val----Ile) close to the carboxy terminus of the beta-amyloid peptide. Screening other cases of familial AD revealed a second unrelated family in which this variant occurs. This suggests that some cases of AD could be caused by mutations in the APP gene.
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
“FAD mutations in APP that cluster near the 𝛃 - and 𝛄 -secretase cleavage sites either elevate the production of total A 𝛃 , as is the case with the K670N/ M671L substitution [Swedish mutation (Mullan et al., 1992a)], or increase the generation of A 𝛃 42 specifically, as occurs with the I716V [Florida mutation (Eckman et al., 1997)] and V717I [London mutation (Goate et al., 1991)] substitutions.”
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 Goate et al., 1991
In the citing paper
“The 5XFAD mouse, along with the APPSLPS1KI, is one of a few known mouse models that exhibits significant neuron loss in addition to displaying other AD hallmarks such as amyloid plaques [10,11,16].”
From Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation (2013) · cites this paper as [10]
In the citing paper
“Frank neuron loss has been observed in two aggressive amyloid plaque transgenic mouse models that also exhibit accumulation of intraneuronal Aβ42 prior to plaque formation: the 5XFAD and APPSLPS1K1 lines [10,11].”
From Neuron loss in the 5XFAD mouse model of Alzheimer’s disease correlates with intraneuronal Aβ42 accumulation and Caspase-3 activation (2013) · cites this paper as [10]
In the citing paper
“Early onset Alzheimer's disease can be caused by mutations in the APP (Chartier-Harlin et al., 1991;Goate et al., 1991;Murrell et al., 1991;Mullan et al., 1992), presenilin 1 (PS1) (Sherrington et al., 1995), and presenilin 2 (PS2) (Levy-Lahad et al., 1995) genes.”
From Age-Dependent Changes in Brain, CSF, and Plasma Amyloid β Protein in the Tg2576 Transgenic Mouse Model of Alzheimer's Disease (2001) · cites this paper as Goate et al., 1991
In the citing paper
“The amyloid cascade hypothesis of Alzheimer disease (AD), which proposes that deposition of the amyloid-β (Aβ) peptide in the brain is a central event in disease pathology (Figure 1), is strongly supported by neuropathological and human genetic evidence”
From The amyloid hypothesis in Alzheimer disease: new insights from new therapeutics (2022) · cites this paper as [2]
In the citing paper
“Mutations in APP, presenilin 1 (PSEN1) and PSEN2 genes that increase Aβ production, elevate Aβ42/Aβ40 ratio and promote plaque formation cause autosomal dominant early-onset familial AD (FAD)”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [38]
In the citing paper
“Less than 1% of all AD cases are early-onset with symptoms developed at an age of 50 s and earlier, and caused by gene mutations in APP, PSEN1 or PSEN2.7,38,39”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [38]
In the citing paper
“This hypothesis gained favor in the 1990s after several gene mutations directly responsible for aberrant Aβ accumulation (APP, PSEN1, PSEN2) were found to underlie rare familial forms of early-onset AD [20–22].”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [21]
Citations
Cites
A simple method for displaying the hydropathic character of a protein
Kyte, J., & Doolittle, R. F. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90515-0 · Cited by 22,927
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Garnier, J., Osguthorpe, D. J., & Robson, B. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90297-8 · Cited by 4,523
Strategies for multilocus linkage analysis in humans.
Lathrop, M. G., Lalouel, J.-M., Julier, C., & Ott, J. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.11.3443 · Cited by 2,560
Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)91209-9 · Cited by 1,693
Amyloid β Protein Gene: cDNA, mRNA Distribution, and Genetic Linkage Near the Alzheimer Locus
Tanzi, R. E., Gusella, J. F., Watkins, P. C., Bruns, G. A. P., St George-Hyslop, P., Van Keuren, M. L., Patterson, D., Pagan, S., Kurnit, D. M., & Neve, R. L. (1987) · Science · doi:10.1126/science.2949367 · Cited by 1,611
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 1,399
Goldgaber, D., Lerman, M. I., McBride, O. W., Saffiotti, U., & Gajdusek, D. C. (1987) · Science · doi:10.1126/science.3810169 · Cited by 1,359
The Genetic Defect Causing Familial Alzheimer's Disease Maps on Chromosome 21
George‐Hyslop, P. S., Tanzi, R. E., Polinsky, R. J., Haines, J. L., Nee, L. E., Watkins, P. C., Myers, R. H., Feldman, R. G., Pollen, D. A., Drachman, D. A., et al. (1987) · Science · doi:10.1126/science.2880399 · Cited by 1,160
Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
Gaboriaud, C., Bissery, V., Benchetrit, T., & Mornon, J. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)80439-8 · Cited by 618
Flagged first, then by citations
Cited by
Sorted by citations
Items 701–800 of 1,066
de Silva, H. A. R., Jen, A., Wickenden, C., Jen, L., Wilkinson, S. L., & Patel, A. J. (1997) · Molecular Brain Research · doi:10.1016/s0169-328x(97)00045-4 · Cited by 141
Phosphatidylinositol and inositol involvement in alzheimer amyloid-β fibril growth and arrest
McLaurin, J., Franklin, T., Chakrabartty, A., & Fraser, P. E. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1677 · Cited by 141
Prince, J. A., Feuk, L., Sawyer, S. L., Gottfries, J., Ricksten, A., Nägga, K., Bogdanović, N., Blennow, K., & Brookes, A. J. (2001) · European Journal of Human Genetics · doi:10.1038/sj.ejhg.5200651 · Cited by 141
Deposits of Amyloid β Protein in the Central Nervous System of Transgenic Mice
Wirak, D. O., Bayney, R. M., Ramabhadran, T. V., Fracasso, R. P., Hart, J., Hauer, P., Hsiau, P., Pekar, S. K., Scangos, G. A., Trapp, B. D., et al. (1991) · Science · doi:10.1126/science.1857970 · Cited by 141
Matsuda, S., Giliberto, L., Matsuda, Y., Davies, P., McGowan, E., Pickford, F., Ghiso, J., Frangione, B., & D'Adamio, L. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500217200 · Cited by 141
The genetic landscape of Alzheimer disease
Carmona, S., Hardy, J., & Guerreiro, R. J. (2018) · Handbook of clinical neurology · doi:10.1016/b978-0-444-64076-5.00026-0 · Cited by 140
Self-citationRisk for Alzheimer's disease correlates with transcriptional activity of the APOE gene
Artiga, M. J., Bullido, M. J., Frank, A., Sastre, I., Recuero, M., Garcia, M. A., Lendon, C. L., Han, S. W., Morris, J. C., Vázquez, J., et al. (1998) · Human Molecular Genetics · doi:10.1093/hmg/7.12.1887 · Cited by 140
Self-citationCell “Self‐Eating” (Autophagy) Mechanism in Alzheimer's Disease
Funderburk, S. F., Marcellino, B. K., & Yue, Z. (2010) · Mount Sinai Journal of Medicine: A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20161 · Cited by 139
Seizures in Alzheimer’s disease
Born, H. A. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.11.051 · Cited by 139
van den Bos, H., Spierings, D. C. J., Taudt, A., Bakker, B., Porubskỳ, D., Falconer, E., Novoa, C. A., Halsema, N., Kazemier, H. G., Hoekstra-Wakker, K., et al. (2016) · Genome biology · doi:10.1186/s13059-016-0976-2 · Cited by 139
Maloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 140
In Vivo Effects of ApoE and Clusterin on Amyloid-β Metabolism and Neuropathology
Holtzman, D. M. (2004) · Journal of Molecular Neuroscience · doi:10.1385/jmn:23:3:247 · Cited by 139
MacGowan, S. H., Wilcock, G. K., & Scott, M. (1998) · International Journal of Geriatric Psychiatry · doi:10.1002/(sici)1099-1166(199809)13:9 · Cited by 139
Alzheimer Disease: Current Concepts and Emerging Diagnostic and Therapeutic Strategies
Clark, C. M., & Karlawish, J. H. (2003) · Annals of Internal Medicine · doi:10.7326/0003-4819-138-5-200303040-00010 · Cited by 139
Cruchaga, C., Del‐Aguila, J. L., Saef, B., Black, K., Fernandez, M. V., Budde, J., Ibanez, L., Deming, Y., Kapoor, M., Tosto, G., et al. (2018) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2017.08.013 · Cited by 138
Self-citationTienari, P. J., Ida, N., Ikonen, E., Simons, M., Weidemann, A., Multhaup, G., Masters, C. L., Dotti, C. G., & Beyreuther, K. T. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.4125 · Cited by 138
Sompol, P. M., Ittarat, W., Tangpong, J., Chen, Y., Doubinskaia, I. E., Batinic-Haberle, I., Abdul, H. M., Butterfield, D. A., & Clair, D. K. S. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2008.01.044 · Cited by 137
Genetic analyses of early-onset Alzheimer’s disease using next generation sequencing
Giau, V. V., Bagyinszky, E., Yang, Y. S., Youn, Y. C., An, S. S. A., & Kim, S. (2019) · Scientific Reports · doi:10.1038/s41598-019-44848-2 · Cited by 137
Genetics of Alzheimer’s Disease
Vilatela, M. E. A., López, M., & Yescas, P. (2012) · Archives of Medical Research · doi:10.1016/j.arcmed.2012.10.017 · Cited by 138
Two rare AKAP9 variants are associated with Alzheimer's disease in African Americans
Logue, M. W., Schu, M., Vardarajan, B. N., Farrell, J., Bennett, D. A., Buxbaum, J. D., Byrd, G. S., Ertekin‐Taner, N., Evans, D., Foroud, T., et al. (2014) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2014.06.010 · Cited by 136
Self-citationGenetics of Alzheimer's disease: recent advances
Avramopoulos, D. (2009) · Genome Medicine · doi:10.1186/gm34 · Cited by 136
Pathophysiology of Alzheimer's Disease
Imbimbo, B. P., Lombard, J., & Pomara, N. (2005) · Neuroimaging Clinics of North America · doi:10.1016/j.nic.2005.09.009 · Cited by 137
Modeling Alzheimer's disease with human induced pluripotent stem (iPS) cells
Mungenast, A. E., Siegert, S., & Tsai, L. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.11.010 · Cited by 136
The Role and Therapeutic Targeting of α-, β- and γ-Secretase in Alzheimer's Disease
MacLeod, R., Hillert, E., Cameron, R. T., & Baillie, G. S. (2015) · Future Science OA · doi:10.4155/fso.15.9 · Cited by 136
Neuroglobin: From structure to function in health and disease
Ascenzi, P., di Masi, A., Leboffe, L., Fiocchetti, M., Nuzzo, M. T., Brunori, M., & Marino, M. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.10.004 · Cited by 135
Oxidative Stress, Antioxidants and Neurodegenerative Diseases
Casetta, I., Govoni, V., & Granieri, E. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612054065729 · Cited by 135
Variations in the neuropathology of familial Alzheimer’s disease
Shepherd, C. E., McCann, H., & Halliday, G. M. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0521-4 · Cited by 135
Secretase Targets for Alzheimer's Disease: Identification and Therapeutic Potential
Wolfe, M. S. (2001) · Journal of Medicinal Chemistry · doi:10.1021/jm0004897 · Cited by 135
Mitochondrial dysfunction in sporadic and genetic Alzheimer's disease
Hauptmann, S., Keil, U., Scherping, I., Bonert, A., Eckert, A., & Müller, W. E. (2006) · Experimental Gerontology · doi:10.1016/j.exger.2006.03.012 · Cited by 135
Fukumoto, N., Fujii, T., Combarros, O., Kamboh, M. I., Tsai, S.-J., Matsushita, S., Nacmias, B., Comings, D. E., Arboleda, H., Ingelsson, M., et al. (2009) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.30986 · Cited by 136
Thal, D. R., Griffin, W. S. T., & Braak, H. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00411.x · Cited by 134
Pedersen, W. A., Kloczewiak, M. A., & Blusztajn, J. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.8068 · Cited by 134
Zinc, Carnosine, and Neurodegenerative Diseases
Kawahara, M., Tanaka, K.-I., & Kato-Negishi, M. (2018) · Nutrients · doi:10.3390/nu10020147 · Cited by 134
Wallon, D., The collaborators of the GMAJ project, Rousseau, S., Rovelet‐Lecrux, A., Quillard‐Muraine, M., Guyant‐Maréchal, L., Martinaud, O., Pariente, J., Puel, M., Rollin‐Sillaire, A., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120172 · Cited by 134
Amyloid-β Peptide: Dr. Jekyll or Mr. Hyde?
Puzzo, D., & Arancio, O. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129033 · Cited by 134
Biometals and Their Therapeutic Implications in Alzheimer's Disease
Ayton, S., Lei, P., & Bush, A. I. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0312-z · Cited by 134
Cheng, X., Zhou, W., & Zhang, Y. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2013.10.002 · Cited by 134
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
BACE1 Cleavage Site Selection Critical for Amyloidogenesis and Alzheimer's Pathogenesis
Zhang, S., Wang, Z., Cai, F., Zhang, M., Wu, Y., Zhang, J., & Song, W. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0340-17.2017 · Cited by 133
Amyloid precursor protein gene mutation in early-onset Alzheimer's disease
Duijn, C. V., Hendriks, L., Cruts, M., Hardy, J., Albert Hofman, D., & Broeckhoven, C. V. (1991) · The Lancet · doi:10.1016/0140-6736(91)91611-w · Cited by 133
Self-citationHirano, M., Shtilbans, A., Mayeux, R. P., Davidson, M. M., DiMauro, S., Knowles, J. A., & Schon, E. A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.26.14894 · Cited by 133
Animal models of Alzheimer disease: historical pitfalls and a path forward
Cavanaugh, S. E. (2014) · ALTEX · doi:10.14573/altex.1310071 · Cited by 132
Kocherhans, S., Madhusudan, A., Doehner, J., Breu, K. S., Nitsch, R. M., Fritschy, J.-M., & Knuesel, I. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0418-10.2010 · Cited by 132
Synaptic remodeling during aging and in Alzheimer's disease
Masliah, E., Crews, L., & Hansen, L. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-9s311 · Cited by 132
Genetic markers for diagnosis and pathogenesis of Alzheimer's disease
Kim, D., Yeo, S. H., Park, J.-M., Choi, J. Y., Lee, T.-H., Park, S. Y., Ock, M. S., Eo, J., Kim, H., & Cha, H. (2014) · Gene · doi:10.1016/j.gene.2014.05.031 · Cited by 133
Aβ and tau prion-like activities decline with longevity in the Alzheimer’s disease human brain
Aoyagi, A., Condello, C., Stöhr, J., Yue, W., Rivera, B. M., Lee, J. C., Woerman, A. L., Halliday, G. M., van Duinen, S. G., Ingelsson, M., et al. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aat8462 · Cited by 132
The current status of Alzheimer?s disease genetics: what do we tell the patients?
Bertram, L. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2003.11.018 · Cited by 132
CELLULAR AND MOLECULAR BIOLOGY OF ALZHEIMER'S DISEASE AND ANIMAL MODELS
Price, D. L., & Sisodia, S. S. (1994) · Annual Review of Medicine · doi:10.1146/annurev.med.45.1.435 · Cited by 132
Genome-wide meta-analysis for Alzheimer’s disease cerebrospinal fluid biomarkers
Jansen, I. E., van der Lee, S. J., Gomez-Fonseca, D., de Rojas, I., Dalmasso, M. C., Grenier-Boley, B., Zettergren, A., Mishra, A., Ali, M., Andrade, V., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02454-z · Cited by 132
Genome-Wide Scan of Copy Number Variation in Late-Onset Alzheimer's Disease
Heinzen, E. L., Need, A. C., Hayden, K. M., Chiba‐Falek, O., Roses, A. D., Strittmatter, W. J., Burke, J. R., Hulette, C. M., Welsh-Bohmer, K. A., & Goldstein, D. B. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1212 · Cited by 131
Self-citationThe beta‐amyloid domain is essential for axonal sorting of amyloid precursor protein.
Tienari, P. J., Strooper, B. D., Ikonen, E., Simons, M., Weidemann, A., Czech, C., Hartmann, T., Ida, N., Multhaup, G., Masters, C. L., et al. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00907.x · Cited by 131
Gómez‐Isla, T., Growdon, W. B., McNamara, M. J., Nochlin, D., Bird, T. D., Arango, J. C., Lopera, F., Kosik, K. S., Lantos, P. L., Cairns, N. J., et al. (1999) · Brain · doi:10.1093/brain/122.9.1709 · Cited by 131
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 131
Davis, J. A., Naruse, S., Chen, H., Eckman, C., Younkin, S. G., Price, D. L., Borchelt, D., Sisodia, S. S., & Wong, P. C. (1998) · Neuron · doi:10.1016/s0896-6273(00)80998-8 · Cited by 131
Ubiquitin in health and disease
Mayer, R. J., Arnold, J., László, L., Landon, M., & Lowe, J. S. (1991) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(91)90002-4 · Cited by 131
MATTSON, M. P. (1994) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1994.tb44401.x · Cited by 166
Dysregulation of protein trafficking in neurodegeneration
Wang, X., Huang, T., Bu, G., & Xu, H. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-31 · Cited by 125
Neurodegeneration and the ordered assembly of α-synuclein
Spillantini, M. G., & Goedert, M. (2017) · Cell and Tissue Research · doi:10.1007/s00441-017-2706-9 · Cited by 130
The amyloid cascade and Alzheimer's disease therapeutics: theory versus observation
Castellani, R. J., Plascencia‐Villa, G., & Perry, G. L. (2019) · Laboratory Investigation · doi:10.1038/s41374-019-0231-z · Cited by 130
Role of Phosphorylation of Alzheimer’s Amyloid Precursor Protein during Neuronal Differentiation
Ando, K., Oishi, M., Takeda, S., Iijima, K., Isohara, T., Nairn, A. C., Kirino, Y., Greengard, P., & Suzuki, T. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-11-04421.1999 · Cited by 130
Hardy, J. (1992) · Nature Genetics · doi:10.1038/ng0792-233 · Cited by 130
Self-citationAlzheimer‐associated presenilin‐2 confers increased sensitivity to poptosis in PC12 cells
Deng, G., Pike, C. J., & Cotman, C. W. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01142-8 · Cited by 130
The pursuit of susceptibility genes for Alzheimer's disease: progress and prospects
Sleegers, K., Lambert, J.-C., Bertram, L., Cruts, M., Amouyel, P., & Van Broeckhoven, C. (2010) · Trends in Genetics · doi:10.1016/j.tig.2009.12.004 · Cited by 129
Protein misfolding disorders and macroautophagy
Menzies, F. M., Moreau, K., & Rubinsztein, D. C. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.10.010 · Cited by 129
Cortical Odor Processing in Health and Disease
Wilson, D. A., Xu, W., Sadrian, B., Courtiol, E., Cohen, Y., & Barnes, D. C. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63350-7.00011-5 · Cited by 129
van Duijn, C. M., Clayton, D. G., Chandra, V., Fratiglioni, L., Graves, A. B., Heyman, A., Jorm, A. F., Kokmen, E., Kondo, K., Mortimer, J. A., et al. (1994) · Genetic Epidemiology · doi:10.1002/gepi.1370110609 · Cited by 129
Lamb, B. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.9.1535 · Cited by 128
Examination of the current top candidate genes for AD in a genome-wide association study
Feulner, T. M., Laws, S. M., Friedrich, P., Wagenpfeil, S., Wurst, S. H. R., Riehle, C., Kuhn, K. A., Krawczak, M., Schreiber, S., Nikolaus, S., et al. (2010) · Molecular Psychiatry · doi:10.1038/mp.2008.141 · Cited by 128
Differential contribution of microglia and monocytes in neurodegenerative diseases
Baufeld, C., O'Loughlin, E. K., Calcagno, N., Madore, C., & Butovsky, O. (2017) · Journal of Neural Transmission · doi:10.1007/s00702-017-1795-7 · Cited by 128
Willsey, A. J., Morris, M. T., Wang, S., Willsey, H. R., Sun, N., Teerikorpi, N., Baum, T., Cagney, G., Bender, K. J., Desai, T. A., et al. (2018) · Cell · doi:10.1016/j.cell.2018.06.016 · Cited by 129
Katzov, H., Chalmers, K. A., Palmgren, J., Andreasen, N., Johansson, B. E. A., Cairns, N. J., Gatz, M., Wilcock, G. K., Love, S., Pedersen, N. L., et al. (2004) · Human Mutation · doi:10.1002/humu.20012 · Cited by 128
Neurofibrillary tangles and β-amyloid deposits in Alzheimer's disease
Goedert, M., Sisodia, S. S., & Price, D. L. (1991) · Current Opinion in Neurobiology · doi:10.1016/0959-4388(91)90067-h · Cited by 128
Blood-brain barrier leakage in Alzheimer’s disease: From discovery to clinical relevance
Nehra, G., Bauer, B., & Hartz, A. M. S. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108119 · Cited by 127
Holstege, H., van der Lee, S. J., Hulsman, M., Wong, T. H., van Rooij, J. G., Weiss, M., Louwersheimer, E., Wolters, F. J., Amin, N., Uitterlinden, A. G., et al. (2017) · European Journal of Human Genetics · doi:10.1038/ejhg.2017.87 · Cited by 140
Synaptic tau: A pathological or physiological phenomenon?
Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 128
Transient receptor potential channels in Alzheimer's disease
Yamamoto, S., Wajima, T., Hara, Y., Nishida, M., & Mori, Y. (2007) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2007.03.006 · Cited by 127
Increased antioxidant enzyme activity in amyloid beta protein-resistant cells
Sagara, Y., Dargusch, R., Klier, F. G., Schubert, D. A., & Behl, C. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-02-00497.1996 · Cited by 127
Mitochondria in Alzheimer's disease
Swerdlow, R. H., & Kish, S. J. (2002) · International review of neurobiology · doi:10.1016/s0074-7742(02)53013-0 · Cited by 126
Epigenomics of Alzheimer's disease
Bennett, D. A., Yu, L., Yang, J., Srivastava, G. P., Aubin, C., & Jager, P. L. D. (2014) · Translational research · doi:10.1016/j.trsl.2014.05.006 · Cited by 126
Neurotoxic effects induced by the Drosophila amyloid-β peptide suggest a conserved toxic function
Carmine-Simmen, K., Proctor, T., Tschäpe, J. A., Poeck, B., Triphan, T., Strauß, R., & Kretzschmar, D. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.10.014 · Cited by 126
Familial and sporadic Alzheimer's disease: Neuropathology cannot exclude a final common pathway
Lippa, C. F., Saunders, A. M., Smith, T. W., Swearer, J. M., Drachman, D. A., Ghetti, B., Nee, L., Pulaski-Salo, D., Dickson, D., Robitaille, Y., et al. (1996) · Neurology · doi:10.1212/wnl.46.2.406 · Cited by 97
Self-citationGenetic susceptibility to Alzheimer disease
Pericak‐Vance, M. A., & Haines, J. L. (1995) · Trends in Genetics · doi:10.1016/s0168-9525(00)89161-1 · Cited by 126
Self-citationAnalysis of chromosome 22 markers in nine schizophrenia pedigrees
Coon, H. H., Holik, J., Hoff, M., Reimherr, F. W., Wender, P. H., Myles‐Worsley, M., Waldo, M. C., Freedman, R., & Byerley, W. (1994) · American Journal of Medical Genetics · doi:10.1002/ajmg.1320540112 · Cited by 126
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
Lehtim�ki, T., Pirttil�, T., Mehta, P., Wisniewski, H., Frey, H., & Nikkari, T. (1995) · Human Genetics · doi:10.1007/bf00225071 · Cited by 125
Genetic diagnosis and prognosis of Alzheimer’s disease: challenges and opportunities
Reitz, C. (2015) · Expert Review of Molecular Diagnostics · doi:10.1586/14737159.2015.1002469 · Cited by 125
Beta-Secretase: Structure, Function, and Evolution
Venugopal, C., Demos, C., Rao, K. S. J., Pappolla, M. A., & Sambamurti, K. (2008) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/187152708784936626 · Cited by 125
Farrer, L. A. (1997) · JAMA · doi:10.1001/jama.1997.03550160069041 · Cited by 124
The Role of PICALM in Alzheimer’s Disease
Xu, W., Tan, L., & Yu, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8878-3 · Cited by 124
Oddo, S., Caccamo, A., Tseng, B., Cheng, D., Vasilevko, V., Cribbs, D. H., & LaFerla, F. M. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2464-08.2008 · Cited by 125
Role of Epigenetics in Alzheimer ‘S and Parkinson‘S Disease
Kwok, J. B. (2010) · Epigenomics · doi:10.2217/epi.10.43 · Cited by 124
Structure and Function of the γ-Secretase Complex
Wolfe, M. S. (2019) · Biochemistry · doi:10.1021/acs.biochem.9b00401 · Cited by 124
Mercken, M. H., Takahashi, H., Honda, T., Sato, K., Murayama, M., Nakazato, Y., Noguchi, K., Imahori, K., & Takashima, A. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00608-4 · Cited by 124
Alzheimer’s disease due to loss of function: A new synthesis of the available data
Kepp, K. P. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.06.004 · Cited by 123
Alzheimer’s Disease: Etiology, Neuropathology and Pathogenesis
Sheppard, O., & Coleman, M. P. (2020) · Exon Publications eBooks · doi:10.36255/exonpublications.alzheimersdisease.2020.ch1 · Cited by 127
Vascular endothelial growth factor gene variability is associated with increased risk for AD
Bo, R. D., Scarlato, M., Ghezzi, S., Boneschi, F. M., Fenoglio, C., Galbiati, S., Virgilio, R., Galimberti, D., Galimberti, G., Crimi, M., et al. (2005) · Annals of Neurology · doi:10.1002/ana.20390 · Cited by 123
Simons, M., Ikonen, E., Tienari, P. J., Arregui, A. C., Mönning, U., Beyreuther, K. T., & Dotti, C. G. (1995) · Journal of Neuroscience Research · doi:10.1002/jnr.490410114 · Cited by 123
Expression of human β‐secretase in the mouse brain increases the steady‐state level of β‐amyloid
Bodendorf, U., Danner, S., Fischer, F., Stefani, M., Sturchler, C., Wiederhold, K., Staufenbiel, M., & Paganetti, P. (2002) · Journal of Neurochemistry · doi:10.1046/j.0022-3042.2002.00770.x · Cited by 123
A comparison of familial and sporadic Alzheimer's disease
Duara, R., Lopez-Alberola, R. F., Barker, W. W., Loewenstein, D. A., Zatinsky, M., Eisdorfer, C. E., & Weinberg, G. B. (1993) · Neurology · doi:10.1212/wnl.43.7.1377 · Cited by 122
A curated gene list for reporting results of newborn genomic sequencing
Ceyhan‐Birsoy, O., Machini, K., Lebo, M. S., Yu, T. W., Agrawal, P. B., Parad, R. B., Holm, I. A., McGuire, A. L., Green, R. C., Beggs, A. H., et al. (2017) · Genetics in Medicine · doi:10.1038/gim.2016.193 · Cited by 122
Metadata
- Authors
- Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., Mant, R., Newton, P., Rooke, K., Roques, P., Talbot, C., Pericak-Vance, M., Roses, A., Williamson, R., Rossor, M., Owen, M., & Hardy, J.
- Affiliations
- St Mary's Hospital (GB)
- Yale University (US)
- University of Wales (GB)
- Duke Medical Center (US)
- Venue
- Nature
- Published
- 1991-02-21
- Volume
- 349
- Issue
- 6311
- Pages
- 704-706
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2058723245
- Cited by
- 4,659
- References
- 30
- Citations by year
- 2026: 62 · 2025: 85 · 2024: 111 · 2023: 88 · 2022: 112 · 2021: 130 · 2020: 149 · 2019: 115 · 2018: 112 · 2017: 130 · 2016: 160 · 2015: 131 · 2014: 129 · 2013: 166 · 2012: 135
- FWCI
- 153.93
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion)
- Funders
- Wellcome Trust
- National Institute on Aging (AG05 128, P50AG005128)
- 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 › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic Associations and Epidemiology
- Keywords
- familial Alzheimer's disease, amyloid precursor protein gene, APP gene mutations, missense mutations, genetic heterogeneity, co-segregation, early-onset Alzheimer's disease, late-onset Alzheimer's disease, beta-amyloid peptide
- MeSH terms
- Alzheimer Disease, Amino Acid Sequence, Base Sequence, Chromosomes, Human, Pair 21, Exons, Genetic Testing, Genotype, Humans, Genetic Linkage, Molecular Sequence Data, Mutation, Pedigree, Protein Precursors, Polymorphism, Restriction Fragment Length, Polymerase Chain Reaction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor
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
