Cited by 4,051Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

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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., Tsuda, T., Mar, L., Foncin, J.-F., Bruni, A. C., Montesi, M. P., Sorbi, S., Rainero, I., Pinessi, L., Nee, L., Chumakov, I., Pollen, D., Brookes, A., Sanseau, P., Polinsky, R. J., Wasco, W., Da Silva, H. A. R., Haines, J. L., Pericak-Vance, M. A., Tanzi, R. E., Roses, A. D., Fraser, P. E., Rommens, J. M., St George-Hyslop, P. H.·1995·Nature

DOI 10.1038/375754a0

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Abstract

Some cases of Alzheimer's disease are inherited as an autosomal dominant trait. Genetic linkage studies have mapped a locus (AD3) associated with susceptibility to a very aggressive form of Alzheimer's disease to chromosome 14q24.3. We have defined a minimal cosegregating region containing the AD3 gene, and isolated at least 19 different transcripts encoded within this region. One of these transcripts (S182) corresponds to a novel gene whose product is predicted to contain multiple transmembrane domains and resembles an integral membrane protein. Five different missense mutations have been found that cosegregate with early-onset familial Alzheimer's disease. Because these changes occurred in conserved domains of this gene, and are not present in normal controls, they are likely to be causative of AD3.

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Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
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
A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366
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
Self-citation
Apolipoprotein E: high-avidity binding to beta-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease.
Strittmatter, W. J., Saunders, A. M., Schmechel, D., Pericak-Vance, M., Enghild, J., Salvesen, G. S., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.5.1977 · Cited by 4,268
Self-citation
Identification of the Cystic Fibrosis Gene: Genetic Analysis
Kerem, B.-S., Rommens, J. M., Buchanan, J. A., Markiewicz, D., Cox, T. K., Chakravarti, A., Buchwald, M., & Tsui, L.-C. (1989) · Science · doi:10.1126/science.2570460 · Cited by 4,142
Self-citation
Association of apolipoprotein E allele ϵ4 with late‐onset familial and sporadic Alzheimer's disease
Saunders, A. M., Strittmatter, W. J., Schmechel, D., St. George-Hyslop, P. H., Pericak-Vance, M. A., Joo, S. H., Rosi, B. L., Gusella, J. F., Crapper-MacLachlan, D. R., Alberts, M. J., et al. (1993) · Neurology · doi:10.1212/wnl.43.8.1467 · Cited by 3,786
Self-citation
The 1993–94 Généthon human genetic linkage map
Gyapay, G., Morissette, J., Alain Vignal, A., Dib, C., Fizames, C., Millasseau, P., Marc, S., Bernardi, G., Lathrop, M. G., & Weissenbach, J. (1994) · Nature Genetics · doi:10.1038/ng0694supp-246 · Cited by 1,835
Structural features in eukaryotic mRNAs that modulate the initiation of translation.
Kozak, M. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54860-2 · Cited by 1,826
A second-generation linkage map of the human genome
Weissenbach, J., Gyapay, G., Dib, C., Alain Vignal, A., Morissette, J., Millasseau, P., Vaysseix, G., & Lathrop, M. G. (1992) · Nature · doi:10.1038/359794a0 · Cited by 1,672

Show all 48 references

Research works printed but not linked: 8

Foncin, J.-F. et al. Rev. Neurol. 141, 194–202 (1985).
Bergamini, L. et al. Acta neurol. 13, 534–538 (1991).
Cruts, M. et al. Neurobiol Aging 15, S129 (1994).
Saleeba, J. A. & Cotton, R. G. Meth. Enzym. 217, 285–295 (1993).
Liu, Q. & Sommer, S. S. BioTechniques 18, 470–476 (1995).
Altschul, S. F., Gish, W., Miller, W., Myers, E. W. & Lipman, D. J. molec. Biol. 215, 403–410 (1990). · DOI · Paper page
Schellenberg, G. D. et al. Am. J. hum. Genet. 53, 619–628 (1993).
Kosik, K. & Greenberg, S. M. in Alzheimer Disease (eds Terry, R. D., Katzman, R. & Bick, K. L.) 335–344 (Raven, New York, 1994).

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Bates, K. A., Verdile, G., Li, Q.-X., Ames, D., Hudson, P., Masters, C. L., & Martins, R. N. (2009) · Molecular Psychiatry · doi:10.1038/mp.2008.96 · Cited by 247
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Jayadev, S., Leverenz, J. B., Steinbart, E. J., Stahl, J. H., Klunk, W. E., Yu, C.-E., & Bird, T. D. (2010) · Brain · doi:10.1093/brain/awq033 · Cited by 255
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Albert, M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13547 · Cited by 254
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Yang, G., Zhou, R., Zhou, Q., Guo, X., Yan, C., Ke, M., Lei, J., & Shi, Y. (2018) · Nature · doi:10.1038/s41586-018-0813-8 · Cited by 245
Oxidative damage and protection by antioxidants in the frontal cortex of Alzheimer’s disease is related to the apolipoprotein E genotype
Ramassamy, C., Averill‐Bates, D. A., Beffert, U., Bastianetto, S., Théroux, L., Lussier‐Cacan, S., Cohn, J. S., Christen, Y., Davignon, J., Quirion, R., et al. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00102-1 · Cited by 244
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Pappolla, M. A., Chyan, Y., Pöeggeler, B., Frangione, B., Wilson, G. L., Ghiso, J. A., & Reiter, R. J. (2000) · Journal of Neural Transmission · doi:10.1007/s007020050018 · Cited by 241
Apolipoprotein E genotyping in Alzheimer's disease
Relkin, N. R. (1996) · The Lancet · doi:10.1016/s0140-6736(96)90284-6 · Cited by 239
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Hughes, E., Burke, R. M., & Doig, A. J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003554200 · Cited by 241
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Waring, S. C., & Rosenberg, R. N. (2008) · Archives of Neurology · doi:10.1001/archneur.65.3.329 · Cited by 248
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Ryan, N. S., Nicholas, J. M., Weston, P. S. J., Liang, Y., Lashley, T., Guerreiro, R. J., Adamson, G., Kenny, J., Beck, J. A., Chávez‐Gutiérrez, L., et al. (2016) · The Lancet Neurology · doi:10.1016/s1474-4422(16)30193-4 · Cited by 241
Self-citation
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Pathogenesis of Alzheimer's disease.
Swerdlow, R. H. (2007) · PubMed · Cited by 242
Interaction between amyloid precursor protein and presenilins in mammalian cells: Implications for the pathogenesis of Alzheimer disease
Xia, W., Zhang, J., Perez, R. G., Koo, E. H., & Selkoe, D. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.15.8208 · Cited by 240
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Ridge, P. G., Hoyt, K. B., Boehme, K., Mukherjee, S., Crane, P. K., Haines, J. L., Mayeux, R., Farrer, L. A., Pericak-Vance, M. A., Schellenberg, G. D., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.02.024 · Cited by 236
Self-citation
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Hirsch-Reinshagen, V., Maia, L. F., Burgess, B. L., Blain, J.-F., Naus, K. E., McIsaac, S. A., Parkinson, P. F., Chan, J. Y., Tansley, G. H., Hayden, M. R., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508781200 · Cited by 233
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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
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Multhaup, G., Ruppert, T., Schlicksupp, A., Hesse, L., Beher, D., Masters, C. L., & Beyreuther, K. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00062-2 · Cited by 228
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Møller, H. J., & Graeber, M. B. (1998) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s004060050027 · Cited by 261
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Walter, J., Capell, A., Grünberg, J., Pesold, B., Schindzielorz, A., Prior, R., Podlisny, M. B., Fraser, P., George‐Hyslop, P. S., Selkoe, D. J., et al. (1996) · Molecular Medicine · doi:10.1007/bf03401652 · Cited by 229
Self-citation
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Liu, P. K., Hsu, C. Y., Dizdaroğlu, M., Floyd, R. A., Kow, Y. W., Karakaya, A., Rabow, L. E., & Cui, J.-K. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-21-06795.1996 · Cited by 224
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Aguzzi, A., & Haass, C. (2003) · Science · doi:10.1126/science.1087348 · Cited by 223
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Regulation of Amyloid Precursor Protein Cleavage
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Review article What causes alzheimer’s disease?
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Neurotherapeutic applications of nanoparticles in Alzheimer’s disease
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Tong, Y., Zhou, W., Fung, V., Christensen, M. A., Qing, H., Sun, X., & Song, W. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0255-3 · Cited by 224
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Wu, L., Rosa‐Neto, P., Hsiung, G. R., Sadovnick, A. D., Masellis, M., Black, S. E., Jia, J., & Gauthier, S. G. (2012) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/s0317167100013949 · Cited by 240
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Self-citation
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Alzheimer presenilins in the nuclear membrane, interphase kinetochores, and centrosomes suggest a role in chromosome segregation.
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Georgakopoulos, A., Marambaud, P., Efthimiopoulos, S., Shioi, J., Cui, W., Li, H., Schütte, M., Gordon, R., Holstein, G. R., Martinelli, G. P., et al. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80219-1 · Cited by 216
Notch1 inhibits neurite outgrowth in postmitotic primary neurons
Berezovska, O., McLean, P. J., Knowles, R. B., Frosh, M. P., Lu, F. M., Lux, S. E., & Hyman, B. T. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00157-8 · Cited by 215
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Self-citation
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Shimizu, T., Watanabe, A., OGAWARA, M., Mori, H., & Shirasawa, T. (2000) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2000.1955 · Cited by 217
Behavioral assays with mouse models of Alzheimer's disease: Practical considerations and guidelines
Puzzo, D., Lee, L. S., Palmeri, A., Calabrese, G., & Arancio, O. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.011 · Cited by 226
Mouse Models of Alzheimer’s Disease
Yokoyama, M., Kobayashi, H., Tatsumi, L., & Tomita, T. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.912995 · Cited by 213
Formation of stable complexes between two Alzheimer's disease gene products: Presenilin-2 and β-amyloid precursor protein
Weidemann, A., Paliga, K., Dürrwang, U., Czech, C., Evin, G. M., Masters, C. L., & Beyreuther, K. T. (1997) · Nature Medicine · doi:10.1038/nm0397-328 · Cited by 214
Alzheimer disease: new concepts on its neurobiology and the clinical role imaging will play
Jack, C. R. (2012) · Radiology · doi:10.1148/radiol.12110433 · Cited by 211
Alzheimer's centennial legacy: origins, landmarks and the current status of knowledge concerning cognitive aspects
Hodges, J. R. (2006) · Brain · doi:10.1093/brain/awl275 · Cited by 227
Transgenic models of Alzheimer’s disease: Learning from animals
Spires‐Jones, T. L., & Hyman, B. T. (2005) · NeuroRx · doi:10.1602/neurorx.2.3.423 · Cited by 217
Towards a Better Understanding of GABAergic Remodeling in Alzheimer’s Disease
Govindpani, K., Calvo-Flores Guzmán, B., Vinnakota, C., Waldvogel, H., Faull, R., & Kwakowsky, A. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081813 · Cited by 208
Genetics of Alzheimer’s Disease
Chouraki, V. A., & Seshadri, S. S. (2014) · Advances in genetics · doi:10.1016/b978-0-12-800149-3.00005-6 · Cited by 220
Molecular genetics of Alzheimer's disease: An update
Brouwers, N., Sleegers, K., & Broeckhoven, C. V. (2008) · Annals of Medicine · doi:10.1080/07853890802186905 · Cited by 213
Mitochondrial and Cell Death Mechanisms in Neurodegenerative Diseases
Martin, L. J. (2010) · Pharmaceuticals · doi:10.3390/ph3040839 · Cited by 213
Presenilin 1 Negatively Regulates β-Catenin/T Cell Factor/Lymphoid Enhancer Factor-1 Signaling Independently of β-Amyloid Precursor Protein and Notch Processing
Soriano, S., Kang, D. E., Fu, M., Pestell, R. G., Chevallier, N., Zheng, H., & Koo, E. H. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.4.785 · Cited by 208
Endoproteolytic Cleavage and Proteasomal Degradation of Presenilin 2 in Transfected Cells
Kim, T., Pettingell, W. H., Hallmark, O. G., Moir, R. D., Wasco, W., & Tanzi, R. E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.17.11006 · Cited by 210
Self-citation
Activation of Ras-ERK Signaling and GSK-3 by Amyloid Precursor Protein and Amyloid Beta Facilitates Neurodegeneration in Alzheimer’s Disease
Kirouac, L., Rajic, A. J., Cribbs, D. H., & Padmanabhan, J. (2017) · eneuro · doi:10.1523/eneuro.0149-16.2017 · Cited by 207
Generation of an Apoptotic Intracellular Peptide by γ-Secretase Cleavage of Alzheimer's Amyloid ß Protein Precursor
Passer, B. J., Pellegrini, L., Russo, C., Siegel, R. M., Lenardo, M. J., Schettini, G., Bachmann, M. F., Tabaton, M., & D'adamio, L. (2000) · Journal of Alzheimer s Disease · doi:10.3233/jad-2000-23-408 · Cited by 213
The Alzheimer's disease mitochondrial cascade hypothesis: an update
Swerdlow, R. H., & Khan, S. M. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.01.011 · Cited by 206
Complete Genomic Screen in Late-Onset Familial Alzheimer Disease: Evidence for a New Locus on Chromosome 12
Pericak-Vance, M. A. (1997) · JAMA · doi:10.1001/jama.1997.03550150041033 · Cited by 206
Self-citation
Full genome screen for Alzheimer disease: Stage II analysis*
Myers, A., DeVriéze, F. W., Holmans, P., Hamshere, M. L., Crook, R., Compton, D., Marshall, H. N., Meyer, D., Shears, S., Booth, J., et al. (2002) · American Journal of Medical Genetics · doi:10.1002/ajmg.10183 · Cited by 208
Endoproteolytic Processing and Stabilization of Wild-type and Mutant Presenilin
Ratovitski, T., Slunt, H. H., Thinakaran, G., Price, D. L., Sisodia, S. S., & Borchelt, D. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24536 · Cited by 208
Molecular biology and genetics of Alzheimer's disease
George‐Hyslop, P. S., & Petit-Paitel, A. (2005) · Comptes Rendus Biologies · doi:10.1016/j.crvi.2004.10.013 · Cited by 208
The Clinical Introduction of Genetic Testing for Alzheimer Disease An Ethical Perspective
Post, S. G. (1997) · JAMA · doi:10.1001/jama.277.10.832 · Cited by 204
Mitochondria and Cell Bioenergetics: Increasingly Recognized Components and a Possible Etiologic Cause of Alzheimer's Disease
Swerdlow, R. H. (2011) · Antioxidants and Redox Signaling · doi:10.1089/ars.2011.4149 · Cited by 206
Screening for PS1 mutations in a referral-based series of AD cases
Rogaeva, E. A., Fafel, K. C., Song, Y., Medeiros, H., Sato, C., Liang, Y., Richard, E., Rogaev, E. I., Frommelt, P., Sadovnick, A. D., et al. (2001) · Neurology · doi:10.1212/wnl.57.4.621 · Cited by 205
Self-citation
Cell type‐specific roles of APOE4 in Alzheimer disease
Blumenfeld, J., Yip, O., Kim, M. J., & Huang, Y. (2024) · Nature Reviews Neuroscience · doi:10.1038/s41583-023-00776-9 · Cited by 202
Beyond endocytosis: LRP function in cell migration, proliferation and vascular permeability
Lillis, A. P., MIKHAILENKO, I. A., & Strickland, D. K. (2005) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2005.01371.x · Cited by 210
Expression and analysis of presenilin 1 in a human neuronal system: localization in cell bodies and dendrites.
Cook, D. G., Sung, J. C., Golde, T. E., Felsenstein, K. M., Wójczyk, B. S., Tanzi, R. E., Trojanowski, J. Q., Lee, V. M., & Doms, R. W. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.17.9223 · Cited by 202
Self-citation
Molecular links between Alzheimer’s disease and diabetes mellitus
Yang, Y., & Song, W. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.07.009 · Cited by 211
Amyloid-β and Tau at the Crossroads of Alzheimer’s Disease
Gallardo, G., & Holtzman, D. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_16 · Cited by 212

Authors: Sherrington, R., Rogaev, E. I., Liang, Y., Rogaeva, E. A., Levesque, G., Ikeda, M., Chi, H., Lin, C., Li, G., Holman, K., Tsuda, T., Mar, L., Foncin, J.-F., Bruni, A. C., Montesi, M. P., Sorbi, S., Rainero, I., Pinessi, L., Nee, L., Chumakov, I., Pollen, D., Brookes, A., Sanseau, P., Polinsky, R. J., Wasco, W., Da Silva, H. A. R., Haines, J. L., Pericak-Vance, M. A., Tanzi, R. E., Roses, A. D., Fraser, P. E., Rommens, J. M., & St George-Hyslop, P. H.
Affiliations: University of Toronto (CA)
Inserm (FR)
University of Florence (IT)
University of Turin (IT)
National Institutes of Health (US)
Fondation Jean Dausset-CEPH (FR)
University of Massachusetts Chan Medical School (US)
Western General Hospital (GB)
Sandoz Group AG (Switzerland) (CH)
Harvard University (US)
Duke University (US)
ORCID: Rogaev, E. I.
Liang, Y.
Rogaeva, E. A.
Ikeda, M.
Lin, C.
Tsuda, T.
Bruni, A. C.
Sorbi, S.
Rainero, I.
Pinessi, L.
Brookes, A.
Haines, J. L.
Tanzi, R. E.
Rommens, J. M.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1995-06
Volume: 375
Issue: 6534
Pages: 754-760
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/375754a0
OpenAlex: W2046209489
Cited by: 4,051
References: 48
Citations by year: 2026: 36 · 2025: 70 · 2024: 78 · 2023: 54 · 2022: 93 · 2021: 93 · 2020: 118 · 2019: 107 · 2018: 105 · 2017: 116 · 2016: 140 · 2015: 100 · 2014: 132 · 2013: 120 · 2012: 134
FWCI: 144.01
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Florence Research (University of Florence) (submittedVersion)
Institutional Research Information System University of Turin (University of Turin) (submittedVersion)
Funders: Canadian Institutes of Health Research (64309)
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: early-onset familial Alzheimer's disease, missense mutations, autosomal dominant inheritance, gene cloning, co-segregation, transmembrane proteins, novel genes, susceptibility genes
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Animals, Base Sequence, Chromosome Mapping, Chromosomes, Human, Pair 14, Cloning, Molecular, Female, Humans, Male, Membrane Proteins, Molecular Sequence Data, Mutation, Pedigree, Transcription, Genetic, Open Reading Frames, Protein Structure, Secondary, Mice, Presenilin-1

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Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease

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