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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Telerman, A., & Amson, R. B. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2589 · Cited by 196
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Mann, D. M. A., Iwatsubo, T., Cairns, N. J., Lantos, P. L., Nochlin, D., Sumi, S. M., Bird, T. D., Poorkaj, P., Hardy, J., Hutton, M., et al. (1996) · Annals of Neurology · doi:10.1002/ana.410400205 · Cited by 184
Advances in the Cellular and Molecular Biology of the Beta-Amyloid Protein in Alzheimer 's Disease
Sambamurti, K., Greig, N. H., & Lahiri, D. K. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:1:1:1 · Cited by 187
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Li, D., Parks, S. B., Kushner, J. D., Nauman, D. J., Burgess, D., Ludwigsen, S., Partain, J., Nixon, R. R., Allen, C. N., Irwin, R. P., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/509900 · Cited by 185
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Mann, D. M. A., Pickering-Brown, S. M., Takeuchi, A., & Iwatsubo, T. (2001) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64688-3 · Cited by 182
The biochemistry of neuronal necrosis: rogue biology?
Syntichaki, P., & Tavernarakis, N. (2003) · Nature reviews. Neuroscience · doi:10.1038/nrn1174 · Cited by 182
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Leissring, M. A., Paul, B. A., Parker, I., Cotman, C. W., & LaFerla, F. M. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0721061.x · Cited by 187
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Pedersen, N. L., Miller, B. L., Wetherell, J. L., Vallø, J., Toga, A. W., Knutson, N., Mehringer, C. M., Small, G. W., & Gatz, M. (1998) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000017097 · Cited by 181
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Baki, L., Marambaud, P., Efthimiopoulos, S., Georgakopoulos, A., Wen, P. H., Cui, W., Shioi, J., Koo, E., Ozawa, M., Friedrich, V. L., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.041603398 · Cited by 183
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Katayama, T., Imaizumi, K., Honda, A., Yoneda, T., Kudo, T., Takeda, M., Mori, K., Rozmahel, R. F., Fraser, P., George‐Hyslop, P. S., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104096200 · Cited by 184
Self-citation
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Emahazion, T. (2001) · Trends in Genetics · doi:10.1016/s0168-9525(01)02342-3 · Cited by 182
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The Genetics of Alzheimer Disease
Blacker, D., & Tanzi, R. E. (1998) · Archives of Neurology · doi:10.1001/archneur.55.3.294 · Cited by 185
Self-citation
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Nixon, R. A., & Yang, D.-S. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a008839 · Cited by 183
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Naj, A. C., & Schellenberg, G. D. (2016) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.32499 · Cited by 186
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Roperch, J.-P., Alvaro, V., Prieur, S., Tuynder, M., Nemani, M., Lethrosne, F., Piouffre, L., Gendron, M., Israeli, D., Dausset, J. B., et al. (1998) · Nature Medicine · doi:10.1038/nm0798-835 · Cited by 175
Degradation of Amyloid β-Protein by a Metalloprotease Secreted by Microglia and Other Neural and Non-neural Cells
Qiu, W. Q., Ye, Z., Kholodenko, D., Seubert, P. A., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.10.6641 · Cited by 182
Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia
Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174
Dementia of the Alzheimer Type
Jalbert, J. J., Daiello, L. A., & Lapane, K. L. (2008) · Epidemiologic Reviews · doi:10.1093/epirev/mxn008 · Cited by 181
δ-catenin, an Adhesive Junction–associated Protein Which Promotes Cell Scattering
Lu, Q., Paredes, M. F., Medina, M., Zhou, J., Cavallo, R., Peifer, M. A., Orecchio, L. D., & Kosik, K. S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.3.519 · Cited by 176
PET amyloid-beta imaging in preclinical Alzheimer's disease
Vlassenko, A. G., Benzinger, T. L. S., & Morris, J. C. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.11.005 · Cited by 188
Development and Mechanism of γ-Secretase Modulators for Alzheimer’s Disease
Crump, C. J., Johnson, D. S., & Li, Y. (2013) · Biochemistry · doi:10.1021/bi400377p · Cited by 174
Modifications and Trafficking of APP in the Pathogenesis of Alzheimer’s Disease
Wang, X., Zhou, X., Li, G., Zhang, Y., Wu, Y., & Song, W. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00294 · Cited by 183
Self-citation
The protein kinase Cdk5
Maccioni, R. B., Carola Otth, L., Concha, I. I., & Muñoz, J. P. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02024.x · Cited by 173
Proteolytic Processing of the Alzheimer's Disease Amyloid Precursor Protein within Its Cytoplasmic Domain by Caspase-like Proteases
Weidemann, A., Paliga, K., Dürrwang, U., Reinhard, F. B. M., Schuckert, O., Evin, G. M., & Masters, C. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5823 · Cited by 179
Stable Association of Presenilin Derivatives and Absence of Presenilin Interactions with APP
Thinakaran, G., Regard, J. B., Bouton, C. M. L. S., Harris, C. L., Price, D. L., Borchelt, D., & Sisodia, S. S. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0171 · Cited by 173
γ-secretases: from cell biology to therapeutic strategies
Bergmans, B. A., & Strooper, B. D. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70332-1 · Cited by 179
Tissue transglutaminase: a possible role in neurodegenerative diseases
Lesort, M. J., Tucholski, J., Miller, M. L., & Johnson, G. V. W. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00052-0 · Cited by 173
High Striatal Amyloid β-Peptide Deposition Across Different Autosomal Alzheimer Disease Mutation Types
Villemagne, V. L., Ataka, S., Mizuno, T., Brooks, W. S., Wada, Y., Kondo, M., Jones, G. R., Watanabe, Y., Mulligan, R. S., Nakagawa, M., et al. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.285 · Cited by 176
The genes associated with early-onset Alzheimer’s disease
Dai, M.-H., Zheng, H., Zeng, L.-D., & Zhang, Y. (2017) · Oncotarget · doi:10.18632/oncotarget.23738 · Cited by 178
A global view of the genetic basis of Alzheimer disease
Reitz, C., Pericak‐Vance, M. A., Foroud, T., & Mayeux, R. P. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00789-z · Cited by 181
Self-citation
Prostaglandins and other lipid mediators in Alzheimer’s disease
Bazan, N. G., Colangelo, V., & Lukiw, W. J. (2002) · Prostaglandins & Other Lipid Mediators · doi:10.1016/s0090-6980(02)00031-x · Cited by 171
Molecular Genetics of Late‐Onset Alzheimer's Disease
Kamboh, M. I. (2004) · Annals of Human Genetics · doi:10.1046/j.1529-8817.2004.00110.x · Cited by 170
Regulation of Amyloid Protein Precursor (APP) Binding to Collagen and Mapping of the Binding Sites on APP and Collagen Type I
Beher, D., Hesse, L., Masters, C. L., & Multhaup, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.3.1613 · Cited by 183
TREM2 in CNS homeostasis and neurodegenerative disease
Painter, M. M., Atagi, Y., Liu, C.-C., Rademakers, R., Xu, H., Fryer, J. D., & Bu, G. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0040-9 · Cited by 169
The roles of amyloid precursor protein (APP) in neurogenesis
Zhou, Z., Chan, C. H.-S., Ma, Q., Xu, X., Xiao, Z., & Tan, E. (2011) · Cell Adhesion & Migration · doi:10.4161/cam.5.4.16986 · Cited by 179
Mutant Human Presenilin 1 Protects presenilin 1 Null Mouse against Embryonic Lethality and Elevates Aβ1–42/43 Expression
Qian, S., Jiang, P., Guan, X.-M., Singh, G., Trumbauer, M. E., Yu, H. H., Chen, H. Y., der Ploeg, L. H. T. V., & Zheng, H. (1998) · Neuron · doi:10.1016/s0896-6273(00)80999-x · Cited by 172
Serum levels of the iron binding protein p97 are elevated in Alzheimer′s disease
Kennard, M. L., Feldman, H., Yamada, T., & Jefferies, W. A. (1996) · Nature Medicine · doi:10.1038/nm1196-1230 · Cited by 170
A review of quality of life after predictive testing for and earlier identification of neurodegenerative diseases
Paulsen, J. S., Nance, M., Kim, J.-I., Carlozzi, N. E., Panegyres, P. K., Erwin, C., Goh, A., McCusker, E., & Williams, J. K. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.08.003 · Cited by 168
Light and Electron Microscopic Localization of Presenilin-1 in Primate Brain
Lah, J. J., Heilman, C. J., Nash, N. R., Rees, H. D., Yi, H., Counts, S. E., & Levey, A. I. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-06-01971.1997 · Cited by 168
Alzheimer's disease as a disorder of mechanisms underlying structural brain self-organization
Arendt, T. (2001) · Neuroscience · doi:10.1016/s0306-4522(00)00516-9 · Cited by 172
Chronic Inflammation and Amyloidogenesis in Alzheimer's Disease -- Role of Spirochetes1
Miklossy, J. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13404 · Cited by 168

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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