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

Flagged first, then by citations

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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Yu, G., Chen, F., Lévesque, G., Nishimura, M., Zhang, D., Lévesque, L., Rogaeva, E., Xu, D., Liang, Y., Duthie, M., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.26.16470 · Cited by 366
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Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
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Hardy, J., Duff, K., Hardy, K. G., Pérez‐Tur, J., & Hutton, M. (1998) · Nature Neuroscience · doi:10.1038/1565 · Cited by 356
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Self-citation
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Self-citation
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Self-citation
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Self-citation
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Self-citation
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Francis, Y. I., Fà, M., Ashraf, H., Zhang, H., Staniszewski, A., Latchman, D. S., & Arancio, O. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1134 · Cited by 306
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Podlisny, M. B., Citron, M., Amarante, P., Sherrington, R., Xia, W., Zhang, J., Diehl, T. S., Levesque, G., Fraser, P., Haass, C., et al. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0129 · Cited by 296
Self-citation
Detection of a Novel Intraneuronal Pool of Insoluble Amyloid β Protein that Accumulates with Time in Culture
Skovronsky, D. M., Doms, R. W., & Lee, V. M.-Y. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.4.1031 · Cited by 290
Aluminium in Alzheimer?s disease: are we still at a crossroad?
Gupta, V. B., Anitha, S., Hegde, M. L., Zecca, L., Garruto, R. M., Ravid, R., Shankar, S. K., Stein, R., Shanmugavelu, P., & Rao, K. S. J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4317-3 · Cited by 294
Monoaminergic neuropathology in Alzheimer’s disease
Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.001 · Cited by 297
Restoring Wnt/β-catenin signaling is a promising therapeutic strategy for Alzheimer’s disease
Jia, L., Piña-Crespo, J., & Li, Y. (2019) · Molecular Brain · doi:10.1186/s13041-019-0525-5 · Cited by 288
Induction of neuronal death by ER stress in Alzheimer’s disease
Katayama, T., Imaizumi, K., Manabe, T., Hitomi, J., Kudo, T., & Tohyama, M. (2004) · Journal of Chemical Neuroanatomy · doi:10.1016/j.jchemneu.2003.12.004 · Cited by 292
Phosphorylation, Subcellular Localization, and Membrane Orientation of the Alzheimer's Disease-associated Presenilins
Strooper, B. D., Beullens, M., Contreras, B., Lévesque, L., Craessaerts, K., Cordell, B., Moechars, D., Bollen, M., Fraser, P., George‐Hyslop, P. S., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.6.3590 · Cited by 291
Self-citation
Expression of Presenilin 1 and 2 (PS1 and PS2) in Human and Murine Tissues
Lee, M. K., Slunt, H. H., Martin, L. J., Thinakaran, G., Kim, G. J., Gandy, S., Seeger, M., Koo, E. H., Price, D. L., & Sisodia, S. S. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-23-07513.1996 · Cited by 293
The genetic architecture of Alzheimer's disease: beyond APP, PSENs and APOE
Guerreiro, R. J., Gustafson, D. R., & Hardy, J. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.03.025 · Cited by 285
The role of Aβ42 in Alzheimer's disease
Younkin, S. G. (1998) · Journal of Physiology-Paris · doi:10.1016/s0928-4257(98)80035-1 · Cited by 282
Enhanced Production and Oligomerization of the 42-residue Amyloid β-Protein by Chinese Hamster Ovary Cells Stably Expressing Mutant Presenilins
Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haass, C., Seubert, P. A., Koo, E. H., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7977 · Cited by 286
APOE in the bullseye of neurodegenerative diseases: impact of the APOE genotype in Alzheimer’s disease pathology and brain diseases
Fernández-Calle, R., Konings, S. C., Frontiñán-Rubio, J., García-Revilla, J., Camprubí-Ferrer, L., Svensson, M., Martinson, I., Boza-Serrano, A., Venero, J. L., Nielsen, H. M., et al. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00566-4 · Cited by 278
Mitochondria and degenerative disorders
Orth, M., & Schapira, A. H. V. (2001) · American Journal of Medical Genetics · doi:10.1002/ajmg.1425 · Cited by 281
Molecular genetics of Alzheimer’s disease
George‐Hyslop, P. S. (2000) · Biological Psychiatry · doi:10.1016/s0006-3223(99)00301-7 · Cited by 281
Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response
Gray, C. W., Ward, R. V., Karran, E. H., Turconi, S., Rowles, A., Viglienghi, D., Southan, C., BARTON, A. J. L., Fantom, K. G. M., West, A., et al. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01589.x · Cited by 277
Implications of GABAergic Neurotransmission in Alzheimer’s Disease
Li, Y., Sun, H., Chen, Z., Xu, H., Bu, G., & Zheng, H. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00031 · Cited by 282
The Ageing Brain: Molecular and Cellular Basis of Neurodegeneration
Azam, S., Haque, M. E., Balakrishnan, R., Kim, I., & Choi, D. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.683459 · Cited by 273
Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy
Götz, J., Streffer, J. R., David, D. C., Schild, A., Hoerndli, F. J., Pennanen, L., Kurosinski, P., & Chen, F. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001508 · Cited by 284
A Role for Presenilin-1 in Nuclear Accumulation of Ire1 Fragments and Induction of the Mammalian Unfolded Protein Response
Niwa, M., Sidrauski, C., Kaufman, R. J., & Walter, P. (1999) · Cell · doi:10.1016/s0092-8674(00)81667-0 · Cited by 274
Exploring the Etiology of Alzheimer Disease Using Molecular Genetics
Lendon, C. L. (1997) · JAMA · doi:10.1001/jama.1997.03540340059034 · Cited by 274
The biological pathways of Alzheimer disease: a review
Calabrò, M., Rinaldi, C., Santoro, G., & Crisafulli, C. (2020) · AIMS neuroscience · doi:10.3934/neuroscience.2021005 · Cited by 287
Statement on Use of Apolipoprotein E Testing for Alzheimer Disease
Farrer, L. A. (1995) · JAMA · doi:10.1001/jama.1995.03530200063039 · Cited by 271
2D versus 3D Human Induced Pluripotent Stem Cell-Derived Cultures for Neurodegenerative Disease Modelling
Centeno, E. G. Z., Cimarosti, H., & Bithell, A. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0258-4 · Cited by 268
Application of Metabolomics in Alzheimer’s Disease
Wilkins, J. M., & Trushina, E. (2018) · Frontiers in Neurology · doi:10.3389/fneur.2017.00719 · Cited by 268
Aluminium in brain tissue in familial Alzheimer’s disease
Mirza, A., King, A., Troakes, C., & Exley, C. (2017) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2016.12.001 · Cited by 261
Filamentous nerve cell inclusions in neurodegenerative diseases
Goedert, M., Spillantini, M. G., & Davies, S. W. (1998) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(98)80090-1 · Cited by 261
Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease
Guo, Q., Fu, W., Xie, J., Luo, H., Sells, S. F., Geddes, J. W., Bondada, V., Rangnekar, V. M., & Mattson, M. P. (1998) · Nature Medicine · doi:10.1038/nm0898-957 · Cited by 260
Astrocyte energy and neurotransmitter metabolism in Alzheimer’s disease: Integration of the glutamate/GABA-glutamine cycle
Andersen, J. V., Schousboe, A., & Verkhratsky, A. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102331 · Cited by 263
Mechanisms contributing to the deficits in hippocampal synaptic plasticity in mice lacking amyloid precursor protein
Seabrook, G. R., Smith, D. W., Bowery, B. J., Easter, A., Reynolds, T., Fitzjohn, S. M., Morton, R. A., Zheng, H., Dawson, G. R., SIRINATHSINGHJI, D. J. S., et al. (1999) · Neuropharmacology · doi:10.1016/s0028-3908(98)00204-4 · Cited by 281
Clinical phenotypic heterogeneity of Alzheimer's disease associated with mutations of the presenilin–1 gene
Larner, A. J., & Doran, M. (2005) · Journal of Neurology · doi:10.1007/s00415-005-0019-5 · Cited by 264
Genetic mapping using haplotype, association and linkage methods suggests a locus for severe bipolar disorder (BPI) at 18q22-q23
Freimer, N. B., Reus, V. I., Escamilla, M., Mclnnes, L. A., Spesny, M., Leon, P. E., Service, S. K., Smith, L. B., da Silva, S. R. A., Rojas, E., et al. (1996) · Nature Genetics · doi:10.1038/ng0496-436 · Cited by 255

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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