Cited by 1,513Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchAmyotrophic Lateral Sclerosis Research

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A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

Mullan, Mike, Crawford, Fiona, Axelman, Karin, Houlden, Henry, Lilius, Lena, Winblad, Bengt, Lannfelt, Lars·1992·Nature Genetics

DOI 10.1038/ng0892-345

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Abstract

Mutations at codon 717 in exon 17 of the beta-amyloid precursor protein (APP) gene have previously been shown to segregate with early onset Alzheimer's disease in some families. We have identified a double mutation at codons 670 and 671 (APP 770 transcript) in exon 16 which co-segregates with the disease in two large (probably related) early-onset Alzheimer's disease families from Sweden. Two base pair transversions (G to T, A to C) from the normal sequence predict Lys to Asn and Met to Leu amino acid substitutions at codons 670 and 671 of the APP transcript. This mutation occurs at the amino terminal of beta-amyloid and may be pathogenic because it occurs at or close to the endosomal/lysosomal cleavage site of the molecule. Thus, pathogenic mutations in APP frame the beta-amyloid sequence.

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Clinical diagnosis of Alzheimer's disease: Report of the NINCDS‐ADRDA Work Group* under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
McKhann, 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
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
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
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
The molecular pathology of Alzheimer's disease
Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708
Cleavage of Amyloid β Peptide During Constitutive Processing of Its Precursor
Esch, F. S., Keim, P. S., Beattie, E. C., Blacher, R. W., Culwell, A. R., Oltersdorf, T., McClure, D., & Ward, P. J. (1990) · Science · doi:10.1126/science.2111583 · Cited by 1,403
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
Early-onset Alzheimer's disease caused by mutations at codon 717 of the β-amyloid precursor protein gene
Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214
Self-citation
A mutation in the Amyloid Precursor Protein Associated with Hereditary Alzheimer's Disease
Murrell, J. R., Farlow, M. R., Ghetti, B. F., & Benson, M. D. (1991) · Science · doi:10.1126/science.1925564 · Cited by 1,142

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Research works printed but not linked: 2

Hardy, J. et al. Lancet 337, 1342–1343 (1991).
Weeks, D.E., Ott, J. & Lathrop, G M. Am. J. hum. Genet. 47(3), A204 (1990).

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Maladie d'Alzheimer
Delacourte, A., Campion, D., & Davous, P. (2007) · Encyclopédie médico-chirurgicale. Neurologie · doi:10.1016/s0246-0378(07)44093-3 · Cited by 23
Early Detection of Aβ Deposition in the 5xFAD Mouse by Amyloid PET
Oh, S. J., Lee, H., Kang, K. J., Han, S. J., Lee, Y. J., Lee, K. C., Lim, S. M., Yoon, D., Kim, K. M., Park, J. A., et al. (2018) · Contrast Media & Molecular Imaging · doi:10.1155/2018/5272014 · Cited by 23
Alzheimer's disease: Molecular genetics and transgenic animal models
Lannfelt, L., Folkesson, R., Mohammed, A. H. S., Winblad, B. G., Hellgren, D., Duff, K., & Hardy, J. (1993) · Behavioural Brain Research · doi:10.1016/0166-4328(93)90137-f · Cited by 23
Self-citation
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Ling, H. H., Mendoza-Viveros, L., Mehta, N., & Cheng, H. M. (2014) · Critical Reviews™ in Oncogenesis · doi:10.1615/critrevoncog.2014011899 · Cited by 23
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Vestling, M., Cedazo-Mínguez, Á., Adem, A., Wiehager, B., Racchi, M., Lannfelt, L., & Cowburn, R. F. (1999) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(99)00003-4 · Cited by 23
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Mayeux, R. P. (2006) · Alzheimer Disease & Associated Disorders · doi:10.1097/00002093-200607001-00008 · Cited by 25
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Pérez, M., Morán, M. A., Ferrer, I., Ávila, J., & Gómez‐Ramos, P. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0420-0 · Cited by 23
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Zubenko, G. S., Winwood, E., Jacobs, B., Teply, I., Stiffler, J. S., Hughes, H. B., Huff, F. J., Sunderland, T., & Martinez, A. J. (1999) · American Journal of Psychiatry · doi:10.1176/ajp.156.1.50 · Cited by 23
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Sadleir, K. R., & Vassar, R. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci171838 · Cited by 22
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Roses, A. D., Pericak‐Vance, M. A., Saunders, A. M., Schmechel, D. E., Goldgaber, D., & Strittmatter, W. J. (1994) · Epilepsia · doi:10.1111/j.1528-1157.1994.tb05925.x · Cited by 23
Diagnosis of Alzheimer's disease: defining genetic profiles (genotype vs phenotype)
Cacabelos, R. (1996) · Acta Neurologica Scandinavica · doi:10.1111/j.1600-0404.1996.tb05875.x · Cited by 23
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de la Vega, M. P., Näslund, C., Brundin, R., Lannfelt, L., Löwenmark, M., Kilander, L., Ingelsson, M., & Giedraitis, V. (2022) · BMC Genomics · doi:10.1186/s12864-022-08343-9 · Cited by 21
Self-citation
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Lee, J. H., Bacskai, B. J., & Ayata, C. (2011) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394596-9.00002-0 · Cited by 21
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Am, A., Uddin, M. S., Wahid, F., Mohammed, A. I., & Rahman, M. M. (2016) · Journal of Neurology and Neuroscience · doi:10.21767/2171-6625.1000126 · Cited by 21
Fluid‐based proteomics targeted on pathophysiological processes and pathologies in neurodegenerative diseases
Brinkmalm, A., Portelius, E., Brinkmalm, G., Pannee, J., Dahlén, R., Gobom, J., Blennow, K., & Zetterberg, H. (2018) · Journal of Neurochemistry · doi:10.1111/jnc.14594 · Cited by 23
Mouse induced pluripotent stem cells-derived Alzheimer’s disease cerebral organoid culture and neural differentiation disorders
Fan, W., Yizheng, S., Shi, Z., Wang, H., & Deng, J. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.134433 · Cited by 21
Imbalance in the response of pre- and post-synaptic components to amyloidopathy
Stephen, T., Tamagnini, F., Piegsa, J., Sung, K., Harvey, J., Oliver‐Evans, A., Murray, T. K., Ahmed, Z., Hutton, M. L., Randall, A. D., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-50781-1 · Cited by 23
CSF in Alzheimer's Disease
Zetterberg, H., Lautner, R., Skillbäck, T. B., Rosén, C., Shahim, P., Mattsson, N., & Blennow, K. (2014) · Advances in clinical chemistry · doi:10.1016/b978-0-12-800141-7.00005-x · Cited by 21
A graphene oxide-based fluorescent scheme for the determination of the activity of the β-site amyloid precursor protein (BACE1) and its inhibitors
Liu, L., Xia, N., & Yu, J. (2015) · Microchimica Acta · doi:10.1007/s00604-015-1647-9 · Cited by 21
The significance of the Swedish APP670/671 mutation for the development of Alzheimer's disease amyloidosis
Johnston, J. A., O’Neill, C., Lannfelt, L., Winblad, B. G., & Cowburn, R. F. (1994) · Neurochemistry International · doi:10.1016/0197-0186(94)90056-6 · Cited by 23
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Olsson, B., Legros, L., Guilhot, F., Strömberg, K., Smith, J. C., Livesey, F. J., Wilson, D. H., Zetterberg, H., & Blennow, K. (2013) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2013.08.283 · Cited by 21
Early-onset Alzheimer's disease in Scotland: environmental and familial factors
Whalley, L. J. (2001) · The British Journal of Psychiatry · doi:10.1192/bjp.178.40.s53 · Cited by 21

Authors: Mullan, M., Crawford, F., Axelman, K., Houlden, H., Lilius, L., Winblad, B., & Lannfelt, L.
Affiliations: University of South Florida (US)
Karolinska Institutet (SE)
St Mary's Hospital (GB)
ORCID: Crawford, Fiona
Houlden, Henry
Winblad, Bengt
Lannfelt, Lars
Venue: Nature Genetics
Publisher: Springer Science and Business Media LLC
Published: 1992-08
Volume: 1
Issue: 5
Pages: 345-347
ISSN: 1061-4036 (ISSN-L)
1546-1718
DOI: 10.1038/ng0892-345
OpenAlex: W2030641075
Cited by: 1,513
References: 22
Citations by year: 2026: 24 · 2025: 30 · 2024: 50 · 2023: 47 · 2022: 49 · 2021: 46 · 2020: 52 · 2019: 56 · 2018: 48 · 2017: 48 · 2016: 47 · 2015: 31 · 2014: 62 · 2013: 31 · 2012: 32
FWCI: 49.77
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Genetics (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
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
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: Alzheimer's disease, APP gene, amyloid-beta, early-onset familial Alzheimer's disease, Swedish families
MeSH terms: Alzheimer Disease, Amino Acid Sequence, Base Sequence, Brain, Codon, Exons, Female, Humans, Genetic Linkage, Male, Middle Aged, Molecular Sequence Data, Oligodeoxyribonucleotides, Pedigree, Transcription, Genetic, Genetic Variation, Amyloid beta-Protein Precursor, Point Mutation

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A pathogenic mutation for probable Alzheimer's disease in the APP gene at the N–terminus of β–amyloid

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