Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate α-secretase activity
Open accessAbstract
ADAM10, a member of a disintegrin and metalloprotease family, is an alpha-secretase capable of anti-amyloidogenic proteolysis of the amyloid precursor protein. Here, we present evidence for genetic association of ADAM10 with Alzheimer's disease (AD) as well as two rare potentially disease-associated non-synonymous mutations, Q170H and R181G, in the ADAM10 prodomain. These mutations were found in 11 of 16 affected individuals (average onset age 69.5 years) from seven late-onset AD families. Each mutation was also found in one unaffected subject implying incomplete penetrance. Functionally, both mutations significantly attenuated alpha-secretase activity of ADAM10 (>70% decrease), and elevated Abeta levels (1.5-3.5-fold) in cell-based studies. In summary, we provide the first evidence of ADAM10 as a candidate AD susceptibility gene, and report two potentially pathogenic mutations with incomplete penetrance for late-onset familial AD.
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The ADAM and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions, and are involved in a range of human diseases.
“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [22]
The Introduction (page unavailable) identifies ADAM proteins as metalloproteases and discusses ADAM10 in relation to Alzheimer’s disease, supporting the neurological-disease example. Our copy does not state that the ADAM and ADAMTS families comprise over 40 human genes, mediate cell–cell or cell–matrix interactions, or are involved in the other listed diseases. Searches for those family-wide claims found no supporting passage. (LLM, conf=0.82)
Experimental — accuracy not yet measuredMutations of ADAM10 that reduce its activity enhance amyloidogenic APP processing and Aβ deposition and are linked to late-onset AD.
“Mutations of ADAM10 that reduce its activity and enhance amyloidogenic APP processing and Aβ deposition have recently been linked to late-onset AD (LOAD) (10, 11), establishing ADAM10 as a susceptibility gene for AD.”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [10]
The Discussion reports that Q170H and R181G reduce ADAM10 α-secretase activity, increase Aβ levels in cultured cells, and occur in families with late-onset AD. It does not show that these mutations increase Aβ deposition; it also describes ADAM10 as a possible or candidate susceptibility gene rather than an established one. The APP-processing results did not detect an increase in β-cleavage fragments. (LLM, conf=0.88)
Experimental — accuracy not yet measuredADAM10 is a susceptibility gene for AD.
“establishing ADAM10 as a susceptibility gene for AD.”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [10]
The Abstract calls ADAM10 a “candidate AD susceptibility gene” and reports evidence of an association with AD. The Results section notes that the initially tested SNPs did not show an association in an independent sample. The citing sentence’s “establishing” overstates the paper’s qualified conclusion. (LLM, conf=0.90)
Experimental — accuracy not yet measuredACE and ADAM10 were previously reported as Alzheimer's disease candidate genes but were not replicated in some subsequent studies.
“ACE and ADAM10 were previously reported as Alzheimer’s disease candidate genes18–22 but were not replicated in some subsequent studies23–25.”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [19]
Two rare ADAM10 alterations segregating with disease in LOAD families increased Aβ plaque load in 'Alzheimer-like' mice, with diminished α-secretase activity from the alterations probably the causal mechanism.
“two rare ADAM10 alterations segregating with disease in LOAD families increased Aβ plaque load in ‘Alzheimer-like’ mice, with diminished α-secretase activity from the alterations probably the causal mechanism19,44.”
From Genetic meta-analysis of diagnosed Alzheimer’s disease identifies new risk loci and implicates Aβ, tau, immunity and lipid processing (2019) · cites this paper as [19]
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Cites
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 · see citing works
Statistical Methods for Research Workers
Fisher, R. A. (1945) · American Journal of Clinical Pathology · doi:10.1093/ajcp/15.11.552b · Cited by 10,883 · see citing works
Candidate gene for the chromosome 1 familial Alzheimer’s disease locus
Levy-Lahad, E., Wasco, W., Poorkaj, P., Romano, D. M., Oshima, J., Pettingell, W. H., Yu, C.-E., Jondro, P. D., Schmidt, S. D., Wang, K., et al. (1995) · Science · doi:10.1126/science.7638622 · Cited by 2,577 · see citing works
Self-citationSystematic meta-analyses of Alzheimer disease genetic association studies: the AlzGene database
Bertram, L., McQueen, M. B., Mullin, K., Blacker, D., & Tanzi, R. E. (2007) · Nature Genetics · doi:10.1038/ng1934 · Cited by 1,857 · see citing works
Self-citationVan Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475 · see citing works
Statistical Methods for Research Workers
Fisher, B. R. A. (1926) · Journal of Comparative Pathology and Therapeutics · doi:10.1016/s0368-1742(26)80018-9 · Cited by 1,287 · see citing works
Lammich, S., Kojro, E., Postina, R., Gilbert, S., Pfeiffer, R., Jasionowski, M., Haass, C., & Fahrenholz, F. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3922 · Cited by 1,132 · see citing works
The ADAMs family of metalloproteases: multidomain proteins with multiple functionsPreprint
Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,058 · see citing works
Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 933 · see citing works
Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680 · see citing works
Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., et al. (2004) · Journal of Clinical Investigation · doi:10.1172/jci20864 · Cited by 638 · see citing works
Buxbaum, J. D., Oishi, M., Chen, H. I., Pinkas‐Kramarski, R., JAFFE, E. A., Gandy, S., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10075 · Cited by 558 · see citing works
Bertram, L., Lange, C., Mullin, K., Parkinson, M., Hsiao, M., Hogan, M. F., Schjeide, B. M. M., Hooli, B., DiVito, J., Ionita, I., et al. (2008) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2008.10.008 · Cited by 511 · see citing works
Self-citationApoE-4 and Age at Onset of Alzheimer's Disease: The NIMH Genetics Initiative
Blacker, D., Haines, J. L., Rodes, L., Terwedow, H., Go, R. C. P., Harrell, L. E., Perry, R. T., Bassett, S. S., Chase, G., Meyers, D., et al. (1997) · Neurology · doi:10.1212/wnl.48.1.139 · Cited by 479 · see citing works
Self-citationSecreted form of amyloid β protein precursor is involved in the growth regulation of fibroblasts
Saitoh, T., Sundsmo, M. P., Roch, J., Kimura, N., Cole, G. M., Schubert, D. A., Oltersdorf, T., & Schenk, D. B. (1989) · Cell · doi:10.1016/0092-8674(89)90096-2 · Cited by 471 · see citing works
ADAMs family members as amyloid precursor protein α‐secretases
Allinson, T. M. J., Parkin, E. T., Turner, A. J., & Hooper, N. M. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10737 · Cited by 441 · see citing works
Processing of the β‐Amyloid Precursor Protein and Its Regulation in Alzheimer's Disease
Checler, F. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65041431.x · Cited by 437 · see citing works
Furukawa, K., Sopher, B. L., Rydel, R. E., Begley, J. G., Pham, D. G., Martin, G. M., Fox, M., & Mattson, M. P. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67051882.x · Cited by 414 · see citing works
Activation of protein kinase C inhibits cellular production of the amyloid beta-protein.
Hung, A. Y., Haass, C., Nitsch, R. M., Qiu, W. Q., Citron, M., Wurtman, R. J., Growdon, J. H., & Selkoe, D. J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49409-x · Cited by 399 · see citing works
Méziane, H., Dodart, J., Mathis, C., Little, S. H., Clemens, J. A., Paul, S. M., & Ungerer, A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12683 · Cited by 355 · see citing works
Results of a high-resolution genome screen of 437 Alzheimer's Disease families
Blacker, D. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg007 · Cited by 344 · see citing works
Protein phosphorylation regulates secretion of Alzheimer beta/A4 amyloid precursor protein.
Caporaso, G. L., Gandy, S., Buxbaum, J. D., Ramabhadran, T. V., & Greengard, P. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.3055 · Cited by 338 · see citing works
Skovronsky, D., Moore, D. B., Milla, M. E., Doms, R. W., & Lee, V. M. ‐. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.4.2568 · Cited by 325 · see citing works
Blacker, D., Albert, M., Bassett, S. S., Go, R. C. P., Harrell, L., & Folstein, M. (1994) · Archives of Neurology · doi:10.1001/archneur.1994.00540240042014 · Cited by 293 · see citing works
Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide.
Buxbaum, J. D., Koo, E. H., & Greengard, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.19.9195 · Cited by 272 · see citing works
Lichtenthaler, S. F., Dominguez, D.-I., Westmeyer, G. G., Reiß, K., Haass, C., Säftig, P., Strooper, B. D., & Seed, B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m303861200 · Cited by 256 · see citing works
α-Secretase ADAM10 as Well as αAPPs Is Reduced in Platelets and CSF of Alzheimer Disease Patients
Colciaghi, F., Borroni, B., Pastorino, L., Marcello, E. E., Zimmermann, M., Cattabeni, F., Padovani, A., & Luca, M. D. (2002) · Molecular Medicine · doi:10.1007/bf03402076 · Cited by 246 · see citing works
Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases
Anders, A., Gilbert, S., Garten, W., Postina, R., & Fahrenholz, F. (2001) · The FASEB Journal · doi:10.1096/fj.01-0007fje · Cited by 241 · see citing works
Family-Based Association between Alzheimer's Disease and Variants inUBQLN1
Bertram, L., Hiltunen, M. O., Parkinson, M., Ingelsson, M., Lange, C., Ramasamy, K., Mullin, K., Menon, R., Sampson, A. J., Hsiao, M., et al. (2005) · New England Journal of Medicine · doi:10.1056/nejmoa042765 · Cited by 227 · see citing works
Self-citationWeskamp, G., Cai, H., Brodie, T. A., Higashyama, S., Manova, K., Ludwig, T. E., & Blobel, C. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1537-1544.2002 · Cited by 215 · see citing works
Marcinkiewicz, M. M., & Seidah, N. G. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0752133.x · Cited by 185 · see citing works
Milla, M. E., Leesnitzer, M. A., Moss, M. L., Clay, W. C., Carter, H. L., Miller, A. B., Su, J., Lambert, M. H., Willard, D. H., Sheeley, D. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.30563 · Cited by 156 · see citing works
Inhibition of β‐Amyloid Production by Activation of Protein Kinase C
Gabuzda, D. H., Busciglio, J. A., & Yankner, B. A. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb07479.x · Cited by 138 · see citing works
Merlos‐Suárez, A., Ruíz-Paz, S., Baselga, J. M., & Arribas, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103488200 · Cited by 132 · see citing works
Regulation of Human ADAM 12 Protease by the Prodomain
Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R., & Wewer, U. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13427 · Cited by 131 · see citing works
Lopez‐Perez, E., Zhang, Y., Frank, S. J., Creemers, J. W. M., Seidah, N. G., & Checler, F. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00180.x · Cited by 126 · see citing works
Part-Time α-Secretases: The Functional Biology of ADAM 9, 10 and 17
Deuss, M., Reiss, K., & Hartmann, D. (2008) · Current Alzheimer Research · doi:10.2174/156720508783954686 · Cited by 98 · see citing works
Mattson, M. P., Guo, Z. H., & Geiger, J. D. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0730532.x · Cited by 96 · see citing works
The release of Alzheimer's disease beta amyloid peptide is reduced by phorbol treatment.
Jacobsen, J. S., Spruyt, M. A., Brown, A. M., Sahasrabudhe, S. R., Blume, A. J., Vitek, M. P., Muenkel, H. A., & Sonnenberg‐Reines, J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37204-6 · Cited by 91 · see citing works
Merlos‐Suárez, A., Fernández-Larrea, J., Reddy, P., Baselga, J. M., & Arribas, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.38.24955 · Cited by 88 · see citing works
Kauwe, J. S. K., Jacquart, S., Chakraverty, S., Wang, J., Mayo, K., Fagan, A. M., Holtzman, D. M., Morris, J. C., & Goate, A. M. (2007) · Annals of Neurology · doi:10.1002/ana.21099 · Cited by 84 · see citing works
Assessment of Alzheimer’s disease case–control associations using family-based methods
Schjeide, B. M., McQueen, M. B., Mullin, K., DiVito, J. R., Hogan, M. F., Parkinson, M., Hooli, B. V., Lange, C., Blacker, D., Tanzi, R. E., et al. (2008) · Neurogenetics · doi:10.1007/s10048-008-0151-3 · Cited by 70 · see citing works
Self-citationLeonard, J. D., Lin, F. C., & Milla, M. E. (2005) · Biochemical Journal · doi:10.1042/bj20041727 · Cited by 60 · see citing works
α-Secretase Activation – An Approach to Alzheimer’s Disease Therapy
Fahrenholz, F., & Postina, R. (2006) · Neurodegenerative Diseases · doi:10.1159/000095264 · Cited by 59 · see citing works
Blacker, M., Noe, M. C., Carty, T. J., Goodyer, C. G., & LeBlanc, A. C. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01228.x · Cited by 42 · see citing works
Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress
Clement, A. B., Hanstein, R., Schröder, A., et al. (2008) · Neuroscience · doi:10.1016/j.neuroscience.2007.10.060 · Cited by 35 · see citing works
Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis
Gandy, S., & Greengard, P. (1994) · Biochimie · doi:10.1016/0300-9084(94)90162-7 · Cited by 30 · see citing works
Mills, J., & Reiner, P. B. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00381-4 · Cited by 24 · see citing works
Dynamite extended: two new services to simplify protein dynamic analysis
Barrett, C. P., & Noble, M. E. M. (2005) · Computer applications in the biosciences · doi:10.1093/bioinformatics/bti464 · Cited by 23 · see citing works
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Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,542 · see citing works
Alzheimer Disease Genetics Consortium (ADGC), Kunkle, B. W., The European Alzheimer’s Disease Initiative (EADI), Cohorts for Heart and Aging Research in Genomic Epidemiology Consortium (CHARGE), Genetic and Environmental Risk in AD/Defining Genetic, P. A. E. R. F. A. D. C. (., Grenier-Boley, B., Sims, R., Bis, J. C., Damotte, V., Naj, A. C., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0358-2 · Cited by 2,946 · see citing works
Self-citationAlzheimer’s Disease Risk Genes and Mechanisms of Disease Pathogenesis
Karch, C. M., & Goate, A. M. (2015) · Biological Psychiatry · doi:10.1016/j.biopsych.2014.05.006 · Cited by 1,357 · see citing works
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Bertram, L., Lill, C. M., & Tanzi, R. E. (2010) · Neuron · doi:10.1016/j.neuron.2010.10.013 · Cited by 834 · see citing works
Self-citationKuhn, P., Wang, H., Dislich, B., Colombo, A., Zeitschel, U., Ellwart, J. W., Kremmer, E., Roßner, S., & Lichtenthaler, S. F. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.167 · Cited by 621 · see citing works
GWAS on family history of Alzheimer’s disease
Marioni, R. E., Harris, S. E., Zhang, Q., McRae, A. F., Hagenaars, S. P., Hill, W. D., Davies, G., Ritchie, C. W., Gale, C. R., Starr, J. M., et al. (2018) · Translational Psychiatry · doi:10.1038/s41398-018-0150-6 · Cited by 564 · see citing works
Alzheimer’s Disease Genetics: From the Bench to the Clinic
Karch, C. M., Cruchaga, C., & Goate, A. M. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.041 · Cited by 473 · see citing works
Immune Signaling in Neurodegeneration
Hammond, T. R., Marsh, S. E., & Stevens, B. (2019) · Immunity · doi:10.1016/j.immuni.2019.03.016 · Cited by 336 · see citing works
Cruchaga, C., Chakraverty, S., Mayo, K., Vallania, F. L. M., Mitra, R. D., Faber, K., Williamson, J., Bird, T., Diaz-Arrastia, R., Foroud, T. M., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031039 · Cited by 320 · see citing works
Genes associated with Alzheimer's disease: an overview and current status
Giri, M., Lü, Y., & Zhang, M. (2016) · Clinical Interventions in Aging · doi:10.2147/cia.s105769 · Cited by 311 · see citing works
Untangling Genetic Risk for Alzheimer’s Disease
Pimenova, A. A., Raj, T., & Goate, A. M. (2018) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.05.014 · Cited by 223 · see citing works
Suh, J., Choi, S. H., Romano, D. M., Gannon, M. A., Lesinski, A. N., Kim, D. Y., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.08.035 · Cited by 217 · see citing works
Self-citationSoluble amyloid precursor protein-α modulates β-secretase activity and amyloid-β generation
Obregon, D., Hou, H., Deng, J., Giunta, B., Tian, J., Darlington, D., Shahaduzzaman, M., Zhu, Y., Mori, T., Mattson, M. P., et al. (2012) · Nature Communications · doi:10.1038/ncomms1781 · Cited by 192 · see citing works
Vardarajan, B. N., Ghani, M., Kahn, A., Sheikh, S., Sato, C., Barral, S., Lee, J. H., Cheng, R., Reitz, C., Lantigua, R., et al. (2015) · Annals of Neurology · doi:10.1002/ana.24466 · Cited by 148 · see citing works
Genetic variability in response to amyloid beta deposition influences Alzheimer’s disease risk
Salih, D. A., Bayram, S., Guelfi, S., Reynolds, R. H., Shoai, M., Ryten, M., Brenton, J. W., Zhang, D., Matarin, M., Botia, J. A., et al. (2019) · Brain Communications · doi:10.1093/braincomms/fcz022 · Cited by 110 · see citing works
Alzheimer disease pathology and the cerebrospinal fluid proteome
Dayon, L., Núñez Galindo, A., Wojcik, J., Cominetti, O., Corthésy, J., Oikonomidi, A., Henry, H., Kussmann, M., Migliavacca, E., Severin, I., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0397-4 · Cited by 101 · see citing works
Rivastigmine modifies the α-secretase pathway and potentially early Alzheimer’s disease
Ray, B., Maloney, B., Sambamurti, K., Karnati, H. K., Nelson, P. T., Greig, N. H., & Lahiri, D. K. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-0709-x · Cited by 91 · see citing works
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Del-Aguila, J. L., Koboldt, D. C., Black, K., Chasse, R., Norton, J., Wilson, R. K., & Cruchaga, C. (2015) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2015.07.008 · Cited by 41 · see citing works
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Vassar, R. (2013) · Neuron · doi:10.1016/j.neuron.2013.09.031 · Cited by 32 · see citing works
The Retinoic Acid Receptor Agonist Am80 Increases Hippocampal ADAM10 in Aged SAMP8 Mice
Kitaoka, K., Shimizu, N., Ono, K., Chikahisa, S., Nakagomi, M., Shudo, K., Ishimura, K., Séi, H., & Yoshizaki, K. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.04.009 · Cited by 27 · see citing works
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Genetic associations with age at dementia onset in the <i>PSEN1 E280A</i> Colombian kindred
Cochran, J. N., Acosta‐Uribe, J., Esposito, B. T., Madrigal, L., Aguillón, D., Giraldo, M. M., Taylor, J. W., Bradley, J., Fulton‐Howard, B., Andrews, S. J., et al. (2023) · Alzheimer's & Dementia · doi:10.1002/alz.13021 · Cited by 21 · see citing works
- Authors
- Kim, M., Suh, J., Romano, D., Truong, M. H., Mullin, K., Hooli, B., Norton, D., Tesco, G., Elliott, K., Wagner, S. L., Moir, R. D., Becker, K. D., & Tanzi, R. E.
- Affiliations
- Harvard University (US)
- Corresponding author
- Tanzi, Rudolph E.
- ORCID
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-07-15
- Volume
- 18
- Issue
- 20
- Pages
- 3987-3996
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC2748890
- OpenAlex
- W2160264227
- Cited by
- 234
- References
- 49
- Citations by year
- 2026: 9 · 2025: 4 · 2024: 11 · 2023: 16 · 2022: 17 · 2021: 13 · 2020: 9 · 2019: 24 · 2018: 19 · 2017: 13 · 2016: 20 · 2015: 23 · 2014: 13 · 2013: 6 · 2012: 13
- FWCI
- 8.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Human Molecular Genetics (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cure Alzheimer's Fund
- National Institute on Aging (P01AG015379, U24AG021886)
- National Institute of Mental Health (R37MH060009)
- Topics
- Health Sciences › Medicine › Physiology › 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 › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- ADAM10, late-onset Alzheimer's disease, amyloid precursor protein, non-synonymous mutations, amyloid-beta, incomplete penetrance, familial Alzheimer's disease, genetic susceptibility
- MeSH terms
- ADAM10 Protein, Aged, Aged, 80 and over, Alzheimer Disease, Animals, Cricetulus, Female, Cricetinae, Humans, Male, Membrane Proteins, Middle Aged, Mutation, Pedigree, CHO Cells, Polymorphism, Single Nucleotide, ADAM Proteins, Amyloid Precursor Protein Secretases
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 ›
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