A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
Abstract
Alzheimer disease (AD) is characterized by excessive deposition of amyloid beta-peptides (A beta peptides) in the brain. In the nonamyloidogenic pathway, the amyloid precursor protein (APP) is cleaved by the alpha-secretase within the A beta peptide sequence. Proteinases of the ADAM family (adisintegrin and metalloproteinase) are the main candidates as physiologically relevant alpha-secretases, but early lethality of knockout animals prevented a detailed analysis in neuronal cells. To overcome this restriction, we have generated transgenic mice that overexpress either ADAM10 or a catalytically inactive ADAM10 mutant. In this report we show that a moderate neuronal overexpression of ADAM10 in mice transgenic for human APP([V717I]) increased the secretion of the neurotrophic soluble alpha-secretase-released N-terminal APP domain (APPs alpha), reduced the formation of A beta peptides, and prevented their deposition in plaques. Functionally, impaired long-term potentiation and cognitive deficits were alleviated. Expression of mutant catalytically inactive ADAM10 led to an enhancement of the number and size of amyloid plaques in the brains of double-transgenic mice. The results provide the first in vivo evidence for a proteinase of the ADAM family as an alpha-secretase of APP, reveal activation of ADAM10 as a promising therapeutic target, and support the hypothesis that a decrease in alpha-secretase activity contributes to the development of AD.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
GDE2 is required to control neuronal ADAM10 α-secretase activity.
“these observations support the model that GDE2 is required to control neuronal ADAM10 α-secretase activity.”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [30]
Overexpression of ADAM10 in mouse models can halt Aβ production and subsequent aggregation.
“Overexpression of ADAM10 in mouse models can halt Aβ production and subsequent aggregation69.”
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 [69]
Cites
The Mouse Brain in Stereotaxic Coordinates
Paxinos, G. (2001) · Cited by 12,859 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Developments of a water-maze procedure for studying spatial learning in the rat
Morris, R. (1984) · Journal of Neuroscience Methods · doi:10.1016/0165-0270(84)90007-4 · Cited by 7,180 · see citing works
Ashburner, M. (1989) · Cold Spring Harbor Laboratory eBooks · Cited by 6,739 · see citing works
Alzheimer's Disease: Genes, Proteins, and Therapy
Selkoe, D. J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.741 · Cited by 6,063 · see citing works
Manipulating the mouse embryo: A laboratory manual
Hogan, B., Costantini, F. D., & Lacy, E. (1986) · Cited by 4,467 · see citing works
Walsh, D. M., Klyubin, I., Fadeeva, J. V., Cullen, W. K., Anwyl, R., Wolfe, M. S., Rowan, M. J., & Selkoe, D. J. (2002) · Nature · doi:10.1038/416535a · Cited by 4,291 · see citing works
Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works
Applications of the Morris water maze in the study of learning and memory
D’Hooge, R., & Deyn, P. P. D. (2001) · Brain Research Reviews · doi:10.1016/s0165-0173(01)00067-4 · Cited by 2,035 · see citing works
Purification and cloning of amyloid precursor protein β-secretase from human brain
Sinha, S., Anderson, J. P., Barbour, R., Basi, G. S., Caccavello, R., Davis, D., Doan, M., Dovey, H. F., Frigon, N., Hong, J., et al. (1999) · Nature · doi:10.1038/990114 · Cited by 1,612 · see citing works
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works
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 · 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
Self-citationBuxbaum, 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
Haass, C., Koo, E. H., Mellon, A., Hung, A. Y., & Selkoe, D. J. (1992) · Nature · doi:10.1038/357500a0 · Cited by 899 · see citing works
Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
Kojro, E., Gimpl, G., Lammich, S., März, W., & Fahrenholz, F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.081612998 · Cited by 804 · see citing works
Self-citationA learning deficit related to age and β-amyloid plaques in a mouse model of Alzheimer's disease
Chen, G., Chen, K. S., Knox, J., Inglis, J., Bernard, A., Martin, S. J., Justice, A., McConlogue, L., Games, D., Freedman, S. B., et al. (2000) · Nature · doi:10.1038/35050103 · Cited by 740 · see citing works
Beta-amyloid precursor protein cleavage by a membrane-bound protease.
Sisodia, S. S. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.13.6075 · Cited by 738 · see citing works
Hes1 and Hes5 as Notch effectors in mammalian neuronal differentiation
Ohtsuka, T., Ishibashi, M., Gradwohl, G., Nakanishi, S., Guillemot, F., & Kageyama, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.8.2196 · Cited by 735 · see citing works
Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 708 · see citing works
Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680 · see citing works
Moechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668 · see citing works
Self-citationAging renders the brain vulnerable to amyloid β-protein neurotoxicity
Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520 · see citing works
Regulated Cleavage of a Contact-Mediated Axon Repellent
Hattori, M., Osterfield, M., & Flanagan, J. G. (2000) · Science · doi:10.1126/science.289.5483.1360 · Cited by 518 · see citing works
Näslund, J., Schierhorn, A., Hellman, U., Lannfelt, L., Roses, A. D., Tjernberg, L. O., Silberring, J., Gandy, S. E., Winblad, B., & Greengard, P. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.18.8378 · Cited by 468 · 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
Maturation and Endosomal Targeting of β-Site Amyloid Precursor Protein-cleaving Enzyme
Huse, J. T., Pijak, D. S., Leslie, G. J., Lee, V. M.-Y., & Doms, R. W. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004175200 · Cited by 402 · see citing works
Mechtersheimer, S., Gutwein, P., Agmon-Levin, N., Stoeck, A., Oleszewski, M., Riedle, S., Postina, R., Fahrenholz, F., Fogel, M., Lemmon, V., et al. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200101099 · Cited by 391 · see citing works
Self-citationSmall, D. H., Nurcombe, V., Reed, G., Clarris, H. J., Moir, R. D., Beyreuther, K. T., & Masters, C. L. (1994) · Journal of Neuroscience · doi:10.1523/jneurosci.14-04-02117.1994 · Cited by 389 · 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
Vassar, R. J., & Citron, M. (2000) · Neuron · doi:10.1016/s0896-6273(00)00051-9 · Cited by 299 · see citing works
KOIKE, H., Tomioka, S., Sorimachi, H., Saido, T. C., Maruyama, K., Okuyama, A., Fujisawa‐Sehara, A., Ohno, S., Suzuki, K., & Ishiura, S. (1999) · Biochemical Journal · doi:10.1042/bj3430371 · Cited by 278 · see citing works
Dewachter, I., Reversé, D., Caluwaerts, N., Ris, L., Kuipéri, C., den Haute, C. V., Spittaels, K., Umans, L., Serneels, L., Thiry, E., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-09-03445.2002 · Cited by 237 · see citing works
Self-citationGowing, E., Roher, A. E., Woods, A. S., Cotter, R. J., Chaney, M., Little, S. P., & Ball, M. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78080-6 · Cited by 223 · see citing works
Dorpe, J. V., Smeijers, L., Dewachter, I., Nuyens, D., Spittaels, K., den Haute, C. V., Mercken, M. H., Moechars, D., Laenen, I., Kuipéri, C., et al. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64644-5 · Cited by 223 · see citing works
Self-citationLedesma, M. D., Silva, J. S. D., Craessaerts, K., Delacourte, A., Strooper, B. D., & Dotti, C. G. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd107 · Cited by 216 · see citing works
In vivo reduction of amyloid-β by a mutant copper transporter
Phinney, A. L., Drisaldi, B., Schmidt, S. D., Lugowski, S. J., Coronado, V. A., Liang, Y., Horne, P., Yang, J., Sekoulidis, J., Coomaraswamy, J., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332851100 · Cited by 201 · see citing works
Parvathy, S., Hussain, I., Karran, E. H., Turner, A. J., & Hooper, N. M. (1999) · Biochemistry · doi:10.1021/bi9906827 · Cited by 200 · see citing works
Zhang, Y., Calon, F., Zhu, C., Boado, R. J., & Pardridge, W. M. (2003) · Human Gene Therapy · doi:10.1089/10430340360464660 · Cited by 194 · see citing works
Sennvik, K., Fastbom, J., Blomberg, M. E., Wahlund, L., Winblad, B., & Benedikz, E. (2000) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00929-5 · Cited by 193 · see citing works
Wei, W., Wang, X., & Kusiak, J. W. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m111704200 · Cited by 190 · 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
Ishida, A., Furukawa, K., Keller, J. N., & Mattson, M. P. (1997) · Neuroreport · doi:10.1097/00001756-199707070-00009 · Cited by 178 · see citing works
Lüthi, A., van der Putten, H., Botteri, F., Mansuy, I., Meins, M., Frey, U., Sansig, G., Portet, C., Schmutz, M., Schröder, M. S., et al. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-12-04688.1997 · Cited by 176 · see citing works
Lannfelt, L., Basun, H., Wahlund, L., Rowe, B. A., & Wagner, S. L. (1995) · Nature Medicine · doi:10.1038/nm0895-829 · Cited by 173 · see citing works
Abeta 17-42 in Alzheimer's disease activates JNK and caspase-8 leading to neuronal apoptosis
Wei, W. (2002) · Brain · doi:10.1093/brain/awf205 · Cited by 155 · see citing works
In search of a better mouse test.
Wahlsten, D., Rustay, N., Metten, P., & Crabbe, J. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00033-x · Cited by 149 · see citing works
Barelli, H., Lebeau, A., Vizzavona, J., Delaère, P., Chevallier, N., Drouot, C., Marambaud, P., Ancolio, K., Buxbaum, J. D., Khorkova, O., et al. (1997) · Molecular Medicine · doi:10.1007/bf03401708 · Cited by 139 · see citing works
The Search for α-Secretase and its Potential as a Therapeutic Approach to Alzheimer's Disease
Hooper, N. M., & Turner, A. J. (2002) · Current Medicinal Chemistry · doi:10.2174/0929867023370121 · Cited by 127 · see citing works
Lee, J., Lau, K., Perkinton, M. S., Standen, C. L., Shemilt, S. J. A., Mercken, L., Cooper, J. D., McLoughlin, D. M., & Miller, C. C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300503200 · Cited by 86 · see citing works
Higgins, L. S., Murphy, G. M., Forno, L. S., Catalano, R., & Cordell, B. (1996) · Europe PMC (PubMed Central) · Cited by 70 · see citing works
Anderson, J. J., Höltz, G., Baskin, P. P., Wang, R., Mazzarelli, L., Wagner, S. L., & Menzaghi, F. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00244-4 · Cited by 62 · see citing works
Kozikowski, A. P., Nowak, I., Petukhov, P. A., et al. (2002) · Journal of Medicinal Chemistry · doi:10.1021/jm020350r · Cited by 47 · see citing works
Howard, L., & Glynn, P. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)48025-0 · Cited by 44 · see citing works
Caswell, M. D., Mok, S. S., Henry, A., et al. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00886.x · Cited by 18 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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
Amyloid Precursor Protein Processing and Alzheimer's Disease
O'Brien, R. J., & Wong, P. C. (2011) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-061010-113613 · Cited by 2,061 · see citing works
Trafficking and Proteolytic Processing of APP
Haass, C., Kaether, C., Thinakaran, G., & Sisodia, S. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006270 · Cited by 1,075 · see citing works
Kuhn, 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
Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease
Barage, S. H., & Sonawane, K. D. (2015) · Neuropeptides · doi:10.1016/j.npep.2015.06.008 · Cited by 579 · 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
η-Secretase processing of APP inhibits neuronal activity in the hippocampus
Willem, M., Tahirovic, S., Busche, M. A., Ovsepian, S. V., Chafai, M., Kootar, S., Hornburg, D., Evans, L. D. B., Moore, S., Daria, A., et al. (2015) · Nature · doi:10.1038/nature14864 · Cited by 398 · see citing works
The role of metallobiology and amyloid-β peptides in Alzheimer's disease
Roberts, B. R., Ryan, T. M., Bush, A. I., Masters, C. L., & Duce, J. A. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07500.x · Cited by 266 · see citing works
Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism
Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256 · see citing works
Self-citationKim, M., Suh, J., Romano, D., Truong, M. H., Mullin, K., Hooli, B., Norton, D., Tesco, G., Elliott, K., Wagner, S. L., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp323 · Cited by 234 · 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
Zhang, Y., Calon, F., Zhu, C., Boado, R. J., & Pardridge, W. M. (2003) · Human Gene Therapy · doi:10.1089/10430340360464660 · Cited by 194 · see citing works
Soluble 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
Haining, E. J., Yang, J., Bailey, R. L., Khan, K., Collier, R., Tsai, S., Watson, S. P., Frampton, J., Garcia, P., & Tomlinson, M. G. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.416503 · Cited by 163 · see citing works
The Role of Zinc in Alzheimer′s Disease
Watt, N. T., Whitehouse, I. J., & Hooper, N. M. (2011) · International Journal of Alzheimer’s Disease · doi:10.4061/2011/971021 · Cited by 148 · see citing works
Stancu, I.-C., Vasconcelos, B., Ris, L., Wang, P., Villers, A., Peeraer, E., Buist, A., Terwel, D., Baatsen, P., Oyelami, T., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1413-4 · Cited by 143 · see citing works
Self-citationAvramovich‐Tirosh, Y., Amit, T., Bar‐Am, O., Zheng, H., Fridkin, M., & Youdim, M. B. H. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04258.x · Cited by 130 · see citing works
Kojro, E., Postina, R., Buro, C., Meiringer, C., Gehrig‐Burger, K., & Fahrenholz, F. (2006) · The FASEB Journal · doi:10.1096/fj.05-4812fje · Cited by 118 · see citing works
Self-citationDisease modifying therapy for AD?<sup>1</sup>
Golde, T. E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04211.x · Cited by 117 · see citing works
Li, B., Liu, J., Gu, G., Han, X., Zhang, Q., & Zhang, W. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15001 · Cited by 110 · see citing works
Western, D., Timsina, J., Wang, L., Wang, C., Yang, C., Phillips, B., Wang, Y., Liu, M., Ali, M., Beric, A., et al. (2024) · Nature Genetics · doi:10.1038/s41588-024-01972-8 · Cited by 111 · see citing works
Wnt/&#946;-Catenin Signaling in Alzheimer’s Disease
Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95 · see citing works
Genetical genomics of behavior: a novel chicken genomic model for anxiety behavior
Johnsson, M., Williams, M. J., Jensen, P., & Wright, D. (2016) · Genetics · doi:10.1534/genetics.115.179010 · Cited by 62 · see citing works
Tackenberg, C., & Nitsch, R. M. (2019) · Molecular Brain · doi:10.1186/s13041-019-0447-2 · Cited by 56 · see citing works
LRP1 is critical for the surface distribution and internalization of the NR2B NMDA receptor subtype
Maier, W., Bednorz, M., Meister, S., Roebroek, A., Weggen, S., Schmitt, U., & Pietrzik, C. U. (2013) · Molecular Neurodegeneration · doi:10.1186/1750-1326-8-25 · Cited by 50 · see citing works
Self-citationEggert, S., Kins, S., Endres, K., & Brigadski, T. (2022) · Biological Chemistry · doi:10.1515/hsz-2021-0330 · Cited by 46 · see citing works
Self-citationTauopathy contributes to synaptic and cognitive deficits in a murine model for Alzheimer’s disease
Stancu, I., Ris, L., Vasconcelos, B., Marinangeli, C., Goeminne, L., Laporte, V., Haylani, L. E., Couturier, J., Schakman, O., Gailly, P., et al. (2014) · The FASEB Journal · doi:10.1096/fj.13-246702 · Cited by 48 · see citing works
Self-citationGDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein
Nakamura, M., Li, Y., Choi, B.-R., Matas-Rico, E., Troncoso, J., Takahashi, C., & Sockanathan, S. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe6178 · Cited by 38 · see citing works
Pathophysiological function of ADAMTS enzymes on molecular mechanism of Alzheimer’s disease
Gurses, M. S., Ural, M. N., Gulec, M. A., Akyol, O., & Akyol, S. (2016) · Aging and disease · doi:10.14336/ad.2016.0111 · Cited by 35 · see citing works
ADAM10 Prodomain Mutations Cause Late-Onset Alzheimer’s Disease: Not Just the Latest FAD
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
GUO, P., WANG, D., WANG, X., FENG, H., TANG, Y., SUN, R., ZHENG, Y., DONG, L., ZHAO, J., ZHANG, X., et al. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4957 · Cited by 30 · see citing works
- Authors
- Postina, R., Schroeder, A., Dewachter, I., Bohl, J., Schmitt, U., Kojro, E., Prinzen, C., Endres, K., Hiemke, C., Blessing, M., Flamez, P., Dequenne, A., Godaux, E., van Leuven, F., & Fahrenholz, F.
- Affiliations
- Johannes Gutenberg University Mainz (DE)
- KU Leuven (BE)
- University of Mons (BE)
- Corresponding author
- Fahrenholz, Falk
- Venue
- Journal of Clinical Investigation
- Published
- 2004-05-15
- Volume
- 113
- Issue
- 10
- Pages
- 1456-1464
- ISSN
- 0021-9738 (ISSN-L)
- OpenAlex
- W2132810311
- Cited by
- 638
- References
- 56
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 19 · 2023: 25 · 2022: 18 · 2021: 30 · 2020: 26 · 2019: 31 · 2018: 29 · 2017: 34 · 2016: 34 · 2015: 34 · 2014: 37 · 2013: 39 · 2012: 31
- FWCI
- 20.82
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Clinical Investigation (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Fonds Wetenschappelijk Onderzoek
- Fritz Thyssen Stiftung
- KU Leuven
- Vlaamse regering
- 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 › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, ADAM10, alpha-secretase, amyloid-beta, amyloid plaques, amyloid precursor protein, soluble APP alpha, long-term potentiation, cognitive impairment, hippocampus, non-amyloidogenic pathway, therapeutic target
- MeSH terms
- Alzheimer Disease, Amyloid, Amyloidosis, Animals, Disease Models, Animal, Hippocampus, Humans, Mice, Transgenic, Endopeptidases, Gene Expression, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Mice, 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 ›
Are you an author, or do you see a problem with this page? Request a review