Soluble amyloid precursor protein-α modulates β-secretase activity and amyloid-β generation
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In sporadic age-related forms of Alzheimer's disease (AD), it is unclear why amyloid-β (Aβ) peptides accumulate. Here we show that soluble amyloid precursor protein-α (sAPP-α) decreases Aβ generation by directly associating with β-site APP-converting enzyme (BACE)1, thereby modulating APP processing. Whereas specifically targeting sAPP-α using antibodies enhances Aβ production; in transgenic mice with AD-like pathology, sAPP-α overexpression decreases β-amyloid plaques and soluble Aβ. In support, immunoneutralization of sAPP-α increases APP amyloidogenic processing in these mice. Given our current findings, and because a number of risk factors for sporadic AD serve to lower levels of sAPP-α in brains of AD patients, inadequate sAPP-α levels may be sufficient to polarize APP processing towards the amyloidogenic, Aβ-producing route. Therefore, restoration of sAPP-α or enhancement of its association with BACE may be viable strategies to ameliorate imbalances in APP processing that can lead to AD pathogenesis.
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sAPPα interacts with β-secretase to inhibit its cleavage of APP, further stimulating non-amyloidogenic APP processing.
“sAPPα interacts with β-secretase to inhibit its cleavage of APP, to further stimulate non-amyloidogenic APP processing (6).”
From GDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein (2021) · cites this paper as [6]
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RETRACTED: SIRT1 Suppresses β-Amyloid Production by Activating the α-Secretase Gene ADAM10
Dönmez, G., Wang, D., Cohen, D. E., & Guarente, L. (2010) · Cell · doi:10.1016/j.cell.2010.06.020 · Cited by 433 · see citing works
RetractedThe Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · 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
Vassar, R., Bennett, B. D., Babu-Khan, S., Kahn, S., Mendiaz, E. A., Denis, P., Teplow, D. B., Ross, S., Amarante, P., Loeloff, R., et al. (1999) · Science · doi:10.1126/science.286.5440.735 · Cited by 3,876 · see citing works
Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works
Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes
Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · see citing works
Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006 · see citing works
Self-citationMattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I. M., & Rydel, R. E. (1993) · Neuron · doi:10.1016/0896-6273(93)90315-i · Cited by 795 · see citing works
Self-citationγ-Secretase is a membrane protein complex comprised of presenilin, nicastrin, aph-1, and pen-2
Kimberly, W. T., LaVoie, M. J., Ostaszewski, B. L., Ye, W., Wolfe, M. S., & Selkoe, D. J. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1037392100 · Cited by 763 · see citing works
Control of Peripheral Nerve Myelination by the ß-Secretase BACE1
Willem, M., Garratt, A. N., Novak, B., Citron, M., Kaufmann, S., Rittger, A., DeStrooper, B., Saftig, P., Birchmeier, C., & Haass, C. (2006) · Science · doi:10.1126/science.1132341 · Cited by 703 · see citing works
Lower cognitive function in the presence of obesity and hypertension: the Framingham heart study
Elias, M. F., Elias, P. K., SULLIVAN, L. M., Wolf, P. A., & D’Agostino, R. B. (2003) · International Journal of Obesity · doi:10.1038/sj.ijo.802225 · Cited by 691 · see citing works
Diabetes Mellitus and Risk of Alzheimer's Disease and Dementia with Stroke in a Multiethnic Cohort
Luchsinger, J. A. (2001) · American Journal of Epidemiology · doi:10.1093/aje/154.7.635 · Cited by 682 · 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
Bace1 modulates myelination in the central and peripheral nervous system
Hu, X., Hicks, C. W., He, W., Wong, P., Macklin, W. B., Trapp, B. D., & Yan, R. (2006) · Nature Neuroscience · doi:10.1038/nn1797 · Cited by 608 · see citing works
Kapogiannis, D., & Mattson, M. P. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70277-5 · Cited by 594 · see citing works
Self-citationOltersdorf, T., Fritz, L. C., Schenk, D. B., Lieberburg, I. M., Johnson‐Wood, K., Beattie, E. C., Ward, P. J., Blacher, R. W., Dovey, H. F., & Sinha, S. (1989) · Nature · doi:10.1038/341144a0 · Cited by 457 · see citing works
Cholesterol-Dependent γ-Secretase Activity in Buoyant Cholesterol-Rich Membrane Microdomains
Schindler, S. E., Das, P., Nyborg, A. C., McLendon, C., Shoji, M., Kawarabayashi, T., Younkin, L. H., Younkin, S. G., & Golde, T. E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0470 · Cited by 426 · 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
Self-citationA vector for expressing foreign genes in the brains and hearts of transgenic mice
Borchelt, D., Davis, J. A., Fischer, M., Lee, M. K., Slunt, H. H., Ratovitski, T., Regard, J. B., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., et al. (1996) · Genetic Analysis Biomolecular Engineering · doi:10.1016/s1050-3862(96)00167-2 · Cited by 362 · 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
Tamagno, E., Guglielmotto, M., Aragno, M., Borghi, R., Autelli, R., Giliberto, L., Muraca, G., Danni, O., Zhu, X., Smith, M. A., et al. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.05072.x · Cited by 338 · see citing works
Self-citationFurukawa, K., Barger, S. W., Blalock, E. M., & Mattson, M. P. (1996) · Nature · doi:10.1038/379074a0 · Cited by 332 · see citing works
Self-citationNeuronal membrane cholesterol loss enhances amyloid peptide generation
Abad‐Rodríguez, J., Ledesma, M. D., Craessaerts, K., Perga, S., Medina, M., Delacourte, A., Dingwall, C., Strooper, B. D., & Dotti, C. G. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404149 · Cited by 329 · see citing works
Tamagno, E., Parola, M., Bardini, P., Piccini, A., Borghi, R., Guglielmotto, M., Santoro, G., Davit, A., Danni, O., Smith, M. A., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02895.x · Cited by 324 · see citing works
Benjannet, S., Elagoz, A., Wickham, L., Mamarbachi, M., Munzer, J. S., Basak, A., Lazure, C., Cromlish, J. A., Sisodia, S., Checler, F., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009899200 · Cited by 301 · see citing works
Wong, H. K., Sakurai, T., Oyama, F., Kaneko, K., Wada, K., Miyazaki, H., Kurosawa, M., Strooper, B. D., Säftig, P., & Nukina, N. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414648200 · Cited by 290 · see citing works
Epidemiology of clinically diagnosed Alzheimer's disease
Rocca, W. A., Amaducci, L. A., & Schoenberg, B. S. (1986) · Annals of Neurology · doi:10.1002/ana.410190502 · Cited by 287 · see citing works
Kitazume, S., Tachida, Y., Oka, R., Shirotani, K., Saido, T. C., & Hashimoto, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.241509198 · Cited by 277 · see citing works
Stein, T. D., Anders, N. J., DeCarli, C. S., Chan, S. L., Mattson, M. P., & Johnson, J. A. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.2211-04.2004 · Cited by 276 · see citing works
Self-citationCortical senile plaques in coronary artery disease, aging and Alzheimer's disease
Sparks, D. L., Hunsaker, J. C., Scheff, S. W., Kryscio, R. J., Henson, J. L., & Markesbery, W. R. (1990) · Neurobiology of Aging · doi:10.1016/0197-4580(90)90024-t · Cited by 271 · 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
The Low Density Lipoprotein Receptor-related Protein (LRP) Is a Novel β-Secretase (BACE1) Substrate
Arnim, C. A. F. V., Kinoshita, A., Peltan, I. D., Tangredi, M. M., Herl, L. D., Lee, B. M., Spoelgen, R., Hshieh, T. T., Ranganathan, S., Battey, F. D., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414248200 · Cited by 255 · see citing works
Kim, 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
Walsh, D. M., Klyubin, I., Shankar, G. M., Townsend, M., Fadeeva, J. V., Betts, V., Podlisny, M. B., Cleary, J. P., Ashe, K. H., Rowan, M. J., et al. (2005) · Biochemical Society Transactions · doi:10.1042/bst20051087 · Cited by 220 · see citing works
Young-Pearse, T. L., Chen, A. C., Chang, R., Marquez, C., & Selkoe, D. J. (2008) · Neural Development · doi:10.1186/1749-8104-3-15 · Cited by 210 · see citing works
Genetic deletion of BACE1 in mice affects remyelination of sciatic nerves
Hu, X., He, W.-X., Diaconu, C., Tang, X., Kidd, G., Macklin, W., Trapp, B. D., & Yan, R. (2008) · The FASEB Journal · doi:10.1096/fj.08-106666 · Cited by 199 · see citing works
Hussain, I., Hawkins, J., Harrison, D. C., Hille, C. J., Wayne, G. J., Cutler, L., Buck, T., Walter, D. S., Demont, E. H., Howes, C., et al. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04260.x · Cited by 197 · see citing works
Yan, R., Han, P., Miao, H., Greengard, P., & Xu, H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104350200 · Cited by 179 · see citing works
Ishida, A., Furukawa, K., Keller, J. N., & Mattson, M. P. (1997) · Neuroreport · doi:10.1097/00001756-199707070-00009 · Cited by 177 · see citing works
Self-citationHydrogen Peroxide Promotes Aβ Production through JNK-dependent Activation of γ-Secretase
Shen, C., Chen, Y., Liu, H., Zhang, K., Zhang, T., Lin, A., & Jing, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800013200 · Cited by 168 · see citing works
Tong, X., Nicolakakis, N., Kocharyan, A., & Hamel, É. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4031-05.2005 · Cited by 153 · see citing works
Racchi, M., Baetta, R., Salvietti, N., Ianna, P., Franceschini, G., Paoletti, R., Fumagalli, R., Govoni, S. M., Trabucchi, M., & Soma, M. R. (1997) · Biochemical Journal · doi:10.1042/bj3220893 · Cited by 151 · see citing works
Barger, S. W., Fiscus, R. R., Ruth, P., Hofmann, F. B., & Mattson, M. P. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.64052087.x · Cited by 144 · see citing works
Self-citationGralle, M., Caarls, M. B., & Wouters, F. S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808755200 · Cited by 138 · see citing works
ADAM-10 over-expression increases cortical synaptogenesis
Bell, K. F. S., Zheng, L., Fahrenholz, F., & Cuello, A. C. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.11.004 · Cited by 120 · see citing works
Quiroz‐Baez, R., Rojas, E., & Arias, C. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.06.012 · Cited by 92 · see citing works
Kaden, D., Munter, L. M., Joshi, M., Treiber, C., Weise, C., Bethge, T., Voigt, P., Schaefer, M., Beyermann, M., Reif, B., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m708046200 · Cited by 90 · see citing works
Soriano, S., Chyung, A. S. C., Chen, X., Stokin, G. B., Lee, V. M. ‐., & Koo, E. H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.45.32295 · Cited by 89 · see citing works
CD45 Deficiency Drives Amyloid-β Peptide Oligomers and Neuronal Loss in Alzheimer's Disease Mice
Zhu, Y., Hou, H., Rezai-Zadeh, K. P., Giunta, B. N., Ruscin, A., Gemma, C., Jin, J., Dragicevic, N., Bradshaw, P. C., Rasool, S., et al. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3268-10.2011 · Cited by 89 · see citing works
Self-citationKamboh, M. I., Ferrell, R. E., & DeKosky, S. T. (1998) · Neuroscience Letters · doi:10.1016/s0304-3940(98)00141-4 · Cited by 79 · see citing works
Hussain, I., Hawkins, J., Shikotra, A., Riddell, D. R., Faller, A., & Dingwall, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304186200 · Cited by 60 · see citing works
Hahn, S., Brüning, T., Neß, J., Czirr, E., Baches, S., Gijsen, H. J. M., Korth, C., Pietrzik, C. U., Bulic, B., & Weggen, S. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.07118.x · Cited by 56 · see citing works
Webster, N. J., Green, K. N., Peers, C., & Vaughan, P. F. T. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01236.x · Cited by 56 · see citing works
Takeda, K., Araki, W., Akiyama, H., & Tabira, T. (2004) · The FASEB Journal · doi:10.1096/fj.03-1070fje · Cited by 53 · see citing works
Webster, N. J., Green, K. N., Settle, V. J., Peers, C., & Vaughan, P. F. T. (2004) · Molecular Brain Research · doi:10.1016/j.molbrainres.2004.06.042 · Cited by 38 · see citing works
Auerbach, I. D., & Vinters, H. V. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-200606000-00009 · Cited by 27 · see citing works
Bailey, A. R., Hou, H., Obregon, D. F., Tian, J., Zhu, Y., Zou, Q., Nikolic, W. V., Bengtson, M. A., Mori, T., Murphy, T. K., et al. (2011) · The FASEB Journal · doi:10.1096/fj.11-195438 · Cited by 21 · see citing works
Self-citationNa, C. H., Jeon, S. H., Zhang, G., Olson, G. L., & Chae, C. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04441.x · Cited by 15 · see citing works
BACE1 is a newly discovered protein secreted by the pancreas which cleaves enteropeptidase in vitro.
Hoffmeister, A., Dietz, G., Zeitschel, U., Mössner, J., Roßner, S., & Stahl, T. (2009) · PubMed · Cited by 13 · see citing works
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1 of the 60 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [42]Milne JC Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes Nature 450 712 716 2007 18046409 PMC2753457
Cited by
Sorted by citations
Not just amyloid: physiological functions of the amyloid precursor protein family
Müller, U. C., Deller, T., & Korte, M. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.29 · Cited by 634 · see citing works
Cellular Functions of the Amyloid Precursor Protein from Development to Dementia
van der Kant, R., & Goldstein, L. S. B. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.022 · Cited by 246 · see citing works
Reversal of cognitive decline: A novel therapeutic program
Bredesen, D. E. (2014) · Aging · doi:10.18632/aging.100690 · Cited by 231 · see citing works
Olloquequi, J., Cornejo-Córdova, E., Verdaguer, E., Soriano, F. X., Binvignat, O., Auladell, C., & Camins, A. (2018) · Journal of Psychopharmacology · doi:10.1177/0269881118754680 · Cited by 190 · see citing works
The Alzheimer’s Disease Amyloid-Beta Hypothesis in Cardiovascular Aging and Disease
Stakos, D. A., Stamatelopoulos, K., Bampatsias, D., Sachse, M., Zormpas, E., Vlachogiannis, N. I., Tual-Chalot, S., & Stellos, K. (2020) · Journal of the American College of Cardiology · doi:10.1016/j.jacc.2019.12.033 · Cited by 188 · see citing works
Acute function of secreted amyloid precursor protein fragment APPsα in synaptic plasticity
Hick, M., Herrmann, U., Weyer, S. W., Mallm, J., Tschäpe, J., Borgers, M., Mercken, M. H., Roth, F. C., Draguhn, A., Slomianka, L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1368-x · Cited by 186 · see citing works
Exercise and BDNF reduce Aβ production by enhancing α‐secretase processing of APP
Nigam, S. M., Xu, S., Kritikou, J. S., Marosi, K., Brodin, L., & Mattson, M. P. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14034 · Cited by 186 · see citing works
Self-citationSalivary biomarkers for the diagnosis and monitoring of neurological diseases
Farah, R., Haraty, H., Salame, Z., Fares, Y., Ojcius, D. M., & Sadier, N. S. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.03.004 · Cited by 170 · see citing works
Viral gene transfer of APPsα rescues synaptic failure in an Alzheimer’s disease mouse model
Fol, R. R., Braudeau, J., Ludewig, S., Abel, T., Weyer, S. W., Roederer, J.-P., Brod, F., Audrain, M., Bemelmans, A., Buchholz, C. J., et al. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1498-9 · Cited by 168 · see citing works
Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161 · see citing works
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160 · see citing works
Seizures in Alzheimer’s disease
Born, H. A. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.11.051 · Cited by 131 · see citing works
Amyloid Precursor Protein and Alzheimer’s Disease
Orobets, K. S., & Karamyshev, A. L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914794 · Cited by 141 · see citing works
Uddin, M. S., Kabir, M. T., Rahman, M. S., Behl, T., Jeandet, P., Ashraf, G. M., Najda, A., Bin-Jumah, M. N., El-Seedi, H. R., & Abdel‐Daim, M. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165858 · Cited by 127 · see citing works
Zhang, S., Obregon, D. F., Ehrhart, J. C., Deng, J., Tian, J., Hou, H., Giunta, B. N., Sawmiller, D. R., & Tan, J. (2013) · Journal of Neuroscience Research · doi:10.1002/jnr.23244 · Cited by 123 · see citing works
Self-citationTherapeutic Potential of Secreted Amyloid Precursor Protein APPsα
Mockett, B. G., Richter, M., Abraham, W. C., & Müller, U. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00030 · Cited by 115 · see citing works
Phosphorylation Signaling in APP Processing in Alzheimer’s Disease
Zhang, T., Chen, D., & Lee, T. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010209 · Cited by 114 · see citing works
APP Receptor? To Be or Not To Be
Deyts, C., Thinakaran, G., & Parent, A. (2016) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2016.01.005 · Cited by 109 · see citing works
Mori, T., Koyama, N., Tan, J., Segawa, T., Maeda, M., & Town, T. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004280 · Cited by 99 · see citing works
Self-citationHu, Y., Li, C., & Shen, W. (2014) · Neuropathology · doi:10.1111/neup.12115 · Cited by 99 · see citing works
Weyer, S. W., Zagrebelsky, M., Herrmann, U., Hick, M., Ganss, L., Gobbert, J., Gruber, M., Altmann, C., Körte, M., Deller, T., et al. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-36 · Cited by 98 · see citing works
Single-Cell Detection of Secreted Aβ and sAPPα from Human IPSC-Derived Neurons and Astrocytes
Liao, M.-C., Muratore, C., Gierahn, T. M., Sullivan, S. E., Srikanth, P., Jager, P. L. D., Love, J. C., & Young‐Pearse, T. L. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2735-15.2016 · Cited by 96 · see citing works
Habib, A., Sawmiller, D. R., & Tan, J. (2016) · Journal of Neuroscience Research · doi:10.1002/jnr.23823 · Cited by 95 · see citing works
Self-citationIsolation Housing Exacerbates Alzheimer's Disease-Like Pathophysiology in Aged APP/PS1 Mice
Huang, H., Wang, L., Cao, M., Marshall, C., Gao, J., Xiao, N., Hu, G., & Xiao, M. (2015) · The International Journal of Neuropsychopharmacology · doi:10.1093/ijnp/pyu116 · Cited by 92 · see citing works
Deng, J., Habib, A., Obregon, D. F., Barger, S. W., Giunta, B. N., Wang, Y., Hou, H., Sawmiller, D. R., & Tan, J. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13351 · Cited by 91 · see citing works
Self-citationAPP as a Protective Factor in Acute Neuronal Insults
Hefter, D., & Draguhn, A. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00022 · Cited by 89 · see citing works
Richter, M., Ludewig, S., Winschel, A., Abel, T., Bold, C. S., Salzburger, L., Klein, S., Han, K., Weyer, S. W., Fritz, A., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798335 · Cited by 86 · see citing works
ADAM10 and BACE1 are localized to synaptic vesicles
Lundgren, J. L., Ahmed, S., Schedin‐Weiss, S., Gouras, G. K., Winblad, B. G., Tjernberg, L. O., & Frykman, S. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13287 · Cited by 82 · see citing works
Wang, L., & Mao, X. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22052360 · Cited by 84 · see citing works
SIRT3 activator Honokiol attenuates β-Amyloid by modulating amyloidogenic pathway
Ramesh, S., Govindarajulu, M., Lynd, T. O., Briggs, G. H., Adamek, D., Jones, E., Heiner, J., Majrashi, M., Moore, T., Amin, R., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0190350 · Cited by 81 · see citing works
García-González, L., Pilat, D., Baranger, K., & Rivera, S. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00244 · Cited by 65 · see citing works
Alzheimer culprits: Cellular crossroads and interplay
Claeysen, S., Cochet, M., Donneger, R., Dumuis, A., Bockaert, J., & Giannoni, P. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.05.008 · Cited by 79 · see citing works
Amyloid, APP, and Electrical Activity of the Brain
Hefter, D., Ludewig, S., Draguhn, A., & Körte, M. (2019) · The Neuroscientist · doi:10.1177/1073858419882619 · Cited by 76 · see citing works
Mori, T., Koyama, N., Yokoo, T., Segawa, T., Maeda, M., Sawmiller, D. R., Tan, J., & Town, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012330 · Cited by 78 · see citing works
Self-citationThe Ubiquitin System in Alzheimer’s Disease
Harris, L. D., Jasem, S., & Licchesi, J. D. F. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-38266-7_8 · Cited by 76 · see citing works
Characterization of AD-like phenotype in aged APPSwe/PS1dE9 mice
Huang, H., Nie, S., Cao, M., Marshall, C., Gao, J., Xiao, N., Hu, G., & Xiao, M. (2016) · AGE · doi:10.1007/s11357-016-9929-7 · Cited by 75 · see citing works
Dar, N., & Glazner, G. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03404-x · Cited by 62 · see citing works
β-Secretase: its biology as a therapeutic target in diseases
Wang, H., Li, R., & Shen, Y. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.01.008 · Cited by 74 · see citing works
Amyloid Cascade Hypothesis for the Treatment of Alzheimer’s Disease: Progress and Challenges
Wu, T., Ding, L., Cheng, Y., Jiang, S., Riaz, M. W., Fu, N., Mou, C., Ye, M., & Zheng, Y. (2022) · Aging and Disease · doi:10.14336/ad.2022.0412 · Cited by 75 · see citing works
Pasciuto, E., Ahmed, T., Wahle, T., Gardoni, F., D’Andrea, L., Pacini, L., Jacquemont, S., Tassone, F., Balschun, D., Dotti, C. G., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.06.032 · Cited by 71 · see citing works
Nizari, S., Guo, L., Davis, B. M., Normando, E. M., Galvão, J., Turner, L., Bizrah, M., Dehabadi, M. H., Tian, K., & Cordeiro, M. F. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.397 · Cited by 69 · see citing works
Exercise decreases BACE and APP levels in the hippocampus of a rat model of Alzheimer's disease
Alkadhi, K. A., & Dao, A. T. (2017) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2017.11.008 · Cited by 62 · see citing works
Huang, W., Chen, P., Yu, K., Han, Y., Song, M., & Li, Y. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.09.114 · Cited by 59 · see citing works
Expression and Processing of Amyloid Precursor Protein in Vascular Endothelium
d’Uscio, L. V., He, T., & Katušić, Z. S. (2016) · Physiology · doi:10.1152/physiol.00021.2016 · Cited by 56 · see citing works
Bai, N., Li, N., Cheng, R., Guan, Y., Zhao, X., Song, Z., Xu, H., Yi, F., Jiang, B., Li, X., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111062 · Cited by 57 · see citing works
sAβPPα is a Potent Endogenous Inhibitor of BACE1
Peters-Libeu, C. A., Campagna, J. J., Mitsumori, M., Poksay, K. S., Spilman, P. R., Sabogal, A., Bredesen, D. E., & John, V. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150282 · Cited by 56 · see citing works
Mori, T., Koyama, N., Tan, J., Segawa, T., Maeda, M., & Town, T. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.762658 · Cited by 57 · see citing works
Self-citationPotential Enzymatic Targets in Alzheimer’s: A Comprehensive Review
Alam, J., & Sharma, L. K. (2018) · Current Drug Targets · doi:10.2174/1389450119666180820104723 · Cited by 56 · see citing works
Role of Receptors in Relation to Plaques and Tangles in Alzheimer’s Disease Pathology
Sharma, K., Pradhan, S., Duffy, L. K., Yeasmin, S., Bhattarai, N., & Schulte, M. K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312987 · Cited by 59 · see citing works
MMP13 inhibition rescues cognitive decline in Alzheimer transgenic mice via BACE1 regulation
Zhu, B., Long, Y., Luo, W., Yan, Z., Lai, Y., Zhao, L., Zhou, W., Wang, Y., Shen, L., Liu, L., et al. (2018) · Brain · doi:10.1093/brain/awy305 · Cited by 53 · see citing works
Al-Kuraishy, H. M., Jabir, M. S., Al-Gareeb, A. I., Albuhadily, A. K., Albukhaty, S., Sulaiman, G. M., & Batiha, G. E. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102119 · Cited by 53 · see citing works
Supraphysiologic-dose anabolic–androgenic steroid use: A risk factor for dementia?
Kaufman, M. J., Kanayama, G., Hudson, J. I., & Pope, H. G. (2019) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2019.02.014 · Cited by 54 · see citing works
The role of synaptic activity in the regulation of amyloid beta levels in Alzheimer's disease
Cheng, X., Wu, J., Geng, M., & Xiong, J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.11.021 · Cited by 48 · see citing works
miR-30a-5p induces Aβ production via inhibiting the nonamyloidogenic pathway in Alzheimer’s disease
Sun, T., Zhao, K., Liu, M., Cai, Z., Zeng, L., Zhang, J., Li, Z., & Liu, R. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106153 · Cited by 49 · see citing works
Jarosz-Griffiths, H., Corbett, N. J., Rowland, H. A., Fisher, K., Jones, A. C., Baron, J., Howell, G. J., Cowley, S. A., Chintawar, S., Cader, M. Z., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005364 · Cited by 44 · see citing works
Regulation of the α-secretase ADAM10 at transcriptional, translational and post-translational levels
Vincent, B. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.020 · Cited by 45 · see citing works
Tok, S., Ahnaou, A., & Drinkenburg, W. H. I. M. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-210397 · Cited by 44 · see citing works
Mockett, B. G., Guévremont, D., Elder, M. K., Parfitt, K. D., Peppercorn, K., Morrissey, J. A., Singh, A., Hintz, T. J., Kochen, L., Dieck, S. T., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1826-18.2019 · Cited by 43 · see citing works
Secretases Related to Amyloid Precursor Protein Processing
Liu, X., Liu, Y., & Ji, S. (2021) · Membranes · doi:10.3390/membranes11120983 · Cited by 41 · see citing works
Srinivasan, E., Chandrasekhar, G., Chandrasekar, P., Anbarasu, K., Vickram, A., Tayubi, I. A., Rajasekaran, R., & Karunakaran, R. (2021) · Frontiers in Chemistry · doi:10.3389/fchem.2021.753146 · Cited by 41 · see citing works
Hefter, D., Kaiser, M., Weyer, S. W., Papageorgiou, I. E., Both, M., Kann, O., Müller, U., & Draguhn, A. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.4130-15.2016 · Cited by 41 · see citing works
Durand, D., Carniglia, L., Turati, J., Ramírez, D., Saba, J., Caruso, C. M., & Lasaga, M. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.05.008 · Cited by 41 · see citing works
Ryan, M. M., Morris, G. P., Mockett, B. G., Bourne, K., Abraham, W. C., Tate, W. P., & Williams, J. M. (2013) · BMC Genomics · doi:10.1186/1471-2164-14-376 · Cited by 39 · see citing works
Spilman, P. R., Corset, V., Gorostiza, O., Poksay, K. S., Galvan, V., Zhang, J., Rao, R., Peters-Libeu, C., Vincelette, J., McGeehan, A., et al. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-151046 · Cited by 39 · see citing works
Astroglial mGlu3 receptors promote alpha-secretase-mediated amyloid precursor protein cleavage
Durand, D., Carniglia, L., Beauquis, J., Caruso, C. M., Saravia, F., & Lasaga, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.11.015 · Cited by 39 · see citing works
GDE2-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
Liu, P., Zhao, B., Wei, M., Li, Y., Liu, J., Ma, L., Shang, S., Huo, K., Wang, J., Li, R., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-191317 · Cited by 38 · see citing works
Ristori, E., Donnini, S., & Ziche, M. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.01056 · Cited by 38 · see citing works
Sawmiller, D. R., Habib, A., Hou, H., Mori, T., Fan, A., Tian, J., Jin, Z., Giunta, B. N., Sanberg, P. R., Mattson, M. P., et al. (2019) · Biological Psychiatry · doi:10.1016/j.biopsych.2019.04.026 · Cited by 37 · see citing works
Self-citationRetractedFernandez, A. M., Hervás, R., Dominguez-Fraile, M., Navarro, V., Gómez‐Gutierrez, P., Vega, M., Vitórica, J., Pérez, J. J., & Torres‐Alemán, I. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160149 · Cited by 36 · see citing works
Hoey, S. E., Buonocore, F., Cox, C. J., Hammond, V. J., Perkinton, M. S., & Williams, R. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078155 · Cited by 33 · see citing works
Perez, F. P., Maloney, B., Chopra, N., Morisaki, J., & Lahiri, D. K. (2021) · Scientific Reports · doi:10.1038/s41598-020-77808-2 · Cited by 32 · see citing works
Jackson, H. M., Onos, K. D., Pepper, K. W., Graham, L. C., Akeson, E. C., Byers, C., Reinholdt, L. G., Frankel, W. N., & Howell, G. R. (2015) · PLoS ONE · doi:10.1371/journal.pone.0125897 · Cited by 32 · see citing works
Meng, T., Cao, Q. C., Lei, P., Bush, A. I., Xiang, Q., Su, Z., He, X., Rogers, J. T., Chiu, I., Zhang, Q., et al. (2017) · Molecular Therapy — Nucleic Acids · doi:10.1016/j.omtn.2017.05.004 · Cited by 31 · see citing works
Family C G-Protein-Coupled Receptors in Alzheimer’s Disease and Therapeutic Implications
Prà, I. D., Armato, U., & Chiarini, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01282 · Cited by 31 · see citing works
Li, S., Hou, H., Mori, T., Sawmiller, D. R., Smith, A., Tian, J., Wang, Y., Giunta, B. N., Sanberg, P. R., Zhang, S., et al. (2015) · Scientific Reports · doi:10.1038/srep11322 · Cited by 28 · see citing works
Self-citationAnimal models of Alzheimer’s disease: preclinical insights and challenges
Xu, Q., Yang, W., Zhong, M., Lin, Z., Gray, N. E., & Xian, Y. (2023) · Acta Materia Medica · doi:10.15212/amm-2023-0001 · Cited by 28 · see citing works
Post-translational regulation of the β-secretase BACE1
Araki, W. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.04.009 · Cited by 28 · see citing works
Cosmosiin Increases ADAM10 Expression via Mechanisms Involving 5’UTR and PI3K Signaling
Min, Z., Tang, Y., Hu, X., Zhu, B., Ma, Y., Zha, J., Deng, X., Yan, Z., & Chen, G. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00198 · Cited by 27 · see citing works
Wang, X., Song, R., Lu, W., Liu, Z., Wang, L., Zhu, X., Liu, Y., Sun, Z., Li, J., & Li, X. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00157 · Cited by 27 · see citing works
Neuroprotective Role of Omega-3 Fatty Acids: Fighting Alzheimer’s Disease
Chávez-Castillo, M., Gotera, M. P., Durán, P., Diaz, M. P., Nava, M., Cano, C., Díaz-Camargo, E. A., Cano, G., Cano, R., Rivera-Porras, D., et al. (2025) · Molecules · doi:10.3390/molecules30153057 · Cited by 26 · see citing works
Vasconcelos-Filho, F. S. L., Oliveira, L. C. D. R., de Freitas, T. B. C., de Pontes, P. A. D. S., da Rocha-e-Silva, R. C., Godinho, W. D. N., Chaves, E. M. C., da Silva, C. G. L., Soares, P. M., & Ceccatto, V. M. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111502 · Cited by 26 · see citing works
Upregulation of APP, ADAM10 and ADAM17 in the Denervated Mouse Dentate Gyrus
Turco, D. D., Schlaudraff, J., Bonin, M., & Deller, T. (2014) · PLoS ONE · doi:10.1371/journal.pone.0084962 · Cited by 26 · see citing works
Platelet-Derived Secreted Amyloid-Precursor Protein-β as a Marker for Diagnosing Alzheimer’s Disease
Marksteiner, J., & Humpel, C. (2013) · Current Neurovascular Research · doi:10.2174/15672026113109990022 · Cited by 24 · see citing works
Mitochondrial defects: An emerging theranostic avenue towards Alzheimer's associated dysregulations
Mani, S., Swargiary, G., Singh, M., Agarwal, S., Dey, A., Ojha, S. K., & Jha, N. K. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119985 · Cited by 23 · see citing works
Waigi, E. W., Webb, R. C., Moss, M. A., Uline, M. J., McCarthy, C. G., & Wenceslau, C. F. (2023) · GeroScience · doi:10.1007/s11357-023-00748-y · Cited by 24 · see citing works
Masi, M., Biundo, F., Fiou, A., Racchi, M., Pascale, A., & Buoso, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076639 · Cited by 20 · see citing works
Wittrahm, R., Takalo, M., Kuulasmaa, T., Mäkinen, P. M., Mäkinen, P., Končarević, S., Fartzdinov, V., Selzer, S., Kokkola, T., Antikainen, L., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106140 · Cited by 21 · see citing works
Sun, R., He, T., Pan, Y., & Katušić, Z. S. (2018) · Aging · doi:10.18632/aging.101362 · Cited by 23 · see citing works
The Potential Regulators of Amyloidogenic Pathway of APP Processing in Alzheimer’s Disease
Krawczuk, D., Kulczyńska‐Przybik, A., & Mroczko, B. (2025) · Biomedicines · doi:10.3390/biomedicines13071513 · Cited by 23 · see citing works
Huang, W., Chen, W., Jiang, L., Yang, Y., Yao, L., & Li, K. (2018) · Frontiers in Genetics · doi:10.3389/fgene.2018.00540 · Cited by 22 · see citing works
Yang, Y., Zhang, J., Yang, X., Li, Z., Wang, J., Lu, C., Nan, A., & Zou, Y. (2021) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2021.112365 · Cited by 21 · see citing works
APP mediates tau uptake and its overexpression leads to the exacerbated tau pathology
Chen, J., Fan, A., Li, S., Xiao, Y. C., Fu, Y., Chen, J.-S., Zi, D., Zeng, L., & Tan, J. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04774-z · Cited by 21 · see citing works
Self-citationRoselli, S., Şatır, T. M., Camacho, R., Fruhwürth, S., Bergström, P., Zetterberg, H., & Agholme, L. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01374-0 · Cited by 22 · see citing works
Ohline, S. M., Chan, C., Schoderboeck, L., Wicky, H. E., Tate, W., Hughes, S., & Abraham, W. (2021) · Molecular Brain · doi:10.1186/s13041-021-00889-1 · Cited by 13 · see citing works
Song, C., Li, S., Mai, Y., Li, L., Dai, G., Zhou, Y., Liang, X., Zou, O. M., Wang, Y., Zhou, L., et al. (2024) · Journal of Neuroinflammation · doi:10.1186/s12974-024-03162-z · Cited by 19 · see citing works
The Role of Neprilysin and Insulin-Degrading Enzyme in the Etiology of Sporadic Alzheimer's Disease
Morito, T., Hashimoto, S., Takamura, R., Watamura, N., Kakiya, N., Fujioka, R., Mihara, N., Sekiguchi, M., Watanabe-Iwata, K., Kamano, N., et al. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.2152-24.2025 · Cited by 21 · see citing works
Chen, R., Zhang, T., Sun, Y.-Y., Sun, Y.-M., Chen, W., Shi, N., Shen, F., Zhang, Y., Liu, K.-Y., & Sun, X.-J. (2015) · Neural Regeneration Research · doi:10.4103/1673-5374.165511 · Cited by 20 · see citing works
Matrone, C. (2023) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2023.01.008 · Cited by 17 · see citing works
Proteases at work: cues for understanding neural development and degeneration
Säftig, P. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00013 · Cited by 17 · see citing works
- Authors
- Obregon, D., Hou, H., Deng, J., Giunta, B., Tian, J., Darlington, D., Shahaduzzaman, M., Zhu, Y., Mori, T., Mattson, M. P., & Tan, J.
- Affiliations
- University of South Florida (US)
- Social Insurance Saitama Chuo Hospital (JP)
- National Institute on Aging (US)
- Corresponding author
- Tan, Jun
- Venue
- Nature Communications
- Published
- 2012-04-10
- Volume
- 3
- Issue
- 1
- Pages
- 777-777
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC3520614
- OpenAlex
- W2065184914
- Cited by
- 192
- References
- 60
- Citations by year
- 2026: 14 · 2025: 13 · 2024: 14 · 2023: 16 · 2022: 11 · 2021: 18 · 2020: 14 · 2019: 12 · 2018: 18 · 2017: 12 · 2016: 15 · 2015: 12 · 2014: 10 · 2013: 10 · 2012: 2
- FWCI
- 7.29
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- U.S. Department of Veterans Affairs
- Office of Research and Development
- National Institutes of Health
- Japan Society for the Promotion of Science (22500320)
- National Institute on Aging (R42AG031586, R01AG032432)
- 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
- sAPPα, BACE1, beta-secretase, amyloid-beta production, APP processing, Alzheimer's disease, amyloid plaques, neurotrophic factors, sporadic Alzheimer's disease, transgenic mouse model, immunoneutralization
- MeSH terms
- Alzheimer Disease, Animals, Cell Line, Humans, Mice, Inbred C3H, Mice, Inbred C57BL, Mice, Transgenic, Protein Processing, Post-Translational, Amyloid beta-Peptides, Aspartic Acid Endopeptidases, Amyloid beta-Protein Precursor, Amino Acid Motifs, Mice, Amyloid Precursor Protein Secretases
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