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Neurotoxicity of Alzheimer’s disease Aβ peptides is induced by small changes in the Aβ42 to Aβ40 ratio
Open accessAbstract
The amyloid peptides Aβ(40) and Aβ(42) of Alzheimer's disease are thought to contribute differentially to the disease process. Although Aβ(42) seems more pathogenic than Aβ(40), the reason for this is not well understood. We show here that small alterations in the Aβ(42):Aβ(40) ratio dramatically affect the biophysical and biological properties of the Aβ mixtures reflected in their aggregation kinetics, the morphology of the resulting amyloid fibrils and synaptic function tested in vitro and in vivo. A minor increase in the Aβ(42):Aβ(40) ratio stabilizes toxic oligomeric species with intermediate conformations. The initial toxic impact of these Aβ species is synaptic in nature, but this can spread into the cells leading to neuronal cell death. The fact that the relative ratio of Aβ peptides is more crucial than the absolute amounts of peptides for the induction of neurotoxic conformations has important implications for anti-amyloid therapy. Our work also suggests the dynamic nature of the equilibrium between toxic and non-toxic intermediates.
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“The increased Aβ 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates [28,42,43]”
From Selective suppression of oligodendrocyte-derived amyloid beta rescues neuronal dysfunction in Alzheimer’s disease (2024) · cites this paper as [43]
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“Aβ40 is present in larger amounts in the brain, yet Aβ42 is more neurotoxic and has a higher tendency to aggregate.8–11”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [10]
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“the longer and more hydrophobic Aβ42 isoform has a higher tendency to generate neurotoxic oligomeric species.9,10”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [10]
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“Although Aβ40 is present in larger amounts in the brain, Aβ42 was found to be more neurotoxic and have a higher tendency to aggregate.4,5”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [5]
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“Although it was shown in previous studies9,10,21 that the Aβ42 peptide is more prone to form neurotoxic soluble Aβ oligomers than the Aβ40 peptide”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [10]
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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“…potently disrupt synaptic plasticity (Klyubin et al, 2008; Shankar et al, 2008), an Ab species of 56 kDa has been found neurotoxic in Tg2576 mice (Lesne et al, 2006), lipid-induced oligomers from mature fibrils (Martins et al, 2008), ADDLs (Lambert et al, 1998; Gong et al, 2003; Lacor et al,…”
BackgroundRetractedThe 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
Terry, R. D., Masliah, E., Salmon, D. P., Butters, N., DeTeresa, R., Hill, R., Hansen, L. A., & Katzman, R. (1991) · Annals of Neurology · doi:10.1002/ana.410300410 · Cited by 4,397
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
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
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
Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
Scheuner, D., Eckman, C., Jensen, M., Song, X., Citron, M., Suzuki, N., Bird, T. D., Hardy, J., Hutton, M., Kukull, W., et al. (1996) · Nature Medicine · doi:10.1038/nm0896-864 · Cited by 2,599
Jarrett, J. T., & Lansbury, P. T. (1993) · Cell · doi:10.1016/0092-8674(93)90635-4 · Cited by 2,178
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2004) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,722
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Items 101–200 of 538
Short Aβ peptides attenuate Aβ42 toxicity in vivo
Moore, B. D., Martin, J., de Mena, L., Sánchez, J., Cruz, P. E., Ceballos‐Diaz, C., Ladd, T. B., Ran, Y., Levites, Y., Kukar, T. L., et al. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20170600 · Cited by 89
Effect of phosphodiesterase-5 inhibition on apoptosis and beta amyloid load in aged mice
Puzzo, D., Loreto, C., Giunta, S., Musumeci, G., Frasca, G., Podda, M. V., Arancio, O., & Palmeri, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.002 · Cited by 90
Spike bursts increase amyloid-β 40/42 ratio by inducing a presenilin-1 conformational change
Dolev, I., Fogel, H., Milshtein-Parush, H., Berdichevsky, Y., Lipstein, N., Brose, N., Gazit, N., & Slutsky, I. (2013) · Nature Neuroscience · doi:10.1038/nn.3376 · Cited by 87
Tapia‐Rojas, C., & Inestrosa, N. C. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14278 · Cited by 87
ECM in brain aging and dementia
Morawski, M., Filippov, M., Tzinia, A., Tsilibary, E., & Vargova, L. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00010-4 · Cited by 84
Ryan, P., Xu, M., Davey, A. K., Danon, J. J., Mellick, G. D., Kassiou, M., & Rudrawar, S. (2019) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.9b00143 · Cited by 84
Jakobsson, J., Zetterberg, H., Blennow, K., Ekman, C. J., Johansson, A. G. M., & Landén, M. (2012) · Neuropsychopharmacology · doi:10.1038/npp.2012.231 · Cited by 83
Muratore, C., Zhou, C. Q., Liao, M., Fernandez, M. A., Taylor, W. M., Lagomarsino, V. N., Pearse, R. V., Rice, H. C., Negri, J. M., He, A., et al. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.10.015 · Cited by 82
Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation
Lu, J., Cao, Q., Wang, C., Zheng, J., Luo, F., Xie, J., Li, Y., Ma, X., He, L., Eisenberg, D. S., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00054 · Cited by 80
Signature Amyloid β Profiles Are Produced by Different γ-Secretase Complexes
Acx, H., Chávez‐Gutiérrez, L., Serneels, L., Lismont, S., Benurwar, M., Elad, N., & Strooper, B. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.530907 · Cited by 79
Guix, F. X., Wahle, T., Vennekens, K. M., Snellinx, A., Chávez‐Gutiérrez, L., ILL‐Raga, G., Ramos‐Fernández, E., Guardia‐Laguarta, C., Lleó, A., Arimon, M., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200243 · Cited by 82
Tapia‐Rojas, C., Burgos, P. V., & Inestrosa, N. C. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13873 · Cited by 76
Novel APP/Aβ mutation K16N produces highly toxic heteromeric Aβ oligomers
Kaden, D., Harmeier, A., Weise, C., Munter, L. M., Althoff, V., Rost, B. R., Hildebrand, P. W., Schmitz, D., Schaefer, M., Lurz, R., et al. (2012) · EMBO Molecular Medicine · doi:10.1002/emmm.201200239 · Cited by 76
Sasahara, K., Morigaki, K., & Shinya, K. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp44517h · Cited by 75
Seed-induced acceleration of amyloid-β mediated neurotoxicity in vivo
Sowade, R. F., & Jahn, T. R. (2017) · Nature Communications · doi:10.1038/s41467-017-00579-4 · Cited by 78
Longitudinal Cerebrospinal Fluid Biomarkers over Four Years in Mild Cognitive Impairment
Mattsson, N., Portelius, E., Rolstad, S., Gustavsson, M. K., Andréasson, U., Stridsberg, M., Wallin, A., Blennow, K., & Zetterberg, H. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120019 · Cited by 75
Leal, N. S., Dentoni, G., Schreiner, B., Naia, L., Piras, A., Graff, C., Cattaneo, A., Meli, G., Hamasaki, M., Nilsson, P., et al. (2020) · Cells · doi:10.3390/cells9122552 · Cited by 77
Al‐kuraishy, H. M., Jabir, M. S., Albuhadily, A. K., Al-Gareeb, A. I., & Rafeeq, M. F. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.102084 · Cited by 75
Valensin, D., Gabbiani, C., & Luigi Messori, A. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.04.010 · Cited by 77
Viles, J. H. (2023) · Angewandte Chemie International Edition · doi:10.1002/anie.202215785 · Cited by 74
Presenilin-1 adopts pathogenic conformation in normal aging and in sporadic Alzheimer’s disease
Wahlster, L., Arimon, M., Nasser‐Ghodsi, N., Post, K. L., Serrano‐Pozo, A., Uemura, K., & Berezovska, O. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-1065-6 · Cited by 72
Islet Amyloid Polypeptide: A Partner in Crime With Aβ in the Pathology of Alzheimer's Disease
Raimundo, A., Ferreira, S., Martins, I. C., & Menezes, R. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00035 · Cited by 74
Self-citationHashimoto, T., Adams, K. W., Fan, Z., McLean, P. J., & Hyman, B. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.257378 · Cited by 71
Olive Biophenols Reduces Alzheimer’s Pathology in SH-SY5Y Cells and APPswe Mice
Omar, S. H., Scott, C., Hamlin, A. S., & Obied, H. K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms20010125 · Cited by 71
Chakraborty, D., Straub, J. E., & Thirumalai, D. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002570117 · Cited by 69
Armato, U., Chiarini, A., Chakravarthy, B., Chioffi, F., Pacchiana, R., Colarusso, E., Whitfield, J. F., & Dal Prà, I. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.04.020 · Cited by 68
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.
Iljina, M., Garcia, G. A., Dear, A. J., Flint, J., Narayan, P., Michaels, T. C. T., Dobson, C. M., Frenkel, D., Knowles, T. P. J., & Klenerman, D. (2016) · Scientific Reports · doi:10.1038/srep28658 · Cited by 68
Chang, Y., & Chen, Y. (2014) · FEBS Journal · doi:10.1111/febs.12813 · Cited by 68
Omtri, R. S., Davidson, M. W., Arumugam, B., Poduslo, J. F., & Kandimalla, K. K. (2012) · Molecular Pharmaceutics · doi:10.1021/mp200530q · Cited by 69
Kretner, B., Trambauer, J., Fukumori, A., Mielke, J., Kuhn, P., Kremmer, E., Giese, A., Lichtenthaler, S. F., Haass, C., Arzberger, T., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505952 · Cited by 68
Hu, Y., Zeng, Z., Wang, B., & Guo, S. (2017) · International Immunopharmacology · doi:10.1016/j.intimp.2017.07.009 · Cited by 69
O’Malley, T. T., Oktaviani, N. A., Zhang, D., Lomakin, A., O’Nuallain, B., Linse, S. S., Benedek, G. B., Rowan, M. J., Mulder, F. A. A., & Walsh, D. M. (2014) · Biochemical Journal · doi:10.1042/bj20140219 · Cited by 68
Brownjohn, P. W., Smith, J. C., Portelius, E., Serneels, L., Kvartsberg, H., Strooper, B. D., Blennow, K., Zetterberg, H., & Livesey, F. J. (2017) · Stem Cell Reports · doi:10.1016/j.stemcr.2017.02.006 · Cited by 68
Antibody-Based Drugs and Approaches Against Amyloid-β Species for Alzheimer’s Disease Immunotherapy
Liu, J., Yang, B., Ke, J., Li, W., & Suen, W.-C. (2016) · Drugs & Aging · doi:10.1007/s40266-016-0406-x · Cited by 67
Effects of Anesthetic Isoflurane and Desflurane on Human Cerebrospinal Fluid Aβ and τ Level
Zhang, B., Tian, M., Zheng, H., Yu, Z., Yue, Y., Li, T., Li, S., Marcantonio, E. R., & Xie, Z. (2013) · Anesthesiology · doi:10.1097/aln.0b013e31828ce55d · Cited by 67
Hyperphosphorylated Tau is Elevated in Alzheimer's Disease with Psychosis
Murray, P. S., Kirkwood, C. M., Gray, M. C., Fish, K. N., Ikonomović, M. D., Hamilton, R. L., Kofler, J., Klunk, W. E., López, O. L., & Sweet, R. A. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131166 · Cited by 67
A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration
Marshall, K. E., Vadukul, D. M., Dahal, L., Theisen, A., Fowler, M. W., Al‐Hilaly, Y. K., Ford, L. K., Kemenes, G., Day, I. J., Staras, K., et al. (2016) · Scientific Reports · doi:10.1038/srep30182 · Cited by 67
Selenoprotein P and selenoprotein M block Zn2+-mediated Aβ42 aggregation and toxicity
Du, X., Li, H., Wang, Z., Qiu, S., Liu, Q., & Ni, J. (2013) · Metallomics · doi:10.1039/c3mt20282h · Cited by 67
Pohanka, M. (2011) · Journal of Applied Biomedicine · doi:10.2478/v10136-011-0003-6 · Cited by 64
Chong, S., Benilova, I., Shaban, H., Strooper, B. D., Devijver, H., Moechars, D., Eberle, W., Bartic, C., LEUVEN, F. V., & Callewaert, G. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.07.006 · Cited by 64
Self-citationUngureanu, A.-A., Benilova, I., Krylychkina, O., Braeken, D., Strooper, B. D., Haesendonck, C. V., Dotti, C. G., & Bartic, C. (2016) · Scientific Reports · doi:10.1038/srep25841 · Cited by 64
Self-citationKaiser, D., Acharya, M., Leighton, P. L. A., Wang, H., Daude, N., Wohlgemuth, S. L., Shi, B., & Allison, W. T. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051305 · Cited by 63
Matheou, C. J., Younan, N. D., & Viles, J. H. (2014) · Biochemical Journal · doi:10.1042/bj20141168 · Cited by 64
Amyloid-beta immunotherapy: the hope for Alzheimer disease?
Barrera-Ocampo, A. A., & Lopera, F. J. (2016) · Colombia medica · doi:10.25100/cm.v47i4.2640 · Cited by 64
Amyloid-β Protofibrils: Size, Morphology and Synaptotoxicity of an Engineered Mimic
Dubnovitsky, A. P., Sandberg, A., Rahman, M. M., Benilova, I., Lendel, C., & Härd, T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066101 · Cited by 65
Self-citationFindeis, M. A., Schroeder, F. C., McKee, T. D., Yager, D., Fraering, P. C., Creaser, S. P., Austin, W., Clardy, J., Wang, R., Selkoe, D. J., et al. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn3000857 · Cited by 61
Imaging Aβ(1–42) fibril elongation reveals strongly polarised growth and growth incompetent states
Young, L. J., Schierle, G. S. K., & Kaminski, C. F. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp03412a · Cited by 61
Mixing Aβ(1–40) and Aβ(1–42) peptides generates unique amyloid fibrils
Cerofolini, L., Ravera, E., Bologna, S., Wiglenda, T., Böddrich, A., Purfürst, B., Benilova, I., Korsak, M., Gallo, G., Rizzo, D., et al. (2020) · Chemical Communications · doi:10.1039/d0cc02463e · Cited by 60
Self-citationBalducci, C., Mehdawy, B., Mare, L., Giuliani, A., Lorenzini, L., Sivilia, S., Giardino, L., Calzà, L., Lanzillotta, A., Sarnico, I., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101839 · Cited by 58
Huang, Y., Cho, H.-J., Bandara, N., Sun, L., Tran, D., Rogers, B. E., & Mirica, L. M. (2020) · Chemical Science · doi:10.1039/d0sc02641g · Cited by 62
Rajani, R. M., Ellingford, R., Hellmuth, M., Harris, S. S., Taso, O. S., Graykowski, D., Lam, F. K. W., Arber, C., Fertan, E., Danial, J. S. H., et al. (2024) · PLOS Biology · doi:10.1371/journal.pbio.3002727 · Cited by 62
“The increased A β 42:40 ratio in oligodendrocytes could contribute to the high proportion of soluble aggregates [28,42,43]; it is also worth noting that the relationship between A β monomer concentration and aggregate concentration is nonlinear, so small changes in monomer can result in larger…”
BackgroundPotential neurotoxic activity of diverse molecules released by microglia
Lindhout, I. A., Murray, T. E., Richards, C. M., & Klegeris, A. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105117 · Cited by 58
Ballesteros‐Álvarez, J., Nguyen, W., Sivapatham, R., Rane, A., & Andersen, J. K. (2022) · GeroScience · doi:10.1007/s11357-022-00708-y · Cited by 60
Pain, C., Dumont, J., & Dumoulin, M. (2015) · Biochimie · doi:10.1016/j.biochi.2015.01.012 · Cited by 60
Vandendriessche, C., Balusu, S., Cauwenberghe, C. V., Brkić, M., Pauwels, M. J., Plehiers, N., Bruggeman, A., Dujardin, P., Imschoot, G. V., Wonterghem, E. V., et al. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01245-z · Cited by 58
β-Amyloid 42/40 ratio and kalirin expression in Alzheimer disease with psychosis
Murray, P. S., Kirkwood, C. M., Gray, M. C., Ikonomović, M. D., Paljug, W. R., Abrahamson, E. E., Henteleff, R. A., Hamilton, R. L., Kofler, J., Klunk, W. E., et al. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.02.015 · Cited by 58
Gu, L., Tran, J., Jiang, L., & Guo, Z. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.01.013 · Cited by 56
Liu, S., Ando, F., Fujita, Y., Liu, J., Maeda, T., Shen, X., Kikuchi, K., Matsumoto, A., Yokomori, M., Tanabe, C., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006420 · Cited by 58
Mechanisms of neurodegeneration — Insights from familial Alzheimer’s disease
Chávez‐Gutiérrez, L., & Szaruga, M. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.03.005 · Cited by 59
Rolstad, S., Jakobsson, J., Sellgren, C. M., Ekman, C. J., Blennow, K., Zetterberg, H., Pålsson, E., & Landén, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0127100 · Cited by 52
Negri, J. M., Menon, V., & Young‐Pearse, T. L. (2020) · eNeuro · doi:10.1523/eneuro.0080-19.2019 · Cited by 53
Alzheimer's Therapeutics: Translation of Preclinical Science to Clinical Drug Development
Savonenko, A. V., Melnikova, T., Hiatt, A., Li, T., Worley, P. F., Troncoso, J. C., Wong, P. C., & Price, D. L. (2011) · Neuropsychopharmacology · doi:10.1038/npp.2011.211 · Cited by 52
Meli, G., Lecci, A., Manca, A., Jakovljevic, N. K., Albertini, V., Benussi, L., Ghidoni, R., & Cattaneo, A. (2014) · Nature Communications · doi:10.1038/ncomms4867 · Cited by 51
Neuronal receptors as targets for the action of amyloid-beta protein (Aβ) in the brain
Patel, A. N., & Jhamandas, J. H. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399411002134 · Cited by 51
mGluR5 Contribution to Neuropathology in Alzheimer Mice Is Disease Stage-Dependent
Abd‐Elrahman, K. S., Hamilton, A., Albaker, A. B., & Ferguson, S. S. G. (2020) · ACS Pharmacology & Translational Science · doi:10.1021/acsptsci.0c00013 · Cited by 51
Modulation of the Aβ peptide aggregation pathway by KP1019 limits Aβ-associated neurotoxicity
Jones, M. R., Mu, C., Wang, M. C. P., Webb, M. I., Walsby, C. J., & Storr, T. (2015) · Metallomics · doi:10.1039/c4mt00252k · Cited by 50
Plasma Aβ and PET PiB binding are inversely related in mild cognitive impairment
Devanand, D. P., Schupf, N., Stern, Y., Parsey, R. V., Pelton, G. H., Mehta, P. D., & Mayeux, R. P. (2011) · Neurology · doi:10.1212/wnl.0b013e318224afb7 · Cited by 50
Key Peptides and Proteins in Alzheimer’s Disease
Penke, B., Bogár, F., Paragi, G., Gera, J., & Fülöp, L. (2019) · Current Protein and Peptide Science · doi:10.2174/1389203720666190103123434 · Cited by 51
Recent developments of small molecule γ-secretase modulators for Alzheimer's disease
Mekala, S., Nelson, G. L., & Li, Y. (2020) · RSC Medicinal Chemistry · doi:10.1039/d0md00196a · Cited by 51
Mrđenović, D., Pieta, I. S., Nowakowski, R., Kutner, W., Lipkowski, J., & Pięta, P. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.01.117 · Cited by 53
Membrane Dynamics of γ-Secretase Provides a Molecular Basis for β-Amyloid Binding and Processing
Somavarapu, A. K., & Kepp, K. P. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00208 · Cited by 49
Shanmuganathan, B., Suryanarayanan, V., Sathya, S., Narenkumar, M., Singh, S. K., Kandasamy, R., & Devi, K. P. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.10.017 · Cited by 50
Sharma, A. K., Kim, J., Prior, J. T., Hawco, N. J., Rath, N. P., Kim, J., & Mirica, L. M. (2014) · Inorganic Chemistry · doi:10.1021/ic500926c · Cited by 48
Nguyen, P. H., Campanera, J. M., Ngô, S. T., Loquet, A., & Derreumaux, P. (2019) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.9b01206 · Cited by 48
Amyloid peptide Aβ40 inhibits aggregation of Aβ42: Evidence from molecular dynamics simulations
Man, V. H., & Li, M. S. (2012) · The Journal of Chemical Physics · doi:10.1063/1.4730410 · Cited by 47
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Zou, K., Liu, J., Watanabe, A., Hiraga, S., Liu, S., Tanabe, C., Maeda, T., Terayama, Y., Takahashi, S., Michikawa, M., et al. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.01.053 · Cited by 48
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Self-citationDan, Y., Yin, Q., Wang, J., Yang, J. N., Chen, Z., Gao, Z., Huang, Q., & Li, S. (2021) · International Journal of Nanomedicine · doi:10.2147/ijn.s293042 · Cited by 46
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Duplan, E., Sévalle, J., Viotti, J., Goiran, T., Bauer, C., Renbaum, P., Levy‐Lahad, E., Gautier, C., Corti, O., Leroudier, N., et al. (2013) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjt003 · Cited by 45
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Xiao, Y. M., Dai, Y., Li, L., Geng, F., Xu, Y., Wang, J., Wang, S., & Zhao, J. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111651 · Cited by 45
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Vandersteen, A., Masman, M. F., Baets, G. D., Jonckheere, W., van der Werf, K., Marrink, . J., Rozenski, J., Benilova, I., Strooper, B. D., Subramaniam, V., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394635 · Cited by 46
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Morishima‐Kawashima, M. (2014) · Frontiers in Physiology · doi:10.3389/fphys.2014.00463 · Cited by 46
Reinert, J., Richard, B. C., Klafki, H., Friedrich, B., Bayer, T. A., Wiltfang, J., Kovács, G. G., Ingelsson, M., Lannfelt, L., Paetau, A. E., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0294-7 · Cited by 44
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Gangoda, S. V. S., Avadhanam, B., Jufri, N. F., Sohn, E. H., Butlin, M., Gupta, V., Chung, R. S., & Avolio, A. P. (2018) · Scientific Reports · doi:10.1038/s41598-018-20117-6 · Cited by 45
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Dufort‐Gervais, J., Provost, C., Charbonneau, L., Norris, C. M., Calon, F., Mongrain, V., & Brouillette, J. (2020) · Scientific Reports · doi:10.1038/s41598-020-63255-6 · Cited by 48
Abramowski, D., Rabe, S., Upadhaya, A. R., Reichwald, J., Danner, S., Staab, D., Capetillo-Zarate, E., Yamaguchi, H., Saido, T. C., Wiederhold, K.-H., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4586-11.2012 · Cited by 41
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Metadata
- Authors
- Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., Braeken, D., Callewaert, G., Bartic, C., D'Hooge, R., Martins, I. C., Rousseau, F., Schymkowitz, J., & De Strooper, B.
- Affiliations
- Vlaams Instituut voor Biotechnologie (BE)
- Vrije Universiteit Brussel (BE)
- Rega Institute for Medical Research (BE)
- University of Twente (NL)
- IMEC (BE)
- Corresponding author
- Schymkowitz, Joost
- ORCID
- Venue
- The EMBO Journal
- Published
- 2010-09-03
- Volume
- 29
- Issue
- 19
- Pages
- 3408-3420
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC2957213
- OpenAlex
- W1966694507
- Cited by
- 532
- References
- 61
- Citations by year
- 2026: 16 · 2025: 23 · 2024: 36 · 2023: 39 · 2022: 27 · 2021: 39 · 2020: 32 · 2019: 33 · 2018: 31 · 2017: 35 · 2016: 48 · 2015: 31 · 2014: 30 · 2013: 42 · 2012: 43
- FWCI
- 24.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- VU Research Portal (publishedVersion)
- University of Twente Research Information (publishedVersion, other-oa)
- Lirias (submittedVersion)
- VUBIR (Vrije Universiteit Brussel) (submittedVersion)
- University of Twente Research Information (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- European Commission (200611)
- Fonds Wetenschappelijk Onderzoek (P6/43)
- Vlaamse regering
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, amyloid-beta, Aβ42/Aβ40 ratio, neurotoxicity, oligomeric intermediates, fibril morphology, synaptic dysfunction, neuronal cell death, anti-amyloid therapy, peptide mixtures
- MeSH terms
- Alzheimer Disease, Analysis of Variance, Animals, Biophysics, Fluorescent Dyes, Humans, Kinetics, Microelectrodes, Neurons, Peptide Fragments, Protein Binding, Thiazoles, Amyloid beta-Peptides, Spectroscopy, Fourier Transform Infrared, Patch-Clamp Techniques, Microscopy, Electron, Transmission, Mice, Benzothiazoles, Plaque, Amyloid
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