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Aβ Oligomers – a decade of discovery
Open accessAbstract
Converging lines of evidence suggest that progressive accumulation of the amyloid β‐protein (Aβ) plays a central role in the genesis of Alzheimer’s disease, but it was long assumed that Aβ had to be assembled into extracellular amyloid fibrils to exert its cytotoxic effects. Over the past decade, data have emerged from the use of synthetic Aβ peptides, cell culture models, β‐amyloid precursor protein transgenic mice and human brain to suggest that pre‐fibrillar, diffusible assemblies of Aβ are also deleterious. Although the precise molecular identity of these soluble toxins remains unsettled, accumulating evidence suggests that soluble forms of Aβ are indeed the proximate effectors of synapse loss and neuronal injury. Here we review recent progress in understanding the role of soluble oligomers in Alzheimer’s disease.
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“recent studies have shown that the soluble Aβ oligomers are more neurotoxic both in vitro and in vivo.5−8”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [5]
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“For the preformed Aβ42 fibrils, no significant cell toxicity was observed in either the absence or presence of Cu2+ (Figure 9, lanes 1 and 2), supporting the previously reported diminished toxicity of Aβ42 fibrils.5,7,54−56”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [5]
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“However, recent in vivo studies have shown that soluble Aβ oligomers are more neurotoxic than amyloid plaques and most likely responsible for synaptic dysfunction and memory loss in AD.7–11”
From The effect of Cu2+ and Zn2+ on the Aβ42 peptide aggregation and cellular toxicity (2013) · cites this paper as [7]
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“However, recent in vivo studies have shown that the soluble Aβ oligomers are possibly more neurotoxic than amyloid plaques,14–17 and are likely responsible for synaptic dysfunction and memory loss in AD patients and AD animal models.18–21”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [19]
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“which was also shown to form neurotoxic soluble Aβ oligomers.18–20”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [19]
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“This is confirmed by the decreased cell survival of 44±8% in presence of soluble Aβ42 oligomers (Figure 11, lane 2), supporting the increased neurotoxicity of Aβ42 oligomers versus Aβ42 fibrils.16,19”
From Bifunctional Compounds for Controlling Metal-Mediated Aggregation of the Aβ42Peptide (2012) · cites this paper as [19]
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“the Aβ42 peptide was employed in these studies because it was shown to form neurotoxic soluble Aβ oligomers.5,8,48”
From Small Bifunctional Chelators That Do Not Disaggregate Amyloid β Fibrils Exhibit Reduced Cellular Toxicity (2014) · cites this paper as [5]
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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 4×
“…performance in a hippocampaldependent contextual fear conditioning assay, decreased spine density in the dentate gyrus, and impairment of long-term potentiation (LTP) at ages long before the first apparent detection of Ab dodecamer (Dineley et al. 2002; Jacobsen et al. 2006; Lesne et al. 2006).”
BackgroundInfluentialRetractedCorder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Glenner, G. G., & Wong, C. W. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(84)80190-4 · Cited by 5,404
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
Amyloid plaque core protein in Alzheimer disease and Down syndrome.
Masters, C. L., Simms, G., Weinman, N. A., Multhaup, G., McDonald, B. L., & Beyreuther, K. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.12.4245 · Cited by 4,431
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
Self-citationTriple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles
Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126
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
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 · cited 3×
“The initial cleavage leading to amyloid b-protein (Ab) production is mediated by the aspartyl protease, b-secretase (also called b-amyloid cleaving enzyme-1, BACE-1), and occurs immediately N-terminal to the Ab domain, simultaneously generating APPsb and the membranetethered C-terminal fragment, C99 (Vassar et al. 199…”
Background
Research works printed but not linked: 2
- Selkoe D. J., 2003, Annu. Rev. Pharmacol. Toxicol., 545
- Shankar G. M., 2007, Natural oligomers of the Alzheimer amyloid beta‐protein induce hippocampal synapse loss but can be neutralized by antibodies and small molecules, J. Neurosci.
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Sorted by citations
Items 701–800 of 1,010
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Rodríguez-Lebrón, E., Gouvion, C. M., Moore, S. A., Davidson, B. L., & Paulson, H. L. (2009) · Molecular Therapy · doi:10.1038/mt.2009.123 · Cited by 54
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Matz, H. C., & Dooley, H. M. (2018) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2018.09.007 · Cited by 54
Caraci, F., Bosco, P., Signorelli, M. S., Spada, R. S., Cosentino, F., Toscano, G., Bonforte, C., Muratore, S., Prestianni, G., Panerai, S., et al. (2011) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2011.08.006 · Cited by 54
Antonios, G., Saiepour, N., Bouter, Y., Richard, B. C., Paetau, A., Verkkoniemi-Ahola, A., Lannfelt, L., Ingelsson, M., Kovacs, G. G., Pillot, T., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-56 · Cited by 53
Al-Tel, T. H., Semreen, M. H., Al-Qawasmeh, R. A., Schmidt, M. F., El-Awadi, R., Ardah, M., Zaarour, R., Rao, S. N., & El-Agnaf, O. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201181f · Cited by 53
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Tomidokoro, Y., Rostagno, A. A., Neubert, T. A., Lu, Y., Rebeck, G. W., Frangione, B., Greenberg, S. M., & Ghiso, J. A. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090636 · Cited by 54
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Pham, J. D., Chim, N., Goulding, C. W., & Nowick, J. S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4068854 · Cited by 53
Simone, A. D., Esposito, L., Pedone, C., & Vitagliano, L. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.129213 · Cited by 55
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Campion, D., Pottier, C. P., Nicolas, G., Guennec, K. L., & Rovelet‐Lecrux, A. (2016) · Molecular Psychiatry · doi:10.1038/mp.2016.38 · Cited by 55
Sun, Z. J., Asberom, T., Bara, T. A., Bennett, C. E., Burnett, D. A., Chu, I., Clader, J. W., Cohen-Williams, M. E., Cole, D., Czarniecki, M., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm201407j · Cited by 53
Emerging role of amyloid beta in stress response: Implication for depression and diabetes
Morgese, M. G., Schiavone, S., & Trabace, L. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.08.031 · Cited by 54
Kayed, R., & Jackson, G. R. (2009) · Current Opinion in Immunology · doi:10.1016/j.coi.2009.05.001 · Cited by 56
Antonini, V., Marrazzo, A., Kleiner, G., Coradazzi, M., Ronsisvalle, S., Prezzavento, O., Ronsisvalle, G., & Leanza, G. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101794 · Cited by 53
Monte Carlo Study of the Formation and Conformational Properties of Dimers of Aβ42 Variants
Mitternacht, S., Staneva, I., Härd, T., & Irbäck, A. (2011) · Journal of Molecular Biology · doi:10.1016/j.jmb.2011.05.014 · Cited by 53
Effect of the English Familial Disease Mutation (H6R) on the Monomers and Dimers of Aβ40 and Aβ42
Man, V. H., Nguyen, P. H., Derreumaux, P., & Li, M. S. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500007j · Cited by 52
Zarazúa, S., Bürger, S., Delgado, J. M., Jiménez-Capdeville, M. E., & Schliebs, R. (2011) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2011.03.004 · Cited by 52
Carlo, M. D. (2009) · European Biophysics Journal · doi:10.1007/s00249-009-0439-8 · Cited by 56
Song, S.-Y., Jung, Y. Y., Hwang, C. J., Lee, H. P., Sok, C. H., Kim, J. H., Lee, S., Seo, H. O., Hyun, B. K., Choi, D. Y., et al. (2014) · Journal of Neuroinflammation · doi:10.1186/1742-2094-11-118 · Cited by 52
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Stanga, S., Lanni, C., Govoni, S. M., Uberti, D. L., D’Orazi, G., & Racchi, M. (2010) · Aging · doi:10.18632/aging.100205 · Cited by 50
Hawkes, C. A., Deng, L., Shaw, J. E., Nitz, M., & McLaurin, J. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07052.x · Cited by 53
Feinberg, H., Saldanha, J. W., Diep, L., Goel, A. S., Widom, A., Veldman, G. M., Weis, W. I., Schenk, D., & Basi, G. S. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt261 · Cited by 52
Li, S., Hayden, E. Y., Garcia, V. J., Fuchs, D.-T. S., Sheyn, J., Daley, D. A., Rentsendorj, A., Torbati, T., Black, K. L., Rutishauser, U., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00049 · Cited by 48
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Jagota, S., & Rajadas, J. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0580-5 · Cited by 52
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LoPachin, R. M., Gavin, T., & Barber, D. S. (2008) · NeuroToxicology · doi:10.1016/j.neuro.2008.04.016 · Cited by 53
Taniguchi, K., Yamamoto, F., Amano, A., Tamaoka, A., Sanjo, N., Yokota, T., Kametani, F., & Araki, W. (2022) · Neuroscience Research · doi:10.1016/j.neures.2022.03.001 · Cited by 57
Portelius, E., Olsson, M., Brinkmalm, G., Rüetschi, U., Mattsson, N., Andréasson, U., Gobom, J., Brinkmalm, A., Hölttä, M., Blennow, K., et al. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120994 · Cited by 51
C-terminal fragment of N-cadherin accelerates synapse destabilization by amyloid-β
Andreyeva, A., Nieweg, K., Horstmann, K., Klapper, S. D., Müller‐Schiffmann, A., Korth, C., & Gottmann, K. (2012) · Brain · doi:10.1093/brain/aws120 · Cited by 52
Rózga, M., & Bal, W. (2009) · Chemical Research in Toxicology · doi:10.1021/tx900358j · Cited by 54
Tang, J., Song, M., Wang, Y., Fan, X., Xu, H., & Bai, Y. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.05.067 · Cited by 50
Zhou, X., Xi, W., Luo, Y., Cao, S., & Wei, G. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp503458w · Cited by 50
Jang, H., Kwon, H., Yang, J., Hong, J., Kim, Y., Kim, K. W., Lee, J. S., Jang, Y. K., Kim, S. T., Lee, K. H., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10074-x · Cited by 52
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Hermann, D., Both, M., Ebert, U., Gross, G., Schoemaker, H., Draguhn, A., Wicke, K. M., & Nimmrich, V. (2009) · Neuroscience · doi:10.1016/j.neuroscience.2009.05.044 · Cited by 50
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Jang, H., Connelly, L. S., Arce, F. T., Ramachandran, S., Lal, R., Kagan, B. L., & Nussinov, R. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp00017f · Cited by 50
Portelius, E., Lashley, T., Westerlund, A., Persson, R., Fox, N. C., Blennow, K., Révész, T., & Zetterberg, H. (2015) · Neurodegenerative Diseases · doi:10.1159/000369465 · Cited by 51
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Fawzi, N. L., Libich, D. S., Ying, J., Tugarinov, V., & Clore, G. M. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201405180 · Cited by 50
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Ezra, A., Rabinovich-Nikitin, I., Rabinovich‐Toidman, P., & Solomon, B. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150694 · Cited by 52
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O’Nuallain, B., Acero, L. F., Williams, A. D., McWilliams‐Koeppen, H. P., Weber, A., Schwarz, H. P., Wall, J. S., Weiss, D. T., & Solomon, A. (2008) · Biochemistry · doi:10.1021/bi801767k · Cited by 50
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Michaels, T. C. T., Lazell, H. W., Arosio, P., & Knowles, T. P. J. (2015) · The Journal of Chemical Physics · doi:10.1063/1.4927655 · Cited by 49
High-resolution optical tweezers for single-molecule manipulation.
Zhang, X., Ma, L., & Zhang, Y. (2013) · Europe PMC (PubMed Central) · Cited by 47
Gerritz, S., Zhai, W., Shi, S., Zhu, S., Toyn, J., Meredith, J., Iben, L., Burton, C., Albright, C., Good, A., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300931y · Cited by 45
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Interdisciplinary challenges and promising theranostic effects of nanoscience in Alzheimer's disease
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Scott-McKean, J. J., Surewicz, K. A., Choi, J.-K., Ruffin, V. A., Salameh, A., Nieznański, K., Costa, A. C. S., & Surewicz, W. K. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.03.001 · Cited by 49
Morel, B., Carrasco, M. P., Jurado, S., Marco, C., & Conejero‐Lara, F. (2018) · Physical Chemistry Chemical Physics · doi:10.1039/c8cp02685h · Cited by 50
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Haroutunian, V. H., Hoffman, L. B., & Been, M. S. (2009) · Dialogues in Clinical Neuroscience · doi:10.31887/dcns.2009.11.2/vharoutunian · Cited by 52
Preda, S., Govoni, S. M., Lanni, C., Racchi, M., Mura, E., Grilli, M., & Marchi, M. (2007) · Neuropsychopharmacology · doi:10.1038/sj.npp.1301485 · Cited by 49
Stark, D. T., & Bazan, N. G. (2011) · Molecular Neurobiology · doi:10.1007/s12035-011-8174-4 · Cited by 49
Young, K. F., Pasternak, S., & Rylett, R. J. (2009) · Neurochemistry International · doi:10.1016/j.neuint.2009.08.002 · Cited by 49
Anastasio, T. J. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00016 · Cited by 49
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
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Török, B., Sood, A., Bag, S., Kulkarni, A., Borkin, D., Lawler, E., Dasgupta, S., Landge, S. M., Abid, M. A., Zhou, W., et al. (2012) · ChemMedChem · doi:10.1002/cmdc.201100569 · Cited by 49
Lee, Y., Choi, D., Choi, I. S., Han, J., Jeong, H., Han, S., Oh, K., & Hong, J. T. (2011) · Journal of Neuroinflammation · doi:10.1186/1742-2094-8-132 · Cited by 48
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Lee, E., Giovanello, K. S., Saykin, A. J., Xie, F., Kong, D., Wang, Y., Yang, L., Ibrahim, J. G., Doraiswamy, P. M., Hongtu Zhu, B., et al. (2017) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2017.04.004 · Cited by 50
Stefanovski, L., Meier, J. M., Pai, R. K., Triebkorn, P., Lett, T. A. P., Martin, L., Bülau, K., Hofmann‐Apitius, M., Solodkin, A., McIntosh, A. R., et al. (2021) · Frontiers in Neuroinformatics · doi:10.3389/fninf.2021.630172 · Cited by 47
Kreutz, F., Frozza, R. L., Breier, A. C., de Oliveira, V. A., Horn, A. P., Pettenuzzo, L. F., Netto, C. A., Salbego, C. G., & Trindade, V. M. T. (2011) · Neurochemistry International · doi:10.1016/j.neuint.2011.06.007 · Cited by 48
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Madhu, P., & Mukhopadhyay, S. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.30141 · Cited by 53
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Villarejo, L. G., Bachmann, L., Marks, D., Brachthäuser, M., Geidies, A., & Müller, T. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094656 · Cited by 48
Li, J., Long, Q., Ding, H., Wang, Y., Luo, D., Li, Z., & Zhang, W. (2024) · Advanced Science · doi:10.1002/advs.202308677 · Cited by 47
Accumulation of murine amyloid-β mimics early Alzheimer’s disease
Krohn, M., Bracke, A., Avchalumov, Y., Schumacher, T., Hofrichter, J., Paarmann, K., Fröhlich, C., Lange, C., Brüning, T., von Bohlen und Halbach, O., et al. (2015) · Brain · doi:10.1093/brain/awv137 · Cited by 47
Johnson, R. D., Schauerte, J. A., Wisser, K. C., Gafni, A., & Steel, D. G. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023970 · Cited by 48
Rezaei‐Ghaleh, N., Andreetto, E., Yan, L., Kapurniotu, A., & Zweckstetter, M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020289 · Cited by 47
Eph receptors: New players in Alzheimer's disease pathogenesis
Cissé, M., & Checler, F. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.028 · Cited by 50
Dockens, R. C., Wang, J.-S., Castaneda, L., Sverdlov, O., Huang, S., Slemmon, R., Gu, H., Wong, O. T., Li, H., Berman, R., et al. (2012) · Clinical Pharmacokinetics · doi:10.1007/s40262-012-0005-x · Cited by 47
Biophysical Comparison of Soluble Amyloid-β(1–42) Protofibrils, Oligomers, and Protofilaments
Nichols, M. R., Colvin, B. A., Hood, E. A., Paranjape, G. S., Osborn, D. C., & Terrill, S. E. (2015) · Biochemistry · doi:10.1021/bi500957g · Cited by 45
Assembly of Peptides Derived from β-Sheet Regions of β-Amyloid
Truex, N. L., Wang, Y., & Nowick, J. S. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b06000 · Cited by 50
Marasco, D., Vicidomini, C., Krupa, P., Cioffi, F., Huy, P. D. Q., Li, M. S., Florio, D., Broersen, K., Pandis, M. F. D., & Roviello, G. N. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109300 · Cited by 46
Qu, L., Ji, L., Wang, C., Luo, H., Li, S., Peng, W., Yin, F., Lu, D., Liu, X., Kong, L., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113441 · Cited by 47
A qualitative model for aggregation and diffusion of $$\beta $$ -amyloid in Alzheimer’s disease
Achdou, Y., Franchi, B., Marcello, N., & Tesi, M. C. (2012) · Journal of Mathematical Biology · doi:10.1007/s00285-012-0591-0 · Cited by 47
Kim, H. J., Cha, J., Lee, J.-M., Shin, J. S., Jung, N.-Y., Kim, Y. J., Choe, Y. S., Lee, K. H., Kim, S. T., Kim, J. S., et al. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150637 · Cited by 46
Primary Nucleation Kinetics of Short Fibril-Forming Amyloidogenic Peptides
Luiken, J. A., & Bolhuis, P. G. (2015) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5b05799 · Cited by 47
Dante, S., Hauß, T., Steitz, R., Canale, C., & Dencher, N. A. (2011) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2011.07.024 · Cited by 46
Belluti, F., Bartolini, M., Bottegoni, G., Bisi, A., Cavalli, A., Andrisano, V., & Rampa, A. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.02.019 · Cited by 46
Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin
Noormägi, A., Gavrilova, J., Smirnova, J., Tõugu, V., & Palumaa, P. (2010) · Biochemical Journal · doi:10.1042/bj20100627 · Cited by 46
Saadipour, K., Yang, M., Lim, Y. P., Georgiou, K. R., Sun, Y., Keating, D. J., Liu, J., Wang, Y., Gai, W., Zhong, J., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12383 · Cited by 52
Colostrinin™: An Oxidative Stress Modulator for Prevention and Treatment of Age-related Disorders
Boldogh, I. R., & Kruzel, M. L. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-13308 · Cited by 45
Ferrari, E., Capucciati, A., Prada, I., Zucca, F. A., D’Arrigo, G., Pontiroli, D., Bridelli, M. G., Sturini, M., Bubacco, L., Monzani, E., et al. (2016) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.6b00231 · Cited by 46
Meilandt, W. J., Maloney, J. A., Imperio, J., Lalehzadeh, G., Earr, T., Crowell, S., Bainbridge, T. W., Lu, Y., Ernst, J. A., Fuji, R. N., et al. (2019) · Alzheimer's Research & Therapy · doi:10.1186/s13195-019-0553-5 · Cited by 45
Gallagher, J. J., Zhang, X., Ziomek, G. J., Jacobs, R. E., & Bearer, E. L. (2012) · NeuroImage · doi:10.1016/j.neuroimage.2012.01.132 · Cited by 46
Benedetti, E., D’Angelo, B., Cristiano, L., Giacomo, E. D., Fanelli, F., Moreno, S., Cecconi, F., Fidoamore, A., Antonosante, A., Falcone, R., et al. (2014) · Cell Cycle · doi:10.4161/cc.28295 · Cited by 45
Anti-Amyloidogenic Properties of Some Phenolic Compounds
Porzoor, A., Alford, B. L., Hügel, H., Grando, D., Caine, J. M., & Macreadie, I. G. (2015) · Biomolecules · doi:10.3390/biom5020505 · Cited by 46
Quinn, S. D., Dalgarno, P. A., Cameron, R. T., Hedley, G. J., Hacker, C., Lucocq, J. M., Baillie, G. S., Samuel, I. D. W., & Penedo, J. C. (2013) · Molecular BioSystems · doi:10.1039/c3mb70272c · Cited by 46
Understanding protein aggregation from the view of monomer dynamics
Lapidus, L. J. (2012) · Molecular BioSystems · doi:10.1039/c2mb25334h · Cited by 45
Metadata
- Authors
- Walsh, D. M., & Selkoe, D. J.
- Affiliations
- University College Dublin (IE)
- Brigham and Women's Hospital (US)
- Corresponding author
- Walsh, Dominic M.
- Selkoe, Dennis J.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2007-01-04
- Volume
- 101
- Issue
- 5
- Pages
- 1172-1184
- ISSN
- 0022-3042 (ISSN-L)
- 1471-4159
- OpenAlex
- W1981458288
- Cited by
- 1,938
- References
- 147
- Citations by year
- 2026: 48 · 2025: 36 · 2024: 46 · 2023: 47 · 2022: 50 · 2021: 63 · 2020: 76 · 2019: 81 · 2018: 81 · 2017: 109 · 2016: 120 · 2015: 136 · 2014: 134 · 2013: 159 · 2012: 167
- FWCI
- 14.23
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neurochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Foundation for Neurologic Diseases
- Wellcome Trust (067660)
- National Institutes of Health
- National Institute on Aging (AG-06173)
- 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
- amyloid-beta oligomers, Alzheimer's disease, soluble amyloid-beta, synaptic loss, neuronal injury, amyloid fibrils, amyloid precursor protein, transgenic mouse model
- MeSH terms
- Alzheimer Disease, Humans, Male, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Protein Structure, Secondary
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