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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.
Cited by
Sorted by citations
Items 601–700 of 1,010
The functional neurophysiology of the amyloid precursor protein (APP) processing pathway
Randall, A. D., Witton, J., Booth, C., Hynes-Allen, A. M., & Brown, J. T. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.02.011 · Cited by 66
Korábečný, J., Nepovimová, E., Cikánková, T., Špilovská, K., Vašková, L., Mezeiová, E., Kuča, K., & Hroudová, J. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2017.06.034 · Cited by 64
Alzheimer’s disease: biological aspects, therapeutic perspectives and diagnostic tools
Carlo, M. D., Giacomazza, D., & Biagio, P. L. S. (2012) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/24/24/244102 · Cited by 67
Monitoring the Formation of Amyloid Oligomers Using Photoluminescence Anisotropy
Jiang, B., Aliyan, A., Cook, N. P., Augustine, A., Bhak, G., Maldonado, R., McWilliams, A. D. S., Flores, E., Méndez, N., Shahnawaz, M., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.9b06966 · Cited by 64
Thangudu, S., Cheng, F., & Su, C. (2020) · Polymers · doi:10.3390/polym12123055 · Cited by 65
The Quest for Small Molecules as Amyloid Inhibiting Therapies for Alzheimer's Disease
Amijee, H., & Scopes, D. I. C. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1044 · Cited by 65
Tauroursodeoxycholic acid prevents E22Q Alzheimer’s Aβ toxicity in human cerebral endothelial cells
Viana, R. J. S., Nunes, A. F., Castro, R. E., Ramalho, R. M., Meyerson, J. L., Fossati, S., Ghiso, J. A., Rostagno, A. A., & Rodrigues, C. M. P. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-8746-x · Cited by 64
Lee, S., Youn, K., Lim, G., Lee, J., & Jun, M. (2018) · Molecules · doi:10.3390/molecules23071509 · Cited by 64
Cantero, J. L., Iglesias, J. E., Van Leemput, K., & Atienza, M. (2016) · The Journals of Gerontology Series A: Biological Sciences and Medical Sciences · doi:10.1093/gerona/glw022 · Cited by 63
Toh, W. H., & Gleeson, P. A. (2016) · Biochemical Journal · doi:10.1042/bcj20160147 · Cited by 62
Strategic Design of Amyloid-β Species Fluorescent Probes for Alzheimer’s Disease
Su, D., Diao, W., Li, J., Pan, L., Zhang, X., Wu, X., & Mao, W. (2022) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.1c00810 · Cited by 64
Kim, H., Lee, E., Park, M. K., Min, K., Diep, Y. N., Kim, J., Ahn, H., Lee, E., Kim, S., Kim, Y., et al. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.08.051 · Cited by 66
Targeting β-Amyloid Pathology in Alzheimer's Disease with Aβ Immunotherapy
Nitsch, R. M., & Höck, C. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.013 · Cited by 62
Ettcheto, M., Petrov, D., Pedrós, I., Alva, N., Carbonell, T., Beas‐Zárate, C., Pallàs, M., Auladell, C., Folch, J., & Camins, A. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160150 · 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
Fišar, Z., Hansíková, H., Křížová, J., Jirák, R., Kitzlerová, E., Zvěřová, M., Hroudová, J., Wenchich, L., Zeman, J., & Raboch, J. (2019) · Mitochondrion · doi:10.1016/j.mito.2019.07.013 · Cited by 64
Prion Neurotoxicity: Insights from Prion Protein Mutants
Solomon, I. H., Schepker, J. A., & Harris, D. A. (2010) · Caister Academic Press eBooks · doi:10.21775/9781912530076.01 · Cited by 63
Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin
Sakono, M., Zako, T., Ueda, H., Yohda, M., & Maeda, M. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06727.x · Cited by 64
Neutralization of Soluble, Synaptotoxic Amyloid β Species by Antibodies Is Epitope Specific
Zago, W., Buttini, M., Comery, T. A., Nishioka, C., Gardai, S. J., Seubert, P., Games, D., Bard, F., Schenk, D., & Kinney, G. G. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.1676-11.2012 · Cited by 62
Armijo, E., González, C., Shahnawaz, M., Flores, A., Davis, B. R., & Soto, C. A. (2016) · Neuroscience Letters · doi:10.1016/j.neulet.2016.12.060 · Cited by 61
Kotarek, J. A., Johnson, K. C., & Moss, M. A. (2008) · Analytical Biochemistry · doi:10.1016/j.ab.2008.03.022 · Cited by 62
Tang, J. X., Eckenhoff, M. F., & Eckenhoff, R. G. (2010) · Anesthesia & Analgesia · doi:10.1213/ane.0b013e3181b80939 · Cited by 60
Disruption of zinc homeostasis and the pathogenesis of senile dementia
Kawahara, M., Mizuno, D., Koyama, H., Konoha, K., Ohkawara, S., & Sadakane, Y. (2013) · Metallomics · doi:10.1039/c3mt00257h · Cited by 61
Gregori, M., Taylor, M., Salvati, E., Re, F., Mancini, S., Balducci, C., Forloni, G., Zambelli, V., Sesana, S., Michael, M., et al. (2016) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2016.10.006 · Cited by 65
Linking insulin with Alzheimer’s disease: emergence as type III diabetes
Ahmed, S. A. A., Mahmood, Z., & Zahid, S. (2015) · Neurological Sciences · doi:10.1007/s10072-015-2352-5 · Cited by 65
Motamedi‐Shad, N., Monsellier, É., & Chiti, F. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp128 · Cited by 64
Dulin, F., Léveillé, F., Becerril-Ortega, J., Mornon, J., Buisson, A., Callebaut, I., & Colloc’h, N. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.05.002 · Cited by 73
Modeling Alzheimer’s disease: from past to future
Saraceno, C., Musardo, S., Marcello, E. E., Pelucchi, S., & Luca, M. D. (2013) · Frontiers in Pharmacology · doi:10.3389/fphar.2013.00077 · Cited by 62
Novel targets in Alzheimer’s disease: A special focus on microglia
Balducci, C., & Forloni, G. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.01.017 · Cited by 62
The interaction with gold suppresses fiber-like conformations of the amyloid β (16–22) peptide
Bellucci, L., Ardèvol, A., Parrinello, M., Lutz, H., Lü, H., Weidner, T., & Corni, S. (2016) · Nanoscale · doi:10.1039/c6nr01539e · Cited by 59
Ventricular and Periventricular Anomalies in the Aging and Cognitively Impaired Brain
Todd, K. L., Brighton, T., Norton, E. S., Schick, S., Elkins, W., Pletniková, O., Fortinsky, R. H., Troncoso, J. C., Molfese, P. J., Resnick, S. M., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00445 · Cited by 62
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
Viayna, E., Gómez, T., Galdeano, C., Ramírez, L., Ratia, M., Badı́a, A., Clos, M. V., Verdaguer, E., Junyent, F., Camins, A., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.201000322 · Cited by 63
Lehmann, M., Ghosh, P., Madison, C. A., Karydas, A., Coppola, G., O’Neil, J. P., Huang, Y., Miller, B. L., Jagust, W., & Rabinovici, G. D. (2013) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2013-305858 · Cited by 61
Membrane-Mediated Neuroprotection by Curcumin from Amyloid-β-Peptide-Induced Toxicity
Thapa, A., Vernon, B. C., la Peña, K. D., Soliz, G., Moreno, H. A., López, G. P., & Chi, E. Y. (2013) · Langmuir · doi:10.1021/la4020459 · Cited by 62
Chakraborty, S., Bandyopadhyay, J., Chakraborty, S., & Basu, S. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.03.057 · Cited by 59
Cell-to-Cell Transmission of α-Synuclein Aggregates
Lee, S., Desplats, P., Lee, H.-J., Spencer, B. J., & Masliah, E. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-551-0_23 · Cited by 61
Sharma, A. K., Schultz, J. W., Prior, J. T., Rath, N. P., & Mirica, L. M. (2017) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.7b01883 · Cited by 64
Ge, X., Yang, Y., Sun, Y., Cao, W., & Ding, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00396 · Cited by 61
Type 2 diabetes mellitus in the pathophysiology of Alzheimer's disease
de Nazareth, A. M. (2017) · Dementia & Neuropsychologia · doi:10.1590/1980-57642016dn11-020002 · Cited by 64
Stravalaci, M., Bastone, A., Beeg, M., Cagnotto, A., Colombo, L., Fede, G. D., Tagliavini, F., Cantú, L., Favero, E. D., Mazzanti, M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334979 · Cited by 60
Local Structure and Global Patterning of Cu2+Binding in Fibrillar Amyloid-β [Aβ(1–40)] Protein
Gunderson, W. A., Hernández‐Guzmán, J., Karr, J. W., Sun, L., Szalai, V. A., & Warncke, K. (2012) · Journal of the American Chemical Society · doi:10.1021/ja306946q · Cited by 59
Dendrimers reduce toxicity of Aβ 1-28 peptide during aggregation and accelerate fibril formation
Klajnert‐Maculewicz, B., Wasiak, T., Йонов, М., Fernandez‐Villamarin, M., Sousa‐Herves, A., Correa, J., Riguera, R., & Fernández-Megía, E. (2012) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2012.03.005 · Cited by 59
Lang, M., Wang, L., Fan, Q., Xiao, G., Wang, X., Zhong, Y., & Zhou, B. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002683 · Cited by 60
Khan, G. M., Tong, M., Jhun, M., Arora, K., & Nichols, R. A. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2010.07116.x · Cited by 59
Herring, A., Lewejohann, L., Panzer, A.-L., Donath, A., Kröll, O., Sachser, N., Paulus, W., & Keyvani, K. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.03.007 · Cited by 63
Pineda, D., Ampurdanés, C., Medina, M. G., Serratosa, J., Tusell, J. M., Saura, J., Planas, A. M., & Navarro, P. (2011) · Glia · doi:10.1002/glia.22284 · Cited by 62
Zaręba-Kozioł, M., Figiel, I., Bartkowiak, A., & Włodarczyk, J. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00175 · Cited by 59
Kopp, M. R. G., Linsenmeier, M., Hettich, B., Prantl, S., Stavrakis, S., Leroux, J., & Arosio, P. (2020) · Analytical Chemistry · doi:10.1021/acs.analchem.9b05329 · Cited by 59
Arrozi, A. P., Shukri, S. N. S., Ngah, W. Z. W., Yusof, Y. A. M., Damanhuri, H. A., Jaafar, F., & Makpol, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-65570-4 · Cited by 59
Tank, E. M. H., & True, H. L. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000382 · Cited by 58
Increased CSF-BACE1 activity associated with decreased hippocampus volume in Alzheimer’s disease
Ewers, M., Cheng, X., Zhong, Z., Nural, H. F., Walsh, C., Meindl, T., Teipel, S. J., Buerger, K., He, P., Shen, Y., et al. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-091153 · Cited by 58
Evolutionary changes to transthyretin: structure–function relationships
Prapunpoj, P., & Leelawatwattana, L. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07243.x · Cited by 57
Zou, C., Montagna, E., Shi, Y., Peters, F., Blázquez‐Llorca, L., Shi, S., Filser, S., Dorostkar, M. M., & Herms, J. W. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1421-4 · Cited by 63
Rauch, S. M., Huen, K. H. Y., Miller, M. C., Chaudry, H., Lau, M., Sanes, J. R., Johanson, C. E., Stopa, E. G., & Burgess, R. W. (2011) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31823b0b12 · Cited by 59
Polymorphic Structures of Alzheimer's β-Amyloid Globulomers
Yu, X., & Zheng, J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020575 · Cited by 58
AD synapses contain abundant Aβ monomer and multiple soluble oligomers, including a 56-kDa assembly
Sokolow, S., Henkins, K. M., Bilousova, T. V., Miller, C. A., Vinters, H. V., Poon, W. W., Cole, G. M., & Gylys, K. H. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.011 · Cited by 61
Sarkar, B., Das, A. K., & Maiti, S. (2013) · Frontiers in Physiology · doi:10.3389/fphys.2013.00084 · Cited by 56
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Šarić, A., Michaels, T. C. T., Zaccone, A., Knowles, T. P. J., & Frenkel, D. (2016) · UCL Discovery (University College London) · doi:10.17863/cam.6652 · Cited by 58
Xie, Z., Liu, Z., Zhang, X., Yang, H., Wei, L., Wang, Y., Xu, S., Sun, L., Lai, C., Bi, J., et al. (2015) · Clinical and Experimental Medicine · doi:10.1007/s10238-015-0375-0 · Cited by 60
Lilja, A. M., Porras, O., Storelli, E., Nordberg, A., & Marutle, A. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-101242 · Cited by 57
Chakrabarti, M., McDonald, A. J., Will Reed, J., Moss, M. A., Das, B. C., & Ray, S. K. (2016) · Journal of Alzheimer's Disease · doi:10.3233/jad-150450 · Cited by 57
Neurodegenerative pathways as targets for acquired epilepsy therapy development
Casillas-Espinosa, P. M., Ali, I. Y., & O'Brien, T. J. (2020) · Epilepsia Open · doi:10.1002/epi4.12386 · Cited by 59
Österlund, N., Lundqvist, M., Ilag, L. L., Gräslund, A., & Emanuelsson, C. S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013459 · Cited by 57
Giménez‐Llort, L., Rivera-Hernández, G., Marin‐Argany, M., Sánchez‐Quesada, J. L., & Villegas, S. (2013) · mAbs · doi:10.4161/mabs.25424 · Cited by 60
Tõugu, V., & Palumaa, P. (2011) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2011.12.008 · Cited by 60
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Plasma amyloid-β oligomers level is a biomarker for Alzheimer’s disease diagnosis
Zhou, L., Chan, K. H., Chu, L., Kwan, J., Song, Y., Chen, L. H., Ho, P. W., Cheng, O., Ho, J. W.-M., & Lam, K. S. L. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.017 · Cited by 59
Ahmed, T., Zahid, S., Mahboob, A., & Farhat, S. M. (2016) · Current Neuropharmacology · doi:10.2174/1570159x14666160325121145 · Cited by 60
Rui, Y., & Zheng, J. Q. (2016) · Molecular Brain · doi:10.1186/s13041-016-0261-z · Cited by 57
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Yang, J., Zeng, F., Li, X., Ran, C., Xu, Y., & Li, Y. (2019) · Chemical Communications · doi:10.1039/c9cc08894f · Cited by 57
Chen, J., Bassot, A., Giuliani, F., & Simmen, T. (2021) · Cells · doi:10.3390/cells10071789 · Cited by 58
Humanin and the Receptors for Humanin
Matsuoka, M., & Hashimoto, Y. (2009) · Molecular Neurobiology · doi:10.1007/s12035-009-8090-z · Cited by 56
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Pain, C., Dumont, J., & Dumoulin, M. (2015) · Biochimie · doi:10.1016/j.biochi.2015.01.012 · Cited by 60
Gomes, L. M., Mahammed, A., Prosser, K. E., Smith, J. R., Silverman, M. A., Walsby, C. J., Gross, Z., & Storr, T. (2018) · Chemical Science · doi:10.1039/c8sc04660c · Cited by 56
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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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