The DOI matches its Crossref record; 146 of the 147 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
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…”
BackgroundDiffusible, 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
Jarrett, J. T., Berger, E. P., & Lansbury, P. T. (1993) · Biochemistry · doi:10.1021/bi00069a001 · Cited by 2,022
Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function
SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014
Wolfe, M. S., Xia, W., Ostaszewski, B. L., Diehl, T. S., Kimberly, W. T., & Selkoe, D. J. (1999) · Nature · doi:10.1038/19077 · Cited by 1,959
Self-citationAmyloid β-peptide is produced by cultured cells during normal metabolism
Haass, C., Schlossmacher, M. G., Hung, A. Y., Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., et al. (1992) · Nature · doi:10.1038/359322a0 · Cited by 1,921
Self-citationMucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Citron, M., Oltersdorf, T., Haass, C., McConlogue, L., Hung, A. Y., Seubert, P., Vigo-Pelfrey, C., Lieberburg, I., & Selkoe, D. J. (1992) · Nature · doi:10.1038/360672a0 · Cited by 1,757
Self-citationIsolation and quantification of soluble Alzheimer's β-peptide from biological fluids
Seubert, P., Vigo-Pelfrey, C., Esch, F., Lee, M., Dovey, H., Davis, D., Sinha, S., Schiossmacher, M., Whaley, J., Swindlehurst, C., et al. (1992) · Nature · doi:10.1038/359325a0 · Cited by 1,731
Self-citationNatural 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
Self-citationEnhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561
Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer's Disease
Lue, L.-F., Kuo, Y.-M., Roher, A. E., Brachova, L., Shen, Y., Sue, L., Beach, T., Kurth, J. H., Rydel, R. E., & Rogers, J. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65184-x · Cited by 1,530
Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils
Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526
Suzuki, N., Cheung, T. T., Cai, X.-D., Odaka, A., Otvos, L., Eckman, C., Golde, T. E., & Younkin, S. G. (1994) · Science · doi:10.1126/science.8191290 · Cited by 1,471
Oligomeric and fibrillar species of amyloid-β peptides differentially affect neuronal viability
Dahlgren, K. N., Manelli, A. M., Stine, W. B., Baker, L. K., Krafft, G. A., & LaDu, M. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201750200 · Cited by 1,452
Production of the Alzheimer Amyloid β Protein by Normal Proteolytic Processing
Shoji, M., Golde, T. E., Ghiso, J., Cheung, T. T., Estus, S., Shaffer, L. M., Cai, X.-D., McKay, D. M., Tintner, R., Frangione, B., et al. (1992) · Science · doi:10.1126/science.1439760 · Cited by 1,447
Mutation of the Alzheimer's Disease Amyloid Gene in Hereditary Cerebral Hemorrhage, Dutch Type
Levy, E., Carman, M. D., Fernandez-Madrid, I. J., Power, M. D., Lieberburg, I. M., van Duinen, S. G., Bots, G. T. A. M., Luyendijk, W., & Frangione, B. (1990) · Science · doi:10.1126/science.2111584 · Cited by 1,399
Neuropathology of human Alzheimer disease after immunization with amyloid-β peptide: a case report
Nicoll, J. A. R., Wilkinson, D., Holmes, C., Steart, P., Markham, H., & Weller, R. O. (2003) · Nature Medicine · doi:10.1038/nm840 · Cited by 1,397
Strittmatter, W. J., Weisgraber, K. H., Huang, D. Y., Dong, L. M., Salvesen, G. S., Pericak-Vance, M., Schmechel, D., Saunders, A. M., Goldgaber, D., & Roses, A. D. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.8098 · Cited by 1,363
Clinical effects of Aβ immunization (AN1792) in patients with AD in an interrupted trial
Gilman, S., Koller, M., Black, R. S., Jenkins, L., Griffith, S. G., Fox, N. C., Eisner, L., Kirby, L., Rovira, M. B., Forette, F., et al. (2005) · Neurology · doi:10.1212/01.wnl.0000159740.16984.3c · Cited by 1,329
Rovelet‐Lecrux, A., Hannequin, D., Raux, G., Meur, N. L., Laquerrière, A., Vital, A., Dumanchin‐Njock, C., Feuillette, S., Brice, A., Vercelletto, M., et al. (2005) · Nature Genetics · doi:10.1038/ng1718 · Cited by 1,284
Identification, biogenesis, and localization of precursors of Alzheimer's disease A4 amyloid protein
Weidemann, A., König, G., Bunke, D., Fischer, P. Q., Salbaum, J. M., Masters, C. L., & Beyreuther, K. T. (1989) · Cell · doi:10.1016/0092-8674(89)90177-3 · Cited by 1,233
Chartier-Harlin, M.-C., Crawford, F., Houlden, H., Warren, A., Hughes, D., Fidani, L., Goate, A., Rossor, M., Roques, P., Hardy, J., et al. (1991) · Nature · doi:10.1038/353844a0 · Cited by 1,214
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Lomakin, A., Benedek, G. B., Condron, M. M., & Teplow, D. B. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.22364 · Cited by 1,156
Self-citationPlaque-independent disruption of neural circuits in Alzheimer’s disease mouse models
Hsia, A. Y., Masliah, E., McConlogue, L., Yu, G.-Q., Tatsuno, G., Hu, K., Kholodenko, D., Malenka, R. C., Nicoll, R. A., & Mucke, L. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.3228 · Cited by 1,123
Apolipoprotein E in sporadic Alzheimer's disease: Allelic variation and receptor interactions
William Rebeck, G., Reiter, J. S., Strickland, D. K., & Hyman, B. T. (1993) · Neuron · doi:10.1016/0896-6273(93)90070-8 · Cited by 1,107
BACE1 is the major β-secretase for generation of Aβ peptides by neurons
Cai, H., Wang, Y., McCarthy, D. B., Wen, H., Borchelt, D., Price, D. L., & Wong, P. C. (2001) · Nature Neuroscience · doi:10.1038/85064 · Cited by 1,087
Gong, Y., Chang, L., Viola, K. L., Lacor, P. N., Lambert, M. P., Finch, C. E., Krafft, G. A., & Klein, W. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1834302100 · Cited by 1,061
Demuro, A., Mina, E. W., Kayed, R., Milton, S. C. F., Parker, I., & Glabe, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500997200 · Cited by 1,057
Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Self-citationAssembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954
Impaired synaptic plasticity and learning in aged amyloid precursor protein transgenic mice
Chapman, P. F., White, G. L., Jones, M. W., Cooper-Blacketer, D., Marshall, V. J., Irizarry, M., Younkin, L., Good, M. A., Bliss, T. V. P., Hyman, B. T., et al. (1999) · Nature Neuroscience · doi:10.1038/6374 · Cited by 946
Release of Excess Amyloid β Protein from a Mutant Amyloid β Protein Precursor
Cai, X.-D., Golde, T. E., & Younkin, S. G. (1993) · Science · doi:10.1126/science.8424174 · Cited by 913
Environmental Enrichment Reduces Aβ Levels and Amyloid Deposition in Transgenic Mice
Lazarov, O., Robinson, J., Tang, Y.-P., Hairston, I. S., Korade-Mirnics, Z., Lee, V. M.-Y., Hersh, L. B., Sapolsky, R. M., Mirnics, K., & Sisodia, S. S. (2005) · Cell · doi:10.1016/j.cell.2005.01.015 · Cited by 885
Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
Li, Y.-M., Xu, M., Lai, M.-T., Huang, Q., Castro, J. L., DiMuzio-Mower, J., Harrison, T., Lellis, C., Nadin, A., Neduvelil, J. G., et al. (2000) · Nature · doi:10.1038/35015085 · Cited by 866
Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model
Dodart, J.-C., Bales, K. R., Gannon, K. S., Greene, S. J., DeMattos, R. B., Mathis, C., DeLong, C. A., Wu, S., Wu, X., Holtzman, D. M., et al. (2002) · Nature Neuroscience · doi:10.1038/nn842 · Cited by 858
In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity
Pike, C. J., Walencewicz, A. J., Glabe, C. G., & Cotman, C. W. (1991) · Brain Research · doi:10.1016/0006-8993(91)91553-d · Cited by 841
Voluntary Exercise Decreases Amyloid Load in a Transgenic Model of Alzheimer's Disease
Adlard, P. A., Perreau, V. M., Pop, V., & Cotman, C. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0496-05.2005 · Cited by 829
Alzheimer's Disease: Molecular Understanding Predicts Amyloid-Based Therapeutics
Selkoe, D. J., & Schenk, D. (2003) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.43.100901.140248 · Cited by 829
Self-citationHartley, D. M., Walsh, D. M., Ye, C. P., Diehl, T., Vasquez, S., Vassilev, P. M., Teplow, D. B., & Selkoe, D. J. (1999) · The Journal of Neuroscience · doi:10.1523/jneurosci.19-20-08876.1999 · Cited by 817
Self-citationKatzman, R. (1986) · New England Journal of Medicine · doi:10.1056/nejm198604103141506 · Cited by 801
Antibodies against β-Amyloid Slow Cognitive Decline in Alzheimer's Disease
Höck, C., Konietzko, U., Streffer, J. R., Tracy, J., Signorell, A., Müller-Tillmanns, B., Lemke, U., Henke, K., Moritz, E., Garcia, E., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00294-0 · Cited by 786
The Relationship between Aβ and Memory in the Tg2576 Mouse Model of Alzheimer's Disease
Westerman, M. A., Cooper-Blacketer, D., Mariash, A., Kotilinek, L., Kawarabayashi, T., Younkin, L. H., Carlson, G. A., Younkin, S. G., & Ashe, K. H. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-05-01858.2002 · Cited by 731
Leissring, M. A., Farris, W., Chang, A. Y., Walsh, D. M., Wu, X., Sun, X., Frosch, M. P., & Selkoe, D. J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00787-6 · Cited by 725
Self-citationEarly-onset behavioral and synaptic deficits in a mouse model of Alzheimer's disease
Jacobsen, J. S., Wu, C.-C., Redwine, J. M., Comery, T. A., Arias, R., Bowlby, M., Martone, R., Morrison, J. H., Pangalos, M. N., Reinhart, P. H., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600948103 · Cited by 701
Observation of metastable Aβ amyloid protofibrils by atomic force microscopy
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90255-6 · Cited by 699
Moechars, D., Dewachter, I., Lorent, K., Reversé, D., Baekelandt, V., Naidu, A., Tesseur, I., Spittaels, K., Haute, C. V. D., Checler, F., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.10.6483 · Cited by 668
Townsend, M., Shankar, G. M., Mehta, T., Walsh, D. M., & Selkoe, D. J. (2006) · The Journal of Physiology · doi:10.1113/jphysiol.2005.103754 · Cited by 619
Self-citationWang, J., Dickson, D. W., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Experimental Neurology · doi:10.1006/exnr.1999.7085 · Cited by 567
Barghorn, S., Nimmrich, V., Striebinger, A., Krantz, C., Keller, P., Janson, B., Bahr, M., Schmidt, M., Bitner, R. S., Harlan, J., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03407.x · Cited by 559
γ-Secretase: proteasome of the membrane?
Kopan, R., & Ilagan, M. X. G. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1406 · Cited by 554
Wang, H.-W., Pasternak, J. F., Kuo, H., Ristic, H., Lambert, M. P., Chromy, B., Viola, K. L., Klein, W. L., Stine, W. B., Krafft, G. A., et al. (2002) · Brain Research · doi:10.1016/s0006-8993(01)03058-x · Cited by 527
Aging renders the brain vulnerable to amyloid β-protein neurotoxicity
Guela, C., Wu, C.-K., Saroff, D., Lorenzo, A., Yuan, M., & Yankner, B. A. (1998) · Nature Medicine · doi:10.1038/nm0798-827 · Cited by 520
Transition-state analogue inhibitors of γ-secretase bind directly to presenilin-1
Esler, W. P., Kimberly, W. T., Ostaszewski, B. L., Diehl, T. S., Moore, C. L., Tsai, J.-Y., Rahmati, T., Xia, W., Selkoe, D. J., & Wolfe, M. S. (2000) · Nature Cell Biology · doi:10.1038/35017062 · Cited by 514
Self-citationDeshpande, A. M., Mina, E. W., Glabe, C. G., & Busciglio, J. A. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.1189-06.2006 · Cited by 508
Amyloid-β oligomers: their production, toxicity and therapeutic inhibition
Walsh, D. M., Klyubin, I. V., Fadeeva, J. V., Rowan, M. J., & Selkoe, D. J. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300552 · Cited by 507
Self-citationHoshi, M. M., Sato, M., Matsumoto, S., Noguchi, A., Yasutake, K., Yoshida, N., & Sato, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1237107100 · Cited by 498
Saunders, A. M., Roses, A. D., Pericak‐Vance, M. A., Dole, K. C., Strittmatter, W. J., Schmechel, D. E., Szymanski, M. H., McCown, N., Manwaring, M., Schmader, K. E., et al. (1993) · The Lancet · doi:10.1016/0140-6736(93)91709-u · Cited by 498
Roher, A. E., Chaney, M. O., Kuo, Y., Webster, S. D., Stine, W. B., Haverkamp, L. J., Woods, A. S., Cotter, R. J., Tuohy, J. M., Krafft, G. A., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20631 · Cited by 494
Amyloid β protein immunotherapy neutralizes Aβ oligomers that disrupt synaptic plasticity in vivo
Klyubin, I., Walsh, D. M., Lemere, C. A., Cullen, W. K., Shankar, G. M., Betts, V., Spooner, E. T., Jiang, L., Anwyl, R., Selkoe, D. J., et al. (2005) · Nature Medicine · doi:10.1038/nm1234 · Cited by 489
Self-citationAntiamyloidogenic and Neuroprotective Functions of Cathepsin B: Implications for Alzheimer's Disease
Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E. D., Sun, B., Chen, J., Wang, X., Yu, G.-Q., Esposito, L., Mucke, L., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.027 · Cited by 482
Kirschner, D. A., Inouye, H., Duffy, L. K., Sinclair, A. J., Lind, M., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.19.6953 · Cited by 481
Self-citationIda, N., Hartmann, T., Pantel, J., Schrüder, J., Zerfaß, R., Fürstl, H., Sandbrink, R., Masters, C. L., & Beyreuther, K. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.37.22908 · Cited by 478
Harper, J. D., Wong, S. S., Lieber, C. M., & Lansbury, P. T. (1999) · Biochemistry · doi:10.1021/bi9904149 · Cited by 454
Harper, J. D., Lieber, C. M., & Lansbury, P. T. (1997) · Chemistry & Biology · doi:10.1016/s1074-5521(97)90303-3 · Cited by 452
Isolation of Low‐Molecular‐Weight Proteins from Amyloid Plaque Fibers in Alzheimer's Disease
Selkoe, D. J., Abraham, C. R., Podlisny, M. B., & Duffy, L. K. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb08501.x · Cited by 452
Self-citationPresenilin clinical mutations can affect γ‐secretase activity by different mechanisms
Bentahir, M., Nyabi, O., Verhamme, J., Tolia, A., Horré, K., Wiltfang, J., Esselmann, H., & Strooper, B. D. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03578.x · Cited by 427
Molecular mapping of alzheimer‐type dementia in Down's syndrome
Prasher, V. P., Farrer, M. J., Kessling, A. M., Fisher, E. M. C., West, R. J., Barber, P. C., & Butler, A. C. (1998) · Annals of Neurology · doi:10.1002/ana.410430316 · Cited by 414
Correlations of synaptic and pathological markers with cognition of the elderly
Dickson, D. W., Crystal, H. A., Bevona, C., Honer, W., Vincent, I., & Davies, P. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00013-5 · Cited by 410
The Oligomerization of Amyloid β-Protein Begins Intracellularly in Cells Derived from Human Brain
Walsh, D. M., Tseng, B. P., Rydel, R. E., Podlisny, M. B., & Selkoe, D. J. (2000) · Biochemistry · doi:10.1021/bi001048s · Cited by 401
Self-citationRapid Communication: Characterization of β‐Amyloid Peptide from Human Cerebrospinal Fluid
Vigo‐Pelfrey, C., Lee, D., Keim, P., Lieberburg, I., & Schenk, D. B. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb09841.x · Cited by 385
Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., & Holzman, T. F. (1994) · Biophysical Journal · doi:10.1016/s0006-3495(94)80591-0 · Cited by 381
McLaurin, J., Kierstead, M. E., Brown, M. E., Hawkes, C. A., Lambermon, M. H. L., Phinney, A. L., Darabie, A. A., Cousins, J. E., French, J. E., Lan, M. F., et al. (2006) · Nature Medicine · doi:10.1038/nm1423 · Cited by 373
Podlisny, M. B., Ostaszewski, B. L., Squazzo, S. L., Koo, E. H., Rydel, R. E., Teplow, D. B., & Selkoe, D. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9564 · Cited by 369
Self-citationWeidemann, A., Eggert, S., Reinhard, F. B. M., Vogel, M., Paliga, K., Baier, G., Masters, C. L., Beyreuther, K. T., & Evin, G. M. (2002) · Biochemistry · doi:10.1021/bi015794o · Cited by 362
Aβ vaccination effects on plaque pathology in the absence of encephalitis in Alzheimer disease
Masliah, E., Hansen, L., Adame, A., Crews, L. A., Bard, F., Lee, C., Seubert, P. A., Games, D., Kirby, L., & Schenk, D. (2005) · Neurology · doi:10.1212/01.wnl.0000148590.39911.df · Cited by 355
Oda, T., Wals, P., Osterburg, H. H., Johnson, S. A., Pasinetti, G. M., Morgan, T. E., Rozovsky, I., Stine, W. B., Snyder, S. W., Holzman, T. F., et al. (1995) · Experimental Neurology · doi:10.1006/exnr.1995.1080 · Cited by 352
Vaccination with soluble Aβ oligomers generates toxicity‐neutralizing antibodies
Lambert, M. P., Viola, K. L., Chromy, B. A., Chang, L., Morgan, T. E., Yu, J., Venton, D. L., Krafft, G. A., Finch, C. E., & Klein, W. L. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00592.x · Cited by 349
Mann, D. M. A., Yates, P. O., & Marcyniuk, B. (1984) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1984.tb00351.x · Cited by 345
Kumar‐Singh, S., Theuns, J., Broeck, B. V., Pirici, D. N., Vennekens, K., Corsmit, E., Cruts, M., Dermaut, B., Wang, R., & Broeckhoven, C. V. (2006) · Human Mutation · doi:10.1002/humu.20336 · Cited by 330
Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
Zhao, L., Ma, Q.-L., Calon, F., Harris-White, M. E., Yang, F., Lim, G. P., Morihara, T., Ubeda, O. J., Ambegaokar, S., Hansen, J. E., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1630 · Cited by 317
Targeting soluble Aβ peptide with Tramiprosate for the treatment of brain amyloidosis
Gervais, F., Paquette, J., Morissette, C., Krzywkowski, P., Yu, M. W. N., Azzi, M., Lacombe, D., Kong, X., Aman, A. M., Laurin, J., et al. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.02.015 · Cited by 313
Walsh, D. M., Townsend, M., Podlisny, M. B., Shankar, G. M., Fadeeva, J. V., El‐Agnaf, O. M. A., Hartley, D. M., & Selkoe, D. J. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.4391-04.2005 · Cited by 295
Self-citationGu, Y., Misonou, H., Sato, T., Dohmae, N., Takio, K., & Ihara, Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100357200 · Cited by 292
Effects of a γ-secretase inhibitor in a randomized study of patients with Alzheimer disease
Siemers, E., Quinn, J. F., Kaye, J. A., Farlow, M. R., Porsteinsson, A. P., Tariot, P. N., Zoulnouni, P., Galvin, J. E., Holtzman, D. M., Knopman, D. S., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000198762.41312.e1 · Cited by 291
Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0483 · Cited by 290
PRESENILE DEMENTIA AND ALZHEIMER'S DISEASE IN MONGOLISM
Olson, M. I., & Shaw, C. (1969) · Brain · doi:10.1093/brain/92.1.147 · Cited by 290
Copper levels are increased in the cerebral cortex and liver of APP and APLP2 knockout mice
White, A. R., Reyes, R., Mercer, J. F. B., Camakaris, J., Zheng, H., Bush, A. I., Multhaup, G., Beyreuther, K. T., Masters, C. L., & Cappai, R. (1999) · Brain Research · doi:10.1016/s0006-8993(99)01861-2 · Cited by 287
Xia, W., Zhang, J., Kholodenko, D., Citron, M., Podlisny, M. B., Teplow, D. B., Haass, C., Seubert, P. A., Koo, E. H., & Selkoe, D. J. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.12.7977 · Cited by 286
Self-citationGoldsbury, C. S., Wirtz, S., Müller, S. A., Sunderji, S., Wicki, P., Aebi, U., & Frey, P. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4259 · Cited by 279
Pathogenic Effects of D23N Iowa Mutant Amyloid β-Protein
Nostrand, W. E. V., Melchor, J. P., Cho, H. S., Greenberg, S. M., & Rebeck, G. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104135200 · Cited by 249
Wısnıewskı, T., Ghiso, J. A., & Frangione, B. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91706-i · Cited by 248
Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 244
Molecular bases of long-term memories: a question of persistence
Dudai, Y. (2002) · Current Opinion in Neurobiology · doi:10.1016/s0959-4388(02)00305-7 · Cited by 233
Castaño, E. M., Ghiso, J. A., Prelli, F. C., Gorevic, P. D., Migheli, A., & Frangione, B. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80241-8 · Cited by 225
Selective neuronal degeneration induced by soluble oligomeric amyloid beta‐protein
Kim, H., Chae, S., Lee, D., Chromy, B. A., Lee, S. C., Park, Y., Klein, W. L., Krafft, G. A., & Hong, S. (2002) · The FASEB Journal · doi:10.1096/fj.01-0987fje · Cited by 219
Comery, T. A., Martone, R. L., Aschmies, S., Atchison, K. P., Diamantidis, G., Gong, X., Zhou, H., Kreft, A. F., Pangalos, M. N., Sonnenberg‐Reines, J., et al. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.2693-05.2005 · Cited by 214
Dineley, K. T., Xia, X., Bui, D., Sweatt, J. D., & Zheng, H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200164200 · Cited by 212
Methodological variables in the assessment of beta amyloid neurotoxicity
Busciglio, J. A., Lorenzo, A., & Yankner, B. A. (1992) · Neurobiology of Aging · doi:10.1016/0197-4580(92)90065-6 · Cited by 211
Schroeter, E. H., Ilagan, M. X. G., Brunkan, A. L., Hecimovic, S. K., Li, Y., Xu, M., Lewis, H. D., Saxena, M. T., Strooper, B. D., Coonrod, A., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1735338100 · Cited by 197
Huang, S.-M., Mouri, A., Kokubo, H., Nakajima, R., Suemoto, T., Higuchi, M., Staufenbiel, M., Noda, Y., Yamaguchi, H., Nabeshima, T., et al. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601372200 · Cited by 182
Solution State Characterization of Amyloid β-Derived Diffusible Ligands
Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Chen-Dodson, E., Acton, P. J., Keller, P. M., Yeager, M. D., Wang, H., Shughrue, P. J., et al. (2006) · Biochemistry · doi:10.1021/bi061850f · Cited by 182
Orally available compound prevents deficits in memory caused by the Alzheimer amyloid‐β oligomers
Townsend, M., Cleary, J. P., Mehta, T., Hofmeister, J. J., Lesné, S., O‘Hare, E., Walsh, D. M., & Selkoe, D. J. (2006) · Annals of Neurology · doi:10.1002/ana.21051 · Cited by 169
Self-citationLoss of Neprilysin Function Promotes Amyloid Plaque Formation and Causes Cerebral Amyloid Angiopathy
Farris, W., Schütz, S. G., Cirrito, J. R., Shankar, G. M., Sun, X., George, A., Leissring, M. A., Walsh, D. M., Qiu, W. Q., Holtzman, D. M., et al. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070105 · Cited by 159
Self-citationZhao, G., Mao, G., Tan, J., Dong, Y., Cui, M., Kim, S.-H., & Xu, X. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c400473200 · Cited by 154
Jonghe, C. D., Zehr, C., Yager, D., Prada, C.-M., Younkin, S. G., Hendriks, L., Broeckhoven, C. V., & Eckman, C. B. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0202 · Cited by 151
Kakuda, N., Funamoto, S., Yagishita, S., Takami, M., Osawa, S., Dohmae, N., & Ihara, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513453200 · Cited by 150
Acceleration of Amyloid β-Peptide Aggregation by Physiological Concentrations of Calcium
Isaacs, A. M., Senn, D. B., Yuan, M., Shine, J. P., & Yankner, B. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602061200 · Cited by 149
New Class of Inhibitors of Amyloid-β Fibril Formation
Lashuel, H. A., Hartley, D. M., Balakhaneh, D., Aggarwal, A. K., Teichberg, S., & Callaway, D. J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206593200 · Cited by 146
Morishima‐Kawashima, M., & Ihara, Y. (1998) · Biochemistry · doi:10.1021/bi981843u · Cited by 146
Quantitation of amyloid beta-protein (A beta) in the cortex during aging and in Alzheimer's disease.
(1998) · Europe PMC (PubMed Central) · Cited by 145
Maloney, M. T., Minamide, L. S., Kinley, A. W., Boyle, J. A., & Bamburg, J. R. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.3711-05.2005 · Cited by 140
Huppert, S. S., Ilagan, M. X. G., Strooper, B. D., & Kopan, R. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.02.019 · Cited by 136
Motte, J., & Williams, R. S. (1989) · Acta Neuropathologica · doi:10.1007/bf00687256 · Cited by 126
Transgenic mice expressing Alzheimer amyloid precursor proteins
Hsiao, K. (1998) · Experimental Gerontology · doi:10.1016/s0531-5565(98)00045-x · Cited by 122
Tamagno, E., Bardini, P., Guglielmotto, M., Danni, O., & Tabaton, M. (2006) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2006.01.021 · Cited by 119
Appearance of Sodium Dodecyl Sulfate-Stable Amyloid β-Protein (Aβ) Dimer in the Cortex During Aging
Enya, M., Morishima-Kawashima, M., Yoshimura, M., Shinkai, Y., Kusui, K., Khan, K., Games, D., Schenk, D., Sugihara, S., Yamaguchi, H., et al. (1999) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)65273-x · Cited by 111
Amyloid‐β oligomers are inefficiently measured by enzyme‐linked immunosorbent assay
Stenh, C., Englund, H., Lord, A., Johansson, A., Almeida, C. G., Gellerfors, P., Greengard, P., Gouras, G. K., Lannfelt, L., & Nilsson, L. N. G. (2005) · Annals of Neurology · doi:10.1002/ana.20524 · Cited by 99
Wu, C.-C., Chawla, F., Games, D., Rydel, R. E., Freedman, S. B., Schenk, D., Young, W. G., Morrison, J. H., & Bloom, F. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402147101 · Cited by 91
Chang, L., Bakhos, L., Wang, Z., Venton, D. L., & Klein, W. L. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:3:305 · Cited by 81
Whalen, B. M., Selkoe, D. J., & Hartley, D. M. (2005) · Neurobiology of Disease · doi:10.1016/j.nbd.2005.03.007 · Cited by 79
Self-citationProtofibrils of amyloid β-protein inhibit specific K+ currents in neocortical cultures
Ye, C. P., Selkoe, D. J., & Hartley, D. M. (2003) · Neurobiology of Disease · doi:10.1016/s0969-9961(03)00068-8 · Cited by 74
Self-citationLemere, C. A., Maier, M., Jiang, L., Peng, Y., & Seabrook, T. J. (2006) · Rejuvenation Research · doi:10.1089/rej.2006.9.77 · Cited by 68
Funato, H., Enya, M., Yoshimura, M., Morishima‐Kawashima, M., & Ihara, Y. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65094-8 · Cited by 64
Cloning and Expression of the cDNA for aDrosophilaInsulin-Degrading Enzyme
Kuo, W., Gehm, B. D., & Rosner, M. R. (1990) · Molecular Endocrinology · doi:10.1210/mend-4-10-1580 · Cited by 63
Richardson, R. L., Kim, E.-M., Shephard, R. A., Gardiner, T. A., Cleary, J. P., & O‘Hare, E. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03006-8 · Cited by 62
Aβ Immunotherapy: Lessons Learned for Potential Treatment of Alzheimer’s Disease
Schenk, D. B., Seubert, P. A., Grundman, M., & Black, R. (2005) · Neurodegenerative Diseases · doi:10.1159/000090365 · Cited by 60
An Ultrastructural Study of Amyloid Intermediates in Aβ1–42 Fibrillogenesis
Nybo, M., Svehag, & Nielsen, H. (1999) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.1999.00526.x · Cited by 55
Mechanisms of memory loss in Aβ and tau mouse models
Ashe, K. H. (2005) · Biochemical Society Transactions · doi:10.1042/bst0330591 · Cited by 42
[Senile dementia and Alzheimer's disease ].
Sanz, G. (1991) · PubMed · Cited by 30
The Many Faces of Aβ: Structures and Activity
Walsh, D. M., Hartley, D. M., & Selkoe, D. J. (2003) · Current Medicinal Chemistry - Immunology Endocrine & Metabolic Agents · doi:10.2174/1568013033483311 · Cited by 20
Self-citationO‘Hare, E., Levine, A. S., Semotuk, M., Tierney, K. J., Shephard, R. A., Grace, M. K., & Cleary, J. P. (1996) · PubMed · Cited by 19
Gan, L., Mueller-Steiner, S., Zhou, Y., Arai, H., Roberson, E. D., Wang, X., Chen, J., Yu, G.-Q., Esposito, L., & Mucke, L. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2006.05.340 · Cited by 2
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
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569
Hyman, B. T., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Carrillo, M. C., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., et al. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.10.007 · Cited by 3,092
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Cerebrospinal fluid and plasma biomarkers in Alzheimer disease
Blennow, K., Hampel, H., Weiner, M., & Zetterberg, H. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.4 · Cited by 1,863
Amyloid-β–induced neuronal dysfunction in Alzheimer's disease: from synapses toward neural networks
Palop, J. J., & Mucke, L. (2010) · Nature Neuroscience · doi:10.1038/nn.2583 · Cited by 1,651
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review