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…”
Background
Flagged first, then by citations
1 of the 147 references couldn’t be matched to a known paper.
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 1,001–1,010 of 1,010
Some evolutionary perspectives on Alzheimer's disease pathogenesis and pathology
Glass, D. J., & Arnold, S. E. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.05.2408 · Cited by 29
Neuronal Cx3cr1 Deficiency Protects against Amyloid β-Induced Neurotoxicity
Dworzak, J., Renvoisé, B., Habchi, J., Yates, E. V., Combadière, C., Knowles, T. P., Dobson, C. M., Blackstone, C., Paulsen, O., & Murphy, P. M. (2015) · PLOS ONE · doi:10.1371/journal.pone.0127730 · Cited by 30
O’Nuallain, B., Klyubin, I. V., Donald, J. M. M., Foster, J. S., Welzel, A. T., Barry, A. E., Dykoski, R. K., Cleary, J. P., Gebbink, M. F. B. G., Rowan, M. J., et al. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07389.x · Cited by 33
Self-citationTikhonova, M. A., Amstislavskaya, T. G., Belichenko, V. M., Fedoseeva, L. A., Kovalenko, S. P., Pisareva, E. E., Avdeeva, A. S., Kolosova, N. G., Belyaev, N. D., & Aftanas, L. I. (2018) · BMC Neuroscience · doi:10.1186/s12868-018-0412-5 · Cited by 30
Opposing Roles of apolipoprotein E in aging and neurodegeneration
Hudry, E., Klickstein, J., Cannavo, C., Jackson, R., Muzikansky, A., Gandhi, S., Urick, D., Sargent, T., Wrobleski, L., Roe, A. D., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900325 · Cited by 30
Spires-Jones, T. L., Calignon, A. D., Meyer-Luehmann, M., Bacskai, B. J., & Hyman, B. T. (2011) · Methods · doi:10.1016/j.ymeth.2010.12.009 · Cited by 24
Peptidomimetics That Inhibit and Partially Reverse the Aggregation of Aβ1–42
Stark, T., Lieblein, T., Pohland, M., Kalden, E., Freund, P., Zangl, R., Grewal, R., Heilemann, M., Eckert, G. P., Morgner, N., et al. (2017) · Biochemistry · doi:10.1021/acs.biochem.7b00223 · Cited by 17
Jeon, J., & Shell, M. S. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.03.019 · Cited by 16
A Chronological Review of Potential Disease-Modifying Therapeutic Strategies for Alzheimer’s Disease
Ettcheto, M., Busquets, O., Espinosa-Jiménez, T., Verdaguer, E., Auladell, C., & Camins, A. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200211121416 · Cited by 13
Beta-amyloid oligomers: recent developments
Borutaite, V., Morkuniene, R., & Valincius, G. (2011) · bmc · doi:10.1515/bmc.2011.019 · Cited by 9
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
