The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Aβ40 Oligomers Identified as a Potential Biomarker for the Diagnosis of Alzheimer's Disease
Open accessAbstract
Alzheimer's Disease (AD) is the most prevalent form of dementia worldwide, yet the development of therapeutics has been hampered by the absence of suitable biomarkers to diagnose the disease in its early stages prior to the formation of amyloid plaques and the occurrence of irreversible neuronal damage. Since oligomeric Aβ species have been implicated in the pathophysiology of AD, we reasoned that they may correlate with the onset of disease. As such, we have developed a novel misfolded protein assay for the detection of soluble oligomers composed of Aβ x-40 and x-42 peptide (hereafter Aβ40 and Aβ42) from cerebrospinal fluid (CSF). Preliminary validation of this assay with 36 clinical samples demonstrated the presence of aggregated Aβ40 in the CSF of AD patients. Together with measurements of total Aβ42, diagnostic sensitivity and specificity greater than 95% and 90%, respectively, were achieved. Although larger sample populations will be needed to confirm this diagnostic sensitivity, our studies demonstrate a sensitive method of detecting circulating Aβ40 oligomers from AD CSF and suggest that these oligomers could be a powerful new biomarker for the early detection of AD.
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“These assays, which can be many orders of magnitude more sensitive than ELISAs, have established an AD-dependent accumulation of oligomers in human CSF (Fukumoto et al., 2010; Gao et al., 2010; Georganopoulou et al., 2005; Haes et al., 2005).”
From The Aβ oligomer hypothesis for synapse failure and memory loss in Alzheimer’s disease (2011) · cites this paper as Gao et al., 2010
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedMcKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., & Stadlan, E. M. (1984) · Neurology · doi:10.1212/wnl.34.7.939 · Cited by 27,915 · cited 1×
“and the criteria of probable AD defined by NINCDS-ADRDA”
BackgroundGlobal prevalence of dementia: a Delphi consensus study
Ferri, C. P., Prince, M. J., Brayne, C., Brodaty, H., Fratiglioni, L., Ganguli, M., Hall, K. S., Hasegawa, K., Hendrie, H. C., Huang, Y., et al. (2005) · The Lancet · doi:10.1016/s0140-6736(05)67889-0 · Cited by 5,336 · cited 1×
“It is the most prevalent form of dementia, estimated to affect 13 million people worldwide [1].”
BackgroundSoluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744 · cited 1×
“Its chemical composition is also poorly defined, although several lines of evidence suggest that AD-associated oligomers are primarily composed of Ab42 [3].”
BackgroundCommon 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 · cited 2×
“As amyloid aggregates are characterized by similar cross-beta sheet structure, they share conformational epitopes that are recognized by amyloid-binding molecules such as Congo Red and thioflavin T [15,16] as well as conformation-specific antibodies [17,18].”
BackgroundShankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685
Atomic structures of amyloid cross-β spines reveal varied steric zippers
Sawaya, M. R., Sambashivan, S., Nelson, R. A., Ivanova, M. I., Sievers, S. A., Apostol, M. I., Thompson, M. J., Balbirnie, M., Wiltzius, J. J. W., McFarlane, H. T., et al. (2007) · Nature · doi:10.1038/nature05695 · Cited by 2,279 · cited 1×
“While the precise conformation of in vivo oligomers is unknown, several lines of evidence suggest that aggregated proteins share a number of structural properties. For instance, amyloid fibrils composed of different proteins have similar cross beta sheet structure, allowing binding and detection by a number of compoun…”
BackgroundAlzheimer Disease in the US Population: Prevalence Estimates Using the 2000 Census
Hebert, L. E., Scherr, P. A., Bienias, J. L., Bennett, D. A., & Evans, D. A. (2003) · Archives of Neurology · doi:10.1001/archneur.60.8.1119 · Cited by 2,168 · cited 1×
“elderly population greater than 85 years old [29].”
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“interpretation of these results is that aggregation of the less soluble Ab42 would precede and recruit subsequent aggregation of Ab40, as has been previously suggested [12,35].”
ResultAβ Oligomers – a decade of discovery
Walsh, D. M., & Selkoe, D. J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04426.x · Cited by 1,938 · cited 1×
“In addition, Ab42 appears to be more amyloidogenic than Ab40 and is found more frequently in plaques despite existing at much lower physiological concentrations [13].”
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Diagnosis of Alzheimer’s disease
Rosa‐Neto, P., Rowley, J., Leuzy, A., Mohades, S., Shin, M., Dauar, M. T., & Gauthier, S. G. (2012) · doi:10.2217/ebo.12.66
Neuroimaging and Molecular Biomarkers for Dementia
Polyakova, T., & Араблинский, А. В. (2019) · Neuroscience and Behavioral Physiology · doi:10.1007/s11055-019-00747-7
Cerebrospinal Fluid Biomarkers in Alzheimer’s Disease and Frontotemporal Dementia
Mattsson, N., & Zetterberg, H. (2014) · Springer eBooks · doi:10.1007/978-1-4471-6380-0_9
Recent Advances in Peptoids: Synthesis, Self‐Assembly, and Applications
Malik, S., & Ghosh, G. (2026) · ChemNanoMat · doi:10.1002/cnma.202500725
In vivo evidence for soluble Aβ oligomer-driven neuronal metabolic dysfunction in 5xFAD mice
Dashora, C., & Patel, A. B. (2026) · Alzheimer s Research & Therapy · doi:10.1186/s13195-026-02130-4
“While these relationships are associative and do not permit causal inference, they are consistent with prior clinical and experimental reports implicating soluble Aβ 40 oligomers in metabolic and synaptic dysfunction [74, 75].”
Metadata
- Authors
- Gao, C. M., Yam, A. Y., Wang, X., Magdangal, E., Salisbury, C., Peretz, D., Zuckermann, R. N., Connolly, M. D., Hansson, O., Minthon, L., Zetterberg, H., Blennow, K., Fedynyshyn, J. P., & Allauzen, S.
- Affiliations
- Lund University (SE)
- Sahlgrenska University Hospital (SE)
- Corresponding author
- Fedynyshyn, Joseph P.
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2010-12-30
- Volume
- 5
- Issue
- 12
- Pages
- e15725
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3012719
- OpenAlex
- W2135057867
- Cited by
- 105
- References
- 39
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 2 · 2019: 8 · 2018: 4 · 2017: 11 · 2016: 9 · 2015: 10 · 2014: 17 · 2013: 13 · 2012: 12
- FWCI
- 6.72
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- UCL Discovery (University College London) (submittedVersion)
- Lund University Publications (Lund University) (submittedVersion, other-oa)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, Aβ40, amyloid-beta 42, cerebrospinal fluid biomarkers, early diagnosis, amyloid plaques, sensitivity and specificity
- MeSH terms
- Aged, Alzheimer Disease, Epitopes, Brain, Enzyme-Linked Immunosorbent Assay, Gene Expression Regulation, Humans, Middle Aged, Models, Chemical, Molecular Conformation, Peptide Fragments, Peptides, Protein Conformation, Sensitivity and Specificity, Biomarkers, Amyloid beta-Peptides
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