The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Size-dependent neurotoxicity of β-amyloid oligomers
Open accessAbstract
The link between the size of soluble amyloid β (Aβ) oligomers and their toxicity to rat cerebellar granule cells (CGC) was investigated. Variation in conditions during in vitro oligomerization of Aβ1-42 resulted in peptide assemblies with different particle size as measured by atomic force microscopy and confirmed by the dynamic light scattering and fluorescence correlation spectroscopy. Small oligomers of Aβ1-42 with a mean particle z-height of 1-2 nm exhibited propensity to bind to the phospholipid vesicles and they were the most toxic species that induced rapid neuronal necrosis at submicromolar concentrations whereas the bigger aggregates (z-height above 4-5 nm) did not bind vesicles and did not cause detectable neuronal death. Similar neurotoxic pattern was also observed in primary cultures of cortex neurons whereas Aβ1–42 oligomers, monomers and fibrils were non-toxic to glial cells in CGC cultures or macrophage J774 cells. However, both oligomeric forms of Aβ1-42 induced reduction of neuronal cell densities in the CGC cultures.
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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RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory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
RetractedWalsh, 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
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
Shankar, 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
Diffusible, 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
Aβ 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
In vitro characterization of conditions for amyloid-β peptide oligomerization and fibrillogenesis
Stine, W. B., Dahlgren, K. N., Krafft, G. A., & LaDu, M. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210207200 · Cited by 1,015
Klyubin, I., Betts, V., Welzel, A. T., Blennow, K., Zetterberg, H., Wallin, A., Lemere, C. A., Cullen, W. K., Peng, Y., Wisniewski, T., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.5161-07.2008 · Cited by 321
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Cited by
Biochemistry of Amyloid -Protein and Amyloid Deposits in Alzheimer Disease
Masters, C. L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006262 · Cited by 542
Different soluble aggregates of Aβ42 can give rise to cellular toxicity through different mechanisms
De, S., Wirthensohn, D. C., Flagmeier, P., Hughes, C., Aprile, F. A., Ruggeri, F. S., Whiten, D. R., Emin, D., Xia, Z., Varela, J. A., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09477-3 · Cited by 448
Nanotechnologies for Alzheimer's disease: diagnosis, therapy, and safety issues
Brambilla, D., Le Droumaguet, B., Nicolas, J., Hashemi, S. H., Wu, L.-P., Moghimi, S. M., Couvreur, P., & Andrieux, K. (2011) · Nanomedicine: Nanotechnology, Biology and Medicine · doi:10.1016/j.nano.2011.03.008 · Cited by 294
Amyloid β-protein oligomers and Alzheimer’s disease
Hayden, E. Y., & Teplow, D. B. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt226 · Cited by 276
Soluble Aβ oligomers and protofibrils induce NLRP3 inflammasome activation in microglia
Lučiūnaitė, A., McManus, R. M., Jankunec, M., Rácz, I., Dansokho, C., Dalgėdienė, I., Schwartz, S., Brosseron, F., & Heneka, M. T. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.14945 · Cited by 192
Metadata
- Authors
- Cizas, P., Budvytyte, R., Morkuniene, R., Moldovan, R., Broccio, M., Lösche, M., Niaura, G., Valincius, G., & Borutaite, V.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2010-04
- Volume
- 496
- Issue
- 2
- Pages
- 84-92
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2135370282
- Cited by
- 179
- References
- 9
- FWCI
- 6.28
- Type
- journal article
- Language
- en
- Open access
- green
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- Cizas, P., Budvytyte, R., Morkuniene, R., Moldovan, R., Broccio, M., Lösche, M., Niaura, G., Valincius, G., & Borutaite, V. (2010). Size-dependent neurotoxicity of β-amyloid oligomers. Archives of Biochemistry and Biophysics. https://doi.org/10.1016/j.abb.2010.02.001
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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