The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides
Open accessAbstract
Significance: Alzheimer's disease and several related disorders are associated with the assembly of specific proteins into ordered fibrillar aggregates. In Alzheimer's disease, the key component of pathological aggregates, the Aβ peptide, is produced from a precursor protein in variable lengths: Aβ40 is more abundant and Aβ42 more aggregation-prone. To shed light on the molecular basis of disease progression, the aggregation process has been studied in vitro. New theoretical models allow us to relate kinetic measurements to the rates of the individual processes underlying the aggregation reaction. We find that the loss of two residues in Aβ40 relative to Aβ42 significantly slows nucleation of aggregates in solution, thereby shifting the mechanism yet more strongly towards nucleation on the surface of fibrils.
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Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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
Amyloid seeds formed by cellular uptake, concentration, and aggregation of the amyloid-beta peptide
Hu, X., Crick, S. L., Bu, G., Frieden, C., Pappu, R. V., & Lee, J.-M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911281106 · Cited by 426 · cited 1×
“2 m 0 k+ m n2 0 k2 1+ m n2 0 KM uut [5]”
Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Self-citationLipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation
Galvagnion, C., Buell, A. K., Meisl, G., Michaels, T. C. T., Vendruscolo, M., Knowles, T. P. J., & Dobson, C. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1750 · Cited by 661
Self-citationCSF A β 42/A β 40 and A β 42/A β 38 ratios: better diagnostic markers of Alzheimer disease
Janelidze, S., Zetterberg, H., Mattsson, N., Palmqvist, S., Vanderstichele, H., Lindberg, O., van Westen, D., Stomrud, E., Minthon, L., Blennow, K., et al. (2016) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.274 · Cited by 456
Quantitative analysis of co-oligomer formation by amyloid-beta peptide isoforms.
Iljina, M., Garcia, G. A., Dear, A. J., Flint, J., Narayan, P., Michaels, T. C. T., Dobson, C. M., Frenkel, D., Knowles, T. P. J., & Klenerman, D. (2016) · Scientific Reports · doi:10.1038/srep28658 · Cited by 68
Self-citationBelsare, K. D., Wu, H., Mondal, D., Bond, A., Castillo, E., Jin, J., Jo, H., Roush, A. E., Pilla, K. B., Sali, A., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2114486119 · Cited by 68
Metadata
- Authors
- Meisl, G., Yang, X., Hellstrand, E., Frohm, B., Kirkegaard, J. B., Cohen, S. I. A., Dobson, C. M., Linse, S., & Knowles, T. P. J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2014-06-17
- Volume
- 111
- Issue
- 26
- Pages
- 9384-9389
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2049421402
- Cited by
- 505
- References
- 4
- FWCI
- 21.19
- Type
- journal article
- Language
- en
- Open access
- green
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- Meisl, G., Yang, X., Hellstrand, E., Frohm, B., Kirkegaard, J. B., Cohen, S. I. A., Dobson, C. M., Linse, S., & Knowles, T. P. J. (2014). Differences in nucleation behavior underlie the contrasting aggregation kinetics of the Aβ40 and Aβ42 peptides. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1401564111
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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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