The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A partially folded structure of amyloid-beta(1–40) in an aqueous environment
Open accessAbstract
Aggregation of the Aβ1-40 peptide is linked to the development of extracellular plaques characteristic of Alzheimer’s disease. While previous studies commonly show the Aβ1-40 is largely unstructured in solution, we show that Aβ1-40 can adopt a compact, partially folded structure. In this structure, the central hydrophobic region of the peptide forms a 310 helix from H13 to D23 and the N- and C-termini collapse against the helix due to the clustering of hydrophobic residues. Helical intermediates have been predicted to be crucial on-pathway intermediates in amyloid fibrillogenesis, and the structure presented here presents a new target for investigation of early events in Aβ1-40 fibrillogenesis.
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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
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538
The redox chemistry of the Alzheimer's disease amyloid β peptide
Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608
Cited by
Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Self-citationAmyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N.-V., Coté, S., De Simone, A., Doig, A. J., Faller, P., Garcia, A., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 584
Untangling Amyloid-β, Tau, and Metals in Alzheimer’s Disease
Savelieff, M. G., Lee, S., Liu, Y., & Lim, M. H. (2013) · ACS Chemical Biology · doi:10.1021/cb400080f · Cited by 400
Self-citationMembrane Protein Structure, Function, and Dynamics: a Perspective from Experiments and Theory
Cournia, Z., Allen, T. W., Andricioaei, I., Antonny, B., Baum, D., Brannigan, G., Buchete, N.-V., Deckman, J. T., Delemotte, L., del Val, C., et al. (2015) · The Journal of Membrane Biology · doi:10.1007/s00232-015-9802-0 · Cited by 235
Metadata
- Authors
- Vivekanandan, S., Brender, J. R., Lee, S. Y., & Ramamoorthy, A.
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 411
- Issue
- 2
- Pages
- 312-316
- ISSN
- 0006-291X (ISSN-L)
- OpenAlex
- W2022756726
- Cited by
- 432
- References
- 3
- FWCI
- 15.41
- Type
- journal article
- Language
- en
- Open access
- green
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- Vivekanandan, S., Brender, J. R., Lee, S. Y., & Ramamoorthy, A. (2011). A partially folded structure of amyloid-beta(1–40) in an aqueous environment. Biochemical and Biophysical Research Communications. https://doi.org/10.1016/j.bbrc.2011.06.133
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
