The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
Interpreting the Aggregation Kinetics of Amyloid Peptides
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Cites
CHARMM: A program for macromolecular energy, minimization, and dynamics calculations
Brooks, B. R., Bruccoleri, R. E., Olafson, B. D., States, D. J., Swaminathan, S., & Karplus, M. (1983) · Journal of Computational Chemistry · doi:10.1002/jcc.540040211 · Cited by 14,944
Hierarchical Clustering Schemes
Johnson, S. C. (1967) · Psychometrika · doi:10.1007/bf02289588 · Cited by 4,897
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
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
Structure of the cross-β spine of amyloid-like fibrils
Nelson, R., Sawaya, M. R., Balbirnie, M., Madsen, A. Ø., Riekel, C., Grothe, R., & Eisenberg, D. (2005) · Nature · doi:10.1038/nature03680 · Cited by 2,202
Molecular Biology of Prion Diseases
Prusiner, S. B. (1991) · Science · doi:10.1126/science.1675487 · Cited by 1,988
Natural oligomers of the amyloid-β protein specifically disrupt cognitive function
Cleary, J. P., Walsh, D. M., Hofmeister, J. J., Shankar, G. M., Kuskowski, M. A., Selkoe, D. J., & Ashe, K. H. (2005) · Nature Neuroscience · doi:10.1038/nn1372 · Cited by 1,687
Conway, K. A., Lee, S.-J., Rochet, J.-C., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,541
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Serio, T. R., Cashikar, A. G., Kowal, A. S., Sawicki, G. J., Moslehi, J. J., Serpell, L., Arnsdorf, M. F., & Lindquist, S. L. (2000) · Science · doi:10.1126/science.289.5483.1317 · Cited by 963
Cited by
Mechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303
Membrane 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
Insulin-Degrading Enzyme in the Fight against Alzheimer's Disease
Kurochkin, I. V., Guarnera, E., & Berezovsky, I. N. (2018) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.10.008 · Cited by 185
Qiao, Q., Bowman, G. R., & Huang, X. (2013) · Journal of the American Chemical Society · doi:10.1021/ja403147m · Cited by 182
Metadata
- Authors
- Pellarin, R., & Caflisch, A.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2006-07
- Volume
- 360
- Issue
- 4
- Pages
- 882-892
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1995394213
- Cited by
- 254
- References
- 47
- FWCI
- 11.37
- Type
- journal article
- Language
- en
- Open access
- closed
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- Pellarin, R., & Caflisch, A. (2006). Interpreting the Aggregation Kinetics of Amyloid Peptides. Journal of Molecular Biology. https://doi.org/10.1016/j.jmb.2006.05.033
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
