The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Exploring amyloid formation by a de novo design
Open accessAbstract
Protein deposition as amyloid fibrils underlies many debilitating human disorders. The complexity and size of disease-related polypeptides, however, often hinders a detailed rational approach to study effects that contribute to the process of amyloid formation. We report here a simplified peptide sequence successfully designed de novo to fold into a coiled-coil conformation under ambient conditions but to transform into amyloid fibrils at elevated temperatures. We have determined the crystal structure of the coiled-coil form and propose a detailed molecular model for the peptide in its fibrillar state. The relative stabilities of the two structural forms and the kinetics of their interconversion were found to be highly sensitive to small sequence changes. The results reveal the importance of specific packing interactions on the kinetics of amyloid formation and show the potential of this exceptionally favorable system for probing details of the molecular origins of amyloid disease.
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Cites
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
Self-citationToxic Proteins in Neurodegenerative Disease
Taylor, J. P., Hardy, J., & Fischbeck, K. H. (2002) · Science · doi:10.1126/science.1067122 · Cited by 1,251
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
Self-citationAmyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Cited by
Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
The Design of Coiled-Coil Structures and Assemblies
Woolfson, D. N. (2005) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(05)70004-8 · Cited by 585
Molecular structure of amyloid fibrils: insights from solid-state NMR
Tycko, R. (2006) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583506004173 · Cited by 527
Dong, H., Paramonov, S. E., Aulisa, L., Bakota, E. L., & Hartgerink, J. D. (2007) · Journal of the American Chemical Society · doi:10.1021/ja072536r · Cited by 344
Yerbury, J. J., Poon, S., Meehan, S., Thompson, B., Kumita, J. R., Dobson, C. M., & Wilson, M. R. (2007) · The FASEB Journal · doi:10.1096/fj.06-7986com · Cited by 324
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Metadata
- Authors
- Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., & Steinmetz, M. O.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-02-26
- Volume
- 101
- Issue
- 13
- Pages
- 4435-4440
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2125172857
- Cited by
- 164
- References
- 4
- FWCI
- 12.16
- Type
- journal article
- Language
- en
- Open access
- green
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- Kammerer, R. A., Kostrewa, D., Zurdo, J., Detken, A., García-Echeverría, C., Green, J. D., Müller, S. A., Meier, B. H., Winkler, F. K., Dobson, C. M., & Steinmetz, M. O. (2004). Exploring amyloid formation by a de novo design. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0306786101
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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.
