The DOI matches its Crossref record; 92 of the 92 references it cites were found in a registry or an index.
Structure of an Intermediate State in Protein Folding and Aggregation
Abstract
Protein Tipping Point: Amyloid fibrils are insoluble protein aggregates that play a role in various degenerative diseases. Recent experiments have provided insight into fibrillar structures; however, the mechanisms of aggregation remain unclear. Neudecker et al. (p. 362 ; see the Perspective by Eliezer ) report the structure of a transient folding intermediate in a protein SH3 domain known to undergo aggregation. The intermediate is stabilized by non-native interactions and exposes an aggregation-prone β strand. Thus, for this protein, folding from the intermediate state will compete with aggregation.
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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
The amyloid state and its association with protein misfolding diseases.
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Self-citationProtein misfolding in neurodegenerative diseases: Implications and strategies
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Chemical exchange in biomacromolecules: Past, present, and future
Palmer, A. G. (2014) · Journal of Magnetic Resonance · doi:10.1016/j.jmr.2014.01.008 · Cited by 263
Characterization of the free-energy landscapes of proteins by NMR-guided metadynamics
Granata, D., Camilloni, C., Vendruscolo, M., & Laio, A. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1218350110 · Cited by 143
Self-citation
Metadata
- Authors
- Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., & Kay, L. E.
- Venue
- Science
- Published
- 2012-04-20
- Volume
- 336
- Issue
- 6079
- Pages
- 362-366
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2066000489
- Cited by
- 398
- References
- 92
- FWCI
- 16.61
- Type
- journal article
- Language
- en
- Open access
- closed
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- Neudecker, P., Robustelli, P., Cavalli, A., Walsh, P., Lundström, P., Zarrine-Afsar, A., Sharpe, S., Vendruscolo, M., & Kay, L. E. (2012). Structure of an Intermediate State in Protein Folding and Aggregation. Science. https://doi.org/10.1126/science.1214203
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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.
