The DOI matches its Crossref record; 209 of the 209 references it cites were found in a registry or an index.
Folding versus aggregation: Polypeptide conformations on competing pathways
Open accessAbstract
Protein aggregation has now become recognised as an important and generic aspect of protein energy landscapes. Since the discovery that numerous human diseases are caused by protein aggregation, the biophysical characterisation of misfolded states and their aggregation mechanisms has received increased attention. Utilising experimental techniques and computational approaches established for the analysis of protein folding reactions has ensured rapid advances in the study of pathways leading to amyloid fibrils and amyloid-related aggregates. Here we describe recent experimental and theoretical advances in the elucidation of the conformational properties of dynamic, heterogeneous and/or insoluble protein ensembles populated on complex, multidimensional protein energy landscapes. We discuss current understanding of aggregation mechanisms in this context and describe how the synergy between biochemical, biophysical and cell-biological experiments are beginning to provide detailed insights into the partitioning of non-native species between protein folding and aggregation pathways.
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1 retracted
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A quantitative measure for protein conformational heterogeneity
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Balistreri, A., Kolli, D., Jayaweera, S. W., Lundahl, D., Han, Y., Kalcec, L., Goetzler, E., Alessio, R., Ruotolo, B., Olofsson, A., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110217 · Cited by 10
Metadata
- Authors
- Jahn, T. R., & Radford, S. E.
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2008-01
- Volume
- 469
- Issue
- 1
- Pages
- 100-117
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2014875724
- Cited by
- 428
- References
- 209
- FWCI
- 7.66
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Jahn, T. R., & Radford, S. E. (2008). Folding versus aggregation: Polypeptide conformations on competing pathways. Archives of Biochemistry and Biophysics. https://doi.org/10.1016/j.abb.2007.05.015
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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.
