The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Protein aggregation processes: In search of the mechanism
Open accessAbstract
Amyloid formation typically follows a time course in which there is a long lag period followed by a rapid formation of fibrils. In this review, I show that the standard mechanisms of polymerization need to be expanded to consider that the monomeric proteins/peptides involved in amyloid formation are intrinsically disordered and exist as an ensemble of disordered‐collapsed states. The review focuses primarily on events which occur in the long lag period defining these as protein folding issues, coupled with formation of oligomers. Experimental methods to explore folding and oligomerization issues over a wide range of protein concentrations using primarily fluorescence and 19 F‐NMR methods are discussed.
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Citations
Cites
Necula, M., Kayed, R., Milton, S., & Glabe, C. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608207200 · Cited by 680
Cited by
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
- Frieden, C.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2007-11
- Volume
- 16
- Issue
- 11
- Pages
- 2334-2344
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- OpenAlex
- W2042978261
- Cited by
- 181
- References
- 1
- FWCI
- 5.93
- Type
- journal article
- Language
- en
- Open access
- green
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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.
