The DOI matches its Crossref record; 292 of the 292 references it cites were found in a registry or an index.
Targeting protein aggregation for the treatment of degenerative diseases
Open accessAbstract
The aggregation of specific proteins is hypothesized to underlie several degenerative diseases, which are collectively known as amyloid disorders. However, the mechanistic connection between the process of protein aggregation and tissue degeneration is not yet fully understood. Here, we review current and emerging strategies to ameliorate aggregation-associated degenerative disorders, with a focus on disease-modifying strategies that prevent the formation of and/or eliminate protein aggregates. Persuasive pharmacological and genetic evidence now supports protein aggregation as the cause of postmitotic tissue dysfunction or loss. However, a more detailed understanding of the factors that trigger and sustain aggregate formation and of the structure–activity relationships underlying proteotoxicity is needed to develop future disease-modifying therapies.
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1 retracted
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Metadata
- Authors
- Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2015-09-04
- Volume
- 14
- Issue
- 11
- Pages
- 759-780
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W1856496738
- Cited by
- 419
- References
- 292
- FWCI
- 5.02
- Type
- journal article
- Language
- en
- Open access
- green
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- Eisele, Y. S., Monteiro, C., Fearns, C., Encalada, S. E., Wiseman, R. L., Powers, E. T., & Kelly, J. W. (2015). Targeting protein aggregation for the treatment of degenerative diseases. Nature Reviews Drug Discovery. https://doi.org/10.1038/nrd4593
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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.
