The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding
Abstract
Significance: Aggregation of tumor suppressor p53 oncogenic mutants not only loses their activity but may also lead to gain of oncogenic function, possibly by coaggregation with other proteins. We explored how a destabilized p53 mutant may coaggregate with WT p53 and its homologs p63 and p73. The results are explained by the simple two-step initiation mechanism we proposed. Rather than the oncogenic mutant seeding coaggregation by a prion-like process, coaggregation results from the simultaneous unfolding and cross-reaction of WT and mutant molecules. Consequently, preformed p53 aggregate displays little seeding of aggregation of p53, and high concentrations of p53 mutants are required to trap WT p53 into aggregate. Coaggregation is predominantly by trapping rather than seeding and induced propagation.
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“p53 aggregation not only causes the loss of DNA recognition capacity and loss of the proapoptotic function of p53 but also promotes GOF effects.152,153”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [152]
In the citing paper
“p53 aggregation not only causes the loss of DNA recognition capacity and loss of the proapoptotic function of p53 but also promotes GOF effects.152,153”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [152]
In the citing paper
“p53 aggregation not only causes the loss of DNA recognition capacity and loss of the proapoptotic function of p53 but also promotes GOF effects.152,153”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [152]
In the citing paper
“Once mutated, its structural stability is compromised, exposing adhesion sequences encased in the hydrophobic core of p53, which drives the formation of p53 aggregates,481 thereby depriving p53 of its DNA recognition function and proapoptotic capacity482,483”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [483]
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Citations
Cites
Self-propagation of pathogenic protein aggregates in neurodegenerative diseases
Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663
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Cited by
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
(2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.08.002 · Cited by 78
p53: from understanding its structure to advances in therapeutic targeting
Wang, W., Liu, X., Liu, H., Abolhassani, H., Yan, H., Zhang, H., & Wang, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02549-5 · Cited by 30
Metadata
- Authors
- Wang, G., & Fersht, A. R.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2015-02-09
- Volume
- 112
- Issue
- 8
- Pages
- 2443-2448
- ISSN
- 0027-8424
- 1091-6490
- Cited by
- 78
- References
- 1
- Language
- en
- Funders
- EC | European Research Council (268506)
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- Wang, G., & Fersht, A. R. (2015). Propagation of aggregated p53: Cross-reaction and coaggregation vs. seeding. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1500262112
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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.
