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Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53
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“The NMR experiments on full-length p53 were carried out with protein concentrations of at least 30 μM, far above the Kd for p53 tetramerization (50 nM).50,62”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [50]
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Citations
Cites
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610
Petitjean, A., Mathe, E., Kato, S., Ishioka, C., Tavtigian, S. V., Hainaut, P., & Olivier, M. (2007) · Human Mutation · doi:10.1002/humu.20495 · Cited by 1,598 · cited 1×
“p53 is mutated in 50% of cancers, and the DNA-binding domain is the main carrier of oncogenic mutations (3).”
BackgroundHow p53 binds DNA as a tetramer
McLure, K. G., & Lee, P. W. K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.12.3342 · Cited by 260
Core domain interactions in full-length p53 in solution
Veprintsev, D. B., Freund, S. M. V., Andreeva, A., Rutledge, S. E., Tidow, H., Cañadillas, J. M. P., Blair, C. M., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0511130103 · Cited by 95
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Cited by
The p53 Pathway in Glioblastoma
Zhang, Y., Dube, C., Gibert, M., Cruickshanks, N., Wang, B., Coughlan, M., Yang, Y., Setiady, I., Deveau, C., Saoud, K., et al. (2018) · Cancers · doi:10.3390/cancers10090297 · Cited by 440
Pathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins
Natan, E., Endoh, T., Haim-Vilmovsky, L., Flock, T., Chalancon, G., Hopper, J. T. S., Kintses, B., Horvath, P., Daruka, L., Fekete, G., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0029-5 · Cited by 56
Krois, A. S., Park, S., Martinez-Yamout, M. A., Dyson, H. J., & Wright, P. E. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00528 · Cited by 14
Metadata
- Authors
- Rajagopalan, S., Huang, F., & Fersht, A. R.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2010-11-18
- Volume
- 39
- Issue
- 6
- Pages
- 2294-2303
- ISSN
- 0305-1048
- 1362-4962
- Cited by
- 112
- References
- 5
- Language
- en
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- CoChat. (2026). Citation check: Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53. https://app.cochat.ai/papers/10.1093/nar/gkq800
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- Rajagopalan, S., Huang, F., & Fersht, A. R. (2011). Single-Molecule characterization of oligomerization kinetics and equilibria of the tumor suppressor p53. Nucleic Acids Research. https://doi.org/10.1093/nar/gkq800
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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.
