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Unfolding, Aggregation, and Amyloid Formation by the Tetramerization Domain from Mutant p53 Associated with Lung Cancer
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“The G334V mutant contributed to a beta-dominated structural transition leading to amyloid formation at physiological temperature.317”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [317]
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Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
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- Abbreviations CD, circular dichroism
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
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
- Higashimoto, Y., Asanomi, Y., Takakusagi, S., Lewis, M. S., Uosaki, K., Durell, S. R., Anderson, C. W., Appella, E., & Sakaguchi, K.
- Affiliations
- Department of Medical Biochemistry, Kurume University School of Medicine, Kurume 830-0011, Japan, and Biological Chemistry and Physical Chemistry, Division of Chemistry, Graduate School of Science, Hokkaido University, Sapporo 060-0810, Japan, Molecular Interactions Resource, Division of Bioengineering and Physical Science, Office of Research Services, Office of Director, and Center for Cancer Research Nanobiology Program, National Institutes of Health, Bethesda, Maryland 20892, Biology Department,...
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2006-01-24
- Volume
- 45
- Issue
- 6
- Pages
- 1608-1619
- ISSN
- 0006-2960
- 1520-4995
- Cited by
- 75
- References
- 3
- Language
- en
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