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Repurposing antiparasitic antimonials to noncovalently rescue temperature-sensitive p53 mutations
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In the citing paper
“Potassium antimony tartrate (PAT) was identified as binding to the p53 V272M mutant (Kd = 9.09 μM) in a non-covalent manner, increasing its thermostability by 3.6 °C and remarkably restoring protein folding and transcriptional activity.432”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [432]
In the citing paper
“Further testing identified 65 of p53 mutants that could be rescued by PAT, but all were non-hotspot mutations.432”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [432]
In the citing paper
“PAT and ATO bind to mutant p53 at similar sites (Fig. 9d), but differ in two aspects, with PAT non-covalently binding mutant p53 and preferentially rescuing temperature-sensitive mutants (a subtype of structural mutants), whereas ATO covalently binding mutant p53 and apparently rescuing more structural p53 mutants.432”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [432]
In the citing paper
“PAT exhibited specific p53 V272M antitumor activity in both cellular and xenograft mouse models.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [432]
In the citing paper
“Complex structures show that MQ can bind to six of the ten cysteines,425 while ATO431 and PAT432 bind at a pocket formed by Cys124, Cys135, Cys141 and Met133.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [432]
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Drug repurposing: progress, challenges and recommendations
Pushpakom, S., Iorio, F., Eyers, P. A., Escott, K. J., Hopper, S., Wells, A., Doig, A., Guilliams, T., Latimer, J., McNamee, C., et al. (2019) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.168 · Cited by 4,718
The single-cell transcriptional landscape of mammalian organogenesis
Cao, J., Spielmann, M., Qiu, X., Huang, X., Ibrahim, D. M., Hill, A. J., Zhang, F., Mundlos, S., Christiansen, L., Steemers, F. J., et al. (2019) · Nature · doi:10.1038/s41586-019-0969-x · Cited by 4,490
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551
Hoadley, K. A., Yau, C., Hinoue, T., Wolf, D. M., Lazar, A. J., Drill, E., Shen, R., Taylor, A. M., Cherniack, A. D., Thorsson, V., et al. (2018) · Cell · doi:10.1016/j.cell.2018.03.022 · Cited by 2,546
Self-citationMutant p53 in Cancer: New Functions and Therapeutic Opportunities
Muller, P. A. J., & Vousden, K. H. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.01.021 · Cited by 1,545
Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067
Drugging the ‘undruggable’ cancer targets
Dang, C. V., Reddy, E. P., Shokat, K. M., & Soucek, L. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2017.36 · Cited by 927
A 17-gene stemness score for rapid determination of risk in acute leukaemia
Ng, S. W. K., Mitchell, A., Kennedy, J. A., Chen, W. C., McLeod, J., Ibrahimova, N., Arruda, A., Popescu, A., Gupta, V., Schimmer, A. D., et al. (2016) · Nature · doi:10.1038/nature20598 · Cited by 912
PRIMA-1 reactivates mutant p53 by covalent binding to the core domain
Lambert, J. M. R., Gorzov, P., Veprintsev, D. B., Söderqvist, M., Segerbäck, D., Bergman, J., Fersht, A. R., Hainaut, P., Wiman, K. G., & Bykov, V. J. N. (2009) · Cancer Cell · doi:10.1016/j.ccr.2009.03.003 · Cited by 592
Targeted Covalent Inhibitors for Drug Design
Baillie, T. A. (2016) · Angewandte Chemie International Edition · doi:10.1002/anie.201601091 · Cited by 578
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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
Small-molecule correctors and stabilizers to target p53
Fallatah, M. M. J., Law, F. V., Chow, W. A., & Kaiser, P. (2023) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2023.02.007 · Cited by 44
Metadata
- Authors
- Tang, Y., Song, H., Wang, Z., Xiao, S., Xiang, X., Zhan, H., Wu, L., Wu, J., Xing, Y., Tan, Y., Liang, Y., Yan, N., Li, Y., Li, J., Wu, J., Zheng, D., Jia, Y., Chen, Z., Li, Y., Zhang, Q., Zhang, J., Zeng, H., Tao, W., Liu, F., Wu, Y., & Lu, M.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2022-04
- Volume
- 39
- Issue
- 2
- Pages
- 110622
- ISSN
- 2211-1247
- Cited by
- 37
- References
- 19
- Language
- en
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- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by-nc-nd/4.0/ (vor)
- Funders
- National Key Research and Development Program of China (2017YFA0506200)
- Science and Technology Commission of Shanghai Municipality (21S11900100)
- Shanghai Jiao Tong University (20210104)
- National Natural Science Foundation of China (81900157, 82073292, 82102756, 82130075)
- Shanghai Municipal Education Commission (21SG18)
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- Tang, Y., Song, H., Wang, Z., Xiao, S., Xiang, X., Zhan, H., Wu, L., Wu, J., Xing, Y., Tan, Y., Liang, Y., Yan, N., Li, Y., Li, J., Wu, J., Zheng, D., Jia, Y., Chen, Z., Li, Y., . . . Lu, M. (2022). Repurposing antiparasitic antimonials to noncovalently rescue temperature-sensitive p53 mutations. Cell Reports. https://doi.org/10.1016/j.celrep.2022.110622
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