The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations
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“Second site suppressor mutations could help correct the conformation of mutant p53, improve the stability of p53-DNA binding, and provide a theoretical basis for the reactivation of mutant p53 (Table 4).531–545”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [531]
In the citing paper
“Second site suppressor mutations could help correct the conformation of mutant p53, improve the stability of p53-DNA binding, and provide a theoretical basis for the reactivation of mutant p53 (Table 4).531–545”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [531]
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Citations
Cites
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 · cited 13×
“co-ordinates were used to display only chain B of p53 (amino acids 94–312) in a complex with the DNA double helix (Cho et al., 1994).”
BackgroundMethodInfluentialHot-spot mutants of p53 core domain evince characteristic local structural changes
Wong, K.-B., DeDecker, B. S., Freund, S. M. V., Proctor, M. R., Bycroft, M., & Fersht, A. R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.15.8438 · Cited by 221
Self-citationStructural Aspects of the p53 Protein in Relation to Gene Evolution: A Second Look
Soussi, T., & May, P. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0425 · Cited by 208
Walker, D. R., Bond, J. P., Tarone, R. E., Harris, C. C., Makalowski, W., Boguski, M. S., & Greenblatt, M. S. (1999) · Oncogene · doi:10.1038/sj.onc.1202298 · Cited by 198
Research works printed but not linked: 28
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Cited by
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
mCSM: Predicting the effects of mutations in proteins using graph-based signatures
Pires, D. E. V., Ascher, D. B., & Blundell, T. L. (2014) · Bioinformatics · doi:10.1093/bioinformatics/btt691 · Cited by 1,066
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
Targeting mutant p53 for efficient cancer therapy
Bykov, V. J. N., Eriksson, S. E., Bianchi, J., & Wiman, K. G. (2018) · Nature Reviews Cancer · doi:10.1038/nrc.2017.109 · Cited by 889
Structural basis for understanding oncogenic p53 mutations and designing rescue drugs
Joerger, A. C., Ang, H. C., & Fersht, A. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607286103 · Cited by 353
Self-citation
Metadata
- Authors
- Nikolova, P. V., Wong, K., DeDecker, B., Henckel, J., & Fersht, A. R.
- Venue
- The EMBO Journal
- Published
- 2000-02-01
- Volume
- 19
- Issue
- 3
- Pages
- 370-378
- ISSN
- 0261-4189
- 1460-2075
- Cited by
- 152
- References
- 4
- Language
- en
- Licence
- www.springer.com/tdm (tdm)
- www.springer.com/tdm (vor)
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- Nikolova, P. V., Wong, K., DeDecker, B., Henckel, J., & Fersht, A. R. (2000). Mechanism of rescue of common p53 cancer mutations by second‐site suppressor mutations. The EMBO Journal. https://doi.org/10.1093/emboj/19.3.370
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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.
