The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Crystal Structure of a Superstable Mutant of Human p53 Core Domain
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In the citing paper
“R282 plays a role in stabilizing the DNA-binding Loop-Sheet-Helix motif but does not directly contact the DNA (PDBs:1UOL, 1TUP) 16, 17.”
From Combined Point Mutation in a Single Allele of the TP53 Gene Potentiates the Oncogenic and Transcriptional Properties of TP53 in Lung Cancer (2026) · cites this paper as [16]
In the citing paper
“All experiments used a quadruple mutant flp53 that contains stabilizing mutations in the core that do not perturb the structure or impair activity (6).”
From Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain (2008) · cites this paper as [6]
In the citing paper
“Crystal structures show that the second-site suppressor mutations usually cause only small local structural changes, whereas do not alter the overall structure of the p53 protein.534,536,545,546”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [534]
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 [534]
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 [534]
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Citations
Cites
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
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
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
14-3-3σ is required to prevent mitotic catastrophe after DNA damage
Chan, T. A., Hermeking, H., Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1999) · Nature · doi:10.1038/44188 · Cited by 895
Hot-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-citation
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Cited by
Flexible nets: The roles of intrinsic disorder in protein interaction networks
Dunker, A. K., Cortese, M. S., Romero, P., Iakoucheva, L. M., & Uversky, V. N. (2005) · The FEBS Journal · doi:10.1111/j.1742-4658.2005.04948.x · Cited by 1,122
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
Structure of tumor suppressor p53 and its intrinsically disordered N-terminal transactivation domain
Wells, M., Tidow, H., Rutherford, T. J., Markwick, P., Jensen, M. R., Mylonas, E., Svergun, D. I., Blackledge, M., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801353105 · Cited by 434
Self-citationStructural 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-citationReactivation of mutant p53: molecular mechanisms and therapeutic potential
Selivanova, G., & Wiman, K. G. (2007) · Oncogene · doi:10.1038/sj.onc.1210295 · Cited by 186
Metadata
- Authors
- Joerger, A. C., Allen, M. D., & Fersht, A. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-01
- Volume
- 279
- Issue
- 2
- Pages
- 1291-1296
- ISSN
- 0021-9258
- Cited by
- 163
- References
- 5
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 6145 d)
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- CoChat. (2026). Citation check: Crystal Structure of a Superstable Mutant of Human p53 Core Domain. https://app.cochat.ai/papers/10.1074/jbc.m309732200
- The paper
- Joerger, A. C., Allen, M. D., & Fersht, A. R. (2004). Crystal Structure of a Superstable Mutant of Human p53 Core Domain. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m309732200
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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.
