The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions
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“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 [536]
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 [536]
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 [536]
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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
TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier, M., Hollstein, M., & Hainaut, P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001008 · Cited by 2,199 · cited 1×
“The majority of tumor-related p53 mutations, particularly those defined as mutational ‘hotspots’, occur within the DNA-binding core domain of p53 (10).”
BackgroundDefinition of a consensus binding site for p53
El-Deiry, W. S., Kern, S. E., Pietenpol, J. A., Kinzler, K. W., & Vogelstein, B. (1992) · Nature Genetics · doi:10.1038/ng0492-45 · Cited by 1,985
The p53 pathway: positive and negative feedback loops
Harris, S. L., & Levine, A. J. (2005) · Oncogene · doi:10.1038/sj.onc.1208615 · Cited by 1,967
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×
“Mutations in the p53 gene that lead to inactivation of the protein are observed in 50% of human cancers (8,9).”
BackgroundThe IARC TP53 database: new online mutation analysis and recommendations to users
Olivier, M., Eeles, R., Hollstein, M., Khan, M. A., Harris, C. C., & Hainaut, P. (2002) · Human Mutation · doi:10.1002/humu.10081 · Cited by 1,248
A Global Map of p53 Transcription-Factor Binding Sites in the Human Genome
Wei, C.-L., Wu, Q., Vega, V. B., Chiu, K. P., Ng, P., Zhang, T., Shahab, A., Yong, H. C., Fu, Y., Weng, Z., et al. (2006) · Cell · doi:10.1016/j.cell.2005.10.043 · Cited by 1,141
The role of DNA shape in protein–DNA recognition
Rohs, R., West, S. M., Sosinsky, A., Liu, P., Mann, R. S., & Honig, B. (2009) · Nature · doi:10.1038/nature08473 · Cited by 1,096
Self-citationTranscriptional Regulation by P53
Beckerman, R., & Prives, C. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000935 · Cited by 569
Research works printed but not linked: 30
- Vogelstein, 2000, Nature; Physical Science (London), 408, 307, 10.1038/35042675 · DOI · Paper page
- Oren, 2003, Cell death and differentiation, 10, 431, 10.1038/sj.cdd.4401183 · DOI · Paper page
- Funk, 1992, Molecular and Cellular Biology, 12, 2866, 10.1128/MCB.12.6.2866 · DOI · Paper page
- Joerger, 2007, Advances in cancer research, 97, 1, 10.1016/S0065-230X(06)97001-8 · DOI · Paper page
- Kitayner, 2006, Molecular cell, 22, 741, 10.1016/j.molcel.2006.05.015 · DOI · Paper page
- Malecka, 2009, Oncogene, 28, 325, 10.1038/onc.2008.400 · DOI
- Chen, 2010, Structure (London), 18, 246, 10.1016/j.str.2009.11.011 · DOI · Paper page
- Kitayner, 2010, Nature structural & molecular biology, 17, 423, 10.1038/nsmb.1800 · DOI · Paper page
- 2011, The EMBO Journal, 30, 2167, 10.1038/emboj.2011.127 · DOI · Paper page
- Bullock, 2001, Nature reviews. Cancer, 1, 68, 10.1038/35094077 · DOI · Paper page
- Wieczorek, 1996, Nature medicine, 2, 1143, 10.1038/nm1096-1143 · DOI
- 2004, PNAS, 101, 4930, 10.1073/pnas.0401162101 · DOI
- 2006, PNAS, 103, 15056, 10.1073/pnas.0607286103 · DOI · Paper page
- Otsuka, 2007, International journal of cancer. Journal international du cancer, 121, 559, 10.1002/ijc.22724 · DOI · Paper page
- Suad, 2009, Journal of molecular biology, 385, 249, 10.1016/j.jmb.2008.10.063 · DOI · Paper page
- Bourenkov, 2006, Acta Crystallographica, Section D: Biological Crystallography, 62, 58, 10.1107/S0907444905033998 · DOI
- 1997, Methods in enzymology, 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
- Adams, 2010, Acta Crystallographica, Section D: Biological Crystallography, 66, 213, 10.1107/S0907444909052925 · DOI · Paper page
- Wang, 2007, Acta Crystallographica, Section D: Biological Crystallography, 63, 276, 10.1107/S0907444906048499 · DOI
- Collaborative Computational Project Number, 1994, Acta Crystallographica, Section D: Biological Crystallography, 50, 760, 10.1107/S0907444994003112 · DOI · Paper page
- McCoy, 2007, Journal of Applied Crystallography, 40, 658, 10.1107/S0021889807021206 · DOI · Paper page
- Emsley, 2004, Acta Crystallographica, Section D: Biological Crystallography, 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- 1993, Journal of Applied Crystallography, 26, 283, 10.1107/S0021889892009944 · DOI · Paper page
- Lavery, 1989, Journal of biomolecular structure & dynamics, 6, 655, 10.1080/07391102.1989.10507728 · DOI · Paper page
- Rocchia, 2002, Journal of computational chemistry, 23, 128, 10.1002/jcc.1161 · DOI · Paper page
- 2005, Journal of Biological Chemistry, 280, 16030, 10.1074/jbc.M500179200 · DOI · Paper page
- 2007, 46, 2630, 10.1021/bi062106y · DOI
- Loh, 2010, 2, 442, 10.1039/c003915b · DOI
- Joerger, 2007, Oncogene, 26, 2226, 10.1038/sj.onc.1210291 · DOI · Paper page
- Wiman, 2010, Oncogene, 29, 4245, 10.1038/onc.2010.188 · DOI · Paper page
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
Targeting Therapies for the p53 Protein in Cancer Treatments
Levine, A. J. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055455 · Cited by 84
Degtjarik, O., Golovenko, D., Diskin-Posner, Y., Abrahmsén, L., Rozenberg, H., & Shakked, Z. (2021) · Nature Communications · doi:10.1038/s41467-021-27142-6 · Cited by 78
Self-citationLow, L., Goh, A., Koh, J., Lim, S., & Wang, C.-I. (2019) · Nature Communications · doi:10.1038/s41467-019-13305-z · Cited by 48
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
- Eldar, A., Rozenberg, H., Diskin-Posner, Y., Rohs, R., & Shakked, Z.
- Venue
- Nucleic Acids Research
- Publisher
- Oxford University Press (OUP)
- Published
- 2013-07-17
- Volume
- 41
- Issue
- 18
- Pages
- 8748-8759
- ISSN
- 0305-1048
- 1362-4962
- Cited by
- 72
- References
- 9
- Language
- en
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- CoChat. (2026). Citation check: Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions. https://app.cochat.ai/papers/10.1093/nar/gkt630
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- Eldar, A., Rozenberg, H., Diskin-Posner, Y., Rohs, R., & Shakked, Z. (2013). Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions. Nucleic Acids Research. https://doi.org/10.1093/nar/gkt630
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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.
