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Structure of the p53 Core Domain Dimer Bound to DNA
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“p53 binds to a full consensus DNA response element as a tetramer through a highly cooperative self-assembling mechanism (Fig. 7b).”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [297]
In the citing paper
“Two DBDs bind each decameric half-site as a symmetrical dimer (A-B), and two such dimers (A-B and C-D) constitute a tetramer on a full DNA response element via protein-protein and base stacking interactions.11,70,295–299”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [297]
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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
Definition 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
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
Research works printed but not linked: 39
- Vousden, 2002, Nat. Rev. Cancer, 2, 594, 10.1038/nrc864 · DOI · Paper page
- Weinberg, 2004, J. Mol. Biol., 341, 1145, 10.1016/j.jmb.2004.06.071 · DOI · Paper page
- Jeffrey, 1995, Science, 267, 1498, 10.1126/science.7878469 · DOI · Paper page
- Clore, 1995, Nat. Struct. Biol., 2, 321, 10.1038/nsb0495-321 · DOI
- Pavletich, 1993, Gene Dev., 7, 2556, 10.1101/gad.7.12b.2556 · DOI · Paper page
- Wang, 1993, Genes Dev., 7, 2575, 10.1101/gad.7.12b.2575 · DOI · Paper page
- Balagurumoorthy, 1995, Proc. Natl. Acad. Sci. U. S. A., 92, 8591, 10.1073/pnas.92.19.8591 · DOI
- Wang, 1995, Mol. Cell. Biol., 15, 2157, 10.1128/MCB.15.4.2157 · DOI
- Hupp, 1994, Curr. Biol., 4, 865, 10.1016/S0960-9822(00)00195-0 · DOI · Paper page
- Halazonetis, 1993, EMBO J., 12, 5057, 10.1002/j.1460-2075.1993.tb06199.x · DOI · Paper page
- Waterman, 1995, EMBO J., 14, 512, 10.1002/j.1460-2075.1995.tb07027.x · DOI
- Zhao, 2001, J. Biol. Chem., 276, 12120, 10.1074/jbc.M011644200 · DOI
- Pietenpol, 1994, P. Natl. Acad. Sci. U. S. A., 91, 1998, 10.1073/pnas.91.6.1998 · DOI · Paper page
- Rippin, 2002, J. Mol. Biol., 319, 351, 10.1016/S0022-2836(02)00326-1 · DOI · Paper page
- Nagaich, 1997, J. Biol. Chem., 272, 14830, 10.1074/jbc.272.23.14830 · DOI
- Ma, 2005, Proc. Natl. Acad. Sci. U. S. A., 102, 3988, 10.1073/pnas.0500215102 · DOI
- Lebrun, 2001, Protein Eng., 14, 233, 10.1093/protein/14.4.233 · DOI
- Klein, 2001, J. Biol. Chem., 276, 49020, 10.1074/jbc.M107516200 · DOI · Paper page
- Dehner, 2005, Angew. Chem. Int. Ed. Engl., 44, 5247, 10.1002/anie.200501887 · DOI
- Huang, 2000, Biol. Chem., 7, 355, 10.1016/S1074-5521(00)00113-7 · DOI
- Huang, 1998, Science, 282, 1669, 10.1126/science.282.5394.1669 · DOI · Paper page
- Xu, 1992, J. Org. Chem., 57, 3839, 10.1021/jo00040a024 · DOI
- MacMillan, 1991, Tetrahedron, 47, 2603, 10.1016/S0040-4020(01)81793-2 · DOI
- Macmillan, 1990, J. Org. Chem., 55, 5931, 10.1021/jo00311a005 · doi:10.1021/jo00311a005
- Vagin, 1997, J. Appl. Crystallogr., 30, 1022, 10.1107/S0021889897006766 · DOI · Paper page
- Otwinowski, 1997, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
- Brunger, 1998, Acta Crystallogr. Sect. D Biol. Crystallogr., 54, 905, 10.1107/S0907444998003254 · DOI · Paper page
- Emsley, 2004, Acta Crystallogr. Sect. D Biol. Crystallogr., 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- Jones, 1991, Acta Crystallogr. Sect. A, 47, 110, 10.1107/S0108767390010224 · DOI · Paper page
- Laskowski, 1993, J Appl. Crystallogr., 26, 283, 10.1107/S0021889892009944 · DOI · Paper page
- Lu, 2003, Nucleic Acids Res., 31, 5108, 10.1093/nar/gkg680 · DOI · Paper page
- Joerger, 2005, J. Biol. Chem., 280, 16030, 10.1074/jbc.M500179200 · DOI · Paper page
- Joerger, 2004, J. Biol. Chem., 279, 1291, 10.1074/jbc.M309732200 · DOI · Paper page
- Huyen, 2004, Structure (Camb.), 12, 1237, 10.1016/j.str.2004.05.007 · DOI
- Rainwater, 1995, Mol. Cell. Biol., 15, 3892, 10.1128/MCB.15.7.3892 · DOI · Paper page
- Yang, 1998, Mol. Cell, 2, 305, 10.1016/S1097-2765(00)80275-0 · DOI · Paper page
- Schmale, 1997, Oncogene, 15, 1363, 10.1038/sj.onc.1201500 · DOI · Paper page
- Klein, 2001, J. Biol. Chem., 276, 37390, 10.1074/jbc.M103801200 · DOI
- Nagaich, 1999, Proc. Natl. Acad. Sci. U. S. A., 96, 1875, 10.1073/pnas.96.5.1875 · DOI
Cited by
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
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
Principles of Protein−Protein Interactions: What are the Preferred Ways For Proteins To Interact?
Keskin, O., Gursoy, A., Ma, B., & Nussinov, R. (2008) · Chemical Reviews · doi:10.1021/cr040409x · Cited by 697
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
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
Metadata
- Authors
- Ho, W. C., Fitzgerald, M. X., & Marmorstein, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-07
- Volume
- 281
- Issue
- 29
- Pages
- 20494-20502
- ISSN
- 0021-9258
- Cited by
- 118
- References
- 3
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- creativecommons.org/licenses/by/4.0/ (vor, 5213 d)
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- The paper
- Ho, W. C., Fitzgerald, M. X., & Marmorstein, R. (2006). Structure of the p53 Core Domain Dimer Bound to DNA. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m603634200
Data sources
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.
