The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer
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In the citing paper
“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 [298]
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 [298]
In the citing paper
“Zn2+ can help stabilize the interaction between p53 and DNA by tetrahedral coordination with the imidazole group of H179 and the thiol groups of Cys238, Cys242 and Cys176298”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [298]
In the citing paper
“Zn2+ is crucial for DNA recognition by p53.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [298]
In the citing paper
“Cys176, Cys238 and Cys242 are relatively unlikely to be modified, as they involve the coordination of a zinc atom.298”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [298]
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Citations
Cites
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · cited 1×
“p53 is essential for the prevention of cancer development; its function is inactivated by mutations and signal-dependent modifications in a majority of human cancers (Horn and Vousden, 2007; Vogelstein et al., 2000).”
PHENIX : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361
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
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 7×
“The overall structure of the core tetramer:DNA complex is similar to that described in various modeling analyses (Cho et al., 1994; Ho et al., 2006; McLure and Lee, 1998; Pan and Nussinov , 2007) .”
InfluentialDefinition 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 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
Cytoplasmic functions of the tumour suppressor p53
Green, D. R., & Kroemer, G. (2009) · Nature · doi:10.1038/nature07986 · Cited by 1,106
p53 isoforms can regulate p53 transcriptional activity
Bourdon, J.-C., Fernandes, K., Murray-Zmijewski, F., Liu, G., Diot, A., Xirodimas, D. P., Saville, M. K., & Lane, D. P. (2005) · Genes & Development · doi:10.1101/gad.1339905 · Cited by 810
Acetylation of the p53 DNA-binding domain regulates apoptosis induction.
Sykes, S. M., Mellert, H. S., Holbert, M. A., Li, K., Marmorstein, R., Lane, W. S., & McMahon, S. B. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.11.026 · Cited by 752
Research works printed but not linked: 29
- Balagurumoorthy, 1995, Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA, Proc. Natl. Acad. Sci. USA, 92, 8591, 10.1073/pnas.92.19.8591 · DOI
- Brunger, 1998, Crystallography & NMR system: A new software suite for macromolecular structure determination, Acta Crystallogr. D Biol. Crystallogr., 54, 905, 10.1107/S0907444998003254 · DOI · Paper page
- 1994, The CCP4 suite: programs for protein crystallography, Acta Crystallogr. D Biol. Crystallogr., 50, 760, 10.1107/S0907444994003112 · DOI · Paper page
- Chen, 1999, Combinatorial gene regulation by eukaryotic transcription factors, Curr. Opin. Struct. Biol., 9, 48, 10.1016/S0959-440X(99)80007-4 · DOI
- Funk, 1992, A transcriptionally active DNA-binding site for human p53 protein complexes, Mol. Cell. Biol., 12, 2866, 10.1128/MCB.12.6.2866 · DOI · Paper page
- Ho, 2006, Structure of the p53 core domain dimer bound to DNA, J. Biol. Chem., 281, 20494, 10.1074/jbc.M603634200 · DOI · Paper page
- Joerger, 2008, Structural biology of the tumor suppressor p53, Annu. Rev. Biochem., 77, 557, 10.1146/annurev.biochem.77.060806.091238 · DOI · Paper page
- Jones, 1991, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr. A, 47, 110, 10.1107/S0108767390010224 · DOI · Paper page
- Kitayner, 2006, Structural basis of DNA recognition by p53 tetramers, Mol. Cell, 22, 741, 10.1016/j.molcel.2006.05.015 · DOI · Paper page
- Klein, 2001, NMR spectroscopy reveals the solution dimerization interface of p53 core domains bound to their consensus DNA, J. Biol. Chem., 276, 49020, 10.1074/jbc.M107516200 · DOI · Paper page
- Lilyestrom, 2006, Crystal structure of SV40 large T-antigen bound to p53: interplay between a viral oncoprotein and a cellular tumor suppressor, Genes Dev., 20, 2373, 10.1101/gad.1456306 · DOI · Paper page
- Lu, 2003, 3DNA: a software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures, Nucleic Acids Res., 31, 5108, 10.1093/nar/gkg680 · DOI · Paper page
- Ma, 2005, Comparison of the protein-protein interfaces in the p53-DNA crystal structures: towards elucidation of the biological interface, Proc. Natl. Acad. Sci. USA, 102, 3988, 10.1073/pnas.0500215102 · DOI
- Ma, 2007, Sequence analysis of p53 response-elements suggests multiple binding modes of the p53 tetramer to DNA targets, Nucleic Acids Res., 35, 2986, 10.1093/nar/gkm192 · DOI
- Malecka, 2009, Crystal structure of a p53 core tetramer bound to DNA, Oncogene, 28, 325, 10.1038/onc.2008.400 · DOI
- Nagaich, 1999, p53-induced DNA bending and twisting: p53 tetramer binds on the outer side of a DNA loop and increases DNA twisting, Proc. Natl. Acad. Sci. USA, 96, 1875, 10.1073/pnas.96.5.1875 · DOI
- Olson, 2001, A standard reference frame for the description of nucleic acid base-pair geometry, J. Mol. Biol., 313, 229, 10.1006/jmbi.2001.4987 · DOI · Paper page
- Otwinowski, 1997, Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol., 276, 307, 10.1016/S0076-6879(97)76066-X · DOI · Paper page
- Pan, 2007, Structural basis for p53 binding-induced DNA bending, J. Biol. Chem., 282, 691, 10.1074/jbc.M605908200 · DOI
- Pan, 2008, p53-Induced DNA bending: the interplay between p53-DNA and p53-p53 interactions, J. Phys. Chem. B, 112, 6716, 10.1021/jp800680w · DOI
- Rippin, 2002, Recognition of DNA by p53 core domain and location of intermolecular contacts of cooperative binding, J. Mol. Biol., 319, 351, 10.1016/S0022-2836(02)00326-1 · DOI · Paper page
- Smeenk, 2008, Characterization of genome-wide p53-binding sites upon stress response, Nucleic Acids Res., 36, 3639, 10.1093/nar/gkn232 · DOI · Paper page
- Suzuki, 2009, Modulation of microRNA processing by p53, Nature, 460, 529, 10.1038/nature08199 · DOI · Paper page
- Tang, 2006, Tip60-dependent acetylation of p53 modulates the decision between cell-cycle arrest and apoptosis, Mol. Cell, 24, 827, 10.1016/j.molcel.2006.11.021 · DOI · Paper page
- Tidow, 2007, Quaternary structures of tumor suppressor p53 and a specific p53 DNA complex, Proc. Natl. Acad. Sci. USA, 104, 12324, 10.1073/pnas.0705069104 · DOI · Paper page
- Weinberg, 2004, Cooperative binding of tetrameric p53 to DNA, J. Mol. Biol., 341, 1145, 10.1016/j.jmb.2004.06.071 · DOI · Paper page
- Wu, 2006, FOXP3 controls regulatory T cell function through cooperation with NFAT, Cell, 126, 375, 10.1016/j.cell.2006.05.042 · DOI · Paper page
- Zhao, 2001, Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution, J. Biol. Chem., 276, 12120, 10.1074/jbc.M011644200 · DOI
- Zupnick, 2006, Mutational analysis of the p53 core domain L1 loop, J. Biol. Chem., 281, 20464, 10.1074/jbc.M603387200 · DOI
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
Self-citationPathological Unfoldomics of Uncontrolled Chaos: Intrinsically Disordered Proteins and Human Diseases
Uversky, V. N., Davé, V., Iakoucheva, L. M., Malaney, P., Metallo, S. J., Pathak, R. R., & Joerger, A. C. (2014) · Chemical Reviews · doi:10.1021/cr400713r · Cited by 288
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
Extensive Post-translational Modification of Active and Inactivated Forms of Endogenous p53
DeHart, C. J., Chahal, J. S., Flint, S. J., & Perlman, D. H. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.030254 · Cited by 70
Terakawa, T., Higo, J., & Takada, S. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.026 · Cited by 32
Metadata
- Authors
- Chen, Y., Dey, R., & Chen, L.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 18
- Issue
- 2
- Pages
- 246-256
- ISSN
- 0969-2126
- Cited by
- 150
- References
- 13
- Language
- en
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1293 d)
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- Chen, Y., Dey, R., & Chen, L. (2010). Crystal Structure of the p53 Core Domain Bound to a Full Consensus Site as a Self-Assembled Tetramer. Structure. https://doi.org/10.1016/j.str.2009.11.011
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