The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
The p53 protein is an unusually shaped tetramer that binds directly to DNA.
Open accessAbstract
We have analyzed the size and structure of native immunopurified human p53 protein. By using a combination of chemical crosslinking, gel filtration chromatography, and zonal velocity gradient centrifugation, we have determined that the predominant form of p53 in such preparations is a tetramer. The behavior of purified p53 in gels and sucrose gradients implies that the protein has an extended shape. Wild-type p53 has been shown to bind specifically to sites in cellular and viral DNA. We show in this study by Southwestern ligand blotting and by analysis of DNA-bound crosslinked p53 that p53 monomers, dimers, and tetramers can bind directly to DNA.
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In the citing paper
“p53 regulates gene transcription through binding the response element (RE), which consists of two decameric half-site palindromes of the general form 5’-RRRCWWGYYY-3’ (R = A, G; W = A, T; Y = C, T) and is divided by 0–13 base pairs.32,33”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [32]
In the citing paper
“Some REs are cluster sites that have more than two half-sites.”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [291]
In the citing paper
“Most p53 target genes contain a consensus response element (RE) composed of two decametric half-sites of RRRCWWGYYY (R = A, G; W = A, T; Y = C, T) separated by 0–13 base pairs.289–292”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [291]
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Citations
Cites
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018
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
Wild-type p53 activates transcription in vitro
Farmer, G., Bargonetti, J., Zhu, H., Friedman, P., Prywes, R., & Prives, C. (1992) · Nature · doi:10.1038/358083a0 · Cited by 579
Shaulsky, G., Goldfinger, N., Ben-Ze'ev, A., & Rotter, V (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.12.6565 · Cited by 356
Cited by
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
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
Stommel, J. M., Marchenko, N. D., Jimenez, G. S., Moll, U. M., Hope, T. J., & Wahl, G. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.6.1660 · Cited by 738
MDM2 — master regulator of the p53 tumor suppressor protein
Momand, J., Wu, H.-H., & Dasgupta, G. (2000) · Gene · doi:10.1016/s0378-1119(99)00487-4 · Cited by 641
Mutational processes shape the landscape of TP53 mutations in human cancer
Giacomelli, A. O., Yang, X., Lintner, R. E., McFarland, J. M., Duby, M., Kim, J., Howard, T. P., Takeda, D. Y., Ly, S. H., Kim, E., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0204-y · Cited by 556
Metadata
- Authors
- Friedman, P. N., Chen, X., Bargonetti, J., & Prives, C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1993-04-15
- Volume
- 90
- Issue
- 8
- Pages
- 3319-3323
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032660991
- Cited by
- 264
- References
- 4
- FWCI
- 5.35
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: The p53 protein is an unusually shaped tetramer that binds directly to DNA. https://app.cochat.ai/papers/10.1073/pnas.90.8.3319
- The paper
- Friedman, P. N., Chen, X., Bargonetti, J., & Prives, C. (1993). The p53 protein is an unusually shaped tetramer that binds directly to DNA. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.90.8.3319
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.
