The DOI matches its Crossref record; 63 of the 63 references it cites were found in a registry or an index.
Understanding the complexity of p53 in a new era of tumor suppression
Open accessAbstract
SUMMARY p53 was discovered 45 years ago as a SV40 large T antigen binding protein, coded by the most frequently mutated TP53 gene in human cancers. As a transcription factor, p53 is tightly regulated by a rich network of post-translational modifications to execute its diverse functions in tumor suppression. Although early studies established p53-mediated cell-cycle arrest, apoptosis, and senescence as the classic barriers in cancer development, a growing number of new functions of p53 have been discovered and the scope of p53-mediated anti-tumor activity is largely expanded. Here, we review the complexity of different layers of p53 regulation, and the recent advance of the p53 pathway in metabolism, ferroptosis, immunity, and others that contribute to tumor suppression. We also discuss the challenge regarding how to activate p53 function specifically effective in inhibiting tumor growth without harming normal homeostasis for cancer therapy.
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In the citing paper
“The transcription factor activity of p53 modulates the expression of specific genes involved in the following processes: apoptosis, cell cycle arrest, metabolism, senescence, ferroptosis, and autophagy.1,2”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [2]
In the citing paper
“The p53 protein, encoded by the TP53 gene, is expressed in almost all human tissues and plays a pivotal role in cancer suppression as a tumor suppressor.”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [2]
In the citing paper
“The p53 protein, encoded by the TP53 gene, not only binds to many targeted genes but also regulates apoptosis, autophagy, cell cycle arrest, metabolism, senescence and the tumor immune microenvironment to suppress tumorigenesis.”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [2]
In the citing paper
“The p53 protein is a transcription factor comprising five domains: a transactivation domain divided into two regions responsible for activating the transcription of multiple genes, a proline‐rich domain (PRD) involved in the regulation of apoptosis, a 200‐amino‐acid‐residue DNA‐binding domain (DBD), a tetramerization domain (TET) that enables the oligomerization of the p53 monomers, and a negative”
From The TP53 tumor suppressor gene: From molecular biology to clinical investigations (2025) · cites this paper as [26]
In the citing paper
“In these normal conditions, p53 mainly exists as a cytoplasmic dimer with low DNA binding efficiency [26, 27].”
From The TP53 tumor suppressor gene: From molecular biology to clinical investigations (2025) · cites this paper as [26]
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Citations
Cites
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In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
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Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398
Self-citationBlinded 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
p53 is required for radiation-induced apoptosis in mouse thymocytes
Lowe, S. W., Schmitt, E. M., Smith, S. W., Osborne, B. A., & Jacks, T. (1993) · Nature · doi:10.1038/362847a0 · Cited by 2,864
Senescence and tumour clearance is triggered by p53 restoration in murine liver carcinomas
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Senescence of Activated Stellate Cells Limits Liver Fibrosis
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Cited by
Hepatocellular carcinoma: signaling pathways and therapeutic advances
Zheng, J., Wang, S., Xia, L., Sun, Z., Chan, K. M., Bernards, R., Qin, W., Chen, J., Xia, Q., & Jin, H. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02075-w · Cited by 341
The TP53 tumor suppressor gene: From molecular biology to clinical investigations
Baliakas, P., & Soussi, T. (2025) · Journal of Internal Medicine · doi:10.1111/joim.20106 · Cited by 50
p53: from understanding its structure to advances in therapeutic targeting
Wang, W., Liu, X., Liu, H., Abolhassani, H., Yan, H., Zhang, H., & Wang, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02549-5 · Cited by 30
Research progress on interferon and cellular senescence
Wang, D., Chen, K., Wang, Z., Wu, H., & Li, Y. (2024) · The FASEB Journal · doi:10.1096/fj.202400808rr · Cited by 23
Gao, E., Wang, Z., Zhao, S., Zhu, X., Xu, S., Xu, Y., Wang, Y., Xu, N., & Tao, B. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.154878 · Cited by 18
Metadata
- Authors
- Liu, Y., Su, Z., Tavana, O., & Gu, W.
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2024-06
- Volume
- 42
- Issue
- 6
- Pages
- 946-967
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W4396769373
- Cited by
- 495
- References
- 63
- FWCI
- 75.81
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
