The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Structural Biology of the Tumor Suppressor p53
Abstract
The tumor suppressor protein p53 induces or represses the expression of a variety of target genes involved in cell cycle control, senescence, and apoptosis in response to oncogenic or other cellular stress signals. It exerts its function as guardian of the genome through an intricate interplay of independently folded and intrinsically disordered functional domains. In this review, we provide insights into the structural complexity of p53, the molecular mechanisms of its inactivation in cancer, and therapeutic strategies for the pharmacological rescue of p53 function in tumors. p53 emerges as a paradigm for a more general understanding of the structural organization of modular proteins and the effects of disease-causing mutations.
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“All three of the C-terminal regions are essential for p53 function, with the NLS region driving nuclear import.9-11, the TET domain regulating oligomeric state,12-14 and the CTD functioning in a multitude of roles.3,15”
From Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR (2022) · cites this paper as [3]
In the citing paper
“The TADs are followed by a PRD (AA residues 62–94) that includes five PXXP (P: proline; X: any AA) motifs.15 This region plays a critical role in promoting cell cycle arrest and p53-associated death.24,25”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [15]
In the citing paper
“Thus, the interaction with p300 prevents the MDM2-mediated proteasomal degradation of p53. In contrast, binding to negative regulators (MDM2/4) inhibits the interaction of p300 with components of the transcription machinery.”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [15]
In the citing paper
“The TAD is a disordered binding region for a larger cohort of interacting proteins, including molecules involved in the transcriptional machinery, the negative regulators MDM2/4, and the transcriptional coactivators p300/CREB-binding protein (CBP).15,18,19”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [15]
In the citing paper
“In its active conformation, the p53 protein is a tetramer formed by four identical chains of 393 residues each (Joerger and Fersht 2008).”
From Structural Evolution and Dynamics of the p53 Proteins (2017) · cites this paper as Joerger and Fersht 2008
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Cites
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In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
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
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206
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
Restoration of p53 function leads to tumour regression in vivo
Ventura, A., Kirsch, D. G., McLaughlin, M. E., Tuveson, D. A., Grimm, J., Lintault, L., Newman, J., Reczek, E. E., Weissleder, R., & Jacks, T. (2007) · Nature · doi:10.1038/nature05541 · Cited by 1,820
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Goodman, R. H., & Smolik, S. (2000) · Genes & Development · doi:10.1101/gad.14.13.1553 · Cited by 1,778
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Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
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Mutant p53 in Cancer: New Functions and Therapeutic Opportunities
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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
Function and structure of inherently disordered proteins
Dunker, A. K., Silman, I., Uversky, V. N., & Sussman, J. L. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.002 · Cited by 963
Awakening guardian angels: drugging the p53 pathway
Brown, C. J., Lain, S., Verma, C. S., Fersht, A. R., & Lane, D. P. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2763 · Cited by 881
Self-citationThe role of p53 in cancer drug resistance and targeted chemotherapy
Hientz, K., Mohr, A., Bhakta-Guha, D., & Efferth, T. (2017) · Oncotarget · doi:10.18632/oncotarget.13475 · Cited by 587
Metadata
- Authors
- Joerger, A. C., & Fersht, A. R.
- Venue
- Annual Review of Biochemistry
- Publisher
- Annual Reviews
- Published
- 2008-06-01
- Volume
- 77
- Issue
- 1
- Pages
- 557-582
- ISSN
- 0066-4154 (ISSN-L)
- 1545-4509
- OpenAlex
- W2166269098
- Cited by
- 693
- References
- 26
- FWCI
- 2.54
- Type
- journal article
- Language
- en
- Open access
- closed
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