The DOI matches its Crossref record; 141 of the 141 references it cites were found in a registry or an index.
Structural Aspects of the p53 Protein in Relation to Gene Evolution: A Second Look
Abstract
Several years ago, a comparison of the amino acid sequences of p53 proteins from a variety of species enabled us to reveal structural features of this protein, giving clues to its function. Since then, numerous studies on the biochemical, immunological and biological functions of p53 as well as on its structure (including crystallography data) have provided considerable insight into the multifunctional aspects of p53. The purpose of this review is to present the most recent data concerning the various structural features of the p53 protein with special emphasis on its flexibility, which plays a key role in regulation of its biological activity.
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Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321
Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
Toshiyuki, M., & Reed, J. C. (1995) · Cell · doi:10.1016/0092-8674(95)90412-3 · Cited by 4,063
Participation of p53 protein in the cellular response to DNA damage.
Kastan, M. B., Onyekwere, O. C., Sidransky, D., Vogelstein, B., & Craig, R. W. (1991) · PubMed · Cited by 3,761
Mutations in the p53 tumor suppressor gene: clues to cancer etiology and molecular pathogenesis.
Greenblatt, M. S., Bennett, W. P., Hollstein, M., & Harris, C. C. (1994) · PubMed · Cited by 3,463
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 4×
“This hypothesis has been confirmed by crystallographic data (Cho et al., 1994).”
BackgroundInfluentialDefinition 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 p53-mdm-2 autoregulatory feedback loop.
Wu, X., Bayle, J. H., Olson, D., & Levine, A. J. (1993) · Genes & Development · doi:10.1101/gad.7.7a.1126 · Cited by 1,801
Oncoprotein MDM2 conceals the activation domain of tumour suppressor p53
Oliner, J. D., Pietenpol, J. A., Thiagalingam, S., Gyuris, J., Kinzler, K. W., & Vogelstein, B. (1993) · Nature · doi:10.1038/362857a0 · Cited by 1,451
Finlay, C. A., Hinds, P. W., Tan, T. H., Eliyahu, D., Oren, M., & Levine, A. J. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.2.531 · Cited by 1,144
The structure and function of proline-rich regions in proteins
Williamson, M. P. (1994) · Biochemical Journal · doi:10.1042/bj2970249 · Cited by 1,005
Cited by
p53 and Human Cancer: The First Ten Thousand Mutations
(1999) · Advances in Cancer Research · doi:10.1016/s0065-230x(08)60785-x · Cited by 986
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
Twenty years of p53 research: structural and functional aspects of the p53 protein
May, P., & May, E. (1999) · Oncogene · doi:10.1038/sj.onc.1203285 · Cited by 663
Self-citationMDM2 — 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
Drosophila p53 Binds a Damage Response Element at the reaper Locus
Brodsky, M. H., Nordstrom, W., Tsang, G., Kwan, E., Rubin, G. M., & Abrams, J. M. (2000) · Cell · doi:10.1016/s0092-8674(00)80627-3 · Cited by 473
Metadata
- Authors
- Soussi, T., & May, P.
- Affiliations
- Inserm (FR)
- Commissariat à l'Énergie Atomique et aux Énergies Alternatives (FR)
- Corresponding author
- Soussi, Thierry
- ORCID
- Soussi, Thierry
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1996-08
- Volume
- 260
- Issue
- 5
- Pages
- 623-637
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2012183441
- Cited by
- 208
- References
- 141
- Citations by year
- 2026: 2 · 2024: 1 · 2023: 3 · 2022: 1 · 2021: 6 · 2020: 1 · 2018: 4 · 2016: 3 · 2015: 6 · 2014: 5 · 2013: 7 · 2012: 1
- FWCI
- 13.06
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ligue Contre le Cancer
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- p53, protein structure, gene evolution, protein flexibility, protein sequence comparison, crystallography, protein function, tumor suppressor
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cricetinae, Molecular Sequence Data, Phylogeny, Protein Conformation, Structure-Activity Relationship, Genes, p53, Tumor Suppressor Protein p53, Conserved Sequence, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Evolution, Molecular
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- CoChat. (2026). Citation check: Structural Aspects of the p53 Protein in Relation to Gene Evolution: A Second Look. https://app.cochat.ai/papers/10.1006/jmbi.1996.0425
- The paper
- Soussi, T., & May, P. (1996). Structural Aspects of the p53 Protein in Relation to Gene Evolution: A Second Look. Journal of Molecular Biology. https://doi.org/10.1006/jmbi.1996.0425
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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.