ArticleThe EMBO journal2006
The structure of p53 tumour suppressor protein reveals the basis for its functional plasticity.
Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
63 citing papers in PubMed, 127 citations in OpenAlex.
- p53: from understanding its structure to advances in therapeutic targeting.Signal transduction and targeted therapy · 2026Review
- Mechanistic Insights of a p53-Targeting Small Molecule.ACS pharmacology & translational science · 2025Article
- Navigating the complexity of p53-DNA binding: implications for cancer therapy.Biophysical reviews · 2024Review
- A Bio-Indicator Pilot Study Screening Selected Heavy Metals in Female Hair, Nails, and Serum from Lifestyle Cosmetic, Canned Food, and Manufactured Drink Choices.Molecules (Basel, Switzerland) · 2023Article
- How Do Cancer-Related Mutations Affect the Oligomerisation State of the p53 Tetramerisation Domain?Current issues in molecular biology · 2023Article
- Structural assessment of the full-length wild-type tumor suppressor protein p53 by mass spectrometry-guided computational modeling.Scientific reports · 2023Article
- Mapping Interactions of the Intrinsically Disordered C-Terminal Regions of Tetrameric p53 by Segmental Isotope Labeling and NMR.Biochemistry · 2022Article
- High-Resolution Imaging of Human Cancer Proteins Using Microprocessor Materials.Chembiochem : a European journal of chemical biology · 2022Article
- Structural Basis of Mutation-Dependent p53 Tetramerization Deficiency.International journal of molecular sciences · 2022Article
- Review
- FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA.Protein science : a publication of the Protein Society · 2022Article
- Protein of a thousand faces: The tumor-suppressive and oncogenic responses of p53.Frontiers in molecular biosciences · 2022Review
- Novel Allosteric Mechanism of Dual p53/MDM2 and p53/MDM4 Inhibition by a Small Molecule.Frontiers in molecular biosciences · 2022Article
- The Δ40p53 isoform inhibits p53-dependent eRNA transcription and enables regulation by signal-specific transcription factors during p53 activation.PLoS biology · 2021Article
- Structure of the p53/RNA polymerase II assembly.Communications biology · 2021Article
- Single molecule studies reveal that p53 tetramers dynamically bind response elements containing one or two half sites.Scientific reports · 2020Article
- The Status of p53 Oligomeric and Aggregation States in Cancer.Biomolecules · 2020Review
- Therapeutic potential of ReACp53 targeting mutant p53 protein in CRPC.Prostate cancer and prostatic diseases · 2020Article
- Homologs of the Tumor Suppressor Protein p53: A Bioinformatics Study for Drug Design.MOJ proteomics & bioinformatics · 2020Article
- Mutant p53 in cancer therapy-the barrier or the path.Journal of molecular cell biology · 2019Review
3 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
p53 major tumour suppressor protein has presented a challenge for structural biology for two decades. The intact and complete p53 molecule has eluded previous attempts to obtain its structure, largely due to the intrinsic flexibility of the protein. Using ATP-stabilised p53, we have employed cryoelectron microscopy and single particle analysis to solve the first three-dimensional structure of the full-length p53 tetramer (resolution 13.7 A). The p53 molecule is a D2 tetramer, resembling a hollow skewed cube with node-like vertices of two sizes. Four larger nodes accommodate central core domains, as was demonstrated by fitting of its X-ray structure. The p53 monomers are connected via their juxtaposed N- and C-termini within smaller N/C nodes to form dimers. The dimers form tetramers through the contacts between core nodes and N/C nodes. This structure revolutionises existing concepts of p53's molecular organisation and resolves conflicting data relating to its biochemical properties. This architecture of p53 in toto suggests novel mechanisms for structural plasticity, which enables the protein to bind variably spaced DNA target sequences, essential for p53 transactivation and tumour suppressor functions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.