ArticleCell cycle (Georgetown, Tex.)2013
Molecular dynamics of the full-length p53 monomer.
Article in Cell cycle (Georgetown, Tex.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Integrated molecular dynamics elucidation of TP53 H179 zinc-binding variants: genomic and structural characterization across NSCLC subtypes.Frontiers in bioinformatics · 2026Article
- Article
- Elucidating structural variability in p53 conformers using combinatorial refinement strategies and molecular dynamics.Cancer biology & therapy · 2024Article
- p53: The Multifaceted Roles of Covalent Modifications in Cancer.Pharmaceuticals (Basel, Switzerland) · 2024Review
- Molecular dynamics-based computational investigations on the influence of tumor suppressor p53 binding protein against other proteins/peptides.Scientific reports · 2024Article
- Realization of Amyloid-like Aggregation as a Common Cause for Pathogenesis in Diseases.Life (Basel, Switzerland) · 2023Review
- PRIMA-1 inhibits Y220C p53 amyloid aggregation and synergizes with cisplatin in hepatocellular carcinoma.Frontiers in molecular biosciences · 2023Article
- Conformational Heterogeneity and Frustration of the Tumor Suppressor p53 as Tuned by Punctual Mutations.International journal of molecular sciences · 2022Article
- Most Probable Druggable Pockets in Mutant p53-Arg175His Clusters Extracted from Gaussian Accelerated Molecular Dynamics Simulations.The protein journal · 2022Article
- Direct Interaction of miRNA and circRNA with the Oncosuppressor p53: An Intriguing Perspective in Cancer Research.Cancers · 2021Review
- An integrated view of p53 dynamics, function, and reactivation.Current opinion in structural biology · 2021Review
- Investigating Conformational Dynamics and Allostery in the p53 DNA-Binding Domain Using Molecular Simulations.Methods in molecular biology (Clifton, N.J.) · 2021Article
- Smyd2 conformational changes in response to p53 binding: role of the C-terminal domain.Molecular oncology · 2019Article
- Roles of computational modelling in understanding p53 structure, biology, and its therapeutic targeting.Journal of molecular cell biology · 2019Review
- A new technique for predicting intrinsically disordered regions based on average distance map constructed with inter-residue average distance statistics.BMC structural biology · 2019Article
- Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Structural Evolution and Dynamics of the p53 Proteins.Cold Spring Harbor perspectives in medicine · 2017Review
- DNA-binding protects p53 from interactions with cofactors involved in transcription-independent functions.Nucleic acids research · 2016Article
- The p53 tetramer shows an induced-fit interaction of the C-terminal domain with the DNA-binding domain.Oncogene · 2016Article
- Discovery of Novel Isatin-Based p53 Inducers.ACS medicinal chemistry letters · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The p53 protein is frequently mutated in a very large proportion of human tumors, where it seems to acquire gain-of-function activity that facilitates tumor onset and progression. A possible mechanism is the ability of mutant p53 proteins to physically interact with other proteins, including members of the same family, namely p63 and p73, inactivating their function. Assuming that this interaction might occurs at the level of the monomer, to investigate the molecular basis for this interaction, here, we sample the structural flexibility of the wild-type p53 monomeric protein. The results show a strong stability up to 850 ns in the DNA binding domain, with major flexibility in the N-terminal transactivations domains (TAD1 and TAD2) as well as in the C-terminal region (tetramerization domain). Several stable hydrogen bonds have been detected between N-terminal or C-terminal and DNA binding domain, and also between N-terminal and C-terminal. Essential dynamics analysis highlights strongly correlated movements involving TAD1 and the proline-rich region in the N-terminal domain, the tetramerization region in the C-terminal domain; Lys120 in the DNA binding region. The herein presented model is a starting point for further investigation of the whole protein tetramer as well as of its mutants.
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