ArticleJournal of the American Chemical Society2012
Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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Who cites it
27 citing papers in PubMed.
- Hierarchical multi-timescale structural dynamics of the disordered N-terminal of p53.Nature communications · 2026Article
- Heterochiral and Heterotypic Self-Assembly of Intrinsically Disordered Peptides Confers Peptide Supercoils with Exceptional Proteolytic Stability.Journal of the American Chemical Society · 2025Article
- Second-order allosteric control as a mechanism for compensatory mutations in B-cell translocation gene 2.Protein science : a publication of the Protein Society · 2025Article
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- Article
- Computational Methods to Investigate Intrinsically Disordered Proteins and their Complexes.ArXiv · 2024Article
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Re-Balancing Replica Exchange with Solute Tempering for Sampling Dynamic Protein Conformations.Journal of chemical theory and computation · 2023Article
- Variable Regions of p53 Isoforms Allosterically Hard Code DNA Interaction.The journal of physical chemistry. B · 2022Article
- Quantitative prediction of ensemble dynamics, shapes and contact propensities of intrinsically disordered proteins.PLoS computational biology · 2022Article
- Multisite phosphorylation and binding alter conformational dynamics of the 4E-BP2 protein.Biophysical journal · 2022Article
- Structural diversity of p63 and p73 isoforms.Cell death and differentiation · 2022Review
- Conformational Dynamics of Intrinsically Disordered Proteins Regulate Biomolecular Condensate Chemistry.Chemical reviews · 2022Review
- Novel Allosteric Mechanism of Dual p53/MDM2 and p53/MDM4 Inhibition by a Small Molecule.Frontiers in molecular biosciences · 2022Article
- Cancer-Associated Mutations Perturb the Disordered Ensemble and Interactions of the Intrinsically Disordered p53 Transactivation Domain.Journal of molecular biology · 2021Article
- Tumor-Suppressor p53TADChembiochem : a European journal of chemical biology · 2020Article
- Gradual compaction of the nascent peptide during cotranslational folding on the ribosome.eLife · 2020Article
- Residual Structures and Transient Long-Range Interactions of p53 Transactivation Domain: Assessment of Explicit Solvent Protein Force Fields.Journal of chemical theory and computation · 2019Article
- Allostery in Its Many Disguises: From Theory to Applications.Structure (London, England : 1993) · 2019Review
- Transient Secondary Structures as General Target-Binding Motifs in Intrinsically Disordered Proteins.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The tumor suppressor p53 is a hub protein with a multitude of binding partners, many of which target its intrinsically disordered N-terminal domain, p53-TAD. Partners, such as the N-terminal domain of MDM2, induce formation of local structure and leave the remainder of the domain apparently disordered. We investigated segmental chain motions in p53-TAD using fluorescence quenching of an extrinsic label by tryptophan in combination with fluorescence correlation spectroscopy (PET-FCS). We studied the loop closure kinetics of four consecutive segments within p53-TAD and their response to protein binding and phosphorylation. The kinetics was multiexponential, showing that the conformational ensemble of the domain deviates from random coil, in agreement with previous findings from NMR spectroscopy. Phosphorylations or binding of MDM2 changed the pattern of intrachain kinetics. Unexpectedly, we found that upon binding and phosphorylation chain motions were altered not only within the targeted segments but also in remote regions. Long-range interactions can be induced in an intrinsically disordered domain by partner proteins that induce apparently only local structure or by post-translational modification.
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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.