ArticleJournal of biomolecular NMR2019
NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.
Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 40 citations in OpenAlex.
- Recognition of two hydrophobic pockets in the KIX domain of CBP by FOXO4 transactivation domain.Communications biology · 2025Article
- Peptide Inhibitors Targeting FOXO4-p53 Interactions and Inducing Senescent Cancer Cell-specific Apoptosis.Journal of medicinal chemistry · 2025Article
- The disordered p53 transactivation domain is the target of FOXO4 and the senolytic compound FOXO4-DRI.Nature communications · 2025Article
- Structural plasticity of the FOXO-DBD:p53-TAD interaction.Nature communications · 2025Article
- Structural and Functional Relevance of Charge Based Transient Interactions inside Intrinsically Disordered Proteins.bioRxiv : the preprint server for biology · 2024Article
- Characterization of Intrinsically Disordered Proteins in Healthy and Diseased States by Nuclear Magnetic Resonance.Reviews on recent clinical trials · 2024Review
- Observation of pH-Dependent Residual Structure in the Pmel17 Repeat Domain and the Implication for Its Amyloid Formation.Biochemistry · 2023Article
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA.Protein science : a publication of the Protein Society · 2022Article
- p53 Transactivation Domain Mediates Binding and Phase Separation with Poly-PR/GR.International journal of molecular sciences · 2021Article
- NMR illuminates intrinsic disorder.Current opinion in structural biology · 2021Review
- Recent Developments in Data-Assisted Modeling of Flexible Proteins.Frontiers in molecular biosciences · 2021Review
- NMR Methods for Structural Characterization of Protein-Protein Complexes.Frontiers in molecular biosciences · 2020Article
- Metal-Chelated Polymer Nanodiscs for NMR Studies.Angewandte Chemie (International ed. in English) · 2019Article
- Integrative methods in structural biology.Journal of biomolecular NMR · 2019Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
In order to understand the conformational behavior of intrinsically disordered proteins (IDPs) and their biological interaction networks, the detection of residual structure and long-range interactions is required. However, the large number of degrees of conformational freedom of disordered proteins require the integration of extensive sets of experimental data, which are difficult to obtain. Here, we provide a straightforward approach for the detection of residual structure and long-range interactions in IDPs under near-native conditions using solvent paramagnetic relaxation enhancement (sPRE). Our data indicate that for the general case of an unfolded chain, with a local flexibility described by the overwhelming majority of available combinations, sPREs of non-exchangeable protons can be accurately predicted through an ensemble-based fragment approach. We show for the disordered protein α-synuclein and disordered regions of the proteins FOXO4 and p53 that deviation from random coil behavior can be interpreted in terms of intrinsic propensity to populate local structure in interaction sites of these proteins and to adopt transient long-range structure. The presented modification-free approach promises to be applicable to study conformational dynamics of IDPs and other dynamic biomolecules in an integrative approach.
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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.