ArticleJournal of chemical theory and computation2024
Effects of Phosphorylation on Protein Backbone Dynamics and Conformational Preferences.
Article in Journal of chemical theory and computation, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Evolutionary tuning of the molecular charge state of UBP24 shapes responses to high temperature.Nature plants · 2026Article
- Cyclic Peptides in Modern Drug Discovery: Trends and Therapeutic Directions.Journal of medicinal chemistry · 2026Review
- A CHK1-mediated phosphorylation switch suppresses human Topoisomerase 1-associated genomic instability.The EMBO journal · 2026Article
- Peroxidasin enables melanoma immune escape by inhibiting natural killer cell cytotoxicity.Molecular oncology · 2026Article
- Post-Translational Modifications of NTCP: A Regulatory Nexus for Bile Acid Transport and HBV Entry.Biomedicines · 2026Review
- RNA polymerase II: the elephant in the room.Trends in genetics : TIG · 2026Review
- Methods for studying the effects of phosphorylation patterns in proteins.Biochemical Society transactions · 2026Review
- Regulation of Keratin Chemical Modifications: Potential Molecular Mechanisms in Proliferative Diseases.International journal of molecular sciences · 2026Review
- The Protonic Brain: Nanoscale pH Dynamics, Proton Wires, and Acid-Base Information Coding in Neural Tissue.International journal of molecular sciences · 2026Review
- Assessing the relation between protein phosphorylation, AlphaFold3 models, and conformational variability.Protein science : a publication of the Protein Society · 2026Article
- Research advances in epigenetic modifications and post-translational modifications in endothelial-mesenchymal transition.Epigenetics & chromatin · 2025Review
- Global comparative structural analysis of responses to protein phosphorylation.Nature communications · 2025Article
- Intrinsically Disordered Peptide Nanofibers from a Structured Motif Within Proteins.Angewandte Chemie (International ed. in English) · 2025Article
- Progress in Lactate Metabolism and Its Regulation via Small Molecule Drugs.Molecules (Basel, Switzerland) · 2024Review
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Authors and funding
2 authors.
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Abstract
Phosphorylations are the most common and extensively studied post-translational modification (PTM) of proteins in eukaryotes. They constitute a major regulatory mechanism, modulating protein function, protein-protein interactions, as well as subcellular localization. Phosphorylation sites are preferably located in intrinsically disordered regions and have been shown to trigger structural rearrangements and order-to-disorder transitions. They can therefore have a significant effect on protein backbone dynamics or conformation, but only sparse experimental data are available. To obtain a more general description of how and when phosphorylations have a significant effect on protein behavior, molecular dynamics (MD) currently provides the only suitable framework to study these effects at a large scale in atomistic detail. This study develops a systematic MD simulation framework to explore the influence of phosphorylations on the local backbone dynamics and conformational propensities of proteins. Through a series of glycine-backbone peptides, we studied the effects of amino acid residues including the three most common phosphorylations (Ser, Thr, and Tyr), on local backbone dynamics and conformational propensities. We further extended our study to investigate the interactions of all such residues between position
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