ArticleBiophysical journal2016
Phosphorylation Increases Persistence Length and End-to-End Distance of a Segment of Tau Protein.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
- Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions.The Journal of biological chemistry · 2026Article
- Backbone rigidity of disordered protein linkers from NMR experiments and MD simulations.Biophysical journal · 2026Article
- Structural insights into the role of the proline rich region in tau function.Structure (London, England : 1993) · 2025Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.Biophysical journal · 2024Article
- Phosphorylation of disordered proteins tunes local and global intramolecular interactions.bioRxiv : the preprint server for biology · 2024Article
- Effects of high-pressure homogenization and ultrasound on the composition, structure, and physicochemical properties of proteins extracted from Nannochloropsis Oceania.Ultrasonics sonochemistry · 2024Article
- Structural Preferences Shape the Entropic Force of Disordered Protein Ensembles.The journal of physical chemistry. B · 2023Article
- Structural preferences shape the entropic force of disordered protein ensembles.bioRxiv : the preprint server for biology · 2023Article
- Role of non-specific interactions in the phase-separation and maturation of macromolecules.PLoS computational biology · 2022Article
- The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins.International journal of molecular sciences · 2021Article
- Molecular Dynamics Simulations of Phosphorylated Intrinsically Disordered Proteins: A Force Field Comparison.International journal of molecular sciences · 2021Article
- Diverse Aggregation Kinetics Predicted by a Coarse-Grained Peptide Model.The journal of physical chemistry. B · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Hidden dynamic signatures drive substrate selectivity in the disordered phosphoproteome.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A "Russian Doll" Approach to More Efficient Acquisition of IDP NMR Spectra.Biophysical journal · 2019Article
- The role of annealing and fragmentation in human tau aggregation dynamics.The Journal of biological chemistry · 2019Article
- Architectural Dynamics of CaMKII-Actin Networks.Biophysical journal · 2019Article
- N-terminal domain of human uracil DNA glycosylase (hUNG2) promotes targeting to uracil sites adjacent to ssDNA-dsDNA junctions.Nucleic acids research · 2018Article
- Electrostatic Interactions in Protein Structure, Folding, Binding, and Condensation.Chemical reviews · 2018Review
- Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation.Journal of the American Chemical Society · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Intrinsically disordered regions of proteins, which lack unique tertiary structure under physiological conditions, are enriched in phosphorylation sites and in significant local bias toward the polyproline II conformation. The overrepresented coincidence of this posttranslational regulatory signal and local conformational bias within unstructured regions raises a question: can phosphorylation serve to manipulate the conformational preferences of a disordered protein? In this study, we use time-resolved fluorescence resonance energy transfer and a, to our knowledge, novel data analysis method to directly measure the end-to-end distance distribution of a phosphorylatable peptide derived from the human microtubule associated protein tau. Our results show that phosphorylation at threonine or serine extends the end-to-end distance and increases the effective persistence length of the tested model peptides. Unexpectedly, the extension is independent of salt concentration, suggestive of a nonelectrostatic origin. The phosphorylation extension and stiffening effect provides a peptide-scale physical interpretation for the posttranslational regulation of the highly abundant protein-protein interactions found in disordered proteins, as well as a potential insight into the regulatory mechanism of the tau protein's microtubule binding activity.
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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.