ArticleChemical science2019
Residue-specific identification of phase separation hot spots of Alzheimer's-related protein tau.
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 88 citations in OpenAlex.
- RNA-Mediated Inhibition Mechanism of Liquid-Liquid Phase Separation and Subsequent Aggregation Revealed by Raman Microscopy.JACS Au · 2025Article
- Ion Valency as a Molecular Switch for Salt-Resistant Underwater Adhesion.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Quantifying collective interactions in biomolecular phase separation.Nature communications · 2025Article
- Catalytic Droplets: Enzyme Containing Microcompartments.Sub-cellular biochemistry · 2025Review
- Conformations of a low-complexity protein in homogeneous and phase-separated frozen solutions.Biophysical journal · 2024Article
- Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins.International journal of molecular sciences · 2024Article
- Conformations of a Low-Complexity Protein in Homogeneous and Phase-Separated Frozen Solutions.bioRxiv : the preprint server for biology · 2024Article
- Tau liquid-liquid phase separation: At the crossroads of tau physiology and tauopathy.Journal of cellular physiology · 2024Review
- Backbone interactions and secondary structures in phase separation of disordered proteins.Biochemical Society transactions · 2024Review
- Large dynamics of a phase separating arginine-glycine-rich domain revealed via nuclear and electron spins.Nature communications · 2024Article
- Methylene blue accelerates liquid-to-gel transition of tau condensates impacting tau function and pathology.Nature communications · 2023Article
- Structural basis of protein condensation on microtubules underlying branching microtubule nucleation.Nature communications · 2023Article
- Fyn nanoclustering requires switching to an open conformation and is enhanced by FTLD-Tau biomolecular condensates.Molecular psychiatry · 2023Article
- Biomolecular condensates formed by designer minimalistic peptides.Nature communications · 2023Article
- A call to order: Examining structured domains in biomolecular condensates.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023Article
- Reversible protein assemblies in the proteostasis network in health and disease.Frontiers in molecular biosciences · 2023Review
- The Role of Post-Translational Modifications on the Structure and Function of Tau Protein.Journal of molecular neuroscience : MN · 2022Review
- Tau liquid-liquid phase separation in neurodegenerative diseases.Trends in cell biology · 2022Review
- Review
- Driving force of biomolecular liquid-liquid phase separation probed by nuclear magnetic resonance spectroscopy.Biophysics reports · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Liquid-liquid phase separation (LLPS) of proteins enables the formation of non-membrane-bound organelles in cells and is associated with cancer and neurodegeneration. Little is known however about the structure and dynamics of proteins in LLPS conditions, because of the polymorphic nature of liquid-like protein droplets. Using carbon-detected NMR experiments we here show that the conversion of the aggregation-prone repeat region of the Alzheimer's-related protein tau from the dispersed monomeric state to phase-separated liquid-like droplets involves tau's aggregation-prone hexapeptides and regulatory KXGS motifs. Droplet dissolution in presence of 1,6-hexanediol revealed that chemical shift perturbations in the hexapeptide motifs are temperature driven, while those in KXGS motifs report on phase separation. Residue-specific secondary structure analysis further indicated that tau's repeat region exists in extended conformation in the dispersed state and attains transient β-hairpin propensity upon LLPS. Taken together our work shows that NMR spectroscopy can provide high-resolution insights into LLPS-induced changes in intrinsically disordered proteins.
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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.