ArticleJournal of biological physics2012
Temperature and solvent dependence of the dynamical landscape of tau protein conformations.
Article in Journal of biological physics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- Direct Observation of the Conformational Transitions in Tau and Their Correlation with Phase Behavior.JACS Au · 2025Article
- Interactions of Therapeutic Antibodies With Presynaptically-Released Misfolded Proteins in Neurodegenerative Diseases. A Spatial Monte-Carlo Simulation Study.CPT: pharmacometrics & systems pharmacology · 2025Article
- Recent Advances in the Label-Free Characterization of Exosomes for Cancer Liquid Biopsy: From Scattering and Spectroscopy to Nanoindentation and Nanodevices.Nanomaterials (Basel, Switzerland) · 2021Review
- Narrow equilibrium window for complex coacervation of tau and RNA under cellular conditions.eLife · 2019Article
- Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer's disease and other tauopathies.Oncotarget · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report the variation with temperature of the ensemble distribution of conformations spanned by the tau protein in its dynamical states measured by small-angle X-ray scattering (SAXS) using synchrotron radiation. The SAXS data show a clear temperature variation of the distribution of occupied protein conformations from 293 to 318 K. More conformations with a smaller radius of gyration are occupied at higher temperature. The protein-solvent interactions are shown by computer simulation to be essential for controlling the dynamics of protein conformations, providing evidence for the key role of water solvent in the protein dynamics, as proposed by Giorgio Careri.
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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.