Year |
Citation |
Score |
2023 |
Pounot K, Piersson C, Goring AK, Rosu F, Gabelica V, Weik M, Han S, Fichou Y. Mutations in Tau Protein Promote Aggregation by Favoring Extended Conformations. Jacs Au. 4: 92-100. PMID 38274251 DOI: 10.1021/jacsau.3c00550 |
0.575 |
|
2022 |
Pounot K, Appel M, Beck C, Weik M, Schirò G, Fichou Y, Seydel T, Schreiber F. High-resolution Neutron Spectroscopy to Study Picosecond-nanosecond Dynamics of Proteins and Hydration Water. Journal of Visualized Experiments : Jove. PMID 35575532 DOI: 10.3791/63664 |
0.738 |
|
2021 |
Schirò G, Fichou Y, Brogan APS, Sessions R, Lohstroh W, Zamponi M, Schneider GJ, Gallat FX, Paciaroni A, Tobias DJ, Perriman A, Weik M. Diffusivelike Motions in a Solvent-Free Protein-Polymer Hybrid. Physical Review Letters. 126: 088102. PMID 33709739 DOI: 10.1103/PhysRevLett.126.088102 |
0.762 |
|
2020 |
Giamblanco N, Fichou Y, Janot JM, Balanzat E, Han S, Balme S. Mechanisms of heparin-induced tau aggregation revealed by single nanopore. Acs Sensors. PMID 32216272 DOI: 10.1021/Acssensors.0C00193 |
0.365 |
|
2020 |
Lin Y, Fichou Y, Zeng Z, Hu NY, Han S. Electrostatically driven complex coacervation and amyloid aggregation of tau are independent processes with overlapping conditions. Acs Chemical Neuroscience. PMID 31971365 DOI: 10.1021/Acschemneuro.9B00627 |
0.347 |
|
2019 |
Fichou Y, Oberholtzer ZR, Ngo H, Cheng CY, Keller TJ, Eschmann NA, Han S. Tau-Cofactor Complexes as Building Blocks of Tau Fibrils. Frontiers in Neuroscience. 13: 1339. PMID 31920504 DOI: 10.3389/Fnins.2019.01339 |
0.326 |
|
2019 |
Fichou Y, Han S. Publisher Correction: Tauopathies: Protein shapes at the core of chronic traumatic encephalopathy. Nature Structural & Molecular Biology. PMID 31123350 DOI: 10.1038/S41594-019-0251-9 |
0.327 |
|
2019 |
Fichou Y, Han S. Protein shapes at the core of chronic traumatic encephalopathy. Nature Structural & Molecular Biology. PMID 31011211 DOI: 10.1038/S41594-019-0221-2 |
0.397 |
|
2018 |
Fichou Y, Lin Y, Rauch JN, Vigers M, Zeng Z, Srivastava M, Keller TJ, Freed JH, Kosik KS, Han S. Cofactors are essential constituents of stable and seeding-active tau fibrils. Proceedings of the National Academy of Sciences of the United States of America. PMID 30538196 DOI: 10.1073/Pnas.1810058115 |
0.314 |
|
2018 |
Fichou Y, Eschmann N, Han S. Capturing Conformational Changes of the Tau Protein Upon Aggregation Biophysical Journal. 114: 429a. DOI: 10.1016/J.Bpj.2017.11.2378 |
0.419 |
|
2017 |
Barnes R, Sun S, Fichou Y, Dahlquist FW, Heyden M, Han S. Spatially heterogeneous surface water diffusivity around structured protein surfaces at equilibrium. Journal of the American Chemical Society. PMID 29091442 DOI: 10.1021/Jacs.7B08606 |
0.597 |
|
2017 |
Fichou Y, Eschmann NA, Keller TJ, Han S. Conformation-based assay of tau protein aggregation. Methods in Cell Biology. 141: 89-112. PMID 28882313 DOI: 10.1016/Bs.Mcb.2017.06.008 |
0.407 |
|
2016 |
Zaccai G, Bagyan I, Combet J, Cuello GJ, Demé B, Fichou Y, Gallat FX, Galvan Josa VM, von Gronau S, Haertlein M, Martel A, Moulin M, Neumann M, Weik M, Oesterhelt D. Neutrons describe ectoine effects on water H-bonding and hydration around a soluble protein and a cell membrane. Scientific Reports. 6: 31434. PMID 27527336 DOI: 10.1038/Srep31434 |
0.733 |
|
2015 |
Fichou Y, Heyden M, Zaccai G, Weik M, Tobias DJ. Molecular Dynamics Simulations of a Powder Model of the Intrinsically Disordered Protein Tau. The Journal of Physical Chemistry. B. 119: 12580-9. PMID 26351734 DOI: 10.1021/Acs.Jpcb.5B05849 |
0.739 |
|
2015 |
Fichou Y, Schirò G, Gallat FX, Laguri C, Moulin M, Combet J, Zamponi M, Härtlein M, Picart C, Mossou E, Lortat-Jacob H, Colletier JP, Tobias DJ, Weik M. Hydration water mobility is enhanced around tau amyloid fibers. Proceedings of the National Academy of Sciences of the United States of America. 112: 6365-70. PMID 25918405 DOI: 10.1073/Pnas.1422824112 |
0.693 |
|
2015 |
Schirò G, Fichou Y, Gallat FX, Wood K, Gabel F, Moulin M, Härtlein M, Heyden M, Colletier JP, Orecchini A, Paciaroni A, Wuttke J, Tobias DJ, Weik M. Translational diffusion of hydration water correlates with functional motions in folded and intrinsically disordered proteins. Nature Communications. 6: 6490. PMID 25774711 DOI: 10.1038/Ncomms7490 |
0.723 |
|
2012 |
Gallat FX, Brogan AP, Fichou Y, McGrath N, Moulin M, Härtlein M, Combet J, Wuttke J, Mann S, Zaccai G, Jackson CJ, Perriman AW, Weik M. A polymer surfactant corona dynamically replaces water in solvent-free protein liquids and ensures macromolecular flexibility and activity. Journal of the American Chemical Society. 134: 13168-71. PMID 22853639 DOI: 10.1021/Ja303894G |
0.746 |
|
2003 |
Le Rumeur E, Fichou Y, Pottier S, Gaboriau F, Rondeau-Mouro C, Vincent M, Gallay J, Bondon A. Interaction of dystrophin rod domain with membrane phospholipids. Evidence of a close proximity between tryptophan residues and lipids. The Journal of Biological Chemistry. 278: 5993-6001. PMID 12480947 DOI: 10.1074/Jbc.M207321200 |
0.34 |
|
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