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Chemical Physics|May 15, 2012
Water Diffusion In And Out Of The β-Barrel Of GFP and The Fast Maturing Fluorescent Protein, TurboGFPBinsen Li, Ramza Shahid, Paola Peshkepija, et al.
Frontiers in Molecular Neuroscience|December 3, 2019
Different Amyloid-β Self-Assemblies Have Distinct Effects on Intracellular Tau AggregationWoo Shik Shin, Jing Di, Kevin A Murray, et al.
Nature Structural & Molecular Biology|November 8, 2019
Structures of fibrils formed by α-synuclein hereditary disease mutant H50Q reveal new polymorphsDavid R Boyer, Binsen Li, Chuanqi Sun, et al.
Alzheimer'S Research & Therapy|October 20, 2019
Amyloid β-protein oligomers promote the uptake of tau fibril seeds potentiating intracellular tau aggregationWoo Shik Shin, Jing Di, Qin Cao, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 5, 2020
The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structureDavid R Boyer, Binsen Li, Chuanqi Sun, et al.
Journal of Neuroscience Research|May 21, 2019
Quantitative in vivo imaging of neuronal glucose concentrations with a genetically encoded fluorescence lifetime sensorCarlos Manlio Díaz-García, Carolina Lahmann, Juan Ramón Martínez-François, et al.
Nature Communications|September 8, 2018
Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernelBinsen Li, Peng Ge, Kevin A Murray, et al.
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