Ziao Fu
Affiliations: | Columbia University, New York, NY |
Area:
Cryo-EMGoogle:
"Ziao Fu"Mean distance: (not calculated yet)
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Publications
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| Park J, Zuo H, Frangaj A, et al. (2021) Symmetric activation and modulation of the human calcium-sensing receptor. Proceedings of the National Academy of Sciences of the United States of America. 118 |
| Park J, Fu Z, Frangaj A, et al. (2020) Author Correction: Structure of human GABA receptor in an inactive state. Nature |
| Park J, Fu Z, Frangaj A, et al. (2020) Structure of human GABA receptor in an inactive state. Nature |
| Zheng X, Fu Z, Su D, et al. (2020) Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel. Nature Structural & Molecular Biology |
| Owji AP, Zhao Q, Ji C, et al. (2020) Structural and functional characterization of the bestrophin-2 anion channel. Nature Structural & Molecular Biology |
| Fu Z, Indrisiunaite G, Kaledhonkar S, et al. (2019) The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy. Nature Communications. 10: 2579 |
| Kaledhonkar S, Fu Z, Caban K, et al. (2019) Late steps in bacterial translation initiation visualized using time-resolved cryo-EM. Nature |
| Qiu W, Fu Z, Xu GG, et al. (2018) Structure and activity of lipid bilayer within a membrane-protein transporter. Proceedings of the National Academy of Sciences of the United States of America. 115: 12985-12990 |
| Kaledhonkar S, Fu Z, White H, et al. (2018) Time-Resolved Cryo-electron Microscopy Using a Microfluidic Chip. Methods in Molecular Biology (Clifton, N.J.). 1764: 59-71 |
| Caban K, Pavlov M, Kaledhonkar S, et al. (2018) The Structural Basis for Initiation Factor 2 Activation during Translation Initiation Biophysical Journal. 114: 593a |