Zhao Wang Lab



Yu, X. et al. Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes. Mol. Cell 79, 812–823.e4 (2020).

Kumar, D. et al. 2.7 Å cryo-EM structure of rotavirus core protein VP3, a unique capping machine with a helicase activity. Sci Adv 6, eaay6410 (2020).

Zhang, H. et al. TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential. Nat. Commun.11, 547 (2020).

Wang, Z. et al. In situ structure of the AcrAB-TolC efflux pump at subnanometer resolution. bioRxiv (2020).

Chen, M. et al. A complete data processing workflow for cryo-ET and subtomogram averaging. Nature Methods vol. 16 1161–1168 (2019).

Meng, R. et al. Structural basis for the adsorption of a single-stranded RNA bacteriophage. Nat. Commun. 10, 3130 (2019).

Shi, X. et al. In situ structure and assembly of the multidrug efflux pump AcrAB-TolC. Nature Communications 10, 2635 (2019).

Xie, Q. et al. Structure basis of neutralization by a novel site II/IV antibody against respiratory syncytial virus fusion protein. PLoS One 14, e0210749 (2019).

Dosey, T. L. et al. Structures of TRPV2 in distinct conformations provide insight into role of the pore turret. Nat. Struct. Mol. Biol. 26, 40–49 (2019).

Fan, G. et al. Cryo-EM reveals ligand induced allostery underlying InsP 3 R channel gating. Cell Res. 28, 1158–1170 (2018).

Dosey, T. L. et al. TRPV2 Ion Channel Gating Through Allosteric Domain Coupling Revealed by Cryo-EM. Available at SSRN 3155836 (2018).

Du, D., Wang, Z., Chiu, W. & Luisi, B. F. Purification of AcrAB-TolC Multidrug Efflux Pump for Cryo-EM Analysis. Methods Mol. Biol. 1700, 71–81 (2018).

bibliography on NCBI