Molecular insights into receptor binding of recent emerging SARS-CoV-2 variants
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DOI: 10.1038/s41467-021-26401-w
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- Zhennan Zhao & Jingya Zhou & Mingxiong Tian & Min Huang & Sheng Liu & Yufeng Xie & Pu Han & Chongzhi Bai & Pengcheng Han & Anqi Zheng & Lutang Fu & Yuanzhu Gao & Qi Peng & Ying Li & Yan Chai & Zengyua, 2022. "Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
- Zhennan Zhao & Yufeng Xie & Bin Bai & Chunliang Luo & Jingya Zhou & Weiwei Li & Yumin Meng & Linjie Li & Dedong Li & Xiaomei Li & Xiaoxiong Li & Xiaoyun Wang & Junqing Sun & Zepeng Xu & Yeping Sun & W, 2023. "Structural basis for receptor binding and broader interspecies receptor recognition of currently circulating Omicron sub-variants," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
- Valeria Calvaresi & Antoni G. Wrobel & Joanna Toporowska & Dietmar Hammerschmid & Katie J. Doores & Richard T. Bradshaw & Ricardo B. Parsons & Donald J. Benton & Chloë Roustan & Eamonn Reading & Micha, 2023. "Structural dynamics in the evolution of SARS-CoV-2 spike glycoprotein," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
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