Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-c...
Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-civet ACE2s
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Author / Creator
Li, Linjie , Han, Pu , Huang, Baihan , Xie, Yufeng , Li, Weiwei , Zhang, Di , Han, Pengcheng , Xu, Zepeng , Bai, Bin , Zhou, Jingya , Kang, Xinrui , Li, Xiaomei , Zheng, Anqi , Zhang, Rong , Qiao, Shitong , Zhao, Xin , Qi, Jianxun , Wang, Qihui , Liu, Kefang and Gao, George Fu
Publisher
Singapore: Springer Nature Singapore
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Language
English
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Publisher
Singapore: Springer Nature Singapore
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Contents
The Omicron variant of SARS-CoV-2 carries multiple unusual mutations, particularly in the receptor-binding domain (RBD) of the spike (S) protein. Moreover, host-adapting mutations, such as residues 493, 498, and 501, were also observed in the Omicron RBD, which indicates that it is necessary to evaluate the interspecies transmission risk of the Omi...
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Full title
Broader-species receptor binding and structural bases of Omicron SARS-CoV-2 to both mouse and palm-civet ACE2s
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TN_cdi_doaj_primary_oai_doaj_org_article_edca1a8f88b1468b9628df57774793d6
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_edca1a8f88b1468b9628df57774793d6
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ISSN
2056-5968
E-ISSN
2056-5968
DOI
10.1038/s41421-022-00431-0
