S
Sarah M. Sterling
Researcher at Harvard University
Publications - 16
Citations - 1856
Sarah M. Sterling is an academic researcher from Harvard University. The author has contributed to research in topics: Septin & Signal peptide. The author has an hindex of 11, co-authored 15 publications receiving 805 citations. Previous affiliations of Sarah M. Sterling include University of Maine & University of California, Berkeley.
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Journal ArticleDOI
Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai,Yongfei Cai,Jun Zhang,Jun Zhang,Tianshu Xiao,Tianshu Xiao,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Shaun Rawson,Sophia Rits-Volloch,Bing Chen,Bing Chen +12 more
TL;DR: Two cryo–electron microscopy structures derived from a preparation of the full-length S protein, representing its prefusion and postfusion conformations, are reported, advancing the understanding of SARS-CoV-2 entry and may guide the development of vaccines and therapeutics.
Journal ArticleDOI
Structural impact on SARS-CoV-2 spike protein by D614G substitution.
Jun Zhang,Jun Zhang,Yongfei Cai,Yongfei Cai,Tianshu Xiao,Tianshu Xiao,Jianming Lu,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Sophia Rits-Volloch,Haisun Zhu,Alec N. Woosley,Wei Yang,Piotr Sliz,Piotr Sliz,Bing Chen,Bing Chen +17 more
TL;DR: In this paper, the authors reported the structure of a full-length G614 S trimer, which adopts three distinct prefusion conformations that differ primarily by the position of one receptor-binding domain.
Posted ContentDOI
Distinct conformational states of SARS-CoV-2 spike protein
Yongfei Cai,Yongfei Cai,Jun Zhang,Jun Zhang,Tianshu Xiao,Tianshu Xiao,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Shaun Rawson,Sophia Rits-Volloch,Bing Chen,Bing Chen +12 more
TL;DR: Two cryo-EM structures derived from a single preparation of the full-length S protein, representing the prefusion and postfusion conformations, advance the understanding of how SARS-CoV-2 enters a host cell and may guide development of vaccines and therapeutics.
Journal ArticleDOI
Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants.
Yongfei Cai,Yongfei Cai,Jun Zhang,Jun Zhang,Tianshu Xiao,Tianshu Xiao,Christy L. Lavine,Shaun Rawson,Hanqin Peng,Haisun Zhu,Krishna Anand,Pei Tong,Avneesh Gautam,Shen Lu,Sarah M. Sterling,Richard M. Walsh,Sophia Rits-Volloch,Jianming Lu,Duane R. Wesemann,Wei Yang,Michael S. Seaman,Bing Chen,Bing Chen +22 more
TL;DR: In this article, the full-length spike (S) trimers of the B.1.7 and B.351 variants of SARS-CoV-2 have been analyzed.
Posted ContentDOI
Structural impact on SARS-CoV-2 spike protein by D614G substitution
Jun Zhang,Jun Zhang,Yongfei Cai,Yongfei Cai,Tianshu Xiao,Tianshu Xiao,Jianming Lu,Hanqin Peng,Sarah M. Sterling,Richard M. Walsh,Sophia Rits-Volloch,Piotr Sliz,Piotr Sliz,Bing Chen,Bing Chen +14 more
TL;DR: Cryo-EM structures of a full-length S trimer carrying G614 are reported, which adopts three distinct prefusion conformations differing primarily by the position of one receptor-binding domain (RBD), which extend the understanding of viral entry and suggest an improved immunogen for vaccine development.