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Cited by 386

The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.

Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody

Open access
Lv, Zhe, Deng, Yong-Qiang, Ye, Qing, Cao, Lei, Sun, Chun-Yun, Fan, Changfa, Huang, Weijin, Sun, Shihui, Sun, Yao, Zhu, Ling, Chen, Qi, Wang, Nan, Nie, Jianhui, Cui, Zhen, Zhu, Dandan, Shaw, Neil, Li, Xiao-Feng, Li, Qianqian, Xie, Liangzhi, Wang, Youchun, Rao, Zihe, Qin, Cheng-Feng, Wang, Xiangxi·2020·Science

Published version of a preprint

Abstract

A steric block to SARS-CoV-2: In response to infection by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the immune system makes antibodies, many of which target the spike protein, a key player in host cell entry. Antibodies that potently neutralize the virus hold promise as therapeutics and could inform vaccine design. Lv et al. report a humanized monoclonal antibody that protected against SARS-CoV-2 in a mouse model. The cryo–electron microscopy structure, together with biochemical, cellular, and virological studies, showed that the antibody acts by binding to the receptor-binding domain of the spike and blocking its attachment to the host receptor. Science , this issue p. 1505

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Crossref · 10.1126/science.abc5881

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Research works printed but not linked: 2

  1. 10.1016/j.cell.2020.02.058 · doi:10.1016/j.cell.2020.02.058 · Paper page
  2. Z. Z. Junxian Ou J. Zhang W. Lan S. Zhao J. Wu D. Seto G. Zhang Q. Zhang RBD mutations from circulating SARS-CoV-2 strains enhance the structural stability and human ACE2 affinity of the spike protein. bioRxiv 2020.03.15.991844 [Preprint]. 23 March 2020. https://doi.org/10.1101/2020.03.15.991844. · DOI

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Metadata

Authors
Lv, Z., Deng, Y.-Q., Ye, Q., Cao, L., Sun, C.-Y., Fan, C., Huang, W., Sun, S., Sun, Y., Zhu, L., Chen, Q., Wang, N., Nie, J., Cui, Z., Zhu, D., Shaw, N., Li, X.-F., Li, Q., Xie, L., Wang, Y., Rao, Z., Qin, C.-F., & Wang, X.
Venue
Science
Published
2020-09-18
Volume
369
Issue
6510
Pages
1505-1509
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W3044050454
Cited by
386
References
43
FWCI
10.29
Type
journal article
Language
en
Open access
hybrid
Funders
  • Ministry of Science and Technology of the People's Republic of China (2020YFA0707500, 2018YFA0900801)
  • National Science Fund for Distinguished Young Scholars (No. 81925025)
  • Beijing Municipal Science and Technology Project (Z201100005420017)
  • the Strategic Priority Research Program (XDB29010000)
  • Innovation Fund for Medical Sciences (No.2019-I2M-5-049)
  • Innovative Research Group from the NSFC (No. 81621005)
  • Ten Thousand Talent Program and the NSFS Innovative Research Group (No. 81921005)

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CoChat. (2026). Citation check: Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody. https://app.cochat.ai/papers/10.1126/science.abc5881
The paper
Lv, Z., Deng, Y.-Q., Ye, Q., Cao, L., Sun, C.-Y., Fan, C., Huang, W., Sun, S., Sun, Y., Zhu, L., Chen, Q., Wang, N., Nie, J., Cui, Z., Zhu, D., Shaw, N., Li, X.-F., Li, Q., Xie, L., . . . Wang, X. (2020). Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody. Science. https://doi.org/10.1126/science.abc5881

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.