Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

2020/04/09 by Qihui Wang, Yanfang Zhang, Lili Wu +12 · 7 citations
Agricultural and Biological Sciences · Medicine · #Animal Virus Infections Studies #COVID-19 Clinical Research Studies #SARS-CoV-2 and COVID-19 Research

paper · pdf · doi:10.1016/j.cell.2020.03.045

openalex publication_date 2020/04/09 · crossref created 2020/04/09 · crossref issued 2020/05/01 · crossref published 2020/05/01 · crossref published-print 2020/05/01 · openalex created_date 2025/10/10 · crossref deposited 2026/05/13 · crossref indexed 2026/07/27 · openalex updated_date 2026/07/31

Citations

• A novel coronavirus outbreak of global health concern
• A Novel Coronavirus from Patients with Pneumonia in China, 2019
• A new coronavirus associated with human respiratory disease in China
• A pneumonia outbreak associated with a new coronavirus of probable bat origin
• Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation
• Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein
• The species Severe acute respiratory syndrome-related coronavirus: classifying 2019-nCoV and naming it SARS-CoV-2
• SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
• Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2

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• The SARS-CoV-2 spike protein is vulnerable to moderate electric fields
• SARS-CoV-2 uses CD4 to infect T helper lymphocytes
• HKU5 bat merbecoviruses engage bat and mink ACE2 as entry receptors
• Extrapulmonary manifestations of COVID-19