Multiple sites on SARS‐CoV ‐2 spike protein are susceptible to proteolysis by cathepsins B, K, L, S, and V
Author:
Affiliation:
1. Wallace H. Coulter Department of Biomedical Engineering Georgia Institute of Technology & Emory University Atlanta Georgia USA
2. Biomedical Engineering Peking University Beijing China
Funder
National Science Foundation
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.4073
Reference53 articles.
1. Characterization of spike glycoprotein of SARS-CoV-2 on virus entry and its immune cross-reactivity with SARS-CoV
2. A Novel Coronavirus from Patients with Pneumonia in China, 2019
3. Structure, Function, and Evolution of Coronavirus Spike Proteins
4. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor
5. The spike glycoprotein of the new coronavirus 2019-nCoV contains a furin-like cleavage site absent in CoV of the same clade
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