Interactions of angiotensin-converting enzyme-2 (ACE2) and SARS-CoV-2 spike receptor-binding domain (RBD): a structural perspective

[21] Jaimes JA(2021)The flexibility of ACE2 in the context of SARS-CoV-2 infection Biophys J 120 1072-3921

[22] Millet JK(2020)Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 Science 367 1444-1136e11

[23] Whittaker GR(2020)Cryo-EM structures of SARS-CoV-2 spike without and with ACE2 Reveal a pH-dependent switch to mediate endosomal positioning of receptor-binding domains Cell Host Microbe 28 867-1214

[24] Mjokane N(2020)Structure, function, and antigenicity of the SARS-CoV-2 Spike glycoprotein Cell 181 281-160

[25] Maliehe M(2020)Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation Science 367 1260-387e7

[26] Folorunso OS(2020)A pneumonia outbreak associated with a new coronavirus of probable bat origin Nature 579 270-undefined

[27] Ogundeji AO(2021)Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: an insight from structural data J Cell Physiol 236 7045-undefined

[28] Gcilitshana OMN(2021)Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex J Biomol Struct Dyn 23 26451-undefined

[29] Albertyn J(2021)Mechanistic insights into the effects of key mutations on SARS-CoV-2 RBD–ACE2 binding Phys Chem Chem Phys 27 2728-undefined

[30] Pohl CH(2021)Emergence of SARS-COV-2 spike protein escape mutation Q493R after treatment for COVID-19 Emerg Infect Dis 13 3915-undefined

[21] Jaimes JA(2021)The flexibility of ACE2 in the context of SARS-CoV-2 infection Biophys J 120 1072-3921

[22] Millet JK(2020)Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2 Science 367 1444-1136e11

[23] Whittaker GR(2020)Cryo-EM structures of SARS-CoV-2 spike without and with ACE2 Reveal a pH-dependent switch to mediate endosomal positioning of receptor-binding domains Cell Host Microbe 28 867-1214

[24] Mjokane N(2020)Structure, function, and antigenicity of the SARS-CoV-2 Spike glycoprotein Cell 181 281-160

[25] Maliehe M(2020)Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation Science 367 1260-387e7

[26] Folorunso OS(2020)A pneumonia outbreak associated with a new coronavirus of probable bat origin Nature 579 270-undefined

[27] Ogundeji AO(2021)Higher infectivity of the SARS-CoV-2 new variants is associated with K417N/T, E484K, and N501Y mutants: an insight from structural data J Cell Physiol 236 7045-undefined

[28] Gcilitshana OMN(2021)Structural genetics of circulating variants affecting the SARS-CoV-2 spike/human ACE2 complex J Biomol Struct Dyn 23 26451-undefined

[29] Albertyn J(2021)Mechanistic insights into the effects of key mutations on SARS-CoV-2 RBD–ACE2 binding Phys Chem Chem Phys 27 2728-undefined

[30] Pohl CH(2021)Emergence of SARS-COV-2 spike protein escape mutation Q493R after treatment for COVID-19 Emerg Infect Dis 13 3915-undefined