The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2
Open accessAbstract
How SARS-CoV-2 binds to human cells: Scientists are racing to learn the secrets of severe acute respiratory syndrome–coronavirus 2 (SARS-CoV-2), which is the cause of the pandemic disease COVID-19. The first step in viral entry is the binding of the viral trimeric spike protein to the human receptor angiotensin-converting enzyme 2 (ACE2). Yan et al. present the structure of human ACE2 in complex with a membrane protein that it chaperones, B 0 AT1. In the context of this complex, ACE2 is a dimer. A further structure shows how the receptor binding domain of SARS-CoV-2 interacts with ACE2 and suggests that it is possible that two trimeric spike proteins bind to an ACE2 dimer. The structures provide a basis for the development of therapeutics targeting this crucial interaction. Science , this issue p. 1444
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“During the revision of our manuscript, the full-length hACE2 structure was reported to form a dimer in the presence of B0AT1 (an amino acid transporter), as revealed by cryoelectron microscopy (cryo-EM) analysis (Yan et al., 2020).”
Self-citationMechanisms of SARS-CoV-2 entry into cells
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Evidence for gastrointestinal infection of SARS-CoV-2
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Metadata
- Authors
- Yan, R., Zhang, Y., Li, Y., Xia, L., Guo, Y., & Zhou, Q.
- Venue
- Science
- Published
- 2020-03-27
- Volume
- 367
- Issue
- 6485
- Pages
- 1444-1448
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W3010441732
- Cited by
- 5,040
- References
- 14
- FWCI
- 134.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
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