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dc.contributor.authorKlegerman, Melvin E.-
dc.date.accessioned2024-01-04T08:57:26Z-
dc.date.available2024-01-04T08:57:26Z-
dc.date.issued2021-
dc.identifier.otherOER000002965vi
dc.identifier.urihttp://dlib.hust.edu.vn/handle/HUST/23829-
dc.description.abstractIn the SARS-CoV-2 coronavirus pandemic of 2019 (COVID-19), it has become evident that the ACE-2 receptor-binding domain (RBD) of the viral spike protein (SP) is the arget of neutralizing antibodies that comprise a critical element of protective immunit to the virus. The most definitive confirmation of this contention is that the two mRNA COVID-19 vaccines in general use, which elicit antibodies specific for the RBD, exhibit approximately 95% protective efficacy against COVID-19. A potential challenge to vaccine efficacy is the emergence of SARS-CoV-2 variants possessing multiple mutations affecting amino acid residues in the RBD.vi
dc.description.urihttps://www.biorxiv.org/content/10.1101/2021.04.26.441517v1.full.pdf+htmlvi
dc.formatPDFvi
dc.language.isoenvi
dc.publisherbioRxivvi
dc.rightsAttribution-NonCommercial-NoDerivs 3.0 Vietnam*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/vn/*
dc.subjectĐột biếnvi
dc.subjectProtein RBDvi
dc.subjectSự ức chếvi
dc.subjectN501Y SARS-CoV-2 Spikevi
dc.subject.lccTP248vi
dc.titleRelative Mutant N501Y SARS-CoV-2 Spike Protein RBD Inhibition of Anti-Spike Protein IgG and ACE-2 Binding to Spike Protein Speciesvi
dc.typeJournal articlevi
dc.description.noteCC BY-NC-ND 4.0vi
Appears in Collections:OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường

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