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Significance of the RBD mutations in the SARS-CoV-2 omicron: from spike opening to antibody escape and cell attachment - Physical Chemistry Chemical Physics (RSC Publishing) DOI:10.1039/D2CP00169A
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An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies | Nature Medicine
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Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 - ScienceDirect
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Molecular and computational analysis of spike protein of newly emerged omicron variant in comparison to the delta variant of SARS-CoV-2 in Iraq | SpringerLink
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Bioengineering | Free Full-Text | Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of Escherichia coli
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Frontiers | Predictions of the SARS-CoV-2 Omicron Variant (B.1.1.529) Spike Protein Receptor-Binding Domain Structure and Neutralizing Antibody Interactions
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Characterization of SARS-CoV-2 Omicron spike RBD reveals significantly decreased stability, severe evasion of neutralizing-antibody recognition but unaffected engagement by decoy ACE2 modified for enhanced RBD binding | Signal Transduction and Targeted ...
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IJMS | Free Full-Text | Improved Binding Affinity of Omicron’s Spike Protein for the Human Angiotensin-Converting Enzyme 2 Receptor Is the Key behind Its Increased Virulence
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Omicron mutations enhance infectivity and reduce antibody neutralization of SARS-CoV-2 virus-like particles | PNAS
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Analysis of a SARS-CoV-2 convalescent cohort identified a common strategy for escape of vaccine-induced anti-RBD antibodies by Beta and Omicron variants - eBioMedicine
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Interaction Analysis of the Spike Protein of Delta and Omicron Variants of SARS-CoV-2 with hACE2 and Eight Monoclonal Antibodies Using the Fragment Molecular Orbital Method | Journal of Chemical Information and Modeling
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Mutations in the spike RBD of SARS-CoV-2 omicron variant may increase infectivity without dramatically altering the efficacy of current multi-dosage vaccinations | bioRxiv
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IJMS | Free Full-Text | The Increased Amyloidogenicity of Spike RBD and pH-Dependent Binding to ACE2 May Contribute to the Transmissibility and Pathogenic Properties of SARS-CoV-2 Omicron as Suggested by In Silico
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Implications of the Mutations in the Spike Protein of the Omicron Variant of Concern (VoC) of SARS-CoV-2 – Signature Science
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Mutations in the spike RBD of SARS-CoV-2 omicron variant may increase infectivity without dramatically altering the efficacy of current multi-dosage vaccinations | bioRxiv
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