Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift | Nature
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift | Nature
Reagents for coronavirus omicron variant research
SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex | Science
Omicron mutations enhance infectivity and reduce antibody neutralization of SARS-CoV-2 virus-like particles | PNAS
Frontiers | Omicron: A Heavily Mutated SARS-CoV-2 Variant Exhibits Stronger Binding to ACE2 and Potently Escapes Approved COVID-19 Therapeutic Antibodies
SARS-CoV-2 Spike Mutant Protein | Sino Biological
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
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
Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum - ScienceDirect
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
BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection | Nature
Sequence analysis of the emerging SARS‐CoV‐2 variant Omicron in South Africa - Wang - 2022 - Journal of Medical Virology - Wiley Online Library
Addgene: pαH-S-GSAS-OMICRON.BA.2-RBD
SARS-CoV-2 Omicron varient (B.1.1.529) Spike RBD Recombinant Protein - Cat. No. 21-844 | ProSci
Bioengineering | Free Full-Text | Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of Escherichia coli
Frontiers | Predictions of the SARS-CoV-2 Omicron Variant (B.1.1.529) Spike Protein Receptor-Binding Domain Structure and Neutralizing Antibody Interactions
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
Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement | Science
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain | Nature Communications
Omicron and Delta Variant of SARS-CoV-2: A Comparative Computational Study of Spike protein | bioRxiv
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
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
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
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 ...
Viruses | Free Full-Text | Structural Characteristics of Heparin Binding to SARS-CoV-2 Spike Protein RBD of Omicron Sub-Lineages BA.2.12.1, BA.4 and BA.5
Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies | Nature
