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Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead  to a non-RBM-binding monoclonal antibody escape | Nature Communications
Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape | Nature Communications

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
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

Bioengineering | Free Full-Text | Functional Expression of the Recombinant  Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of  Escherichia coli
Bioengineering | Free Full-Text | Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm of Escherichia coli

BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection |  Nature
BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection | Nature

IJMS | Free Full-Text | Distinct Conformations of SARS-CoV-2 Omicron Spike  Protein and Its Interaction with ACE2 and Antibody
IJMS | Free Full-Text | Distinct Conformations of SARS-CoV-2 Omicron Spike Protein and Its Interaction with ACE2 and Antibody

Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain | Nature  Communications
Cryo-EM structure of a SARS-CoV-2 omicron spike protein ectodomain | Nature Communications

Implications of the Mutations in the Spike Protein of the Omicron Variant  of Concern (VoC) of SARS-CoV-2 – Signature Science
Implications of the Mutations in the Spike Protein of the Omicron Variant of Concern (VoC) of SARS-CoV-2 – Signature Science

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 ...
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 ...

SARS-CoV-2 Spike Mutant Protein | Sino Biological
SARS-CoV-2 Spike Mutant Protein | Sino Biological

Omicron: What Makes the Latest SARS-CoV-2 Variant of Concern So Concerning?  | Journal of Virology
Omicron: What Makes the Latest SARS-CoV-2 Variant of Concern So Concerning? | Journal of Virology

Reagents for coronavirus omicron variant research
Reagents for coronavirus omicron variant research

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
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

Frontiers | Omicron: A Heavily Mutated SARS-CoV-2 Variant Exhibits Stronger  Binding to ACE2 and Potently Escapes Approved COVID-19 Therapeutic  Antibodies
Frontiers | Omicron: A Heavily Mutated SARS-CoV-2 Variant Exhibits Stronger Binding to ACE2 and Potently Escapes Approved COVID-19 Therapeutic Antibodies

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
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

Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift  | Nature
Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift | Nature

Frontiers | Predictions of the SARS-CoV-2 Omicron Variant (B.1.1.529) Spike  Protein Receptor-Binding Domain Structure and Neutralizing Antibody  Interactions
Frontiers | Predictions of the SARS-CoV-2 Omicron Variant (B.1.1.529) Spike Protein Receptor-Binding Domain Structure and Neutralizing Antibody Interactions

Receptor binding and complex structures of human ACE2 to spike RBD from  omicron and delta SARS-CoV-2 - ScienceDirect
Receptor binding and complex structures of human ACE2 to spike RBD from omicron and delta SARS-CoV-2 - ScienceDirect

Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1  serum - ScienceDirect
Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum - ScienceDirect

Omicron (B.1.1.529) variant | Pseudotyping plasmid | InvivoGen
Omicron (B.1.1.529) variant | Pseudotyping plasmid | InvivoGen

Addgene: pαH-S-GSAS-OMICRON.BA.2-RBD
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
SARS-CoV-2 Omicron varient (B.1.1.529) Spike RBD Recombinant Protein - Cat. No. 21-844 | ProSci

SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike  protein–ACE2 complex | Science
SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex | Science

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
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

Understanding the Omicron variant's mutations - The Washington Post
Understanding the Omicron variant's mutations - The Washington Post

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
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