Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement

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Items 201–300 of 535

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  18. Distinct Conformations of SARS-CoV-2 Omicron Spike Protein and Its Interaction with ACE2 and Antibody
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  21. How Do Point Mutations Enhancing the Basic Character of the RBDs of SARS-CoV-2 Variants Affect Their Transmissibility and Infectivity Capacities?
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  23. Frustration-driven allosteric regulation and signal transmission in the SARS-CoV-2 spike omicron trimer structures: a crosstalk of the omicron mutation sites allosterically regulates tradeoffs of protein stability and conformational adaptability
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  24. Evolutionary progression of collective mutations in Omicron sub-lineages towards efficient RBD-hACE2: Allosteric communications between and within viral and human proteins
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  36. In Silico Analyses Indicate a Lower Potency for Dimerization of TLR4/MD-2 as the Reason for the Lower Pathogenicity of Omicron Compared to Wild-Type Virus and Earlier SARS-CoV-2 Variants
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  37. Molecular basis of SARS-CoV-2 Omicron variant receptor engagement and antibody evasion and neutralization
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  38. Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1
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