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Updated: May 15, 2024

Rbd 362

Rbd 362

Updated: May 15, 2024

Home / RBD 362

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Mosaic RBD nanoparticles induce intergenus cross-reactive antibodies and protect against SARS-CoV-2 challenge | PNAS

RBD Instruments 9103 USB Picoammeter - View Pricing, Buy Online | EMA Store

Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models | Science

Mosaic receptor-binding domain nanoparticles induce protective immunity against SARS-CoV-2 challenges | bioRxiv

Frontiers | The First Chemically-Synthesised, Highly Immunogenic Anti-SARS-CoV-2 Peptides in DNA Genotyped Aotus Monkeys for Human Use

Single-dose replicating poxvirus vector-based RBD vaccine drives robust humoral and T cell immune response against SARS-CoV-2 infection: Molecular Therapy

Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models | Science

A mosaic-type trimeric RBD-based COVID-19 vaccine candidate induces potent neutralization against Omicron and other SARS-CoV-2 variants | eLife

Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models | Science

Neutralizing antibodies for the prevention and treatment of COVID-19 | Cellular & Molecular Immunology

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein | eLife

Neutralizing antibody vaccine for pandemic and pre-emergent coronaviruses | Nature

Immunization with RBD-P2 and N protects against SARS-CoV-2 in nonhuman primates | Science Advances

Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants | Nature Communications

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein | eLife

A human monoclonal antibody targeting a conserved pocket in the SARS-CoV-2 receptor-binding domain core | bioRxiv

Cells | Free Full-Text | Mechanistic Origin of Different Binding Affinities of SARS-CoV and SARS-CoV-2 Spike RBDs to Human ACE2

The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein | eLife

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

Mosaic RBD nanoparticles protect against challenge by diverse sarbecoviruses in animal models | Science

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