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  1. 8 de jul. de 2023 · Defining a highly conserved cryptic epitope for antibody recognition of SARS-CoV-2 variants. Aihua Hao, Wenping Song, Cheng Li, Xiang Zhang, Chao Tu, Xun Wang, Pengfei Wang, Yanling Wu, Tianlei...

  2. 3 de abr. de 2020 · CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and ...

  3. 5 de may. de 2020 · CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the “up” conformation and ...

  4. 8 de may. de 2020 · CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and ...

  5. 8 de jul. de 2023 · Defining a highly conserved cryptic epitope for antibody recognition of SARS-CoV-2 variants - PMC. Journal List. Signal Transduct Target Ther. v.8; 2023. PMC10329685. As a library, NLM provides access to scientific literature.