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  • Crystal structure of SARS-CoV-2 spike receptor-binding . . . - RCSB PDB
    Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2
  • RCSB PDB - 6M17: The 2019-nCoV RBD ACE2-B0AT1 complex
    The 2019-nCoV RBD ACE2-B0AT1 complex Angiotensin-converting enzyme 2 (ACE2) is the cellular receptor for severe acute respiratory syndrome-coronavirus (SARS-CoV) and the new coronavirus (SARS-CoV-2) that is causing the serious coronavirus disease 2019 (COVID-19) epidemic Here, we present cryo-electron microscopy structures of full-length human ACE2 in the presence of the neutral amino acid
  • 5DO2: Complex structure of MERS-RBD bound with 4C2 antibody - RCSB PDB
    Both mAbs potently bind to MERS-RBD and block virus entry in vitro with high efficacy We further investigated their mechanisms of neutralization by crystallizing the complex between the Fab fragments and the RBD, and solved the structure of the 4C2 Fab MERS-RBD complex
  • RCSB PDB - 7BWJ: crystal structure of SARS-CoV-2 antibody with RBD
    Here we report the isolation and characterization of 206 RBD-specific monoclonal antibodies derived from single B cells from 8 individuals infected with SARS-CoV-2 We identified antibodies that potently neutralize SARS-CoV-2; this activity correlates with competition with ACE2 for binding to RBD
  • RCSB PDB - 8Z27: The structure of TGEV RBD and dog APN complex
    We further resolved the complex structures of dAPN bound to the PDCoV RBD TGEV RBD, respectively, establishing its divergent receptor-binding modes We identified R325 of dAPN as an important residue in the PDCoV RBD-dAPN interaction, and found the central role of Q746 and T749 in dAPN in the interaction with the TGEV RBD
  • RCSB PDB - 8K4U: Structure of BtKY72 spike receptor-binding domain (RBD . . .
    The cryo-electron microscopy structure of BtKY72 RBD bound to bat ACE2 identified a key residue important for the interaction between RBD and ACE2 In addition, we demonstrated that the mutations involving four types of core residues enabled the sarbecoviruses with deletion (s) to bind to human ACE2 (hACE2) and broadened the ACE2 usage of SARS
  • RCSB PDB - 9IU1: Structure of SARS-CoV-2 JN. 1 spike RBD in complex with . . .
    The SARS-CoV-2 spike protein, crucial for cellular entry, binds to the ACE2 receptor exclusively when its receptor-binding domain (RBD) adopts the up-conformation However, whether ACE2 also interacts with the RBD in the down-conformation to facilitate the conformational shift to RBD-up remains unclear
  • RCSB PDB - 8UPX: Omicron-S-MERS-RBD
    Nevertheless, the highly mutated RBD of SARS-CoV-2 variants, especially Omicron, significantly reduces the efficacy of current vaccines against SARS-CoV-2 variants Here a protein-based pan-beta-CoV subunit vaccine is designed by fusing the potent and conserved RBD of MERS-CoV into an RBD-truncated Omicron S protein
  • PDB-101: Molecule of the Month: SARS-CoV-2 Spike
    Spike protein from SARS-CoV, with one receptor binding domain (RBD) in the up position, and a closed conformation of the SARS-CoV-2 spike The S1 fragment is shown in magenta and the S2 fragment in red, with glycosylation in lighter shades
  • RCSB PDB - 9JJ6: BtHKU5-CoV-2-441 Spike RBD domain binding to hACE2
    Cryo-EM analysis of HKU5-CoV-2 receptor-binding domain (RBD) and human ACE2 complex revealed an entirely distinct binding mode compared with other ACE2-utilizing merbecoviruses with RBD footprint largely shared with ACE2-using sarbecoviruses and NL63





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