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In particular, combined residue substitutions involving L506A, W553A and V555A resulted in even more profound reduction in viral entry efficiency, suggesting that the hydrophobic core formed between MERS-CoV RBD and DPP4 plays a critical role in mediating viral binding and entry into the target cells.
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The WNV Envelope (E) glycoprotein mediates viral binding to cellular receptors and is essential for the subsequent membrane fusion [ 5].
HA, the most abundant and immunogenic surface antigen of the influenza virus, is responsible for mediating viral attachment by binding to sialic acid residues on the host cell surface, and for fusing the viral envelope to the host cell membrane [ 8].
The HIV-1 co-receptor CCR5 possesses sulfo-tyrosine (TYS) residues at its N-terminus (Nt) that are required for binding HIV-1 gp120 and mediating viral entry.
It is the primary antigen that elicits host immune response, and is also responsible for binding to sialic-acid receptors and for mediating viral entry into host cells [39].
Influenza virus surface glycoprotein, hemagglutinin, holds a critical role in mediating viral entry into host cell.
As in HIV-1, they mediate viral fusion via binding to CD4 and a co-receptor, mainly CCR5 or CXCR4, on the target cell.
The HA1 subunit contains the receptor-binding site which mediates viral attachment to the cell membrane, whereas, the HA2 subunit contributes to membrane fusion [17], [18].
In our DNA binding assay, BSCTV C4 was shown to bind both dsDNA and ssDNA in vitro, which provide us a clue that BSCTV may bind its own viral DNA and may mediate viral DNA transport in certain stages of virus movement.
The Spike (S) glycoprotein of coronaviruses (CoV) mediates viral entry into host cells.
The Spike (S) protein of SARS-coronavirus (SARS-CoV) mediates viral entry into host cells.
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