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1 193T substitution is involved in binding the sialic acid receptor.
2 nin-neuraminidase (HN) glycoprotein with its sialic acid receptor.
3 nin-neuraminidase (HN) glycoprotein with its sialic acid receptor.
4 lates also displayed binding to "human-like" sialic acid receptors.
5 a preference for avian-like alpha2,3-linked sialic acid receptors.
6 ges to recognize host-specific variations in sialic acid receptors.
7 h of these mutations increased HA binding to sialic acid receptors.
8 e [HN]) protein, which binds to cell surface sialic acid receptors.
9 agglutinin (HA) that often affect binding to sialic acid receptors.
10 residues and failed to bind alpha2,3-linked sialic acid receptors.
11 te, which is critical for binding human type sialic acid receptors.
12 viral entry and egress, including binding to sialic acid receptors, activating the fusion (F) protein
14 relatively high affinity for alpha2,6-linked sialic acid receptor and acid and temperature stability.
17 a key role in the recognition process of the sialic acid receptors and catalytic efficiency of NA.
19 and duck myotubes expressed avian and human sialic acid receptors and were readily susceptible to lo
20 virulence by its ability to bind avian-type sialic acid receptors, and that pdm/09 RNP conferred the
21 wcastle disease virus mediates attachment to sialic acid receptors, as well as cleavage of the same m
22 ion of complexes with the NA protein and the sialic acid receptors, as well as provide HA activity to
27 ricate balance between host cell binding and sialic acid receptor destruction is carefully maintained
28 and C-22, that exhibit increased avidity for sialic acid receptors due to single amino acid changes i
30 parasite strain that is heavily dependent on sialic-acid receptors for invasion, and show that the Pf
31 in interactions and HN protein attachment to sialic acid receptors, HN and F protein-containing compl
32 nhance binding to human-like alpha2,6-linked sialic acid receptors.IMPORTANCE The interaction of infl
33 ity from the preference of avian viruses for sialic acid receptors in alpha2,3 linkage to the prefere
34 rcine Kupffer cells, suggesting a role for a sialic-acid receptor in innate cellular recognition of x
36 -adapted influenza virus hemagglutinins bind sialic acid receptors linked via alpha2-3 glycosidic bon
39 lutinin ligands on influenza viruses and the sialic acid receptors on biosensors or on host cells, ou
41 avian alpha-2,3- and human alpha-2,6-linked sialic acid receptors on the apical surface and supports
43 es attach to cells via a sialic acid moiety (sialic acid receptor) that is alpha2-3 linked or alpha2-
44 ping reagents with an increased affinity for sialic acid receptors through linking CBM40 modules toge
45 that human influenza A virus uses canonical sialic acid receptors to infect bat cells, even though b
47 es generally mediate binding to cell surface sialic acid receptors via the hemagglutinin (HA) glycopr
49 se (HN) attachment protein of NDV recognizes sialic acid receptors, whereas the NiV G attachment prot
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