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1 nd neutralizing humoral immunity against the viral hemagglutinin.
2 nd neutralizing humoral immunity against the viral hemagglutinin.
3 rrent vaccine containing 2009 (Cal0709) H1N1 viral hemagglutinin.
4 dulate the dissociation of nectin-4 from the viral hemagglutinin.
5 ry capacity to escape immunity targeting the viral hemagglutinin.
6 ies that react with the globular head of the viral hemagglutinin.
7 pitopes, the antibody-binding domains of the viral hemagglutinin.
8 with specificity to the stalk domain of the viral hemagglutinin.
9 s via binding of cell-surface glycans by the viral hemagglutinin.
10 by blocking membrane fusion mediated by the viral hemagglutinin.
11 ctions, each composed of a dimer of VP4, the viral hemagglutinin.
12 tal globular head domain of their respective viral hemagglutinins.
13 adaptive mutations occurred in the gene for viral hemagglutinin, a gene that frequently acquires cha
14 the N-terminal fragment, VP8*, which is the viral hemagglutinin and an important target of neutraliz
15 s of adaptive evolution, most notably in the viral hemagglutinin and compatible with the action of an
16 duced nonsynonymous genetic diversity in the viral hemagglutinin and nucleoprotein, and (iii) intraho
17 ne renal cell carcinoma expressing influenza viral hemagglutinin as a defined surrogate antigen (Renc
18 y selectively blocking the maturation of the viral hemagglutinin at a stage preceding resistance to e
19 argeted cell population, we displayed on the viral hemagglutinin (H) a single-chain antibody (scAb) s
20 he method, the optimization was done using a viral hemagglutinin (HA) as a model protein and then app
21 potential of highly conserved regions of the viral hemagglutinin (HA) as targets for broadly neutrali
23 antibodies against conserved epitopes on the viral hemagglutinin (HA) could confer immunity to the di
24 demic influenza vaccine that deliver various viral hemagglutinin (HA) doses with or without AS03 (a t
26 d in this study a novel DNA vaccine in which viral hemagglutinin (HA) is bivalently targeted to MHC c
28 eceptors, NKp44 and NKp46, interact with the viral hemagglutinin (HA) protein expressed on the cell s
31 o experimentally introduced mutations in the viral hemagglutinin (HA) receptor-binding domain conferr
33 ty directed against the stalk domains of the viral hemagglutinin (HA) show promise for protecting aga
34 es in the receptor binding site (RBS) of the viral hemagglutinin (HA) that alter receptor preference
35 s irreversible conformational changes of the viral hemagglutinin (HA) that drive the membrane fusion
36 tical is the acquisition of mutations on the viral hemagglutinin (HA) to "quantitatively switch" its
37 -specific mAbs target the head domain of the viral hemagglutinin (HA), whereas broadly reactive mAbs
38 ions in the proteolytic cleavage site of the viral hemagglutinin (HA), which activates HA and exposes
43 ed against the conserved stalk domain of the viral hemagglutinin have attracted increasing attention
45 induce IgE class switching, suggesting that viral hemagglutinin is involved in this synergistic effe
46 us (NDV) requires an interaction between the viral hemagglutinin-neuraminidase (HN) and fusion (F) pr
47 type 3 (HPF3) require the interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with
48 us type 3 (HPF3) requires interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with
50 ote fusion of Cos-7 cells independent of the viral hemagglutinin-neuraminidase (HN) protein and exhib
51 , initiates infection with attachment of the viral hemagglutinin-neuraminidase (HN) protein to sialic
52 that bind the conserved stalk domain of the viral hemagglutinin of H1 and H5 subtypes and protect mi
54 eptide (IFP) is the N-terminal domain of the viral hemagglutinin protein, binds to the endosomal memb
59 d with virion aggregation and coating of the viral hemagglutinin receptor; however, viral lysis did n
60 have been reported to bind the stalk of the viral hemagglutinin, suggesting that a vaccine based on
61 haracterizing the binding specificity of the viral hemagglutinin to the sialylated glycan receptors (
63 e any clustering or spatial rearrangement of viral hemagglutinin, which affects the rate-limiting ste
64 protein, and no changes were observed in the viral hemagglutinin, which is the receptor attachment pr
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