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1 nd neutralizing humoral immunity against the viral hemagglutinin.
2 rrent vaccine containing 2009 (Cal0709) H1N1 viral hemagglutinin.
3 dulate the dissociation of nectin-4 from the viral hemagglutinin.
4 ry capacity to escape immunity targeting the viral hemagglutinin.
5 ies that react with the globular head of the viral hemagglutinin.
6 pitopes, the antibody-binding domains of the viral hemagglutinin.
7  with specificity to the stalk domain of the viral hemagglutinin.
8 s via binding of cell-surface glycans by the viral hemagglutinin.
9  by blocking membrane fusion mediated by the viral hemagglutinin.
10 ctions, each composed of a dimer of VP4, the viral hemagglutinin.
11  to stimulate an immune response against the viral hemagglutinin.
12 nd neutralizing humoral immunity against the viral hemagglutinin.
13 tal globular head domain of their respective viral hemagglutinins.
14  adaptive mutations occurred in the gene for viral hemagglutinin, a gene that frequently acquires cha
15  the N-terminal fragment, VP8*, which is the viral hemagglutinin and an important target of neutraliz
16 s of adaptive evolution, most notably in the viral hemagglutinin and compatible with the action of an
17 irus by blocking the interaction between the viral hemagglutinin and host cell receptors.
18  we have analyzed the N-glycans of influenza viral hemagglutinin and neuraminidase from several subty
19 ability, it is desirable to deliver both the viral hemagglutinin and neuraminidase glycoproteins.
20 duced nonsynonymous genetic diversity in the viral hemagglutinin and nucleoprotein, and (iii) intraho
21 ne renal cell carcinoma expressing influenza viral hemagglutinin as a defined surrogate antigen (Renc
22 y selectively blocking the maturation of the viral hemagglutinin at a stage preceding resistance to e
23 pervariable receptor-binding domain (RBD) of viral hemagglutinin displayed on a nanoparticle (np) abl
24 argeted cell population, we displayed on the viral hemagglutinin (H) a single-chain antibody (scAb) s
25 he method, the optimization was done using a viral hemagglutinin (HA) as a model protein and then app
26 potential of highly conserved regions of the viral hemagglutinin (HA) as targets for broadly neutrali
27  the sialic acid (SA) receptors to which the viral hemagglutinin (HA) binds.
28 antibodies against conserved epitopes on the viral hemagglutinin (HA) could confer immunity to the di
29 demic influenza vaccine that deliver various viral hemagglutinin (HA) doses with or without AS03 (a t
30          While the importance of antibody to viral hemagglutinin (HA) has long been recognized, the l
31 d in this study a novel DNA vaccine in which viral hemagglutinin (HA) is bivalently targeted to MHC c
32            Here, we uncovered that influenza viral hemagglutinin (HA) protein causes the degradation
33 eceptors, NKp44 and NKp46, interact with the viral hemagglutinin (HA) protein expressed on the cell s
34  have identified molecular phenotypes of the viral hemagglutinin (HA) protein that contribute to pand
35 ly diverse epitopes within the "head" of the viral hemagglutinin (HA) protein.
36 ecific for the immunodominant epitope of the viral hemagglutinin (HA) protein.
37       TCR transgenic mice (TS1) specific for viral hemagglutinin (HA) provided antigen-specific T cel
38 o experimentally introduced mutations in the viral hemagglutinin (HA) receptor-binding domain conferr
39 lied the above approach to analyze influenza viral hemagglutinin (HA) sequences.
40 ty directed against the stalk domains of the viral hemagglutinin (HA) show promise for protecting aga
41 es in the receptor binding site (RBS) of the viral hemagglutinin (HA) that alter receptor preference
42 s irreversible conformational changes of the viral hemagglutinin (HA) that drive the membrane fusion
43 tical is the acquisition of mutations on the viral hemagglutinin (HA) to "quantitatively switch" its
44 -specific mAbs target the head domain of the viral hemagglutinin (HA), whereas broadly reactive mAbs
45 ions in the proteolytic cleavage site of the viral hemagglutinin (HA), which activates HA and exposes
46                       Recent advancements in viral hemagglutinin (HA)-targeting small-molecule entry
47  type I IFN receptor 1 (IFNAR1) by utilizing viral hemagglutinin (HA).
48 enic changes that occur predominantly on the viral hemagglutinin (HA).
49 ntibodies targeting the globular head of the viral hemagglutinin (HA).
50 ucture, including addition of glycans to the viral hemagglutinin (HA).
51 ral and endosomal membranes catalyzed by the viral hemagglutinin (HA).
52 IAV particles competes with incorporation of viral hemagglutinin (HA).
53 c and structural variability of the targeted viral hemagglutinin (HA).
54 bodies recognizing conserved surfaces on the viral hemagglutinin (HA).
55                   The conserved stalk of the viral hemagglutinin has been identified as potential tar
56 ed against the conserved stalk domain of the viral hemagglutinin have attracted increasing attention
57                                              Viral hemagglutinin is a homotrimeric receptor, and thus
58  induce IgE class switching, suggesting that viral hemagglutinin is involved in this synergistic effe
59 us (NDV) requires an interaction between the viral hemagglutinin-neuraminidase (HN) and fusion (F) pr
60 type 3 (HPF3) require the interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with
61 us type 3 (HPF3) requires interaction of the viral hemagglutinin-neuraminidase (HN) glycoprotein with
62           Coexpression of M protein with the viral hemagglutinin-neuraminidase (HN) or fusion (F) gly
63 ote fusion of Cos-7 cells independent of the viral hemagglutinin-neuraminidase (HN) protein and exhib
64 , initiates infection with attachment of the viral hemagglutinin-neuraminidase (HN) protein to sialic
65  that bind the conserved stalk domain of the viral hemagglutinin of H1 and H5 subtypes and protect mi
66                                          The viral hemagglutinins of conventional influenza A viruses
67 tion and performed similarly for recombinant viral hemagglutinin protein detection.
68 eptide (IFP) is the N-terminal domain of the viral hemagglutinin protein, binds to the endosomal memb
69 acid mutations at key antigenic sites of the viral hemagglutinin protein.
70 e immunodominant globular head domain of the viral hemagglutinin protein.
71 a process of membrane fusion mediated by the viral hemagglutinin protein.
72 hat the EB peptide specifically binds to the viral hemagglutinin protein.
73                     Sequence analysis of the viral hemagglutinin receptor-binding domain performed on
74 d with virion aggregation and coating of the viral hemagglutinin receptor; however, viral lysis did n
75  have been reported to bind the stalk of the viral hemagglutinin, suggesting that a vaccine based on
76 haracterizing the binding specificity of the viral hemagglutinin to the sialylated glycan receptors (
77               Among those, a mutation in the viral hemagglutinin was identified that increases 2009 p
78 e any clustering or spatial rearrangement of viral hemagglutinin, which affects the rate-limiting ste
79 protein, and no changes were observed in the viral hemagglutinin, which is the receptor attachment pr