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1 of folding instability (BiP binding) of the viral envelope protein.
2 complemented by expression of a heterologous viral envelope protein.
3 ty of gp41, the transmembrane subunit of the viral envelope protein.
4 e viral lumen, as a C-terminal fusion on the viral envelope protein.
5 ecretary pathway for proteolytic cleavage of viral envelope protein.
6 ing intense selection on this segment of the viral envelope protein.
7 he membrane and hence its accessibility to a viral envelope protein.
8 hitosan (chi) to replace the function of the viral envelope protein.
9 LV-A), induces conformational changes in the viral envelope protein.
10 timated binding constant of the receptor and viral envelope protein.
11 efficient activation of this pH-independent viral envelope protein.
12 rocessing and cell surface expression of the viral envelope protein.
13 va is essential for efficient binding to the viral envelope protein.
14 proposals for a general fusion mechanism for viral envelope proteins.
15 lowed M1 particle budding without additional viral envelope proteins.
16 likely required for direct interaction with viral envelope proteins.
17 kinesin and the cytoplasmic tails from five viral envelope proteins.
18 r and conformational epitopes throughout the viral envelope proteins.
19 ion molecular sizing method, to the study of viral envelope proteins.
20 surface receptors and appropriately modified viral envelope proteins.
21 study of HBV tissue tropism conferred by the viral envelope proteins.
22 Nef on infectivity in the context of various viral envelope proteins.
24 nown to be determined by the sequence of the viral envelope protein, although the nature of the neuro
25 e first example for any RNA virus in which a viral envelope protein and a known viral RNA packaging s
26 Antagonists targeting the interaction of the viral envelope protein and receptors on the cell surface
27 , permitting sufficient affinity between the viral envelope protein and the antibody to neutralize th
29 to perinuclear, neuronal regions expressing viral envelope protein and the endoplasmic reticulum (ER
30 ry hypothesize that interactions between the viral envelope protein and the host receptor(s) induce c
31 arget cells by forming a complex between the viral envelope protein and two cell-surface membrane rec
33 ms of receptor-mediated interactions between viral envelope proteins and host cell receptors at the s
34 ells and point out that interactions between viral envelope proteins and host cell receptors can have
35 charide sequence offers the binding site for viral envelope proteins and plays critical roles in assi
36 so-called "mature" NCs) are enveloped by the viral envelope proteins and secreted as virions; "immatu
37 compatibilities of analogous or orthologous viral envelope proteins, and it could have important bio
38 lights the fact that interactions of M1 with viral envelope proteins are essential to direct M1 to th
40 this approach, the transmembrane domains of viral envelope proteins are selectively targeted by the
42 other tegument proteins in the cytoplasm or viral envelope proteins at the site of final envelopment
44 artment (ERGIC) requires accumulation of the viral envelope proteins at this point in the secretory p
47 Neutralizing antibodies are directed to the viral envelope protein (E) and an accepted correlate of
48 stem drives the transmembrane anchor of the viral envelope protein (E) toward the fusion loop, burie
49 The necessity of detecting antibodies to viral envelope proteins (E1 and E2) and to different gen
54 s, HIV, is the formation of a complex of the viral envelope protein gp120 and its human receptor CD4.
55 human immunodeficiency virus type 1 (HIV-1) viral envelope protein gp120 and proposed to function as
57 dent dorsal root ganglia (DRG) cultures, HIV viral envelope protein gp120 results in neurotoxicity an
58 analysis of the V1/V2 and V3 regions of the viral envelope protein gp120 revealed that the more effi
59 initial infection depends on binding of the viral envelope protein gp120 to CD4 on the cell surface,
60 involves sequential interactions between the viral envelope protein, gp120, cell surface CD4, and a G
65 119E, and R169P mutations in the S domain of viral envelope proteins impair virion secretion and that
66 s expressed, there were increased amounts of viral envelope proteins, including A33, A36, B5, and F13
67 irus (SARS-CoV) synthesizes several putative viral envelope proteins, including the spike (S), membra
68 ased vectors pseudotyped with many different viral envelope proteins, including VSV-G, while the same
69 ctions between the host cell receptor(s) and viral envelope protein induce structural changes in the
70 0 and the leucine zipper (LZ) region of gp41 viral envelope proteins interact cooperatively to determ
71 s, as several reports have revealed that the viral envelope proteins interact with the cellular TNF r
72 llular compartment in which specific IgA and viral envelope proteins interact, further strengthening
74 d mixing, but pH-dependent redistribution of viral envelope proteins into the target cell membrane wa
76 unity to characterize immunogenic domains on viral envelope proteins involved in entry into target ce
78 as been associated in part with variation in viral envelope proteins leading to antigenic variation a
79 ve two alternative fates: (i) envelopment by viral envelope proteins, leading to secretion extracellu
82 rs, blood-clotting components, and even many viral envelope proteins) occurring in almost all eukaryo
83 or direct CD4-independent association of the viral envelope protein of the HIV-1 strain III with the
84 heparin binding to many proteins, including viral envelope proteins, protein tyrosine phosphatases,
85 tion activity results for two panels bearing viral envelope proteins representing either an intergeno
86 and R169P substitutions in the S domains of viral envelope proteins, respectively, without modifying
89 o be initiated by inefficient folding of its viral envelope protein, suggesting that the neurodegener
90 sed in these analyses differ solely in their viral envelope proteins, suggesting that the block to XM
91 Influenza virus hemagglutinin (HA) is the viral envelope protein that mediates viral attachment to
92 form a trimeric coiled coil, reminiscent of viral envelope proteins that direct homotypic membrane f
93 very little of the middle and small surface (viral envelope) proteins that are translated from these
94 rulence is determined by the sequence of the viral envelope protein, though the specific role of this
95 nitiates with binding of the pre-S domain of viral envelope protein to surface receptors present on t
97 be pseudotyped by introducing a heterologous viral envelope protein (vesicular stomatitis virus G pro
98 t of the R peptide on the fusion activity of viral envelope proteins, we expressed simian immunodefic
99 tes were detected in the pre-S domain of the viral envelope protein, which is believed to determine v
100 IV-1) requires functional interaction of the viral envelope protein with a coreceptor belonging to th
101 y requires the functional interaction of the viral envelope protein with both CD4 and the CCR-5 corec
102 cells requires the sequential engagement of viral envelope protein with CD4 and coreceptor, we propo
103 ltistep process involving the interaction of viral envelope proteins with cell surface receptors.
104 oteins required specific interactions of the viral envelope proteins with the internal capsid protein
105 ed a common theme of a sequential binding of viral envelope proteins with two coreceptors to mediate
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