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1 domains (TMDs) of cell surface receptors and viral membrane proteins.
2 ere replaced only by TM domains from related viral membrane proteins.
3 age or glycosylation, in any of the numerous viral membrane proteins.
4         In addition, A27 associates with the viral membrane protein A17 to anchor to the viral membra
5 rc-dependent tyrosine phosphorylation of the viral membrane protein A36R.
6 ever, axonal entry and localization of other viral membrane proteins and endogenous cellular proteins
7 teine-containing domains of the E10R and L1R viral membrane proteins and the glutaredoxin are in the
8                                        Three viral membrane proteins are required for efficient anter
9  outside-in signaling cascade induced by the viral membrane protein B5R is required to potently activ
10 tein controls axonal localization of diverse viral membrane proteins but not that of capsid or tegume
11 lization and nanoparticle incorporation of a viral membrane protein complex from the virus membrane.
12                  Fusion is mediated by E1, a viral membrane protein containing the putative fusion pe
13 xed with the genomic RNA, interacts with the viral membrane protein during virion assembly, and plays
14 ow pH in the endosome and is mediated by the viral membrane protein E1.
15 ells but did result in specific decreases in viral membrane protein expression and assembly, leading
16 fluenza virus entry but play direct roles in viral membrane protein expression and assembly.
17 rticle, which results in dissociation of the viral membrane protein from the ribonucleo-protein core.
18                               At least three viral membrane proteins (gE, gI, and Us9) are necessary
19                                The influenza viral membrane protein hemagglutinin (HA) is required at
20                     Entry is mediated by the viral membrane protein hemagglutinin (HA), which trigger
21 was linked to the capsid by many copies of a viral membrane protein in the mature infectous virus.
22 read of infection and may disrupt packing of viral membrane proteins in lipid rafts, an essential ste
23 lustrate exciting opportunities to visualize viral membrane proteins in their native and possibly tra
24 undly decreased the stability of a subset of viral membrane proteins including those comprising the e
25 ontaneously "uncoated" with diffusion of the viral membrane proteins into the host plasma membrane an
26 poration of cellular as well as heterologous viral membrane proteins into the SIV envelope and may be
27 nervous system correlated with the amount of viral membrane proteins localized to axons.
28 ormation changes and reorganization of these viral membrane proteins occur during the transition from
29 dies suggest that antibodies to two or three viral membrane proteins optimally derived from the outer
30 s repressed, A11 did not colocalize with any viral membrane proteins or associate with membranes.
31                                          The viral membrane proteins P3 and P6 are organized into a l
32                              For a number of viral membrane proteins, Th cell epitopes are localized
33  virus (PRV) glycoprotein E (gE) is a type I viral membrane protein that facilitates the anterograde
34 tein (F) is highly conserved and is the only viral membrane protein that is essential for infection.
35 erpesvirus envelope protein Us9 is a type II viral membrane protein that is required for anterograde
36 s are short ( approximately 100 amino acids) viral membrane proteins that form oligomers of a defined
37                        Fusion is mediated by viral membrane proteins through their acid-dependent con
38 oprotein B, required for membrane fusion, or viral membrane protein Us9, required for sorting virions
39 e selective as this mutant did not prevent a viral membrane protein, VSVGtsO45 or wild-type pendrin f
40       We showed that the highly conserved A9 viral membrane protein was inserted into the ER of uninf
41 singly, capsid and tegument proteins but not viral membrane proteins were detected in axons.

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