ライフサイエンスコーパス: viral fusion protein

1 n, although E2 is predicted to be a class II viral fusion protein.

2 ible and did not lead to inactivation of the viral fusion protein.

3 ks any of the defining features of a typical viral fusion protein.

4 ein, while gH/gL does not resemble any known viral fusion protein.

5 H/gL has no structural homology to any known viral fusion protein.

6 r epitope-specific responses compared to the viral fusion protein.

7 the viral spike (S) glycoprotein, a class I viral fusion protein.

8 RS-CoV viral spike glycoprotein is a class I viral fusion protein.

9 iniscent of the conformational transition of viral fusion proteins.

10 sponsible for proteolytic activation of many viral fusion proteins.

11 roposed for the fusion mechanisms of class I viral fusion proteins.

12 le similar to the proposed fusogenic core of viral fusion proteins.

13 g domain is not critical for the activity of viral fusion proteins.

14 he mechanism of fusion promoted by these two viral fusion proteins.

15 entiates them from many other low-pH-induced viral fusion proteins.

16 cule inhibitors of both class I and class II viral fusion proteins.

17 ign concepts can be applied to other Class 1 viral fusion proteins.

18 lambda spanins, which are similar to class I viral fusion proteins.

19 and an evolutionary connection between these viral fusion proteins.

20 g blocks of the unilaterally acting class-II viral fusion proteins.

21 oteins and falls into the group of class III viral fusion proteins.

22 consistent with the requirement for TMRs in viral fusion proteins.

23 oped viruses proceeds through the actions of viral fusion proteins.

24 k domains may be a common feature of class I viral fusion proteins.

25 le fusogenic conformational changes in other viral fusion proteins.

26 onmental pH that can trigger the activity of viral fusion proteins.

27 ons of which extend to BNAb targets on other viral fusion proteins.

28 a founder member of the class III family of viral fusion proteins.

29 tions mediated by their structurally similar viral fusion proteins.

30 ils like those in cellular SNAREs or in some viral fusion proteins.

31 precedented glimpses into the interaction of viral fusion proteins and membranes, revealing fusion in

32 fy initial strategies to stabilize class III viral fusion proteins and provide tools to probe gB-dire

33 Similarity between viral fusion proteins and recently discovered cellular p

34 Other viral fusion proteins and the SNARE fusion protein compl

35 ry that assembles between cells includes the viral fusion proteins and various accessory proteins tha

36 protein that is very large compared to other viral fusion proteins, and all except a short carboxy-te

37 idate for structural studies of the class II viral fusion proteins, and we report conditions that gen

38 ediated by influenza hemagglutinin and other viral fusion proteins apparently involve local lipidic c

39 SAV entry machinery exhibits typical class I viral fusion protein architecture.

40 Viral fusion proteins are also major targets of neutrali

41 Viral fusion proteins are intriguing molecular machines

42 Class II viral fusion proteins are present on the envelope of fla

43 Many viral fusion proteins are primed by proteolytic cleavage

44 The transmembrane (TM) domains of viral fusion proteins are required for fusion, but their

45 ished data showed that both peripherin-2 and viral fusion proteins are transmembrane proteins that pr

46 Many viral fusion proteins are type I integral membrane prote

47 The transmembrane (TM) domains of viral fusion proteins are typically required for fusion.

48 tein, gH/gL does not resemble any documented viral fusion protein at a structural level.

49 Many class I, II, and III viral fusion proteins bear fusion loops for target membr

50 epeat regions (HR1 and HR2, respectively) of viral fusion proteins can block infection of viruses in

51 dies have shown that the membrane anchors of viral fusion proteins can form highly specific oligomers

52 Viral fusion proteins catalyze merger of viral and cell

53 Viral fusion proteins catalyze the merger of the virus e

54 n residues can affect folding or function of viral fusion proteins, direct analysis of TM-TM interact

55 ion and postfusion crystal structures of the viral fusion protein E1 in conjunction with biochemical

56 lls expressing the low pH-triggered class II viral fusion protein E1 of Semliki Forest virus (SFV) we

57 lains how specific residues in this class II viral fusion protein enable virus infectivity.

58 are useful tools to study the properties of viral fusion proteins, especially those from highly path

59 Many viral fusion proteins exhibit a six-helix bundle as a co

60 of endosomal protease for activation of the viral fusion protein (F).

61 earing a single amino acid alteration in the viral fusion protein (F; L454W) was previously identifie

62 Paramyxovirus viral fusion proteins (F) insert into the target cell me

63 Viral fusion proteins facilitate cellular infection by f

64 membranes.Crystal structures for a number of viral fusion proteins facilitating this process have con

65 on peptide and transmembrane domains of many viral fusion proteins form stable helical bundles and in

66 HIV-1 gp41, providing further evidence that viral fusion proteins from diverse families such as Orth

67 cells by fusion, it behooves us to know how viral fusion proteins function.

68 The viral fusion protein gB is nonfusogenic on its own and r

69 The viral fusion protein glycoprotein B (gB) is conserved in

70 Unlike other class I viral fusion proteins, GPC retains its stable signal pep

71 fusion (F) protein, a member of the class I viral fusion protein group.

72 y requires the proteolytic activation of the viral fusion protein, HA.

73 While work with viral fusion proteins has demonstrated that the transmem

74 nistic properties, three distinct classes of viral fusion proteins have been identified to date.

75 While some viral fusion proteins have been shown to elicit stronger

76 ture, VSV G has been classified as class III viral fusion protein, having a predicted bipartite fusio

77 ruses utilize host proteases to activate the viral fusion protein, hemagglutinin (HA), into its fusio

78 The absence of a viral fusion protein implies that these quasi-enveloped

79 have shown that GPC is unique among class I viral fusion proteins in that the mature complex retains

80 ith the structures observed for other type 1 viral fusion proteins in their fusion-competent state.

81 e have used glycoprotein B (gB), a class III viral fusion protein, in its postfusion form.

82 shares the characteristics of FPs of class I viral fusion proteins, including high Ala/Gly content, i

83 with functionally analogous regions of other viral fusion proteins, including the presence and distri

84 against other enveloped viruses with class I viral fusion proteins, indicating specificity for arenav

85 organisation of glycosylation across class I viral fusion proteins influence not only individual glyc

86 Our data allow the visualization of a viral fusion protein inserted in its target membrane and

87 authors show that a chemical inhibitor to a viral fusion protein is effective in reducing viral titr

88 ovirus and lentivirus vectors with different viral fusion proteins is a useful strategy to alter the

89 present at the N-terminal region of class I viral fusion proteins is believed to initiate viral and

90 Because the trimeric oligomer of many viral fusion proteins is often stabilized by hydrophobic

91 tion of a hydrophobic fusion peptide (FP) in viral fusion proteins is still poorly understood.

92 monstrated similarities between gB and other viral fusion proteins, leading to the hypothesis that gB

93 e trimer-of-hairpins conformation of class I viral fusion proteins, less is known about intermediate

94 and exposed to low pH, indicating that this viral fusion protein may function in a manner unique amo

95 Thus, Gly residues in the TM domain of other viral fusion proteins may also prove to be important for

96 Understanding how viral fusion proteins mediate entry will provide valuabl

97 ng hMPV is the fusion (F) protein, a class I viral fusion protein mediating virus-cell membrane fusio

98 ke previous observations for several class I viral fusion proteins, mice immunized with postfusion or

99 Viral fusion proteins of classes I and II differ radical

100 Within the class I viral fusion proteins of many enveloped viruses, the FP

101 ng genetic engineering approaches to express viral fusion proteins on the surface of cell membrane-co

102 on models developed from numerous studies of viral fusion proteins, our results indicate that these a

103 We propose that the viral fusion proteins produced by virulent PRV infection

104 In the case of class I viral fusion proteins, recent advances in cryo-electron

105 The viral fusion proteins require a triggering event to unde

106 a host cell is mediated by spike, a class I viral fusion protein responsible for merging the viral a

107 Class I viral fusion proteins share common mechanistic and struc

108 identified structural relationships between viral fusion proteins shift the paradigm for how these p

109 now extends this description to "class III" viral fusion proteins, showing that reversibility of the

110 n of TM-TM interactions significantly impact viral fusion protein stability and function, presenting

111 The C-terminal transmembrane domain (TMD) of viral fusion proteins such as HIV gp41 and influenza hem

112 n proteins distinguish them from the class I viral fusion proteins, such as influenza virus hemagglut

113 Its topological similarity to viral fusion proteins suggests how the SNARE complex mig

114 = 0.004) more abundant in the TM domains of viral fusion proteins than in those of nonfusion protein

115 ARS-CoV) spike glycoprotein (S) is a class I viral fusion protein that binds to its receptor glycopro

116 It is a type 1 viral fusion protein that characteristically contains tw

117 executed by glycoprotein B (gB), a class III viral fusion protein that is conserved across all herpes

118 Glycoprotein B (gB) is an essential viral fusion protein that is conserved in all herpesviru

119 nucleopolyhedrovirus (AcMNPV) is a class III viral fusion protein that mediates pH-triggered membrane

120 tides are short N-terminal regions of type-1 viral fusion proteins that are critical for virus entry.

121 hat of postfusion gB, unlike certain class I viral fusion proteins that have been used as vaccine ant

122 Similar to other class I viral fusion proteins, the fusogenic stalk domain sponta

123 Similar to other class 1 viral fusion proteins, the heptad repeat regions of SARS

124 Unlike other class I viral fusion proteins, the mature GP-C complex retains a

125 In the HIV-1 gp41 and other viral fusion proteins, the minimal oligomerization state

126 Like all class 1 viral fusion proteins, the paramyxovirus F protein is th

127 Typical of many viral fusion proteins, the sequence of the Newcastle dis

128 As in other class I viral fusion proteins, this process proceeds through a s

129 e that AVP-p induces premature activation of viral fusion proteins through membrane perturbance.

130 demonstrate for the first time that class I viral fusion protein TM domains can self-associate as tr

131 Viral fusion protein TM-TM interactions are important fo

132 e receptor-binding molecule must trigger the viral fusion protein to mediate fusion and entry of the

133 with CoV and LP IAV pseudoparticles, cleaved viral fusion proteins to fusion-primed fragments and pot

134 nctions, including endogenous neuropeptides, viral fusion proteins, topogenic peptides, and amyloids.

135 initiated by a conformational change in the viral fusion protein, triggered by receptor binding, an

136 The viral fusion protein triggers from the pre- to the postf

137 During fusion, these class II viral fusion proteins trimerize and refold to form hairp

138 Viral fusion protein trimers can play a critical role in

139 Unlike most other viral fusion protein trimers, the monomers of GP64 are c

140 Since several viral fusion proteins undergo disulfide bond rearrangeme

141 Once activated, viral fusion proteins undergo large protein conformation

142 een widely assumed that HCV E2 is a class II viral fusion protein (VFP), the newly determined structu

143 the membrane fusion activity of heterologous viral fusion proteins when GS is coexpressed with those

144 gB is a class III viral fusion protein, while gH/gL does not resemble any

145 or part of the membrane-spanning domain of a viral fusion protein with sequences that encode signals

146 infection by blocking the interaction of the viral fusion protein with the cell membrane.

147 data suggest a novel priming mechanism for a viral fusion protein, with a critical proteolytic cleava

148 ich is structurally categorized as a class I viral fusion protein, within the same group as influenza