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

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

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

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

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

11 and an evolutionary connection between these viral fusion proteins.

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

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

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

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

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

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

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

19 le fusogenic conformational changes in other viral fusion proteins.

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

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

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

23 tions mediated by their structurally similar viral fusion proteins.

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

25 sponsible for proteolytic activation of many viral fusion proteins.

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

27 Similarity between viral fusion proteins and recently discovered cellular p

28 Other viral fusion proteins and the SNARE fusion protein compl

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

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

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

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

33 Viral fusion proteins are intriguing molecular machines

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

35 Many viral fusion proteins are primed by proteolytic cleavage

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

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

38 Many viral fusion proteins are type I integral membrane prote

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

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

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

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

43 Viral fusion proteins catalyze merger of viral and cell

44 Viral fusion proteins catalyze the merger of the virus e

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

76 Understanding how viral fusion proteins mediate entry will provide valuabl

77 Viral fusion proteins of classes I and II differ radical

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

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

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

81 The viral fusion proteins require a triggering event to unde

82 Class I viral fusion proteins share common mechanistic and struc

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

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

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

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

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

88 = 0.004) more abundant in the TM domains of viral fusion proteins than in those of nonfusion protein

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

108 Viral fusion protein trimers can play a critical role in

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

110 Since several viral fusion proteins undergo disulfide bond rearrangeme

111 Once activated, viral fusion proteins undergo large protein conformation

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

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

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

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

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

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