메뉴 건너뛰기




Volumn 86, Issue 24, 2012, Pages 13642-13652

Acid-activated structural reorganization of the rift valley fever virus Gc fusion protein

Author keywords

[No Author keywords available]

Indexed keywords

CLATHRIN; DYNAMIN; ENHANCED GREEN FLUORESCENT PROTEIN; HISTIDINE; UNCLASSIFIED DRUG; VIRUS FUSION PROTEIN; VIRUS FUSION PROTEIN GC;

EID: 84870715857     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01973-12     Document Type: Article
Times cited : (60)

References (69)
  • 1
    • 0022351416 scopus 로고
    • Cell fusion by haemorrhagic fever with renal syndrome (HFRS) viruses and its application for titration of virus infectivity and neutralizing antibody
    • Arikawa J, Takashima I, Hashimoto N. 1985. Cell fusion by haemorrhagic fever with renal syndrome (HFRS) viruses and its application for titration of virus infectivity and neutralizing antibody. Arch. Virol. 86:303-313.
    • (1985) Arch.Virol. , vol.86 , pp. 303-313
    • Arikawa, J.1    Takashima, I.2    Hashimoto, N.3
  • 2
    • 0037292883 scopus 로고    scopus 로고
    • Rift Valley fever: an uninvited zoonosis in the Arabian peninsula
    • Balkhy HH, Memish ZA. 2003. Rift Valley fever: an uninvited zoonosis in the Arabian peninsula. Int. J. Antimicrob. Agents 21:153-157.
    • (2003) Int. J. Antimicrob. Agents , vol.21 , pp. 153-157
    • Balkhy, H.H.1    Memish, Z.A.2
  • 3
    • 84858324994 scopus 로고    scopus 로고
    • Distinct roles in folding, CD81 receptor binding and viral entry for conserved histidine residues of hepatitis C virus glycoprotein E1 and E2
    • Boo I, KteWierik Douam F, Lavillette D, Poumbourios P, Drummer HE. 2012. Distinct roles in folding, CD81 receptor binding and viral entry for conserved histidine residues of hepatitis C virus glycoprotein E1 and E2. Biochem. J. 443:85-94.
    • (2012) Biochem. J. , vol.443 , pp. 85-94
    • Boo, I.1    Douam, K.F.2    Lavillette, D.3    Poumbourios, P.4    Drummer, H.E.5
  • 4
    • 0037853207 scopus 로고    scopus 로고
    • Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation
    • Carneiro FA, et al. 2003. Membrane fusion induced by vesicular stomatitis virus depends on histidine protonation. J. Biol. Chem. 278:13789-13794.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13789-13794
    • Carneiro, F.A.1
  • 5
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K, Sullivan NJ, Felbor U, Whelan SP, Cunningham JM. 2005. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 6
    • 33744918278 scopus 로고    scopus 로고
    • Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein
    • Chanel-Vos C, Kielian M. 2006. Second-site revertants of a Semliki Forest virus fusion-block mutation reveal the dynamics of a class II membrane fusion protein. J. Virol. 80:6115-6122.
    • (2006) J. Virol. , vol.80 , pp. 6115-6122
    • Chanel-Vos, C.1    Kielian, M.2
  • 7
    • 0027480756 scopus 로고
    • Site-directed mutagenesis and chemical modification of histidine residues on an alpha-class chick liver glutathione S-transferase CL 3-3. Histidines are not needed for the activity of the enzyme and diethylpyrocarbonate modifies both histidine and lysine residues
    • Chang LH, Tam MF. 1993. Site-directed mutagenesis and chemical modification of histidine residues on an alpha-class chick liver glutathione S-transferase CL 3-3. Histidines are not needed for the activity of the enzyme and diethylpyrocarbonate modifies both histidine and lysine residues. Eur. J. Biochem. 211:805-811.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 805-811
    • Chang, L.H.1    Tam, M.F.2
  • 8
    • 79551639004 scopus 로고    scopus 로고
    • Cell entry of enveloped viruses
    • Cosset FL, Lavillette D. 2011. Cell entry of enveloped viruses. Adv. Genet. 73:121-183.
    • (2011) Adv. Genet. , vol.73 , pp. 121-183
    • Cosset, F.L.1    Lavillette, D.2
  • 9
    • 77249136744 scopus 로고    scopus 로고
    • Rift Valley fever virus subunit vaccines confer complete protection against a lethal virus challenge
    • de Boer SM, et al. 2010. Rift Valley fever virus subunit vaccines confer complete protection against a lethal virus challenge. Vaccine 28:2330-2339.
    • (2010) Vaccine , vol.28 , pp. 2330-2339
    • Boer, D.S.M.1
  • 10
    • 0042326083 scopus 로고    scopus 로고
    • Conformational changes in enveloped virus surface proteins during cell entry
    • Fass D. 2003. Conformational changes in enveloped virus surface proteins during cell entry. Adv. Protein Chem. 64:325-362.
    • (2003) Adv. Protein Chem. , vol.64 , pp. 325-362
    • Fass, D.1
  • 11
    • 33751059710 scopus 로고    scopus 로고
    • Development and characterization of a Rift Valley fever virus cell-cell fusion assay using alphavirus replicon vectors
    • Filone CM, Heise M, Doms RW, Bertolotti-Ciarlet A. 2006. Development and characterization of a Rift Valley fever virus cell-cell fusion assay using alphavirus replicon vectors. Virology 356:155-164.
    • (2006) Virology , vol.356 , pp. 155-164
    • Filone, C.M.1    Heise, M.2    Doms, R.W.3    Bertolotti-Ciarlet, A.4
  • 12
    • 29444438721 scopus 로고
    • The virus of Rift Valley fever or enzoötic hepatitis
    • Findlay GM, Daubney R. 1931. The virus of Rift Valley fever or enzoötic hepatitis. Lancet ii:1350-1351.
    • (1931) Lancet , vol.2 , pp. 1350-1351
    • Findlay, G.M.1    Daubney, R.2
  • 13
    • 55249110450 scopus 로고    scopus 로고
    • Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography
    • Freiberg AN, Sherman MB, Morais MC, Holbrook MR, Watowich SJ. 2008. Three-dimensional organization of Rift Valley fever virus revealed by cryoelectron tomography. J. Virol. 82:10341-10348.
    • (2008) J. Virol. , vol.82 , pp. 10341-10348
    • Freiberg, A.N.1    Sherman, M.B.2    Morais, M.C.3    Holbrook, M.R.4    Watowich, S.J.5
  • 14
    • 55949108725 scopus 로고    scopus 로고
    • Identification of specific histidines as pH sensors in flavivirus membrane fusion
    • Fritz R, Stiasny K, Heinz FX. 2008. Identification of specific histidines as pH sensors in flavivirus membrane fusion. J. Cell Biol. 183:353-361.
    • (2008) J. Cell Biol. , vol.183 , pp. 353-361
    • Fritz, R.1    Stiasny, K.2    Heinz, F.X.3
  • 15
    • 15444371889 scopus 로고    scopus 로고
    • Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein beta-penetrenes
    • doi:10.1186/1742-4682-1-10
    • Garry CE, Garry RF. 2004. Proteomics computational analyses suggest that the carboxyl terminal glycoproteins of Bunyaviruses are class II viral fusion protein (beta-penetrenes). Theor. Biol. Med. Model. 1:10. doi:10.1186/1742-4682-1-10.
    • (2004) Theor. Biol. Med. Model. , vol.1 , pp. 10
    • Garry, C.E.1    Garry, R.F.2
  • 16
    • 0021932202 scopus 로고
    • La Crosse virus G1 glycoprotein undergoes a conformational change at the pH of fusion
    • Gonzalez-Scarano F. 1985. La Crosse virus G1 glycoprotein undergoes a conformational change at the pH of fusion. Virology 140:209-216.
    • (1985) Virology , vol.140 , pp. 209-216
    • Gonzalez-Scarano, F.1
  • 18
    • 79960881605 scopus 로고    scopus 로고
    • Potential effects of Rift Valley fever in the United States
    • doi:10.3201/eid1708.101088
    • Hartley DM, et al. 2011. Potential effects of Rift Valley fever in the United States. Emerg. Infect. Dis. 17:e1. doi:10.3201/eid1708.101088.
    • (2011) Emerg.Infect.Dis. , vol.17
    • Hartley, D.M.1
  • 19
  • 20
    • 84864057456 scopus 로고    scopus 로고
    • Hantavirus structure-molecular interactions behind the scene
    • Hepojoki J, Strandin T, Lankinen H, Vaheri A. 2012. Hantavirus structure-molecular interactions behind the scene. J. Gen. Virol. 93(Pt 8):1631-1644.
    • (2012) J. Gen. Virol. , vol.93 , Issue.PART 8 , pp. 1631-1644
    • Hepojoki, J.1    Strandin, T.2    Lankinen, H.3    Vaheri, A.4
  • 21
    • 72849128417 scopus 로고    scopus 로고
    • Interactions and oligomerization of hantavirus glycoproteins
    • Hepojoki J, Strandin T, Vaheri A, Lankinen H. 2010. Interactions and oligomerization of hantavirus glycoproteins. J. Virol. 84:227-242.
    • (2010) J. Virol. , vol.84 , pp. 227-242
    • Hepojoki, J.1    Strandin, T.2    Vaheri, A.3    Lankinen, H.4
  • 22
    • 84864390331 scopus 로고    scopus 로고
    • Orthobunyavirus entry into neurons and other mammalian cells occurs via clathrin-mediated endocytosis and requires trafficking into early endosomes
    • Hollidge BS, et al. 2012. Orthobunyavirus entry into neurons and other mammalian cells occurs via clathrin-mediated endocytosis and requires trafficking into early endosomes. J. Virol. 86:7988-8001.
    • (2012) J. Virol. , vol.86 , pp. 7988-8001
    • Hollidge, B.S.1
  • 23
    • 77955902031 scopus 로고    scopus 로고
    • Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells
    • Howes MT, et al. 2010. Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells. J. Cell Biol. 190:675-691.
    • (2010) J. Cell Biol. , vol.190 , pp. 675-691
    • Howes, M.T.1
  • 24
    • 64049094507 scopus 로고    scopus 로고
    • Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers
    • Huiskonen JT, Overby AK, Weber F, Grunewald K. 2009. Electron cryo-microscopy and single-particle averaging of Rift Valley fever virus: evidence for GN-GC glycoprotein heterodimers. J. Virol. 83:3762-3769.
    • (2009) J. Virol. , vol.83 , pp. 3762-3769
    • Huiskonen, J.T.1    Overby, A.K.2    Weber, F.3    Grunewald, K.4
  • 25
    • 0036061569 scopus 로고    scopus 로고
    • Hantaan virus enters cells by clathrin-dependent receptor-mediated endocytosis
    • Jin M, et al. 2002. Hantaan virus enters cells by clathrin-dependent receptor-mediated endocytosis. Virology 294:60-69.
    • (2002) Virology , vol.294 , pp. 60-69
    • Jin, M.1
  • 26
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J, Loureiro S, Abrescia NG, Stuart DI, Jones IM. 2008. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 15:1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 27
    • 0023853159 scopus 로고
    • Rift Valley fever virus M segment: use of recombinant vaccinia viruses to study Phlebovirus gene expression
    • Kakach LT, Wasmoen TL, Collett MS. 1988. Rift Valley fever virus M segment: use of recombinant vaccinia viruses to study Phlebovirus gene expression. J. Virol. 62:826-833.
    • (1988) J. Virol. , vol.62 , pp. 826-833
    • Kakach, L.T.1    Wasmoen, T.L.2    Collett, M.S.3
  • 28
    • 33749266195 scopus 로고    scopus 로고
    • The role of histidine residues in low-pH-mediated viral membrane fusion
    • Kampmann T, Mueller DS, Mark AE, Young PR, Kobe B. 2006. The role of histidine residues in low-pH-mediated viral membrane fusion. Structure 14:1481-1487.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 29
    • 0022472667 scopus 로고
    • Use of bacterial expression cloning to define the amino acid sequences of antigenic determinants on the G2 glycoprotein of Rift Valley fever virus
    • Keegan K, Collett MS. 1986. Use of bacterial expression cloning to define the amino acid sequences of antigenic determinants on the G2 glycoprotein of Rift Valley fever virus. J. Virol. 58:263-270.
    • (1986) J. Virol. , vol.58 , pp. 263-270
    • Keegan, K.1    Collett, M.S.2
  • 30
    • 29144497159 scopus 로고    scopus 로고
    • Class II virus membrane fusion proteins
    • Kielian M. 2006. Class II virus membrane fusion proteins. Virology 344: 38-47.
    • (2006) Virology , vol.344 , pp. 38-47
    • Kielian, M.1
  • 31
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: more than one way to make a hairpin
    • Kielian M, Rey FA. 2006. Virus membrane-fusion proteins: more than one way to make a hairpin. Nat. Rev. Microbiol. 4:67-76.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 32
    • 77049094863 scopus 로고    scopus 로고
    • Intramuscular inoculation of calves with an experimental Newcastle disease virus-based vector vaccine elicits neutralizing antibodies against Rift Valley fever virus
    • Kortekaas J, et al. 2010. Intramuscular inoculation of calves with an experimental Newcastle disease virus-based vector vaccine elicits neutralizing antibodies against Rift Valley fever virus. Vaccine 28:2271-2276.
    • (2010) Vaccine , vol.28 , pp. 2271-2276
    • Kortekaas, J.1
  • 33
    • 81255179998 scopus 로고    scopus 로고
    • Creation of a nonspreading Rift Valley fever virus
    • Kortekaas J, et al. 2011. Creation of a nonspreading Rift Valley fever virus. J. Virol. 85:12622-12630.
    • (2011) J. Virol. , vol.85 , pp. 12622-12630
    • Kortekaas, J.1
  • 34
    • 59649124119 scopus 로고    scopus 로고
    • A histidine switch in hemagglutininneuraminidase triggers paramyxovirus-cell membrane fusion
    • Krishnan A, et al. 2009. A histidine switch in hemagglutininneuraminidase triggers paramyxovirus-cell membrane fusion. J. Virol. 83: 1727-1741.
    • (2009) J. Virol. , vol.83 , pp. 1727-1741
    • Krishnan, A.1
  • 35
    • 22144442056 scopus 로고    scopus 로고
    • Endosome-to-cytosol transport of viral nucleocapsids
    • Le Blanc I, et al. 2005. Endosome-to-cytosol transport of viral nucleocapsids. Nat. Cell Biol. 7:653-664.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 653-664
    • Blanc, L.I.1
  • 36
    • 81255123299 scopus 로고    scopus 로고
    • Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion
    • Li Z, Blissard GW. 2011. Autographa californica multiple nucleopolyhedrovirus GP64 protein: roles of histidine residues in triggering membrane fusion and fusion pore expansion. J. Virol. 85:12492-12504.
    • (2011) J. Virol. , vol.85 , pp. 12492-12504
    • Li, Z.1    Blissard, G.W.2
  • 37
    • 48349131507 scopus 로고    scopus 로고
    • Rift Valley fever virus structural proteins: expression, characterization and assembly of recombinant proteins
    • Liu L, Celma CC, Roy P. 2008. Rift Valley fever virus structural proteins: expression, characterization and assembly of recombinant proteins. Virol. J. 5:82.
    • (2008) Virol. J. , vol.5 , pp. 82
    • Liu, L.1    Celma, C.C.2    Roy, P.3
  • 39
    • 77956536795 scopus 로고    scopus 로고
    • Entry of bunyaviruses into mammalian cells
    • Lozach PY, et al. 2010. Entry of bunyaviruses into mammalian cells. Cell Host Microbe 7:488-499.
    • (2010) Cell Host Microbe , vol.7 , pp. 488-499
    • Lozach, P.Y.1
  • 40
    • 0026070664 scopus 로고
    • Transport of incoming influenza virus nucleocapsids into the nucleus
    • Martin K, Helenius A. 1991. Transport of incoming influenza virus nucleocapsids into the nucleus. J. Virol. 65:232-244.
    • (1991) J. Virol. , vol.65 , pp. 232-244
    • Martin, K.1    Helenius, A.2
  • 41
    • 0002134629 scopus 로고
    • Rift valley fever. I. The occurrence of human cases in Johannesburg
    • Mundel B, Gear J. 1951. Rift valley fever. I. The occurrence of human cases in Johannesburg. S. Afr. Med. J. 25:797-800.
    • (1951) S. Afr. Med. J. , vol.25 , pp. 797-800
    • Mundel, B.1    Gear, J.2
  • 42
    • 4544235675 scopus 로고    scopus 로고
    • Cell fusion activities of Hantaan virus envelope glycoproteins
    • Ogino M, et al. 2004. Cell fusion activities of Hantaan virus envelope glycoproteins. J. Virol. 78:10776-10782.
    • (2004) J. Virol. , vol.78 , pp. 10776-10782
    • Ogino, M.1
  • 43
    • 2642714342 scopus 로고
    • Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents
    • Ohkuma S, Poole B. 1978. Fluorescence probe measurement of the intralysosomal pH in living cells and the perturbation of pH by various agents. Proc. Natl. Acad. Sci. U. S. A. 75:3327-3331.
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 3327-3331
    • Ohkuma, S.1    Poole, B.2
  • 45
    • 33947383002 scopus 로고    scopus 로고
    • The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae) interacts with ribonucleoproteins and is critical for genome packaging
    • Overby AK, Pettersson RF, Neve EP. 2007. The glycoprotein cytoplasmic tail of Uukuniemi virus (Bunyaviridae) interacts with ribonucleoproteins and is critical for genome packaging. J. Virol. 81:3198-3205.
    • (2007) J. Virol. , vol.81 , pp. 3198-3205
    • Overby, A.K.1    Pettersson, R.F.2    Neve, E.P.3
  • 46
    • 77957852165 scopus 로고    scopus 로고
    • Rift Valley fever virus (Bunyaviridae: Phlebovirus): an update on pathogenesis, molecular epidemiology, vectors, diagnostics and prevention
    • Pepin M, Bouloy M, Bird BH, Kemp A, Paweska J. 2010. Rift Valley fever virus (Bunyaviridae: Phlebovirus): an update on pathogenesis, molecular epidemiology, vectors, diagnostics and prevention. Vet. Res. 41:61.
    • (2010) Vet. Res. , vol.41 , pp. 61
    • Pepin, M.1    Bouloy, M.2    Bird, B.H.3    Kemp, A.4    Paweska, J.5
  • 47
    • 79952843129 scopus 로고    scopus 로고
    • Efficient cellular release of Rift Valley fever virus requires genomic RNA
    • doi: 10.1371/journal.pone.0018070
    • Piper ME, Sorenson DR, Gerrard SR. 2011. Efficient cellular release of Rift Valley fever virus requires genomic RNA. PLoS One 6:e18070. doi: 10.1371/journal.pone.0018070.
    • (2011) PLoS One , vol.6
    • Piper, M.E.1    Sorenson, D.R.2    Gerrard, S.R.3
  • 48
    • 33846526211 scopus 로고    scopus 로고
    • Mutagenesis of the La Crosse virus glycoprotein supports a role for Gc (1066-1087) as the fusion peptide
    • Plassmeyer ML, et al. 2007. Mutagenesis of the La Crosse virus glycoprotein supports a role for Gc (1066-1087) as the fusion peptide. Virology 358:273-282.
    • (2007) Virology , vol.358 , pp. 273-282
    • Plassmeyer, M.L.1
  • 49
    • 66149140928 scopus 로고    scopus 로고
    • Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein
    • Qin ZL, Zheng Y, Kielian M. 2009. Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein. J.Virol. 83:4670-4677.
    • (2009) J. Virol. , vol.83 , pp. 4670-4677
    • Qin, Z.L.1    Zheng, Y.2    Kielian, M.3
  • 50
    • 77955649297 scopus 로고    scopus 로고
    • An assessment of the regional and national socio-economic impacts of the 2007 Rift Valley fever outbreak in Kenya
    • Rich KM, Wanyoike F. 2010. An assessment of the regional and national socio-economic impacts of the 2007 Rift Valley fever outbreak in Kenya. Am. J. Trop. Med. Hyg. 83:52-57.
    • (2010) Am. J. Trop. Med. Hyg. , vol.83 , pp. 52-57
    • Rich, K.M.1    Wanyoike, F.2
  • 52
    • 0029163526 scopus 로고
    • Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus
    • Ronka H, Hilden P, Von Bonsdorff CH, Kuismanen E. 1995. Homodimeric association of the spike glycoproteins G1 and G2 of Uukuniemi virus. Virology 211:241-250.
    • (1995) Virology , vol.211 , pp. 241-250
    • Ronka, H.1    Hilden, P.2    Bonsdorff, V.C.H.3    Kuismanen, E.4
  • 53
    • 84870663235 scopus 로고    scopus 로고
    • An assembly model of Rift Valley fever virus
    • Rusu M, et al. 2012. An assembly model of Rift Valley fever virus. Front. Microbiol. 3:254.
    • (2012) Front. Microbiol. , vol.3 , pp. 254
    • Rusu, M.1
  • 54
    • 70350340830 scopus 로고    scopus 로고
    • Dealing with low pH: entry and exit of alphaviruses and flaviviruses
    • Sanchez-San Martin C, Liu CY, Kielian M. 2009. Dealing with low pH: entry and exit of alphaviruses and flaviviruses. Trends Microbiol. 17:514-521.
    • (2009) Trends Microbiol. , vol.17 , pp. 514-521
    • Martin, S.S.C.1    Liu, C.Y.2    Kielian, M.3
  • 55
    • 55749089870 scopus 로고    scopus 로고
    • Oropouche virus entry into HeLa cells involves clathrin and requires endosomal acidification
    • Santos RI, et al. 2008. Oropouche virus entry into HeLa cells involves clathrin and requires endosomal acidification. Virus Res. 138:139-143.
    • (2008) Virus Res. , vol.138 , pp. 139-143
    • Santos, R.I.1
  • 56
    • 34948862521 scopus 로고    scopus 로고
    • Bunyaviridae
    • 5th ed Lippincott Williams & Wilkins, Philadelphia, PA
    • Schmaljohn CS, Nichol ST. 2007. Bunyaviridae, p 1741-1789. In Knipe DM, Howley PM (ed), Fields virology, 5th ed, vol 2. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2007) Fields virology , vol.2 , pp. 1741-1789
    • Schmaljohn, C.S.1    Nichol, S.T.2    Knipe, D.M.3    Howley, P.M.4
  • 57
    • 59749100734 scopus 로고    scopus 로고
    • Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry
    • Schowalter RM, Chang A, Robach JG, Buchholz UJ, Dutch RE. 2009. Low-pH triggering of human metapneumovirus fusion: essential residues and importance in entry. J. Virol. 83:1511-1522.
    • (2009) J. Virol. , vol.83 , pp. 1511-1522
    • Schowalter, R.M.1    Chang, A.2    Robach, J.G.3    Buchholz, U.J.4    Dutch, R.E.5
  • 58
    • 59849116492 scopus 로고    scopus 로고
    • Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesteroldependent
    • Simon M, Johansson C, Mirazimi A. 2009. Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-, pH-and cholesteroldependent. J. Gen. Virol. 90:210-215.
    • (2009) J. Gen. Virol. , vol.90 , pp. 210-215
    • Simon, M.1    Johansson, C.2    Mirazimi, A.3
  • 59
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K, Allison SL, Marchler-Bauer A, Kunz C, Heinz FX. 1996. Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol. 70:8142-8147.
    • (1996) J. Virol. , vol.70 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 60
    • 0021364902 scopus 로고
    • Protein synthesis in Rift Valley fever virus-infected cells
    • Struthers JK, Swanepoel R, Shepherd SP. 1984. Protein synthesis in Rift Valley fever virus-infected cells. Virology 134:118-124.
    • (1984) Virology , vol.134 , pp. 118-124
    • Struthers, J.K.1    Swanepoel, R.2    Shepherd, S.P.3
  • 61
    • 36749003222 scopus 로고    scopus 로고
    • Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion
    • Thoennes S, et al. 2008. Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion.Virology 370:403-414.
    • (2008) Virology , vol.370 , pp. 403-414
    • Thoennes, S.1
  • 63
    • 80051797727 scopus 로고    scopus 로고
    • Class II enveloped viruses
    • Vaney MC, Rey FA. 2011. Class II enveloped viruses. Cell. Microbiol. 13:1451-1459.
    • (2011) Cell. Microbiol. , vol.13 , pp. 1451-1459
    • Vaney, M.C.1    Rey, F.A.2
  • 64
    • 0026584727 scopus 로고
    • Membrane fusion process of Semliki Forest virus
    • I. Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells
    • Wahlberg JM, Garoff H. 1992. Membrane fusion process of Semliki Forest virus. I. Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells. J. Cell Biol. 116:339-348.
    • (1992) J.Cell Biol. , vol.116 , pp. 339-348
    • Wahlberg, J.M.1    Garoff, H.2
  • 65
    • 80053934670 scopus 로고    scopus 로고
    • Recent advances in the molecular and cellular biology of bunyaviruses
    • Walter CT, Barr JN. 2011. Recent advances in the molecular and cellular biology of bunyaviruses. J. Gen. Virol. 92:2467-2484.
    • (2011) J. Gen. Virol. , vol.92 , pp. 2467-2484
    • Walter, C.T.1    Barr, J.N.2
  • 66
    • 0025880220 scopus 로고
    • Structural variation of La Crosse virions under different chemical and physical conditions
    • Wang GJ, Hewlett M, Chiu W. 1991. Structural variation of La Crosse virions under different chemical and physical conditions. Virology 184:455-459.
    • (1991) Virology , vol.184 , pp. 455-459
    • Wang, G.J.1    Hewlett, M.2    Chiu, W.3
  • 68
    • 0019870337 scopus 로고
    • Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses
    • White J, Matlin K, Helenius A. 1981. Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses. J. Cell Biol. 89:674-679.
    • (1981) J. Cell Biol. , vol.89 , pp. 674-679
    • White, J.1    Matlin, K.2    Helenius, A.3
  • 69
    • 0019952878 scopus 로고
    • Infectious cell entry mechanism of influenza virus
    • Yoshimura A, et al. 1982. Infectious cell entry mechanism of influenza virus. J. Virol. 43:284-293.
    • (1982) J. Virol. , vol.43 , pp. 284-293
    • Yoshimura, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.