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Volumn 86, Issue 5, 2012, Pages 2600-2609

The paramyxovirus fusion protein C-terminal region: Mutagenesis indicates an indivisible protein unit

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; VIRUS FUSION PROTEIN;

EID: 84857888959     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.06546-11     Document Type: Article
Times cited : (18)

References (55)
  • 1
    • 34247557393 scopus 로고    scopus 로고
    • Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling
    • Aguilar HC, et al. 2007. Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. J. Virol. 81:4520-4532.
    • (2007) J. Virol. , vol.81 , pp. 4520-4532
    • Aguilar, H.C.1
  • 2
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong RT, Kushnir AS, White JM. 2000. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 151:425-437.
    • (2000) J. Cell Biol. , vol.151 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 3
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker KA, Dutch RE, Lamb RA, Jardetzky TS. 1999. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 3:309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 4
    • 58549102514 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion
    • Bissonnette ML, Donald JE, DeGrado WF, Jardetzky TS, Lamb RA. 2009. Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion. J. Mol. Biol. 386:14-36.
    • (2009) J. Mol. Biol. , vol.386 , pp. 14-36
    • Bissonnette, M.L.1    Donald, J.E.2    DeGrado, W.F.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 5
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • Bose S, et al. 2011. Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J. Virol. 85:12855-12866.
    • (2011) J. Virol. , vol.85 , pp. 12855-12866
    • Bose, S.1
  • 6
    • 0028076285 scopus 로고
    • Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion
    • Bousse T, Takimoto T, Gorman WL, Takahashi T, Portner A. 1994. Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion. Virology 204:506-514.
    • (1994) Virology , vol.204 , pp. 506-514
    • Bousse, T.1    Takimoto, T.2    Gorman, W.L.3    Takahashi, T.4    Portner, A.5
  • 7
    • 0035083470 scopus 로고    scopus 로고
    • The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion
    • Chen L, et al. 2001. The structure of the fusion glycoprotein of Newcastle disease virus suggests a novel paradigm for the molecular mechanism of membrane fusion. Structure 9:255-266.
    • (2001) Structure , vol.9 , pp. 255-266
    • Chen, L.1
  • 8
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley DZ, Lenard J. 1998. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. U. S. A. 95:3425-3430.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 9
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman PM, Lawrence MC. 2003. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell. Biol. 4:309-319.
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 10
    • 33845212315 scopus 로고    scopus 로고
    • Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy
    • Connolly SA, Leser GP, Yin HS, Jardetzky TS, Lamb RA. 2006. Refolding of a paramyxovirus F protein from prefusion to postfusion conformations observed by liposome binding and electron microscopy. Proc. Natl. Acad. Sci. U. S. A. 103:17903-17908.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 17903-17908
    • Connolly, S.A.1    Leser, G.P.2    Yin, H.S.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 11
    • 0033524341 scopus 로고    scopus 로고
    • Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion
    • Deng R, et al. 1999. Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion. Virology 253:43-54.
    • (1999) Virology , vol.253 , pp. 43-54
    • Deng, R.1
  • 12
    • 0029006480 scopus 로고
    • Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike
    • Deng R, Wang Z, Mirza AM, Iorio RM. 1995. Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 209:457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 13
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms RW, Lamb RA, Rose JK, Helenius A. 1993. Folding and assembly of viral membrane proteins. Virology 193:545-562.
    • (1993) Virology , vol.193 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 14
    • 79952748653 scopus 로고    scopus 로고
    • Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion
    • Donald JE, et al. 2011. Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion. Proc. Natl. Acad. Sci. U. S. A. 108:3958-3963.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 3958-3963
    • Donald, J.E.1
  • 15
    • 0034445297 scopus 로고    scopus 로고
    • Virus membrane fusion proteins: biological machines that undergo a metamorphosis
    • Dutch RE, Jardetzky TS, Lamb RA. 2000. Virus membrane fusion proteins: biological machines that undergo a metamorphosis. Biosci. Rep. 20:597-612.
    • (2000) Biosci. Rep. , vol.20 , pp. 597-612
    • Dutch, R.E.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 16
    • 0035037386 scopus 로고    scopus 로고
    • Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement
    • Dutch RE, Lamb RA. 2001. Deletion of the cytoplasmic tail of the fusion protein of the paramyxovirus simian virus 5 affects fusion pore enlargement. J. Virol. 75:5363-5369.
    • (2001) J. Virol. , vol.75 , pp. 5363-5369
    • Dutch, R.E.1    Lamb, R.A.2
  • 18
    • 79952599344 scopus 로고    scopus 로고
    • The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein
    • Gravel KA, McGinnes LW, Reitter J, Morrison TG. 2011. The transmembrane domain sequence affects the structure and function of the Newcastle disease virus fusion protein. J. Virol. 85:3486-3497.
    • (2011) J. Virol. , vol.85 , pp. 3486-3497
    • Gravel, K.A.1    McGinnes, L.W.2    Reitter, J.3    Morrison, T.G.4
  • 20
    • 0025223471 scopus 로고
    • Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion
    • Helseth E, et al. 1990. Changes in the transmembrane region of the human immunodeficiency virus type 1 gp41 envelope glycoprotein affect membrane fusion. J. Virol. 64:6314-6318.
    • (1990) J. Virol. , vol.64 , pp. 6314-6318
    • Helseth, E.1
  • 21
    • 1642540252 scopus 로고    scopus 로고
    • Virology: a class act
    • Jardetzky TS, Lamb RA. 2004. Virology: a class act. Nature 427:307-308.
    • (2004) Nature , vol.427 , pp. 307-308
    • Jardetzky, T.S.1    Lamb, R.A.2
  • 22
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: lessons from paramyxovirus F
    • Lamb RA, Jardetzky TS. 2007. Structural basis of viral invasion: lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 17:427-436.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 23
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: the viruses and their replication
    • Knipe DM, Howley PM (ed), 5th ed. Lippincott/The Williams & Wilkins Co, Philadelphia, PA
    • Lamb RA, Parks GD. 2007. Paramyxoviridae: the viruses and their replication, p 1449-1496. In Knipe DM, Howley PM (ed), Fields virology, 5th ed. Lippincott/The Williams & Wilkins Co, Philadelphia, PA.
    • (2007) Fields virology , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 24
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee JK, et al. 2008. Functional interaction between paramyxovirus fusion and attachment proteins. J. Biol. Chem. 283:16561-16572.
    • (2008) J. Biol. Chem. , vol.283 , pp. 16561-16572
    • Lee, J.K.1
  • 25
    • 79960387921 scopus 로고    scopus 로고
    • Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    • McLellan JS, Yang Y, Graham BS, Kwong PD. 2011. Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J. Virol. 85:7788-7796.
    • (2011) J. Virol. , vol.85 , pp. 7788-7796
    • McLellan, J.S.1    Yang, Y.2    Graham, B.S.3    Kwong, P.D.4
  • 26
    • 0033017030 scopus 로고    scopus 로고
    • Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
    • Melikyan GB, Lin S, Roth MG, Cohen FS. 1999. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion. Mol. Biol. Cell 10:1821-1836.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1821-1836
    • Melikyan, G.B.1    Lin, S.2    Roth, M.G.3    Cohen, F.S.4
  • 27
    • 16244410802 scopus 로고    scopus 로고
    • Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion
    • Miyauchi K, et al. 2005. Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion. J. Virol. 79:4720-4729.
    • (2005) J. Virol. , vol.79 , pp. 4720-4729
    • Miyauchi, K.1
  • 28
    • 55549088556 scopus 로고    scopus 로고
    • The measles virus fusion protein transmembrane region modulates availability of an active glycoprotein complex and fusion efficiency
    • Muhlebach MD, Leonard VH, Cattaneo R. 2008. The measles virus fusion protein transmembrane region modulates availability of an active glycoprotein complex and fusion efficiency. J. Virol. 82:11437-11445.
    • (2008) J. Virol. , vol.82 , pp. 11437-11445
    • Muhlebach, M.D.1    Leonard, V.H.2    Cattaneo, R.3
  • 29
    • 0030874794 scopus 로고    scopus 로고
    • Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G
    • Odell D, Wanas E, Yan J, Ghosh HP. 1997. Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G. J. Virol. 71:7996-8000.
    • (1997) J. Virol. , vol.71 , pp. 7996-8000
    • Odell, D.1    Wanas, E.2    Yan, J.3    Ghosh, H.P.4
  • 30
    • 0028012576 scopus 로고
    • Mutations in the membranespanning domain of the human immunodeficiency envelope glycoprotein that affect fusion activity
    • Owens RJ, Burke C, Rose JK. 1994. Mutations in the membranespanning domain of the human immunodeficiency envelope glycoprotein that affect fusion activity. J. Virol. 68:570-574.
    • (1994) J. Virol. , vol.68 , pp. 570-574
    • Owens, R.J.1    Burke, C.2    Rose, J.K.3
  • 31
    • 0002285832 scopus 로고
    • The molecular biology of influenza viruses and paramyxoviruses
    • Davidson A, Elliott RM(ed), IRL Oxford University Press, Oxford, England
    • Paterson RG, Lamb RA. 1993. The molecular biology of influenza viruses and paramyxoviruses, p 35-73. In Davidson A, Elliott RM(ed), Molecular virology: a practical approach. IRL Oxford University Press, Oxford, England.
    • (1993) Molecular virology: a practical approach , pp. 35-73
    • Paterson, R.G.1    Lamb, R.A.2
  • 32
    • 0034712879 scopus 로고    scopus 로고
    • Fusion protein of the paramyxovirus SV5: destabilizing and stabilizing mutants of fusion activation
    • Paterson RG, Russell CJ, Lamb RA. 2000. Fusion protein of the paramyxovirus SV5: destabilizing and stabilizing mutants of fusion activation. Virology 270:17-30.
    • (2000) Virology , vol.270 , pp. 17-30
    • Paterson, R.G.1    Russell, C.J.2    Lamb, R.A.3
  • 33
    • 0023442009 scopus 로고
    • Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolates
    • Randall RE, Young DF, Goswami KKA, Russell WC. 1987. Isolation and characterization of monoclonal antibodies to simian virus 5 and their use in revealing antigenic differences between human, canine and simian isolates. J. Gen. Virol. 68:2769-2780.
    • (1987) J. Gen. Virol. , vol.68 , pp. 2769-2780
    • Randall, R.E.1    Young, D.F.2    Goswami, K.K.A.3    Russell, W.C.4
  • 34
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion
    • Russell CJ, Jardetzky TS, Lamb RA. 2001. Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J. 20:4024-4034.
    • (2001) EMBO J. , vol.20 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 35
    • 0242298583 scopus 로고    scopus 로고
    • A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion
    • Russell CJ, Kantor KL, Jardetzky TS, Lamb RA. 2003. A dual-functional paramyxovirus F protein regulatory switch segment: activation and membrane fusion. J. Cell Biol. 163:363-374.
    • (2003) J. Cell Biol. , vol.163 , pp. 363-374
    • Russell, C.J.1    Kantor, K.L.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 36
    • 33744734984 scopus 로고    scopus 로고
    • The structural basis of paramyxovirus invasion
    • Russell CJ, Luque LE. 2006. The structural basis of paramyxovirus invasion. Trends Microbiol. 14:243-246.
    • (2006) Trends Microbiol. , vol.14 , pp. 243-246
    • Russell, C.J.1    Luque, L.E.2
  • 37
    • 0031975822 scopus 로고    scopus 로고
    • Fusion activity of transmembrane and cytoplasmic domain chimeras of the influenza virus glycoprotein hemagglutinin
    • Schroth-Diez B, Ponimaskin E, Reverey H, Schmidt MFG, Herrmann A. 1998. Fusion activity of transmembrane and cytoplasmic domain chimeras of the influenza virus glycoprotein hemagglutinin. J. Virol. 72:133-141.
    • (1998) J. Virol. , vol.72 , pp. 133-141
    • Schroth-Diez, B.1    Ponimaskin, E.2    Reverey, H.3    Schmidt, M.F.G.4    Herrmann, A.5
  • 38
    • 0029095449 scopus 로고
    • Mutations in the cytoplasmic domain of the fusion glycoprotein of Newcastle disease virus depress syncytia formation
    • Sergel T, Morrison TG. 1995. Mutations in the cytoplasmic domain of the fusion glycoprotein of Newcastle disease virus depress syncytia formation. Virology 210:264-272.
    • (1995) Virology , vol.210 , pp. 264-272
    • Sergel, T.1    Morrison, T.G.2
  • 39
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • Shang L, Yue L, Hunter E. 2008. Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. J. Virol. 82:5417-5428.
    • (2008) J. Virol. , vol.82 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 40
    • 79959338198 scopus 로고    scopus 로고
    • Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers
    • Swanson K, et al. 2011. Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers. Proc. Natl. Acad. Sci. U. S. A. 108:9619-9624.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9619-9624
    • Swanson, K.1
  • 41
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K, et al. 2010. Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 402:372-379.
    • (2010) Virology , vol.402 , pp. 372-379
    • Swanson, K.1
  • 42
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi K, Compans RW. 1996. Functional interaction of paramyxovirus glycoproteins: identification of a domain in Sendai virus HN which promotes cell fusion. J. Virol. 70:6112-6118.
    • (1996) J. Virol. , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 43
    • 0032865298 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion
    • Taylor GM, Sanders DA. 1999. The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion. Mol. Biol. Cell 10:2803-2815.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2803-2815
    • Taylor, G.M.1    Sanders, D.A.2
  • 44
    • 0036400002 scopus 로고    scopus 로고
    • Regulation of fusion activity by the cytoplasmic domain of a paramyxovirus F protein
    • Tong S, et al. 2002. Regulation of fusion activity by the cytoplasmic domain of a paramyxovirus F protein. Virology 301:322-333.
    • (2002) Virology , vol.301 , pp. 322-333
    • Tong, S.1
  • 45
    • 0034853335 scopus 로고    scopus 로고
    • Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface
    • Tsurudome M, et al. 2001. Hemagglutinin-neuraminidase-independent fusion activity of simian virus 5 fusion (F) protein: difference in conformation between fusogenic and nonfusogenic F proteins on the cell surface. J. Virol. 75:8999-9009.
    • (2001) J. Virol. , vol.75 , pp. 8999-9009
    • Tsurudome, M.1
  • 46
    • 0028850294 scopus 로고
    • Identification of regions on the hemagglutininneuraminidase protein of human parainfluenza virus type 2 important for promoting cell fusion
    • Tsurudome M, et al. 1995. Identification of regions on the hemagglutininneuraminidase protein of human parainfluenza virus type 2 important for promoting cell fusion. Virology 213:190-203.
    • (1995) Virology , vol.213 , pp. 190-203
    • Tsurudome, M.1
  • 47
    • 1642430785 scopus 로고    scopus 로고
    • An oligosaccharide at the C terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion
    • Wang Z, Mirza AM, Li J, Mahon PJ, Iorio RM. 2004. An oligosaccharide at the C terminus of the F-specific domain in the stalk of the human parainfluenza virus 3 hemagglutinin-neuraminidase modulates fusion. Virus Res. 99:177-185.
    • (2004) Virus Res. , vol.99 , pp. 177-185
    • Wang, Z.1    Mirza, A.M.2    Li, J.3    Mahon, P.J.4    Iorio, R.M.5
  • 48
    • 3042550474 scopus 로고    scopus 로고
    • Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
    • Waning DL, Russell CJ, Jardetzky TS, Lamb RA. 2004. Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail. Proc. Natl. Acad. Sci. U. S. A. 101:9217-9222.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 9217-9222
    • Waning, D.L.1    Russell, C.J.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 49
    • 0036720806 scopus 로고    scopus 로고
    • Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5
    • Waning DL, Schmitt AP, Leser GP, Lamb RA. 2002. Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5. J. Virol. 76:9284-9297.
    • (2002) J. Virol. , vol.76 , pp. 9284-9297
    • Waning, D.L.1    Schmitt, A.P.2    Leser, G.P.3    Lamb, R.A.4
  • 50
    • 0034801792 scopus 로고    scopus 로고
    • Mutations within the putative membrane-spanning domain in the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity
    • West JT, Johnston PB, Dubay SR, Hunter E. 2001. Mutations within the putative membrane-spanning domain in the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity. J. Virol. 75:9601-9612.
    • (2001) J. Virol. , vol.75 , pp. 9601-9612
    • West, J.T.1    Johnston, P.B.2    Dubay, S.R.3    Hunter, E.4
  • 51
    • 0029998948 scopus 로고    scopus 로고
    • Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain
    • Wilk T, Pfeiffer T, Bukovsky AA, Moldenhauer G, Bosch V. 1996. Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain. Virology 218:269-274.
    • (1996) Virology , vol.218 , pp. 269-274
    • Wilk, T.1    Pfeiffer, T.2    Bukovsky, A.A.3    Moldenhauer, G.4    Bosch, V.5
  • 53
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS. 2006. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 54
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutininneuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, et al. 2011. Structure of the Newcastle disease virus hemagglutininneuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc. Natl. Acad. Sci. U. S. A. 108:14920-14925.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 14920-14925
    • Yuan, P.1
  • 55
    • 0031583818 scopus 로고    scopus 로고
    • Proper spacing between heptad repeat B and the transmembrane domain boundary of the paramyxovirus SV5 F protein is critical for biological activity
    • Zhou J, Dutch RE, Lamb RA. 1997. Proper spacing between heptad repeat B and the transmembrane domain boundary of the paramyxovirus SV5 F protein is critical for biological activity. Virology 239:327-339.
    • (1997) Virology , vol.239 , pp. 327-339
    • Zhou, J.1    Dutch, R.E.2    Lamb, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.