메뉴 건너뛰기




Volumn 292, Issue 3, 1999, Pages 531-546

Direct evidence that the N-terminal heptad repeat of Sendai virus fusion protein participates in membrane fusion

Author keywords

Flourescence; Fusion peptide; Heptad repeat; Mechanism of membrane fusion; Sendai virus fusion protein

Indexed keywords

HEMAGGLUTININ; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL; VIRUS ENVELOPE PROTEIN; VIRUS FUSION PROTEIN;

EID: 0033600718     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3097     Document Type: Article
Times cited : (41)

References (95)
  • 1
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker K. A., Dutch R. E., Lamb R. A., Jardetzky T. S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell. 3:1999;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
  • 2
    • 70449246528 scopus 로고
    • Phosphorous assay in column chromatography
    • Bartlett G. R. Phosphorous assay in column chromatography. J. Biol. Chem. 234:1959;466-468.
    • (1959) J. Biol. Chem. , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 3
    • 0033555680 scopus 로고    scopus 로고
    • Membrane-induced step in the activation of Sendai virus fusion protein
    • Ben-Efraim I., Kliger Y., Hermesh C., Shai Y. Membrane-induced step in the activation of Sendai virus fusion protein. J. Mol. Biol. 285:1999;609-625.
    • (1999) J. Mol. Biol. , vol.285 , pp. 609-625
    • Ben-Efraim, I.1    Kliger, Y.2    Hermesh, C.3    Shai, Y.4
  • 6
    • 0024399763 scopus 로고
    • Identification of the fusion peptide of primate immunodeficiency viruses
    • Bosch M. L. Identification of the fusion peptide of primate immunodeficiency viruses. Science. 244:1989;694-696.
    • (1989) Science , vol.244 , pp. 694-696
    • Bosch, M.L.1
  • 7
    • 0025054302 scopus 로고
    • Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N terminus of viral fusion proteins
    • Brasseur R., Vandenbranden M., Cornet B., Burny A., Ruysschaert J. M. Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N terminus of viral fusion proteins. Biochim. Biophys. Acta, 1029:1990;267-273.
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 267-273
    • Brasseur, R.1    Vandenbranden, M.2    Cornet, B.3    Burny, A.4    Ruysschaert, J.M.5
  • 8
    • 0023657247 scopus 로고
    • Attenuated total reflectance fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines
    • Brauner J. W., Mendelson R., Prendergast F. G. Attenuated total reflectance fourier transform infrared studies of the interaction of melittin, two fragments of melittin, and δ-hemolysin with phosphatidylcholines. Biochemistry. 26:1987;8151-8158.
    • (1987) Biochemistry , vol.26 , pp. 8151-8158
    • Brauner, J.W.1    Mendelson, R.2    Prendergast, F.G.3
  • 9
    • 0026744238 scopus 로고
    • A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion
    • Buckland R., Malvoisin E., Beauverger P., Wild F. A leucine zipper structure present in the measles virus fusion protein is not required for its tetramerization but is essential for fusion. J. Gen. Virol. 73:1992;1703-1707.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1703-1707
    • Buckland, R.1    Malvoisin, E.2    Beauverger, P.3    Wild, F.4
  • 10
    • 0026662051 scopus 로고
    • Sequence analysis of gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins
    • Chambers P., Pringle C. R., Easton A. J. Sequence analysis of gene encoding the fusion glycoprotein of pneumonia virus of mice suggests possible conserved secondary structure elements in paramyxovirus fusion glycoproteins. J. Gen. Virol. 73:1992;1717-1724.
    • (1992) J. Gen. Virol. , vol.73 , pp. 1717-1724
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 11
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 the HIV envelope protein
    • Chan D. C., Fass D., Berger J. M., Kim P. S. Core structure of gp41 the HIV envelope protein. Cell. 89:1997;263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 12
    • 0027266886 scopus 로고
    • Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein
    • Chen S. S., Lee C. N., Lee W. R., McIntosh K., Lee T. H. Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. J. Virol. 67:1993;3615-3619.
    • (1993) J. Virol. , vol.67 , pp. 3615-3619
    • Chen, S.S.1    Lee, C.N.2    Lee, W.R.3    McIntosh, K.4    Lee, T.H.5
  • 13
    • 0031950368 scopus 로고    scopus 로고
    • Mutations in the leucine zipper-like heptad repeat sequence of human immunodeficiency virus type 1 gp41 dominantly interfere with wild-type virus infectivity
    • Chen S. S., Lee S. F., Hao H. J., Chuang C. K. Mutations in the leucine zipper-like heptad repeat sequence of human immunodeficiency virus type 1 gp41 dominantly interfere with wild-type virus infectivity. J. Virol. 72:1998;4765-4774.
    • (1998) J. Virol. , vol.72 , pp. 4765-4774
    • Chen, S.S.1    Lee, S.F.2    Hao, H.J.3    Chuang, C.K.4
  • 14
    • 0004250838 scopus 로고    scopus 로고
    • B.N. Fields, D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott-Raven Publishers
    • Collins P. L., Chanock R. M., Mcintosh K. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;1205-1241 Lippincott-Raven Publishers, Philadelphia.
    • (1996) Fields Virology , pp. 1205-1241
    • Collins, P.L.1    Chanock, R.M.2    McIntosh, K.3
  • 15
    • 0030010945 scopus 로고    scopus 로고
    • +induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino terminal fusion peptide but not the coiled coil region
    • +induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino terminal fusion peptide but not the coiled coil region. J. Biol. Chem. 271:1996;13417-13421.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Gluck, R.5    Vorherr, T.6    Brunner, J.7
  • 16
    • 0023657261 scopus 로고
    • Lipid mixing during membrane aggregation and fusion: Why fusion assays disagree
    • Duzgunes N., Allen T. M., Fedor J., Papahadjopoulos D. Lipid mixing during membrane aggregation and fusion: why fusion assays disagree. Biochemistry. 26:1987;8435-8442.
    • (1987) Biochemistry , vol.26 , pp. 8435-8442
    • Duzgunes, N.1    Allen, T.M.2    Fedor, J.3    Papahadjopoulos, D.4
  • 17
    • 0033582785 scopus 로고    scopus 로고
    • The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion
    • Epand R. F., Macosko J. C., Russell C. J., Shin Y. K., Epand R. M. The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion. J. Mol. Biol. 286:1999;489-503.
    • (1999) J. Mol. Biol. , vol.286 , pp. 489-503
    • Epand, R.F.1    MacOsko, J.C.2    Russell, C.J.3    Shin, Y.K.4    Epand, R.M.5
  • 18
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed E. O., Myers D. J., Risser R. Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41. Proc. Natl Acad. Sci. USA. 87:1990;4650-4654.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 19
    • 0026544416 scopus 로고
    • A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
    • Freed E. O., Delwart E. L., Buchschacher G. J., Panganiban A. T. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity. Proc. Natl Acad. Sci. USA. 89:1992;70-74.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher, G.J.3    Panganiban, A.T.4
  • 20
    • 0025647096 scopus 로고
    • Membrane insertion and lateral diffusion of fluorescence labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers
    • Frey S., Tamm L. K. Membrane insertion and lateral diffusion of fluorescence labelled cytochrome c oxidase subunit IV signal peptide in charged and uncharged phospholipid bilayers. Biochem. J. 272:1990;713-719.
    • (1990) Biochem. J. , vol.272 , pp. 713-719
    • Frey, S.1    Tamm, L.K.2
  • 21
    • 0025993413 scopus 로고
    • Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study
    • Frey S., Tamm L. K. Orientation of melittin in phospholipid bilayers. A polarized attenuated total reflection infrared study. Biophys. J. 60:1991;922-930.
    • (1991) Biophys. J. , vol.60 , pp. 922-930
    • Frey, S.1    Tamm, L.K.2
  • 23
    • 0027190573 scopus 로고
    • Structural and functional characterization of the α-5 segment of Bacillus thuringiensis delta-endotoxin
    • Gazit E., Shai Y. Structural and functional characterization of the α-5 segment of Bacillus thuringiensis delta-endotoxin. Biochemistry. 32:1993;3429-3436.
    • (1993) Biochemistry , vol.32 , pp. 3429-3436
    • Gazit, E.1    Shai, Y.2
  • 24
    • 0029873933 scopus 로고    scopus 로고
    • Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
    • Gazit E., Miller I. R., Biggin P. C., Sansom M. S. P., Shai Y. Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes. J. Mol. Biol. 258:1996;860-870.
    • (1996) J. Mol. Biol. , vol.258 , pp. 860-870
    • Gazit, E.1    Miller, I.R.2    Biggin, P.C.3    Sansom, M.S.P.4    Shai, Y.5
  • 25
    • 0001026829 scopus 로고
    • Purification of the fusion protein of Sendai virus: Analysis of the NH2-terminal sequence generated during precursor activation
    • Gething M. J., White J. M., Waterfield M. D. Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation. Proc. Natl Acad. Sci. USA. 75:1978;2737-2740.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 2737-2740
    • Gething, M.J.1    White, J.M.2    Waterfield, M.D.3
  • 26
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething M. J., Doms R. W., York D., White J. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:1986;11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 27
    • 0030714006 scopus 로고    scopus 로고
    • A leucine zipper motif in the ectodomain of Sendai virus fusion protein assembles in solution and in membranes and specifically binds biologically active peptides and the virus
    • Ghosh J. K., Ovadia M., Shai Y. A leucine zipper motif in the ectodomain of Sendai virus fusion protein assembles in solution and in membranes and specifically binds biologically active peptides and the virus. Biochemistry. 36:1997;15451-15462.
    • (1997) Biochemistry , vol.36 , pp. 15451-15462
    • Ghosh, J.K.1    Ovadia, M.2    Shai, Y.3
  • 28
    • 0032538618 scopus 로고    scopus 로고
    • Structure-function study of a heptad repeat positioned near the transmembrane domain of Sendai virus fusion protein which blocks virus-cell fusion
    • Ghosh J. K., Peisajovich S. G., Ovadia M., Shai Y. Structure-function study of a heptad repeat positioned near the transmembrane domain of Sendai virus fusion protein which blocks virus-cell fusion. J. Biol. Chem. 273:1998;27182-27190.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27182-27190
    • Ghosh, J.K.1    Peisajovich, S.G.2    Ovadia, M.3    Shai, Y.4
  • 30
    • 0025261733 scopus 로고
    • Membrane fusion of enveloped viruses: Especially a matter of proteins
    • Hoekstra D. Membrane fusion of enveloped viruses: especially a matter of proteins. J. Bioenerg. Biomembr. 22:1990;121.
    • (1990) J. Bioenerg. Biomembr. , vol.22 , pp. 121
    • Hoekstra, D.1
  • 31
    • 0015732097 scopus 로고
    • Trypsin action on the growth of sendai virus in tissue culture cells
    • Homma M., Ohuchi M. Trypsin action on the growth of sendai virus in tissue culture cells. J. Virol. 12:1973;1457-1465.
    • (1973) J. Virol. , vol.12 , pp. 1457-1465
    • Homma, M.1    Ohuchi, M.2
  • 33
    • 0026558240 scopus 로고
    • Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: Roles of conserved residues in cell fusion
    • Horvath C. M., Lamb R. A. Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion. J. Virol. 66:1992;2443-2455.
    • (1992) J. Virol. , vol.66 , pp. 2443-2455
    • Horvath, C.M.1    Lamb, R.A.2
  • 34
    • 0019826468 scopus 로고
    • Activation of the Sendai virus fusion protein involves a conformational change with exposure of a new hydrophobic domain
    • Hsu M. C., Scheid A., Choppin P. W. Activation of the Sendai virus fusion protein involves a conformational change with exposure of a new hydrophobic domain. J. Biol. Chem. 256:1981;3557-3563.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3557-3563
    • Hsu, M.C.1    Scheid, A.2    Choppin, P.W.3
  • 35
    • 0026525004 scopus 로고
    • Functional interactions between the fusion protein and hemagglutinin neuraminidase of human parainfluenza viruses
    • Hu X., Ray R., Compans R. W. Functional interactions between the fusion protein and hemagglutinin neuraminidase of human parainfluenza viruses. J. Virol. 66:1992;2443-2455.
    • (1992) J. Virol. , vol.66 , pp. 2443-2455
    • Hu, X.1    Ray, R.2    Compans, R.W.3
  • 36
    • 0027484593 scopus 로고
    • Orientation of fusion-active synthetic peptides in phospholipid bilayers: Determination by Fourier transform infrared spectroscopy
    • Ishiguro R., Kimura N., Takahashi S. Orientation of fusion-active synthetic peptides in phospholipid bilayers: determination by Fourier transform infrared spectroscopy. Biochemistry. 32:1993;9792-9797.
    • (1993) Biochemistry , vol.32 , pp. 9792-9797
    • Ishiguro, R.1    Kimura, N.2    Takahashi, S.3
  • 37
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M., Mantsch H. H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30:1995;95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 38
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi S. B., Dutch R. E., Lamb R. A. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology. 248:1998;20-34.
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 41
    • 0015237803 scopus 로고
    • A new fluorescent probe for protein and nucleoprotein conformation. Binding of 7-(p-methoxybenzylamino)-4-nitrobenzoxadiazole to bovine trypsinogen and bacterial ribosomes
    • Kenner R. A., Aboderin A. A. A new fluorescent probe for protein and nucleoprotein conformation. Binding of 7-(p-methoxybenzylamino)-4-nitrobenzoxadiazole to bovine trypsinogen and bacterial ribosomes. Biochemistry. 10:1971;4433-4440.
    • (1971) Biochemistry , vol.10 , pp. 4433-4440
    • Kenner, R.A.1    Aboderin, A.A.2
  • 43
    • 0031010455 scopus 로고    scopus 로고
    • Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion: Structure-function study
    • Kliger Y., Aharoni A., Rapaport D., Jones P., Blumenthal R., Shai Y. Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell fusion: structure-function study. J. Biol. Chem. 272:1997;13496-13505.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13496-13505
    • Kliger, Y.1    Aharoni, A.2    Rapaport, D.3    Jones, P.4    Blumenthal, R.5    Shai, Y.6
  • 44
    • 0027430672 scopus 로고
    • Paramyxovirus fusion: A hypothesis for changes
    • Lamb R. A. Paramyxovirus fusion: a hypothesis for changes. Virology. 197:1993;1-11.
    • (1993) Virology , vol.197 , pp. 1-11
    • Lamb, R.A.1
  • 45
    • 0004250845 scopus 로고    scopus 로고
    • B.N. Fields, D.M. Knipe, & P.M. Howley. Philadelphia: Lippincott-Raven Publishers
    • Lamb R. A., Kolakofsky D. Fields B. N., Knipe D. M., Howley P. M. Fields Virology. 1996;1117-1204 Lippincott-Raven Publishers, Philadelphia.
    • (1996) Fields Virology , pp. 1117-1204
    • Lamb, R.A.1    Kolakofsky, D.2
  • 47
    • 0029926552 scopus 로고    scopus 로고
    • HIV-1 membrane fusion mechanism: Structural studies of the interactions between biologically active peptides from gp41
    • Lawless M. K., Barney S., Guthrie K. I., Bucy T. B., Petteway S. R., Merutka G. HIV-1 membrane fusion mechanism: structural studies of the interactions between biologically active peptides from gp41. Biochemistry. 35:1996;13697-13708.
    • (1996) Biochemistry , vol.35 , pp. 13697-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway, S.R.5    Merutka, G.6
  • 48
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
    • Lear J. D., DeGrado W. F. Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2. J. Biol. Chem. 262:1987;6500-6505.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6500-6505
    • Lear, J.D.1    Degrado, W.F.2
  • 49
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu M., Blacklow S. C., Kim P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Stuct. Biol. 2:1995;1075-1082.
    • (1995) Nature Stuct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 52
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • Martin I., Schaal H., Scheid A., Ruysschaert J. M. Lipid membrane fusion induced by the human immunodeficiency virus type 1 gp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70:1996;298-304.
    • (1996) J. Virol. , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.M.4
  • 53
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin A (1-33)
    • Merrifield R. B., Vizioli L. D., Boman H. G. Synthesis of the antibacterial peptide cecropin A (1-33). Biochemistry. 21:1982;5020-5031.
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.B.1    Vizioli, L.D.2    Boman, H.G.3
  • 54
    • 0023423183 scopus 로고
    • PH-dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin
    • Murata M., Sugahara Y., Takahashi S., Ohnishi S. pH-dependent membrane fusion activity of a synthetic twenty amino acid peptide with the same sequence as that of the hydrophobic segment of influenza virus hemagglutinin. J. Biochem. 102:1987;957-962.
    • (1987) J. Biochem. , vol.102 , pp. 957-962
    • Murata, M.1    Sugahara, Y.2    Takahashi, S.3    Ohnishi, S.4
  • 55
    • 0028218423 scopus 로고
    • Interaction of the HIV-1 fusion peptide with phospholipid vesicles: Different structural requirements for fusion and leakage
    • Nieva J. L., Nir S., Muga A., Goni F. M., Wilschut J. Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage. Biochemistry. 33:1994;3201-3209.
    • (1994) Biochemistry , vol.33 , pp. 3201-3209
    • Nieva, J.L.1    Nir, S.2    Muga, A.3    Goni, F.M.4    Wilschut, J.5
  • 56
    • 0019331565 scopus 로고
    • Mass action kinetics of phosphatidylserine vesicle fusion as monitored by coalescence of internal vesicle volumes
    • Nir S., Bentz J., Wilschut J. Mass action kinetics of phosphatidylserine vesicle fusion as monitored by coalescence of internal vesicle volumes. Biochemistry. 19:1980;6030-6036.
    • (1980) Biochemistry , vol.19 , pp. 6030-6036
    • Nir, S.1    Bentz, J.2    Wilschut, J.3
  • 58
    • 0021744176 scopus 로고
    • Membrane-bound antiviral antibodies as receptors for Sendai virions in receptor-depleted erythrocytes
    • Nussbaum O., Zakai N., Loyter A. Membrane-bound antiviral antibodies as receptors for Sendai virions in receptor-depleted erythrocytes. Virology. 138:1984;185-197.
    • (1984) Virology , vol.138 , pp. 185-197
    • Nussbaum, O.1    Zakai, N.2    Loyter, A.3
  • 59
    • 0027164674 scopus 로고
    • Sendai virus-induced cell fusion
    • Okada Y. Sendai virus-induced cell fusion. Methods Enzymol. 221:1993;18-41.
    • (1993) Methods Enzymol. , vol.221 , pp. 18-41
    • Okada, Y.1
  • 60
    • 0025999791 scopus 로고
    • Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids
    • Pastrana B., Mautone A. J., Mendelsohn R. Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids. Biochemistry. 30:1991;10058-10064.
    • (1991) Biochemistry , vol.30 , pp. 10058-10064
    • Pastrana, B.1    Mautone, A.J.2    Mendelsohn, R.3
  • 61
    • 0342506479 scopus 로고    scopus 로고
    • Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: Dose and sequence effect
    • Pereira F. B., Goni F. M., Muga A., Nieva J. L. Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effect. Biophys. J. 73:1997;1977-1986.
    • (1997) Biophys. J. , vol.73 , pp. 1977-1986
    • Pereira, F.B.1    Goni, F.M.2    Muga, A.3    Nieva, J.L.4
  • 62
    • 0016173457 scopus 로고
    • Fusion of intact human erythrocytes and erythrocytes ghosts
    • Peretz H., Toister Z., Laster Y., Loyter A. Fusion of intact human erythrocytes and erythrocytes ghosts. J. Cell Biol. 63:1974;1-11.
    • (1974) J. Cell Biol. , vol.63 , pp. 1-11
    • Peretz, H.1    Toister, Z.2    Laster, Y.3    Loyter, A.4
  • 63
    • 0026787169 scopus 로고
    • Interaction of D -amino acid incorporated analogues of pardaxin with membranes
    • Pouny Y., Shai Y. Interaction of D -amino acid incorporated analogues of pardaxin with membranes. Biochemistry. 31:1992;9482-9490.
    • (1992) Biochemistry , vol.31 , pp. 9482-9490
    • Pouny, Y.1    Shai, Y.2
  • 64
    • 0032560463 scopus 로고    scopus 로고
    • A synthetic all D -amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion
    • Pritsker M., Jones P., Blumenthal R., Shai Y. A synthetic all D -amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion. Proc. Natl Acad. Sci. USA. 95:1998;7287-7292.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7287-7292
    • Pritsker, M.1    Jones, P.2    Blumenthal, R.3    Shai, Y.4
  • 65
    • 0028838458 scopus 로고
    • A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled coil formation
    • Rabenstein M., Shin Y. K. A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled coil formation. Biochemistry. 34:1995;13390-13397.
    • (1995) Biochemistry , vol.34 , pp. 13390-13397
    • Rabenstein, M.1    Shin, Y.K.2
  • 66
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski M., Lear J. D., DeGrado W. F. Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41. Biochemistry. 29:1990;7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    Degrado, W.F.3
  • 67
    • 0024594990 scopus 로고
    • Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes
    • Rajarathnam K., Hochman J., Schindler M., Ferguson M. S. Synthesis, location, and lateral mobility of fluorescently labeled ubiquinone 10 in mitochondrial and artificial membranes. Biochemistry. 28:1989;3168-3176.
    • (1989) Biochemistry , vol.28 , pp. 3168-3176
    • Rajarathnam, K.1    Hochman, J.2    Schindler, M.3    Ferguson, M.S.4
  • 68
    • 0026354984 scopus 로고
    • Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers
    • Rapaport D., Shai Y. Interaction of fluorescently labeled pardaxin and its analogues with lipid bilayers. J. Biol. Chem. 266:1991;23769-23775.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23769-23775
    • Rapaport, D.1    Shai, Y.2
  • 69
    • 0026758174 scopus 로고
    • Aggregation and organization of pardaxin in phospholipid membranes. A fluorescence energy transfer study
    • Rapaport D., Shai Y. Aggregation and organization of pardaxin in phospholipid membranes. A fluorescence energy transfer study. J. Biol. Chem. 267:1992;6502-6509.
    • (1992) J. Biol. Chem. , vol.267 , pp. 6502-6509
    • Rapaport, D.1    Shai, Y.2
  • 70
    • 0028306273 scopus 로고
    • Interaction of fluorescently labeled analogues of the amino terminal fusion peptide of Sendai virus with phospholipid membranes
    • Rapaport D., Shai Y. Interaction of fluorescently labeled analogues of the amino terminal fusion peptide of Sendai virus with phospholipid membranes. J. Biol. Chem. 269:1994;15124-15131.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15124-15131
    • Rapaport, D.1    Shai, Y.2
  • 71
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport D., Ovadia M., Shai Y. A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of Sendai virus-cell fusion: an emerging similarity with functional domains of other viruses. EMBO J. 14:1995;5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 72
    • 0029132009 scopus 로고
    • Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein
    • Reitter J. N., Sergel T., Morrison T. G. Mutational analysis of the leucine zipper motif in the Newcastle disease virus fusion protein. J. Virol. 69:1995;5995-6004.
    • (1995) J. Virol. , vol.69 , pp. 5995-6004
    • Reitter, J.N.1    Sergel, T.2    Morrison, T.G.3
  • 73
    • 0018347397 scopus 로고
    • Anomalous amide I infrared absorption of purple membrane
    • Rothschild K. J., Clark N. A. Anomalous amide I infrared absorption of purple membrane. Science. 204:1979;311-312.
    • (1979) Science , vol.204 , pp. 311-312
    • Rothschild, K.J.1    Clark, N.A.2
  • 74
    • 0015990842 scopus 로고
    • Identification of the biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus
    • Scheid A., Choppin P. W. Identification of the biological activities of paramyxovirus glycoproteins. Activation of cell fusion, hemolysis and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology. 50:1974;475-490.
    • (1974) Virology , vol.50 , pp. 475-490
    • Scheid, A.1    Choppin, P.W.2
  • 75
    • 0017404533 scopus 로고
    • Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses
    • Scheid A., Choppin P. W. Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology. 80:1977;54-60.
    • (1977) Virology , vol.80 , pp. 54-60
    • Scheid, A.1    Choppin, P.W.2
  • 76
    • 0015449722 scopus 로고
    • Isolation of paramyxovirus glycoproteins. Association of hemagglutinating and neuraminidase activities with larger SV5 glycoprotein
    • Scheid A., Caliguiri L. A., Compans R. W., Choppin P. W. Isolation of paramyxovirus glycoproteins. Association of hemagglutinating and neuraminidase activities with larger SV5 glycoprotein. Virology. 50:1972;640.
    • (1972) Virology , vol.50 , pp. 640
    • Scheid, A.1    Caliguiri, L.A.2    Compans, R.W.3    Choppin, P.W.4
  • 77
    • 0027286406 scopus 로고
    • The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation
    • Sergel T., McGinnes M. E., Peeples M. E., Morrison T. The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation. Virology. 193:1993;717-726.
    • (1993) Virology , vol.193 , pp. 717-726
    • Sergel, T.1    McGinnes, M.E.2    Peeples, M.E.3    Morrison, T.4
  • 78
    • 0028116668 scopus 로고
    • Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion
    • Sergel Germano T., McQuain C., Morrison T. Mutations in the fusion peptide and heptad repeat regions of the Newcastle disease virus fusion protein block fusion. J. Virol. 68:1994;7654-7658.
    • (1994) J. Virol. , vol.68 , pp. 7654-7658
    • Sergel Germano, T.1    McQuain, C.2    Morrison, T.3
  • 79
    • 0025245504 scopus 로고
    • Channel formation properties of synthetic pardaxin and analogues
    • Shai Y., Bach D., Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 265:1990;20202-20209.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20202-20209
    • Shai, Y.1    Bach, D.2    Yanovsky, A.3
  • 80
    • 0025748640 scopus 로고
    • PH-dependent pore formation properties of pardaxin analogues
    • Shai Y., Hadari Y. R., Finkels A. pH-dependent pore formation properties of pardaxin analogues. J. Biol. Chem. 266:1991;22346-22354.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22346-22354
    • Shai, Y.1    Hadari, Y.R.2    Finkels, A.3
  • 81
    • 0029964418 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41
    • Shugars D. C., Wild C. T., Greenwell T. K., Matthews T. J. Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 70:1996;2982-2991.
    • (1996) J. Virol. , vol.70 , pp. 2982-2991
    • Shugars, D.C.1    Wild, C.T.2    Greenwell, T.K.3    Matthews, T.J.4
  • 84
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck D. K., Hoekstra D., Pagano R. E. Use of resonance energy transfer to monitor membrane fusion. Biochemistry. 20:1981;4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 85
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm L. K., Tatulian S. A. Infrared spectroscopy of proteins and peptides in lipid bilayers. Quart. Rev. Biophys. 30:1997;365-429.
    • (1997) Quart. Rev. Biophys. , vol.30 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 87
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White J. M. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:1990;75-97.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 75-97
    • White, J.M.1
  • 88
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild C., Oas T., McDanal C., Bolognesi D., Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl Acad. Sci. USA. 89:1992;10537-10541.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 89
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 are potent inhibitors of virus infection
    • Wild C. T., Shugars D. C., Greenwell T. K., McDanal C. B., Matthews T. J. Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 are potent inhibitors of virus infection. Proc. Natl Acad. Sci. USA. 91:1994;9770-9774.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 9770-9774
    • Wild, C.T.1    Shugars, D.C.2    Greenwell, T.K.3    McDanal, C.B.4    Matthews, T.J.5
  • 90
    • 0028953212 scopus 로고
    • The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure
    • Wild C., Greenwell T., Shugars D., Rimsky-Clarke L., Matthews T. The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. AIDS Res. Human Retroviruses. 11:1995;323-325.
    • (1995) AIDS Res. Human Retroviruses , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 91
    • 0019871847 scopus 로고
    • Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution
    • Wu C. S. C., Ikeda K., Yang J. T. Ordered conformation of polypeptides and proteins in acidic dodecyl sulfate solution. Biochemistry. 20:1981;566-570.
    • (1981) Biochemistry , vol.20 , pp. 566-570
    • Wu, C.S.C.1    Ikeda, K.2    Yang, J.T.3
  • 92
    • 0016744248 scopus 로고
    • The major cell surfac glycoprotein of chick embryo fibroblasts is an agglutinin
    • Yamada K. M., Yamada S. S., Pastan I. The major cell surfac glycoprotein of chick embryo fibroblasts is an agglutinin. Proc. Natl Acad. Sci. USA. 72:1975;3158-3162.
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 3158-3162
    • Yamada, K.M.1    Yamada, S.S.2    Pastan, I.3
  • 93
    • 0023667423 scopus 로고
    • Polarized attenuated total reflectance spectra of oriented purple membranes
    • Yang P. W., Stewart L. C., Mantsch H. H. Polarized attenuated total reflectance spectra of oriented purple membranes. Biochem. Biophys. Res. Commun. 145:1987;298-302.
    • (1987) Biochem. Biophys. Res. Commun. , vol.145 , pp. 298-302
    • Yang, P.W.1    Stewart, L.C.2    Mantsch, H.H.3
  • 94
    • 0027967960 scopus 로고
    • Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
    • Yu Y. G., King D. S., Shin Y.-K. Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes. Science. 266:1994;274-276.
    • (1994) Science , vol.266 , pp. 274-276
    • Yu, Y.G.1    King, D.S.2    Shin, Y.-K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.