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Volumn 42, Issue 12, 2003, Pages 3527-3535

Synthesis, enhanced fusogenicity, and solid state NMR measurements of cross-linked HIV-1 fusion peptides

Author keywords

[No Author keywords available]

Indexed keywords

ENHANCED FUSOGENICITY;

EID: 0037379448     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027052g     Document Type: Article
Times cited : (36)

References (71)
  • 3
    • 0034705288 scopus 로고    scopus 로고
    • Cell biology of virus entry
    • Dimitrov, D. S. (2000) Cell biology of virus entry, Cell 101, 697-702.
    • (2000) Cell , vol.101 , pp. 697-702
    • Dimitrov, D.S.1
  • 4
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and Kim, P. S. (2001) Mechanisms of viral membrane fusion and its inhibition, Annu. Rev. Biochem. 70, 777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 5
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell, S. R., Martin, I., Ruysschaert, J. M., Shai, Y., and Blumenthal, R. (1997) What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion (review), Mol. Membr. Biol. 14, 97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.M.3    Shai, Y.4    Blumenthal, R.5
  • 6
    • 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., and Epand, R. M. (1999) The ectodomain of HA2 of influenza virus promotes rapid pH dependent membrane fusion, J. Mol. Biol. 286, 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
  • 7
    • 0034700998 scopus 로고    scopus 로고
    • The polar region consecutive to the HIV fusion peptide participates in membrane fusion
    • Peisajovich, S. G., Epand, R. F., Pritsker, M., Shai, Y., and Epand, R. M. (2000) The polar region consecutive to the HIV fusion peptide participates in membrane fusion, Biochemistry 39, 1826-1833.
    • (2000) Biochemistry , vol.39 , pp. 1826-1833
    • Peisajovich, S.G.1    Epand, R.F.2    Pritsker, M.3    Shai, Y.4    Epand, R.M.5
  • 8
    • 0034628898 scopus 로고    scopus 로고
    • Paramyxovirus F1 protein has two fusion peptides: Implications for the mechanism of membrane fusion
    • Peisajovich, S. G., Samuel, O., and Shai, Y. (2000) Paramyxovirus F1 protein has two fusion peptides: implications for the mechanism of membrane fusion, J. Mol. Biol. 296, 1353-1365.
    • (2000) J. Mol. Biol. , vol.296 , pp. 1353-1365
    • Peisajovich, S.G.1    Samuel, O.2    Shai, Y.3
  • 9
    • 0033869815 scopus 로고    scopus 로고
    • Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: Putative role during viral fusion
    • Suarez, T., Gallaher, W. R., Agirre, A., Goni, F. M., and Nieva, J. L. (2000) Membrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusion, J. Virol. 74, 8038-8047.
    • (2000) J. Virol. , vol.74 , pp. 8038-8047
    • Suarez, T.1    Gallaher, W.R.2    Agirre, A.3    Goni, F.M.4    Nieva, J.L.5
  • 10
    • 0037046147 scopus 로고    scopus 로고
    • The HIV-1 gp41 N-terminal heptad repeat plays an essential role in membrane fusion
    • Sackett, K., and Shai, Y. (2002) The HIV-1 gp41 N-terminal heptad repeat plays an essential role in membrane fusion, Biochemistry 41, 4678-4685.
    • (2002) Biochemistry , vol.41 , pp. 4678-4685
    • Sackett, K.1    Shai, Y.2
  • 11
    • 0025297179 scopus 로고
    • Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41
    • Freed, E. O., Myers, D. J., and Risser, R. (1990) Characterization of the fusion domain of the human immunodeficiency virus type 1 envelope glycoprotein gp41, Proc. Natl. Acad. Sci. U.S.A. 87, 4650-4654.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4650-4654
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 12
    • 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. L., Jr., and Panganiban, A. T. (1992) A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity, Proc. Natl. Acad. Sci. U.S.A. 89, 70-74.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 70-74
    • Freed, E.O.1    Delwart, E.L.2    Buchschacher G.L., Jr.3    Panganiban, A.T.4
  • 13
    • 0029062097 scopus 로고
    • Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion
    • Schaal, H., Klein, M., Gehrmann, P., Adams, O., and Scheid, A. (1995) Requirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusion, J. Virol. 69, 3308-3314.
    • (1995) J. Virol. , vol.69 , pp. 3308-3314
    • Schaal, H.1    Klein, M.2    Gehrmann, P.3    Adams, O.4    Scheid, A.5
  • 14
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: Identification of critical glycine residues
    • Delahunty, M. D., Rhee, I., Freed, E. O., and Bonifacino, J. S. (1996) Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1: identification of critical glycine residues, Virology 218, 94-102.
    • (1996) Virology , vol.218 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3    Bonifacino, J.S.4
  • 15
    • 0037926157 scopus 로고    scopus 로고
    • Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion
    • Pecheur, E., Sainte-Marie, J., Bienvenue, A., and Hoekstra, D. (1999) Peptides and membrane fusion: towards an understanding of the molecular mechanism of protein-induced fusion, J. Membr. Biol. 167, 1-17.
    • (1999) J. Membr. Biol. , vol.167 , pp. 1-17
    • Pecheur, E.1    Sainte-Marie, J.2    Bienvenue, A.3    Hoekstra, D.4
  • 16
    • 0025050505 scopus 로고
    • Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41
    • Rafalski, M., Lear, J. D., and DeGrado, W. F. (1990) Phospholipid interactions of synthetic peptides representing the N-terminus of HIV gp41, Biochemistry 29, 7917-7922.
    • (1990) Biochemistry , vol.29 , pp. 7917-7922
    • Rafalski, M.1    Lear, J.D.2    DeGrado, W.F.3
  • 19
    • 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., and Wilschut, J. (1994) Interaction of the HIV-1 fusion peptide with phospholipid vesicles: different structural requirements for fusion and leakage, Biochemistry 33, 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
  • 21
    • 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., and Ruysschaert, J. M. (1996) 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, 298-304.
    • (1996) J. Virol. , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.M.4
  • 22
    • 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., and Shai, Y. (1997) 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, 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
  • 23
    • 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 effects
    • Pereira, F. B., Goni, F. M., Muga, A., and Nieva, J. L. (1997) Permeabilization and fusion of uncharged lipid vesicles induced by the HIV-1 fusion peptide adopting an extended conformation: dose and sequence effects, Biophys. J. 73, 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
  • 24
    • 0031861456 scopus 로고    scopus 로고
    • Destabilization and fusion of zwitterionic large unilamellar lipid vesicles induced by a beta-type structure of the HIV-1 fusion peptide
    • Nieva, J. L., Nir, S., and Wilschut, J. (1998) Destabilization and fusion of zwitterionic large unilamellar lipid vesicles induced by a beta-type structure of the HIV-1 fusion peptide, J. Liposome Res. 8, 165-182.
    • (1998) J. Liposome Res. , vol.8 , pp. 165-182
    • Nieva, J.L.1    Nir, S.2    Wilschut, J.3
  • 25
    • 0033621026 scopus 로고    scopus 로고
    • Effect of nonpolar substitutions of the conserved Phe1-1 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes
    • Pritsker, M., Rucker, J., Hoffman, T. L., Doms, R. W., and Shai, Y. (1999) Effect of nonpolar substitutions of the conserved Phe1-1 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes, Biochemistry 38, 11359-11371.
    • (1999) Biochemistry , vol.38 , pp. 11359-11371
    • Pritsker, M.1    Rucker, J.2    Hoffman, T.L.3    Doms, R.W.4    Shai, Y.5
  • 26
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P. A., Hughson, F. M., Skehel, J. J., and Wiley, D. C. (1994) Structure of influenza haemagglutinin at the pH of membrane fusion, Nature 371, 37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 27
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan, D. C., Fass, D., Berger, J. M., and Kim, P. S. (1997) Core structure of gp41 from the HIV envelope glycoprotein, Cell 89, 263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 29
    • 0030780614 scopus 로고    scopus 로고
    • Atomic structure of a thermostable subdomain of HIV-1 gp41
    • Tan, K., Liu, J., Wang, J., Shen, S., and Lu, M. (1997) Atomic structure of a thermostable subdomain of HIV-1 gp41, Proc. Natl. Acad. Sci. U.S.A. 94, 12303-12308.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12303-12308
    • Tan, K.1    Liu, J.2    Wang, J.3    Shen, S.4    Lu, M.5
  • 32
  • 33
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and Kim, P. S. (1993) A spring-loaded mechanism for the conformational change of influenza hemagglutinin, Cell 73, 823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 34
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., Skehel, J. J., and Wiley, D. C. (1981) Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution, Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 35
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz, J. (2000) Membrane fusion mediated by coiled coils: a hypothesis, Biophys. J. 78, 886-900.
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 36
    • 0034031590 scopus 로고    scopus 로고
    • Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion
    • Bentz, J. (2000) Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion, Biophys. J. 78, 227-245.
    • (2000) Biophys. J. , vol.78 , pp. 227-245
    • Bentz, J.1
  • 37
    • 0028111660 scopus 로고
    • Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120
    • Kang, C. Y., Hariharan, K., Nara, P. L., Sodroski, J., and Moore, J. P. (1994) Immunization with a soluble CD4-gp120 complex preferentially induces neutralizing anti-human immunodeficiency virus type 1 antibodies directed to conformation-dependent epitopes of gp120, J. Virol. 68, 5854-5862.
    • (1994) J. Virol. , vol.68 , pp. 5854-5862
    • Kang, C.Y.1    Hariharan, K.2    Nara, P.L.3    Sodroski, J.4    Moore, J.P.5
  • 38
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong, P. D., Wyatt, R., Robinson, J., Sweet, R. W., Sodroski, J., and Hendrickson, W. A. (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody, Nature 393, 648-659.
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 39
    • 0038065763 scopus 로고    scopus 로고
    • Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41
    • Munoz-Barroso, I., Durell, S., Sakaguchi, K., Appella, E., and Blumenthal, R. (1998) Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41, J. Cell Biol. 140, 315-323.
    • (1998) J. Cell Biol. , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 40
    • 0030841309 scopus 로고    scopus 로고
    • The aminoterminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface
    • Chang, D. K., Cheng, S. F., and Chien, W. J. (1997) The aminoterminal fusion domain peptide of human immunodeficiency virus type 1 gp41 inserts into the sodium dodecyl sulfate micelle primarily as a helix with a conserved glycine at the micelle-water interface, J. Virol. 71, 6593-6602.
    • (1997) J. Virol. , vol.71 , pp. 6593-6602
    • Chang, D.K.1    Cheng, S.F.2    Chien, W.J.3
  • 41
    • 0039256708 scopus 로고    scopus 로고
    • Structure analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin
    • Glaser, R. W., Grune, M., Wandelt, C., and Ulrich, A. S. (1999) Structure analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin, Biochemistry 38, 2560-2569.
    • (1999) Biochemistry , vol.38 , pp. 2560-2569
    • Glaser, R.W.1    Grune, M.2    Wandelt, C.3    Ulrich, A.S.4
  • 42
    • 0033024286 scopus 로고    scopus 로고
    • The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids
    • Curtain, C., Separovic, F., Nielsen, K., Craik, D., Zhong, Y., and Kirkpatrick, A. (1999) The interactions of the N-terminal fusogenic peptide of HIV-1 gp41 with neutral phospholipids, Eur. Biophys. J. 28, 427-436.
    • (1999) Eur. Biophys. J. , vol.28 , pp. 427-436
    • Curtain, C.1    Separovic, F.2    Nielsen, K.3    Craik, D.4    Zhong, Y.5    Kirkpatrick, A.6
  • 43
    • 0040952847 scopus 로고    scopus 로고
    • Oblique membrane insertion of viral fusion peptide probed by neutron diffraction
    • Bradshaw, J. P., Darkes, M. J., Harroun, T. A., Katsaras, J., and Epand, R. M. (2000) Oblique membrane insertion of viral fusion peptide probed by neutron diffraction, Biochemistry 39, 6581-6585.
    • (2000) Biochemistry , vol.39 , pp. 6581-6585
    • Bradshaw, J.P.1    Darkes, M.J.2    Harroun, T.A.3    Katsaras, J.4    Epand, R.M.5
  • 44
    • 0034666555 scopus 로고    scopus 로고
    • Structure of a fusion peptide analogue at the air-water interface, determined from surface activity, infrared spectroscopy, and scanning force microscopy
    • Taylor, S. E., Desbat, B., Blaudez, D., Jacobi, S., Chi, L. F., Fuchs, H., and Schwarz, G. (2000) Structure of a fusion peptide analogue at the air-water interface, determined from surface activity, infrared spectroscopy, and scanning force microscopy, Biophys. Chem. 87, 63-72.
    • (2000) Biophys. Chem. , vol.87 , pp. 63-72
    • Taylor, S.E.1    Desbat, B.2    Blaudez, D.3    Jacobi, S.4    Chi, L.F.5    Fuchs, H.6    Schwarz, G.7
  • 45
    • 0034671359 scopus 로고    scopus 로고
    • pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers
    • Han, X., and Tamm, L. K. (2000) pH-dependent self-association of influenza hemagglutinin fusion peptides in lipid bilayers, J. Mol. Biol. 304, 953-965.
    • (2000) J. Mol. Biol. , vol.304 , pp. 953-965
    • Han, X.1    Tamm, L.K.2
  • 46
    • 0035838516 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide
    • Yang, J., Gabrys, C. M., and Weliky, D. P. (2001) Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide, Biochemistry 40, 8126-8137.
    • (2001) Biochemistry , vol.40 , pp. 8126-8137
    • Yang, J.1    Gabrys, C.M.2    Weliky, D.P.3
  • 47
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han, X., Bushweller, J. H., Cafiso, D. S., and Tamm, L. K. (2001) Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin, Nat. Struct. Biol. 8, 715-720.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 48
    • 0035979369 scopus 로고    scopus 로고
    • Membrane interactions of mutated forms of the influenza fusion peptide
    • Epand, R. M., Epand, R. F., Martin, I., and Ruysschaert, J. M. (2001) Membrane interactions of mutated forms of the influenza fusion peptide, Biochemistry 40, 8800-8807.
    • (2001) Biochemistry , vol.40 , pp. 8800-8807
    • Epand, R.M.1    Epand, R.F.2    Martin, I.3    Ruysschaert, J.M.4
  • 49
    • 0037151005 scopus 로고    scopus 로고
    • Structural characterizations of fusion peptide analogues of influenza virus hemagglutinin-Implication of the necessity of a helixhinge-helix motif in fusion activity
    • Hsu, C. H., Wu, S. H., Chang, D. K., and Chen, C. P. (2002) Structural characterizations of fusion peptide analogues of influenza virus hemagglutinin-Implication of the necessity of a helixhinge-helix motif in fusion activity, J. Biol. Chem. 277, 22725-22733.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22725-22733
    • Hsu, C.H.1    Wu, S.H.2    Chang, D.K.3    Chen, C.P.4
  • 50
    • 0037084030 scopus 로고    scopus 로고
    • Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using C-13-enhanced Fourier transform infrared spectroscopy
    • Gordon, L. M., Mobley, P. W., Pilpa, R., Sherman, M. A., and Waring, A. J. (2002) Conformational mapping of the N-terminal peptide of HIV-1 gp41 in membrane environments using C-13-enhanced Fourier transform infrared spectroscopy, Biochim. Biophys. Acta 1559, 96-120.
    • (2002) Biochim. Biophys. Acta , vol.1559 , pp. 96-120
    • Gordon, L.M.1    Mobley, P.W.2    Pilpa, R.3    Sherman, M.A.4    Waring, A.J.5
  • 51
    • 0037136052 scopus 로고    scopus 로고
    • Conformational transitions of membrane-bound HIV-1 fusion peptide
    • Saez-Cirion, A., and Nieva, J. L. (2002) Conformational transitions of membrane-bound HIV-1 fusion peptide, Biochim. Biophys. Acta 1564, 57-65.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 57-65
    • Saez-Cirion, A.1    Nieva, J.L.2
  • 52
    • 0036931991 scopus 로고    scopus 로고
    • Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides
    • Yang, J., Parkanzky, P. D., Bodner, M. L., Duskin, C. G., and Weliky, D. P. (2002) Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides, J. Magn. Reson. 159, 101-110.
    • (2002) J. Magn. Reson. , vol.159 , pp. 101-110
    • Yang, J.1    Parkanzky, P.D.2    Bodner, M.L.3    Duskin, C.G.4    Weliky, D.P.5
  • 53
    • 0029665093 scopus 로고    scopus 로고
    • On the dynamics and confirmation of the HA2 domain of the influenza virus hemagglutinin
    • Kim, C. H., Macosko, J. C., Yu, Y. G., and Shin, Y. K. (1996) On the dynamics and confirmation of the HA2 domain of the influenza virus hemagglutinin, Biochemistry 35, 5359-5365.
    • (1996) Biochemistry , vol.35 , pp. 5359-5365
    • Kim, C.H.1    Macosko, J.C.2    Yu, Y.G.3    Shin, Y.K.4
  • 54
    • 0031576994 scopus 로고    scopus 로고
    • The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR
    • Macosko, J. C., Kim, C. H., and Shin, Y. K. (1997) The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR, J. Mol. Biol. 267, 1139-1148.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1139-1148
    • Macosko, J.C.1    Kim, C.H.2    Shin, Y.K.3
  • 55
    • 0032488623 scopus 로고    scopus 로고
    • The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin
    • Kim, C. H., Macosko, J. C., and Shin, Y. K. (1998) The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin, Biochemistry 37, 137-144.
    • (1998) Biochemistry , vol.37 , pp. 137-144
    • Kim, C.H.1    Macosko, J.C.2    Shin, Y.K.3
  • 56
    • 0034646448 scopus 로고    scopus 로고
    • Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin
    • LeDuc, D. L., Shin, Y. K., Epand, R. F., and Epand, R. M. (2000) Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin, Biochemistry 39, 2733-2739.
    • (2000) Biochemistry , vol.39 , pp. 2733-2739
    • LeDuc, D.L.1    Shin, Y.K.2    Epand, R.F.3    Epand, R.M.4
  • 57
    • 0035902438 scopus 로고    scopus 로고
    • The 1-127 HA2 construct of influenza virus hemagglutinin induces cell-cell hemifusion
    • Leikina, E., LeDuc, D. L., Macosko, J. C., Epand, R., Shin, Y. K., and Chernomordik, L. V. (2001) The 1-127 HA2 construct of influenza virus hemagglutinin induces cell-cell hemifusion, Biochemistry 40, 8378-8386.
    • (2001) Biochemistry , vol.40 , pp. 8378-8386
    • Leikina, E.1    LeDuc, D.L.2    Macosko, J.C.3    Epand, R.4    Shin, Y.K.5    Chernomordik, L.V.6
  • 58
    • 0035817232 scopus 로고    scopus 로고
    • Self-assembly of influenza hemagglutinin: Studies of ectodomain aggregation by in situ atomic force microscopy
    • Epand, R. F., Yip, C. M., Chernomordik, L. V., LeDuc, D. L., Shin, Y. K., and Epand, R. M. (2001) Self-assembly of influenza hemagglutinin: studies of ectodomain aggregation by in situ atomic force microscopy, Biochim. Biophys. Acta 1513, 167-175.
    • (2001) Biochim. Biophys. Acta , vol.1513 , pp. 167-175
    • Epand, R.F.1    Yip, C.M.2    Chernomordik, L.V.3    LeDuc, D.L.4    Shin, Y.K.5    Epand, R.M.6
  • 59
    • 0034700147 scopus 로고    scopus 로고
    • A host-guest system to study structure-function relationships of membrane fusion peptides
    • Han, X., and Tamm, L. K. (2000) A host-guest system to study structure-function relationships of membrane fusion peptides, Proc. Natl. Acad. Sci. U.S.A. 97, 13097-13102.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13097-13102
    • Han, X.1    Tamm, L.K.2
  • 60
    • 0027325411 scopus 로고
    • Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes
    • Aloia, R. C., Tian, H., and Jensen, F. C. (1993) Lipid composition and fluidity of the human immunodeficiency virus envelope and host cell plasma membranes, Proc. Natl. Acad. Sci. U.S.A. 90, 5181-5185.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 5181-5185
    • Aloia, R.C.1    Tian, H.2    Jensen, F.C.3
  • 61
    • 0021909644 scopus 로고
    • Production of large unilamellar vesicles by a rapid extrusion procedure-Characterization of size distribution, trapped volume, and ability to maintain a membrane-potential
    • Hope, M. J., Bally, M. B., Webb, G., and Cullis, P. R. (1985) Production of large unilamellar vesicles by a rapid extrusion procedure-Characterization of size distribution, trapped volume, and ability to maintain a membrane-potential, Biochim. Biophys. Acta 812, 55-65.
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 55-65
    • Hope, M.J.1    Bally, M.B.2    Webb, G.3    Cullis, P.R.4
  • 62
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., Hoekstra, D., and Pagano, R. E. (1981) Use of resonance energy transfer to monitor membrane fusion, Biochemistry 20, 4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 63
    • 45149145322 scopus 로고
    • Rotational-echo double-resonance NMR
    • Gullion, T., and Schaefer, J. (1989) Rotational-echo double-resonance NMR, J. Magn. Reson. 81, 196-200.
    • (1989) J. Magn. Reson. , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 65
    • 42649130559 scopus 로고
    • New, compensated Carr-Purcell sequences
    • Gullion, T., Baker, D. B., and Conradi, M. S. (1990) New, compensated Carr-Purcell sequences, J. Magn. Reson. 89, 479-484.
    • (1990) J. Magn. Reson. , vol.89 , pp. 479-484
    • Gullion, T.1    Baker, D.B.2    Conradi, M.S.3
  • 66
    • 0000734747 scopus 로고
    • Elimination of resonance offset effects in rotational-echo, double-resonance NMR
    • Gullion, T., and Schaefer, J. (1991) Elimination of resonance offset effects in rotational-echo, double-resonance NMR, J. Magn. Reson. 92, 439-442.
    • (1991) J. Magn. Reson. , vol.92 , pp. 439-442
    • Gullion, T.1    Schaefer, J.2
  • 67
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D. S., Sykes, B. D., and Richards, F. M. (1991) Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 68
    • 0033605369 scopus 로고    scopus 로고
    • Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism
    • Chang, D. K., Cheng, S. F., and Trivedi, V. D. (1999) Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism, J. Biol. Chem. 274, 5299-5309.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5299-5309
    • Chang, D.K.1    Cheng, S.F.2    Trivedi, V.D.3
  • 69
    • 0345489104 scopus 로고    scopus 로고
    • unpublished experiments
    • Yang, J., and Weliky, D. P., unpublished experiments.
    • Yang, J.1    Weliky, D.P.2


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