메뉴 건너뛰기




Volumn 78, Issue 6, 2004, Pages 2808-2818

Structural and Functional Properties of an Unusual Internal Fusion Peptide in a Nonenveloped Virus Membrane Fusion Protein

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; GLYCINE; HYBRID PROTEIN; LIPOSOME; PROTEIN P10; VIRUS PROTEIN;

EID: 1542287540     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.6.2808-2818.2004     Document Type: Article
Times cited : (40)

References (62)
  • 1
    • 0028815675 scopus 로고
    • Mutational evidence for an internal fusion peptide in flavivirus envelope protein E
    • Allison, S. L., J. Schalich, K. Stiasny, C. W. Mandl, C. Kunz, and F. X. Heinz. 1995. Mutational evidence for an internal fusion peptide in flavivirus envelope protein E. J. Virol. 69:695-700.
    • (1995) J. Virol. , vol.69 , pp. 695-700
    • Allison, S.L.1    Schalich, J.2    Stiasny, K.3    Mandl, C.W.4    Kunz, C.5    Heinz, F.X.6
  • 2
    • 0033572639 scopus 로고    scopus 로고
    • Identification of an anti-mycobacterial domain in NK-lysin and granulysin
    • Andreu, D., C. Carreno, C. Linde, H. G. Boman, and M. Andersson. 1999. Identification of an anti-mycobacterial domain in NK-lysin and granulysin. Biochem. J. 344:845-849.
    • (1999) Biochem. J. , vol.344 , pp. 845-849
    • Andreu, D.1    Carreno, C.2    Linde, C.3    Boman, H.G.4    Andersson, M.5
  • 4
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker, K. A., R. E. Dutch, R. A. Lamb, and T. S. Jardetzky. 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
  • 5
    • 0034109366 scopus 로고    scopus 로고
    • Mutational analysis of the subgroup A avian sarcoma and leukosis virus putative fusion peptide domain
    • Balliet, J. W., K. Gendron, and P. Bates. 2000. Mutational analysis of the subgroup A avian sarcoma and leukosis virus putative fusion peptide domain. J. Virol. 74:3731-3739.
    • (2000) J. Virol. , vol.74 , pp. 3731-3739
    • Balliet, J.W.1    Gendron, K.2    Bates, P.3
  • 6
    • 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. 78:886-900.
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 7
    • 0016752682 scopus 로고
    • Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components
    • Blobel, G., and B. Dobberstein. 1975. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67:852-862.
    • (1975) J. Cell Biol. , vol.67 , pp. 852-862
    • Blobel, G.1    Dobberstein, B.2
  • 8
    • 0037124077 scopus 로고    scopus 로고
    • Modification of late membrane permeability in avian reovirus-infected cells
    • Bodelon, G., L. Labrada, J. Martinez-Costas, and J. Benavente. 2002. Modification of late membrane permeability in avian reovirus-infected cells. J. Biol. Chem. 277:17789-17796.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17789-17796
    • Bodelon, G.1    Labrada, L.2    Martinez-Costas, J.3    Benavente, J.4
  • 9
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 10
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA 94:14306-14316.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14306-14316
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 13
    • 0033809570 scopus 로고    scopus 로고
    • Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leucosis virus envelope glycoprotein
    • Delos, S. E., and J. M. White. 2000. Critical role for the cysteines flanking the internal fusion peptide of avian sarcoma/leucosis virus envelope glycoprotein. J. Virol. 74:9738-9741.
    • (2000) J. Virol. , vol.74 , pp. 9738-9741
    • Delos, S.E.1    White, J.M.2
  • 14
    • 0033947260 scopus 로고    scopus 로고
    • The central proline of an internal viral fusion peptide serves two important roles
    • Delos, S. E., J. M. Gilbert, and J. M. White. 2000. The central proline of an internal viral fusion peptide serves two important roles. J. Virol. 74:1686-1693.
    • (2000) J. Virol. , vol.74 , pp. 1686-1693
    • Delos, S.E.1    Gilbert, J.M.2    White, J.M.3
  • 15
    • 0033179264 scopus 로고    scopus 로고
    • Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: A species proposal
    • Duncan, R. 1999. Extensive sequence divergence and phylogenetic relationships between the fusogenic and nonfusogenic orthoreoviruses: a species proposal. Virology 260:316-328.
    • (1999) Virology , vol.260 , pp. 316-328
    • Duncan, R.1
  • 16
    • 0030588265 scopus 로고    scopus 로고
    • Avian reovirus-induced syncytium formation is independent of infectious progeny virus production and enhances the rate, but is not essential, for virus-induced cytopathology and virus egress
    • Duncan, R., Z. Chen, S. Walsh, and S. Wu. 1996. Avian reovirus-induced syncytium formation is independent of infectious progeny virus production and enhances the rate, but is not essential, for virus-induced cytopathology and virus egress. Virology 224:453-464.
    • (1996) Virology , vol.224 , pp. 453-464
    • Duncan, R.1    Chen, Z.2    Walsh, S.3    Wu, S.4
  • 17
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell, S. R., I. Martin, J. M. Ruysschaert, Y. Shai, and R. Blumenthal. 1997. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. 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
  • 18
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 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
  • 20
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. 1984. Three-dimensional structure of membrane and surface proteins. Annu. Rev. Biochem. 53:595-623.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 21
    • 0035968172 scopus 로고    scopus 로고
    • The omega-loop region of the human prothrombin gamma-carboxyglutamic
    • Falls, L. A., B. C. Furie, M. Jacobs, B. Furie, and A. C. Rigby. 2001. The omega-loop region of the human prothrombin gamma-carboxyglutamic. J. Biol. Chem. 276:23895-23902.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23895-23902
    • Falls, L.A.1    Furie, B.C.2    Jacobs, M.3    Furie, B.4    Rigby, A.C.5
  • 22
    • 0030591276 scopus 로고    scopus 로고
    • Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses
    • Gallaher, W. R. 1996. Similar structural models of the transmembrane proteins of Ebola and avian sarcoma viruses. Cell 17:477-478.
    • (1996) Cell , vol.17 , pp. 477-478
    • Gallaher, W.R.1
  • 23
    • 0035909081 scopus 로고    scopus 로고
    • Solution structure of PAFP-S: A new knottin-type anti-fungal peptide from the seeds of Phytolacca americana
    • Gao, G. H., W. Liu, J. X. Dai, J. F. Wang, Z. Hu, Y. Zhang, and D. C. Wang. 2001. Solution structure of PAFP-S: a new knottin-type anti-fungal peptide from the seeds of Phytolacca americana. Biochemistry 40:10973-10978.
    • (2001) Biochemistry , vol.40 , pp. 10973-10978
    • Gao, G.H.1    Liu, W.2    Dai, J.X.3    Wang, J.F.4    Hu, Z.5    Zhang, Y.6    Wang, D.C.7
  • 24
    • 0032930505 scopus 로고    scopus 로고
    • Mutations in the glycoprotein of viral haemorrhagic septicaemia virus that affect virulence for fish and the pH threshold for membrane fusion
    • Gaudin, Y., P. de Kinkelin, and A. Benmansour. 1999. Mutations in the glycoprotein of viral haemorrhagic septicaemia virus that affect virulence for fish and the pH threshold for membrane fusion. J. Gen. Virol. 80:1221-1229.
    • (1999) J. Gen. Virol. , vol.80 , pp. 1221-1229
    • Gaudin, Y.1    De Kinkelin, P.2    Benmansour, A.3
  • 25
    • 0344791717 scopus 로고    scopus 로고
    • The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules
    • Glombik, M. M., A. Kromer, T. Salm, W. B. Huttner, and H. H. Gerdes. 1999. The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. EMBO J. 18:1059-1070.
    • (1999) EMBO J. , vol.18 , pp. 1059-1070
    • Glombik, M.M.1    Kromer, A.2    Salm, T.3    Huttner, W.B.4    Gerdes, H.H.5
  • 26
    • 0031793435 scopus 로고    scopus 로고
    • pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers
    • Gray, C., and L. K. Tamm. 1998. pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers. Protein Sci. 7:2359-2373.
    • (1998) Protein Sci. , vol.7 , pp. 2359-2373
    • Gray, C.1    Tamm, L.K.2
  • 27
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han, X., J. H. Bushweller, D. S. Cafiso, and L. K. Tamm. 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
  • 29
    • 0030568005 scopus 로고    scopus 로고
    • A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase
    • Henderson, H. E., F. Hassan, D. Marais, and M. R. Hayden. 1996. A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase. Biochem. Biophys. Res. Commun. 227:189-194.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 189-194
    • Henderson, H.E.1    Hassan, F.2    Marais, D.3    Hayden, M.R.4
  • 31
    • 0037151005 scopus 로고    scopus 로고
    • Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-helix motif in fusion activity
    • Hsu, C. H., S. H. Wu, D. K. Chang, and C. Chen. 2002. Structural characterizations of fusion peptide analogs of influenza virus hemagglutinin. Implication of the necessity of a helix-hinge-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.4
  • 32
    • 0029840915 scopus 로고    scopus 로고
    • Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus
    • Kielian, M., M. R. Klimjack, S. Ghosh, and W. A. Duffus. 1996. Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus. J. Cell Biol. 134:863-872.
    • (1996) J. Cell Biol. , vol.134 , pp. 863-872
    • Kielian, M.1    Klimjack, M.R.2    Ghosh, S.3    Duffus, W.A.4
  • 33
    • 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., A. Aharoni, D. Rapaport, P. Jones, R. Blumenthal, and Y. Shai. 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
  • 34
    • 0031678678 scopus 로고    scopus 로고
    • A mechanism of protein-mediated fusion: Coupling between refolding of the influenza hemagglutinin and lipid rearrangements
    • Kozlov, M., and L. Chernomordik. 1998. A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements. Biophys. J. 75:1384-1396.
    • (1998) Biophys. J. , vol.75 , pp. 1384-1396
    • Kozlov, M.1    Chernomordik, L.2
  • 36
    • 0027367886 scopus 로고
    • Lysophosphatidylcholine mediates the mode of insertion of the NH2-terminal SIV fusion peptide into the lipid bilayer
    • Martin, I., M. C. Dubois, T. Saermark, R. M. Epand, and J. M. Ruysschaert. 1993. Lysophosphatidylcholine mediates the mode of insertion of the NH2-terminal SIV fusion peptide into the lipid bilayer. FEBS Lett. 333:325-330.
    • (1993) FEBS Lett. , vol.333 , pp. 325-330
    • Martin, I.1    Dubois, M.C.2    Saermark, T.3    Epand, R.M.4    Ruysschaert, J.M.5
  • 37
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocation: Tunnel vision
    • Matlack, K. E. S., W. Mothes, and T. A. Rapoport. 1998. Protein translocation: tunnel vision. Cell 92:381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.S.1    Mothes, W.2    Rapoport, T.A.3
  • 38
    • 0035663883 scopus 로고    scopus 로고
    • What drives membrane fusion in eukaryotes?
    • Mayer, A. 2001. What drives membrane fusion in eukaryotes? Trends Biochem. Sci. 26:717-723.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 717-723
    • Mayer, A.1
  • 39
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 40
    • 0027265161 scopus 로고
    • Characterization of avian reovirus-induced cell fusion: The role of viral structural proteins
    • Ni, Y., and R. F. Ramig. 1993. Characterization of avian reovirus-induced cell fusion: the role of viral structural proteins. Virology 194:705-714.
    • (1993) Virology , vol.194 , pp. 705-714
    • Ni, Y.1    Ramig, R.F.2
  • 41
    • 0034440270 scopus 로고    scopus 로고
    • Hydrophobic-at-interface regions in viral fusion protein ectodomains
    • Nieva, J. L., and T. Suarez. 2000. Hydrophobic-at-interface regions in viral fusion protein ectodomains. Biosci. Rep. 20:519-533.
    • (2000) Biosci. Rep. , vol.20 , pp. 519-533
    • Nieva, J.L.1    Suarez, T.2
  • 42
    • 0033621026 scopus 로고    scopus 로고
    • Effect of nonpolar substitutions of the conserved Phe11 in the fusion peptide of HIV-1 gp41 on its function, structure, and organization in membranes
    • Pritsker, M., J. Rucker, T. L. Hoffman, R. W. Doms, and Y. Shai. 1999. Effect of nonpolar substitutions of the conserved Phe11 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
  • 43
    • 0028306273 scopus 로고
    • Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes
    • Rapaport, D., and Y. Shai. 1994. Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes. J. Biol. Chem. 269:15124-15131.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15124-15131
    • Rapaport, D.1    Shai, Y.2
  • 44
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution
    • Rey, F. A., F. X. Heinz, C. Mandl, C. Kunz, and S. C. Harrison. 1995. The envelope glycoprotein from tick-borne encephalitis virus at 2 Å resolution. Nature 375:291-298.
    • (1995) Nature , vol.375 , pp. 291-298
    • Rey, F.A.1    Heinz, F.X.2    Mandl, C.3    Kunz, C.4    Harrison, S.C.5
  • 45
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. 1994. Mechanisms of intracellular protein transport. Nature 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 46
    • 0034161496 scopus 로고    scopus 로고
    • A new class of fusion-associated small transmembrane (FAST) proteins encoded by the nonenveloped fusogenic reoviruses
    • Shmulevitz, M., and R. Duncan. 2000. A new class of fusion-associated small transmembrane (FAST) proteins encoded by the nonenveloped fusogenic reoviruses. EMBO J. 19:902-912.
    • (2000) EMBO J. , vol.19 , pp. 902-912
    • Shmulevitz, M.1    Duncan, R.2
  • 47
    • 0036138025 scopus 로고    scopus 로고
    • Sequential partially overlapping gene arrangement in the tricistronic S1 genome segments of avian reovirus and Nelson Bay reovirus: Implications for translation initiation
    • Shmulevitz, M., Z. Yameen, S. Dawe, J. Shou, D. O'Hara, I. Holmes, and R. Duncan. 2002. Sequential partially overlapping gene arrangement in the tricistronic S1 genome segments of avian reovirus and Nelson Bay reovirus: implications for translation initiation. J. Virol. 76:609-618.
    • (2002) J. Virol. , vol.76 , pp. 609-618
    • Shmulevitz, M.1    Yameen, Z.2    Dawe, S.3    Shou, J.4    O'Hara, D.5    Holmes, I.6    Duncan, R.7
  • 48
    • 0141682123 scopus 로고    scopus 로고
    • Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation
    • Shmulevitz, M., J. Salsman, and R. Duncan. 2003. Palmitoylation, membrane-proximal basic residues, and transmembrane glycine residues in the reovirus p10 protein are essential for syncytium formation. J. Virol. 77:9769-9779.
    • (2003) J. Virol. , vol.77 , pp. 9769-9779
    • Shmulevitz, M.1    Salsman, J.2    Duncan, R.3
  • 49
    • 0030783371 scopus 로고    scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions
    • Siegel, D. P., and R. M. Epand. 1997. The mechanism of lamellar-to-inverted hexagonal phase transitions. Biophys. J. 73:3089-3111.
    • (1997) Biophys. J. , vol.73 , pp. 3089-3111
    • Siegel, D.P.1    Epand, R.M.2
  • 50
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J. J., and D. C. Wiley. 1998. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95:871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 51
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza haemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza haemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 52
    • 0033042935 scopus 로고    scopus 로고
    • Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy
    • Sreerama, N., S. Y. Venyaminov, and R. W. Woody. 1999. Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8:370-380.
    • (1999) Protein Sci , vol.8 , pp. 370-380
    • Sreerama, N.1    Venyaminov, S.Y.2    Woody, R.W.3
  • 54
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D. K., D. Hoekstra, and R. E. Pagano. 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
  • 55
    • 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., W. R. Gallaher, A. Agirre, F. M. Goni, and J. L. Nieva. 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
  • 56
    • 0034444121 scopus 로고    scopus 로고
    • Viral fusion peptides: A tool set to disrupt and connect biological membranes
    • Tamm, L. K., and X. Han. 2000. Viral fusion peptides: a tool set to disrupt and connect biological membranes. Biosci. Rep. 20:501-518.
    • (2000) Biosci. Rep. , vol.20 , pp. 501-518
    • Tamm, L.K.1    Han, X.2
  • 57
    • 0036948265 scopus 로고    scopus 로고
    • Structure and function of membrane fusion peptides
    • Tamm, L. K., X. Han, Y. Li, and A. L. Lai. 2002. Structure and function of membrane fusion peptides. Biopolymers 66:249-260.
    • (2002) Biopolymers , vol.66 , pp. 249-260
    • Tamm, L.K.1    Han, X.2    Li, Y.3    Lai, A.L.4
  • 59
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. M. 1990. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:675-679.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-679
    • White, J.M.1
  • 60
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. 1992. Membrane fusion. Science 258:917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 61
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and S. H. White. 1996. Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Biol. 3:842-848.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.