메뉴 건너뛰기




Volumn 71, Issue 5, 1997, Pages 4062-4070

Molecular mechanism underlying the action of a novel fusion inhibitor of influenza A virus

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; BMS 195161; BMS 198254; BMY 27709; DRUG ANALOG; UNCLASSIFIED DRUG; VIRUS HEMAGGLUTININ;

EID: 0030894782     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.71.5.4062-4070.1997     Document Type: Article
Times cited : (99)

References (53)
  • 1
    • 0026782108 scopus 로고
    • Intermediates and kinetics of membrane fusion
    • Bentz, J. 1992. Intermediates and kinetics of membrane fusion. Biophys. J. 63:448-459.
    • (1992) Biophys. J. , vol.63 , pp. 448-459
    • Bentz, J.1
  • 2
    • 0002282242 scopus 로고
    • Architecture of the influenza hemagglutinin fusion site
    • J. Bentz (ed.), CRC Press, Boca Raton, Fla
    • Bentz, J., H. Ellens, and D. Alford. 1993. Architecture of the influenza hemagglutinin fusion site, p. 163-199. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Boca Raton, Fla.
    • (1993) Viral Fusion Mechanisms , pp. 163-199
    • Bentz, J.1    Ellens, H.2    Alford, D.3
  • 3
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian, D. L., R. B. Yamasaki, R. L. Buswell, J. F. Stearns, J. M. White, and I. D. Kuntz. 1993. Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32:2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1    Yamasaki, R.B.2    Buswell, R.L.3    Stearns, J.F.4    White, J.M.5    Kuntz, I.D.6
  • 4
    • 0002345765 scopus 로고
    • Fusion-protein membrane interactions as studied by hydrophobic photolabeling
    • J. Bentz (ed.), CRC Press, Boca Raton, Fla
    • Brunner, J., and M. Tsurudome. 1993. Fusion-protein membrane interactions as studied by hydrophobic photolabeling, p. 67-88. In J. Bentz (ed.), Viral fusion mechanisms. CRC Press, Boca Raton, Fla.
    • (1993) Viral Fusion Mechanisms , pp. 67-88
    • Brunner, J.1    Tsurudome, M.2
  • 5
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza hemagglutinin 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
  • 6
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. Kim. 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.2
  • 7
    • 0028089983 scopus 로고
    • Flu virus invasion: Halfway there
    • Carr, C. M., and P. Kim. 1994. Flu virus invasion: halfway there. Science 266:234-236.
    • (1994) Science , vol.266 , pp. 234-236
    • Carr, C.M.1    Kim, P.2
  • 8
    • 0025816519 scopus 로고
    • Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density
    • Clague, M. J., C. Schoch, and R. Blumenthal. 1991. Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density. J. Virol. 65:2402-2407.
    • (1991) J. Virol. , vol.65 , pp. 2402-2407
    • Clague, M.J.1    Schoch, C.2    Blumenthal, R.3
  • 9
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli, T., S. L. Pelletier, Y. I. Henis, and J. M. White. 1996. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 133:559-569.
    • (1996) J. Cell Biol. , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 11
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: The low pH-induced conformational change
    • Doms, R. W., A. Helenius, and J. M. White. 1985. Membrane fusion activity of the influenza virus hemagglutinin: the low pH-induced conformational change. J. Biol. Chem. 260:2973-2981.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.M.3
  • 12
    • 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. 271:13417-13421.
    • (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
  • 13
    • 0025109728 scopus 로고
    • Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: Role of hemagglutinin surface density
    • Ellens, H., J. Bentz, D. Mason, F. Zhang, and J. M. White. 1990. Fusion of influenza hemagglutinin-expressing fibroblasts with glycophorin-bearing liposomes: role of hemagglutinin surface density. Biochemistry 29:9697-9707.
    • (1990) Biochemistry , vol.29 , pp. 9697-9707
    • Ellens, H.1    Bentz, J.2    Mason, D.3    Zhang, F.4    White, J.M.5
  • 14
    • 0029022681 scopus 로고
    • Low-pH induced conformational changes in viral fusion proteins: Implications for the fusion mechanism
    • Gaudin, Y., R. W. H. Ruigrok, and J. Brunner. 1995. Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. J. Gen. Virol. 76:1541-1556.
    • (1995) J. Gen. Virol. , vol.76 , pp. 1541-1556
    • Gaudin, Y.1    Ruigrok, R.W.H.2    Brunner, J.3
  • 15
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site specific mutagenesis of the hemagglutinin of influenza virus
    • Gething, M.-J., R. W. Doms, D. York, and J. M. White. 1986. Studies on the mechanism of membrane fusion: site specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.-J.1    Doms, R.W.2    York, D.3    White, J.M.4
  • 16
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley, L., J. Pfeifer, D. Steinhauer, B. Ely, G. Shaw, R. Kaufmann, E. Suchanek, C. Pabo, J. J. Skehel, D. C. Wiley, and S. Wharton. 1992. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell 68:635-645.
    • (1992) Cell , vol.68 , pp. 635-645
    • Godley, L.1    Pfeifer, J.2    Steinhauer, D.3    Ely, B.4    Shaw, G.5    Kaufmann, R.6    Suchanek, E.7    Pabo, C.8    Skehel, J.J.9    Wiley, D.C.10    Wharton, S.11
  • 17
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius, A. 1992. Unpacking the incoming influenza virus. Cell 69:577-578.
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 18
    • 0019400775 scopus 로고
    • Complete sequence analysis shows that the hemagglutinins of the H1 and H2 subtypes of human influenza virus are closely related
    • Hiti, A. L., A. R. Davis, and D. R. Nayak. 1981. Complete sequence analysis shows that the hemagglutinins of the H1 and H2 subtypes of human influenza virus are closely related. Virology 111:113-124.
    • (1981) Virology , vol.111 , pp. 113-124
    • Hiti, A.L.1    Davis, A.R.2    Nayak, D.R.3
  • 19
    • 0029257245 scopus 로고
    • Structural characterization of viral fusion proteins
    • Hughson, F. M. 1995. Structural characterization of viral fusion proteins. Curr. Biol. 5:265-274.
    • (1995) Curr. Biol. , vol.5 , pp. 265-274
    • Hughson, F.M.1
  • 20
    • 0025336478 scopus 로고
    • Autoradiography using storage phosphor technology
    • Johnston, R. F., S. C. Pickett, and D. L. Barker. 1990. Autoradiography using storage phosphor technology. Electrophoresis 11:355-360.
    • (1990) Electrophoresis , vol.11 , pp. 355-360
    • Johnston, R.F.1    Pickett, S.C.2    Barker, D.L.3
  • 21
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., T. Danieli, and J. M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76:383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0026747168 scopus 로고
    • Mechanism of attenuation of a chimeric influenza A/B transfectant virus
    • Luo, G.-X., M. Bergmann, A. Garcia-Sastre, and P. Palese. 1992. Mechanism of attenuation of a chimeric influenza A/B transfectant virus. J. Virol. 66: 4679-4685.
    • (1992) J. Virol. , vol.66 , pp. 4679-4685
    • Luo, G.-X.1    Bergmann, M.2    Garcia-Sastre, A.3    Palese, P.4
  • 24
    • 0030560967 scopus 로고    scopus 로고
    • Characterization of a hemagglutinin-specific inhibitor of influenza A virus
    • Luo, G.-X., R. Colonno, and M. Krystal. 1996. Characterization of a hemagglutinin-specific inhibitor of influenza A virus. Virology 226:66-76.
    • (1996) Virology , vol.226 , pp. 66-76
    • Luo, G.-X.1    Colonno, R.2    Krystal, M.3
  • 25
    • 0027715108 scopus 로고
    • Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: Flickering to final expansion
    • Melikian, G. B., W. D. Niles, M. E. Peeples, and F. S. Cohen. 1993. Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: flickering to final expansion. J. Gen. Physiol. 102:1131-1149.
    • (1993) J. Gen. Physiol. , vol.102 , pp. 1131-1149
    • Melikian, G.B.1    Niles, W.D.2    Peeples, M.E.3    Cohen, F.S.4
  • 26
    • 0024564649 scopus 로고
    • Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells
    • Morris, S. J., D. P. Sarkar, J. M. White, and R. Blumenthal. 1989. Kinetics of pH-dependent fusion between 3T3 fibroblasts expressing influenza hemagglutinin and red blood cells. J. Biol. Chem. 264:3972-3978.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3972-3978
    • Morris, S.J.1    Sarkar, D.P.2    White, J.M.3    Blumenthal, R.4
  • 27
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa, E., T. Aoyama, H. Kato, Y. Suzuki, Y. Tateno, and K. Nakajima. 1991. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182:475-485.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 28
    • 0027952589 scopus 로고
    • Intermediates in influenza virus PR/8 haemagglutinin-induced membrane fusion
    • Pak, C. C., M. Krumbiegel, and R. Blumenthal. 1994. Intermediates in influenza virus PR/8 haemagglutinin-induced membrane fusion. J. Gen. Virol. 75:395-399.
    • (1994) J. Gen. Virol. , vol.75 , pp. 395-399
    • Pak, C.C.1    Krumbiegel, M.2    Blumenthal, R.3
  • 29
    • 0025719093 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: Interaction of HA2 N-terminal peptides with phosphlipid vesicles
    • Rafalski, M., A. Ortiz, A. Rockwell, L. C. Van Ginkel, J. D. Lear, W. F. DeGrado, and J. Wilschut. 1991. Membrane fusion activity of the influenza virus hemagglutinin: interaction of HA2 N-terminal peptides with phosphlipid vesicles. Biochemistry 30:10211-10220.
    • (1991) Biochemistry , vol.30 , pp. 10211-10220
    • Rafalski, M.1    Ortiz, A.2    Rockwell, A.3    Van Ginkel, L.C.4    Lear, J.D.5    Degrado, W.F.6    Wilschut, J.7
  • 30
    • 0003077804 scopus 로고
    • Membrane insertion and intracellular transport of influenza virus glycoproteins
    • R. M. Krug (ed.), Plenum Press, New York, N.Y.
    • Roth, M. G., M.-J. Gething, and J. Sambrook. 1989. Membrane insertion and intracellular transport of influenza virus glycoproteins, p. 219-267. In R. M. Krug (ed.), Plenum Press, The influenza viruses. New York, N.Y.
    • (1989) The Influenza Viruses , pp. 219-267
    • Roth, M.G.1    Gething, M.-J.2    Sambrook, J.3
  • 32
    • 0024406233 scopus 로고
    • Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: Cytoplasmic continuity and lipid mixing
    • Sarkar, D. P., S. J. Morris, O. Eidelman, J. Zimmerberg, and R. Blumenthal. 1989. Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing. J. Cell Biol. 109:113-122.
    • (1989) J. Cell Biol. , vol.109 , pp. 113-122
    • Sarkar, D.P.1    Morris, S.J.2    Eidelman, O.3    Zimmerberg, J.4    Blumenthal, R.5
  • 33
    • 0027190432 scopus 로고
    • Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion
    • Schoch, C., and R. Blumenthal. 1993. Role of the fusion peptide sequence in initial stages of influenza hemagglutinin-induced cell fusion. J. Biol. Chem. 268:9267-9274.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9267-9274
    • Schoch, C.1    Blumenthal, R.2
  • 35
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell-fusion events mediated by a viral fusion protein
    • Spruce, A. E., A. Iwata, J. M. White, and W. Almers. 1989. Patch clamp studies of single cell-fusion events mediated by a viral fusion protein. Nature 342:555-558.
    • (1989) Nature , vol.342 , pp. 555-558
    • Spruce, A.E.1    Iwata, A.2    White, J.M.3    Almers, W.4
  • 36
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann, T., J. M. White, and A. Helenius. 1990. Intermediates in influenza induced membrane fusion. EMBO J. 9:4231-4241.
    • (1990) EMBO J. , vol.9 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 37
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann, T., J. M. Delfino, R. Richards, and A. Helenius. 1991. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J. Biol. Chem. 266:18404-18410.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, R.3    Helenius, A.4
  • 39
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer, D. A., S. A. Wharton, J. J. Skehel, and D. C. Wiley. 1995. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 40
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian, S. A., P. Hinterdorfer, G. Baber and L. K. Tamm. 1995. Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy. EMBO J. 14:5514-5523.
    • (1995) EMBO J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 41
    • 0027180538 scopus 로고
    • Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
    • Tse, F. W., A. Iwata, and W. Almers. 1993. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. J. Cell Biol. 121:543-552.
    • (1993) J. Cell Biol. , vol.121 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 42
    • 0023915219 scopus 로고
    • Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid
    • Weis, W., J. H. Brown, S. Cusack, J. C. Paulson, J. J. Skehel, and D. C. Wiley. 1988. Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 43
    • 0020355569 scopus 로고
    • Haemagglutinin of influenza virus expressed from a cloned gene promotes membrane fusion
    • White, J. M., A. Helenius, and M.-J. Gething. 1982. Haemagglutinin of influenza virus expressed from a cloned gene promotes membrane fusion. Nature 300:658-659.
    • (1982) Nature , vol.300 , pp. 658-659
    • White, J.M.1    Helenius, A.2    Gething, M.-J.3
  • 44
    • 0020338520 scopus 로고
    • Membrane fusion activity of influenza virus
    • White, J. M., J. Kartenbeck, and A. Helenius. 1982. Membrane fusion activity of influenza virus. EMBO J. 1:217-222.
    • (1982) EMBO J. , vol.1 , pp. 217-222
    • White, J.M.1    Kartenbeck, J.2    Helenius, A.3
  • 45
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White, J. M., and I. A. Wilson. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 105:2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 46
    • 0025276435 scopus 로고
    • Viral and cellular membrane fusion proteins
    • White, J. M. 1990. Viral and cellular membrane fusion proteins. Annu. Rev. Physiol. 52:675-97.
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 675-697
    • White, J.M.1
  • 47
    • 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
  • 48
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-374.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-374
    • Wiley, D.C.1    Skehel, J.J.2
  • 49
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 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
  • 50
    • 0020607461 scopus 로고
    • Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/8/34-mediated hemolysis
    • Yewdell, J. W., W. Gerhard, and T. Bachi. 1983. Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/8/34-mediated hemolysis. J. Virol. 48:239-248.
    • (1983) J. Virol. , vol.48 , pp. 239-248
    • Yewdell, J.W.1    Gerhard, W.2    Bachi, T.3
  • 51
    • 0024296435 scopus 로고
    • Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein
    • Yewdell, J. W., A. Yellen, and T. Bachi. 1988. Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein. Cell 52:843-852.
    • (1988) Cell , vol.52 , pp. 843-852
    • Yewdell, J.W.1    Yellen, A.2    Bachi, T.3
  • 52
    • 0027967960 scopus 로고
    • Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
    • Yu, Y. G., D. S. King, and Y.-K. Shin. 1994. Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes. Science 266:274-276.
    • (1994) Science , vol.266 , pp. 274-276
    • Yu, Y.G.1    King, D.S.2    Shin, Y.-K.3
  • 53
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • Zimmerberg, J., R. Blumenthal, D. P. Sarkar, M. Curran, and S. J. Morris. 1994. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. J. Cell Biol. 127:1885-1894.
    • (1994) J. Cell Biol. , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.