메뉴 건너뛰기




Volumn 16, Issue 1, 1999, Pages 3-9

Structural basis for membrane fusion by enveloped viruses

Author keywords

Ebola virus Gp2; HIV gp41; Influenza virus haemagglutinin; Membrane fusion

Indexed keywords

GLYCOPROTEIN GP 41; VIRUS ENVELOPE PROTEIN; VIRUS GLYCOPROTEIN; VIRUS RNA;

EID: 0032902197     PISSN: 09687688     EISSN: None     Source Type: Journal    
DOI: 10.1080/096876899294706     Document Type: Conference Paper
Times cited : (335)

References (76)
  • 1
    • 0028872697 scopus 로고
    • The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus
    • Becker, S., Spiess, M. and Klenk, H.-D., 1995, The asialoglycoprotein receptor is a potential liver-specific receptor for Marburg virus. Journal of General Virology, 76, 393-399.
    • (1995) Journal of General Virology , vol.76 , pp. 393-399
    • Becker, S.1    Spiess, M.2    Klenk, H.-D.3
  • 3
    • 0028864614 scopus 로고
    • A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein
    • Blacklow, S. C., Lu, M. and Kim, P. S., 1995, A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry, 34, 14955-14962.
    • (1995) Biochemistry , vol.34 , pp. 14955-14962
    • Blacklow, S.C.1    Lu, M.2    Kim, P.S.3
  • 4
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal, R., Sarkar, D. P., Durell, S., Howard, D. E. and Morris, S. J., 1996, Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. Journal of Cell Biology, 135, 63-71.
    • (1996) Journal of Cell Biology , vol.135 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 6
    • 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
  • 7
    • 0027499917 scopus 로고
    • Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type gp41 envelope glycoprotein
    • Cao, J., Bergeron, L., Helseth, E., Thali, M., Repke, H. and Sodroski, J., 1993, Effects of amino acid changes in the extracellular domain of the human immunodeficiency virus type gp41 envelope glycoprotein. Journal of Virology, 67, 2747-2755.
    • (1993) Journal of Virology , vol.67 , pp. 2747-2755
    • Cao, J.1    Bergeron, L.2    Helseth, E.3    Thali, M.4    Repke, H.5    Sodroski, J.6
  • 8
    • 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
  • 9
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr, C. M., Chaudhry, C. and Kim, P. S., 1997, Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proceedings of the National Academy of Sciences, 94, 14306-14313.
    • (1997) Proceedings of the National Academy of Sciences , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 10
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers, P., Pringle, C. R. and Easton, A. J., 1990, Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. Journal of General Virology, 71, 3075-3080.
    • (1990) Journal of General Virology , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 11
    • 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
  • 12
    • 0029072191 scopus 로고
    • A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: Implication for viral fusion
    • Chen, C. H., Matthews, T. J., McDanal, C. B., Bolognesi, D. P. and Greenberg, M. L., 1995, A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusion. Journal of Virology, 69, 3771-3777.
    • (1995) Journal of Virology , vol.69 , pp. 3771-3777
    • Chen, C.H.1    Matthews, T.J.2    McDanal, C.B.3    Bolognesi, D.P.4    Greenberg, M.L.5
  • 13
    • 0029558245 scopus 로고
    • A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation
    • Chen, J., Wharton, S. A., Weissenhorn, W., Calder, L. J., Hughson, F. M., Skehel, J. J. and Wiley, D. C., 1995, A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation. Proceedings of the National Academy of Sciences, 92, 12205-12209.
    • (1995) Proceedings of the National Academy of Sciences , vol.92 , pp. 12205-12209
    • Chen, J.1    Wharton, S.A.2    Weissenhorn, W.3    Calder, L.J.4    Hughson, F.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 14
    • 0028107566 scopus 로고
    • Functional role of the zipper motif region of human immunodeficiency virus type 1 envelope transmembrane glycoprotein
    • Chen, S. S., 1994, Functional role of the zipper motif region of human immunodeficiency virus type 1 envelope transmembrane glycoprotein. Journal of Virology, 68, 2002-2010.
    • (1994) Journal of Virology , vol.68 , pp. 2002-2010
    • Chen, S.S.1
  • 15
    • 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. and Lee, T. H., 1993, Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein. Journal of Virology, 67, 3615-3619.
    • (1993) Journal of Virology , vol.67 , pp. 3615-3619
    • Chen, S.S.1    Lee, C.N.2    Lee, W.R.3    McIntosh, K.4    Lee, T.H.5
  • 16
    • 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., Pelletier, S. L., Henis, Y. I. and White, J. M., 1996, Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. Journal of Cell Biology, 133, 559-569.
    • (1996) Journal of Cell Biology , vol.133 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 17
    • 0029802605 scopus 로고    scopus 로고
    • Chemokines and HIV-1 second receptors: Confluence of two fields generates optimism in AIDS research
    • D'Souza, M. P. and Harden, V. A., 1996, Chemokines and HIV-1 second receptors: confluence of two fields generates optimism in AIDS research. Nature Medicine, 2, 1293-1300.
    • (1996) Nature Medicine , vol.2 , pp. 1293-1300
    • D'Souza, M.P.1    Harden, V.A.2
  • 18
    • 0026652457 scopus 로고
    • Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity
    • Dubay, J. W., Roberts, S. J., Brody, B. and Hunter, E., 1992, Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity. Journal of Virology, 66, 4748-4756.
    • (1992) Journal of Virology , vol.66 , pp. 4748-4756
    • Dubay, J.W.1    Roberts, S.J.2    Brody, B.3    Hunter, E.4
  • 19
    • 0028355456 scopus 로고
    • Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicts diverse monoclonal antibody reactivities
    • Earl, P. L., Broder, C. C., Long, D., Lee, S. A., Peterson, J., Chakrabarti, S., Doms, R. W. and Moss, B., 1994, Native oligomeric human immunodeficiency virus type 1 envelope glycoprotein elicts diverse monoclonal antibody reactivities. Journal of Virology, 68, 3015-3026.
    • (1994) Journal of Virology , vol.68 , pp. 3015-3026
    • Earl, P.L.1    Broder, C.C.2    Long, D.3    Lee, S.A.4    Peterson, J.5    Chakrabarti, S.6    Doms, R.W.7    Moss, B.8
  • 20
  • 21
    • 0025760333 scopus 로고
    • Glycosylation and oligomerization of the spike protein of Marburg virus
    • Feldmann, H., Will, C., Schikore, M., Slenczka, W. and Klenk, D.-D., 1991, Glycosylation and oligomerization of the spike protein of Marburg virus. Virology, 182, 353-356.
    • (1991) Virology , vol.182 , pp. 353-356
    • Feldmann, H.1    Will, C.2    Schikore, M.3    Slenczka, W.4    Klenk, D.-D.5
  • 22
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta, R. A., Wild, C. T., Weng, Y. and Weiss, C. D., 1998, Capture of an early fusion-active conformation of HIV-1 gp41. Nature Structural Biology, 5, 276-279.
    • (1998) Nature Structural Biology , vol.5 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 23
    • 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, 85, 477-478.
    • (1996) Cell , vol.85 , pp. 477-478
    • Gallaher, W.R.1
  • 25
    • 0029022681 scopus 로고
    • Low-pH induced conformational changes in viral fusion proteins: Implications for the fusion mechanism
    • Gaudin, Y., Ruigrok, R. W. and Brunner, J., 1995, Low-pH induced conformational changes in viral fusion proteins: implications for the fusion mechanism. Journal of General Virology, 76, 1541-1556.
    • (1995) Journal of General Virology , vol.76 , pp. 1541-1556
    • Gaudin, Y.1    Ruigrok, R.W.2    Brunner, J.3
  • 26
    • 0026716831 scopus 로고
    • Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160
    • Hallenberger, S., Bosch, V., Angliker, H., Shaw, E., Klenk, H. D. and Garten, W., 1992, Inhibition of furin-mediated cleavage activation of HIV-1 glycoprotein gp160. Nature, 360, 358-361.
    • (1992) Nature , vol.360 , pp. 358-361
    • Hallenberger, S.1    Bosch, V.2    Angliker, H.3    Shaw, E.4    Klenk, H.D.5    Garten, W.6
  • 27
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deepetch electron microscopy
    • Hanson, P. I., Roth, R., Morisaki, H., Jahn, R. and Heuser, J. E., 1997, Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deepetch electron microscopy. Cell, 90, 523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 28
    • 0027934571 scopus 로고
    • Crystal structure of an isoleucine-zipper trimer
    • Harbury, P. B., Kim, P. S. and Alber, T., 1994, Crystal structure of an isoleucine-zipper trimer. Nature, 371, 80-83.
    • (1994) Nature , vol.371 , pp. 80-83
    • Harbury, P.B.1    Kim, P.S.2    Alber, T.3
  • 30
    • 0024564217 scopus 로고
    • Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the 'fusion peptide'
    • Harter, C., Lames, P., Bachi, T., Semenza, G. and Brunner, J., 1989, Hydrophobic binding of the ectodomain of influenza hemagglutinin to membranes occurs through the 'fusion peptide'. Journal of Biological Chemistry, 264, 6459-6464.
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 6459-6464
    • Harter, C.1    Lames, P.2    Bachi, T.3    Semenza, G.4    Brunner, J.5
  • 33
    • 0031962175 scopus 로고    scopus 로고
    • Conformational changes in cell surface HIV-1 envelope glycoprotein are triggered by cooperation between cell surface CD4 and coreceptors
    • Jones, P., Korte, T. and Blumenthal, R., 1998, Conformational changes in cell surface HIV-1 envelope glycoprotein are triggered by cooperation between cell surface CD4 and coreceptors. Journal of Biological Chemistry, 273, 404-409.
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 404-409
    • Jones, P.1    Korte, T.2    Blumenthal, R.3
  • 34
    • 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. and Lamb, R. A., 1998, A core trimer of the Paramyxovirus fusion protein: Parallels to Influenza virus hemagglutinin and HIV-1 gp41. Virology, 248, 20-34
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 35
    • 0030965051 scopus 로고    scopus 로고
    • Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy
    • Kanaseki, T., Kawasaki, K., Murata, M., Ikeuchi, Y. and Ohnishi, S.-I., 1997, Structural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopy. Journal of Cell Biology, 137, 1041-1052.
    • (1997) Journal of Cell Biology , vol.137 , pp. 1041-1052
    • Kanaseki, T.1    Kawasaki, K.2    Murata, M.3    Ikeuchi, Y.4    Ohnishi, S.-I.5
  • 36
    • 0028179011 scopus 로고
    • Lipid anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G. W., Danieli, T. and White, J. M., 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
  • 38
    • 0023803844 scopus 로고
    • The molecular biology of influenza virus pathogenicity
    • Klenk, H. D. and Rott, R., 1988. The molecular biology of influenza virus pathogenicity. Advances in Virus Research, 34, 247-281.
    • (1988) Advances in Virus Research , vol.34 , pp. 247-281
    • Klenk, H.D.1    Rott, R.2
  • 40
    • 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
  • 41
    • 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, Jr S. R. and Merutka, G., 1996, HIV-1 membrane fusion mechanism: structural studies of the interactions between biologically-active peptides from gp41. Biochemistry, 35, 13679-13708.
    • (1996) Biochemistry , vol.35 , pp. 13679-13708
    • Lawless, M.K.1    Barney, S.2    Guthrie, K.I.3    Bucy, T.B.4    Petteway S.R., Jr.5    Merutka, G.6
  • 42
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA-2
    • Lear, J. D. and DeGrado, W. F., 1987, Membrane binding and Conformational properties of peptides representing the NH2 terminus of influenza HA-2. Journal of Biological Chemistry, 262, 6500-6505.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 6500-6505
    • Lear, J.D.1    DeGrado, W.F.2
  • 44
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., Blacklow, S. C. and Kim, P. S., 1995, A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature Structural Biology, 2, 1075-1082.
    • (1995) Nature Structural Biology , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 45
    • 0025572710 scopus 로고
    • Dissociation of gp120 from HIV-1 virions induced by soluble CD4
    • Moore, J. P., McKeating, J. A., Weiss, R. A. and Sattentau, Q. J., 1990, Dissociation of gp120 from HIV-1 virions induced by soluble CD4. Science, 250, 1139-1142.
    • (1990) Science , vol.250 , pp. 1139-1142
    • Moore, J.P.1    McKeating, J.A.2    Weiss, R.A.3    Sattentau, Q.J.4
  • 46
    • 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. Journal of Cell Biology, 140, 315-323.
    • (1998) Journal of Cell Biology , vol.140 , pp. 315-323
    • Munoz-Barroso, I.1    Durell, S.2    Sakaguchi, K.3    Appella, E.4    Blumenthal, R.5
  • 48
    • 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
  • 49
    • 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. and Shai, Y., 1995, 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 Journal, 14, 5524-5531.
    • (1995) EMBO Journal , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 50
    • 0029014434 scopus 로고
    • The envelope glycoprotein from tick-borne encephalitis virus at 2Å resolution
    • Rey, F. A., Heinz, F. X., Mandl, C., Kunz, C. and Harrison, S. C., 1995, The envelope glycoprotein from tick-borne encephalitis virus at 2Å 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
  • 52
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau, Q. J. and Moore, J. P., 1991, Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. Journal of Experimental Medicine, 174, 407-415.
    • (1991) Journal of Experimental Medicine , vol.174 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 53
    • 0027286538 scopus 로고
    • Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease
    • Schnittler, H. J., Mahner, F., Drenckhahn, D., Klenk, H.-D., Feldmann, H., 1993, Replication of Marburg virus in human endothelial cells. A possible mechanism for the development of viral hemorrhagic disease. Journal of Clinical Investigation, 91, 1301-1309.
    • (1993) Journal of Clinical Investigation , vol.91 , pp. 1301-1309
    • Schnittler, H.J.1    Mahner, F.2    Drenckhahn, D.3    Klenk, H.-D.4    Feldmann, H.5
  • 56
    • 0025875216 scopus 로고
    • The first millisecond of the pore formed by a fusogenic viral envelope protein during membrane fusion
    • Spruce, A. E., Iwata, A. and Almers, W., 1991, The first millisecond of the pore formed by a fusogenic viral envelope protein during membrane fusion. Proceedings of the National Academy of Sciences, 88, 3623-3627.
    • (1991) Proceedings of the National Academy of Sciences , vol.88 , pp. 3623-3627
    • Spruce, A.E.1    Iwata, A.2    Almers, W.3
  • 57
    • 0024331657 scopus 로고
    • Patch clamp studies of single cell fusion events mediated by a viral fusion protein
    • Spruce, A. E., Iwata, A., White, J. M. and Almers, W., 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
  • 60
    • 0028298880 scopus 로고
    • Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal sequence generated during precursor activation
    • Weber, T., Paesold, G., Galli, C., Mischler, R., Semenza, G. and Brunner, J., 1994, Evidence for H+-induced insertion of the influenza hemagglutinin HA2 N-terminal sequence generated during precursor activation. Journal of Biological Chemistry, 269, 18353-18357.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 18353-18357
    • Weber, T.1    Paesold, G.2    Galli, C.3    Mischler, R.4    Semenza, G.5    Brunner, J.6
  • 63
    • 0032568634 scopus 로고    scopus 로고
    • The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple stranded coiled coil
    • Weissenhorn, W., Calder, L. J., Wharton, S. A., Skehel J. J. and Wiley D. C., 1998, The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple stranded coiled coil. Proceedings of the National Academy of Sciences, 95, 6032-6036.
    • (1998) Proceedings of the National Academy of Sciences , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel J, J.4    Wiley D, C.5
  • 65
    • 0029878665 scopus 로고    scopus 로고
    • The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide
    • Weissenhorn, W., Wharton, S. A., Calder, L. J., Earl, P. L., Moss, B., Aliprandis, E., Skehel, J. J. and Wiley, D. C., 1996, The ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptide. EMBO Journal, 15, 1507-1514.
    • (1996) EMBO Journal , vol.15 , pp. 1507-1514
    • Weissenhorn, W.1    Wharton, S.A.2    Calder, L.J.3    Earl, P.L.4    Moss, B.5    Aliprandis, E.6    Skehel, J.J.7    Wiley, D.C.8
  • 66
    • 0028855669 scopus 로고
    • Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
    • Wharton, S. A., Calder, L. J., Ruigrok, R. W., Skehel, J. J., Steinhauer, D. A. and Wiley, D. C., 1995, Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation. EMBO Journal, 14, 240-246.
    • (1995) EMBO Journal , vol.14 , pp. 240-246
    • Wharton, S.A.1    Calder, L.J.2    Ruigrok, R.W.3    Skehel, J.J.4    Steinhauer, D.A.5    Wiley, D.C.6
  • 68
    • 0028575843 scopus 로고
    • Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex
    • Wild, C., Dubay, J. W., Greenwell, T., Baird, T., Oas, T. G., McDanal, C. B., Hunter, E. and Matthews, T., 1994a, Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex. Proceedings of the National Academy of Sciences, 91, 12676-12680.
    • (1994) Proceedings of the National Academy of Sciences , vol.91 , pp. 12676-12680
    • Wild, C.1    Dubay, J.W.2    Greenwell, T.3    Baird, T.4    Oas, T.G.5    McDanal, C.B.6    Hunter, E.7    Matthews, T.8
  • 69
    • 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. and Matthews, T., 1995. The inhibitory activity of an HIV type 1 peptide correlates with its ability to interact with a leucine zipper structure. Aids Research and Human Retroviruses, 11, 323-325.
    • (1995) Aids Research and Human Retroviruses , vol.11 , pp. 323-325
    • Wild, C.1    Greenwell, T.2    Shugars, D.3    Rimsky-Clarke, L.4    Matthews, T.5
  • 70
    • 0026465468 scopus 로고
    • A synthetic inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition
    • Wild, C. T., Oas, T., McDanal, C. B., Bolognesi, D. and Matthews, T., 1992, A synthetic inhibitor of human immunodeficiency virus replication: Correlation between solution structure and viral inhibition. Proceedings of the National Academy of Sciences, 89, 10537-10541.
    • (1992) Proceedings of the National Academy of Sciences , vol.89 , pp. 10537-10541
    • Wild, C.T.1    Oas, T.2    McDanal, C.B.3    Bolognesi, D.4    Matthews, T.5
  • 71
    • 0027959493 scopus 로고
    • Peptides corresponding to a predictive a-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection
    • Wild, C. T., Shugars, D. C., Greenwell, T. K., McDanal, C. B. and Matthews, T. J., 1994b, Peptides corresponding to a predictive a-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection. Proceedings of the National Academy of Sciences, 91, 9770-9774.
    • (1994) Proceedings of the National Academy of Sciences , 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
  • 72
    • 0023082135 scopus 로고
    • The structure and function of the haemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C. and Skehel, J. J., 1987, The structure and function of the haemagglutinin membrane glycoprotein of influenza virus. Annual Review in Biochemistry, 56, 365-394.
    • (1987) Annual Review in Biochemistry , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 73
    • 0017664543 scopus 로고
    • Evidence from studies with a cross-linking reagent that the haemagglutinin of influenza virus is a trimer
    • Wiley, D. C., Skehel, J. J. and Waterfield, M., 1977, Evidence from studies with a cross-linking reagent that the haemagglutinin of influenza virus is a trimer. Virology, 79, 446-448.
    • (1977) Virology , vol.79 , pp. 446-448
    • Wiley, D.C.1    Skehel, J.J.2    Waterfield, M.3
  • 74
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I. A., Skehel, J. J. and Wiley, D. C., 1981, Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature, 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 75
    • 0032512668 scopus 로고    scopus 로고
    • Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins
    • Yang, Z., Delgado, R., Xu, L., Todd, R. F., Nabel, E. G., Sanchez, A. and Nabel, G. J., 1998, Distinct cellular interactions of secreted and transmembrane Ebola virus glycoproteins. Science, 279, 1034-1037.
    • (1998) Science , vol.279 , pp. 1034-1037
    • Yang, Z.1    Delgado, R.2    Xu, L.3    Todd, R.F.4    Nabel, E.G.5    Sanchez, A.6    Nabel, G.J.7
  • 76
    • 0030245704 scopus 로고    scopus 로고
    • Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection
    • Yao, Q. and Compans, R. W., 1996, Peptides corresponding to the heptad repeat sequence of human parainfluenza virus fusion protein are potent inhibitors of virus infection. Virology, 223, 103-112.
    • (1996) Virology , vol.223 , pp. 103-112
    • Yao, Q.1    Compans, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.