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Volumn 15, Issue 2, 2013, Pages 270-284

Assembly of the Marburg virus envelope

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN VP40; VIRUS GLYCOPROTEIN;

EID: 84872610552     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12076     Document Type: Article
Times cited : (28)

References (59)
  • 1
    • 34247557393 scopus 로고    scopus 로고
    • Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling
    • Aguilar, H.C., Matreyek, K.A., Choi, D.Y., Filone, C.M., Young, S., and Lee, B. (2007) Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. J Virol 81: 4520-4532.
    • (2007) J Virol , vol.81 , pp. 4520-4532
    • Aguilar, H.C.1    Matreyek, K.A.2    Choi, D.Y.3    Filone, C.M.4    Young, S.5    Lee, B.6
  • 2
    • 27144503018 scopus 로고    scopus 로고
    • VP24 of Marburg virus influences formation of infectious particles
    • Bamberg, S., Kolesnikova, L., Moller, P., Klenk, H.D., and Becker, S. (2005) VP24 of Marburg virus influences formation of infectious particles. J Virol 79: 13421-13433.
    • (2005) J Virol , vol.79 , pp. 13421-13433
    • Bamberg, S.1    Kolesnikova, L.2    Moller, P.3    Klenk, H.D.4    Becker, S.5
  • 3
    • 0037018099 scopus 로고    scopus 로고
    • Lipid raft microdomains: a gateway for compartmentalized trafficking of Ebola and Marburg viruses
    • Bavari, S., Bosio, C.M., Wiegand, E., Ruthel, G., Will, A.B., Geisbert, T.W., et al. (2002) Lipid raft microdomains: a gateway for compartmentalized trafficking of Ebola and Marburg viruses. J Exp Med 195: 593-602.
    • (2002) J Exp Med , vol.195 , pp. 593-602
    • Bavari, S.1    Bosio, C.M.2    Wiegand, E.3    Ruthel, G.4    Will, A.B.5    Geisbert, T.W.6
  • 4
    • 84858275052 scopus 로고    scopus 로고
    • Structural dissection of Ebola virus and its assembly determinants using cryoelectron tomography
    • Bharat, T.A., Noda, T., Riches, J.D., Kraehling, V., Kolesnikova, L., Becker, S., et al. (2012) Structural dissection of Ebola virus and its assembly determinants using cryoelectron tomography. Proc Natl Acad Sci USA 109: 4275-4280.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4275-4280
    • Bharat, T.A.1    Noda, T.2    Riches, J.D.3    Kraehling, V.4    Kolesnikova, L.5    Becker, S.6
  • 5
    • 82455175799 scopus 로고    scopus 로고
    • Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells
    • Bharat, T.A.M., Riches, J.D., Kolesnikova, L., Welsch, S., Krähling, V., Davey, N., et al. (2011) Cryo-electron tomography of Marburg virus particles and their morphogenesis within infected cells. PLoS Biol 9: e1001196.
    • (2011) PLoS Biol , vol.9
    • Bharat, T.A.M.1    Riches, J.D.2    Kolesnikova, L.3    Welsch, S.4    Krähling, V.5    Davey, N.6
  • 6
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • Bieniasz, P.D. (2006) Late budding domains and host proteins in enveloped virus release. Virology 344: 55-63.
    • (2006) Virology , vol.344 , pp. 55-63
    • Bieniasz, P.D.1
  • 8
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran, K., Sullivan, N.J., Felbor, U., Whelan, S.P., and Cunningham, J.M. (2005) Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 308: 1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 9
    • 80052868218 scopus 로고    scopus 로고
    • Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection
    • Cote, M., Misasi, J., Ren, T., Bruchez, A., Lee, K., Filone, C.M., et al. (2011) Small molecule inhibitors reveal Niemann-Pick C1 is essential for Ebola virus infection. Nature 477: 344-348.
    • (2011) Nature , vol.477 , pp. 344-348
    • Cote, M.1    Misasi, J.2    Ren, T.3    Bruchez, A.4    Lee, K.5    Filone, C.M.6
  • 10
    • 0034663762 scopus 로고    scopus 로고
    • Crystal structure of the matrix protein VP40 from Ebola virus
    • Dessen, A., Volchkov, V., Dolnik, O., Klenk, H.-D., and Weissenhorn, W. (2000) Crystal structure of the matrix protein VP40 from Ebola virus. EMBO J 19: 4228-4236.
    • (2000) EMBO J , vol.19 , pp. 4228-4236
    • Dessen, A.1    Volchkov, V.2    Dolnik, O.3    Klenk, H.-D.4    Weissenhorn, W.5
  • 11
    • 40449125013 scopus 로고    scopus 로고
    • Filoviruses: interactions with the host cell
    • Dolnik, O., Kolesnikova, L., and Becker, S. (2008) Filoviruses: interactions with the host cell. Cell Mol Life Sci 65: 756-776.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 756-776
    • Dolnik, O.1    Kolesnikova, L.2    Becker, S.3
  • 12
    • 77954471091 scopus 로고    scopus 로고
    • Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles
    • Dolnik, O., Kolesnikova, L., Stevermann, L., and Becker, S. (2010) Tsg101 is recruited by a late domain of the nucleocapsid protein to support budding of Marburg virus-like particles. J Virol 84: 7847-7856.
    • (2010) J Virol , vol.84 , pp. 7847-7856
    • Dolnik, O.1    Kolesnikova, L.2    Stevermann, L.3    Becker, S.4
  • 13
    • 0025760333 scopus 로고
    • Glycosylation and oligomerization of the spike protein of Marburg virus
    • Feldmann, H., Will, C., Schikore, M., Slenczka, W., and Klenk, H.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, H.D.5
  • 15
  • 16
    • 0037389018 scopus 로고    scopus 로고
    • The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties
    • Gomis-Rüth, F.X., Dessen, A., Timmins, J., Bracher, A., Kolesnikowa, L., Becker, S., et al. (2003) The matrix protein VP40 from Ebola virus octamerizes into pore-like structures with specific RNA binding properties. Structure 11: 423-433.
    • (2003) Structure , vol.11 , pp. 423-433
    • Gomis-Rüth, F.X.1    Dessen, A.2    Timmins, J.3    Bracher, A.4    Kolesnikowa, L.5    Becker, S.6
  • 17
    • 84859180550 scopus 로고    scopus 로고
    • Marburg virus glycoprotein GP2: pH-dependent stability of the ectodomain alpha-helical bundle
    • Harrison, J.S., Koellhoffer, J.F., Chandran, K., and Lai, J.R. (2012) Marburg virus glycoprotein GP2: pH-dependent stability of the ectodomain alpha-helical bundle. Biochemistry 51: 2515-2525.
    • (2012) Biochemistry , vol.51 , pp. 2515-2525
    • Harrison, J.S.1    Koellhoffer, J.F.2    Chandran, K.3    Lai, J.R.4
  • 19
    • 0002677020 scopus 로고    scopus 로고
    • Virus isolation and quantitation
    • Kangro, B.W.M.a.H. O. (ed.). London: Academic Press Limited
    • Hierholzer, J.C., and Killington, R.A. (1996) Virus isolation and quantitation. In Virology Methods Manual. Kangro, B.W.M.a.H.O. (ed.). London: Academic Press Limited, pp. 36-38.
    • (1996) Virology Methods Manual , pp. 36-38
    • Hierholzer, J.C.1    Killington, R.A.2
  • 20
    • 77953742423 scopus 로고    scopus 로고
    • Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription
    • Hoenen, T., Biedenkopf, N., Zielecki, F., Jung, S., Groseth, A., Feldmann, H., and Becker, S. (2010) Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription. J Virol 84: 7053-7063.
    • (2010) J Virol , vol.84 , pp. 7053-7063
    • Hoenen, T.1    Biedenkopf, N.2    Zielecki, F.3    Jung, S.4    Groseth, A.5    Feldmann, H.6    Becker, S.7
  • 21
    • 77649174605 scopus 로고    scopus 로고
    • Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity
    • Hood, C.L., Abraham, J., Boyington, J.C., Leung, K., Kwong, P.D., and Nabel, G.J. (2010) Biochemical and structural characterization of cathepsin L-processed Ebola virus glycoprotein: implications for viral entry and immunogenicity. J Virol 84: 2972-2982.
    • (2010) J Virol , vol.84 , pp. 2972-2982
    • Hood, C.L.1    Abraham, J.2    Boyington, J.C.3    Leung, K.4    Kwong, P.D.5    Nabel, G.J.6
  • 22
    • 0035148629 scopus 로고    scopus 로고
    • Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies
    • Ito, H., Watanabe, S., Takada, A., and Kawaoka, Y. (2001) Ebola virus glycoprotein: proteolytic processing, acylation, cell tropism, and detection of neutralizing antibodies. J Virol 75: 1576-1580.
    • (2001) J Virol , vol.75 , pp. 1576-1580
    • Ito, H.1    Watanabe, S.2    Takada, A.3    Kawaoka, Y.4
  • 24
    • 0343673805 scopus 로고    scopus 로고
    • Ultrastructural organization of recombinant Marburg virus nucleoprotein: comparison with Marburg virus inclusions
    • Kolesnikova, L., Muhlberger, E., Ryabchikova, E., and Becker, S. (2000) Ultrastructural organization of recombinant Marburg virus nucleoprotein: comparison with Marburg virus inclusions. J Virol 74: 3899-3904.
    • (2000) J Virol , vol.74 , pp. 3899-3904
    • Kolesnikova, L.1    Muhlberger, E.2    Ryabchikova, E.3    Becker, S.4
  • 25
    • 0036150019 scopus 로고    scopus 로고
    • VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment
    • Kolesnikova, L., Bugany, H., Klenk, H.D., and Becker, S. (2002) VP40, the matrix protein of Marburg virus, is associated with membranes of the late endosomal compartment. J Virol 76: 1825-1838.
    • (2002) J Virol , vol.76 , pp. 1825-1838
    • Kolesnikova, L.1    Bugany, H.2    Klenk, H.D.3    Becker, S.4
  • 26
    • 7644231754 scopus 로고    scopus 로고
    • Multivesicular bodies as a platform for formation of the Marburg virus envelope
    • Kolesnikova, L., Berghöfer, B., Bamberg, S., and Becker, S. (2004a) Multivesicular bodies as a platform for formation of the Marburg virus envelope. J Virol 78: 12277-12287.
    • (2004) J Virol , vol.78 , pp. 12277-12287
    • Kolesnikova, L.1    Berghöfer, B.2    Bamberg, S.3    Becker, S.4
  • 27
    • 1242342119 scopus 로고    scopus 로고
    • The matrix protein of Marburg virus is transported to the plasma membrane along cellular membranes: exploiting the retrograde late endosomal pathway
    • Kolesnikova, L., Bamberg, S., Berghöfer, B., and Becker, S. (2004b) The matrix protein of Marburg virus is transported to the plasma membrane along cellular membranes: exploiting the retrograde late endosomal pathway. J Virol 78: 2382-2393.
    • (2004) J Virol , vol.78 , pp. 2382-2393
    • Kolesnikova, L.1    Bamberg, S.2    Berghöfer, B.3    Becker, S.4
  • 29
    • 38449102557 scopus 로고    scopus 로고
    • Basolateral budding of Marburg virus: VP40 retargets viral glycoprotein GP to the basolateral surface
    • Kolesnikova, L., Ryabchikova, E., Shestopalov, A., and Becker, S. (2007b) Basolateral budding of Marburg virus: VP40 retargets viral glycoprotein GP to the basolateral surface. J Infect Dis 196: S232.
    • (2007) J Infect Dis , vol.196
    • Kolesnikova, L.1    Ryabchikova, E.2    Shestopalov, A.3    Becker, S.4
  • 31
    • 84856035746 scopus 로고    scopus 로고
    • Phosphorylation of Marburg virus matrix protein VP40 triggers assembly of nucleocapsids with the viral envelope at the plasma membrane
    • Kolesnikova, L., Mittler, E., Schudt, G., Shams-Eldin, H., and Becker, S. (2012) Phosphorylation of Marburg virus matrix protein VP40 triggers assembly of nucleocapsids with the viral envelope at the plasma membrane. Cell Microbiol 14: 182-197.
    • (2012) Cell Microbiol , vol.14 , pp. 182-197
    • Kolesnikova, L.1    Mittler, E.2    Schudt, G.3    Shams-Eldin, H.4    Becker, S.5
  • 32
    • 78149244480 scopus 로고    scopus 로고
    • Establishment of fruit bat cells (Rousettus aegyptiacus) as a model system for the investigation of filoviral infection
    • Kraehling, V., Dolnik, O., Kolesnikova, L., Schmidt-Chanasit, J., Jordan, I., Sandig, V., et al. (2010) Establishment of fruit bat cells (Rousettus aegyptiacus) as a model system for the investigation of filoviral infection. PLoS Negl Trop Dis 4: e802.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Kraehling, V.1    Dolnik, O.2    Kolesnikova, L.3    Schmidt-Chanasit, J.4    Jordan, I.5    Sandig, V.6
  • 33
    • 33744939483 scopus 로고    scopus 로고
    • Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor
    • Kuhn, J.H., Radoshitzky, S.R., Guth, A.C., Warfield, K.L., Li, W., Vincent, M.J., et al. (2006) Conserved receptor-binding domains of Lake Victoria marburgvirus and Zaire ebolavirus bind a common receptor. J Biol Chem 281: 15951-15958.
    • (2006) J Biol Chem , vol.281 , pp. 15951-15958
    • Kuhn, J.H.1    Radoshitzky, S.R.2    Guth, A.C.3    Warfield, K.L.4    Li, W.5    Vincent, M.J.6
  • 34
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee, J.E., Fusco, M.L., Hessell, A.J., Oswald, W.B., Burton, D.R., and Saphire, E.O. (2008) Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454: 177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5    Saphire, E.O.6
  • 35
    • 77649220531 scopus 로고    scopus 로고
    • Conserved motifs within Ebola and Marburg virus VP40 proteins are important for stability, localization, and subsequent budding of virus-like particles
    • Liu, Y., Cocka, L., Okumura, A., Zhang, Y.A., Sunyer, J.O., and Harty, R.N. (2010) Conserved motifs within Ebola and Marburg virus VP40 proteins are important for stability, localization, and subsequent budding of virus-like particles. J Virol 84: 2294-2303.
    • (2010) J Virol , vol.84 , pp. 2294-2303
    • Liu, Y.1    Cocka, L.2    Okumura, A.3    Zhang, Y.A.4    Sunyer, J.O.5    Harty, R.N.6
  • 36
    • 84860837223 scopus 로고    scopus 로고
    • Anti-tetherin activities of HIV-1 Vpu and Ebola virus glycoprotein do not involve removal of tetherin from lipid rafts
    • Lopez, L.A., Yang, S.J., Exline, C.M., Rengarajan, S., Haworth, K.G., and Cannon, P.M. (2012) Anti-tetherin activities of HIV-1 Vpu and Ebola virus glycoprotein do not involve removal of tetherin from lipid rafts. J Virol 86: 5467-5480.
    • (2012) J Virol , vol.86 , pp. 5467-5480
    • Lopez, L.A.1    Yang, S.J.2    Exline, C.M.3    Rengarajan, S.4    Haworth, K.G.5    Cannon, P.M.6
  • 37
    • 0029912922 scopus 로고    scopus 로고
    • Budding of rabies virus particles in the absence of the spike glycoprotein
    • Mebatsion, T., Konig, M., and Conzelmann, K.K. (1996) Budding of rabies virus particles in the absence of the spike glycoprotein. Cell 84: 941-951.
    • (1996) Cell , vol.84 , pp. 941-951
    • Mebatsion, T.1    Konig, M.2    Conzelmann, K.K.3
  • 38
    • 84859907529 scopus 로고    scopus 로고
    • Ebola virus entry requires the host-programmed recognition of an intracellular receptor
    • Miller, E.H., Obernosterer, G., Raaben, M., Herbert, A.S., Deffieu, M.S., Krishnan, A., et al. (2012) Ebola virus entry requires the host-programmed recognition of an intracellular receptor. EMBO J 31: 1947-1960.
    • (2012) EMBO J , vol.31 , pp. 1947-1960
    • Miller, E.H.1    Obernosterer, G.2    Raaben, M.3    Herbert, A.S.4    Deffieu, M.S.5    Krishnan, A.6
  • 39
    • 34247139357 scopus 로고    scopus 로고
    • Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope
    • Mittler, E., Kolesnikova, L., Strecker, T., Garten, W., and Becker, S. (2007) Role of the transmembrane domain of marburg virus surface protein GP in assembly of the viral envelope. J Virol 81: 3942-3948.
    • (2007) J Virol , vol.81 , pp. 3942-3948
    • Mittler, E.1    Kolesnikova, L.2    Strecker, T.3    Garten, W.4    Becker, S.5
  • 40
    • 79961195612 scopus 로고    scopus 로고
    • The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection
    • Mittler, E., Kolesnikova, L., Hartlieb, B., Davey, R., and Becker, S. (2011) The cytoplasmic domain of Marburg virus GP modulates early steps of viral infection. J Virol 85: 8188-8196.
    • (2011) J Virol , vol.85 , pp. 8188-8196
    • Mittler, E.1    Kolesnikova, L.2    Hartlieb, B.3    Davey, R.4    Becker, S.5
  • 41
    • 0031657064 scopus 로고    scopus 로고
    • Three of the four nucleocapsid proteins of Marburg virus, NP, VP35, and L, are sufficient to mediate replication and transcription of Marburg virus-specific monocistronic minigenomes
    • Mühlberger, E., Lötfering, B., Klenk, H.D., and Becker, S. (1998) Three of the four nucleocapsid proteins of Marburg virus, NP, VP35, and L, are sufficient to mediate replication and transcription of Marburg virus-specific monocistronic minigenomes. J Virol 72: 8756-8764.
    • (1998) J Virol , vol.72 , pp. 8756-8764
    • Mühlberger, E.1    Lötfering, B.2    Klenk, H.D.3    Becker, S.4
  • 42
    • 0034733392 scopus 로고    scopus 로고
    • Structural characterization and membrane binding properties of the matrix protein VP40 of ebola virus
    • Ruigrok, R.W.H., Schoehn, G., Dessen, A., Forest, E., Volchkov, V., Dolnik, O., et al. (2000) Structural characterization and membrane binding properties of the matrix protein VP40 of ebola virus. J Mol Biol 300: 103-112.
    • (2000) J Mol Biol , vol.300 , pp. 103-112
    • Ruigrok, R.W.H.1    Schoehn, G.2    Dessen, A.3    Forest, E.4    Volchkov, V.5    Dolnik, O.6
  • 43
    • 0033037010 scopus 로고    scopus 로고
    • An analysis of features of pathogenesis in two animal models of Ebola virus infection
    • Ryabchikova, E.I., Kolesnikova, L.V., and Luchko, S.V. (1999) An analysis of features of pathogenesis in two animal models of Ebola virus infection. J Infect Dis 179 (Suppl. 1): S199-S202.
    • (1999) J Infect Dis , vol.179 , Issue.SUPPL. 1
    • Ryabchikova, E.I.1    Kolesnikova, L.V.2    Luchko, S.V.3
  • 44
    • 34548512432 scopus 로고    scopus 로고
    • In Fields Virology. Knipe, D., and Howley, P. (eds), Philadelphia, PA: Lippincott Williams and Wilkins
    • Sanchez, A., Geisbert, T.W., and Feldmann, H. (2007) Filoviridae: Marburg and Ebola viruses. In Fields Virology. Knipe, D., and Howley, P. (eds). Philadelphia, PA: Lippincott Williams and Wilkins, pp. 1409-1439.
    • (2007) Filoviridae: Marburg and Ebola viruses , pp. 1409-1439
    • Sanchez, A.1    Geisbert, T.W.2    Feldmann, H.3
  • 45
    • 0035148474 scopus 로고    scopus 로고
    • Sorting of Marburg virus surface protein and virus release take place at opposite surfaces of infected polarized epithelial cells
    • Sanger, C., Muhlberger, E., Ryabchikova, E., Kolesnikova, L., Klenk, H.D., and Becker, S. (2001) Sorting of Marburg virus surface protein and virus release take place at opposite surfaces of infected polarized epithelial cells. J Virol 75: 1274-1283.
    • (2001) J Virol , vol.75 , pp. 1274-1283
    • Sanger, C.1    Muhlberger, E.2    Ryabchikova, E.3    Kolesnikova, L.4    Klenk, H.D.5    Becker, S.6
  • 46
    • 0032473424 scopus 로고    scopus 로고
    • Requirement for a nonspecific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus
    • Schnell, M.J., Buonocore, L., Boritz, E., Ghosh, H.P., Chernish, R., and Rose, J.K. (1998) Requirement for a nonspecific glycoprotein cytoplasmic domain sequence to drive efficient budding of vesicular stomatitis virus. EMBO J 17: 1289-1296.
    • (1998) EMBO J , vol.17 , pp. 1289-1296
    • Schnell, M.J.1    Buonocore, L.2    Boritz, E.3    Ghosh, H.P.4    Chernish, R.5    Rose, J.K.6
  • 47
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg, K., Matsuyama, S., Kabsch, K., Delos, S., Bouton, A., and White, J. (2006) Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J Virol 80: 4174-4178.
    • (2006) J Virol , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 48
    • 0034672008 scopus 로고    scopus 로고
    • Membrane association induces a conformational change in the Ebola virus matrix protein
    • Scianimanico, S., Schoehn, G., Timmins, J., Ruigrok, R.H., Klenk, H.D., and Weissenhorn, W. (2000) Membrane association induces a conformational change in the Ebola virus matrix protein. EMBO J 19: 6732-6741.
    • (2000) EMBO J , vol.19 , pp. 6732-6741
    • Scianimanico, S.1    Schoehn, G.2    Timmins, J.3    Ruigrok, R.H.4    Klenk, H.D.5    Weissenhorn, W.6
  • 52
    • 73149117324 scopus 로고    scopus 로고
    • Regulation of Marburg virus (MARV) budding by Nedd4. 1: a different WW domain of Nedd4.1 is critical for binding to MARV and Ebola virus VP40
    • Urata, S., and Yasuda, J. (2010) Regulation of Marburg virus (MARV) budding by Nedd4. 1: a different WW domain of Nedd4. 1 is critical for binding to MARV and Ebola virus VP40. J Gen Virol 91: 228-234.
    • (2010) J Gen Virol , vol.91 , pp. 228-234
    • Urata, S.1    Yasuda, J.2
  • 53
    • 34247633960 scopus 로고    scopus 로고
    • Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP
    • Urata, S., Noda, T., Kawaoka, Y., Morikawa, S., Yokosawa, H., and Yasuda, J. (2007) Interaction of Tsg101 with Marburg virus VP40 depends on the PPPY motif, but not the PT/SAP motif as in the case of Ebola virus, and Tsg101 plays a critical role in the budding of Marburg virus-like particles induced by VP40, NP, and GP. J Virol 81: 4895-4899.
    • (2007) J Virol , vol.81 , pp. 4895-4899
    • Urata, S.1    Noda, T.2    Kawaoka, Y.3    Morikawa, S.4    Yokosawa, H.5    Yasuda, J.6
  • 55
    • 0036720806 scopus 로고    scopus 로고
    • Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5
    • Waning, D.L., Schmitt, A.P., Leser, G.P., and Lamb, R.A. (2002) Roles for the cytoplasmic tails of the fusion and hemagglutinin-neuraminidase proteins in budding of the paramyxovirus simian virus 5. J Virol 76: 9284-9297.
    • (2002) J Virol , vol.76 , pp. 9284-9297
    • Waning, D.L.1    Schmitt, A.P.2    Leser, G.P.3    Lamb, R.A.4
  • 56
    • 3042550474 scopus 로고    scopus 로고
    • Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
    • Waning, D.L., Russell, C.J., Jardetzky, T.S., and Lamb, R.A. (2004) Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail. Proc Natl Acad Sci USA 101: 9217-9222.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9217-9222
    • Waning, D.L.1    Russell, C.J.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 57
    • 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. Proc Natl Acad Sci USA 95: 6032-6036.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6032-6036
    • Weissenhorn, W.1    Calder, L.J.2    Wharton, S.A.3    Skehel, J.J.4    Wiley, D.C.5
  • 58
    • 77951060977 scopus 로고    scopus 로고
    • Establishment and application of an infectious virus-like particle system for Marburg virus
    • Wenigenrath, J., Kolesnikova, L., Hoenen, T., Mittler, E., and Becker, S. (2010) Establishment and application of an infectious virus-like particle system for Marburg virus. J Gen Virol 91: 1325-1334.
    • (2010) J Gen Virol , vol.91 , pp. 1325-1334
    • Wenigenrath, J.1    Kolesnikova, L.2    Hoenen, T.3    Mittler, E.4    Becker, S.5
  • 59
    • 0027407071 scopus 로고
    • Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein
    • Will, C., Muhlberger, E., Linder, D., Slenczka, W., Klenk, H.D., and Feldmann, H. (1993) Marburg virus gene 4 encodes the virion membrane protein, a type I transmembrane glycoprotein. J Virol 67: 1203-1210.
    • (1993) J Virol , vol.67 , pp. 1203-1210
    • Will, C.1    Muhlberger, E.2    Linder, D.3    Slenczka, W.4    Klenk, H.D.5    Feldmann, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.