메뉴 건너뛰기




Volumn 359, Issue , 2012, Pages 79-94

Henipavirus membrane fusion and viral entry

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN B2; EPHRIN B3; GLYCOPROTEIN; HYBRID PROTEIN;

EID: 84868304865     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82-2012-200     Document Type: Article
Times cited : (48)

References (99)
  • 1
    • 0037225634 scopus 로고    scopus 로고
    • Cytoplasmic tail of moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: Implications for mechanism of action of the R peptide
    • DOI 10.1128/JVI.77.2.1281-1291.2003
    • Aguilar HC, Anderson WF, Cannon PM (2003) Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide. J Virol 77:1281-1291 (Pubitemid 36055551)
    • (2003) Journal of Virology , vol.77 , Issue.2 , pp. 1281-1291
    • Aguilar, H.C.1    Anderson, W.F.2    Cannon, P.M.3
  • 3
    • 34247557393 scopus 로고    scopus 로고
    • Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling
    • DOI 10.1128/JVI.02205-06
    • Aguilar HC, Matreyek KA, Choi DY, Filone CM, Young S, 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 (Pubitemid 46668650)
    • (2007) Journal of Virology , vol.81 , Issue.9 , 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
  • 4
    • 59449099994 scopus 로고    scopus 로고
    • A novel receptor-induced activation site in the nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)
    • Aguilar HC, Ataman ZA, Aspericueta V, Fang AQ, Stroud M, Negrete OA, Kammerer RA, Lee B (2009) A novel receptor-induced activation site in the nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J Biol Chem 284:1628-1635
    • (2009) J Biol Chem , vol.284 , pp. 1628-1635
    • Aguilar, H.C.1    Ataman, Z.A.2    Aspericueta, V.3    Fang, A.Q.4    Stroud, M.5    Negrete, O.A.6    Kammerer, R.A.7    Lee, B.8
  • 5
    • 77954976612 scopus 로고    scopus 로고
    • A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascade
    • doi:10.1128/JVI.00469-10, JVI.00469-10 [pii]
    • Aguilar HC, Aspericueta V, Robinson LR Aanensen KE, Lee B (2010) A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascade. J Virol 84:8033-8041. doi:10.1128/JVI.00469-10, JVI.00469-10 [pii]
    • (2010) J Virol , vol.84 , pp. 8033-8041
    • Aguilar, H.C.1    Aspericueta, V.2    Robinson, L.R.3    Aanensen, K.E.4    Lee, B.5
  • 6
    • 79956089435 scopus 로고    scopus 로고
    • Emerging paramyxoviruses: Molecular mechanisms and antiviral strategies
    • doi:10.1017/S1462399410001754,S1462399410001754 [pii]
    • Aguilar HC, Lee B (2011) Emerging paramyxoviruses: molecular mechanisms and antiviral strategies. Expert Rev Mol Med 13:e6. doi:10.1017/ S1462399410001754,S1462399410001754 [pii]
    • (2011) Expert Rev Mol Med , vol.13
    • Aguilar, H.C.1    Lee, B.2
  • 7
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • DOI 10.1016/S1097-2765(00)80458-X
    • Baker KA, Dutch RE, Lamb RA, Jardetzky TS (1999) Structural basis for paramyxovirus-mediated membrane fusion. Mol Cell 3:309-319 (Pubitemid 29290671)
    • (1999) Molecular Cell , vol.3 , Issue.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 8
    • 0036376658 scopus 로고    scopus 로고
    • Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment
    • DOI 10.1006/viro.2002.1497
    • Begona Ruiz-Arguello M, Gonzalez-Reyes L, Calder LJ, Palomo C, Martin D, Saiz MJ, Garcia-Barreno B, Skehel JJ, Melero JA (2002) Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment. Virology 298:317-326. S0042682202914972, [pii] (Pubitemid 35034547)
    • (2002) Virology , vol.298 , Issue.2 , pp. 317-326
    • Begona Ruiz-Arguello, M.1    Gonzalez-Reyes, L.2    Calder, L.J.3    Palomo, C.4    Martin, D.5    Saiz, M.J.6    Garcia-Barreno, B.7    Skehel, J.J.8    Melero, J.A.9
  • 10
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, Hickey AC, Khetawat D, Patch JR, Bossart KN, Zhu Z, Wang LF, Dimitrov DS, Broder CC (2008) Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding. J Virol 82:11398-11409
    • (2008) J Virol , vol.82 , pp. 11398-11409
    • Bishop, K.A.1    Hickey, A.C.2    Khetawat, D.3    Patch, J.R.4    Bossart, K.N.5    Zhu, Z.6    Wang, L.F.7    Dimitrov, D.S.8    Broder, C.C.9
  • 12
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • doi:10.1128/JVI.06350-11
    • Bose S, Welch BD, Kors CA, Yuan P, Jardetzky TS, Lamb RA (2011) Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J Virol 85:12855-12866. doi:10.1128/JVI.06350-11
    • (2011) J Virol , vol.85 , pp. 12855-12866
    • Bose, S.1    Welch, B.D.2    Kors, C.A.3    Yuan, P.4    Jardetzky, T.S.5    Lamb, R.A.6
  • 13
    • 0035841668 scopus 로고    scopus 로고
    • Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus
    • DOI 10.1006/viro.2001.1158
    • Bossart KN, Wang LF, Eaton BT, Broder CC (2001) Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology 290:121-135 (Pubitemid 33111883)
    • (2001) Virology , vol.290 , Issue.1 , pp. 121-135
    • Bossart, K.N.1    Wang, L.-F.2    Eaton, B.T.3    Broder, C.C.4
  • 14
    • 0036827695 scopus 로고    scopus 로고
    • Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins
    • DOI 10.1128/JVI.76.22.11186-11198.2002
    • Bossart KN, Wang LF, Flora MN, Chua KB, Lam SK, Eaton BT, Broder CC (2002) Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins. J Virol 76:11186-11198 (Pubitemid 35231273)
    • (2002) Journal of Virology , vol.76 , Issue.22 , pp. 11186-11198
    • Bossart, K.N.1    Wang, L.-F.2    Flora, M.N.3    Chua, K.B.4    Lam, S.K.5    Eaton, B.T.6    Broder, C.C.7
  • 15
    • 24944483017 scopus 로고    scopus 로고
    • Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein
    • Bossart KN, Mungall BA, Crameri G, Wang LF, Eaton BT, Broder CC (2005) Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein. Virol J 2:57
    • (2005) Virol J , vol.2 , pp. 57
    • Bossart, K.N.1    Mungall, B.A.2    Crameri, G.3    Wang, L.F.4    Eaton, B.T.5    Broder, C.C.6
  • 19
    • 56449121966 scopus 로고    scopus 로고
    • Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: A template for antiviral and vaccine design
    • Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM, Jones EY, Stuart DI (2008b) Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. J Virol 82:11628-11636
    • (2008) J Virol , vol.82 , pp. 11628-11636
    • Bowden, T.A.1    Crispin, M.2    Harvey, D.J.3    Aricescu, A.R.4    Grimes, J.M.5    Jones, E.Y.6    Stuart, D.I.7
  • 20
    • 33749556658 scopus 로고    scopus 로고
    • Galectin-1: A small protein with major functions
    • DOI 10.1093/glycob/cwl025
    • Camby I, Le Mercier M, Lefranc F, Kiss R (2006) Galectin-1: a small protein with major functions. Glycobiology 16:137R-157R. doi:10.1093/glycob/ cwl025, cwl025 [pii] (Pubitemid 44530693)
    • (2006) Glycobiology , vol.16 , Issue.11
    • Camby, I.1    Le Mercier, M.2    Lefranc, F.3    Kiss, R.4
  • 21
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • DOI 10.1016/0092-8674(93)90260-W
    • Carr CM, Kim PS (1993) A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73:823-832 (Pubitemid 23159019)
    • (1993) Cell , vol.73 , Issue.4 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 22
    • 19944415289 scopus 로고    scopus 로고
    • Role of N-linked glycosylation of the Hendra virus fusion protein
    • DOI 10.1128/JVI.79.12.7922-7925.2005
    • Carter JR, Pager CT, Fowler SD, Dutch RE (2005) Role of N-linked glycosylation of the Hendra virus fusion protein. J Virol 79:7922-7925 (Pubitemid 40756830)
    • (2005) Journal of Virology , vol.79 , Issue.12 , pp. 7922-7925
    • Carter, J.R.1    Pager, C.T.2    Fowler, S.D.3    Dutch, R.E.4
  • 23
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    • DOI 10.1128/JVI.00909-07
    • Corey EA, Iorio RM (2007) Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein. J Virol 81:9900-9910 (Pubitemid 350067693)
    • (2007) Journal of Virology , vol.81 , Issue.18 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 24
    • 23844555503 scopus 로고    scopus 로고
    • The Nipah virus fusion protein is cleaved within the endosomal compartment
    • DOI 10.1074/jbc.M504598200
    • Diederich S, Moll M, Klenk HD, Maisner A (2005) The Nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem 280:29899-29903 (Pubitemid 41177067)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.33 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.-D.3    Maisner, A.4
  • 25
    • 43249094400 scopus 로고    scopus 로고
    • Role of endocytosis and cathepsin-mediated activation in Nipah virus entry
    • Diederich S, Thiel L, Maisner A (2008) Role of endocytosis and cathepsin-mediated activation in Nipah virus entry. Virology 375:391-400
    • (2008) Virology , vol.375 , pp. 391-400
    • Diederich, S.1    Thiel, L.2    Maisner, A.3
  • 26
    • 0027426010 scopus 로고
    • The human CD46 molecule is a receptor for measles virus (Edmonston strain)
    • DOI 10.1016/0092-8674(93)80071-L
    • Dorig RE, Marcil A, Chopra A, Richardson CD (1993) The human CD46 molecule is a receptor for measles virus (Edmonston strain). Cell 75:295-305 (Pubitemid 23320293)
    • (1993) Cell , vol.75 , Issue.2 , pp. 295-305
    • Dorig, R.E.1    Marcil, A.2    Chopra, A.3    Richardson, C.D.4
  • 27
    • 77954683314 scopus 로고    scopus 로고
    • Entry and fusion of emerging paramyxoviruses
    • doi:10.1371/journal.ppat.1000881
    • Dutch RE (2010) Entry and fusion of emerging paramyxoviruses. PLoS Pathog 6:e1000881. doi:10.1371/journal.ppat.1000881
    • (2010) PLoS Pathog , vol.6
    • Dutch, R.E.1
  • 28
    • 0029914299 scopus 로고    scopus 로고
    • Retrovirus envelope domain at 1.7 Angstrom resolution
    • Fass D, Harrison SC, Kim PS (1996) Retrovirus envelope domain at 1.7 Angstrom resolution. Nat Struct Biol 3:465-469
    • (1996) Nat Struct Biol , vol.3 , pp. 465-469
    • Fass, D.1    Harrison, S.C.2    Kim, P.S.3
  • 29
    • 34547131827 scopus 로고    scopus 로고
    • 2 subunit of paramyxovirus fusion proteins is involved in fusion regulation
    • DOI 10.1128/JVI.00366-07
    • Gardner AE, Dutch RE (2007) A conserved region in the F(2) subunit of paramyxovirus fusion proteins is involved in fusion regulation. J Virol 81:8303-8314. doi: 10.1128/JVI.00366-07, JVI.00366-07 [pii] (Pubitemid 47101515)
    • (2007) Journal of Virology , vol.81 , Issue.15 , pp. 8303-8314
    • Gardner, A.E.1    Dutch, R.E.2
  • 30
    • 34247555336 scopus 로고    scopus 로고
    • A conserved region between the heptad repeats of paramyxovirus fusion proteins is critical for proper F protein folding
    • DOI 10.1021/bi6025648
    • Gardner AE, Martin KL, Dutch RE (2007) A conserved region between the heptad repeats of paramyxovirus fusion proteins is critical for proper F protein folding. Biochemistry 46:5094-5105. doi:10.1021/bi6025648 (Pubitemid 46683007)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5094-5105
    • Gardner, A.E.1    Martin, K.L.2    Dutch, R.E.3
  • 32
    • 0028074306 scopus 로고
    • Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones
    • Garten W, Hallenberger S, Ortmann D, Schafer W, Vey M, Angliker H, Shaw E, Klenk HD (1994) Processing of viral glycoproteins by the subtilisin-like endoprotease furin and its inhibition by specific peptidylchloroalkylketones. Biochimie 76: 217-25. 0300-9084(94) 90149-X [pii] (Pubitemid 24295536)
    • (1994) Biochimie , vol.76 , Issue.3-4 , pp. 217-225
    • Garten, W.1    Hallenberger, S.2    Ortmann, D.3    Schafer, W.4    Vey, M.5    Angliker, H.6    Shaw, E.7    Klenk, H.D.8
  • 34
    • 0141454790 scopus 로고    scopus 로고
    • Interacting domains of the HN and F proteins of Newcastle disease virus
    • DOI 10.1128/JVI.77.20.11040-11049.2003
    • Gravel KA, Morrison TG (2003) Interacting domains of the HN and F proteins of newcastle disease virus. J Virol 77:11040-11049 (Pubitemid 37204295)
    • (2003) Journal of Virology , vol.77 , Issue.20 , pp. 11040-11049
    • Gravel, K.A.1    Morrison, T.G.2
  • 37
    • 45549093277 scopus 로고    scopus 로고
    • Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor
    • doi:10.1074/jbc.M800200200, M800200200 [pii]
    • He Y, Xiao Y, Song H, Liang Q, Ju D, Chen X, Lu H, Jing W, Jiang S, Zhang L (2008) Design and evaluation of sifuvirtide, a novel HIV-1 fusion inhibitor. J Biol Chem 283:11126-11134. doi: 10.1074/jbc.M800200200, M800200200 [pii]
    • (2008) J Biol Chem , vol.283 , pp. 11126-11134
    • He, Y.1    Xiao, Y.2    Song, H.3    Liang, Q.4    Ju, D.5    Chen, X.6    Lu, H.7    Jing, W.8    Jiang, S.9    Zhang, L.10
  • 38
    • 50149093248 scopus 로고    scopus 로고
    • Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon
    • doi:10.1128/JVI.00472-08
    • Herfst S, Mas V, Ver LS, Wierda RJ, Osterhaus AD, Fouchier RA, Melero JA (2008) Low-pH-induced membrane fusion mediated by human metapneumovirus F protein is a rare, strain-dependent phenomenon. J Virol 82:8891-8895. doi:10.1128/JVI.00472-08
    • (2008) J Virol , vol.82 , pp. 8891-8895
    • Herfst, S.1    Mas, V.2    Ver, L.S.3    Wierda, R.J.4    Osterhaus, A.D.5    Fouchier, R.A.6    Melero, J.A.7
  • 39
    • 0028899494 scopus 로고
    • Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein
    • Hu A, Cathomen T, Cattaneo R, Norrby E (1995) Influence of N-linked oligosaccharide chains on the processing, cell surface expression and function of the measles virus fusion protein. J Gen Virol 76(Pt 3):705-710
    • (1995) J Gen Virol , vol.76 , Issue.PART 3 , pp. 705-710
    • Hu, A.1    Cathomen, T.2    Cattaneo, R.3    Norrby, E.4
  • 40
    • 13844269257 scopus 로고    scopus 로고
    • Fine-scale SNP map of an 11-kb genomic region at 22q13.1 containing the galectin-1 gene
    • DOI 10.1007/s10038-004-0218-4
    • Iida A, Ozaki K, Tanaka T, Nakamura Y (2005) Fine-scale SNP map of an 11-kb genomic region at 22q13.1 containing the galectin-1 gene. J Hum Genet 50:42-45. doi:10.1007/s10038-004-0218-4 (Pubitemid 40248315)
    • (2005) Journal of Human Genetics , vol.50 , Issue.1 , pp. 42-45
    • Iida, A.1    Ozaki, K.2    Tanaka, T.3    Nakamura, Y.4
  • 41
    • 41549166734 scopus 로고    scopus 로고
    • Paramyxoviruses: Different receptors - Different mechanisms of fusion
    • Iorio RM, Mahon PJ (2008) Paramyxoviruses: different receptors - different mechanisms of fusion. Trends Microbiol 16:135-137
    • (2008) Trends Microbiol , vol.16 , pp. 135-137
    • Iorio, R.M.1    Mahon, P.J.2
  • 42
    • 70350089241 scopus 로고    scopus 로고
    • Glycoprotein interactions in paramyxovirus fusion
    • doi:10.2217/fvl.09.17
    • Iorio RM, Melanson VR, Mahon PJ (2009) Glycoprotein interactions in paramyxovirus fusion. Future Virol 4:335-351. doi:10.2217/fvl.09.17
    • (2009) Future Virol , vol.4 , pp. 335-351
    • Iorio, R.M.1    Melanson, V.R.2    Mahon, P.J.3
  • 43
    • 0033079672 scopus 로고    scopus 로고
    • Recombinant vesicular stomatitis virus expressing respiratory syncytial virus (RSV) glycoproteins: RSV fusion protein can mediate infection and cell fusion
    • DOI 10.1006/viro.1998.9535
    • Kahn JS, Schnell MJ, Buonocore L, Rose JK (1999) Recombinant vesicular stomatitis virus expressing respiratory syncytial virus (RSV) glycoproteins: RSV fusion protein can mediate infection and cell fusion. Virology 254:81-91. doi:10.1006/viro.1998.9535 (Pubitemid 29391716)
    • (1999) Virology , vol.254 , Issue.1 , pp. 81-91
    • Kahn, J.S.1    Schnell, M.J.2    Buonocore, L.3    Rose, J.K.4
  • 44
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • DOI 10.1016/j.virol.2005.09.007, PII S0042682205005684
    • Lamb RA, Paterson RG, Jardetzky TS (2006) Paramyxovirus membrane fusion: lessons from the F and HN atomic structures. Virology 344:30-37 (Pubitemid 41814447)
    • (2006) Virology , vol.344 , Issue.1 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 45
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: lessons from paramyxovirus F
    • DOI 10.1016/j.sbi.2007.08.016, PII S0959440X07001236
    • Lamb RA, Jardetzky TS (2007) Structural basis of viral invasion: lessons from paramyxovirus F. Curr Opin Struct Biol 17:427-436 (Pubitemid 47451774)
    • (2007) Current Opinion in Structural Biology , vol.17 , Issue.4 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 46
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • Knipe DM, Howley PM (eds) 5th edn, vol 1. Lippincott Williams & Wilkins, Philadelphia
    • Lamb RA, Parks GD (2007) Paramyxoviridae: the viruses and their replication. In: Knipe DM, Howley PM (eds) Fields virology, 5th edn, vol 1. Lippincott Williams & Wilkins, Philadelphia, pp 1449-1496
    • (2007) Fields Virology , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 48
    • 44849109991 scopus 로고    scopus 로고
    • Evil versus 'eph-ective' use of ephrin-B2
    • DOI 10.1038/nsmb0608-540, PII NSMB0608540
    • Lee B, Ataman ZA, Jin L (2008a) Evil versus 'eph-ective' use of ephrin-B2. Nat Struct Mol Biol 15:540-542 (Pubitemid 351799145)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.6 , pp. 540-542
    • Lee, B.1    Ataman, Z.A.2    Jin, L.3
  • 49
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee JK, Prussia A, Paal T, White LK, Snyder JP, Plemper RK (2008b) Functional interaction between paramyxovirus fusion and attachment proteins. J Biol Chem 283:16561-16572
    • (2008) J Biol Chem , vol.283 , pp. 16561-16572
    • Lee, J.K.1    Prussia, A.2    Paal, T.3    White, L.K.4    Snyder, J.P.5    Plemper, R.K.6
  • 50
    • 21244502470 scopus 로고    scopus 로고
    • Novel innate immune functions for galectin-1: Galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines
    • Levroney EL, Aguilar HC, Fulcher JA, Kohatsu L, Pace KE, Pang M, Gurney KB, Baum LG, Lee B (2005) Novel innate immune functions for galectin-1: galectin-1 inhibits cell fusion by Nipah virus envelope glycoproteins and augments dendritic cell secretion of proinflammatory cytokines. J Immunol 175:413-420 (Pubitemid 40884345)
    • (2005) Journal of Immunology , vol.175 , Issue.1 , pp. 413-420
    • Levroney, E.L.1    Aguilar, H.C.2    Fulcher, J.A.3    Kohatsu, L.4    Pace, K.E.5    Pang, M.6    Gurney, K.B.7    Baum, L.G.8    Lee, B.9
  • 51
    • 33748747845 scopus 로고    scopus 로고
    • Crystal structures of Nipah and Hendra virus fusion core proteins
    • DOI 10.1111/j.1742-4658.2006.05459.x
    • Lou Z, Xu Y, Xiang K, Su N, Qin L, Li X, Gao GF, Bartlam M, Rao Z (2006) Crystal structures of Nipah and Hendra virus fusion core proteins. FEBS J 273:4538-4547 (Pubitemid 44401604)
    • (2006) FEBS Journal , vol.273 , Issue.19 , pp. 4538-4547
    • Lou, Z.1    Xu, Y.2    Xiang, K.3    Su, N.4    Qin, L.5    Li, X.6    Gao, G.F.7    Bartlam, M.8    Rao, Z.9
  • 52
    • 80655142480 scopus 로고    scopus 로고
    • Role of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion
    • doi:10.1128/JVI.05679-11
    • Mahon PJ, Mirza AM, Iorio RM (2011) Role of the two sialic acid binding sites on the newcastle disease virus HN protein in triggering the interaction with the F protein required for the promotion of fusion. J Virol 85:12079-12082. doi:10.1128/JVI.05679-11
    • (2011) J Virol , vol.85 , pp. 12079-12082
    • Mahon, P.J.1    Mirza, A.M.2    Iorio, R.M.3
  • 53
    • 65549115032 scopus 로고    scopus 로고
    • The fusion inhibitor enfuvirtide in recent antiretroviral strategies
    • doi:10.1097/COH.0b013e32832498d8, 01222929-200903000-00013 [pii]
    • Makinson A, Reynes J (2009) The fusion inhibitor enfuvirtide in recent antiretroviral strategies. Curr Opin HIV AIDS 4:150-158. doi:10.1097/COH. 0b013e32832498d8, 01222929-200903000-00013 [pii]
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 150-158
    • Makinson, A.1    Reynes, J.2
  • 54
    • 0035837043 scopus 로고    scopus 로고
    • Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity
    • DOI 10.1006/viro.2001.0899
    • McGinnes L, Sergel T, Reitter J, Morrison T (2001) Carbohydrate modifications of the NDV fusion protein heptad repeat domains influence maturation and fusion activity. Virology 283:332-342 (Pubitemid 32881180)
    • (2001) Virology , vol.283 , Issue.2 , pp. 332-342
    • McGinnes, L.1    Sergel, T.2    Reitter, J.3    Morrison, T.4
  • 55
    • 70350165412 scopus 로고    scopus 로고
    • Novel drug classes: Entry inhibitors [enfuvirtide, chemokine (C-C motif) receptor 5 antagonists]
    • doi:10.1097/COH.0b013e328331d3d0, 01222929-200911000-00010 [pii]
    • McKinnell JA, Saag MS (2009) Novel drug classes: entry inhibitors [enfuvirtide, chemokine (C-C motif) receptor 5 antagonists]. Curr Opin HIV AIDS 4: 513-517. doi:10.1097/COH.0b013e328331d3d0, 01222929-200911000-00010 [pii]
    • (2009) Curr Opin HIV AIDS , vol.4 , pp. 513-517
    • McKinnell, J.A.1    Saag, M.S.2
  • 56
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • DOI 10.1128/JVI.78.23.13053-13061.2004
    • Melanson VR, Iorio RM (2004) Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. J Virol 78:13053-13061 (Pubitemid 39507813)
    • (2004) Journal of Virology , vol.78 , Issue.23 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 57
    • 30344467852 scopus 로고    scopus 로고
    • Addition of N-Glycans in the stalk of the newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    • DOI 10.1128/JVI.80.2.623-633.2006
    • Melanson VR, Iorio RM (2006) Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion. J Virol 80:623-633 (Pubitemid 43062875)
    • (2006) Journal of Virology , vol.80 , Issue.2 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 58
    • 26444565765 scopus 로고    scopus 로고
    • Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein
    • DOI 10.1128/JVI.79.20.12643-12649.2005
    • Meulendyke KA, Wurth MA, McCann RO, Dutch RE (2005) Endocytosis plays a critical role in proteolytic processing of the Hendra virus fusion protein. J Virol 79:12643-12649 (Pubitemid 41433183)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12643-12649
    • Meulendyke, K.A.1    Wurth, M.A.2    McCann, R.O.3    Dutch, R.E.4
  • 59
    • 79955975776 scopus 로고    scopus 로고
    • Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors
    • doi:10.1074/jbc.M111.233965
    • Mirza AM, Aguilar HC, Zhu Q, Mahon PJ, Rota PA, Lee B, Iorio RM (2011) Triggering of the newcastle disease virus fusion protein by a chimeric attachment protein that binds to Nipah virus receptors. J Biol Chem 286:17851-17860. doi:10.1074/jbc.M111.233965
    • (2011) J Biol Chem , vol.286 , pp. 17851-17860
    • Mirza, A.M.1    Aguilar, H.C.2    Zhu, Q.3    Mahon, P.J.4    Rota, P.A.5    Lee, B.6    Iorio, R.M.7
  • 60
    • 70349677167 scopus 로고    scopus 로고
    • Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation
    • doi:10.1371/journal.ppat.1000585
    • Miyauchi K, Kozlov MM, Melikyan GB (2009) Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation. PLoS Pathog 5:e1000585. doi:10.1371/journal.ppat.1000585
    • (2009) PLoS Pathog , vol.5
    • Miyauchi, K.1    Kozlov, M.M.2    Melikyan, G.B.3
  • 61
    • 2942647917 scopus 로고    scopus 로고
    • Influence of N-glycans on processing and biological activity of the Nipah virus fusion protein
    • DOI 10.1128/JVI.78.13.7274-7278.2004
    • Moll M, Kaufmann A, Maisner A (2004) Influence of N-glycans on processing and biological activity of the nipah virus fusion protein. J Virol 78:7274-7278 (Pubitemid 38781566)
    • (2004) Journal of Virology , vol.78 , Issue.13 , pp. 7274-7278
    • Moll, M.1    Kaufmann, A.2    Maisner, A.3
  • 63
    • 0034830879 scopus 로고    scopus 로고
    • Mini-plasmin found in the epithelial cells of bronchioles triggers infection by broad-spectrum influenza A viruses and Sendai virus
    • DOI 10.1046/j.1432-1327.2001.02166.x
    • Murakami M, Towatari T, Ohuchi M, Shiota M, Akao M, Okumura Y, Parry MA, Kido H (2001) Mini-plasmin found in the epithelial cells of bronchioles triggers infection by broad-spectrum influenza A viruses and Sendai virus. Eur J Biochem 268:2847-55. ejb2166 [pii] (Pubitemid 32862967)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.10 , pp. 2847-2855
    • Murakami, M.1    Towatari, T.2    Ohuchi, M.3    Shiota, M.4    Akao, M.5    Okumura, Y.6    Parry, M.A.A.7    Kido, H.8
  • 64
    • 77950670872 scopus 로고    scopus 로고
    • An overview on different classes of viral entry and respiratory syncitial virus (RSV) fusion inhibitors
    • BSP/CMC/E-Pub/067 [pii]
    • Murineddu G, Murruzzu C, Pinna GA (2010) An overview on different classes of viral entry and respiratory syncitial virus (RSV) fusion inhibitors. Curr Med Chem 17:1067-1091. BSP/CMC/E-Pub/067 [pii]
    • (2010) Curr Med Chem , vol.17 , pp. 1067-1091
    • Murineddu, G.1    Murruzzu, C.2    Pinna, G.A.3
  • 67
    • 34648830167 scopus 로고    scopus 로고
    • Single amino acid changes in the Nipah and Hendra virus attachment glycoproteins distinguish ephrinb2 from ephrinb3 usage
    • DOI 10.1128/JVI.00999-07
    • Negrete OA, Chu D, Aguilar HC, Lee B (2007) Single amino acid changes in the Nipah and Hendra virus attachment glycoproteins distinguish ephrinB2 from ephrinB3 usage. J Virol 81:10804-10814 (Pubitemid 47463353)
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10804-10814
    • Negrete, O.A.1    Chu, D.2    Aguilar, H.C.3    Lee, B.4
  • 68
    • 80052315535 scopus 로고    scopus 로고
    • Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus
    • doi:10.1371/journal.ppat.1002240
    • Noyce RS, Bondre DG, Ha MN, Lin LT, Sisson G, Tsao MS, Richardson CD (2011) Tumor cell marker PVRL4 (nectin 4) is an epithelial cell receptor for measles virus. PLoS pathogens 7:e1002240. doi:10.1371/journal.ppat.1002240
    • (2011) PLoS Pathogens , vol.7
    • Noyce, R.S.1    Bondre, D.G.2    Ha, M.N.3    Lin, L.T.4    Sisson, G.5    Tsao, M.S.6    Richardson, C.D.7
  • 69
    • 0028196642 scopus 로고
    • Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2
    • Ortmann D, Ohuchi M, Angliker H, Shaw E, Garten W, Klenk HD (1994) Proteolytic cleavage of wild type and mutants of the F protein of human parainfluenza virus type 3 by two subtilisin-like endoproteases, furin and Kex2. J Virol 68:2772-2776 (Pubitemid 24091961)
    • (1994) Journal of Virology , vol.68 , Issue.4 , pp. 2772-2776
    • Ortmann, D.1    Ohuchi, M.2    Angliker, H.3    Shaw, E.4    Garten, W.5    Klenk, H.-D.6
  • 70
    • 70349747076 scopus 로고    scopus 로고
    • Probing the spatial organization of measles virus fusion complexes
    • doi:10.1128/JVI.01195-09, JVI.01195-09 [pii]
    • Paal T, Brindley MA, St Clair C, Prussia A, Guas D, Krumm SA, Synder JP, Plemper RK (2009) Probing the spatial organization of measles virus fusion complexes. J Virol 83: 10480-93. doi:10.1128/JVI.01195-09, JVI.01195-09 [pii]
    • (2009) J Virol , vol.83 , pp. 10480-10493
    • Paal, T.1    Brindley, M.A.2    St Clair, C.3    Prussia, A.4    Guas, D.5    Krumm, S.A.6    Synder, J.P.7    Plemper, R.K.8
  • 71
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein
    • DOI 10.1128/JVI.79.20.12714-12720.2005
    • Pager CT, Dutch RE (2005) Cathepsin L is involved in proteolytic processing of the Hendra virus fusion protein. J Virol 79:12714-12720 (Pubitemid 41433191)
    • (2005) Journal of Virology , vol.79 , Issue.20 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 72
    • 33644822934 scopus 로고    scopus 로고
    • A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L
    • DOI 10.1016/j.virol.2006.01.007, PII S0042682206000122
    • Pager CT, Craft WW Jr, Patch J, Dutch RE (2006) A mature and fusogenic form of the Nipah virus fusion protein requires proteolytic processing by cathepsin L. Virology 346:251-257 (Pubitemid 43357869)
    • (2006) Virology , vol.346 , Issue.2 , pp. 251-257
    • Pager, C.T.1    Craft Jr., W.W.2    Patch, J.3    Dutch, R.E.4
  • 74
    • 34648830863 scopus 로고    scopus 로고
    • Molecular determinants of antiviral potency of paramyxovirus entry inhibitors
    • DOI 10.1128/JVI.01181-07
    • Porotto M, Carta P, Deng Y, Kellogg GE, Whitt M, Lu M, Mungall BA, Moscona A (2007) Molecular determinants of antiviral potency of paramyxovirus entry inhibitors. J Virol 81:10567-10574. doi:10.1128/JVI.01181-07, JVI.01181-07 [pii] (Pubitemid 47463330)
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10567-10574
    • Porotto, M.1    Carta, P.2    Deng, Y.3    Kellogg, G.E.4    Whitt, M.5    Lu, M.6    Mungall, B.A.7    Moscona, A.8
  • 75
    • 67449092278 scopus 로고    scopus 로고
    • Kinetic dependence of paramyxovirus entry inhibition
    • doi:10.1128/JVI.00416-09, JVI.00416-09 [pii]
    • Porotto M, Yokoyama CC, Orefice G, Kim HS, Aljofan M, Mungall BA, Moscona A (2009) Kinetic dependence of paramyxovirus entry inhibition. J Virol 83:6947-6951. doi:10.1128/JVI.00416-09, JVI.00416-09 [pii]
    • (2009) J Virol , vol.83 , pp. 6947-6951
    • Porotto, M.1    Yokoyama, C.C.2    Orefice, G.3    Kim, H.S.4    Aljofan, M.5    Mungall, B.A.6    Moscona, A.7
  • 77
    • 84855270854 scopus 로고    scopus 로고
    • Spring-loaded model revisited: Paramyxovirus fusion requires engagementofa receptor binding protein beyond initial triggering of the fusion protein
    • doi:10.1128/JVI.05873-11
    • Porotto M, Devito I, Palmer SG, Jurgens EM, Yee JL, Yokoyama CC, Pessi A, Moscona A (2011) Spring-loaded model revisited: Paramyxovirus fusion requires engagementofa receptor binding protein beyond initial triggering of the fusion protein. J Virol. doi:10.1128/JVI.05873-11
    • (2011) J Virol.
    • Porotto, M.1    Devito, I.2    Palmer, S.G.3    Jurgens, E.M.4    Yee, J.L.5    Yokoyama, C.C.6    Pessi, A.7    Moscona, A.8
  • 78
    • 27944455637 scopus 로고    scopus 로고
    • Enfuvirtide, the first fusion inhibitor to treat HIV infection
    • Poveda E, Briz V, Soriano V (2005) Enfuvirtide, the first fusion inhibitor to treat HIV infection. AIDS Rev 7:139-147 (Pubitemid 41671913)
    • (2005) AIDS Reviews , vol.7 , Issue.3 , pp. 139-147
    • Poveda, E.1    Briz, V.2    Soriano, V.3
  • 79
    • 44949087724 scopus 로고    scopus 로고
    • Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity
    • DOI 10.1128/JVI.00078-08
    • Rawling J, Garcia-Barreno B, Melero JA (2008) Insertion of the two cleavage sites of the respiratory syncytial virus fusion protein in Sendai virus fusion protein leads to enhanced cell-cell fusion and a decreased dependency on the HN attachment protein for activity. J Virol 82:5986-5998. doi:10.1128/JVI.00078-08 (Pubitemid 351822272)
    • (2008) Journal of Virology , vol.82 , Issue.12 , pp. 5986-5998
    • Rawling, J.1    Garcia-Barreno, B.2    Melero, J.A.3
  • 80
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • DOI 10.1093/emboj/20.15.4024
    • Russell CJ, Jardetzky TS, Lamb RA (2001) Membrane fusion machines of paramyxoviruses: capture of intermediates of fusion. EMBO J 20:4024-4034 (Pubitemid 32751819)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 81
    • 10044243988 scopus 로고    scopus 로고
    • Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state
    • DOI 10.1128/JVI.78.24.13727-13742.2004
    • Russell CJ, Jardetzky TS, Lamb RA (2004) Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state. J Virol 78:13727-13742. doi:10.1128/JVI.78.24.13727-13742.2004 (Pubitemid 39612771)
    • (2004) Journal of Virology , vol.78 , Issue.24 , pp. 13727-13742
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 82
    • 33750698660 scopus 로고    scopus 로고
    • Characterization of human metapneumovirus F protein-promoted membrane fusion: Critical roles for proteolytic processing and low pH
    • DOI 10.1128/JVI.01287-06
    • Schowalter RM, Smith SE, Dutch RE (2006a) Characterization of human metapneumovirus F protein-promoted membrane fusion: critical roles for proteolytic processing and low pH. J Virol 80:10931-10941 (Pubitemid 44706534)
    • (2006) Journal of Virology , vol.80 , Issue.22 , pp. 10931-10941
    • Schowalter, R.M.1    Smith, S.E.2    Dutch, R.E.3
  • 83
    • 33745241365 scopus 로고    scopus 로고
    • Rho GTPase activity modulates paramyxovirus fusion protein-mediated cell-cell fusion
    • DOI 10.1016/j.virol.2006.01.033, PII S0042682206000626
    • Schowalter RM, Wurth MA, Aguilar HC, Lee B, Moncman CL, McCann RO, Dutch RE (2006b) Rho GTPase activity modulates paramyxovirus fusion protein-mediated cell-cell fusion. Virology 350:323-334 (Pubitemid 43928101)
    • (2006) Virology , vol.350 , Issue.2 , pp. 323-334
    • Schowalter, R.M.1    Wurth, M.A.2    Aguilar, H.C.3    Lee, B.4    Moncman, C.L.5    McCann, R.O.6    Dutch, R.E.7
  • 84
    • 0033914327 scopus 로고    scopus 로고
    • Functional analysis of the individual oligosaccharide chains of Sendai virus fusion protein
    • Segawa H, Yamashita T, Kawakita M, Taira H (2000) Functional analysis of the individual oligosaccharide chains of sendai virus fusion protein. J Biochem 128:65-72 (Pubitemid 30485370)
    • (2000) Journal of Biochemistry , vol.128 , Issue.1 , pp. 65-72
    • Segawa, H.1    Yamashita, T.2    Kawakita, M.3    Taira, H.4
  • 85
    • 0028054825 scopus 로고
    • Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain
    • Spies CP, Ritter GD Jr, Mulligan MJ, Compans RW (1994) Truncation of the cytoplasmic domain of the simian immunodeficiency virus envelope glycoprotein alters the conformation of the external domain. J Virol 68:585-591 (Pubitemid 24022156)
    • (1994) Journal of Virology , vol.68 , Issue.2 , pp. 585-591
    • Spies, C.P.1    Ritter Jr., G.D.2    Mulligan, M.J.3    Compans, R.W.4
  • 86
    • 0032899490 scopus 로고    scopus 로고
    • Mutational analysis of heptad repeats in the membrane-proximal region of newcastle disease virus HN protein
    • Stone-Hulslander J, Morrison TG (1999) Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein. J Virol 73:3630-3637 (Pubitemid 29189804)
    • (1999) Journal of Virology , vol.73 , Issue.5 , pp. 3630-3637
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 87
    • 0034710650 scopus 로고    scopus 로고
    • Slam (CDw150) is a cellular receptor for measles virus
    • DOI 10.1038/35022579
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y (2000) SLAM (CDw150) is a cellular receptor for measles virus. Nature 406:893-897. doi:10.1038/35022579 (Pubitemid 30664265)
    • (2000) Nature , vol.406 , Issue.6798 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 89
    • 0141521694 scopus 로고    scopus 로고
    • N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion
    • DOI 10.1128/JVI.77.19.10202-10212.2003
    • von Messling V, Cattaneo R (2003) N-linked glycans with similar location in the fusion protein head modulate paramyxovirus fusion. J Virol 77:10202-10212 (Pubitemid 37129664)
    • (2003) Journal of Virology , vol.77 , Issue.19 , pp. 10202-10212
    • Von Messling, V.1    Cattaneo, R.2
  • 91
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M, Hirano A, Stenglein S, Nelson J, Thomas G, Wong TC (1995) Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J Virol 69:3206-3210
    • (1995) J Virol , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5    Wong, T.C.6
  • 92
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • DOI 10.1080/10409230802058320, PII 794225034
    • White JM, Delos SE, Brecher M, Schornberg K (2008) Structures and mechanisms of viral membrane fusion proteins: multiple variations on a common theme. Crit Rev Biochem Mol Biol 43:189-219 (Pubitemid 351883153)
    • (2008) Critical Reviews in Biochemistry and Molecular Biology , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 93
    • 69249217927 scopus 로고    scopus 로고
    • Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: Implications for F-G complex formation
    • doi:10.1128/JVI.00414-09, JVI.00414-09 [pii]
    • Whitman SD, Smith EC, Dutch RE (2009) Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation. J Virol 83:8998-9001. doi:10.1128/JVI.00414-09, JVI.00414-09 [pii]
    • (2009) J Virol , vol.83 , pp. 8998-9001
    • Whitman, S.D.1    Smith, E.C.2    Dutch, R.E.3
  • 94
    • 25144488199 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail
    • DOI 10.1128/JVI.79.19.12231-12241.2005
    • Wyss S, Dimitrov AS, Baribaud F, Edwards TG, Blumenthal R, Hoxie JA (2005) Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail. J Virol 79:12231-12241 (Pubitemid 41346084)
    • (2005) Journal of Virology , vol.79 , Issue.19 , pp. 12231-12241
    • Wyss, S.1    Dimitrov, A.S.2    Baribaud, F.3    Edwards, T.G.4    Blumenthal, R.5    Hoxie, J.A.6
  • 95
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the henipaviruses: Crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3
    • Xu K, Rajashankar KR, Chan YP, Himanen JP, Broder CC, Nikolov DB (2008) Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci U S A 105:9953-9958
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9953-9958
    • Xu, K.1    Rajashankar, K.R.2    Chan, Y.P.3    Himanen, J.P.4    Broder, C.C.5    Nikolov, D.B.6
  • 96
    • 5344242318 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the fusion core from two new zoonotic paramyxoviruses, Nipah virus and Hendra virus
    • DOI 10.1107/S0907444904009515
    • Xu Y, Lou Z, Liu Y, Cole DK, Su N, Qin L, Li X, Bai Z, Rao Z, Gao GF (2004) Crystallization and preliminary crystallographic analysis of the fusion core from two new zoonotic paramyxoviruses, Nipah virus and Hendra virus. Acta Crystallogr D Biol Crystallogr 60:1161-1164. doi:10.1107/S0907444904009515 (Pubitemid 41295468)
    • (2004) Acta Crystallographica Section D: Biological Crystallography , vol.60 , Issue.6 , pp. 1161-1164
    • Xu, Y.1    Lou, Z.2    Liu, Y.3    Cole, D.K.4    Su, N.5    Qin, L.6    Li, X.7    Bai, Z.8    Rao, Z.9    Gao, G.F.10
  • 98
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • DOI 10.1038/nature04322
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS (2006) Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439:38-44 (Pubitemid 43053622)
    • (2006) Nature , vol.439 , Issue.7072 , pp. 38-44
    • Yin, H.-S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 99
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • doi:10.1073/pnas.1111691108
    • Yuan P, Swanson KA, Leser GP, Paterson RG, Lamb RA, Jardetzky TS (2011) Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc Natl Acad Sci U S A 108:14920-14925. doi:10.1073/pnas.1111691108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14920-14925
    • Yuan, P.1    Swanson, K.A.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.