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Volumn 4, Issue 1, 2006, Pages 43-55

Developments towards effective treatments for Nipah and Hendra virus infection

Author keywords

Antiviral therapies; Entry; Envelope glycoprotein; Fusion; Hendra; Membrane; Monoclonal antibody; Nipah; Paramyxovirus; Receptor; Vaccine

Indexed keywords

ALPHA2B INTERFERON; ANTIVIRUS AGENT; CATHEPSIN L; CATHEPSIN L INHIBITOR; CELL PROTEIN; ENFUVIRTIDE; EPHRIN B2; EPHRIN B4; GLYCOPROTEIN; HEMAGGLUTININ; HYBRID PROTEIN; INTERFERON; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PALIVIZUMAB; PROTEINASE INHIBITOR; RIBAVIRIN; SIALIDASE; STAT1 PROTEIN; STAT2 PROTEIN; UNCLASSIFIED DRUG; VACCINIA VACCINE; VIRUS PROTEIN; VIRUS RECEPTOR; VIRUS VACCINE; VIRUS ANTIBODY;

EID: 33645086686     PISSN: 14787210     EISSN: 17448336     Source Type: Journal    
DOI: 10.1586/14787210.4.1.43     Document Type: Review
Times cited : (25)

References (110)
  • 1
    • 0001178028 scopus 로고    scopus 로고
    • Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA
    • Lamb RA, Kolakofsky D. Fields Virology. Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA, 1305-1340 (2001).
    • (2001) Fields Virology , pp. 1305-1340
    • Lamb, R.A.1    Kolakofsky, D.2
  • 2
    • 0002641210 scopus 로고    scopus 로고
    • Scheld WM, Armstrong D, Hughes JM (Eds). ASM Press, Washington, DC, USA
    • Murray K, Eaton B, Hooper P et al. Emerging Infections. Scheld WM, Armstrong D, Hughes JM (Eds). ASM Press, Washington, DC, USA, 43-58 (1998).
    • (1998) Emerging Infections , pp. 43-58
    • Murray, K.1    Eaton, B.2    Hooper, P.3
  • 3
    • 0037375269 scopus 로고    scopus 로고
    • Nipah virus outbreak in Malaysia
    • Chua KB. Nipah virus outbreak in Malaysia. J Clin. Virol. 26, 265-275 (2003).
    • (2003) J Clin. Virol. , vol.26 , pp. 265-275
    • Chua, K.B.1
  • 4
    • 0029041280 scopus 로고
    • Infection of humans and horses by a newly described morbillivirus
    • Selvey LA, Wells RM, McCormack JG et al. Infection of humans and horses by a newly described morbillivirus. Med. J. Aust. 162, 642-645 (1995).
    • (1995) Med. J. Aust. , vol.162 , pp. 642-645
    • Selvey, L.A.1    Wells, R.M.2    McCormack, J.G.3
  • 5
    • 0036899143 scopus 로고    scopus 로고
    • Nipah virus infection: Pathology and pathogenesis of an emerging paramyxoviral zoonosis
    • Wong KT, Shieh WJ, Kumar S et al. Nipah virus infection: pathology and pathogenesis of an emerging paramyxoviral zoonosis. Am. J. Pathol. 161, 2153-2167 (2002).
    • (2002) Am. J. Pathol. , vol.161 , pp. 2153-2167
    • Wong, K.T.1    Shieh, W.J.2    Kumar, S.3
  • 6
    • 0037258831 scopus 로고    scopus 로고
    • Nipah encephalitis outbreak in Malaysia
    • Tan CT, Wong KT. Nipah encephalitis outbreak in Malaysia. Ann. Acad. Med. Singapore 32, 112-117 (2003).
    • (2003) Ann. Acad. Med. Singapore , vol.32 , pp. 112-117
    • Tan, C.T.1    Wong, K.T.2
  • 7
    • 0033871684 scopus 로고    scopus 로고
    • Isolation of Hendra virus from pteropid bats: A natural reservoir of Hendra virus
    • Halpin K, Young PL, Field HE, Mackenzie JS. Isolation of Hendra virus from pteropid bats: a natural reservoir of Hendra virus. J Gen. Virol. 81, 1927-1932 (2000).
    • (2000) J Gen. Virol. , vol.81 , pp. 1927-1932
    • Halpin, K.1    Young, P.L.2    Field, H.E.3    Mackenzie, J.S.4
  • 8
    • 0036185623 scopus 로고    scopus 로고
    • Isolation of Nipah virus from Malaysian island flying-foxes
    • Chua KB, Lek Koh C, Hooi PS et al. Isolation of Nipah virus from Malaysian island flying-foxes. Microbes Infect. 4, 145-151 (2002).
    • (2002) Microbes Infect. , vol.4 , pp. 145-151
    • Chua, K.B.1    Lek Koh, C.2    Hooi, P.S.3
  • 10
    • 30344434590 scopus 로고    scopus 로고
    • Emerging infections update: November 2004 to January 2005
    • Anonymous
    • Anonymous. Emerging infections update: November 2004 to January 2005. Commun. Dis. Rep. Wkly 15 (2005).
    • (2005) Commun. Dis. Rep. Wkly , vol.15
  • 11
    • 25644446760 scopus 로고    scopus 로고
    • Nipah encephalitis outbreak over wide area of western Bangladesh 2004
    • Anonymous
    • Anonymous. Nipah encephalitis outbreak over wide area of western Bangladesh, 2004. Health and Science Bulletin (ICDDR,B) 2, 7-11 (2004).
    • (2004) Health and Science Bulletin (ICDDR,B) , vol.2 , pp. 7-11
  • 12
    • 9744233639 scopus 로고    scopus 로고
    • Nipah virus encephalitis reemergence, Bangladesh
    • Hsu VP, Hossain MJ, Parashar UD et al. Nipah virus encephalitis reemergence, Bangladesh. Emerg. Infect. Dis. 10, 2082-2087 (2004).
    • (2004) Emerg. Infect. Dis. , vol.10 , pp. 2082-2087
    • Hsu, V.P.1    Hossain, M.J.2    Parashar, U.D.3
  • 13
    • 18744388130 scopus 로고    scopus 로고
    • Person-to-person transmission of Nipah virus during outbreak in Faridpur District, 2004
    • Anonymous
    • Anonymous. Person-to-person transmission of Nipah virus during outbreak in Faridpur District, 2004. Health and Science Bulletin (ICDDR,B) 2, 5-9 (2004).
    • (2004) Health and Science Bulletin (ICDDR,B) , vol.2 , pp. 5-9
  • 14
    • 0035028638 scopus 로고    scopus 로고
    • Comparative pathology of the diseases caused by Hendra and Nipah viruses
    • Hooper P, Zaki S, Daniels P, Middleton D. Comparative pathology of the diseases caused by Hendra and Nipah viruses. Microbes Infect. 3, 315-322 (2001).
    • (2001) Microbes Infect. , vol.3 , pp. 315-322
    • Hooper, P.1    Zaki, S.2    Daniels, P.3    Middleton, D.4
  • 15
    • 0036570121 scopus 로고    scopus 로고
    • Nipah virus encephalitis outbreak in Malaysia
    • Lam SK, Chua KB. Nipah virus encephalitis outbreak in Malaysia. Clin. Infect. Dis. 34, S48-S51 (2002).
    • (2002) Clin. Infect. Dis. , vol.34
    • Lam, S.K.1    Chua, K.B.2
  • 16
    • 23044517161 scopus 로고    scopus 로고
    • Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus
    • Bonaparte MI, Dimitrov AS, Bossart KN et al. Ephrin-B2 ligand is a functional receptor for Hendra virus and Nipah virus. Proc. Natl Acad. Sci. USA 102, 10652-10657 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 10652-10657
    • Bonaparte, M.I.1    Dimitrov, A.S.2    Bossart, K.N.3
  • 17
    • 22944445501 scopus 로고    scopus 로고
    • EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus
    • Negrete OA, Levroney EL, Aguilar HC et al. EphrinB2 is the entry receptor for Nipah virus, an emergent deadly paramyxovirus. Nature 436, 401-405 (2005).
    • (2005) Nature , vol.436 , pp. 401-405
    • Negrete, O.A.1    Levroney, E.L.2    Aguilar, H.C.3
  • 18
    • 5044240692 scopus 로고    scopus 로고
    • Diverse roles of eph receptors and ephrins in the regulation of cell migration and tissue assembly
    • Poliakov A, Cotrina M, Wilkinson DG. Diverse roles of eph receptors and ephrins in the regulation of cell migration and tissue assembly. Dev. Cell 7, 465-480 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 465-480
    • Poliakov, A.1    Cotrina, M.2    Wilkinson, D.G.3
  • 19
    • 0036668277 scopus 로고    scopus 로고
    • Eph family functions from an evolutionary perspective
    • Drescher U. Eph family functions from an evolutionary perspective. Curr. Opin. Genet. Dev. 12, 397-402 (2002).
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 397-402
    • Drescher, U.1
  • 20
    • 0031922119 scopus 로고    scopus 로고
    • The ephrins and Eph receptors in neural development
    • Flanagan JG, Vanderhaeghen P. The ephrins and Eph receptors in neural development. Ann. Rev. Neurosci. 21, 309-345 (1998).
    • (1998) Ann. Rev. Neurosci. , vol.21 , pp. 309-345
    • Flanagan, J.G.1    Vanderhaeghen, P.2
  • 21
    • 0033082959 scopus 로고    scopus 로고
    • Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis
    • Adams RH, Wilkinson GA, Weiss C et al. Roles of ephrinB ligands and EphB receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. Genes Dev. 13, 295-306 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 295-306
    • Adams, R.H.1    Wilkinson, G.A.2    Weiss, C.3
  • 22
    • 0032577446 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • Wang HU, Chen ZF, Anderson DJ. Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell93, 741-753 (1998).
    • (1998) Cell , vol.93 , pp. 741-753
    • Wang, H.U.1    Chen, Z.F.2    Anderson, D.J.3
  • 23
    • 0035344630 scopus 로고    scopus 로고
    • Nipah virus infection in bats (order Chiroptera) in peninsular Malaysia
    • Yob JM, Field H, Rashdi AM et al. Nipah virus infection in bats (order Chiroptera) in peninsular Malaysia. Emerg. Infect. Dis. 7, 439-441 (2001).
    • (2001) Emerg. Infect. Dis. , vol.7 , pp. 439-441
    • Yob, J.M.1    Field, H.2    Rashdi, A.M.3
  • 25
    • 19944409336 scopus 로고    scopus 로고
    • Invasion of the central nervous system in a porcine host by Nipah virus
    • Weingartl H, Czub S, Copps J et al. Invasion of the central nervous system in a porcine host by Nipah virus. J. Virol. 79, 7528-7534 (2005).
    • (2005) J. Virol. , vol.79 , pp. 7528-7534
    • Weingartl, H.1    Czub, S.2    Copps, J.3
  • 26
    • 0034744393 scopus 로고    scopus 로고
    • Laboratory diagnosis of Nipah and Hendra virus infections
    • Daniels P, Ksiazek T, Eaton BT. Laboratory diagnosis of Nipah and Hendra virus infections. Microbes Infect. 3, 289-295 (2001).
    • (2001) Microbes Infect. , vol.3 , pp. 289-295
    • Daniels, P.1    Ksiazek, T.2    Eaton, B.T.3
  • 27
    • 0029331121 scopus 로고
    • Equine morbillivirus pneumonia: Susceptibility of laboratory animals to the virus
    • Westbury HA, Hooper PT, Selleck PW, Murray PK. Equine morbillivirus pneumonia: susceptibility of laboratory animals to the virus. Aust. Vet. J. 72, 278-279 (1995).
    • (1995) Aust. Vet. J. , vol.72 , pp. 278-279
    • Westbury, H.A.1    Hooper, P.T.2    Selleck, P.W.3    Murray, P.K.4
  • 28
    • 0031183813 scopus 로고    scopus 로고
    • The lesions of experimental equine morbillivirus disease in cats and guinea-pigs
    • Hooper PT, Westbury HA, Russell GM. The lesions of experimental equine morbillivirus disease in cats and guinea-pigs. Vet. Pathol. 34, 323-329 (1997).
    • (1997) Vet. Pathol. , vol.34 , pp. 323-329
    • Hooper, P.T.1    Westbury, H.A.2    Russell, G.M.3
  • 30
    • 0142244178 scopus 로고    scopus 로고
    • A golden hamster model for human acute Nipah virus infection
    • Wong KT, Grosjean I, Brisson C et al. A golden hamster model for human acute Nipah virus infection. Am. J. Pathol. 163, 2127-2137 (2003).
    • (2003) Am. J. Pathol. , vol.163 , pp. 2127-2137
    • Wong, K.T.1    Grosjean, I.2    Brisson, C.3
  • 31
    • 0031179382 scopus 로고    scopus 로고
    • Lesions of experimental equine morbillivirus pneumonia in horses
    • Hooper PT, Ketterer PJ, Hyatt AD, Russell GM. Lesions of experimental equine morbillivirus pneumonia in horses. Vet. Pathol. 34, 312-322 (1997).
    • (1997) Vet. Pathol. , vol.34 , pp. 312-322
    • Hooper, P.T.1    Ketterer, P.J.2    Hyatt, A.D.3    Russell, G.M.4
  • 33
    • 0032234932 scopus 로고    scopus 로고
    • Transmission studies of Hendra virus (equine morbillivirus) in fruit bats, horses and cats
    • Williamson MM, Hooper PT, Selleck PW et al. Transmission studies of Hendra virus (equine morbillivirus) in fruit bats, horses and cats. Aust. Vet. J. 76, 813-818 (1998).
    • (1998) Aust. Vet. J. , vol.76 , pp. 813-818
    • Williamson, M.M.1    Hooper, P.T.2    Selleck, P.W.3
  • 34
    • 0035283309 scopus 로고    scopus 로고
    • The three faces of paramyxovirus attachment proteins
    • Morrison TG. The three faces of paramyxovirus attachment proteins. Trends Microbiol. 9, 103-105 (2001).
    • (2001) Trends Microbiol. , vol.9 , pp. 103-105
    • Morrison, T.G.1
  • 35
    • 0000708194 scopus 로고    scopus 로고
    • Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA
    • Murphy BR, Chanock RM. Fields Virology. Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA, 435-468 (2001).
    • (2001) Fields Virology , pp. 435-468
    • Murphy, B.R.1    Chanock, R.M.2
  • 36
    • 0003063065 scopus 로고    scopus 로고
    • Galasso G, Whitley R, Merigan TC (Eds). Raven Press, NY, USA
    • Quinnan GV. Antiviral Agents and Human Viral Disease. Galasso G, Whitley R, Merigan TC (Eds). Raven Press, NY, USA, 791-834 (1997).
    • (1997) Antiviral Agents and Human Viral Disease , pp. 791-834
    • Quinnan, G.V.1
  • 37
    • 4043060710 scopus 로고    scopus 로고
    • Correlates of immune protection in HIV-1 infection: What we know, what we don't know, what we should know
    • Pantaleo G, Koup RA. Correlates of immune protection in HIV-1 infection: what we know, what we don't know, what we should know. Nat. Med. 10, 806-810 (2004).
    • (2004) Nat. Med. , vol.10 , pp. 806-810
    • Pantaleo, G.1    Koup, R.A.2
  • 38
    • 0028902014 scopus 로고
    • Immune responses during measles virus infection
    • Griffin DE. Immune responses during measles virus infection. Curr. Top. Microbiol. Immunol. 191, 117-134 (1995).
    • (1995) Curr. Top. Microbiol. Immunol. , vol.191 , pp. 117-134
    • Griffin, D.E.1
  • 39
    • 9144273525 scopus 로고    scopus 로고
    • Nipah virus: Vaccination and passive protection studies in a hamster model
    • Guillaume V, Contamin H, Loth P et al. Nipah virus: vaccination and passive protection studies in a hamster model. J. Virol. 78, 834-840 (2004).
    • (2004) J. Virol. , vol.78 , pp. 834-840
    • Guillaume, V.1    Contamin, H.2    Loth, P.3
  • 40
    • 21044446226 scopus 로고    scopus 로고
    • Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus
    • Bossart KN, Crameri G, Dimitrov AS et al. Receptor binding, fusion inhibition, and induction of cross-reactive neutralizing antibodies by a soluble G glycoprotein of Hendra virus. J Virol. 79, 6690-6702 (2005).
    • (2005) J Virol. , vol.79 , pp. 6690-6702
    • Bossart, K.N.1    Crameri, G.2    Dimitrov, A.S.3
  • 41
    • 0141761519 scopus 로고    scopus 로고
    • Vaccinia vectors as candidate vaccines: The development of modified vaccinia virus Ankara for antigen delivery
    • Sutter G, Staib C. Vaccinia vectors as candidate vaccines: the development of modified vaccinia virus Ankara for antigen delivery. Curr. Drug Targets Infect. Disord. 3, 263-271 (2003).
    • (2003) Curr. Drug Targets Infect. Disord. , vol.3 , pp. 263-271
    • Sutter, G.1    Staib, C.2
  • 42
    • 4344684061 scopus 로고    scopus 로고
    • Poxvirus-based vaccine candidates for HIV: Two decades of experience with special emphasis on canarypox vectors
    • Franchini G, Gurunathan S, Baglyos L, Plotkin S, Tartaglia J. Poxvirus-based vaccine candidates for HIV: two decades of experience with special emphasis on canarypox vectors. Expert Rev. Vaccines 3(4 Suppl.), S75-S88 (2004).
    • (2004) Expert Rev. Vaccines , vol.3 , Issue.4 SUPPL.
    • Franchini, G.1    Gurunathan, S.2    Baglyos, L.3    Plotkin, S.4    Tartaglia, J.5
  • 43
    • 0033573545 scopus 로고    scopus 로고
    • Recombinant vaccinia viruses. Design, generation, and isolation
    • Broder CC, Earl PL. Recombinant vaccinia viruses. Design, generation, and isolation. Mol. Biotechnol. 13, 223-245 (1999).
    • (1999) Mol. Biotechnol. , vol.13 , pp. 223-245
    • Broder, C.C.1    Earl, P.L.2
  • 44
  • 45
    • 0027504661 scopus 로고
    • Genetically engineered multi-component virus-like particles as veterinary vaccines
    • Pearson LD, Roy P. Genetically engineered multi-component virus-like particles as veterinary vaccines. Immunol. Cell Biol. 71(Pt 5), 381-389 (1993).
    • (1993) Immunol. Cell Biol. , vol.71 , Issue.PART 5 , pp. 381-389
    • Pearson, L.D.1    Roy, P.2
  • 46
    • 4344691826 scopus 로고    scopus 로고
    • Vaccination strategies for the treatment and prevention of cervical cancer
    • Schreckenberger C, Kaufmann AM. Vaccination strategies for the treatment and prevention of cervical cancer. Curr. Opin. Oncol. 16, 485-491 (2004).
    • (2004) Curr. Opin. Oncol. , vol.16 , pp. 485-491
    • Schreckenberger, C.1    Kaufmann, A.M.2
  • 47
    • 30344474011 scopus 로고    scopus 로고
    • Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodies
    • Zhu Z, Dimitrov, AS, Bossart KN et al. Potent neutralization of Hendra and Nipah viruses by human monoclonal antibodies. J. Virol. 80, 891-899 (2006).
    • (2006) J. Virol. , vol.80 , pp. 891-899
    • Zhu, Z.1    Dimitrov, A.S.2    Bossart, K.N.3
  • 48
    • 0032819934 scopus 로고    scopus 로고
    • Passive antibody therapies: Progress and continuing challenges
    • Casadevall A. Passive antibody therapies: progress and continuing challenges. Clin. Immunol. 93, 5-15 (1999).
    • (1999) Clin. Immunol. , vol.93 , pp. 5-15
    • Casadevall, A.1
  • 49
    • 0027078548 scopus 로고
    • Genetically engineered antibodies: Progress and prospects
    • Wright A, Shin SU, Morrison SL. Genetically engineered antibodies: progress and prospects. Crit. Rev. Immunol. 12, 125-168 (1992).
    • (1992) Crit. Rev. Immunol. , vol.12 , pp. 125-168
    • Wright, A.1    Shin, S.U.2    Morrison, S.L.3
  • 50
    • 0026336406 scopus 로고
    • Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries
    • Kang AS, Jones TM, Burton DR. Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries. Proc. Natl Acad Sci. USA 88, 11120-11123 (1991).
    • (1991) Proc. Natl Acad Sci. USA , vol.88 , pp. 11120-11123
    • Kang, A.S.1    Jones, T.M.2    Burton, D.R.3
  • 52
    • 0030752337 scopus 로고    scopus 로고
    • Phage display of combinatorial antibody libraries
    • Rader C, Barbas CF III. Phage display of combinatorial antibody libraries. Curr. Opin. Biotechnol. 8, 503-508 (1997).
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 503-508
    • Rader, C.1    Barbas III., C.F.2
  • 54
    • 0035462330 scopus 로고    scopus 로고
    • Recombinant antibodies for cancer diagnosis and therapy
    • Hudson PJ, Souriau C. Recombinant antibodies for cancer diagnosis and therapy. Expert Opin. Biol. Ther. 1, 845-855 (2001).
    • (2001) Expert Opin. Biol. Ther. , vol.1 , pp. 845-855
    • Hudson, P.J.1    Souriau, C.2
  • 55
    • 0032902197 scopus 로고    scopus 로고
    • Structural basis for membrane fusion by enveloped viruses
    • Weissenhorn W, Dessen A, Calder LJ et al. Structural basis for membrane fusion by enveloped viruses. Mol. Membr. Biol. 16, 3-9 (1999).
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 3-9
    • Weissenhorn, W.1    Dessen, A.2    Calder, L.J.3
  • 56
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan DC, Kim PS. HIV entry and its inhibition. Cell 93, 681-684 (1998).
    • (1998) Cell , vol.93 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 57
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel JJ, Wiley DC. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 95, 871-874 (1998).
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 58
    • 0033618320 scopus 로고    scopus 로고
    • LearnCoil-VMF: Computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins
    • Singh M, Berger B, Kim PS. LearnCoil-VMF: computational evidence for coiled-coil-like motifs in many viral membrane-fusion proteins. J. Mol. Biol. 290, 1031-1041 (1999).
    • (1999) J. Mol. Biol. , vol.290 , pp. 1031-1041
    • Singh, M.1    Berger, B.2    Kim, P.S.3
  • 59
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: A common mode of membrane fusion?
    • Hughson FM. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7, R565-R569 (1997).
    • (1997) Curr. Biol. , vol.7
    • Hughson, F.M.1
  • 60
    • 1242340426 scopus 로고    scopus 로고
    • Basis for fusion inhibition by peptides: Analysis of the heptad repeat regions of the fusion proteins from Nipah and Hendra viruses, newly emergent zoonotic paramyxoviruses
    • Xu Y, Gao S, Cole DK et al. Basis for fusion inhibition by peptides: analysis of the heptad repeat regions of the fusion proteins from Nipah and Hendra viruses, newly emergent zoonotic paramyxoviruses. Biochem. Biophys. Res. Commun. 315, 664-670 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 664-670
    • Xu, Y.1    Gao, S.2    Cole, D.K.3
  • 61
    • 0035841668 scopus 로고    scopus 로고
    • Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus
    • Bossart KN, Wang LF, Eaton BT, Broder CC. Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology 290, 121-135 (2001).
    • (2001) Virology , vol.290 , pp. 121-135
    • Bossart, K.N.1    Wang, L.F.2    Eaton, B.T.3    Broder, C.C.4
  • 62
    • 0025678671 scopus 로고
    • Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins
    • Chambers P, Pringle CR, Easton AJ. Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins. J. Gen. Virol. 71, 3075-3080 (1990).
    • (1990) J. Gen. Virol. , vol.71 , pp. 3075-3080
    • Chambers, P.1    Pringle, C.R.2    Easton, A.J.3
  • 64
    • 1342265790 scopus 로고    scopus 로고
    • HIV-1 gp41: Mediator of fusion and target for inhibition
    • Weiss CD. HIV-1 gp41: mediator of fusion and target for inhibition. AIDS Rev. 5, 214-221 (2003).
    • (2003) AIDS Rev. , vol.5 , pp. 214-221
    • Weiss, C.D.1
  • 65
    • 0031729823 scopus 로고    scopus 로고
    • Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry
    • Kilby JM, Hopkins S, Venetta TM et al. Potent suppression of HIV-1 replication in humans by T-20, a peptide inhibitor of gp41-mediated virus entry. Nat. Med. 4, 1302-1307 (1998).
    • (1998) Nat. Med. , vol.4 , pp. 1302-1307
    • Kilby, J.M.1    Hopkins, S.2    Venetta, T.M.3
  • 66
    • 0036066762 scopus 로고    scopus 로고
    • The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults
    • Kilby JM, Lalezari JP, Eron JJ et al. The safety, plasma pharmacokinetics, and antiviral activity of subcutaneous enfuvirtide (T-20), a peptide inhibitor of gp41-mediated virus fusion, in HIV-infected adults. AIDS Res. Hum. Retroviruses 18, 685-693 (2002).
    • (2002) AIDS Res. Hum. Retroviruses , vol.18 , pp. 685-693
    • Kilby, J.M.1    Lalezari, J.P.2    Eron, J.J.3
  • 67
    • 5344242318 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic analysis of the fusion core from two new zoonotic paramyxoviruses, Nipah virus and Hendra virus
    • Xu Y, Lou Z, Liu Y et al. 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 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1161-1164
    • Xu, Y.1    Lou, Z.2    Liu, Y.3
  • 68
    • 9044234408 scopus 로고    scopus 로고
    • Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion
    • Lambert DM, Barney S, Lambert AL et al. Peptides from conserved regions of paramyxovirus fusion (F) proteins are potent inhibitors of viral fusion. Proc. Natl Acad. Sci. USA 93, 2186-2191 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 2186-2191
    • Lambert, D.M.1    Barney, S.2    Lambert, A.L.3
  • 69
    • 0032529672 scopus 로고    scopus 로고
    • A core trimer of the paramyxovirus fusion protein: Parallels to influenza virus hemagglutinin and HIV-1 gp41
    • Joshi SB, Dutch RE, Lamb RA. A core trimer of the paramyxovirus fusion protein: parallels to influenza virus hemagglutinin and HIV-1 gp41. Virology 248, 20-34 (1998).
    • (1998) Virology , vol.248 , pp. 20-34
    • Joshi, S.B.1    Dutch, R.E.2    Lamb, R.A.3
  • 70
    • 0031022688 scopus 로고    scopus 로고
    • Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein
    • Wild TF, Buckland R. Inhibition of measles virus infection and fusion with peptides corresponding to the leucine zipper region of the fusion protein. J. Gen. Virol. 78, 107-111 (1997).
    • (1997) J. Gen. Virol. , vol.78 , pp. 107-111
    • Wild, T.F.1    Buckland, R.2
  • 71
    • 0033064154 scopus 로고    scopus 로고
    • Interaction of peptides with sequences from the Newcastle disease virus fusion protein heptad repeat regions
    • Young JK, Li D, Abramowitz MC, Morrison TG. Interaction of peptides with sequences from the Newcastle disease virus fusion protein heptad repeat regions. J. Virol. 73, 5945-5956 (1999).
    • (1999) J. Virol. , vol.73 , pp. 5945-5956
    • Young, J.K.1    Li, D.2    Abramowitz, M.C.3    Morrison, T.G.4
  • 72
    • 0031585556 scopus 로고    scopus 로고
    • Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling
    • Young JK, Hicks RP, Wright GE, Morrison TG. Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling. Virology 238, 291-304 (1997).
    • (1997) Virology , vol.238 , pp. 291-304
    • Young, J.K.1    Hicks, R.P.2    Wright, G.E.3    Morrison, T.G.4
  • 73
    • 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, Shai Y. 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 J. 14, 5524-5531 (1995).
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 74
    • 0036827695 scopus 로고    scopus 로고
    • Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins
    • Bossart KN, Wang LF, Flora MN et al. Membrane fusion tropism and heterotypic functional activities of the Nipah virus and Hendra virus envelope glycoproteins. J. Virol. 76, 11186-11198 (2002).
    • (2002) J. Virol. , vol.76 , pp. 11186-11198
    • Bossart, K.N.1    Wang, L.F.2    Flora, M.N.3
  • 75
    • 4043123101 scopus 로고    scopus 로고
    • Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectors
    • Bossart KN, Broder CC. Viral glycoprotein-mediated cell fusion assays using vaccinia virus vectors. Methods Mol. Biol. 269, 309-332 (2004).
    • (2004) Methods Mol. Biol. , vol.269 , pp. 309-332
    • Bossart, K.N.1    Broder, C.C.2
  • 76
    • 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 et al. Inhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein. Virol. J. 2, 57 (2005).
    • (2005) Virol. J. , vol.2 , pp. 57
    • Bossart, K.N.1    Mungall, B.A.2    Crameri, G.3
  • 77
    • 17844380498 scopus 로고    scopus 로고
    • Pegylation: A novel process for modifying pharmacokinetics
    • Harris JM, Martin NE, Modi M. Pegylation: a novel process for modifying pharmacokinetics. Clin. Pharmacokinet. 40, 539-551 (2001).
    • (2001) Clin. Pharmacokinet. , vol.40 , pp. 539-551
    • Harris, J.M.1    Martin, N.E.2    Modi, M.3
  • 78
    • 0030061068 scopus 로고    scopus 로고
    • Enhanced tumour specificity of an anticarcinoembrionic antigen Fab' fragment by poly(ethylene glycol) (PEG) modification
    • Delgado C, Pedley RB, Herraez A et al. Enhanced tumour specificity of an anticarcinoembrionic antigen Fab' fragment by poly(ethylene glycol) (PEG) modification. Br. J. Cancer 73, 175-182 (1996).
    • (1996) Br. J. Cancer , vol.73 , pp. 175-182
    • Delgado, C.1    Pedley, R.B.2    Herraez, A.3
  • 79
    • 0028606566 scopus 로고
    • Quantitative analysis of polyethylene glycol (PEG) in PEG-modified proteins/cytokines by aqueous two-phase systems
    • Delgado C, Malik F, Selisko B, Fisher D, Francis GE. Quantitative analysis of polyethylene glycol (PEG) in PEG-modified proteins/cytokines by aqueous two-phase systems. J. Biochem. Biophys. Methods 29, 237-250 (1994).
    • (1994) J. Biochem. Biophys. Methods , vol.29 , pp. 237-250
    • Delgado, C.1    Malik, F.2    Selisko, B.3    Fisher, D.4    Francis, G.E.5
  • 80
    • 0344420226 scopus 로고    scopus 로고
    • Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates
    • Caliceti P, Veronese FM. Pharmacokinetic and biodistribution properties of poly(ethylene glycol)-protein conjugates. Adv. Drug Deliv. Rev. 55, 1261-1277 (2003).
    • (2003) Adv. Drug Deliv. Rev. , vol.55 , pp. 1261-1277
    • Caliceti, P.1    Veronese, F.M.2
  • 81
    • 26444552119 scopus 로고    scopus 로고
    • Cathepsin L is involved in proteolytic processing of the hendra virus fusion protein
    • Pager CT, Dutch RE. Cathepsin L is involved in proteolytic processing of the hendra virus fusion protein. J. Virol. 79, 12714-12720 (2005).
    • (2005) J. Virol. , vol.79 , pp. 12714-12720
    • Pager, C.T.1    Dutch, R.E.2
  • 82
    • 0035985071 scopus 로고    scopus 로고
    • Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro
    • Sever N, Filipic M, Brzin J, Lah TT. Effect of cysteine proteinase inhibitors on murine B16 melanoma cell invasion in vitro. Biol. Chem. 383, 839-842 (2002).
    • (2002) Biol. Chem. , vol.383 , pp. 839-842
    • Sever, N.1    Filipic, M.2    Brzin, J.3    Lah, T.T.4
  • 83
    • 0032561376 scopus 로고    scopus 로고
    • Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption
    • Yasuma T, Oi S, Choh N et al. Synthesis of peptide aldehyde derivatives as selective inhibitors of human cathepsin L and their inhibitory effect on bone resorption. J. Med. Chem. 41, 4301-4308 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 4301-4308
    • Yasuma, T.1    Oi, S.2    Choh, N.3
  • 84
    • 23844555503 scopus 로고    scopus 로고
    • The Nipah virus fusion protein is cleaved within the endosomal compartment
    • Diederich S, Moll M, Klenk HD, Maisner A. The Nipah virus fusion protein is cleaved within the endosomal compartment. J. Biol. Chem. 280, 29899-29903 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 29899-29903
    • Diederich, S.1    Moll, M.2    Klenk, H.D.3    Maisner, A.4
  • 85
    • 12844264032 scopus 로고    scopus 로고
    • Ephrin B2 expression in Kaposi sarcoma is induced by human herpesvirus Type 8: Phenotype switch from venous to arterial endothelium
    • Masood R, Xia G, Smith DL et al. Ephrin B2 expression in Kaposi sarcoma is induced by human herpesvirus Type 8: phenotype switch from venous to arterial endothelium. Blood 105, 1310-1318 (2005).
    • (2005) Blood , vol.105 , pp. 1310-1318
    • Masood, R.1    Xia, G.2    Smith, D.L.3
  • 86
    • 2442706421 scopus 로고    scopus 로고
    • Inhibition of tumor growth and angiogenesis by soluble EphB4
    • Martiny-Baron G, Korff T, Schaffner F et al. Inhibition of tumor growth and angiogenesis by soluble EphB4. Neoplasia 6, 248-257 (2004).
    • (2004) Neoplasia , vol.6 , pp. 248-257
    • Martiny-Baron, G.1    Korff, T.2    Schaffner, F.3
  • 88
    • 0000036362 scopus 로고    scopus 로고
    • Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA
    • Crumpacker C. Fields Virology. Knipe DM, Howley PM (Eds). Lippincott Williams & Wilkins, PA, USA, 393-433 (2001).
    • (2001) Fields Virology , pp. 393-433
    • Crumpacker, C.1
  • 89
    • 0015523596 scopus 로고
    • Broad spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide
    • Sidwell RW, Huffman JH, Khare GP et al. Broad spectrum antiviral activity of Virazole: 1-beta-D-ribofuranosyl-1,2,4-triazole-3-carboxamide. Science 177, 705-706 (1972).
    • (1972) Science , vol.177 , pp. 705-706
    • Sidwell, R.W.1    Huffman, J.H.2    Khare, G.P.3
  • 90
    • 0034864547 scopus 로고    scopus 로고
    • Ribavirin-current status of a broad spectrum antiviral agent
    • Snell NJ. Ribavirin-current status of a broad spectrum antiviral agent. Expert Opin. Pharmacother. 2, 1317-1324 (2001).
    • (2001) Expert Opin. Pharmacother. , vol.2 , pp. 1317-1324
    • Snell, N.J.1
  • 91
    • 18344385692 scopus 로고    scopus 로고
    • Treatment of hepatitis C
    • Heathcote J. Main J. Treatment of hepatitis C. J. Viral. Hepat. 12, 223-235 (2005).
    • (2005) J. Viral. Hepat. , vol.12 , pp. 223-235
    • Heathcote, J.1    Main, J.2
  • 92
    • 0034982250 scopus 로고    scopus 로고
    • Treatment of acute Nipah encephalitis with ribavirin
    • Chong HT, Kamarulzaman A, Tan CT et al. Treatment of acute Nipah encephalitis with ribavirin. Ann. Neurol. 49, 810-813 (2001).
    • (2001) Ann. Neurol. , vol.49 , pp. 810-813
    • Chong, H.T.1    Kamarulzaman, A.2    Tan, C.T.3
  • 93
    • 4444333302 scopus 로고    scopus 로고
    • Ribavirin therapy for Nipah virus infection
    • Snell NJ. Ribavirin therapy for Nipah virus infection. J. Virol. 78, 10211 (2004).
    • (2004) J. Virol. , vol.78 , pp. 10211
    • Snell, N.J.1
  • 94
    • 0034767753 scopus 로고    scopus 로고
    • Antiviral actions of interferons
    • Samuel CE. Antiviral actions of interferons. Clin. Microbiol. Rev. 14, 778-809 (2001).
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 778-809
    • Samuel, C.E.1
  • 95
    • 0036715591 scopus 로고    scopus 로고
    • Viruses and interferon: A fight for supremacy
    • Katze MG, He Y, Gale M Jr. Viruses and interferon: a fight for supremacy. Nat. Rev. Immunol. 2, 675-687 (2002).
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 675-687
    • Katze, M.G.1    He, Y.2    Gale Jr., M.3
  • 96
    • 0036920154 scopus 로고    scopus 로고
    • The V proteins of simian virus 5 and other paramyxoviruses inhibit induction of interferon-beta
    • Poole E, He B, Lamb RA, Randall RE, Goodbourn S. The V proteins of simian virus 5 and other paramyxoviruses inhibit induction of interferon-beta. Virology 303, 33-46 (2002).
    • (2002) Virology , vol.303 , pp. 33-46
    • Poole, E.1    He, B.2    Lamb, R.A.3    Randall, R.E.4    Goodbourn, S.5
  • 97
    • 0036924472 scopus 로고    scopus 로고
    • Recovery of paramyxovirus simian virus 5 with a V protein lacking the conserved cysteine-rich domain: The multifunctional V protein blocks both interferon-beta induction and interferon signaling
    • He B, Paterson RG, Stock N et al. Recovery of paramyxovirus simian virus 5 with a V protein lacking the conserved cysteine-rich domain: the multifunctional V protein blocks both interferon-beta induction and interferon signaling. Virology 303, 15-32 (2002).
    • (2002) Virology , vol.303 , pp. 15-32
    • He, B.1    Paterson, R.G.2    Stock, N.3
  • 98
    • 0036847601 scopus 로고    scopus 로고
    • Paramyxovirus strategies for evading the interferon response
    • Gotoh B, Komatsu T, Takeuchi K, Yokoo J. Paramyxovirus strategies for evading the interferon response. Rev. Med. Virol. 12, 337-357 (2002).
    • (2002) Rev. Med. Virol. , vol.12 , pp. 337-357
    • Gotoh, B.1    Komatsu, T.2    Takeuchi, K.3    Yokoo, J.4
  • 99
    • 0032731094 scopus 로고    scopus 로고
    • The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation
    • Didcock L, Young DF, Goodbourn S, Randall RE. The V protein of simian virus 5 inhibits interferon signalling by targeting STAT1 for proteasome-mediated degradation. J. Virol. 73, 9928-9933 (1999).
    • (1999) J. Virol. , vol.73 , pp. 9928-9933
    • Didcock, L.1    Young, D.F.2    Goodbourn, S.3    Randall, R.E.4
  • 100
    • 15244352465 scopus 로고    scopus 로고
    • Mumps virus V protein antagonizes interferon without the complete degradation of STAT1
    • Kubota T, Yokosawa N, Yokota S et al. Mumps virus V protein antagonizes interferon without the complete degradation of STAT1. J. Virol. 79, 4451-4459 (2005).
    • (2005) J. Virol. , vol.79 , pp. 4451-4459
    • Kubota, T.1    Yokosawa, N.2    Yokota, S.3
  • 101
    • 0035837045 scopus 로고    scopus 로고
    • The V protein of human parainfluenza virus 2 antagonizes Type I interferon responses by destabilizing signal transducer and activator of transcription 2
    • Parisien JP, Lau JF, Rodriguez JJ et al. The V protein of human parainfluenza virus 2 antagonizes Type I interferon responses by destabilizing signal transducer and activator of transcription 2. Virology 283, 230-239 (2001).
    • (2001) Virology , vol.283 , pp. 230-239
    • Parisien, J.P.1    Lau, J.F.2    Rodriguez, J.J.3
  • 103
    • 0031931401 scopus 로고    scopus 로고
    • A novel P/V/C gene in a new member of the Paramyxoviridae family, which causes lethal infection in humans, horses, and other animals
    • Wang LF, Michalski WP, Yu M et al. A novel P/V/C gene in a new member of the Paramyxoviridae family, which causes lethal infection in humans, horses, and other animals. J. Virol. 72, 1482-1490 (1998).
    • (1998) J. Virol. , vol.72 , pp. 1482-1490
    • Wang, L.F.1    Michalski, W.P.2    Yu, M.3
  • 104
    • 0034608231 scopus 로고    scopus 로고
    • Molecular characterization of Nipah virus, a newly emergent paramyxovirus
    • Harcourt BH, Tamin A, Ksiazek TG et al. Molecular characterization of Nipah virus, a newly emergent paramyxovirus. Virology 271, 334-349 (2000).
    • (2000) Virology , vol.271 , pp. 334-349
    • Harcourt, B.H.1    Tamin, A.2    Ksiazek, T.G.3
  • 105
    • 3042856034 scopus 로고    scopus 로고
    • Host evasion by emerging paramyxoviruses: Hendra virus and Nipah virus V proteins inhibit interferon signaling
    • Rodriguez JJ, Horvath CM. Host evasion by emerging paramyxoviruses: Hendra virus and Nipah virus V proteins inhibit interferon signaling. Viral Immunol. 17, 210-219 (2004).
    • (2004) Viral Immunol. , vol.17 , pp. 210-219
    • Rodriguez, J.J.1    Horvath, C.M.2
  • 106
    • 2442661542 scopus 로고    scopus 로고
    • Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively
    • Shaw ML, Garcia-Sastre A, Palese P, Basler CF. Nipah virus V and W proteins have a common STAT1-binding domain yet inhibit STAT1 activation from the cytoplasmic and nuclear compartments, respectively. J. Virol. 78, 5633-5641 (2004).
    • (2004) J. Virol. , vol.78 , pp. 5633-5641
    • Shaw, M.L.1    Garcia-Sastre, A.2    Palese, P.3    Basler, C.F.4
  • 107
    • 0037223757 scopus 로고    scopus 로고
    • Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V W, and C proteins
    • Park MS, Shaw ML, Munoz-Jordan J et al. Newcastle disease virus (NDV)-based assay demonstrates interferon-antagonist activity for the NDV V protein and the Nipah virus V W, and C proteins. J Virol. 77, 1501-1511 (2003).
    • (2003) J Virol. , vol.77 , pp. 1501-1511
    • Park, M.S.1    Shaw, M.L.2    Munoz-Jordan, J.3
  • 108
    • 1942496600 scopus 로고    scopus 로고
    • Identification of the nuclear export signal and STAT-binding domains of the Nipah virus V protein reveals mechanisms underlying interferon evasion
    • Rodriguez JJ, Cruz CD, Horvath CM. Identification of the nuclear export signal and STAT-binding domains of the Nipah virus V protein reveals mechanisms underlying interferon evasion. J. Virol. 78, 5358-5367 (2004).
    • (2004) J. Virol. , vol.78 , pp. 5358-5367
    • Rodriguez, J.J.1    Cruz, C.D.2    Horvath, C.M.3
  • 109
    • 18144378011 scopus 로고    scopus 로고
    • Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways
    • Shaw ML, Cardenas WB, Zamarin D, Palese P, Basler CF. Nuclear localization of the Nipah virus W protein allows for inhibition of both virus- and toll-like receptor 3-triggered signaling pathways. J. Virol. 79, 6078-6088 (2005).
    • (2005) J. Virol. , vol.79 , pp. 6078-6088
    • Shaw, M.L.1    Cardenas, W.B.2    Zamarin, D.3    Palese, P.4    Basler, C.F.5
  • 110
    • 0031016297 scopus 로고    scopus 로고
    • Fatal encephalitis due to novel paramyxovirus transmitted from horses
    • O'Sullivan JD, Allworth AM, Paterson DL et al. Fatal encephalitis due to novel paramyxovirus transmitted from horses. Lancet 349, 93-95 (1997).
    • (1997) Lancet , vol.349 , pp. 93-95
    • O'Sullivan, J.D.1    Allworth, A.M.2    Paterson, D.L.3


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