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Volumn 2, Issue 1, 2010, Pages 147-157

Antibody targeting of TSG101 on influenza-infected cells

Author keywords

Infected cells; Influenza; TSG101; Vaccine

Indexed keywords

MATRIX 1 PROTEIN; MATRIX PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 4 8A4; TUMOR SUSCEPTIBILITY GENE 101 PROTEIN; UNCLASSIFIED DRUG;

EID: 79251474083     PISSN: None     EISSN: 11791624     Source Type: Journal    
DOI: 10.2147/VAAT.S13506     Document Type: Article
Times cited : (4)

References (50)
  • 1
    • 0037425564 scopus 로고    scopus 로고
    • Mortality associated with influenza and respiratory syncytial virus in the United States
    • Thompson WW, Shay DK, Weintraub E, et al. Mortality associated with influenza and respiratory syncytial virus in the United States. JAMA. 2003;289(2):179-186.
    • (2003) JAMA , vol.289 , Issue.2 , pp. 179-186
    • Thompson, W.W.1    Shay, D.K.2    Weintraub, E.3
  • 2
    • 34447258584 scopus 로고    scopus 로고
    • John F Enders lecture 2006: Antivirals for influenza
    • Ong AK, Hayden FG. John F Enders lecture 2006: antivirals for influenza. J Infect Dis. 2007;196(2):181-190.
    • (2007) J Infect Dis , vol.196 , Issue.2 , pp. 181-190
    • Ong, A.K.1    Hayden, F.G.2
  • 3
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • Nayak DP, Hui EKW, Barman S. Assembly and budding of influenza virus. Virus Res. 2004;106(2):147-165.
    • (2004) Virus Res , vol.106 , Issue.2 , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.W.2    Barman, S.3
  • 4
    • 26944491901 scopus 로고    scopus 로고
    • Influenza virus assembly and budding at theviral budozone
    • Schmitt AP, Lamb RA. Influenza virus assembly and budding at theviral budozone. Adv Virus Res. 2005;64:383-416.
    • (2005) Adv Virus Res , vol.64 , pp. 383-416
    • Schmitt, A.P.1    Lamb, R.A.2
  • 5
    • 0034468745 scopus 로고    scopus 로고
    • Influenzavirus matrix protein is the major driving force in virus budding
    • Gomez-Puertas P, Albo C, Perez-Pastrana E, Vivo A, Portela A. Influenzavirus matrix protein is the major driving force in virus budding. J Virol. 2000;74(24):11538-11547.
    • (2000) J Virol , vol.74 , Issue.24 , pp. 11538-11547
    • Gomez-Puertas, P.1    Albo, C.2    Perez-Pastrana, E.3    Vivo, A.4    Portela, A.5
  • 6
    • 0034088332 scopus 로고    scopus 로고
    • Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain
    • Accola MA, Strack B, Gottlinger HG. Efficient particle production by minimal gag constructs which retain the carboxy-terminal domain of human immunodeficiency virus type 1 capsid-p2 and a late assembly domain. J Virol. 2000;74(12):5395-5402.
    • (2000) J Virol , vol.74 , Issue.12 , pp. 5395-5402
    • Accola, M.A.1    Strack, B.2    Gottlinger, H.G.3
  • 7
    • 0034972583 scopus 로고    scopus 로고
    • Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins
    • Latham T, Galarza JM. Formation of wild-type and chimeric influenza virus-like particles following simultaneous expression of only four structural proteins. J Virol. 2001;75(13):6154-6165.
    • (2001) J Virol , vol.75 , Issue.13 , pp. 6154-6165
    • Latham, T.1    Galarza, J.M.2
  • 8
    • 0035658023 scopus 로고    scopus 로고
    • HIV-I and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J, Zang T, Bieniasz PD. HIV-I and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat Med. 2001;7(12):1313-1319.
    • (2001) Nat Med , vol.7 , Issue.12 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 9
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus JE, von Schwedler UK, Pornillos OW, et al. Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell. 2001;107(1):55-65.
    • (2001) Cell , vol.107 , Issue.1 , pp. 55-65
    • Garrus, J.E.1    von Schwedler, U.K.2    Pornillos, O.W.3
  • 10
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos O, Alam SL, Davis DR, Sundquist WI. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat Struct Biol. 2002;9(11):812-817.
    • (2002) Nat Struct Biol , vol.9 , Issue.11 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 11
    • 0034940214 scopus 로고    scopus 로고
    • Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag)
    • VerPlank L, Bouamr F, LaGrassa TJ, et al. Tsg101, a homologue of ubiquitin-conjugating (E2) enzymes, binds the L domain in HIV type 1 Pr55(Gag). Proc Natl Acad Sci U S A. 2001;98(14):7724-7729.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.14 , pp. 7724-7729
    • Verplank, L.1    Bouamr, F.2    Lagrassa, T.J.3
  • 12
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano J, Zang T, Bieniasz PD. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat Med. 2001;7(12):1313-1319.
    • (2001) Nat Med , vol.7 , Issue.12 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 13
    • 0029904430 scopus 로고    scopus 로고
    • Tsg101: A novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells
    • Li L, Cohen SN. Tsg101: a novel tumor susceptibility gene isolated by controlled homozygous functional knockout of allelic loci in mammalian cells. Cell. 1996;85(3):319-329.
    • (1996) Cell , vol.85 , Issue.3 , pp. 319-329
    • Li, L.1    Cohen, S.N.2
  • 14
    • 33744985540 scopus 로고    scopus 로고
    • Endosomal and non-endosomal functions of ESCRT proteins
    • Slagsvold T, Pattni K, Malerod L, Stenmark H. Endosomal and non-endosomal functions of ESCRT proteins. Trends Cell Biol. 2006;16(6):317-326.
    • (2006) Trends Cell Biol , vol.16 , Issue.6 , pp. 317-326
    • Slagsvold, T.1    Pattni, K.2    Malerod, L.3    Stenmark, H.4
  • 15
    • 0035667189 scopus 로고    scopus 로고
    • Resistance is futile: Assimilation of cellular machinery by HIV-1
    • Perez OD, Nolan GP. Resistance is futile: assimilation of cellular machinery by HIV-1. Immunity. 2001;15(5):687-690.
    • (2001) Immunity , vol.15 , Issue.5 , pp. 687-690
    • Perez, O.D.1    Nolan, G.P.2
  • 16
    • 33749077805 scopus 로고    scopus 로고
    • The role of viral and cellular proteins in the budding of human immunodeficiency virus
    • Mazze FM, Degreve L. The role of viral and cellular proteins in the budding of human immunodeficiency virus. Acta Virol. 2006;50(2):75-85.
    • (2006) Acta Virol , vol.50 , Issue.2 , pp. 75-85
    • Mazze, F.M.1    Degreve, L.2
  • 17
    • 0036827573 scopus 로고    scopus 로고
    • Tsg101, an inactive homologue of ubiquitin ligase e2, interacts specifically with human immunodeficiency virus type 2 gag polyprotein and results in increased levels of ubiquitinated gag
    • Myers EL, Allen JF. Tsg101, an inactive homologue of ubiquitin ligase e2, interacts specifically with human immunodeficiency virus type 2 gag polyprotein and results in increased levels of ubiquitinated gag. J Virol. 2002;76(22):11226-11235.
    • (2002) J Virol , vol.76 , Issue.22 , pp. 11226-11235
    • Myers, E.L.1    Allen, J.F.2
  • 18
    • 0346734116 scopus 로고    scopus 로고
    • In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding
    • Panchal RG, Ruthel G, Kenny TA, et al. In vivo oligomerization and raft localization of Ebola virus protein VP40 during vesicular budding. Proc Natl Acad Sci U S A. 2003;100(26):15936-15941.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.26 , pp. 15936-15941
    • Panchal, R.G.1    Ruthel, G.2    Kenny, T.A.3
  • 19
    • 0037321831 scopus 로고    scopus 로고
    • The HIV-TSG101 interface: Recent advances in a budding field
    • Freed EO. The HIV-TSG101 interface: recent advances in a budding field. Trends Microbiol. 2003;11(2):56-59.
    • (2003) Trends Microbiol , vol.11 , Issue.2 , pp. 56-59
    • Freed, E.O.1
  • 20
    • 0037688240 scopus 로고    scopus 로고
    • Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression
    • Goila-Gaur R, Demirov DG, Orenstein JM, Ono A, Freed EO. Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression. J Virol. 2003;77(11): 6507-6519.
    • (2003) J Virol , vol.77 , Issue.11 , pp. 6507-6519
    • Goila-Gaur, R.1    Demirov, D.G.2    Orenstein, J.M.3    Ono, A.4    Freed, E.O.5
  • 21
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed EO. Viral late domains. J Virol. 2002;76(10):4679-4687.
    • (2002) J Virol , vol.76 , Issue.10 , pp. 4679-4687
    • Freed, E.O.1
  • 22
    • 39549095341 scopus 로고    scopus 로고
    • Mechanisms for enveloped virus budding: Can some viruses do without an ESCRT?
    • Chen BJ, Lamb RA. Mechanisms for enveloped virus budding: can some viruses do without an ESCRT? Virology. 2008;372(2):221-232.
    • (2008) Virology , vol.372 , Issue.2 , pp. 221-232
    • Chen, B.J.1    Lamb, R.A.2
  • 23
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed EO. Viral late domains. J Virol. 2002;76(10):4679-4687.
    • (2002) J Virol , vol.76 , Issue.10 , pp. 4679-4687
    • Freed, E.O.1
  • 24
    • 0242643727 scopus 로고    scopus 로고
    • Hrs function: Viruses provide the clue
    • Clague MJ, Urbe S. Hrs function: viruses provide the clue. Trends Cell Biol. 2003;13(12):603-606.
    • (2003) Trends Cell Biol , vol.13 , Issue.12 , pp. 603-606
    • Clague, M.J.1    Urbe, S.2
  • 25
    • 0242331710 scopus 로고    scopus 로고
    • A bipartite late-budding domain in human immunodeficiency virus type 1
    • Martin-Serrano J, Bieniasz PD. A bipartite late-budding domain in human immunodeficiency virus type 1. J Virol. 2003;77(22):12373-12377.
    • (2003) J Virol , vol.77 , Issue.22 , pp. 12373-12377
    • Martin-Serrano, J.1    Bieniasz, P.D.2
  • 26
    • 33746317830 scopus 로고    scopus 로고
    • The molecular biology of coronaviruses
    • Masters PS. The molecular biology of coronaviruses. Adv Virus Res.2006;66:193-292.
    • (2006) Adv Virus Res , vol.66 , pp. 193-292
    • Masters, P.S.1
  • 27
    • 26944439528 scopus 로고    scopus 로고
    • Molecular interactions in the assembly of coronaviruses
    • de Haan CAM, Rottier PJM. Molecular interactions in the assembly of coronaviruses. Adv Virus Res. 2005;64:165-230.
    • (2005) Adv Virus Res , vol.64 , pp. 165-230
    • de Haan, C.A.M.1    Rottier, P.J.M.2
  • 28
    • 0242331750 scopus 로고    scopus 로고
    • PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]
    • Bouamr F, Melillo JA, Wang MQ, et al. PPPYVEPTAP motif is the late domain of human T-cell leukemia virus type 1 Gag and mediates its functional interaction with cellular proteins Nedd4 and Tsg101 [corrected]. J Virol. 2003;77(22):11882-11895.
    • (2003) J Virol , vol.77 , Issue.22 , pp. 11882-11895
    • Bouamr, F.1    Melillo, J.A.2    Wang, M.Q.3
  • 29
    • 0141841821 scopus 로고    scopus 로고
    • Association of Japanese encephalitis virus NS3 protein with microtubules and tumour susceptibility gene 101 (TSG101) protein
    • Chiou CT, Hu CC, Chen PH, Liao CL, Lin YL, Wang JJ. Association of Japanese encephalitis virus NS3 protein with microtubules and tumour susceptibility gene 101 (TSG101) protein. J Gen Virol. 2003;84(Pt 10): 2795-2805.
    • (2003) J Gen Virol , vol.84 , Issue.10 , pp. 2795-2805
    • Chiou, C.T.1    Hu, C.C.2    Chen, P.H.3    Liao, C.L.4    Lin, Y.L.5    Wang, J.J.6
  • 30
    • 33847243278 scopus 로고    scopus 로고
    • Role of the TSG101 gene in Epstein- Barr virus late gene transcription
    • Chua HH, Lee HH, Chang SS, et al. Role of the TSG101 gene in Epstein- Barr virus late gene transcription. J Virol. 2007;81(5):2459-2471.
    • (2007) J Virol , vol.81 , Issue.5 , pp. 2459-2471
    • Chua, H.H.1    Lee, H.H.2    Chang, S.S.3
  • 31
    • 0042389562 scopus 로고    scopus 로고
    • The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release
    • Gottwein E, Bodem J, Muller B, Schmechel A, Zentgraf H, Krausslich HG. The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release. J Virol. 2003;77(17):9474-9485.
    • (2003) J Virol , vol.77 , Issue.17 , pp. 9474-9485
    • Gottwein, E.1    Bodem, J.2    Muller, B.3    Schmechel, A.4    Zentgraf, H.5    Krausslich, H.G.6
  • 32
    • 37549055125 scopus 로고    scopus 로고
    • Purification of infectious human herpesvirus 6 A virions and association of host cell proteins
    • Hammarstedt M, Ahlqvist J, Jacobson S, Garoff H, Fogdell-Hahn A. Purification of infectious human herpesvirus 6 A virions and association of host cell proteins. Virol J. 2007;4:101.
    • (2007) Virol J , vol.4 , pp. 101
    • Hammarstedt, M.1    Ahlqvist, J.2    Jacobson, S.3    Garoff, H.4    Fogdell-Hahn, A.5
  • 33
    • 34250842469 scopus 로고    scopus 로고
    • The vaccinia virus F13 L YPPL motif is required for efficient release of extracellular enveloped virus
    • Honeychurch KM, Yang G, Jordan R, Hruby DE. The vaccinia virus F13 L YPPL motif is required for efficient release of extracellular enveloped virus. J Virol. 2007;81(13):7310-7315.
    • (2007) J Virol , vol.81 , Issue.13 , pp. 7310-7315
    • Honeychurch, K.M.1    Yang, G.2    Jordan, R.3    Hruby, D.E.4
  • 34
    • 39749097254 scopus 로고    scopus 로고
    • Molecular characterization of feline immunodeficiency virus budding
    • Luttge BG, Shehu-Xhilaga M, Demirov DG, et al. Molecular characterization of feline immunodeficiency virus budding. J Virol. 2008;82(5):2106-2119.
    • (2008) J Virol , vol.82 , Issue.5 , pp. 2106-2119
    • Luttge, B.G.1    Shehu-Xhilaga, M.2    Demirov, D.G.3
  • 35
    • 44849109935 scopus 로고    scopus 로고
    • Tsg101 can replace Nedd4 function in ASV Gag release but not membrane targeting
    • Medina G, Pincetic A, Ehrlich LS, et al. Tsg101 can replace Nedd4 function in ASV Gag release but not membrane targeting. Virology. 2008;377(1):30-38.
    • (2008) Virology , vol.377 , Issue.1 , pp. 30-38
    • Medina, G.1    Pincetic, A.2    Ehrlich, L.S.3
  • 36
    • 0037770225 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release
    • Tanzi GO, Piefer AJ, Bates P. Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release. J Virol. 2003;77(15):8440-8447.
    • (2003) J Virol , vol.77 , Issue.15 , pp. 8440-8447
    • Tanzi, G.O.1    Piefer, A.J.2    Bates, P.3
  • 37
    • 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, Yasuda J. 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. 2007;81(9):4895-4899.
    • (2007) J Virol , vol.81 , Issue.9 , pp. 4895-4899
    • Urata, S.1    Noda, T.2    Kawaoka, Y.3    Morikawa, S.4    Yokosawa, H.5    Yasuda, J.6
  • 38
    • 33645797370 scopus 로고    scopus 로고
    • Cellular factors required for Lassa virus budding
    • Urata S, Noda T, Kawaoka Y, Yokosawa H, Yasuda J. Cellular factors required for Lassa virus budding. J Virol. 2006;80(8):4191-4195.
    • (2006) J Virol , vol.80 , Issue.8 , pp. 4191-4195
    • Urata, S.1    Noda, T.2    Kawaoka, Y.3    Yokosawa, H.4    Yasuda, J.5
  • 39
    • 77957354608 scopus 로고    scopus 로고
    • TSG101 exposure on the surface of HIV-1 infected cells: Implications for monoclonal antibody therapy for HIV/AIDS
    • Diaz L, Mao H, Zhou Y, et al. TSG101 exposure on the surface of HIV-1 infected cells: implications for monoclonal antibody therapy for HIV/AIDS. Am J Transl Res. 2010;2(4):368-380.
    • (2010) Am J Transl Res , vol.2 , Issue.4 , pp. 368-380
    • Diaz, L.1    Mao, H.2    Zhou, Y.3
  • 40
    • 0038618682 scopus 로고    scopus 로고
    • Basic residues of thehelix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs (Retracted article. See vol. 80, p. 10289, 2006)
    • Hui EKW, Barman S, Yang TY, Nayak DP. Basic residues of thehelix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motifs (Retracted article. See vol. 80, p. 10289, 2006). J Virol. 2003;77(12):7078-7092.
    • (2003) J Virol , vol.77 , Issue.12 , pp. 7078-7092
    • Hui, E.K.W.1    Barman, S.2    Yang, T.Y.3    Nayak, D.P.4
  • 41
    • 33749499847 scopus 로고    scopus 로고
    • YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 (Retraction of vol. 80, p. 2291, 2006)
    • Hui EKW, Barman S, Tang DHP, France B, Nayak DP. YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42 (Retraction of vol. 80, p. 2291, 2006). J Virol. 2006;80(20):10289.
    • (2006) J Virol , vol.80 , Issue.20 , pp. 10289
    • Hui, E.K.W.1    Barman, S.2    Tang, D.H.P.3    France, B.4    Nayak, D.P.5
  • 42
    • 0037135669 scopus 로고    scopus 로고
    • Realities and enigmas of human viral influenza: Pathogenesis, epidemiology and control
    • Hillman MR. Realities and enigmas of human viral influenza: pathogenesis, epidemiology and control. Vaccine. 2002;20(25-26):3068-3087.
    • (2002) Vaccine , vol.20 , Issue.26 , pp. 3068-3087
    • Hillman, M.R.1
  • 43
    • 0032005664 scopus 로고    scopus 로고
    • How to overcome resistance of influenza A viruses against adamantane derivatives
    • Scholtissek C, Quack G, Klenk HD, Webster RG. How to overcome resistance of influenza A viruses against adamantane derivatives. Antiviral Res. 1998;37(2):83-95.
    • (1998) Antiviral Res , vol.37 , Issue.2 , pp. 83-95
    • Scholtissek, C.1    Quack, G.2    Klenk, H.D.3    Webster, R.G.4
  • 44
    • 0034525788 scopus 로고    scopus 로고
    • Influenza chemotherapy: A review of the present state of art and of new drugs in development
    • Luscher-Mattli M. Influenza chemotherapy: a review of the present state of art and of new drugs in development. Arch Virol. 2000;145(11):2233-2248.
    • (2000) Arch Virol , vol.145 , Issue.11 , pp. 2233-2248
    • Luscher-Mattli, M.1
  • 45
    • 0036027825 scopus 로고    scopus 로고
    • Detection of influenza virus resistance to neuraminidase inhibitors by an enzyme inhibition assay
    • Gubareva LV, Webster RG, Hayden FG. Detection of influenza virus resistance to neuraminidase inhibitors by an enzyme inhibition assay. Antiviral Res. 2002;53(1):47-61.
    • (2002) Antiviral Res , vol.53 , Issue.1 , pp. 47-61
    • Gubareva, L.V.1    Webster, R.G.2    Hayden, F.G.3
  • 46
    • 33644499838 scopus 로고    scopus 로고
    • Neuraminidase inhibitor susceptibility network position statement: Antiviral resistance in influenza A/ H5N1 viruses (vol. 10, p. 873, 2005)
    • Hayden F, Klimov A, Tashiro M, et al. Neuraminidase inhibitor susceptibility network position statement: antiviral resistance in influenza A/ H5N1 viruses (vol. 10, p. 873, 2005). Antivir Ther. 2006;11(1):130.
    • (2006) Antivir Ther , vol.11 , Issue.1 , pp. 130
    • Hayden, F.1    Klimov, A.2    Tashiro, M.3
  • 47
    • 34548223154 scopus 로고    scopus 로고
    • Neuraminidase inhibitor resistance in influenza viruses
    • Reece PA. Neuraminidase inhibitor resistance in influenza viruses. J Med Virol. 2007;79(10):1577-1586.
    • (2007) J Med Virol , vol.79 , Issue.10 , pp. 1577-1586
    • Reece, P.A.1
  • 48
    • 40749095573 scopus 로고    scopus 로고
    • Sensitivity of H5N1 influenza viruses to oseltamivir: An update
    • Rameix-Welti MA, van der Werf S, Naffakh N. Sensitivity of H5N1 influenza viruses to oseltamivir: an update. Future Virol. 2008;3(2):157-165.
    • (2008) Future Virol , vol.3 , Issue.2 , pp. 157-165
    • Rameix-Welti, M.A.1    van der Werf, S.2    Naffakh, N.3
  • 49
    • 57049187243 scopus 로고    scopus 로고
    • The potential impact of neuraminidase inhibitor resistant influenza
    • Lackenby A, Thompson CI, Democratis J. The potential impact of neuraminidase inhibitor resistant influenza. Curr Opin Infect Dis. 2008;21(6):626-638.
    • (2008) Curr Opin Infect Dis , vol.21 , Issue.6 , pp. 626-638
    • Lackenby, A.1    Thompson, C.I.2    Democratis, J.3
  • 50
    • 58849121407 scopus 로고    scopus 로고
    • Meeting report: Risk assessment of tamiflu use under pandemic conditions
    • Singer AC, Howard BM, Johnson AC, et al. Meeting report: risk assessment of tamiflu use under pandemic conditions. Environ Health Perspect. 2008;116(11):1563-1567.
    • (2008) Environ Health Perspect , vol.116 , Issue.11 , pp. 1563-1567
    • Singer, A.C.1    Howard, B.M.2    Johnson, A.C.3


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