메뉴 건너뛰기




Volumn 61, Issue 3, 2014, Pages 495-504

Antivirals - current trends in fighting influenza

Author keywords

Antiviral therapy; Antivirals; Influenza virus; Inhibitors; Novel anti influenza drugs

Indexed keywords

ORTHOMYXOVIRIDAE;

EID: 84907687187     PISSN: 0001527X     EISSN: 1734154X     Source Type: Journal    
DOI: 10.18388/abp.2014_1870     Document Type: Review
Times cited : (53)

References (126)
  • 1
    • 38149139549 scopus 로고    scopus 로고
    • Activity of the neuraminidase inhibitor A-315675 against oseltamivir-resistant influenza neuraminidases of N1 and N2 subtypes
    • Abed Y, Nehme B, Baz M, Boivin G (2008) Activity of the neuraminidase inhibitor A-315675 against oseltamivir-resistant influenza neuraminidases of N1 and N2 subtypes. Antiviral Res 77: 163-166.
    • (2008) Antiviral Res , vol.77 , pp. 163-166
    • Abed, Y.1    Nehme, B.2    Baz, M.3    Boivin, G.4
  • 3
    • 84875785705 scopus 로고    scopus 로고
    • Nucleozin targets cytoplasmic trafficking of viral ribonucleoprotein-Rab11 complexes in influenza A virus infection
    • Amorim MJ, Kao RY, Digard P (2013) Nucleozin targets cytoplasmic trafficking of viral ribonucleoprotein-Rab11 complexes in influenza A virus infection. J Virol 87: 4694-4703.
    • (2013) J Virol , vol.87 , pp. 4694-4703
    • Amorim, M.J.1    Kao, R.Y.2    Digard, P.3
  • 4
    • 84907706953 scopus 로고    scopus 로고
    • Polymerase structure and function
    • Wang Q, Tao YJ, eds, Caister Academic Press, Norfolk, United Kingdom
    • Bartlam M, Lou Z, Liu Y, Rao Z (2010) Polymerase structure and function. In Influenza molecular virology. Wang Q, Tao YJ, eds, pp 137152. Caister Academic Press, Norfolk, United Kingdom
    • (2010) Influenza molecular virology , pp. 137152
    • Bartlam, M.1    Lou, Z.2    Liu, Y.3    Rao, Z.4
  • 6
    • 77953262416 scopus 로고    scopus 로고
    • Permissive secondary mutations enable the evolution of influenza oseltamivir resistance
    • Bloom JD, Gong LI, Baltimore D (2010) Permissive secondary mutations enable the evolution of influenza oseltamivir resistance. Science 328: 1272-1275.
    • (2010) Science , vol.328 , pp. 1272-1275
    • Bloom, J.D.1    Gong, L.I.2    Baltimore, D.3
  • 7
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian DL, Yamasaki RB, Buswell RL, Stearns JF, White JM, Kuntz ID (1993) Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32: 2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1    Yamasaki, R.B.2    Buswell, R.L.3    Stearns, J.F.4    White, J.M.5    Kuntz, I.D.6
  • 8
  • 9
    • 34247260773 scopus 로고    scopus 로고
    • High levels of adamantane resistance among influenza A (H3N2) viruses and interim guidelines for use of antiviral agents - United States, 2005-06 influenza season
    • (Reprinted from MMWR, vol. 55, pg 44-46, 2006)
    • Bright RA, Shay D, Bresee J, Klimov A, Cox N, Ortiz J (2006) High levels of adamantane resistance among influenza A (H3N2) viruses and interim guidelines for use of antiviral agents - United States, 2005-06 influenza season (Reprinted from MMWR, vol. 55, pg 44-46, 2006) J Am Med Ass 295: 881-882.
    • (2006) J Am Med Ass , vol.295 , pp. 881-882
    • Bright, R.A.1    Shay, D.2    Bresee, J.3    Klimov, A.4    Cox, N.5    Ortiz, J.6
  • 10
    • 79951603881 scopus 로고    scopus 로고
    • Antiviral agents for the treatment and chemoprophylaxis of Influenza
    • CDC (2011) Antiviral agents for the treatment and chemoprophylaxis of Influenza. MMWR, Recommendations and Reports 60: 1.
    • (2011) MMWR, Recommendations and Reports , vol.60 , pp. 1
  • 11
    • 84863232815 scopus 로고    scopus 로고
    • Design, synthesis, and in vitro biological evaluation of 1H-1,2,3-triazole-4-carboxamide derivatives as new anti-influenza A agents targeting virus nucleoprotein
    • Cheng H, Wan J, Lin MI, Liu Y, Lu X, Liu J, Xu Y, Chen J, Tu Z, Cheng YS, Ding K (2012) Design, synthesis, and in vitro biological evaluation of 1H-1,2,3-triazole-4-carboxamide derivatives as new anti-influenza A agents targeting virus nucleoprotein. J Med Chem 55: 2144-2153.
    • (2012) J Med Chem , vol.55 , pp. 2144-2153
    • Cheng, H.1    Wan, J.2    Lin, M.I.3    Liu, Y.4    Lu, X.5    Liu, J.6    Xu, Y.7    Chen, J.8    Tu, Z.9    Cheng, Y.S.10    Ding, K.11
  • 16
    • 77952576118 scopus 로고    scopus 로고
    • Pharmacokinetics of oseltamivir: an oral antiviral for the treatment and prophylaxis of influenza in diverse populations
    • Davies BE (2010) Pharmacokinetics of oseltamivir: an oral antiviral for the treatment and prophylaxis of influenza in diverse populations. J Antimicrob Chemother 65: ii5-ii10.
    • (2010) J Antimicrob Chemother , vol.65 , pp. 25-210
    • Davies, B.E.1
  • 23
    • 84877355606 scopus 로고    scopus 로고
    • Antiviral agents targeting the influenza virus: a review and publication analysis
    • Eyer L, Hruska K (2013) Antiviral agents targeting the influenza virus: a review and publication analysis. Veterinarni Medicina 58: 113-185.
    • (2013) Veterinarni Medicina , vol.58 , pp. 113-185
    • Eyer, L.1    Hruska, K.2
  • 24
    • 84880367286 scopus 로고    scopus 로고
    • The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication
    • Fodor E (2013) The RNA polymerase of influenza a virus: mechanisms of viral transcription and replication. Acta Virol 57: 113-122.
    • (2013) Acta Virol , vol.57 , pp. 113-122
    • Fodor, E.1
  • 28
    • 2942530436 scopus 로고    scopus 로고
    • Inhibition of influenza virus production in virus-infected mice by RNA interference
    • Ge Q, Filip L, Bai A, Nguyen T, Eisen HN, Chen J (2004) Inhibition of influenza virus production in virus-infected mice by RNA interference. Proc Natl Acad Sci U S A 101: 8676-8681.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8676-8681
    • Ge, Q.1    Filip, L.2    Bai, A.3    Nguyen, T.4    Eisen, H.N.5    Chen, J.6
  • 30
    • 62149122052 scopus 로고    scopus 로고
    • Morbidity and mortality associated with nosocomial transmission of oseltamivir-resistant influenza A(H1N1) virus
    • Gooskens J, Jonges M, Claas EC, Meijer A, van den Broek PJ, Kroes AM (2009) Morbidity and mortality associated with nosocomial transmission of oseltamivir-resistant influenza A(H1N1) virus. J Am Med Ass 301: 1042-1046.
    • (2009) J Am Med Ass , vol.301 , pp. 1042-1046
    • Gooskens, J.1    Jonges, M.2    Claas, E.C.3    Meijer, A.4    van den Broek, P.J.5    Kroes, A.M.6
  • 31
    • 70449258779 scopus 로고
    • On the mechanism underlying initiation of influenza virus infection
    • Gottschalk A (1959) On the mechanism underlying initiation of influenza virus infection. Ergeb Mikrobiol Immunitatsforsch Exp Ther 32: 1-22.
    • (1959) Ergeb Mikrobiol Immunitatsforsch Exp Ther , vol.32 , pp. 1-22
    • Gottschalk, A.1
  • 32
    • 9644262504 scopus 로고    scopus 로고
    • Neuraminidase inhibitor-rimantadine combinations exert additive and synergistic anti-influenza virus effects in MDCK cells
    • Govorkova EA, Fang HB, Tan M, Webster RG (2004) Neuraminidase inhibitor-rimantadine combinations exert additive and synergistic anti-influenza virus effects in MDCK cells. Antimicrob Agents Chemother 48: 4855-4863.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 4855-4863
    • Govorkova, E.A.1    Fang, H.B.2    Tan, M.3    Webster, R.G.4
  • 33
    • 0028930293 scopus 로고
    • Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells
    • Guinea R, Carrasco L (1995) Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells. J Virol 69: 2306-2312.
    • (1995) J Virol , vol.69 , pp. 2306-2312
    • Guinea, R.1    Carrasco, L.2
  • 34
    • 33845399649 scopus 로고    scopus 로고
    • A broad antiviral neutral glycolipid, fattiviracin FV-8, is a membrane fluidity modulator
    • Harada S, Yokomizo K, Monde K, Maeda Y, Yusa K (2007) A broad antiviral neutral glycolipid, fattiviracin FV-8, is a membrane fluidity modulator. Cell Microbiol 9: 196-203.
    • (2007) Cell Microbiol , vol.9 , pp. 196-203
    • Harada, S.1    Yokomizo, K.2    Monde, K.3    Maeda, Y.4    Yusa, K.5
  • 35
    • 33344475829 scopus 로고    scopus 로고
    • Antiviral resistance in influenza viruses - implications for management and pandemic response
    • Hayden FG (2006) Antiviral resistance in influenza viruses - implications for management and pandemic response. N Engl J Med 354: 785-788.
    • (2006) N Engl J Med , vol.354 , pp. 785-788
    • Hayden, F.G.1
  • 38
    • 59149095897 scopus 로고    scopus 로고
    • Inhibitors of V-ATPases: old and new players
    • Huss M, Wieczorek H (2009) Inhibitors of V-ATPases: old and new players. J Exp Biol 212: 341-346.
    • (2009) J Exp Biol , vol.212 , pp. 341-346
    • Huss, M.1    Wieczorek, H.2
  • 39
    • 34249001427 scopus 로고    scopus 로고
    • Amantadine-oseltamivir combination therapy for H5N1 influenza virus infection in mice
    • Ilyushina NA, Hoffmann E, Salomon R, Webster RG, Govorkova EA (2007) Amantadine-oseltamivir combination therapy for H5N1 influenza virus infection in mice. Antivir Ther 12: 363-370.
    • (2007) Antivir Ther , vol.12 , pp. 363-370
    • Ilyushina, N.A.1    Hoffmann, E.2    Salomon, R.3    Webster, R.G.4    Govorkova, E.A.5
  • 42
    • 0036294323 scopus 로고    scopus 로고
    • The H274Y mutation in the influenza A (H1N1) neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo
    • Ives JA, Carr JA, Mendel DB, Tai CY, Lambkin R, Kelly L, Oxford JS, Hayden FG, Roberts NA (2002) The H274Y mutation in the influenza A (H1N1) neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo. Antivir Res 55: 307-317.
    • (2002) Antivir Res , vol.55 , pp. 307-317
    • Ives, J.A.1    Carr, J.A.2    Mendel, D.B.3    Tai, C.Y.4    Lambkin, R.5    Kelly, L.6    Oxford, J.S.7    Hayden, F.G.8    Roberts, N.A.9
  • 43
    • 70249116086 scopus 로고    scopus 로고
    • Neuraminidase inhibitory activities of flavonols isolated from Rhodiola rosea roots and their in vitro anti-influenza viral activities
    • Jeong HJ, Ryu YB, Park SJ, Kim JH, Kwon HJ, Kim JH, Park KH, Rho MC, Lee WS (2009) Neuraminidase inhibitory activities of flavonols isolated from Rhodiola rosea roots and their in vitro anti-influenza viral activities. Bioorg Med Chem 17: 6816-6823.
    • (2009) Bioorg Med Chem , vol.17 , pp. 6816-6823
    • Jeong, H.J.1    Ryu, Y.B.2    Park, S.J.3    Kim, J.H.4    Kwon, H.J.5    Kim, J.H.6    Park, K.H.7    Rho, M.C.8    Lee, W.S.9
  • 50
    • 70350328007 scopus 로고    scopus 로고
    • CS-8958, a prodrug of the novel neuraminidase inhibitor R-125489, demonstrates a favourable long-retention profile in the mouse respiratory tract
    • Koyama K, Takahashi M, Oitate M, Nakai N, Takakusa H, Miura S, Okazaki O (2009) CS-8958, a prodrug of the novel neuraminidase inhibitor R-125489, demonstrates a favourable long-retention profile in the mouse respiratory tract. Antimicrob Agents Chemother 53: 4845-4851.
    • (2009) Antimicrob Agents Chemother , vol.53 , pp. 4845-4851
    • Koyama, K.1    Takahashi, M.2    Oitate, M.3    Nakai, N.4    Takakusa, H.5    Miura, S.6    Okazaki, O.7
  • 52
    • 84870912652 scopus 로고    scopus 로고
    • Polymer-attached zanamivir inhibits synergistically both early and late stages of influenza virus infection
    • Lee CM, Weight AK, Haldar J, Wang L, Klibanov AM, Chen J (2012) Polymer-attached zanamivir inhibits synergistically both early and late stages of influenza virus infection. Proc Natl Acad Sci USA 109: 20385-20390.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 20385-20390
    • Lee, C.M.1    Weight, A.K.2    Haldar, J.3    Wang, L.4    Klibanov, A.M.5    Chen, J.6
  • 53
    • 58249083139 scopus 로고    scopus 로고
    • Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol
    • Leneva IA, Russell RJ, Boriskin YS, Hay AJ (2009) Characteristics of arbidol-resistant mutants of influenza virus: implications for the mechanism of anti-influenza action of arbidol. Antiviral Res 81: 132-140.
    • (2009) Antiviral Res , vol.81 , pp. 132-140
    • Leneva, I.A.1    Russell, R.J.2    Boriskin, Y.S.3    Hay, A.J.4
  • 54
    • 79959520070 scopus 로고    scopus 로고
    • How do aminoadamantanes block the influenza M2 channel, and how does resistance develop?
    • Leonov H, Astrahan P, Krugliak M, Arkin IT (2011) How do aminoadamantanes block the influenza M2 channel, and how does resistance develop? J Am Chem Soc 133: 9903-9911.
    • (2011) J Am Chem Soc , vol.133 , pp. 9903-9911
    • Leonov, H.1    Astrahan, P.2    Krugliak, M.3    Arkin, I.T.4
  • 56
    • 79960587884 scopus 로고    scopus 로고
    • Free energy calculations and binding analysis of two potential anti- influenza drugs with Polymerase basic protein-2 (PB2)
    • Lv HM, Guo XL, Gu RX, Wei DQ (2011) Free energy calculations and binding analysis of two potential anti- influenza drugs with Polymerase basic protein-2 (PB2). Protein Pept Lett 18: 1002-1009.
    • (2011) Protein Pept Lett , vol.18 , pp. 1002-1009
    • Lv, H.M.1    Guo, X.L.2    Gu, R.X.3    Wei, D.Q.4
  • 58
    • 0028932874 scopus 로고
    • In vitro inhibitory effects of combinations of anti-influenza agents
    • Madren LK, Shipman C, Hayden FG (1995) In vitro inhibitory effects of combinations of anti-influenza agents. Antiviral Chem Chemother 6: 109-113.
    • (1995) Antiviral Chem Chemother , vol.6 , pp. 109-113
    • Madren, L.K.1    Shipman, C.2    Hayden, F.G.3
  • 61
    • 60849088256 scopus 로고    scopus 로고
    • Neutralizing anti-influenza virus monoclonal antibodies: therapeutics and tools for discovery
    • Martinez O, Tsibane T, Basler CF (2009) Neutralizing anti-influenza virus monoclonal antibodies: therapeutics and tools for discovery. Int Rev Immunol 28: 69-92.
    • (2009) Int Rev Immunol , vol.28 , pp. 69-92
    • Martinez, O.1    Tsibane, T.2    Basler, C.F.3
  • 62
    • 7644241814 scopus 로고    scopus 로고
    • Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium
    • Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (2004) Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol 78: 12665-12667.
    • (2004) J Virol , vol.78 , pp. 12665-12667
    • Matrosovich, M.N.1    Matrosovich, T.Y.2    Gray, T.3    Roberts, N.A.4    Klenk, H.D.5
  • 64
    • 84873452344 scopus 로고    scopus 로고
    • Mortality and morbidity burden associated with A/H1N1 pdm influenza virus: Who is likely to be infected, experience clinical symptoms, or die from the H1N1 pdm 2009 virus?
    • RRN1013
    • Miller M, Vibound C, Simonsen L, Olson DR, Russell C (2009) Mortality and morbidity burden associated with A/H1N1 pdm influenza virus: Who is likely to be infected, experience clinical symptoms, or die from the H1N1 pdm 2009 virus? PLoSCurr 1, RRN1013.
    • (2009) PLoSCurr , vol.1
    • Miller, M.1    Vibound, C.2    Simonsen, L.3    Olson, D.R.4    Russell, C.5
  • 65
    • 27644439501 scopus 로고    scopus 로고
    • Susceptibilities of antiviral-resistant influenza viruses to novel neuraminidase inhibitors
    • Mishin VP, Hayden FG, Gubareva LV (2005) Susceptibilities of antiviral-resistant influenza viruses to novel neuraminidase inhibitors. Antimicrob Agents Chemother 49: 4515-4520.
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 4515-4520
    • Mishin, V.P.1    Hayden, F.G.2    Gubareva, L.V.3
  • 69
    • 84856078603 scopus 로고    scopus 로고
    • Efficacy of combined therapy with amantadine, oseltamivir, and ribavirin in vivo against susceptible and amantadine-resistant influenza A viruses
    • Nguyen JT, Smee DF, Barnard DL, Julander JG, Gross M, de Jong MD, Went GT (2012) Efficacy of combined therapy with amantadine, oseltamivir, and ribavirin in vivo against susceptible and amantadine-resistant influenza A viruses. PLoS One 7: e31006.
    • (2012) PLoS One , vol.7
    • Nguyen, J.T.1    Smee, D.F.2    Barnard, D.L.3    Julander, J.G.4    Gross, M.5    de Jong, M.D.6    Went, G.T.7
  • 70
    • 84866986941 scopus 로고    scopus 로고
    • Investigating the interaction between influenza and sialic acid: Making and breaking the link
    • von Itzstein M, ed, Springer, Basel
    • Nicholls JM, Lai J, Garcia JM (2012) Investigating the interaction between influenza and sialic acid: Making and breaking the link. In Influenza virus sialidase - a drug discovery target. von Itzstein M, ed, pp 31-47. Springer, Basel.
    • (2012) Influenza virus sialidase - a drug discovery target , pp. 31-47
    • Nicholls, J.M.1    Lai, J.2    Garcia, J.M.3
  • 71
    • 0029115399 scopus 로고
    • Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolar-type proton pump, on the growth of influenza A and B viruses in MDCK cells
    • Ochiai H, Sakai S, Hirabayashi T, Shimizu Y, Terasawa K (1995) Inhibitory effect of bafilomycin A1, a specific inhibitor of vacuolar-type proton pump, on the growth of influenza A and B viruses in MDCK cells. Antiviral Res 27: 425-430.
    • (1995) Antiviral Res , vol.27 , pp. 425-430
    • Ochiai, H.1    Sakai, S.2    Hirabayashi, T.3    Shimizu, Y.4    Terasawa, K.5
  • 72
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno Y, Isegawa Y, Sasao F, Ueda S (1993) A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J Virol 67: 2552-2558.
    • (1993) J Virol , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 73
    • 33745328312 scopus 로고    scopus 로고
    • In vitro inhibition of human influenza A virus replication by chloroquine
    • Ooi EE, Chew JS, Loh JP, Chua RC (2006) In vitro inhibition of human influenza A virus replication by chloroquine. Virol J 3: 39.
    • (2006) Virol J , vol.3 , pp. 39
    • Ooi, E.E.1    Chew, J.S.2    Loh, J.P.3    Chua, R.C.4
  • 76
    • 79851471047 scopus 로고    scopus 로고
    • Generation and characterization of recombinant pandemic influenza A (H1N1) viruses resistant to neuraminidase inhibitors
    • Pizzorno A, Bouhy X, Abed Y, Boivin G (2011) Generation and characterization of recombinant pandemic influenza A (H1N1) viruses resistant to neuraminidase inhibitors. J Infect Dis 203: 25-31.
    • (2011) J Infect Dis , vol.203 , pp. 25-31
    • Pizzorno, A.1    Bouhy, X.2    Abed, Y.3    Boivin, G.4
  • 78
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication
    • Portela A, Digard P (2002). The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. J Gen Virol 83: 723-734.
    • (2002) J Gen Virol , vol.83 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 79
    • 62749124125 scopus 로고    scopus 로고
    • Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection
    • Prabhu N, Prabakaran M, Ho HT, Velumani S, Qiang J, Goutama M, Kwang J (2009) Monoclonal antibodies against the fusion peptide of hemagglutinin protect mice from lethal influenza A virus H5N1 infection. J Virol 83: 2553-2562.
    • (2009) J Virol , vol.83 , pp. 2553-2562
    • Prabhu, N.1    Prabakaran, M.2    Ho, H.T.3    Velumani, S.4    Qiang, J.5    Goutama, M.6    Kwang, J.7
  • 81
    • 84876003028 scopus 로고    scopus 로고
    • Influenza virus resistance to neuraminidase inhibitors
    • Samson M, Pizzorno A, Abed Y, Boivin G (2013) Influenza virus resistance to neuraminidase inhibitors. Antiviral Res 98: 174-185.
    • (2013) Antiviral Res , vol.98 , pp. 174-185
    • Samson, M.1    Pizzorno, A.2    Abed, Y.3    Boivin, G.4
  • 82
    • 0016433781 scopus 로고
    • Susceptibility of different strains of influenza A virus to inhibitory effects of 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA)
    • Schulman JL, Palese P (1975) Susceptibility of different strains of influenza A virus to inhibitory effects of 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA). Virology 63: 98-104.
    • (1975) Virology , vol.63 , pp. 98-104
    • Schulman, J.L.1    Palese, P.2
  • 83
    • 78649549468 scopus 로고    scopus 로고
    • Effect of the antiviral drug Ingaviruin on intracellular transformations and import into the nucleus of influenza A virus nucleocapsid protein
    • Semenova NP, Prokudina EN, Livov DK, Nebol'sin VE (2010) Effect of the antiviral drug Ingaviruin on intracellular transformations and import into the nucleus of influenza A virus nucleocapsid protein. Vopr Virusol 55: 17-20.
    • (2010) Vopr Virusol , vol.55 , pp. 17-20
    • Semenova, N.P.1    Prokudina, E.N.2    Livov, D.K.3    Nebol'sin, V.E.4
  • 85
    • 0036016097 scopus 로고    scopus 로고
    • Peramivir (BCX-1812, RWJ-270201): potential new therapy for influenza
    • Sidwell RW1, Smee DF (2002) Peramivir (BCX-1812, RWJ-270201): potential new therapy for influenza. Expert Opin Investig Drugs 11: 859-869.
    • (2002) Expert Opin Investig Drugs , vol.11 , pp. 859-869
    • Sidwell, R.W.1    Smee, D.F.2
  • 87
    • 0035921095 scopus 로고    scopus 로고
    • Novel 3-(2-adamantyl)pyrrolidines with potent activity against influenza A virus-identification of aminoadamantane derivatives bearing two pharmacophoric amine groups
    • Stamatiou G1, Kolocouris A, Kolocouris N, Fytas G, Foscolos GB, Neyts J, De Clercq E (2001) Novel 3-(2-adamantyl)pyrrolidines with potent activity against influenza A virus-identification of aminoadamantane derivatives bearing two pharmacophoric amine groups. Bioorg Med Chem Lett 11: 2137-2142.
    • (2001) Bioorg Med Chem Lett , vol.11 , pp. 2137-2142
    • Stamatiou, G11    Kolocouris, A.2    Kolocouris, N.3    Fytas, G.4    Foscolos, G.B.5    Neyts, J.6    De Clercq, E.7
  • 88
    • 79952495700 scopus 로고    scopus 로고
    • Influenza A virus haemagglutinin glycoproteins
    • Wang Q, Tao YJ, eds, Caister Academic Press, Norfolk, United Kingdom
    • Steinhauer DA (2010) Influenza A virus haemagglutinin glycoproteins. In Influenza molecular virology. Wang Q, Tao YJ, eds, pp 69-109. Caister Academic Press, Norfolk, United Kingdom
    • (2010) Influenza molecular virology , pp. 69-109
    • Steinhauer, D.A.1
  • 90
    • 0035737252 scopus 로고    scopus 로고
    • Inhibitory effect of modified 5'-capped short RNA fragments on influenza virus RNA polymerase gene expression
    • Tado M, Abe T, Hatta T, Ishikawa M, Nakada S, Yokota T, Takaku H (2001) Inhibitory effect of modified 5'-capped short RNA fragments on influenza virus RNA polymerase gene expression. Antivir Chem Chemother 12: 353-358.
    • (2001) Antivir Chem Chemother , vol.12 , pp. 353-358
    • Tado, M.1    Abe, T.2    Hatta, T.3    Ishikawa, M.4    Nakada, S.5    Yokota, T.6    Takaku, H.7
  • 91
    • 84859053626 scopus 로고    scopus 로고
    • Combinations of favipiravir and peramivir for the treatment of pandemic influenza A/California/04/2009 (H1N1) virus infections in mice
    • Tarbet EB, Maekawa M, Furuta Y, Babu YS, Morrey JD, Smee DF (2012) Combinations of favipiravir and peramivir for the treatment of pandemic influenza A/California/04/2009 (H1N1) virus infections in mice. Antiviral Res 94: 103-110.
    • (2012) Antiviral Res , vol.94 , pp. 103-110
    • Tarbet, E.B.1    Maekawa, M.2    Furuta, Y.3    Babu, Y.S.4    Morrey, J.D.5    Smee, D.F.6
  • 92
    • 84901988238 scopus 로고    scopus 로고
    • In vitro activity of favipiravir and neuraminidase inhibitor combinations against oseltamivir-sensitive and oseltamivir-resistant pandemic influenza A (H1N1) virus
    • Epub ahead of print
    • Tarbet EB, Vollmer AH, Hurst BL, Barnard DL, Furuta Y, Smee DF (2013) In vitro activity of favipiravir and neuraminidase inhibitor combinations against oseltamivir-sensitive and oseltamivir-resistant pandemic influenza A (H1N1) virus. Arch Virol Epub ahead of print.
    • (2013) Arch Virol
    • Tarbet, E.B.1    Vollmer, A.H.2    Hurst, B.L.3    Barnard, D.L.4    Furuta, Y.5    Smee, D.F.6
  • 94
    • 33746210053 scopus 로고    scopus 로고
    • Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates
    • Terabayashi T, Morita M, Ueno M, Nakamura T, Urashima T (2006) Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates. Carbohydr Res 341: 2246-2253.
    • (2006) Carbohydr Res , vol.341 , pp. 2246-2253
    • Terabayashi, T.1    Morita, M.2    Ueno, M.3    Nakamura, T.4    Urashima, T.5
  • 95
    • 84907709689 scopus 로고    scopus 로고
    • The development of carbohydrate-based influenza virus sialidase inhibitors
    • von Itzstein M, ed, Springer, Basel
    • Thomson R, von Itzstein M (2012) The development of carbohydrate-based influenza virus sialidase inhibitors. In Influenza virus sialidase - a drug discovery target. von Itzstein M, ed, pp 31-47. Springer, Basel.
    • (2012) Influenza virus sialidase - a drug discovery target , pp. 31-47
    • Thomson, R.1    von Itzstein, M.2
  • 98
    • 2942620143 scopus 로고    scopus 로고
    • Protection against lethal influenza virus challenge by RNA interference in vivo
    • Tompkins SM, Lo CY, Tumpey TM, Epstein SL (2004) Protection against lethal influenza virus challenge by RNA interference in vivo. Proc Natl Acad Sci U S A 101: 8682-8686.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 8682-8686
    • Tompkins, S.M.1    Lo, C.Y.2    Tumpey, T.M.3    Epstein, S.L.4
  • 100
    • 77950840696 scopus 로고    scopus 로고
    • Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin
    • Vanderlinden E, Goktas F, Cesur Z, Froeyen M, Reed ML, Russell CJ, Cesur N, Naesens L (2010) Novel inhibitors of influenza virus fusion: structure-activity relationship and interaction with the viral hemagglutinin. J Virol 84: 4277-4288.
    • (2010) J Virol , vol.84 , pp. 4277-4288
    • Vanderlinden, E.1    Goktas, F.2    Cesur, Z.3    Froeyen, M.4    Reed, M.L.5    Russell, C.J.6    Cesur, N.7    Naesens, L.8
  • 102
    • 0028454967 scopus 로고
    • The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: a potent influenza virus sialidase inhibitor
    • von Itzstein M, Wu WY, Jin B (1994) The synthesis of 2,3-didehydro-2,4-dideoxy-4-guanidinyl-N-acetylneuraminic acid: a potent influenza virus sialidase inhibitor. Carbohydr Res 259: 301-305.
    • (1994) Carbohydr Res , vol.259 , pp. 301-305
    • von Itzstein, M.1    Wu, W.Y.2    Jin, B.3
  • 103
    • 36749056771 scopus 로고    scopus 로고
    • The war against influenza: discovery and development of sialidase inhibitors
    • von Itzstein M (2007) The war against influenza: discovery and development of sialidase inhibitors. Nat Rev Drug Discov 6: 967-974.
    • (2007) Nat Rev Drug Discov , vol.6 , pp. 967-974
    • von Itzstein, M.1
  • 104
    • 61549097552 scopus 로고    scopus 로고
    • Anti-influenza drugs: the development of sialidase inhibitors
    • von Itzstein M, Thomson R (2009) Anti-influenza drugs: the development of sialidase inhibitors. Handb Exp Pharmacol 189: 111-154.
    • (2009) Handb Exp Pharmacol , vol.189 , pp. 111-154
    • von Itzstein, M.1    Thomson, R.2
  • 108
    • 84876266002 scopus 로고    scopus 로고
    • Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus
    • Wang J, Ma C, Wang J, Jo H, Canturk B, Fiorin G, Pinto LH, Lamb RA, Klein ML, DeGrado WF (2013b) Discovery of novel dual inhibitors of the wild-type and the most prevalent drug-resistant mutant, S31N, of the M2 proton channel from influenza A virus. J Med Chem 56: 2804-2812.
    • (2013) J Med Chem , vol.56 , pp. 2804-2812
    • Wang, J.1    Ma, C.2    Wang, J.3    Jo, H.4    Canturk, B.5    Fiorin, G.6    Pinto, L.H.7    Lamb, R.A.8    Klein, M.L.9    DeGrado, W.F.10
  • 110
    • 82555187501 scopus 로고    scopus 로고
    • Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein
    • Wei G, Meng W, Guo H, Pan W, Liu J, Peng T, Chen L, Chen CY (2011) Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein. PLoS One 6: e28309.
    • (2011) PLoS One , vol.6
    • Wei, G.1    Meng, W.2    Guo, H.3    Pan, W.4    Liu, J.5    Peng, T.6    Chen, L.7    Chen, C.Y.8
  • 111
    • 79251571764 scopus 로고    scopus 로고
    • Attaching zanamivir to a polymer markedly enhances its activity against drug-resistant strains of influenza a virus
    • Weight AK, Haldar J, Alvarez de Cienfuegos L, Gubareva LV, Tumpey TM, Chen J, Klibanov AM (2011) Attaching zanamivir to a polymer markedly enhances its activity against drug-resistant strains of influenza a virus. J Pharm Sci 100: 831-835.
    • (2011) J Pharm Sci , vol.100 , pp. 831-835
    • Weight, A.K.1    Haldar, J.2    de Cienfuegos, A.L.3    Gubareva, L.V.4    Tumpey, T.M.5    Chen, J.6    Klibanov, A.M.7
  • 113
    • 78650622972 scopus 로고    scopus 로고
    • Clinical Aspects of Pandemic (H1N1) 2009 Influenza
    • WHO (2010) Clinical Aspects of Pandemic (H1N1) 2009 Influenza. N Engl J Med 362: 1708-1719.
    • (2010) N Engl J Med , vol.362 , pp. 1708-1719
  • 117
    • 33748645733 scopus 로고    scopus 로고
    • Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses
    • Yen HL, Hoffmann E, Taylor G, Scholtissek C, Monto AS, Webster RG, Govorkova EA (2006) Importance of neuraminidase active-site residues to the neuraminidase inhibitor resistance of influenza viruses. J Virol 80: 8787-8795.
    • (2006) J Virol , vol.80 , pp. 8787-8795
    • Yen, H.L.1    Hoffmann, E.2    Taylor, G.3    Scholtissek, C.4    Monto, A.S.5    Webster, R.G.6    Govorkova, E.A.7
  • 119
    • 63449125762 scopus 로고    scopus 로고
    • Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses
    • Yoshida R, Igarashi M, Ozaki H, Kishida N, Tomabechi D, Kida H, Ito K, Takada A (2009) Cross-protective potential of a novel monoclonal antibody directed against antigenic site B of the hemagglutinin of influenza A viruses. PLoS Pathog 5: e1000350.
    • (2009) PLoS Pathog , vol.5
    • Yoshida, R.1    Igarashi, M.2    Ozaki, H.3    Kishida, N.4    Tomabechi, D.5    Kida, H.6    Ito, K.7    Takada, A.8
  • 120
    • 0033027378 scopus 로고    scopus 로고
    • Identification of a novel HA conformational change inhibitor of human influenza virus
    • Yoshimoto J, Kakui M, Iwasaki H, Fujiwara T, Sugimoto H, Hattori N (1999) Identification of a novel HA conformational change inhibitor of human influenza virus. Arch Virol 144: 865-878.
    • (1999) Arch Virol , vol.144 , pp. 865-878
    • Yoshimoto, J.1    Kakui, M.2    Iwasaki, H.3    Fujiwara, T.4    Sugimoto, H.5    Hattori, N.6
  • 122
    • 78650515603 scopus 로고    scopus 로고
    • Discovery of highly potent agents against influenza A virus
    • Zhao X, Li C, Zeng S, Hu W (2011) Discovery of highly potent agents against influenza A virus. Eur J Med Chem 46: 52-57.
    • (2011) Eur J Med Chem , vol.46 , pp. 52-57
    • Zhao, X.1    Li, C.2    Zeng, S.3    Hu, W.4
  • 124
    • 34548637012 scopus 로고    scopus 로고
    • Effective small interfering RNAs targeting matrix and nucleocapsid protein gene inhibit influenza A virus replication in cells and mice
    • Zhou H, Jin M, Yu Z, Xu X, Peng Y, Wu H, Liu J, Liu H, Cao S, Chen H (2007) Effective small interfering RNAs targeting matrix and nucleocapsid protein gene inhibit influenza A virus replication in cells and mice. Antiviral Res 76: 186-193.
    • (2007) Antiviral Res , vol.76 , pp. 186-193
    • Zhou, H.1    Jin, M.2    Yu, Z.3    Xu, X.4    Peng, Y.5    Wu, H.6    Liu, J.7    Liu, H.8    Cao, S.9    Chen, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.