메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

A dual drug regimen synergistically blocks human parainfluenza virus infection

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; HN PROTEIN; PROTEIN BINDING; SURAMIN; VIRAL PROTEIN; ZANAMIVIR;

EID: 84963690535     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep24138     Document Type: Article
Times cited : (17)

References (54)
  • 1
    • 22144445629 scopus 로고    scopus 로고
    • Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease
    • Moscona, A. Entry of parainfluenza virus into cells as a target for interrupting childhood respiratory disease. J. Clin. Invest. 115, 1688-1698 (2005).
    • (2005) J. Clin. Invest , vol.115 , pp. 1688-1698
    • Moscona, A.1
  • 2
    • 0035927982 scopus 로고    scopus 로고
    • Respiratory syncytial virus and parainfluenza virus
    • Hall, C. B. Respiratory syncytial virus and parainfluenza virus. N. Engl. J. Med. 344, 1917-1928 (2001).
    • (2001) N. Engl. J. Med , vol.344 , pp. 1917-1928
    • Hall, C.B.1
  • 3
    • 80052620543 scopus 로고    scopus 로고
    • Progress in the development of human parainfluenza virus vaccines
    • Schmidt, A. C. et al. Progress in the development of human parainfluenza virus vaccines. Expert Rev. Respir. Med. 5, 515-526 (2011).
    • (2011) Expert Rev. Respir. Med , vol.5 , pp. 515-526
    • Schmidt, A.C.1
  • 4
    • 79951518027 scopus 로고    scopus 로고
    • Human parainfluenza virus type 3 (HPIV 3) viral community-acquired pneumonia (CAP) mimicking swine influenza (H1N1) during the swine flu pandemic
    • Cunha, B. A., Corbett, M., Mickail, N. Human parainfluenza virus type 3 (HPIV 3) viral community-acquired pneumonia (CAP) mimicking swine influenza (H1N1) during the swine flu pandemic. Heart Lung 40, 76-80 (2011).
    • (2011) Heart Lung , vol.40 , pp. 76-80
    • Cunha, B.A.1    Corbett, M.2    Mickail, N.3
  • 5
    • 57349149486 scopus 로고    scopus 로고
    • Viral infection in adults hospitalized with community-acquired pneumonia: Prevalence, pathogens, and presentation
    • Johnstone, J., Majumdar, S. R., Fox, J. D., Marrie, T. J. Viral infection in adults hospitalized with community-acquired pneumonia: prevalence, pathogens, and presentation. Chest 134, 1141-1148 (2008).
    • (2008) Chest , vol.134 , pp. 1141-1148
    • Johnstone, J.1    Majumdar, S.R.2    Fox, J.D.3    Marrie, T.J.4
  • 6
    • 0031927834 scopus 로고    scopus 로고
    • Molecular epidemiology of two consecutive outbreaks of parainfluenza 3 in a bone marrow transplant unit
    • Zambon, M., Bull, T., Sadler, C. J., Goldman, J. M., Ward, K. N. Molecular epidemiology of two consecutive outbreaks of parainfluenza 3 in a bone marrow transplant unit. J. Clin. Microbiol. 36, 2289-2293 (1998).
    • (1998) J. Clin. Microbiol , vol.36 , pp. 2289-2293
    • Zambon, M.1    Bull, T.2    Sadler, C.J.3    Goldman, J.M.4    Ward, K.N.5
  • 7
    • 0035027288 scopus 로고    scopus 로고
    • Receptor specificities of human respiroviruses
    • Suzuki, T. et al. Receptor specificities of human respiroviruses. J. Virol. 75, 4604-4613 (2001).
    • (2001) J. Virol , vol.75 , pp. 4604-4613
    • Suzuki, T.1
  • 8
    • 11144227707 scopus 로고    scopus 로고
    • Infection of ciliated cells by human parainfluenza virus type 3 in an in vitro model of human airway epithelium
    • Zhang, L. et al. Infection of ciliated cells by human parainfluenza virus type 3 in an in vitro model of human airway epithelium. J. Virol. 79, 1113-1124 (2005).
    • (2005) J. Virol , vol.79 , pp. 1113-1124
    • Zhang, L.1
  • 9
    • 0028884662 scopus 로고
    • Hemagglutinin-neuraminidase of human parainfluenza 3: Role of the neuraminidase in the viral life cycle
    • Huberman, K., Peluso, R. W., Moscona, A. Hemagglutinin-neuraminidase of human parainfluenza 3: role of the neuraminidase in the viral life cycle. Virology 214, 294-300 (1995).
    • (1995) Virology , vol.214 , pp. 294-300
    • Huberman, K.1    Peluso, R.W.2    Moscona, A.3
  • 10
    • 84855272388 scopus 로고    scopus 로고
    • Mechanism of Fusion Triggering by Human Parainfluenza Virus Type III COMMUNICATION between VIRAL GLYCOPROTEINS during ENTRY
    • Porotto, M., Palmer, S. G., Palermo, L. M., Moscona, A. Mechanism of Fusion Triggering by Human Parainfluenza Virus Type III COMMUNICATION BETWEEN VIRAL GLYCOPROTEINS DURING ENTRY. J. Biol. Chem. 287, 778-793 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 778-793
    • Porotto, M.1    Palmer, S.G.2    Palermo, L.M.3    Moscona, A.4
  • 11
    • 67449093027 scopus 로고    scopus 로고
    • Human parainfluenza virus infection of the airway epithelium: Viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity
    • Palermo, L. M. et al. Human parainfluenza virus infection of the airway epithelium: viral hemagglutinin-neuraminidase regulates fusion protein activation and modulates infectivity. J. Virol. 83, 6900-6908 (2009).
    • (2009) J. Virol , vol.83 , pp. 6900-6908
    • Palermo, L.M.1
  • 12
    • 84869204459 scopus 로고    scopus 로고
    • Regulation of paramyxovirus fusion Activation: The Hemagglutinin-Neuraminidase protein stabilizes the fusion protein in a pretriggered state
    • Porotto, M. et al. Regulation of Paramyxovirus Fusion Activation: the Hemagglutinin-Neuraminidase Protein Stabilizes the Fusion Protein in a Pretriggered State. J. Virol. 86, 12838-12848 (2012).
    • (2012) J. Virol , vol.86 , pp. 12838-12848
    • Porotto, M.1
  • 13
    • 13444270795 scopus 로고    scopus 로고
    • Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein
    • Porotto, M., Murrell, M., Greengard, O., Doctor, L., Moscona, A. Influence of the human parainfluenza virus 3 attachment protein's neuraminidase activity on its capacity to activate the fusion protein. J. Virol. 79, 2383-2392 (2005).
    • (2005) J. Virol , vol.79 , pp. 2383-2392
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Doctor, L.4    Moscona, A.5
  • 14
    • 0037333844 scopus 로고    scopus 로고
    • Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: An HN mutation diminishes the rate of F activation and fusion
    • Porotto, M., Murrell, M., Greengard, O., Moscona, A. Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: an HN mutation diminishes the rate of F activation and fusion. J. Virol. 77, 3647-3654 (2003).
    • (2003) J. Virol , vol.77 , pp. 3647-3654
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Moscona, A.4
  • 15
    • 31144439130 scopus 로고    scopus 로고
    • Paramyxovirus receptor-binding molecules: Engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site
    • Porotto, M. et al. Paramyxovirus receptor-binding molecules: engagement of one site on the hemagglutinin-neuraminidase protein modulates activity at the second site. J. Virol. 80, 1204-1213 (2006).
    • (2006) J. Virol , vol.80 , pp. 1204-1213
    • Porotto, M.1
  • 16
    • 33847183880 scopus 로고    scopus 로고
    • Synthesis and evaluation of 4-O-alkylated 2-deoxy-2,3-didehydro-N-acetylneuraminic acid derivatives as inhibitors of human parainfluenza virus type-3 sialidase activity
    • Tindal, D. J. et al. Synthesis and evaluation of 4-O-alkylated 2-deoxy-2,3-didehydro-N-acetylneuraminic acid derivatives as inhibitors of human parainfluenza virus type-3 sialidase activity. Bioorg. Med. Chem. Lett. 17, 1655-1658 (2007).
    • (2007) Bioorg. Med. Chem. Lett , vol.17 , pp. 1655-1658
    • Tindal, D.J.1
  • 17
    • 70349129529 scopus 로고    scopus 로고
    • Effect of hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 on growth and pathogenicity of Sendai/human parainfluenza type 3 chimera virus in mice
    • Watanabe, M. et al. Effect of hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 on growth and pathogenicity of Sendai/human parainfluenza type 3 chimera virus in mice. Antimicrob. Agents Chemother. 53, 3942-3951 (2009).
    • (2009) Antimicrob. Agents Chemother , vol.53 , pp. 3942-3951
    • Watanabe, M.1
  • 18
    • 0019501239 scopus 로고
    • Inhibition of the neuraminidase of paramyxoviruses by halide ions: A possible means of modulating the two activities of the HN protein
    • Merz, D. C., Prehm, P., Scheid, A., Choppin, P. W. Inhibition of the neuraminidase of paramyxoviruses by halide ions: a possible means of modulating the two activities of the HN protein. Virology 112, 296-305 (1981).
    • (1981) Virology , vol.112 , pp. 296-305
    • Merz, D.C.1    Prehm, P.2    Scheid, A.3    Choppin, P.W.4
  • 19
    • 84923378919 scopus 로고    scopus 로고
    • Structure-guided discovery of potent and dual-acting human parainfluenza virus haemagglutinin-neuraminidase inhibitors
    • Guillon, P. et al. Structure-guided discovery of potent and dual-acting human parainfluenza virus haemagglutinin-neuraminidase inhibitors. Nat. Commun. 5, 5268 (2014).
    • (2014) Nat. Commun , vol.5 , pp. 5268
    • Guillon, P.1
  • 20
    • 0030444832 scopus 로고    scopus 로고
    • Sialidases: Structures, biological significance and therapeutic potential
    • Taylor, G. Sialidases: structures, biological significance and therapeutic potential. Curr. Opin. Struct. Biol. 6, 830-837 (1996).
    • (1996) Curr. Opin. Struct. Biol , vol.6 , pp. 830-837
    • Taylor, G.1
  • 21
    • 0034469926 scopus 로고    scopus 로고
    • The Anti-Influenza virus agent 4-GU-DANA (Zanamivir) Inhibits Cell Fusion Mediated by Human parainfluenza virus and influenza virus HA
    • Greengard, O., Poltoratskaia, N., Leikina, E., Zimmerberg, J., Moscona, A. The Anti-Influenza Virus Agent 4-GU-DANA (Zanamivir) Inhibits Cell Fusion Mediated by Human Parainfluenza Virus and Influenza Virus HA. J. Virol. 74, 11108-11114 (2000).
    • (2000) J. Virol , vol.74 , pp. 11108-11114
    • Greengard, O.1    Poltoratskaia, N.2    Leikina, E.3    Zimmerberg, J.4    Moscona, A.5
  • 22
    • 0034909749 scopus 로고    scopus 로고
    • Human parainfluenza virus type 3 HN-receptor interaction: Effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant
    • Porotto, M., Greengard, O., Poltoratskaia, N., Horga, M. A., Moscona, A. Human parainfluenza virus type 3 HN-receptor interaction: effect of 4-guanidino-Neu5Ac2en on a neuraminidase-deficient variant. J. Virol. 75, 7481-7488 (2001).
    • (2001) J. Virol , vol.75 , pp. 7481-7488
    • Porotto, M.1    Greengard, O.2    Poltoratskaia, N.3    Horga, M.A.4    Moscona, A.5
  • 23
    • 72249095002 scopus 로고    scopus 로고
    • Efficacy of the novel parainfluenza virus Hemagglutinin-Neuraminidase Inhibitor BCX 2798 in Mice-Further Evaluation
    • Alymova, I. V. et al. Efficacy of the Novel Parainfluenza Virus Hemagglutinin-Neuraminidase Inhibitor BCX 2798 in Mice-Further Evaluation. Antivir. Ther. 14, 891-898 (2009).
    • (2009) Antivir. Ther , vol.14 , pp. 891-898
    • Alymova, I.V.1
  • 24
    • 2142698613 scopus 로고    scopus 로고
    • Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivo
    • Alymova, I. V. et al. Efficacy of novel hemagglutinin-neuraminidase inhibitors BCX 2798 and BCX 2855 against human parainfluenza viruses in vitro and in vivo. Antimicrob. Agents Chemother. 48, 1495-1502 (2004).
    • (2004) Antimicrob. Agents Chemother , vol.48 , pp. 1495-1502
    • Alymova, I.V.1
  • 25
    • 84868573592 scopus 로고    scopus 로고
    • Exposing the flexibility of human parainfluenza virus hemagglutinin-neuraminidase
    • Winger, M., von Itzstein, M. Exposing the flexibility of human parainfluenza virus hemagglutinin-neuraminidase. J. Am. Chem. Soc. 134, 18447-18452 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 18447-18452
    • Winger, M.1    Von Itzstein, M.2
  • 26
    • 84923333478 scopus 로고    scopus 로고
    • The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed
    • Dirr, L. et al. The catalytic mechanism of human parainfluenza virus type 3 haemagglutinin-neuraminidase revealed. Angew. Chem. Int. Ed. Engl. 54, 2936-2940 (2015).
    • (2015) Angew. Chem. Int. Ed. Engl , vol.54 , pp. 2936-2940
    • Dirr, L.1
  • 27
    • 0032233597 scopus 로고    scopus 로고
    • Control and surveillance of African trypanosomiasis. Report of a WHO Expert Committee
    • Control and surveillance of African trypanosomiasis. Report of a WHO Expert Committee. World Health Organ. Tech. Rep. Ser. 881, I-VI, 1-114 (1998).
    • (1998) World Health Organ. Tech. Rep. Ser , vol.881 , Issue.1-6 , pp. 1-114
  • 28
    • 79952459914 scopus 로고    scopus 로고
    • The human African trypanosomiasis control and surveillance programme of the World Health Organization 2000-2009: The way forward
    • Simarro, P. P., Diarra, A., Ruiz Postigo, J. A., Franco, J. R., Jannin, J. G. The human African trypanosomiasis control and surveillance programme of the World Health Organization 2000-2009: the way forward. Plos Negl. Trop. Dis. 5, e1007 (2011).
    • (2011) Plos Negl. Trop. Dis , vol.5 , pp. e1007
    • Simarro, P.P.1    Diarra, A.2    Ruiz Postigo, J.A.3    Franco, J.R.4    Jannin, J.G.5
  • 29
    • 84965232858 scopus 로고
    • The treatment of kala-azar by 'bayer 205'
    • Yorke, W. THE TREATMENT OF KALA-AZAR BY 'BAYER 205'. Br. Med. J 1, 370 (1923).
    • (1923) Br. Med. J , vol.1 , pp. 370
    • Yorke, W.1
  • 30
    • 0033003760 scopus 로고    scopus 로고
    • Simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • Zhang, Chung & Oldenburg, A. Simple Statistical Parameter for Use in Evaluation and Validation of High Throughput Screening Assays. J. Biomol. Screen 4, 67-73 (1999).
    • (1999) J. Biomol. Screen , vol.4 , pp. 67-73
    • Zhang, C.1    Oldenburg, A.2
  • 31
    • 0021333955 scopus 로고
    • Specificity studies on the oligosaccharide neuraminidase of human fibroblasts
    • Mendla, K., Cantz, M. Specificity studies on the oligosaccharide neuraminidase of human fibroblasts. Biochem. J 218, 625-628 (1984).
    • (1984) Biochem. J , vol.218 , pp. 625-628
    • Mendla, K.1    Cantz, M.2
  • 32
    • 0026180780 scopus 로고
    • Lysosomal and plasma membrane ganglioside GM3 sialidases of cultured human fibroblasts. Differentiation by detergents and inhibitors
    • Schneider-Jakob, H. R., Cantz, M. Lysosomal and plasma membrane ganglioside GM3 sialidases of cultured human fibroblasts. Differentiation by detergents and inhibitors. Biol. Chem. 372, 443-450 (1991).
    • (1991) Biol. Chem , vol.372 , pp. 443-450
    • Schneider-Jakob, H.R.1    Cantz, M.2
  • 33
    • 0036869102 scopus 로고    scopus 로고
    • Substrate specificity and inhibitor studies of a membrane-bound ganglioside sialidase isolated from human brain tissue
    • Oehler, C., Kopitz, J., Cantz, M. Substrate specificity and inhibitor studies of a membrane-bound ganglioside sialidase isolated from human brain tissue. Biol. Chem. 383, 1735-1742 (2002).
    • (2002) Biol. Chem , vol.383 , pp. 1735-1742
    • Oehler, C.1    Kopitz, J.2    Cantz, M.3
  • 34
    • 0021118703 scopus 로고
    • Quantitative analysis of dose-effect relationships: The combined effects of multiple drugs or enzyme inhibitors
    • Chou, T. C., Talalay, P. Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv. Enzyme Regul. 22, 27-55 (1984).
    • (1984) Adv. Enzyme Regul , vol.22 , pp. 27-55
    • Chou, T.C.1    Talalay, P.2
  • 35
    • 0000994406 scopus 로고
    • Analysis of combined drug effects: A new look at a very old problem
    • Chou, T.-C., Talalay, P. Analysis of combined drug effects: a new look at a very old problem. Trends Pharmacol. Sci. 4, 450-454 (1983).
    • (1983) Trends Pharmacol. Sci , vol.4 , pp. 450-454
    • Chou, T.-C.1    Talalay, P.2
  • 36
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • Chou, T.-C. Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol. Rev. 58, 621-681 (2006).
    • (2006) Pharmacol. Rev , vol.58 , pp. 621-681
    • Chou, T.-C.1
  • 37
    • 41949101995 scopus 로고    scopus 로고
    • Avian influenza H5-containing virus-like particles (VLPs): Host-cell receptor specificity by STD NMR spectroscopy
    • Haselhorst, T. et al. Avian influenza H5-containing virus-like particles (VLPs): host-cell receptor specificity by STD NMR spectroscopy. Angew. Chem. Int. Ed. Engl. 47, 1910-1912 (2008).
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 1910-1912
    • Haselhorst, T.1
  • 38
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
    • Lawrence, M. C. et al. Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J. Mol. Biol. 335, 1343-1357 (2004).
    • (2004) J. Mol. Biol , vol.335 , pp. 1343-1357
    • Lawrence, M.C.1
  • 39
    • 84855270854 scopus 로고    scopus 로고
    • Spring-loaded model revisited: Paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein
    • Porotto, M. et al. Spring-loaded model revisited: paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein. J. Virol. 85, 12867-12880 (2011).
    • (2011) J. Virol , vol.85 , pp. 12867-12880
    • Porotto, M.1
  • 40
    • 10044296412 scopus 로고    scopus 로고
    • Inhibition of parainfluenza virus type 3 and newcastle disease virus Hemagglutinin-Neuraminidase receptor binding: Effect of receptor avidity and steric hindrance at the inhibitor binding sites
    • Porotto, M. et al. Inhibition of Parainfluenza Virus Type 3 and Newcastle Disease Virus Hemagglutinin-Neuraminidase Receptor Binding: Effect of Receptor Avidity and Steric Hindrance at the Inhibitor Binding Sites. J. Virol. 78, 13911-13919 (2004).
    • (2004) J. Virol , vol.78 , pp. 13911-13919
    • Porotto, M.1
  • 41
    • 33846463757 scopus 로고    scopus 로고
    • Ligand Screening by Saturation-Transfer Difference (STD) NMR spectroscopy
    • Krishnan, V. V. Ligand Screening by Saturation-Transfer Difference (STD) NMR Spectroscopy. Current Analytical Chemistry 1, 307-320 (2005).
    • (2005) Current Analytical Chemistry , vol.1 , pp. 307-320
    • Krishnan, V.V.1
  • 42
    • 84931264421 scopus 로고    scopus 로고
    • The approved pediatric drug suramin identified as a clinical candidate for the treatment of EV71 infection-suramin inhibits EV71 infection in vitro and in vivo
    • Ren, P. et al. The approved pediatric drug suramin identified as a clinical candidate for the treatment of EV71 infection-suramin inhibits EV71 infection in vitro and in vivo. Emerg. Microbes Infect. 3, e62 (2014).
    • (2014) Emerg. Microbes Infect , vol.3 , pp. e62
    • Ren, P.1
  • 43
    • 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, W. Y., Jin, B. 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).
    • (1994) Carbohydr. Res , vol.259 , pp. 301-305
    • Von Itzstein, M.1    Wu, W.Y.2    Jin, B.3
  • 44
    • 0024232637 scopus 로고
    • Isolation of a biologically active soluble form of the hemagglutininneuraminidase protein of Sendai virus
    • Thompson, S. D., Laver, W. G., Murti, K. G., Portner, A. Isolation of a biologically active soluble form of the hemagglutininneuraminidase protein of Sendai virus. J. Virol. 62, 4653-4660 (1988).
    • (1988) J. Virol , vol.62 , pp. 4653-4660
    • Thompson, S.D.1    Laver, W.G.2    Murti, K.G.3    Portner, A.4
  • 45
    • 0018421350 scopus 로고
    • Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate
    • Potier, M., Mameli, L., Bélisle, M., Dallaire, L., Melançon, S. B. Fluorometric assay of neuraminidase with a sodium (4-methylumbelliferyl-alpha-D-N-acetylneuraminate) substrate. Anal. Biochem. 94, 287-296 (1979).
    • (1979) Anal. Biochem , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Bélisle, M.3    Dallaire, L.4    Melançon, S.B.5
  • 46
    • 0035704654 scopus 로고    scopus 로고
    • Inhibition of human parainfluenza virus type 1 sialidase by analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid
    • Suzuki, T. et al. Inhibition of human parainfluenza virus type 1 sialidase by analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid. Glycoconj. J. 18, 331-337 (2001).
    • (2001) Glycoconj. J , vol.18 , pp. 331-337
    • Suzuki, T.1
  • 47
    • 0027287318 scopus 로고
    • Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-Nacetylneuraminic acid modified at the C-4 position
    • Holzer, C. T. et al. Inhibition of sialidases from viral, bacterial and mammalian sources by analogues of 2-deoxy-2,3-didehydro-Nacetylneuraminic acid modified at the C-4 position. Glycoconj. J. 10, 40-44 (1993).
    • (1993) Glycoconj. J , vol.10 , pp. 40-44
    • Holzer, C.T.1
  • 48
    • 63149126249 scopus 로고    scopus 로고
    • Characteristic of neuraminidase inhibitory xanthones from Cudrania tricuspidata
    • Ryu, Y. B. et al. Characteristic of neuraminidase inhibitory xanthones from Cudrania tricuspidata. Bioorg. Med. Chem. 17, 2744-2750 (2009).
    • (2009) Bioorg. Med. Chem , vol.17 , pp. 2744-2750
    • Ryu, Y.B.1
  • 49
    • 77951203559 scopus 로고    scopus 로고
    • Prenylated pterocarpans as bacterial neuraminidase inhibitors
    • Nguyen, P. H. et al. Prenylated pterocarpans as bacterial neuraminidase inhibitors. Bioorg. Med. Chem. 18, 3335-3344 (2010).
    • (2010) Bioorg. Med. Chem , vol.18 , pp. 3335-3344
    • Nguyen, P.H.1
  • 50
    • 77649103933 scopus 로고    scopus 로고
    • N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site
    • Mishin, V. P. et al. N-linked glycan at residue 523 of human parainfluenza virus type 3 hemagglutinin-neuraminidase masks a second receptor-binding site. J. Virol. 84, 3094-3100 (2010).
    • (2010) J. Virol , vol.84 , pp. 3094-3100
    • Mishin, V.P.1
  • 51
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: An open-source platform for biological-image analysis
    • Schindelin, J. et al. Fiji: an open-source platform for biological-image analysis. Nat. Methods 9, 676-682 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 676-682
    • Schindelin, J.1
  • 52
    • 0017076160 scopus 로고
    • Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands
    • Chou, T. C. Derivation and properties of Michaelis-Menten type and Hill type equations for reference ligands. J. Theor. Biol. 59, 253-276 (1976).
    • (1976) J. Theor. Biol , vol.59 , pp. 253-276
    • Chou, T.C.1
  • 53
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott, O., Olson, A. J. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J. Comput. Chem. 31, 455-461 (2010).
    • (2010) J. Comput. Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 54
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • Schüttelkopf, A. W., van Aalten, D. M. F. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr 60, 1355-1363 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , pp. 1355-1363
    • Schüttelkopf, A.W.1    Van Aalten, D.M.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.