메뉴 건너뛰기




Volumn 55, Issue 2, 2015, Pages 308-316

A virtual screening approach for identifying plants with anti H5N1 neuraminidase activity

Author keywords

[No Author keywords available]

Indexed keywords

CHEMISTRY;

EID: 84923319996     PISSN: 15499596     EISSN: 1549960X     Source Type: Journal    
DOI: 10.1021/ci500405g     Document Type: Article
Times cited : (48)

References (66)
  • 2
    • 61549097552 scopus 로고    scopus 로고
    • Anti-Influenza Drugs: The Development of Sialidase Inhibitors
    • Kräusslich, H. G. Bartenschlager, R. Springer-Verlag: Berlin
    • Itzstein, M. V.; Thomson, R. Anti-Influenza Drugs: The Development of Sialidase Inhibitors. In Antiviral Strategies, Handbook of Experimental 111 Pharmacology; Kräusslich, H. G.; Bartenschlager, R., Eds.; Springer-Verlag: Berlin, 2009; p 189.
    • (2009) Antiviral Strategies, Handbook of Experimental 111 Pharmacology , pp. 189
    • Itzstein, M.V.1    Thomson, R.2
  • 3
    • 0028113435 scopus 로고
    • Influenza Virus Neuraminidase: Structure, Antibodies, and Inhibitors
    • Colman, P. M. Influenza Virus Neuraminidase: Structure, Antibodies, and Inhibitors Protein Sci. 1994, 3, 1687-1696
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 5
    • 33845991182 scopus 로고    scopus 로고
    • Structure and Functions of Influenza Virus Neuraminidase
    • Gong, J. Z.; Xu, W. F.; Zhang, J. Structure and Functions of Influenza Virus Neuraminidase Curr. Med. Chem. 2007, 14, 113-122
    • (2007) Curr. Med. Chem. , vol.14 , pp. 113-122
    • Gong, J.Z.1    Xu, W.F.2    Zhang, J.3
  • 6
    • 0034603350 scopus 로고    scopus 로고
    • Influenza Virus Neuraminidase Inhibitors
    • Gubareva, L. V.; Kaiser, L.; Hayden, F. G. Influenza Virus Neuraminidase Inhibitors Lancet 2000, 355, 827-835
    • (2000) Lancet , vol.355 , pp. 827-835
    • Gubareva, L.V.1    Kaiser, L.2    Hayden, F.G.3
  • 7
    • 0026508847 scopus 로고
    • The 2.2-A Resolution Crystal-Structure of Influenza-B Neuraminidase and Its Complex with Sialic-Acid
    • Burmeister, W. P.; Ruigrok, R. W. H.; Cusack, S. The 2.2-a Resolution Crystal-Structure of Influenza-B Neuraminidase and Its Complex with Sialic-Acid EMBO J. 1992, 11, 49-56
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.H.2    Cusack, S.3
  • 8
    • 36749056771 scopus 로고    scopus 로고
    • The War against Influenza: Discovery and Development of Sialidase Inhibitors
    • von Itzstein, M. The War against Influenza: Discovery and Development of Sialidase Inhibitors Nat. Rev. Drug Discovery 2007, 6, 967-974
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 967-974
    • Von Itzstein, M.1
  • 9
    • 33751517736 scopus 로고    scopus 로고
    • Antiviral Agents Active against Influenza a Viruses
    • De Clercq, E. Antiviral Agents Active against Influenza a Viruses Nat. Rev. Drug Discovery 2006, 5, 1015-1025
    • (2006) Nat. Rev. Drug Discovery , vol.5 , pp. 1015-1025
    • De Clercq, E.1
  • 10
    • 15044355539 scopus 로고    scopus 로고
    • Stocks up on Antiviral Drug to Tackle Flu Outbreak
    • Coombes, R. U. Stocks up on Antiviral Drug to Tackle Flu Outbreak BMJ 2005, 330, 495-495
    • (2005) BMJ , vol.330 , pp. 495-495
    • Coombes, R.U.1
  • 11
    • 52049100400 scopus 로고    scopus 로고
    • Stockpiling Prepandemic Influenza Vaccines: A New Cornerstone of Pandemic Preparedness Plans
    • Jennings, L. C.; Monto, A. S.; Chan, P. K. S.; Szucs, T. D.; Nicholson, K. G. Stockpiling Prepandemic Influenza Vaccines: A New Cornerstone of Pandemic Preparedness Plans Lancet Infect. Dis. 2008, 8, 650-658
    • (2008) Lancet Infect. Dis. , vol.8 , pp. 650-658
    • Jennings, L.C.1    Monto, A.S.2    Chan, P.K.S.3    Szucs, T.D.4    Nicholson, K.G.5
  • 12
    • 84887921509 scopus 로고    scopus 로고
    • Influenza Treatment and Prophylaxis with Neuraminidase Inhibitors: A Review
    • Kamali, A.; Holodniy, M. Influenza Treatment and Prophylaxis with Neuraminidase Inhibitors: A Review Infect. Drug Resist. 2013, 6, 187-198
    • (2013) Infect. Drug Resist. , vol.6 , pp. 187-198
    • Kamali, A.1    Holodniy, M.2
  • 15
    • 61849118968 scopus 로고    scopus 로고
    • Global Transmission of Oseltamivir-Resistant Influenza
    • Moscona, A. Global Transmission of Oseltamivir-Resistant Influenza N. Engl. J. Med. 2009, 360, 953-956
    • (2009) N. Engl. J. Med. , vol.360 , pp. 953-956
    • Moscona, A.1
  • 19
    • 84871339523 scopus 로고    scopus 로고
    • Recent Advances in the Structure-Based Design of Neuraminidase Inhibitors as Anti-Influenza Agents
    • Shan, Y. Y.; Ma, Y.; Wang, M. Y.; Dong, Y. L. Recent Advances in the Structure-Based Design of Neuraminidase Inhibitors as Anti-Influenza Agents Curr. Med. Chem. 2012, 19, 5885-5894
    • (2012) Curr. Med. Chem. , vol.19 , pp. 5885-5894
    • Shan, Y.Y.1    Ma, Y.2    Wang, M.Y.3    Dong, Y.L.4
  • 21
    • 82955193130 scopus 로고    scopus 로고
    • Revision of Qsar, Docking, and Molecular Modeling Studies of Anti-Influenza Virus a (H1N1) Drugs and Targets: Analysis of Hemagglutinins 3d Structure
    • Dave, K.; Gandhi, M.; Panchal, H.; Vaidya, M. Revision of Qsar, Docking, and Molecular Modeling Studies of Anti-Influenza Virus a (H1N1) Drugs and Targets: Analysis of Hemagglutinins 3d Structure Curr. Comput.-Aided Drug Des. 2011, 7, 255-262
    • (2011) Curr. Comput.-Aided Drug Des. , vol.7 , pp. 255-262
    • Dave, K.1    Gandhi, M.2    Panchal, H.3    Vaidya, M.4
  • 22
    • 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. Z.; Ma, C. L.; Wang, J.; Jo, H.; Canturk, B.; Fiorin, G.; Pinto, L. H.; Lamb, R. A.; Klein, M. L.; DeGrado, W. F. 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. 2013, 56, 2804-2812
    • (2013) J. Med. Chem. , vol.56 , pp. 2804-2812
    • Wang, J.Z.1    Ma, C.L.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
  • 23
    • 84873623557 scopus 로고    scopus 로고
    • Free Energy Calculations Reveal the Origin of Binding Preference for Aminoadamantane Blockers of Influenza a/M2tm Pore
    • Gkeka, P.; Eleftheratos, S.; Kolocouris, A.; Cournia, Z. Free Energy Calculations Reveal the Origin of Binding Preference for Aminoadamantane Blockers of Influenza a/M2tm Pore J. Chem. Theory Comput. 2013, 9, 1272-1281
    • (2013) J. Chem. Theory Comput. , vol.9 , pp. 1272-1281
    • Gkeka, P.1    Eleftheratos, S.2    Kolocouris, A.3    Cournia, Z.4
  • 24
    • 52049109838 scopus 로고    scopus 로고
    • Natural Products in Drug Discovery
    • Harvey, A. L. Natural Products in Drug Discovery Drug Discovery Today 2008, 13, 894-901
    • (2008) Drug Discovery Today , vol.13 , pp. 894-901
    • Harvey, A.L.1
  • 25
    • 77953434492 scopus 로고    scopus 로고
    • Natural Product Scaffolds as Leads-to Drugs
    • Newman, D. J.; Cragg, G. M. Natural Product Scaffolds as Leads-to Drugs Future Med. Chem. 2009, 1, 1415-1427
    • (2009) Future Med. Chem. , vol.1 , pp. 1415-1427
    • Newman, D.J.1    Cragg, G.M.2
  • 26
    • 0028842287 scopus 로고
    • Mode of Action of the Anti-Influenza Virus Activity of Plant Flavonoid, 5,7,4′-Trihydroxy-8-Methoxyflavone, from the Roots of Scutellaria Baicalensis
    • Nagai, T.; Moriguchi, R.; Suzuki, Y.; Tomimori, T.; Yamada, H. Mode of Action of the Anti-Influenza Virus Activity of Plant Flavonoid, 5,7,4′-Trihydroxy-8-Methoxyflavone, from the Roots of Scutellaria Baicalensis Antiviral Res. 1995, 26, 11-25
    • (1995) Antiviral Res. , vol.26 , pp. 11-25
    • Nagai, T.1    Moriguchi, R.2    Suzuki, Y.3    Tomimori, T.4    Yamada, H.5
  • 30
    • 66349121399 scopus 로고    scopus 로고
    • Comparative Molecular Docking of Antitrypanosomal Natural Products into Multiple Trypanosoma Brucei Drug Targets
    • Ogungbe, I. V.; Setzer, W. N. Comparative Molecular Docking of Antitrypanosomal Natural Products into Multiple Trypanosoma Brucei Drug Targets Molecules 2009, 14, 1513-1536
    • (2009) Molecules , vol.14 , pp. 1513-1536
    • Ogungbe, I.V.1    Setzer, W.N.2
  • 31
    • 78650753990 scopus 로고    scopus 로고
    • Molecular Docking Study on Anticancer Activity of Plant-Derived Natural Products
    • Phosrithong, N.; Ungwitayatorn, J. Molecular Docking Study on Anticancer Activity of Plant-Derived Natural Products Med. Chem. Res. 2010, 19, 817-835
    • (2010) Med. Chem. Res. , vol.19 , pp. 817-835
    • Phosrithong, N.1    Ungwitayatorn, J.2
  • 32
    • 11144229113 scopus 로고    scopus 로고
    • Virtual Screening of Human 5-Aminoimidazole-4-Carboxamide Ribonucleotide Transformylase against the Nci Diversity Set by Use of Autodock to Identify Novel Nonfolate Inhibitors
    • Li, C.; Xu, L.; Wolan, D. W.; Wilson, I. A.; Olson, A. J. Virtual Screening of Human 5-Aminoimidazole-4-Carboxamide Ribonucleotide Transformylase against the Nci Diversity Set by Use of Autodock to Identify Novel Nonfolate Inhibitors J. Med. Chem. 2004, 47, 6681-6690
    • (2004) J. Med. Chem. , vol.47 , pp. 6681-6690
    • Li, C.1    Xu, L.2    Wolan, D.W.3    Wilson, I.A.4    Olson, A.J.5
  • 34
    • 13244266921 scopus 로고    scopus 로고
    • Lead- and Drug-Like Compounds: The Rule-of-Five Revolution
    • Lipinski, C. A. Lead- and Drug-Like Compounds: The Rule-of-Five Revolution Drug Discovery Today: Technol. 2004, 1, 337-341
    • (2004) Drug Discovery Today: Technol. , vol.1 , pp. 337-341
    • Lipinski, C.A.1
  • 35
    • 33846108633 scopus 로고    scopus 로고
    • Bindingdb: A Web-Accessible Database of Experimentally Determined Protein-Ligand Binding Affinities
    • Liu, T.; Lin, Y.; Wen, X.; Jorissen, R. N.; Gilson, M. K. Bindingdb: A Web-Accessible Database of Experimentally Determined Protein-Ligand Binding Affinities Nucleic Acids Res. 2007, 35, D198-201
    • (2007) Nucleic Acids Res. , vol.35 , pp. 198-201
    • Liu, T.1    Lin, Y.2    Wen, X.3    Jorissen, R.N.4    Gilson, M.K.5
  • 36
    • 0036169718 scopus 로고    scopus 로고
    • The Binding Database: Data Management and Interface Design
    • Chen, X.; Lin, Y.; Liu, M.; Gilson, M. K. The Binding Database: Data Management and Interface Design Bioinformatics 2002, 18, 130-139
    • (2002) Bioinformatics , vol.18 , pp. 130-139
    • Chen, X.1    Lin, Y.2    Liu, M.3    Gilson, M.K.4
  • 37
    • 77955709186 scopus 로고    scopus 로고
    • Towards the Comprehensive, Rapid, and Accurate Prediction of the Favorable Tautomeric States of Drug-Like Molecules in Aqueous Solution
    • Greenwood, J. R.; Calkins, D.; Sullivan, A. P.; Shelley, J. C. Towards the Comprehensive, Rapid, and Accurate Prediction of the Favorable Tautomeric States of Drug-Like Molecules in Aqueous Solution J. Comput.-Aided Mol. Des. 2010, 24, 591-604
    • (2010) J. Comput.-Aided Mol. Des. , vol.24 , pp. 591-604
    • Greenwood, J.R.1    Calkins, D.2    Sullivan, A.P.3    Shelley, J.C.4
  • 39
    • 0029912748 scopus 로고    scopus 로고
    • Development and Testing of the Opls All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
    • Jorgensen, W. L.; Maxwell, D. S.; TiradoRives, J. Development and Testing of the Opls All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids J. Am. Chem. Soc. 1996, 118, 11225-11236
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tiradorives, J.3
  • 40
    • 0035913529 scopus 로고    scopus 로고
    • Evaluation and Reparametrization of the Opls-Aa Force Field for Proteins Via Comparison with Accurate Quantum Chemical Calculations on Peptides
    • Kaminski, G. A.; Friesner, R. A.; Tirado-Rives, J.; Jorgensen, W. L. Evaluation and Reparametrization of the Opls-Aa Force Field for Proteins Via Comparison with Accurate Quantum Chemical Calculations on Peptides J. Phys. Chem. B 2001, 105, 6474-6487
    • (2001) J. Phys. Chem. B , vol.105 , pp. 6474-6487
    • Kaminski, G.A.1    Friesner, R.A.2    Tirado-Rives, J.3    Jorgensen, W.L.4
  • 41
    • 14844293471 scopus 로고    scopus 로고
    • A Component-Based Software Environment for Visualizing Large Macromolecular Assemblies
    • Sanner, M. F. A Component-Based Software Environment for Visualizing Large Macromolecular Assemblies Structure 2005, 13, 447-462
    • (2005) Structure , vol.13 , pp. 447-462
    • Sanner, M.F.1
  • 43
    • 11644261806 scopus 로고    scopus 로고
    • Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function J. Comput. Chem. 1998, 19, 1639-1662
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 45
    • 49149147973 scopus 로고
    • Iterative Partial Equalization of Orbital Electronegativity - A Rapid Access to Atomic Charges
    • Gasteiger, J.; Marsili, M. Iterative Partial Equalization of Orbital Electronegativity - a Rapid Access to Atomic Charges Tetrahedron 1980, 36, 3219-3228
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 47
    • 0018421350 scopus 로고
    • Fluorometric Assay of Neuraminidase with a Sodium (4-Methylumbelliferyl-Alpha-D-N-Acetylneuraminate) Substrate
    • Potier, M.; Mameli, L.; Belisle, M.; Dallaire, L.; Melancon, S. B. Fluorometric Assay of Neuraminidase with a Sodium (4-Methylumbelliferyl-Alpha-D-N-Acetylneuraminate) Substrate Anal. Biochem. 1979, 94, 287-296
    • (1979) Anal. Biochem. , vol.94 , pp. 287-296
    • Potier, M.1    Mameli, L.2    Belisle, M.3    Dallaire, L.4    Melancon, S.B.5
  • 48
    • 33751321865 scopus 로고    scopus 로고
    • A Detergent-Based Assay for the Detection of Promiscuous Inhibitors
    • Feng, B. Y.; Shoichet, B. K. A Detergent-Based Assay for the Detection of Promiscuous Inhibitors Nat. Protoc. 2006, 1, 550-553
    • (2006) Nat. Protoc. , vol.1 , pp. 550-553
    • Feng, B.Y.1    Shoichet, B.K.2
  • 52
    • 84923385595 scopus 로고    scopus 로고
    • Available from
    • Lian, G. E. C.; Rahmani, M. B. Available from http://km.upm.edu.my/kmportalweb/infox/assetDetailAction.action?execute=view&assetId=000001421&actionFlg=alllist.
    • Lian, G.E.C.1    Rahmani, M.B.2
  • 56
    • 1642310340 scopus 로고    scopus 로고
    • Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening
    • Halgren, T. A.; Murphy, R. B.; Friesner, R. A.; Beard, H. S.; Frye, L. L.; Pollard, W. T.; Banks, J. L. Glide: A New Approach for Rapid, Accurate Docking and Scoring. 2. Enrichment Factors in Database Screening J. Med. Chem. 2004, 47, 1750-1759
    • (2004) J. Med. Chem. , vol.47 , pp. 1750-1759
    • Halgren, T.A.1    Murphy, R.B.2    Friesner, R.A.3    Beard, H.S.4    Frye, L.L.5    Pollard, W.T.6    Banks, J.L.7
  • 57
    • 79953277006 scopus 로고    scopus 로고
    • Binana: A Novel Algorithm for Ligand-Binding Characterization
    • Durrant, J. D.; McCammon, J. A. Binana: A Novel Algorithm for Ligand-Binding Characterization J. Mol. Graphics Modell. 2011, 29, 888-893
    • (2011) J. Mol. Graphics Modell. , vol.29 , pp. 888-893
    • Durrant, J.D.1    McCammon, J.A.2
  • 58
    • 33747872588 scopus 로고    scopus 로고
    • Molecular Complexes at a Glance: Automated Generation of Two-Dimensional Complex Diagrams
    • Stierand, K.; Maass, P. C.; Rarey, M. Molecular Complexes at a Glance: Automated Generation of Two-Dimensional Complex Diagrams Bioinformatics 2006, 22, 1710-1716
    • (2006) Bioinformatics , vol.22 , pp. 1710-1716
    • Stierand, K.1    Maass, P.C.2    Rarey, M.3
  • 59
    • 78650203607 scopus 로고    scopus 로고
    • Drawing the Pdb: Protein-Ligand Complexes in Two Dimensions
    • Stierand, K.; Rarey, M. Drawing the Pdb: Protein-Ligand Complexes in Two Dimensions Acs. Med. Chem. Lett. 2010, 1, 540-545
    • (2010) Acs. Med. Chem. Lett. , vol.1 , pp. 540-545
    • Stierand, K.1    Rarey, M.2
  • 62
    • 84875763136 scopus 로고    scopus 로고
    • Induced Opening of Influenza Virus Neuraminidase N2 150-Loop Suggests an Important Role in Inhibitor Binding
    • Wu, Y.; Qin, G. R.; Gao, F.; Liu, Y.; Vavricka, C. J.; Qi, J. X.; Jiang, H. L.; Yu, K. Q.; Gao, G. F. Induced Opening of Influenza Virus Neuraminidase N2 150-Loop Suggests an Important Role in Inhibitor Binding Sci. Rep. 2013, 3, 1551
    • (2013) Sci. Rep. , vol.3 , pp. 1551
    • Wu, Y.1    Qin, G.R.2    Gao, F.3    Liu, Y.4    Vavricka, C.J.5    Qi, J.X.6    Jiang, H.L.7    Yu, K.Q.8    Gao, G.F.9
  • 63
    • 84856221119 scopus 로고    scopus 로고
    • Drug Discovery against H1N1 Virus (Influenza a Virus) Via Computational Virtual Screening Approach
    • Sharma, A.; Tendulkar, A. V.; Wangikar, P. P. Drug Discovery against H1N1 Virus (Influenza a Virus) Via Computational Virtual Screening Approach Med. Chem. Res. 2011, 20, 1445-1449
    • (2011) Med. Chem. Res. , vol.20 , pp. 1445-1449
    • Sharma, A.1    Tendulkar, A.V.2    Wangikar, P.P.3
  • 64
    • 67650732727 scopus 로고    scopus 로고
    • Glucosyl Hesperidin Prevents Influenza a Virus Replication in Vitro by Inhibition of Viral Sialidase
    • Saha, R. K.; Takahashi, T.; Suzuki, T. Glucosyl Hesperidin Prevents Influenza a Virus Replication in Vitro by Inhibition of Viral Sialidase Biol. Pharm. Bull. 2009, 32, 1188-1192
    • (2009) Biol. Pharm. Bull. , vol.32 , pp. 1188-1192
    • Saha, R.K.1    Takahashi, T.2    Suzuki, T.3
  • 65
    • 33646482930 scopus 로고    scopus 로고
    • Anti-Influenza Agents from Plants and Traditional Chinese Medicine
    • Wang, X. Y.; Jia, W.; Zhao, A. H.; Wang, X. R. Anti-Influenza Agents from Plants and Traditional Chinese Medicine Phytother. Res. 2006, 20, 335-341
    • (2006) Phytother. Res. , vol.20 , pp. 335-341
    • Wang, X.Y.1    Jia, W.2    Zhao, A.H.3    Wang, X.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.