메뉴 건너뛰기




Volumn 34, Issue 2, 2010, Pages 97-105

Potential drug-like inhibitors of Group 1 influenza neuraminidase identified through computer-aided drug design

Author keywords

Drug design; Flu; H1N1; Influenza; Neuraminidase; Oseltamivir

Indexed keywords

ACTIVE SITE; COMPUTER PROGRAM; COMPUTER-AIDED DRUG DESIGN; DESIGN PROCESS; DRUG DESIGN; DRUG-RESISTANT STRAINS; IMMINENT THREATS; NEURAMINIDASE; OSELTAMIVIR; POTENTIAL DRUG; POTENTIAL INHIBITORS; PROTEIN DYNAMICS;

EID: 77953258396     PISSN: 14769271     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.compbiolchem.2010.03.005     Document Type: Article
Times cited : (23)

References (37)
  • 2
    • 50249114683 scopus 로고    scopus 로고
    • An improved relaxed complex scheme for receptor flexibility in computer-aided drug design
    • Amaro R.E., Baron R., and McCammon J.A. An improved relaxed complex scheme for receptor flexibility in computer-aided drug design. J. Comput.-Aided Mol. Des. 22 (2008) 693-705
    • (2008) J. Comput.-Aided Mol. Des. , vol.22 , pp. 693-705
    • Amaro, R.E.1    Baron, R.2    McCammon, J.A.3
  • 5
    • 0023475950 scopus 로고
    • Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus
    • Baker A.T., Varghese J.N., Laver W.G., Air G.M., and Colman P.M. Three-dimensional structure of neuraminidase of subtype N9 from an avian influenza virus. Proteins 2 (1987) 111-117
    • (1987) Proteins , vol.2 , pp. 111-117
    • Baker, A.T.1    Varghese, J.N.2    Laver, W.G.3    Air, G.M.4    Colman, P.M.5
  • 7
    • 0026813925 scopus 로고
    • The computer program LUDI: a new method for the de novo design of enzyme inhibitors
    • Bohm H.-J. The computer program LUDI: a new method for the de novo design of enzyme inhibitors. J. Comput.-Aided Mol. Des. 6 (1992) 61
    • (1992) J. Comput.-Aided Mol. Des. , vol.6 , pp. 61
    • Bohm, H.-J.1
  • 8
    • 0027658106 scopus 로고
    • A novel computational tool for automated structure-based drug design
    • Bohm H.J. A novel computational tool for automated structure-based drug design. J. Mol. Recogn.: JMR 6 (1993) 131
    • (1993) J. Mol. Recogn.: JMR , vol.6 , pp. 131
    • Bohm, H.J.1
  • 9
    • 0028522983 scopus 로고
    • On the use of LUDI to search the Fine Chemicals Directory for ligands of proteins of known three-dimensional structure
    • Bohm H.J. On the use of LUDI to search the Fine Chemicals Directory for ligands of proteins of known three-dimensional structure. J. Comput.-Aided Mol. Des. 8 (1994) 623-632
    • (1994) J. Comput.-Aided Mol. Des. , vol.8 , pp. 623-632
    • Bohm, H.J.1
  • 11
    • 46849105028 scopus 로고    scopus 로고
    • Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase
    • Cheng L.S., Amaro R.E., Xu D., Li W.W., Arzberger P.W., and McCammon J.A. Ensemble-based virtual screening reveals potential novel antiviral compounds for avian influenza neuraminidase. J. Med. Chem. 51 (2008) 3878-3894
    • (2008) J. Med. Chem. , vol.51 , pp. 3878-3894
    • Cheng, L.S.1    Amaro, R.E.2    Xu, D.3    Li, W.W.4    Arzberger, P.W.5    McCammon, J.A.6
  • 13
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: structure, antibodies, and inhibitors
    • Colman P.M. Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci. 3 (1994) 1687-1696
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 16
    • 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 Discov. 5 (2006) 1015-1025
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 1015-1025
    • De Clercq, E.1
  • 17
    • 34249307213 scopus 로고    scopus 로고
    • Avian influenza A (H5N1) infection: targets and strategies for chemotherapeutic intervention
    • De Clercq E., and Neyts J. Avian influenza A (H5N1) infection: targets and strategies for chemotherapeutic intervention. Trends Pharmacol. Sci. 28 (2007) 280-285
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 280-285
    • De Clercq, E.1    Neyts, J.2
  • 19
    • 58849145223 scopus 로고    scopus 로고
    • AutoGrow: a novel algorithm for protein inhibitor design
    • Durrant J.D., Amaro R.E., and McCammon J.A. AutoGrow: a novel algorithm for protein inhibitor design. Chem. Biol. Drug Des. 73 (2009) 168-178
    • (2009) Chem. Biol. Drug Des. , vol.73 , pp. 168-178
    • Durrant, J.D.1    Amaro, R.E.2    McCammon, J.A.3
  • 20
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases
    • Ewing T.J., Makino S., Skillman A.G., and Kuntz I.D. DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J. Comput.-Aided Mol. Des. 15 (2001) 411
    • (2001) J. Comput.-Aided Mol. Des. , vol.15 , pp. 411
    • Ewing, T.J.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 21
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones G., Willett P., Glen R.C., Leach A.R., and Taylor R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol. 267 (1997) 727
    • (1997) J. Mol. Biol. , vol.267 , pp. 727
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 24
    • 0037157153 scopus 로고    scopus 로고
    • Computational drug design accommodating receptor flexibility: the relaxed complex scheme
    • Lin J.H., Perryman A.L., Schames J.R., and McCammon J.A. Computational drug design accommodating receptor flexibility: the relaxed complex scheme. J. Am. Chem. Soc. 124 (2002) 5632-5633
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5632-5633
    • Lin, J.H.1    Perryman, A.L.2    Schames, J.R.3    McCammon, J.A.4
  • 25
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C.A., Lombardo F., Dominy B.W., and Feeney P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv. Drug Deliv. Rev. 46 (2001) 3-26
    • (2001) Adv. Drug Deliv. Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 26
  • 27
  • 28
    • 29144433925 scopus 로고    scopus 로고
    • Oseltamivir resistance-disabling our influenza defenses
    • Moscona A. Oseltamivir resistance-disabling our influenza defenses. N. Engl. J. Med. 353 (2005) 2633-2636
    • (2005) N. Engl. J. Med. , vol.353 , pp. 2633-2636
    • Moscona, A.1
  • 29
    • 1242285459 scopus 로고    scopus 로고
    • A new millennium conundrum: how to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community
    • Oxford J., Balasingam S., and Lambkin R. A new millennium conundrum: how to use a powerful class of influenza anti-neuraminidase drugs (NAIs) in the community. J. Antimicrob. Chemother. 53 (2004) 133-136
    • (2004) J. Antimicrob. Chemother. , vol.53 , pp. 133-136
    • Oxford, J.1    Balasingam, S.2    Lambkin, R.3
  • 30
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M., Kramer B., Lengauer T., and Klebe G. A fast flexible docking method using an incremental construction algorithm. J. Mol. Biol. 261 (1996) 470
    • (1996) J. Mol. Biol. , vol.261 , pp. 470
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 34
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution
    • Varghese J.N., Laver W.G., and Colman P.M. Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 A resolution. Nature 303 (1983) 35-40
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 36
    • 55249083577 scopus 로고    scopus 로고
    • Structural characterization of the 1918 influenza virus H1N1 neuraminidase
    • Xu X., Zhu X., Dwek R.A., Stevens J., and Wilson I.A. Structural characterization of the 1918 influenza virus H1N1 neuraminidase. J. Virol. 82 (2008) 10493-10501
    • (2008) J. Virol. , vol.82 , pp. 10493-10501
    • Xu, X.1    Zhu, X.2    Dwek, R.A.3    Stevens, J.4    Wilson, I.A.5
  • 37
    • 0027093322 scopus 로고
    • Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability
    • Zhang X.J., Baase W.A., and Matthews B.W. Multiple alanine replacements within alpha-helix 126-134 of T4 lysozyme have independent, additive effects on both structure and stability. Protein Sci. 1 (1992) 761-776
    • (1992) Protein Sci. , vol.1 , pp. 761-776
    • Zhang, X.J.1    Baase, W.A.2    Matthews, B.W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.