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Volumn 62, Issue 3, 2010, Pages 204-213

SAR and pharmacophore models for the rhodanine inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase

Author keywords

Drug design; Inhibitors; Pharmacophores; Rhodanines; Structure activity relationships

Indexed keywords

BENZENE DERIVATIVE; ENOYL ACYL CARRIER PROTEIN REDUCTASE (NADH); FURAN; RHODANINE;

EID: 77951112326     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.306     Document Type: Article
Times cited : (22)

References (42)
  • 1
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock, C.O. and Cronan, J.E. (1996) Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta. 1302, 1-16.
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 2
    • 0037411269 scopus 로고    scopus 로고
    • Structural and functional organization of the animal fatty acid synthase
    • Smith, S., Witkowski, A., and Joshi, A.K. (2003) Structural and functional organization of the animal fatty acid synthase. Prog. Lipid Res. 42, 289-317.
    • (2003) Prog. Lipid Res. , vol.42 , pp. 289-317
    • Smith, S.1    Witkowski, A.2    Joshi, A.K.3
  • 3
    • 14744295748 scopus 로고    scopus 로고
    • The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs
    • DOI 10.1517/14728222.9.1.23
    • Wiesner, J. and Seeber, F. (2005) The plastid-derived organelle of protozoan human parasites as a target of established and emerging drugs. Expert Opin Ther. Targets 9, 23-44. (Pubitemid 40331195)
    • (2005) Expert Opinion on Therapeutic Targets , vol.9 , Issue.1 , pp. 23-44
    • Wiesner, J.1    Seeber, F.2
  • 6
    • 70350752494 scopus 로고    scopus 로고
    • Triclosan inhibits the late liver stage of Plasmodium falciparum
    • Singh, A.P., Surolia, N., and Surolia, A. (2009) Triclosan inhibits the late liver stage of Plasmodium falciparum. IUBMB Life 61, 923-928.
    • (2009) IUBMB Life , vol.61 , pp. 923-928
    • Singh, A.P.1    Surolia, N.2    Surolia, A.3
  • 7
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia, N. and Surolia, A. (2001) Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 7, 167-173.
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 8
    • 0028855972 scopus 로고
    • Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli
    • Heath, R.J. and Rock, C.O. (1995) Enoyl-acyl carrier protein reductase (fabI) plays a determinant role in completing cycles of fatty acid elongation in Escherichia coli. J. Biol. Chem. 270, 26538-26542.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26538-26542
    • Heath, R.J.1    Rock, C.O.2
  • 9
    • 12344300344 scopus 로고    scopus 로고
    • The reductase steps of the type II fatty acid synthase as antimicrobial targets
    • Zhang, Y.M., Lu, Y.J., and Rock, C.O. (2004) The reductase steps of the type II fatty acid synthase as antimicrobial targets. Lipids 39, 1055-1060.
    • (2004) Lipids , vol.39 , pp. 1055-1060
    • Zhang, Y.M.1    Lu, Y.J.2    Rock, C.O.3
  • 10
    • 4344702214 scopus 로고    scopus 로고
    • Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan
    • DOI 10.1042/BJ20031821
    • Kapoor, M., Reddy, C.C., Krishnasastry, M.V., Surolia, N., and Surolia, A. (2004) Slow-tight-binding inhibition of enoyl-acyl carrier protein reductase from Plasmodium falciparum by triclosan. Biochem. J. 381, 719-724. (Pubitemid 39120481)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 719-724
    • Kapoor, M.1    Chandramouli Reddy, C.2    Krishnasastry, M.V.3    Surolia, N.4    Surolia, A.5
  • 11
    • 4344567210 scopus 로고    scopus 로고
    • +
    • DOI 10.1042/BJ20040228
    • Kapoor, M., Mukhi, P.L., Surolia, N., Suguna, K., and Surolia, A. (2004) Kinetic and structural analysis of the increased affinity of enoyl-ACP (acyl-carrier protein) reductase for triclosan in the presence of NAD+. Biochem. J. 381, 725-733. (Pubitemid 39120482)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 725-733
    • Kapoor, M.1    Mukhi, P.L.S.2    Surolia, N.3    Suguna, K.4    Surolia, A.5
  • 12
    • 0035861962 scopus 로고    scopus 로고
    • Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors
    • Kapoor, M., Dar, M.J., Surolia, A., and Surolia, N. (2001) Kinetic determinants of the interaction of enoyl-ACP reductase from Plasmodium falciparum with its substrates and inhibitors. Biochem. Biophys. Res. Commun. 289, 832-837.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 832-837
    • Kapoor, M.1    Dar, M.J.2    Surolia, A.3    Surolia, N.4
  • 13
    • 4344584118 scopus 로고    scopus 로고
    • Mutational analysis of the triclosan-binding region of enoyl-ACP (acyl-carrier protein) reductase from Plasmodium falciparum
    • DOI 10.1042/BJ20040302
    • Kapoor, M., Gopalakrishnapai, J., Surolia, N., and Surolia, A. (2004) Mutational analysis of the triclosan-binding region of enoyl-ACP (acylcarrier protein) reductase from Plasmodium falciparum. Biochem. J. 381, 735-741. (Pubitemid 39120483)
    • (2004) Biochemical Journal , vol.381 , Issue.3 , pp. 735-741
    • Kapoor, M.1    Gopalakrishnapai, J.2    Surolia, N.3    Surolia, A.4
  • 14
    • 0034800157 scopus 로고    scopus 로고
    • Structural basis for triclosan and NAD binding to enoyl-ACP reductase of Plasmodium falciparum
    • Suguna, K., Surolia, A., and Surolia, N. (2001) Structural basis for triclosan and NAD binding to enoyl-ACP reductase of Plasmodium falciparum. Biochem. Biophys. Res. Commun. 283, 224-228.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 224-228
    • Suguna, K.1    Surolia, A.2    Surolia, N.3
  • 15
    • 4644355051 scopus 로고    scopus 로고
    • Structural basis for the variation in triclosan affinity to enoyl reductases
    • Pidugu, L.S., Kapoor, M., Surolia, N., Surolia, A., and Suguna, K. (2004) Structural basis for the variation in triclosan affinity to enoyl reductases. J. Mol. Biol. 343, 147-155.
    • (2004) J. Mol. Biol. , vol.343 , pp. 147-155
    • Pidugu, L.S.1    Kapoor, M.2    Surolia, N.3    Surolia, A.4    Suguna, K.5
  • 16
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo, R., Kuo, M., Sidhu, A.S., Valiyaveettil, J.T., Bittman, R., Jacobs, W.R. Jr., Fidock, D.A., and Sacchettini, J.C. (2002) Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J. Biol. Chem. 277, 13106-13114.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13106-13114
    • Perozzo, R.1    Kuo, M.2    Sidhu, A.S.3    Valiyaveettil, J.T.4    Bittman, R.5    Jacobs Jr., W.R.6    Fidock, D.A.7    Sacchettini, J.C.8
  • 17
    • 34447252551 scopus 로고    scopus 로고
    • Mass spectrometric based approach for identification of inhibitors of P. falciparum fatty acid synthase
    • Sharma, S., Sharma, S.K., Modak, R., Karmodia, K., Surolia, A., and Surolia, N. (2007) Mass spectrometric based approach for identification of inhibitors of P. falciparum fatty acid synthase. Antimicrob. Agents Chemother. 51, 2552-2558.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2552-2558
    • Sharma, S.1    Sharma, S.K.2    Modak, R.3    Karmodia, K.4    Surolia, A.5    Surolia, N.6
  • 18
    • 33750036420 scopus 로고    scopus 로고
    • Novel diphenyl ethers: Design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli
    • Chhibber, M., Kumar, G., Parasuraman, P., Ramya, T.N., Surolia, N., and Surolia, A. (2006) Novel diphenyl ethers: design, docking studies, synthesis and inhibition of enoyl ACP reductase of Plasmodium falciparum and Escherichia coli. Bioorg. Med. Chem. 14, 8086-8098.
    • (2006) Bioorg. Med. Chem. , vol.14 , pp. 8086-8098
    • Chhibber, M.1    Kumar, G.2    Parasuraman, P.3    Ramya, T.N.4    Surolia, N.5    Surolia, A.6
  • 22
    • 33847401359 scopus 로고    scopus 로고
    • Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR)
    • DOI 10.1021/jm061154d
    • Sharma, S.K., Parasuraman, P., Kumar, G., Surolia, N., and Surolia, A. (2007) Green tea catechins potentiate triclosan binding to enoyl-ACP reductase from Plasmodium falciparum (PfENR). J. Med. Chem. 50, 765-775. (Pubitemid 46332989)
    • (2007) Journal of Medicinal Chemistry , vol.50 , Issue.4 , pp. 765-775
    • Sharma, S.K.1    Parasuraman, P.2    Kumar, G.3    Surolia, N.4    Surolia, A.5
  • 23
    • 31144454663 scopus 로고    scopus 로고
    • Synthesis and evaluation of substituted pyrazoles: Potential antimalarials targeting the enoyl-ACP reductase of Plasmodium falciparum
    • Kumar, S., Kumar, G., Kapoor, M., Surolia, A., and Surolia, N. (2006) Synthesis and evaluation of substituted pyrazoles: potential antimalarials targeting the enoyl-ACP reductase of Plasmodium falciparum. Synth. Commun. 36, 215-226.
    • (2006) Synth. Commun. , vol.36 , pp. 215-226
    • Kumar, S.1    Kumar, G.2    Kapoor, M.3    Surolia, A.4    Surolia, N.5
  • 24
    • 34250189143 scopus 로고    scopus 로고
    • Discovery of a rhodanine class of compounds as inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase
    • Kumar, G., Parasuraman, P., Sharma, S.K., Banerjee, T., Karmodiya, K., Surolia, N., and Surolia, A. (2007) Discovery of a rhodanine class of compounds as inhibitors of Plasmodium falciparum enoyl-acyl carrier protein reductase. J. Med. Chem. 50, 2665-2675.
    • (2007) J. Med. Chem. , vol.50 , pp. 2665-2675
    • Kumar, G.1    Parasuraman, P.2    Sharma, S.K.3    Banerjee, T.4    Karmodiya, K.5    Surolia, N.6    Surolia, A.7
  • 26
    • 34948887172 scopus 로고    scopus 로고
    • N-benzoylpyrazoles are novel small-molecule inhibitors of human neutrophil elastase
    • Schepetkin, I.A., Khlebnikov, A.I., and Quinn, M.T. (2007) N-benzoylpyrazoles are novel small-molecule inhibitors of human neutrophil elastase. J. Med. Chem. 50, 4928-4938.
    • (2007) J. Med. Chem. , vol.50 , pp. 4928-4938
    • Schepetkin, I.A.1    Khlebnikov, A.I.2    Quinn, M.T.3
  • 28
    • 0035931471 scopus 로고    scopus 로고
    • Arylalkylidene rhodanine with bulky and hydrophobic functional group as selective HCV NS3 protease inhibitor
    • Sing, W.T., Lee, C.L., Yeo, S.L., Lim, S.P., and Sim, M.M. (2001) Arylalkylidene rhodanine with bulky and hydrophobic functional group as selective HCV NS3 protease inhibitor. Bioorg. Med. Chem. Lett. 11, 91-94.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 91-94
    • Sing, W.T.1    Lee, C.L.2    Yeo, S.L.3    Lim, S.P.4    Sim, M.M.5
  • 30
    • 0025769847 scopus 로고
    • Studies on antidiabetic agents. X. Synthesis and biological activities of pioglitazone and related compounds
    • Momose, Y., Meguro, K., Ikeda, H., Hatanaka, C., Oi, S., and Sohda, T. (1991) Studies on antidiabetic agents. X. Synthesis and biological activities of pioglitazone and related compounds. Chem. Pharm. Bull. (Tokyo) 39, 1440-1445.
    • (1991) Chem. Pharm. Bull. (Tokyo) , vol.39 , pp. 1440-1445
    • Momose, Y.1    Meguro, K.2    Ikeda, H.3    Hatanaka, C.4    Oi, S.5    Sohda, T.6
  • 31
    • 49449109858 scopus 로고    scopus 로고
    • Chemical proteomics-based drug design: Target and antitarget fishing with a catechol-rhodanine privileged scaffold for NAD(P)(H) binding proteins
    • Ge, X., Wakim, B., and Sem, D.S. (2008) Chemical proteomics-based drug design: target and antitarget fishing with a catechol-rhodanine privileged scaffold for NAD(P)(H) binding proteins. J. Med. Chem. 51, 4571-4580.
    • (2008) J. Med. Chem. , vol.51 , pp. 4571-4580
    • Ge, X.1    Wakim, B.2    Sem, D.S.3
  • 32
    • 0004313709 scopus 로고    scopus 로고
    • Chemical Computing Group Inc., 1255, University St., Suite 1600, Montreal, Quebec, Canada, H3B 3X3
    • Molecular Operating Environment (MOE 2005.06), Chemical Computing Group Inc., 1255, University St., Suite 1600, Montreal, Quebec, Canada, H3B 3X3.
    • Molecular Operating Environment (MOE 2005.06)
  • 33
    • 0026332547 scopus 로고
    • Electrostatic effects in proteins: Comparison of dielectric and charge models
    • Mehler, E.L. and Solmajer, T. (1991) Electrostatic effects in proteins: comparison of dielectric and charge models. Protein Eng. 4, 903-910.
    • (1991) Protein Eng. , vol.4 , pp. 903-910
    • Mehler, E.L.1    Solmajer, T.2
  • 35
    • 70349972385 scopus 로고    scopus 로고
    • Pharmacophore modeling and virtual screening for the discovery of new transforming growth factor β type I receptor (ALK5) inhibitors
    • Ren, J.X., Li, L.L., Zou, J., Yang, L., Yang, J.L., and Yang, S.Y. (2009) Pharmacophore modeling and virtual screening for the discovery of new transforming growth factor β type I receptor (ALK5) inhibitors. Eur. J. Med. Chem. 44, 4259-4265.
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 4259-4265
    • Ren, J.X.1    Li, L.L.2    Zou, J.3    Yang, L.4    Yang, J.L.5    Yang, S.Y.6
  • 36
    • 67650831948 scopus 로고    scopus 로고
    • Pharmacophore modeling and virtual screening studies of Checkpoint kinase 1 inhibitors
    • Chen, J.J., Liu, T.L., Yang, L.J., Li, L.L., Wei, Y.Q., and Yang, S.Y. (2009) Pharmacophore modeling and virtual screening studies of Checkpoint kinase 1 inhibitors. Chem. Pharm. Bull. 57, 704-709.
    • (2009) Chem. Pharm. Bull. , vol.57 , pp. 704-709
    • Chen, J.J.1    Liu, T.L.2    Yang, L.J.3    Li, L.L.4    Wei, Y.Q.5    Yang, S.Y.6
  • 37
    • 67650330246 scopus 로고    scopus 로고
    • Molecular determinants of Juvenile hormone action as revealed by 3D QSAR analysis in Drossophila
    • Liszekova, D., Palacovicova, M., Beno, M., and Farkas, R. (2009) Molecular determinants of Juvenile hormone action as revealed by 3D QSAR analysis in Drossophila. Plos One 4, 1-15.
    • (2009) Plos One , vol.4 , pp. 1-15
    • Liszekova, D.1    Palacovicova, M.2    Beno, M.3    Farkas, R.4
  • 41
    • 0029705324 scopus 로고    scopus 로고
    • Automated docking of flexible ligands: Applications of AutoDock
    • Goodsell, D.S., Morris, G.M., and Olson, A.J. (1996) Automated docking of flexible ligands: applications of AutoDock. J. Mol. Recognit. 9, 1-5.
    • (1996) J. Mol. Recognit. , vol.9 , pp. 1-5
    • Goodsell, D.S.1    Morris, G.M.2    Olson, A.J.3
  • 42
    • 0030203710 scopus 로고    scopus 로고
    • Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4
    • Morris, G.M., Goodsell, D.S., Huey, R., and Olson, A.J. (1996) Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4. J. Comput. Aided Mol. Des. 10, 293-304.
    • (1996) J. Comput. Aided Mol. Des. , vol.10 , pp. 293-304
    • Morris, G.M.1    Goodsell, D.S.2    Huey, R.3    Olson, A.J.4


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