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Volumn 8, Issue 5, 2011, Pages 440-451

Homology modeling of α-glucosidase and its interactions with andrograpolide derivatives

Author keywords

glucosidase; Andrographolide; Dock; Homology modeling

Indexed keywords

ALPHA GLUCOSIDASE; ALPHA GLUCOSIDASE INHIBITOR; ANDROGRAPHIS PANICULATA EXTRACT; ANDROGRAPOLIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 79955783954     PISSN: 15701808     EISSN: None     Source Type: Journal    
DOI: 10.2174/157018011795514203     Document Type: Article
Times cited : (2)

References (37)
  • 1
    • 0032992429 scopus 로고    scopus 로고
    • Effects of 14-deoxyandrographolide and 14-deoxy-11,12- didehydroandrographolide on nitric oxide production in cultured human endothelial cells
    • Zhang, C. Y.; Tan, B. K. Effects of 14-deoxyandrographolide and 14-deoxy-11, 12-didehydroandrographolide on nitric oxide production in cultured human endothelial cells. Phytother. Res., 1999, 13(2), 157-159. (Pubitemid 29129452)
    • (1999) Phytotherapy Research , vol.13 , Issue.2 , pp. 157-159
    • Zhang, C.Y.1    Tan, B.K.H.2
  • 2
    • 33645874474 scopus 로고    scopus 로고
    • Intraspecific variation in active principle content and isozymes of Andrographis paniculata (kalmegh): A traditional hepatoprotective medicinal herb of India
    • Sabu, K. K.; Padmesh, P.; Seeni, S. J. Intraspecific variation in active principle content and isozymes of Andrographis paniculata (kalmegh): a traditional hepatoprotective medicinal herb of India. Med. Aromatic. Plant. Sci., 2001, 23(4), 637-647.
    • (2001) Med. Aromatic. Plant. Sci. , vol.23 , Issue.4 , pp. 637-647
    • Sabu, K.K.1    Padmesh, P.2    Seeni, S.J.3
  • 4
    • 0028981092 scopus 로고
    • The alpha-glucosidase i inhibitor castanospermine alters endothelial cell glycosylation, prevents angiogenesis, and inhibits tumor growth
    • Pili, R.; Chang, J.; Partis, R. A.; Mueller, R. A.; Chrest, F. J.; Passaniti, A. The alpha-glucosidase I inhibitor castanospermine alters endothelial cell glycosylation, prevents angiogenesis, and inhibits tumor growth. Cancer Res., 1995, 55(13), 2920-2926.
    • (1995) Cancer Res. , vol.55 , Issue.13 , pp. 2920-2926
    • Pili, R.1    Chang, J.2    Partis, R.A.3    Mueller, R.A.4    Chrest, F.J.5    Passaniti, A.6
  • 5
    • 0022475489 scopus 로고
    • Inhibition of experimental metastasis by castanospermine in mice: Blockage of two distinct stages of tumor colonization by oligosaccharide processing inhibitors
    • Humphries, M. J.; Matsumoto, K.; White, S. L.; Olden, K. Inhibition of experimental metastasis by castanospermine in mice: blockage of two distinct stages of tumor colonization by oligosaccharide processing inhibitors. Cancer Res., 1986, 46(10), 5215-5222. (Pubitemid 16008292)
    • (1986) Cancer Research , vol.46 , Issue.10 , pp. 5215-5222
    • Humphries, M.J.1    Matsumoto, K.2    White, S.L.3    Olden, K.4
  • 6
    • 0036141030 scopus 로고    scopus 로고
    • The α-glucosidase inhibitor 1-deoxynojirimycin blocks human immunodeficiency virus envelope glycoprotein-mediated membrane fusion at the CXCR4 binding step
    • DOI 10.1124/mol.61.1.186
    • Papandreou, M. J.; Barbouche, R.; Guieu, R.; Kieny, M. P.; Fenouillet, E. The alpha-glucosidase inhibitor 1-deoxynojirimycin blocks human immunodeficiency virus envelope glycoproteinmediated membrane fusion at the CXCR4 binding step. Mol. Pharmacol., 2002, 61(1), 186-193. (Pubitemid 34049526)
    • (2002) Molecular Pharmacology , vol.61 , Issue.1 , pp. 186-193
    • Papandreou, M.-J.1    Barbouche, R.2    Guieu, R.3    Kieny, M.P.4    Fenouillet, E.5
  • 7
    • 0036753024 scopus 로고    scopus 로고
    • The combination of interferon α-2b and n-butyl deoxynojirimycin has a greater than additive antiviral effect upon production of infectious bovine viral diarrhea virus (BVDV) in vitro: Implications for hepatitis C virus (HCV) therapy
    • DOI 10.1016/S0166-3542(02)00075-X, PII S016635420200075X
    • Ouzounov, S.; Mehta, A.; Dwek, R. A.; Block, T. M.; Jordan, R. The combination of interferon alpha-2b and n-butyl deoxynojirimycin has a greater than additive antiviral effect upon production of infectious bovine viral diarrhea virus (BVDV) in vitro: implications for hepatitis C virus (HCV) therapy. Antiviral. Res., 2002, 55(3), 425-435. (Pubitemid 35223098)
    • (2002) Antiviral Research , vol.55 , Issue.3 , pp. 425-435
    • Ouzounov, S.1    Mehta, A.2    Dwek, R.A.3    Block, T.M.4    Jordan, R.5
  • 8
    • 0017716475 scopus 로고
    • α-Glucosidase inhibitors. New complex oligosaccharides of microbial origin
    • DOI 10.1007/BF00483561
    • Schmidt, D. D.; Frommer, W.; Junge, B.; Muller, L.; Wingender, W.; Truschei, E.; Schafer, D. Alpha-Glucosidase inhibitors. New complex oligosaccharides of microbial origin. Naturwissenschaften, 1977, 64(10), 535-536. (Pubitemid 8197893)
    • (1977) Naturwissenschaften , vol.64 , Issue.10 , pp. 535-536
    • Schmidt, D.D.1    Frommer, W.2    Junge, B.3
  • 9
    • 0021744391 scopus 로고
    • Valiolamine, a new α-glucosidase inhibiting aminocyclitol. produced by Streptomyces hygroscopicus
    • Kameda, Y.; Asano, N.; Yoshikawa, M.; Takeucki, M.; Yamaguchi, T.; Matsui, K.; Horii, S.; Fukase, H. J. Valiolamine, a new al pha-glucosidase inhibiting aminocyclitol produced by Streptomyces hygroscopicus. Antibiot, 1984, 37(11), 1301-1307. (Pubitemid 15220687)
    • (1984) Journal of Antibiotics , vol.37 , Issue.11 , pp. 1301-1307
    • Kameda, Y.1    Asano, N.2    Yoshikawa, M.3
  • 11
    • 13844262949 scopus 로고    scopus 로고
    • Effect of two α-glucosidase inhibitors, voglibose and acarbose, on postprandial hyperglycemia correlates with subjective abdominal symptoms
    • DOI 10.1016/j.metabol.2004.10.004
    • Fujisawa, T.; Ikegami, H.; Inoue, K.; Kawabata, Y.; Ogihara, T. Effect of two alpha-glucosidase inhibitors, voglibose and acarbose, on postprandial hyperglycemia correlates with subjective abdominal symptoms. Metabolism, 2005, 54(3), 387-390. (Pubitemid 40250100)
    • (2005) Metabolism: Clinical and Experimental , vol.54 , Issue.3 , pp. 387-390
    • Fujisawa, T.1    Ikegami, H.2    Inoue, K.3    Kawabata, Y.4    Ogihara, T.5
  • 13
    • 33645861668 scopus 로고    scopus 로고
    • Studies on the novel alpha-glucosidase inhibitory activity and structureactivity relationships for andrographolide analogues
    • Dai, G. F.; Xu, H. W.; Wang, J. F.; Liu, F. W.; Liu, H. M. Studies on the novel alpha-glucosidase inhibitory activity and structureactivity relationships for andrographolide analogues. Bioorg. Med. Chem., 2006, 16(10), 2710-2713.
    • (2006) Bioorg. Med. Chem. , vol.16 , Issue.10 , pp. 2710-2713
    • Dai, G.F.1    Xu, H.W.2    Wang, J.F.3    Liu, F.W.4    Liu, H.M.5
  • 14
    • 34247636613 scopus 로고    scopus 로고
    • Synthesis of andrographolide derivatives: A new family of alpha-glucosidase inhibitors
    • Xu, H. W.; Dai, G. F.; Liu, G. Z.; Wang. J. F.; Liu, H. M. Synthesis of andrographolide derivatives: A new family of alpha-glucosidase inhibitors. Bioorg. Med. Chem., 2007, 15(12), 4247-4255.
    • (2007) Bioorg. Med. Chem. , vol.15 , Issue.12 , pp. 4247-4255
    • Xu, H.W.1    Dai, G.F.2    Liu, G.Z.3    Wang, J.F.4    Liu, H.M.5
  • 16
    • 0023710771 scopus 로고
    • Effects of graded alpha-glucosidase inhibition on sugar absorption in vivo
    • Madariaga, H.; Lee, P. C.; Heitlinger, L. A.; Lenenthal, M. Effects of graded alpha-glucosidase inhibition on sugar absorption in vivo. Dig. Dis. Sci., 1988, 33(8), 1020-1024.
    • (1988) Dig. Dis. Sci. , vol.33 , Issue.8 , pp. 1020-1024
    • Madariaga, H.1    Lee, P.C.2    Heitlinger, L.A.3    Lenenthal, M.4
  • 17
    • 0035854819 scopus 로고    scopus 로고
    • Genistein, a soy isoflavone, is a potent α-glucosidase inhibitor
    • PII S001457930102631X
    • Lee, D.-S.; Lee, S.-H. Genistein, a soy isoflavone, is a potent alpha- glucosidase inhibitor. FEBS Lett., 2001, 501(1), 84-86. (Pubitemid 33712492)
    • (2001) FEBS Letters , vol.501 , Issue.1-3 , pp. 84-86
    • Lee, D.-S.1    Lee, S.-H.2
  • 18
    • 0020546156 scopus 로고
    • A new approach to the treatment of nocturnal hypoglycemia using alpha-glucosidase inhibition
    • McCulloch, D. K.; Kurtz, A. B.; Tattersall, R. B. A new approach to the treatment of nocturnal hypoglycemia using alpha-glucosidase inhibition. Diabetes Care, 1983, 6(5), 483-487. (Pubitemid 13005558)
    • (1983) Diabetes Care , vol.6 , Issue.5 , pp. 483-487
    • McCulloch, D.K.1    Kurtz, A.B.2    Tattersall, R.B.3
  • 19
    • 0034961298 scopus 로고    scopus 로고
    • α-glucosidase inhibitors with a 4,5,6,7-tetrachlorophthalimide skeleton pendanted with a cycloalkyl or dicarba-closo-dodecaborane group
    • DOI 10.1248/cpb.49.791
    • Sou, S.; Takahashi, H.; Yamasaki, R.; Kagechika, H.; Endo, Y.; Hashimoto, Y. Alpha-glucosidase inhibitors with a 4,5,6,7-tetrachlorophthalimide skeleton pendanted with a cycloalkyl or dicarba-closo-dodecaborane group. Chem. Pharm. Bull., 2001, 49(6), 791-793. (Pubitemid 32587136)
    • (2001) Chemical and Pharmaceutical Bulletin , vol.49 , Issue.6 , pp. 791-793
    • Sou, S.1    Takahashi, H.2    Yamasaki, R.3    Kagechika, H.4    Endo, Y.5    Hashimoto, Y.6
  • 20
    • 33751573419 scopus 로고    scopus 로고
    • α-glucosidase inhibitors: New therapeutic agents for chronic heart failure
    • DOI 10.1291/hypres.29.741
    • Node, K. Alpha-glucosidase inhibitors: new therapeutic agents for chronic heart failure. Hypertens. Res., 2006, 29(10), 741-742. (Pubitemid 44842806)
    • (2006) Hypertension Research , vol.29 , Issue.10 , pp. 741-742
    • Node, K.1
  • 21
    • 0345269288 scopus 로고    scopus 로고
    • Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis
    • DOI 10.1021/jm0209937
    • Brenk, R.; Naerum, L.; Grädler, U.; Gerber, H. D.; Garcia, G. A.; Reuter, K.; Stubbs, M. T.; Klebe, G. Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on new unexpected binding model detected by crystal structure analysis. J. Med. Chem., 2003, 46, 1133-1143. (Pubitemid 36428219)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.7 , pp. 1133-1143
    • Brenk, R.1    Naerum, L.2    Gradler, U.3    Gerber, H.-D.4    Garcia, G.A.5    Reuter, K.6    Stubbs, M.T.7    Klebe, G.8
  • 23
    • 0037103119 scopus 로고    scopus 로고
    • Successful virtual screening for novel inhibitors of human carbonic anhydrase: Strategy and experimental confirmation
    • DOI 10.1021/jm011112j
    • Grünberg, S.; Stubbs, M.; Klebe, G. Successful virtual screening for novel inhibitors of human carbonic anhydrase: strategy and experimental confirmation. J. Med. Chem., 2002, 45, 3588-3602. (Pubitemid 34863232)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.17 , pp. 3588-3602
    • Gruneberg, S.1    Stubbs, M.T.2    Klebe, G.3
  • 24
    • 0037161582 scopus 로고    scopus 로고
    • Rational design and evaluation of new lead compound structures for selective βARK1 inhibitors
    • DOI 10.1021/jm010093a
    • Ilon, M.; Furugori, T.; Mori, T.; Moriyama, S.; Fukuzawa, A.; Shibano, T. Rational design of new lead compounds: structures for selective βARKl inhibitors. J. Med. Chem., 2002, 45, 2150-2159. (Pubitemid 34525795)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.11 , pp. 2150-2159
    • Iino, M.1    Furugori, T.2    Mori, T.3    Moriyama, S.4    Fukuzawa, A.5    Shibano, T.6
  • 25
    • 0036076470 scopus 로고    scopus 로고
    • Structure-based discovery of a novel, noncovalent inhibitor of AmpC β-lactamase
    • DOI 10.1016/S0969-2126(02)00799-2, PII S0969212602007992
    • Power, R. A.; Morandi, F.; Shoichet, B. K. Structure-based discovery of a novel nonvalent inhibitor of AmpC -lactamase. Structure, 2002, 10, 1013-1023. (Pubitemid 34786743)
    • (2002) Structure , vol.10 , Issue.7 , pp. 1013-1023
    • Powers, R.A.1    Morandi, F.2    Shoichet, B.K.3
  • 26
    • 0036191826 scopus 로고    scopus 로고
    • Discovery of new inhibitors of aldose reductase from molecular docking and database screening
    • DOI 10.1016/S0968-0896(01)00410-2, PII S0968089601004102
    • Rastelli, G.; Ferrari, A. M.; Costantino, L.; Gamberini, M. C. Discovery of new inhibitors of aldose reductase from molecular modeling and database searching. Bioorgan. Med. Chem., 2002, 10, 1437-1450. (Pubitemid 34214707)
    • (2002) Bioorganic and Medicinal Chemistry , vol.10 , Issue.5 , pp. 1437-1450
    • Rastelli, G.1    Ferrari, A.M.2    Costantino, L.3    Gamberini, M.C.4
  • 28
    • 34247343346 scopus 로고    scopus 로고
    • Surflex-Dock 2.1: Robust performance from ligand energetic modeling, ring flexibility, and knowledge-based search
    • DOI 10.1007/s10822-007-9114-2
    • Jain, A. N. Surflex-Dock 2.1: Robust performance from ligand energetic modeling, ring flexibility, and knowledge-based search. J. Comput-Aided Mol. Des., 2007, 21(5), 281-306. (Pubitemid 46630055)
    • (2007) Journal of Computer-Aided Molecular Design , vol.21 , Issue.5 , pp. 281-306
    • Jain, A.N.1
  • 29
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • DOI 10.1006/jmbi.2001.4762
    • Shi, J.; Blundell, T. L.; Mizuguchi, K. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J. Mol. Biol., 2001, 310, 243-257. (Pubitemid 32619966)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.1 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 30
    • 0031766401 scopus 로고    scopus 로고
    • HOMSTRAD: A database of protein structure alignments for homologous families
    • Mizuguchi, K.; Deane, C.; Blundell, T.; Overington, J. HOMSTRAD: A database of protein structure alignments for homologous families. Protein Sci., 1998, 7, 2469-2471. (Pubitemid 28506965)
    • (1998) Protein Science , vol.7 , Issue.11 , pp. 2469-2471
    • Mizuguchi, K.1    Deane, C.M.2    Blundell, T.L.3    Overington, J.P.4
  • 32
    • 79955757264 scopus 로고    scopus 로고
    • Dissertation
    • Univ. ZhengZhou, China
    • Shun Xu. Ph.D. Dissertation, Dept. Org. Chem., Univ. ZhengZhou, China. 2006.
    • (2006) Dept. Org. Chem.
    • Xu, S.1
  • 33
    • 77950905123 scopus 로고    scopus 로고
    • QSAR studies on andrographolide derivatives as a-glucosidase inhibitors
    • Jun, X.; Sichao, H.; Haibin, L. QSAR studies on andrographolide derivatives as a-glucosidase inhibitors. Int. J. Mol. Sci., 2010, 11(3), 880-895.
    • (2010) Int. J. Mol. Sci. , vol.11 , Issue.3 , pp. 880-895
    • Jun, X.1    Sichao, H.2    Haibin, L.3
  • 34
    • 75549083531 scopus 로고    scopus 로고
    • Homology modeling, docking, and molecular dynamics reveal HR1039 as a potent inhibitor of 2009 A (H1N1) influenza neuraminidase
    • Wang, Y.T.; Chan, C.H.; Su, Z.Y. Homology modeling, docking, and molecular dynamics reveal HR1039 as a potent inhibitor of 2009 A (H1N1) influenza neuraminidase. Biophys. Chem., 2010, 142(1-2), 74-80.
    • (2010) Biophys. Chem. , vol.142 , Issue.1-2 , pp. 74-80
    • Wang, Y.T.1    Chan, C.H.2    Su, Z.Y.3
  • 35
    • 77954667868 scopus 로고    scopus 로고
    • A computational study on cannabinoid receptors and potent bioactive cannabinoid ligands: Homology modeling docking de novo drug design and molecular dynamics analysis
    • Durdagi, S.; Papadopoulos, M.G.; Zoumpoulakis, P.G. A computational study on cannabinoid receptors and potent bioactive cannabinoid ligands: homology modeling, docking, de novo drug design and molecular dynamics analysis. Mol. Divers., 2010, 14(2), 257-276.
    • (2010) Mol. Divers. , vol.14 , Issue.2 , pp. 257-276
    • Durdagi, S.1    Papadopoulos, M.G.2    Zoumpoulakis, P.G.3
  • 36
    • 79955782874 scopus 로고    scopus 로고
    • http://www.rcsb.org/pdb/explore/explore.do?structureId=1UOK.
  • 37
    • 0031591389 scopus 로고    scopus 로고
    • The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 Å resolution: Structural characterization of proline-substitution sites for protein thermostabilization
    • DOI 10.1006/jmbi.1997.1018
    • Watanabe, K.; Hata, Y.; Kizaki, H. The refined crystal structure of Bacillus cereus oligo-1, 6-glucosidase at 2.0 Ǻ resolution: structural characterization of proline-substitution sites for protein thermostabilization. J. Mol. Biol., 1997, 269(1), 142-153. (Pubitemid 27243627)
    • (1997) Journal of Molecular Biology , vol.269 , Issue.1 , pp. 142-153
    • Watanabe, K.1    Hata, Y.2    Kizaki, H.3    Katsube, Y.4    Suzuki, Y.5


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