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Volumn 65, Issue 5, 2009, Pages 477-484

EDM-DEDM and protein crystal structure solution

Author keywords

EDM DEDM; Model building; Molecular replacement; Phase refinement

Indexed keywords

ALGORITHM; ARTICLE; CHEMICAL MODEL; CHEMICAL STRUCTURE; COMPUTER PROGRAM; CRYSTALLIZATION; ELECTRON; METHODOLOGY; PROBABILITY; PROTEIN CONFORMATION; STATISTICS; X RAY CRYSTALLOGRAPHY;

EID: 65349187156     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444909008609     Document Type: Article
Times cited : (10)

References (107)
  • 15
    • 0033198415 scopus 로고    scopus 로고
    • Cowtan, K. (1999). Acta Cryst. D55, 1555-1567.
    • (1999) Acta Cryst , vol.D55 , pp. 1555-1567
    • Cowtan, K.1
  • 16
    • 33748337934 scopus 로고    scopus 로고
    • Cowtan, K. (2006). Acta Cryst., D62, 1002-1011.
    • (2006) Acta Cryst , vol.D62 , pp. 1002-1011
    • Cowtan, K.1
  • 30
  • 32
    • 84920325457 scopus 로고
    • Navaza, J. (1994). Acta Cryst. A50, 157-163.
    • (1994) Acta Cryst , vol.A50 , pp. 157-163
    • Navaza, J.1
  • 35
    • 0035788107 scopus 로고    scopus 로고
    • Read, R. J. (2001). Acta Cryst. D57, 1373-1382.
    • (2001) Acta Cryst , vol.D57 , pp. 1373-1382
    • Read, R.J.1
  • 49
    • 65349117310 scopus 로고
    • PhD thesis. Technische Universitat München, Germany
    • Turk, D (1992). PhD thesis. Technische Universitat München, Germany.
    • (1992)
    • Turk, D.1
  • 53
    • 84943120540 scopus 로고
    • Yao, J.-X. (1981). Acta Cryst. A37, 642-644.
    • (1981) Acta Cryst , vol.A37 , pp. 642-644
    • Yao, J.-X.1
  • 54
    • 0036849993 scopus 로고    scopus 로고
    • Yao, J.-X. (2002). Acta Cryst. D58, 1941-1947.
    • (2002) Acta Cryst , vol.D58 , pp. 1941-1947
    • Yao, J.-X.1
  • 55
    • 0345989988 scopus 로고    scopus 로고
    • edited by E. Arnold & M. G Rossmann, pp, Dordrecht: Kluwer Academic Publishers
    • Zhang, K. Y J., Cowtan, K. D & Main, P. (2001). International Tables for Crystallography, Vol. F, edited by E. Arnold & M. G Rossmann, pp. 311-331. Dordrecht: Kluwer Academic Publishers.
    • (2001) International Tables for Crystallography , vol.F , pp. 311-331
    • Zhang, K.Y.J.1    Cowtan, K.D.2    Main, P.3
  • 57
    • 0030044141 scopus 로고    scopus 로고
    • von Itzstein, M.; Dyason, J. C; Oliver, S. W.; White, H. F.; Wu, W. Y.; Kok, G. B.; Pegg, M. S. A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs. J. Med. Chem. 1996, 39, 388-391.
    • von Itzstein, M.; Dyason, J. C; Oliver, S. W.; White, H. F.; Wu, W. Y.; Kok, G. B.; Pegg, M. S. A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs. J. Med. Chem. 1996, 39, 388-391.
  • 58
    • 0028925854 scopus 로고    scopus 로고
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
  • 59
    • 0028925854 scopus 로고    scopus 로고
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
  • 60
    • 0028325249 scopus 로고
    • Molecular Modeling Studies on Ligand Binding to Sialidase from Influenza Virus and the Mechanism of Catalysis
    • Taylor, N. R.; von Itzstein, M. Molecular Modeling Studies on Ligand Binding to Sialidase from Influenza Virus and the Mechanism of Catalysis. J. Med. Chem. 1994, 37, 616-624.
    • (1994) J. Med. Chem , vol.37 , pp. 616-624
    • Taylor, N.R.1    von Itzstein, M.2
  • 61
    • 65349089782 scopus 로고    scopus 로고
    • Stoll, V, Stewart, K. D, Marmg, C. J, Muchmore, S, Giranda, V, Gu, Y. G, Wang, G, Chen, Y, Sun, M, Zhao, C; Kennedy, A. L, Madigan, D. L.;
    • Stoll, V.; Stewart, K. D.; Marmg, C. J.; Muchmore, S.; Giranda, V.; Gu, Y. G.; Wang, G.; Chen, Y.; Sun, M.; Zhao, C; Kennedy, A. L.; Madigan, D. L.;
  • 62
    • 0037469141 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors: Structure-based design of a novel inhibitor series
    • Xu, Y.; Saldivar, A.; Kati, W.; Laver, G.; Sowin, T.; Sham, H. L.; Greer, J.; Kempf, D. Influenza neuraminidase inhibitors: structure-based design of a novel inhibitor series. Biochemistry 2003, 42, 718-727.
    • (2003) Biochemistry , vol.42 , pp. 718-727
    • Xu, Y.1    Saldivar, A.2    Kati, W.3    Laver, G.4    Sowin, T.5    Sham, H.L.6    Greer, J.7    Kempf, D.8
  • 66
    • 0029099621 scopus 로고
    • Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction
    • Singh, S.; Jedrzejas, M. J.; Air, G. M.; Luo, M.; Laver, W. G.; Brouillette, W. J. Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction. J. Med. Chem. 1995 58,3217-3225.
    • (1995) J. Med. Chem , vol.58 , pp. 3217-3225
    • Singh, S.1    Jedrzejas, M.J.2    Air, G.M.3    Luo, M.4    Laver, W.G.5    Brouillette, W.J.6
  • 67
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Bhck, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Bhck, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 68
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Bhck, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Bhck, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 69
    • 0028925854 scopus 로고    scopus 로고
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
  • 70
    • 33645458687 scopus 로고    scopus 로고
    • Unsaturated N-acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase
    • Mann, M. C; Islam, T.; Dyason, J. C; Florio, P.; Trower, C. J.; Thomson, R. J.; von Itzstein, M. Unsaturated N-acetyl- D-glucosaminuronic acid glycosides as inhibitors of influenza virus sialidase. Glycoconj. J. 2006 23, 127-133.
    • (2006) Glycoconj. J , vol.23 , pp. 127-133
    • Mann, M.C.1    Islam, T.2    Dyason, J.C.3    Florio, P.4    Trower, C.J.5    Thomson, R.J.6    von Itzstein, M.7
  • 71
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Bhck, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Bhck, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 72
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Bhck, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Bhck, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 73
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Bhck, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Bhck, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 76
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Bhck, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Bhck, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 79
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkin, J.L.; Sahasrabudhe, A.; Blick, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkin, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 81
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Blick, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 82
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Blick, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 83
    • 0031911783 scopus 로고    scopus 로고
    • Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors
    • McKimm-Breschkm, J.L.; Sahasrabudhe, A.; Blick, T.J.; McDonald, M.; Colman, P. M.; Hart, G. J.; Bethell, R. C; Varghese, J. N. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Vir. 1998, 72, 2456-2462.
    • (1998) J. Vir , vol.72 , pp. 2456-2462
    • McKimm-Breschkm, J.L.1    Sahasrabudhe, A.2    Blick, T.J.3    McDonald, M.4    Colman, P.M.5    Hart, G.J.6    Bethell, R.C.7    Varghese, J.N.8
  • 84
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Blick, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 85
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Blick, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 87
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Blick, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 89
    • 0032526697 scopus 로고    scopus 로고
    • Drug design against a shifting target: A structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase
    • Varghese, J. N.; Smith, P. W.; Solhs, S. L.; Blick, T. J.; Sahasrabudhe, A.; McKimm-Breschkm, J. L.; Colman, P. M. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 1998, 6, 735-746.
    • (1998) Structure , vol.6 , pp. 735-746
    • Varghese, J.N.1    Smith, P.W.2    Solhs, S.L.3    Blick, T.J.4    Sahasrabudhe, A.5    McKimm-Breschkm, J.L.6    Colman, P.M.7
  • 94
    • 9644260491 scopus 로고    scopus 로고
    • Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core
    • Wang, G. T.; Wang, S.; Gentles, R.; Sowin, T.; Marmg, C. J.; Kempf, D. J.; Kati, W. M.; Stall, V.; Stewart, K. D.; Laver, G. Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core. Bioorg. Med. Chem. Lett. 2005,15, 125-128.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 125-128
    • Wang, G.T.1    Wang, S.2    Gentles, R.3    Sowin, T.4    Marmg, C.J.5    Kempf, D.J.6    Kati, W.M.7    Stall, V.8    Stewart, K.D.9    Laver, G.10
  • 95
    • 9644260491 scopus 로고    scopus 로고
    • Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core
    • Wang, G. T.; Wang, S.; Gentles, R.; Sowin, T.; Marmg, C. J.; Kempf, D. J.; Kati, W. M.; Stall, V.; Stewart, K. D.; Laver, G. Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core. Bioorg. Med. Chem. Lett. 2005,15, 125-128.
    • (2005) Bioorg. Med. Chem. Lett , vol.15 , pp. 125-128
    • Wang, G.T.1    Wang, S.2    Gentles, R.3    Sowin, T.4    Marmg, C.J.5    Kempf, D.J.6    Kati, W.M.7    Stall, V.8    Stewart, K.D.9    Laver, G.10
  • 97
    • 0032510373 scopus 로고    scopus 로고
    • Dihydropyrancarboxamides related to zanamivir: A new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B
    • Taylor, N. R.; Cleasby, A.; Singh, O.; Skarzynski, T.; Wonacott, A. J.; Smith, P. W.; Solhs, S. L; Howes, P. D.; Cherry, P. C; Bethell, R.; Colman, P.; Varghese, J. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B. J. Med. Chem. 1998, 41, 798-807.
    • (1998) J. Med. Chem , vol.41 , pp. 798-807
    • Taylor, N.R.1    Cleasby, A.2    Singh, O.3    Skarzynski, T.4    Wonacott, A.J.5    Smith, P.W.6    Solhs, S.L.7    Howes, P.D.8    Cherry, P.C.9    Bethell, R.10    Colman, P.11    Varghese, J.12
  • 98
    • 0028925854 scopus 로고    scopus 로고
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
    • White, C. L.; Janakiraman, M. N.; Laver, W. G.; Philippon, C; Vasella, A.; Air, G. M.; Luo, M. A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 1995 245, 623-634.
  • 99
    • 15644379365 scopus 로고    scopus 로고
    • Smith, P. W.; Solhs, S. L.; Howes, P. D.; Cherry, P. C; Starkey, I. D.; Cobley, K. N.; Weston, H.; Scicinski, J.; Merritt, A.; Whittington, A.; Wyatt, P.; Taylor, N.; Green, D.; Bethell, R.; Madar, S.; Fenton, R. J.; Morley, P. J.; Pateman, T.; Beresford, A. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 1. Discovery, synthesis, biological activity, and structure-activity relationships of 4-guanidino- and 4-amino-4H-pyran-6-carboxamides. J. Med. Chem. 1998, 41, 787-797.
    • Smith, P. W.; Solhs, S. L.; Howes, P. D.; Cherry, P. C; Starkey, I. D.; Cobley, K. N.; Weston, H.; Scicinski, J.; Merritt, A.; Whittington, A.; Wyatt, P.; Taylor, N.; Green, D.; Bethell, R.; Madar, S.; Fenton, R. J.; Morley, P. J.; Pateman, T.; Beresford, A. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 1. Discovery, synthesis, biological activity, and structure-activity relationships of 4-guanidino- and 4-amino-4H-pyran-6-carboxamides. J. Med. Chem. 1998, 41, 787-797.
  • 101
    • 0033550314 scopus 로고    scopus 로고
    • Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site
    • Fmley, J. B.; Atigadda, V. R.; Duarte, F.; Zhao, J. J.; Brouillette, W. J.; Air, G. M.; Luo, M. Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. J. Mol. Biol. 1999, 293, 1107-1119.
    • (1999) J. Mol. Biol , vol.293 , pp. 1107-1119
    • Fmley, J.B.1    Atigadda, V.R.2    Duarte, F.3    Zhao, J.J.4    Brouillette, W.J.5    Air, G.M.6    Luo, M.7
  • 103
    • 16644374078 scopus 로고    scopus 로고
    • Lommer, B. S.; Ali, S. M.; Bajpai, S. N.; Brouillette, W. J. ; Air, G. M.; Luo, M. A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase Acta Crystallogr. 2004, D60, 1017-1023.
    • Lommer, B. S.; Ali, S. M.; Bajpai, S. N.; Brouillette, W. J. ; Air, G. M.; Luo, M. A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase Acta Crystallogr. 2004, D60, 1017-1023.
  • 104
    • 16644374078 scopus 로고    scopus 로고
    • Lommer, B. S.; Ali, S. M.; Bajpai, S. N.; Brouillette, W. J. ; Air, G. M.; Luo, M. A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase Acta Crystallogr. 2004, D60, 1017-1023.
    • Lommer, B. S.; Ali, S. M.; Bajpai, S. N.; Brouillette, W. J. ; Air, G. M.; Luo, M. A benzoic acid inhibitor induces a novel conformational change in the active site of Influenza B virus neuraminidase Acta Crystallogr. 2004, D60, 1017-1023.
  • 105
    • 0033550314 scopus 로고    scopus 로고
    • Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site
    • Finley, J. B.; Atigadda, V. R; Duarte, F.; Zhao, J. J.; Brouillette, W. J.; Air, G. M.; Luo, M. Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. J. Mol. Biol. 1999, 293, 1107-1119.
    • (1999) J. Mol. Biol , vol.293 , pp. 1107-1119
    • Finley, J.B.1    Atigadda, V.R.2    Duarte, F.3    Zhao, J.J.4    Brouillette, W.J.5    Air, G.M.6    Luo, M.7
  • 107
    • 0033550314 scopus 로고    scopus 로고
    • Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site
    • Finley, J. B.; Atigadda, V. R.; Duarte, F.; Zhao, J. J.; Bromllette, W. J.; Air, G. M.; Luo, M. Novel aromatic inhibitors of influenza virus neuraminidase make selective interactions with conserved residues and water molecules in the active site. J. Mol. Biol. 1999, 293, 1107-1119.
    • (1999) J. Mol. Biol , vol.293 , pp. 1107-1119
    • Finley, J.B.1    Atigadda, V.R.2    Duarte, F.3    Zhao, J.J.4    Bromllette, W.J.5    Air, G.M.6    Luo, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.