메뉴 건너뛰기




Volumn 5, Issue 9, 1997, Pages 1139-1145

'Flu' and structure-based drug design

Author keywords

[No Author keywords available]

Indexed keywords

HUMAN INFLUENZA VIRUS; INFLUENZA VIRUS; INFLUENZAVIRUS A;

EID: 0030875781     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(97)00265-7     Document Type: Review
Times cited : (85)

References (38)
  • 1
    • 0031048319 scopus 로고    scopus 로고
    • Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: Design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity
    • Kim, C.U., et al., & Stevens, R.C. (1997). Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogues with potent anti-influenza activity. J. Am. Chem. Soc. 119, 681-690.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 681-690
    • Kim, C.U.1    Stevens, R.C.2
  • 2
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman, P.M., Varghese, J.N. & Laver, W.G. (1983). Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303, 41-44.
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 3
    • 0030050255 scopus 로고
    • Neuraminidase inhibitors as potential anti-influenza drugs
    • Bamford, M.J. (1995). Neuraminidase inhibitors as potential anti-influenza drugs. J. Enzyme Inhibition 10, 1-16.
    • (1995) J. Enzyme Inhibition , vol.10 , pp. 1-16
    • Bamford, M.J.1
  • 4
    • 0028113435 scopus 로고
    • Influenza virus neuraminidase: Structure, antibodies, and inhibitors
    • Colman, P.M. (1994). Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci. 3, 1687-1696.
    • (1994) Protein Sci. , vol.3 , pp. 1687-1696
    • Colman, P.M.1
  • 5
    • 0028813628 scopus 로고
    • Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding
    • Liu, C., Eichelberger, M.C., Compans, R.W. & Air, G.M. (1995). Influenza type A virus neuraminidase does not play a role in viral entry, replication, assembly, or budding. J. Virol. 69, 1099-1006.
    • (1995) J. Virol. , vol.69 , pp. 1099-11006
    • Liu, C.1    Eichelberger, M.C.2    Compans, R.W.3    Air, G.M.4
  • 7
    • 84945736084 scopus 로고
    • 2-Deoxy-2,3-dehydrosialic acids II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3, dehydroneuraminic acids
    • Meindl, P. & Tuppy, H. (1969). 2-Deoxy-2,3-dehydrosialic acids II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3, dehydroneuraminic acids. Hoppe-Seyler's Z. Physiol. Chem. 350, 1088-1092.
    • (1969) Hoppe-Seyler's Z. Physiol. Chem. , vol.350 , pp. 1088-1092
    • Meindl, P.1    Tuppy, H.2
  • 8
    • 0015959249 scopus 로고
    • Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid
    • Meindl, P., Bodo, G., Palese, P., Schulman, J. & Tuppy, H. (1974). Inhibition of neuraminidase activity by derivatives of 2-deoxy-2,3-dehydro-N-acetylneuraminic acid. Virology 58, 457-463.
    • (1974) Virology , vol.58 , pp. 457-463
    • Meindl, P.1    Bodo, G.2    Palese, P.3    Schulman, J.4    Tuppy, H.5
  • 9
    • 0020629047 scopus 로고
    • Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution
    • Varghese, J.N., Laver, W.G. & Colman, P.M. (1983). Structure of the influenza virus glycoprotein antigen neuraminidase at 2.9 Å resolution. Nature 303, 35-40.
    • (1983) Nature , vol.303 , pp. 35-40
    • Varghese, J.N.1    Laver, W.G.2    Colman, P.M.3
  • 10
    • 0027287506 scopus 로고
    • Rational design of potent sialidase-based inhibitors of influenza virus replication
    • von Itzstein, M., et al., & Penn, C.R. (1993). Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418-423.
    • (1993) Nature , vol.363 , pp. 418-423
    • Von Itzstein, M.1    Penn, C.R.2
  • 11
    • 0030044141 scopus 로고    scopus 로고
    • A study of the active site of influenza virus sialidase: An approach to the rational design of novel anti-influenza drugs
    • von Itzstein, M., et al., & Pegg, M.S. (1996). A study of the active site of influenza virus sialidase: an approach to the rational design of novel anti-influenza drugs. J. Med. Chem. 39, 388-391.
    • (1996) J. Med. Chem. , vol.39 , pp. 388-391
    • Von Itzstein, M.1    Pegg, M.S.2
  • 12
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P.J. (1985). A computational procedure for determining energetically favorable binding sites on biologically important macromolecules. J. Med. Chem. 28, 849-857.
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 13
    • 0027510004 scopus 로고
    • Further development of hydrogen-bond functions for use in determining energetically favourable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds
    • Wade, R.C. & Goodford, P.J. (1993). Further development of hydrogen-bond functions for use in determining energetically favourable binding sites on molecules of known structure. 2. Ligand probe groups with the ability to form more than two hydrogen bonds. J. Med. Chem. 36, 148-156.
    • (1993) J. Med. Chem. , vol.36 , pp. 148-156
    • Wade, R.C.1    Goodford, P.J.2
  • 14
    • 0030296267 scopus 로고    scopus 로고
    • Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino-Neu5Ac2en leads to instability of the enzyme
    • McKimm-Breschkin, J.L., McDonald, M., Blick, T.J. & Colman, P.M. (1996). Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino-Neu5Ac2en leads to instability of the enzyme. Virology 225, 240-242.
    • (1996) Virology , vol.225 , pp. 240-242
    • McKimm-Breschkin, J.L.1    McDonald, M.2    Blick, T.J.3    Colman, P.M.4
  • 15
    • 0029003145 scopus 로고
    • Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase
    • Varghese, J.N., Epa, V.C. & Colman, P.M. (1995). Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 4, 1081-1087.
    • (1995) Protein Sci. , vol.4 , pp. 1081-1087
    • Varghese, J.N.1    Epa, V.C.2    Colman, P.M.3
  • 16
    • 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. (1994). Molecular modeling studies on ligand binding to sialidase from influenza virus and the mechanism of catalysis. J. Med. Chem. 37, 616-624.
    • (1994) J. Med. Chem. , vol.37 , pp. 616-624
    • Taylor, N.R.1    Von Itzstein, M.2
  • 17
    • 0030157593 scopus 로고    scopus 로고
    • A structural and energetics analysis of the binding of a series of N-acetylneuraminic-acid-based inhibitors to influenza virus sialidase
    • Taylor, N.R. & von Itzstein, M. (1996). A structural and energetics analysis of the binding of a series of N-acetylneuraminic-acid-based inhibitors to influenza virus sialidase. J. Comput Aided Mol. Des. 10, 233-246.
    • (1996) J. Comput Aided Mol. Des. , vol.10 , pp. 233-246
    • Taylor, N.R.1    Von Itzstein, M.2
  • 18
    • 0028925854 scopus 로고
    • A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies
    • White, C.L., et al., & Luo, M. (1995). A sialic acid-derived phosphonate analog inhibits different strains of influenza virus neuraminidase with different efficiencies. J. Mol. Biol. 245, 623-634.
    • (1995) J. Mol. Biol. , vol.245 , pp. 623-634
    • White, C.L.1    Luo, M.2
  • 19
    • 0028940702 scopus 로고
    • Structures of aromatic inhibitors of influenza virus neuraminidase
    • Jedrzejas, M.J., et al., & Luo, M. (1995). Structures of aromatic inhibitors of influenza virus neuraminidase. Biochemistry 34, 3144-3151.
    • (1995) Biochemistry , vol.34 , pp. 3144-3151
    • Jedrzejas, M.J.1    Luo, M.2
  • 20
    • 0029099621 scopus 로고
    • Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction
    • Singh, S., et al., & Brouillette, W.J. (1995). Structure-based inhibitors of influenza virus sialidase. A benzoic acid lead with novel interaction. J. Med. Chem. 38, 3217-3225.
    • (1995) J. Med. Chem. , vol.38 , pp. 3217-3225
    • Singh, S.1    Brouillette, W.J.2
  • 21
    • 0028805201 scopus 로고
    • A strategy for theoretical binding constant, Ki, calculations for neuraminidase aromatic inhibitors designed on the basis of the active site structure of influenza virus neuraminidase
    • Jedrzejas, M.J., Singh, S., Brouillette, W.J., Air, G.M. & Luo, M. (1995). A strategy for theoretical binding constant, Ki, calculations for neuraminidase aromatic inhibitors designed on the basis of the active site structure of influenza virus neuraminidase. Proteins 23, 264-277.
    • (1995) Proteins , vol.23 , pp. 264-277
    • Jedrzejas, M.J.1    Singh, S.2    Brouillette, W.J.3    Air, G.M.4    Luo, M.5
  • 22
    • 0031552380 scopus 로고    scopus 로고
    • Guanidinobenzoic acid inhibitors of influenza virus neuraminidase
    • Sudbeck, E.A., et al., & Luo, M. (1997). Guanidinobenzoic acid inhibitors of influenza virus neuraminidase. J. Mol. Biol. 267, 584-594.
    • (1997) J. Mol. Biol. , vol.267 , pp. 584-594
    • Sudbeck, E.A.1    Luo, M.2
  • 23
    • 5444248415 scopus 로고
    • Synthesis of a carbocyclic analogue of N-acetylneuraminic acid (pseudo-N-acetylneuraminic acid)
    • Ogawa, S., Yoshikawa, M. & Taki, T. (1992). Synthesis of a carbocyclic analogue of N-acetylneuraminic acid (pseudo-N-acetylneuraminic acid). J. Chem. Soc. Chem. Commun., 406-408.
    • (1992) J. Chem. Soc. Chem. Commun. , pp. 406-408
    • Ogawa, S.1    Yoshikawa, M.2    Taki, T.3
  • 24
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I.A., Skehel, J.J. & Wiley, D.C. (1981). Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature 289, 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 25
    • 0027523625 scopus 로고
    • Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones
    • Bodian, D.L., et al., & Kuntz, I.D. (1993). Inhibition of the fusion-inducing conformational change of influenza hemagglutinin by benzoquinones and hydroquinones. Biochemistry 32, 2967-2978.
    • (1993) Biochemistry , vol.32 , pp. 2967-2978
    • Bodian, D.L.1    Kuntz, I.D.2
  • 26
    • 12644259779 scopus 로고
    • An approach to the design of anti-influenza agents
    • (Laver, W.G. & Air, G.M., eds), Academic Press, San Diego, USA
    • Wade, R.C. (1990). An approach to the design of anti-influenza agents. In Use of X-ray Crystallography in the Design of Antiviral Agents. (Laver, W.G. & Air, G.M., eds), pp. 61-74, Academic Press, San Diego, USA.
    • (1990) Use of X-ray Crystallography in the Design of Antiviral Agents , pp. 61-74
    • Wade, R.C.1
  • 27
    • 0026570977 scopus 로고
    • CLIX: A search algorithm for finding novel ligands capable of binding proteins of known three-dimensional structure
    • Lawrence, M.C. & Davis, P.C. (1992). CLIX: a search algorithm for finding novel ligands capable of binding proteins of known three-dimensional structure. Proteins 12, 31-41.
    • (1992) Proteins , vol.12 , pp. 31-41
    • Lawrence, M.C.1    Davis, P.C.2
  • 28
    • 0028282687 scopus 로고
    • HOOK: A program for finding novel molecular architectures that satisfy the chemical and steric requirements of a macromolecule binding site
    • Eisen, M.B., Wiley, D.C., Karplus, M. & Hubbard, R.E. (1994). HOOK: a program for finding novel molecular architectures that satisfy the chemical and steric requirements of a macromolecule binding site. Proteins 19, 199-221.
    • (1994) Proteins , vol.19 , pp. 199-221
    • Eisen, M.B.1    Wiley, D.C.2    Karplus, M.3    Hubbard, R.E.4
  • 29
    • 0026665418 scopus 로고
    • The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor
    • Varghese, J.N., McKimm-Breschkin, J.L., Caldwell, J.B., Kortt, A.A. & Colman, P.M. (1992). The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14, 327-332.
    • (1992) Proteins , vol.14 , pp. 327-332
    • Varghese, J.N.1    McKimm-Breschkin, J.L.2    Caldwell, J.B.3    Kortt, A.A.4    Colman, P.M.5
  • 30
    • 0027930960 scopus 로고
    • Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1.8-Å resolution: Implications for the catalytic mechanism
    • Janakiraman, M.N., White, C.L., Laver, W.G., Air, G.M. & Luo, M. (1994). Structure of influenza virus neuraminidase B/Lee/40 complexed with sialic acid and a dehydro analog at 1.8-Å resolution: implications for the catalytic mechanism. Biochemistry 33, 8172-8179.
    • (1994) Biochemistry , vol.33 , pp. 8172-8179
    • Janakiraman, M.N.1    White, C.L.2    Laver, W.G.3    Air, G.M.4    Luo, M.5
  • 31
    • 0026508847 scopus 로고
    • The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid
    • Burmeister, W.P., Ruigrok, R.W. & Cusack, S. (1992). The 2.2 Å resolution crystal structure of influenza B neuraminidase and its complex with sialic acid. EMBO J. 11, 49-56.
    • (1992) EMBO J. , vol.11 , pp. 49-56
    • Burmeister, W.P.1    Ruigrok, R.W.2    Cusack, S.3
  • 32
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis, W., et al., & Wiley, D.C. (1988). Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333, 426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Wiley, D.C.2
  • 33
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • Sauter, N.K., et al., & Wiley, D.C. (1992). Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 31, 9609-9621.
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1    Wiley, D.C.2
  • 34
    • 0026515091 scopus 로고
    • Use of sialic acid analogues to define functional groups involved in binding to the influenza virus hemagglutinin
    • Kelm, S., et al., & Zbiral, E. (1992). Use of sialic acid analogues to define functional groups involved in binding to the influenza virus hemagglutinin. Eur. J. Biochem. 205, 147-153.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 147-153
    • Kelm, S.1    Zbiral, E.2
  • 35
    • 0000016640 scopus 로고
    • Design and evaluation of a tightly binding fluorescent ligand for influenza A hemagglutinin
    • Weinhold, E.G. & Knowles, J.R. (1992). Design and evaluation of a tightly binding fluorescent ligand for influenza A hemagglutinin. J. Am. Chem. Soc. 114, 9270-9275.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9270-9275
    • Weinhold, E.G.1    Knowles, J.R.2
  • 36
    • 0028774043 scopus 로고
    • Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
    • Watowich, S.J., Skehel, J.J. & Wiley, D.C. (1994). Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure 2, 719-731.
    • (1994) Structure , vol.2 , pp. 719-731
    • Watowich, S.J.1    Skehel, J.J.2    Wiley, D.C.3
  • 37
    • 0028805760 scopus 로고
    • Effective inhibitors of haemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition
    • Mammen, M., Dahmann, G. & Whitesides, G.M. (1995). Effective inhibitors of haemagglutination by influenza virus synthesized from polymers having active ester groups. Insight into mechanism of inhibition. J. Med. Chem. 38, 4179-4190.
    • (1995) J. Med. Chem. , vol.38 , pp. 4179-4190
    • Mammen, M.1    Dahmann, G.2    Whitesides, G.M.3
  • 38
    • 0030250628 scopus 로고    scopus 로고
    • Optically controlled collisions of biological objects to evaluate potent polyvalent inhibitors of virus-cell adhesion
    • Mammen, M., Helmerson, K., Kishore, R., Choi, S.K., Phillips, W.D. & Whitesides, G.M. (1996). Optically controlled collisions of biological objects to evaluate potent polyvalent inhibitors of virus-cell adhesion. Chem. Biol. 3, 757-763.
    • (1996) Chem. Biol. , vol.3 , pp. 757-763
    • Mammen, M.1    Helmerson, K.2    Kishore, R.3    Choi, S.K.4    Phillips, W.D.5    Whitesides, G.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.