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Volumn , Issue , 2011, Pages 78-91

Monovalent and multivalent inhibitors of bacterial toxins

Author keywords

Bacterial toxin; Cholera; Dendrimer; Inhibitor; Multivalency

Indexed keywords


EID: 84882883517     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.2174/978160805277611101010078     Document Type: Chapter
Times cited : (2)

References (102)
  • 1
    • 0037324357 scopus 로고    scopus 로고
    • An evaluation of current cholera treatment
    • Bhattacharya, S.K. An evaluation of current cholera treatment. Exp. Opin. Pharmacother., 2003, 4, 141-146.
    • (2003) Exp. Opin. Pharmacother. , vol.4 , pp. 141-146
    • Bhattacharya, S.K.1
  • 2
    • 20544472058 scopus 로고    scopus 로고
    • Virulence factors, pathogenesis and vaccine protection in cholera and ETEC diarrhea
    • Sánchez, J.; Holmgren, J. Virulence factors, pathogenesis and vaccine protection in cholera and ETEC diarrhea. Curr. Opin. Immunol., 2005, 17, 388-398.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 388-398
    • Sánchez, J.1    Holmgren, J.2
  • 3
    • 84882908711 scopus 로고    scopus 로고
    • World Health Organisation
    • World Health Organisation. Communicable Diseases, 2003, 74-79.
    • (2003) Communicable Diseases , pp. 74-79
  • 4
    • 77950349777 scopus 로고    scopus 로고
    • Cholera vaccines: WHO position paper Wkly Epidemiol
    • Anon
    • Anon. Cholera vaccines: WHO position paper Wkly Epidemiol. Rec., 2010, 85, 117-128.
    • (2010) Rec. , vol.85 , pp. 117-128
  • 5
    • 64149107841 scopus 로고    scopus 로고
    • Zimbabwe's battle against cholera
    • Chambers, K. Zimbabwe's battle against cholera. Lancet, 2009, 373, 993-994.
    • (2009) Lancet , vol.373 , pp. 993-994
    • Chambers, K.1
  • 7
    • 70349763962 scopus 로고    scopus 로고
    • Cholera: Global surveillance summary, 2008
    • Anon
    • Anon. Cholera: Global surveillance summary, 2008. Wkly Epidemiol. Rec., 2009, 84, 309-324.
    • (2009) Wkly Epidemiol. Rec. , vol.84 , pp. 309-324
  • 11
    • 34447505930 scopus 로고    scopus 로고
    • The true burden and risk of cholera: Implications for prevention and control
    • Zuckerman, J.N.; Rombo, L.; Fisch, A. The true burden and risk of cholera: Implications for prevention and control. Lancet Infect. Dis., 2007, 7, 521-530.
    • (2007) Lancet Infect. Dis. , vol.7 , pp. 521-530
    • Zuckerman, J.N.1    Rombo, L.2    Fisch, A.3
  • 12
    • 0021021637 scopus 로고
    • Cholera-toxin genes - nucleotidesequence, deletion analysis and vaccine development
    • Mekalanos, J.J.; Swartz, D.J.; Pearson, G.D.N.; Harford, N.; Groyne, F.; Dewilde, M. Cholera-toxin genes - nucleotidesequence, deletion analysis and vaccine development. Nature, 1983, 306, 551-557.
    • (1983) Nature , vol.306 , pp. 551-557
    • Mekalanos, J.J.1    Swartz, D.J.2    Pearson, G.D.N.3    Harford, N.4    Groyne, F.5    Dewilde, M.6
  • 13
    • 0026458260 scopus 로고
    • Structure and function of cholera-toxin and the related Escherichia coli heat-labile enterotoxin
    • Spangler, B.D. Structure and function of cholera-toxin and the related Escherichia coli heat-labile enterotoxin. Microbiol. Rev., 1992, 56, 622-647.
    • (1992) Microbiol. Rev. , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 14
    • 0018234925 scopus 로고
    • Demonstration of shared and unique immunological determinants in enterotoxins from Vibrio cholerae and Escherichia coli
    • Clements, J.D.; Finkelstein, R.A. Demonstration of shared and unique immunological determinants in enterotoxins from Vibrio cholerae and Escherichia coli. Infect. Immun., 1978, 22, 709-713.
    • (1978) Infect. Immun. , vol.22 , pp. 709-713
    • Clements, J.D.1    Finkelstein, R.A.2
  • 15
  • 16
    • 1842487379 scopus 로고    scopus 로고
    • Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism
    • O'Neal, C.J.; Amaya, E.I.; Jobling, M.G.; Holmes, R.K.; Hol, W.G.J. Crystal structures of an intrinsically active cholera toxin mutant yield insight into the toxin activation mechanism. Biochemistry, 2004, 43, 3772-3782.
    • (2004) Biochemistry , vol.43 , pp. 3772-3782
    • O'Neal, C.J.1    Amaya, E.I.2    Jobling, M.G.3    Holmes, R.K.4    Hol, W.G.J.5
  • 19
    • 20544472058 scopus 로고    scopus 로고
    • Virulence factors, pathogenesis and vaccine protection in cholera and ETEC diarrhea
    • Sanchez, J.; Holmgren, J. Virulence factors, pathogenesis and vaccine protection in cholera and ETEC diarrhea. Curr. Opin. Immunol., 2005, 17, 388-398.
    • (2005) Curr. Opin. Immunol. , vol.17 , pp. 388-398
    • Sanchez, J.1    Holmgren, J.2
  • 21
    • 1942487871 scopus 로고    scopus 로고
    • Cholera toxin: A paradigm for multi-functional engagement of cellular mechanisms
    • De Haan, L.; Hirst, T.R. Cholera toxin: A paradigm for multi-functional engagement of cellular mechanisms. Mol. Membr. Biol., 2004, 21, 77-92.
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 77-92
    • De Haan, L.1    Hirst, T.R.2
  • 22
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B.; Rodighiero, C.; Lencer, W.I.; Rapoport, T.A. Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell, 2001, 104, 937-948.
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 23
    • 43049157532 scopus 로고    scopus 로고
    • Cholera toxin structure, gene regulation and pathophysiological and immunological aspects
    • Sanchez, J.; Holmgren, J. Cholera toxin structure, gene regulation and pathophysiological and immunological aspects. Cell. Mol. Life Sci., 2008, 65, 1347-1360.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1347-1360
    • Sanchez, J.1    Holmgren, J.2
  • 24
    • 0017324358 scopus 로고
    • Mechanism of action of cholera toxin
    • Gill, D.M. Mechanism of action of cholera toxin. Adv. Cyclic Nucleotide Res., 1977, 8, 85-118.
    • (1977) Adv. Cyclic Nucleotide Res. , vol.8 , pp. 85-118
    • Gill, D.M.1
  • 25
    • 0018120221 scopus 로고
    • Genetic evidence that cholera toxin substrates are regulatory components of adenylate-cyclase
    • Johnson, G.L.; Kaslow, H.R.; Bourne, H.R. Genetic evidence that cholera toxin substrates are regulatory components of adenylate-cyclase. J. Biol. Chem., 1978, 253, 7120-7123.
    • (1978) J. Biol. Chem. , vol.253 , pp. 7120-7123
    • Johnson, G.L.1    Kaslow, H.R.2    Bourne, H.R.3
  • 26
    • 1842384421 scopus 로고
    • ADP-ribosylation of membrane proteins catalyzed by cholera toxin - basis of activation of adenylate-cyclase
    • Gill, D.M.; Meren, R. ADP-ribosylation of membrane proteins catalyzed by cholera toxin - basis of activation of adenylate-cyclase. Proc. Natl. Acad. Sci. USA, 1978, 75, 3050-3054.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3050-3054
    • Gill, D.M.1    Meren, R.2
  • 27
    • 0008614480 scopus 로고
    • Mechanism of adenylate-cyclase activation by cholera toxin - inhibition of GTP hydrolysis at regulatory site
    • Cassel, D.; Selinger, Z. Mechanism of adenylate-cyclase activation by cholera toxin - inhibition of GTP hydrolysis at regulatory site. Proc. Natl. Acad. Sci. USA, 1977, 74, 3307-3311.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3307-3311
    • Cassel, D.1    Selinger, Z.2
  • 29
    • 70249106100 scopus 로고    scopus 로고
    • Design and in silico screening of inhibitors of the cholera toxin
    • Zhang, G.T. Design and in silico screening of inhibitors of the cholera toxin. Exp. Opin. Drug Disc., 2009, 4, 923-938.
    • (2009) Exp. Opin. Drug Disc. , vol.4 , pp. 923-938
    • Zhang, G.T.1
  • 30
    • 0037191074 scopus 로고    scopus 로고
    • Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by ERO1
    • Tsai, B.; Rapoport, T.A. Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by ERO1. J. Cell Biol., 2002, 159, 207-215.
    • (2002) J. Cell Biol. , vol.159 , pp. 207-215
    • Tsai, B.1    Rapoport, T.A.2
  • 31
    • 0017286418 scopus 로고
    • Arrangement of subunits in cholera toxin
    • Gill, D.M. Arrangement of subunits in cholera toxin. Biochemistry, 1976, 15, 1242-1248.
    • (1976) Biochemistry , vol.15 , pp. 1242-1248
    • Gill, D.M.1
  • 32
    • 0015631938 scopus 로고
    • Subunit structure of cholera toxin
    • Lonnroth, I.; Holmgren, J. Subunit structure of cholera toxin. J. Gen. Microbiol., 1973, 76, 417-427.
    • (1973) J. Gen. Microbiol. , vol.76 , pp. 417-427
    • Lonnroth, I.1    Holmgren, J.2
  • 33
    • 0004758773 scopus 로고    scopus 로고
    • Structure-based discovery of a pore-binding ligand: Towards assembly inhibitors for cholera and related AB5 toxins
    • Hovey, B.T.; Verlinde, C.L.M.J.; Merritt, E.A.; Hol, W.G.J. Structure-based discovery of a pore-binding ligand: Towards assembly inhibitors for cholera and related AB5 toxins. J. Mol. Biol., 1999, 285, 1169-1178.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1169-1178
    • Hovey, B.T.1    Verlinde, C.L.M.J.2    Merritt, E.A.3    Hol, W.G.J.4
  • 34
    • 0015950912 scopus 로고
    • Cholera Toxin: interaction of subunits with ganglioside GM1
    • van Heyningen, S. Cholera Toxin: interaction of subunits with ganglioside GM1. Science, 1974, 183, 656-657.
    • (1974) Science , vol.183 , pp. 656-657
    • Van Heyningen, S.1
  • 36
    • 0032500378 scopus 로고    scopus 로고
    • The 1.25 Å resolution refinement of the cholera toxin B-pentamer: Evidence of peptide backbone strain at the receptor-binding site
    • Merritt, E.A.; Kuhn, P.; Sarfaty, S.; Erbe, J.L.; Holmes, R.K.; Hol, W.G.J. The 1.25 Å resolution refinement of the cholera toxin B-pentamer: Evidence of peptide backbone strain at the receptor-binding site. J. Mol. Biol., 1998, 282, 1043-1059.
    • (1998) J. Mol. Biol. , vol.282 , pp. 1043-1059
    • Merritt, E.A.1    Kuhn, P.2    Sarfaty, S.3    Erbe, J.L.4    Holmes, R.K.5    Hol, W.G.J.6
  • 37
    • 0024377837 scopus 로고
    • Thermodynamics of intersubunit interactions in cholera toxin upon binding to the oligosaccharide portion of its cell surface receptor, ganglioside GM1
    • Schon, A.; Freire, E. Thermodynamics of intersubunit interactions in cholera toxin upon binding to the oligosaccharide portion of its cell surface receptor, ganglioside GM1. Biochemistry, 1989, 28, 5019-24.
    • (1989) Biochemistry , vol.28 , pp. 5019-5024
    • Schon, A.1    Freire, E.2
  • 38
    • 0026609345 scopus 로고
    • Fuc-GM1 ganglioside mimics the receptor function of GM1 for cholera toxin
    • Masserini, M.; Freire, E.; Palestini, P.; Calappi, E.; Tettamanti, G. Fuc-GM1 ganglioside mimics the receptor function of GM1 for cholera toxin. Biochemistry, 1992, 31, 2422-2426.
    • (1992) Biochemistry , vol.31 , pp. 2422-2426
    • Masserini, M.1    Freire, E.2    Palestini, P.3    Calappi, E.4    Tettamanti, G.5
  • 39
    • 0028939257 scopus 로고
    • Fluorescence analysis of the interaction between ganglioside GM1- containing phospholipid vesicles and the B subunit of cholera toxin
    • Picking, W.L.; Moon, H.; Wu, H.; Picking, W.D. Fluorescence analysis of the interaction between ganglioside GM1- containing phospholipid vesicles and the B subunit of cholera toxin. Biochim. Biophys. Acta, 1995, 1247, 65-73.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 65-73
    • Picking, W.L.1    Moon, H.2    Wu, H.3    Picking, W.D.4
  • 40
    • 0029885779 scopus 로고    scopus 로고
    • Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance
    • Kuziemko, G.M.; Stroh, M.; Stevens, R.C. Cholera toxin binding affinity and specificity for gangliosides determined by surface plasmon resonance. Biochemistry, 1996, 35, 6375-6384.
    • (1996) Biochemistry , vol.35 , pp. 6375-6384
    • Kuziemko, G.M.1    Stroh, M.2    Stevens, R.C.3
  • 41
    • 0030568843 scopus 로고    scopus 로고
    • Fluorescence analysis of galactose, lactose, and fucose interaction with the cholera toxin b subunit
    • Mertz, J.A.; McCann, J.A.; Picking, W.D. Fluorescence analysis of galactose, lactose, and fucose interaction with the cholera toxin b subunit. Biochem. Biophys. Res. Commun., 1996, 226, 140-144.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 140-144
    • Mertz, J.A.1    McCann, J.A.2    Picking, W.D.3
  • 42
    • 0031041314 scopus 로고    scopus 로고
    • Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance
    • MacKenzie, C.R.; Hirama, T.; Lee, K.K.; Altman, E.; Young, N.M. Quantitative analysis of bacterial toxin affinity and specificity for glycolipid receptors by surface plasmon resonance. J. Biol. Chem., 1997, 272, 5533-5538.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5533-5538
    • MacKenzie, C.R.1    Hirama, T.2    Lee, K.K.3    Altman, E.4    Young, N.M.5
  • 43
    • 0037446757 scopus 로고    scopus 로고
    • The binding potential between the cholera toxin B-oligomer and its receptor
    • Cai, X.-E.; Yang, J. The binding potential between the cholera toxin B-oligomer and its receptor. Biochemistry, 2003, 42, 4028-4034.
    • (2003) Biochemistry , vol.42 , pp. 4028-4034
    • Cai, X.-E.1    Yang, J.2
  • 44
    • 0942287128 scopus 로고    scopus 로고
    • Dissecting the cholera toxin-ganglioside GM1 interaction by isothermal titration calorimetry
    • Turnbull, W.B.; Precious, B.L.; Homans, S.W. Dissecting the cholera toxin-ganglioside GM1 interaction by isothermal titration calorimetry. J. Am. Chem. Soc., 2004, 126, 1047-1054.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1047-1054
    • Turnbull, W.B.1    Precious, B.L.2    Homans, S.W.3
  • 46
    • 0037131439 scopus 로고    scopus 로고
    • Second-generation mimics of ganglioside GM1 oligosaccharide: A three-dimensional view of their interactions with bacterial enterotoxins by nmr and computational methods
    • Bernardi, A.; Potenza, D.; Capelli, A.M.; Garcia-Herrero, A.; Canada, F. J.; Jimenez-Barbero, J. Second-generation mimics of ganglioside GM1 oligosaccharide: A three-dimensional view of their interactions with bacterial enterotoxins by nmr and computational methods. Chem. Eur. J., 2002, 8, 4597-4612.
    • (2002) Chem. Eur. J. , vol.8 , pp. 4597-4612
    • Bernardi, A.1    Potenza, D.2    Capelli, A.M.3    Garcia-herrero, A.4    Canada, F.J.5    Jimenez-barbero, J.6
  • 48
    • 84919581851 scopus 로고
    • An investigation of travellers diarrhoea
    • Rowe, B.; Taylor, J.; Bettelhe, K.A. An investigation of travellers diarrhoea. Lancet, 1970, 1, 1-5.
    • (1970) Lancet , vol.1 , pp. 1-5
    • Rowe, B.1    Taylor, J.2    Bettelhe, K.A.3
  • 49
    • 0014591440 scopus 로고
    • A heat-labile enterotoxin from strains of Escherichia coli enteropathogenic for pigs
    • Gyles, C.L.; Barnum, D.A. A heat-labile enterotoxin from strains of Escherichia coli enteropathogenic for pigs. J. Infect. Dis., 1969, 120, 419-426.
    • (1969) J. Infect. Dis. , vol.120 , pp. 419-426
    • Gyles, C.L.1    Barnum, D.A.2
  • 50
    • 0028123001 scopus 로고
    • Galactose-binding site in escherichia-coli heatlabile enterotoxin (LT) and cholera-toxin (CT)
    • Merritt, E.A.; Sixma, T.K.; Kalk, K.H.; Vanzanten, B.A.M.; Hol, W.G.J. Galactose-binding site in escherichia-coli heatlabile enterotoxin (LT) and cholera-toxin (CT). Mol. Microbiol., 1994, 13, 745-753.
    • (1994) Mol. Microbiol. , vol.13 , pp. 745-753
    • Merritt, E.A.1    Sixma, T.K.2    Kalk, K.H.3    Vanzanten, B.A.M.4    Hol, W.G.J.5
  • 51
    • 0019293278 scopus 로고
    • Amino-acid-sequence homology between cholera-toxin and Escherichia coli heat-labile toxin
    • Dallas, W.S.; Falkow, S. Amino-acid-sequence homology between cholera-toxin and Escherichia coli heat-labile toxin. Nature, 1980, 288, 499-501.
    • (1980) Nature , vol.288 , pp. 499-501
    • Dallas, W.S.1    Falkow, S.2
  • 52
    • 0035124907 scopus 로고    scopus 로고
    • Exploration of the GM1 receptor-binding site of heat-labile enterotoxin and cholera toxin by phenyl-ring-containing galactose derivatives
    • Fan, E.; Merritt, E.A.; Zhang, Z.; Pickens, J.C.; Roach, C.; Ahn, M.; Hol, W.G.J. Exploration of the GM1 receptor-binding site of heat-labile enterotoxin and cholera toxin by phenyl-ring-containing galactose derivatives. Acta Cryst. D: Biol. Cryst., 2001, D57, 201-212.
    • (2001) Acta Cryst. D: Biol. Cryst. , vol.D57 , pp. 201-212
    • Fan, E.1    Merritt, E.A.2    Zhang, Z.3    Pickens, J.C.4    Roach, C.5    Ahn, M.6    Hol, W.G.J.7
  • 54
    • 44849143695 scopus 로고    scopus 로고
    • Design, synthesis, and evaluation of bisubstrate analog inhibitors of cholera toxin
    • Zhang, G. Design, synthesis, and evaluation of bisubstrate analog inhibitors of cholera toxin. Bioorg. Med. Chem. Lett., 2008, 18, 3724-3727.
    • (2008) Bioorg. Med. Chem. Lett. , vol.18 , pp. 3724-3727
    • Zhang, G.1
  • 56
    • 21144476404 scopus 로고
    • Synthetic studies on sialoglycoconjugates 48 - total synthesis of gangliosides GM1 and GD1a
    • Hasegawa, A.; Ishida, H.; Nagahama, T.; Kiso, M. Synthetic studies on sialoglycoconjugates 48 - total synthesis of gangliosides GM1 and GD1a. J. Carbohydr. Chem., 1993, 12, 703-718.
    • (1993) J. Carbohydr. Chem. , vol.12 , pp. 703-718
    • Hasegawa, A.1    Ishida, H.2    Nagahama, T.3    Kiso, M.4
  • 58
    • 0023050661 scopus 로고
    • Synthetic studies on cell-surface glycans.50. Total synthesis of gangliosides GM1 and GM2
    • Sugimoto, M.; Numata, M.; Koike, K.; Nakahara, Y.; Ogawa, T. Synthetic studies on cell-surface glycans.50. Total synthesis of gangliosides GM1 and GM2. Carbohydr. Res., 1986, 156, C1-C5.
    • (1986) Carbohydr. Res. , vol.156
    • Sugimoto, M.1    Numata, M.2    Koike, K.3    Nakahara, Y.4    Ogawa, T.5
  • 59
    • 0033958705 scopus 로고    scopus 로고
    • A total synthesis of the methyl glycoside of ganglioside GM(1)
    • Bhattacharya, S.K.; Danishefsky, S.J. A total synthesis of the methyl glycoside of ganglioside GM(1). J. Org. Chem., 2000, 65, 144-151.
    • (2000) J. Org. Chem. , vol.65 , pp. 144-151
    • Bhattacharya, S.K.1    Danishefsky, S.J.2
  • 62
    • 0025007355 scopus 로고
    • Three-dimensional structure of the oligosaccharide chain of GM1 ganglioside revealed by a distance-mapping procedure: A rotating and laboratory frame nuclear overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in waterdodecylphosphocholine solutions
    • Acquotti, D.; Poppe, L.; Dabrowski, J.; Von der Lieth, C.W.; Sonnino, S.; Tettamanti, G. Three-dimensional structure of the oligosaccharide chain of GM1 ganglioside revealed by a distance-mapping procedure: A rotating and laboratory frame nuclear overhauser enhancement investigation of native glycolipid in dimethyl sulfoxide and in waterdodecylphosphocholine solutions. J. Am. Chem. Soc., 1990, 112, 7772-7778.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7772-7778
    • Acquotti, D.1    Poppe, L.2    Dabrowski, J.3    Von Der Lieth, C.W.4    Sonnino, S.5    Tettamanti, G.6
  • 63
    • 0029395918 scopus 로고
    • Solution dynamics of the oligosaccharide moiety of ganglioside GM1: Comparison of solution conformations with the bound state conformation in association with cholera toxin b-pentamer
    • Richardson, J.M.; Milton, M.J.; Homans, S.W. Solution dynamics of the oligosaccharide moiety of ganglioside GM1: Comparison of solution conformations with the bound state conformation in association with cholera toxin b-pentamer. J. Mol. Recognit., 1995, 8, 358-362.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 358-362
    • Richardson, J.M.1    Milton, M.J.2    Homans, S.W.3
  • 64
    • 0029040073 scopus 로고
    • Conformational analysis of gm1 oligosaccharide in water solution with a new set of parameters for the Neu5Ac moiety
    • Bernardi, A.; Raimondi, L. Conformational analysis of gm1 oligosaccharide in water solution with a new set of parameters for the Neu5Ac moiety. J. Org. Chem., 1995, 60, 3370-3377.
    • (1995) J. Org. Chem. , vol.60 , pp. 3370-3377
    • Bernardi, A.1    Raimondi, L.2
  • 67
    • 0034597073 scopus 로고    scopus 로고
    • Second generation mimics of ganglioside GM1 as artificial receptors for cholera toxin: Replacement of the sialic acid moiety
    • Bernardi, A.; Carrettoni, L.; Ciponte, A.G.; Monti, D.; Sonnino, S. Second generation mimics of ganglioside GM1 as artificial receptors for cholera toxin: Replacement of the sialic acid moiety. Bioorg. Med. Chem. Lett., 2000, 10, 2197-2200.
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 2197-2200
    • Bernardi, A.1    Carrettoni, L.2    Ciponte, A.G.3    Monti, D.4    Sonnino, S.5
  • 69
    • 0141545065 scopus 로고    scopus 로고
    • Ganglioside GM1 mimics: Lipophilic substituents improve affinity for cholera toxin
    • Arosio, D.; Baretti, S.; Cattaldo, S.; Potenza, D.; Bernardi, A. Ganglioside GM1 mimics: Lipophilic substituents improve affinity for cholera toxin. Bioorg. Med. Chem. Lett., 2003, 13, 3831-3834.
    • (2003) Bioorg. Med. Chem. Lett. , vol.13 , pp. 3831-3834
    • Arosio, D.1    Baretti, S.2    Cattaldo, S.3    Potenza, D.4    Bernardi, A.5
  • 70
    • 75749146598 scopus 로고    scopus 로고
    • Synthesis and affinity evaluation of a small library of bidentate cholera toxin ligands: Towards nonhydrolyzable ganglioside mimics
    • Cheshev, P.; Morelli, L.; Marchesi, M.; Podlipnik, C.; Bergstrom, M.; Bernardi, A. Synthesis and affinity evaluation of a small library of bidentate cholera toxin ligands: Towards nonhydrolyzable ganglioside mimics. Chem. Eur. J., 2010, 16, 1951-1967.
    • (2010) Chem. Eur. J. , vol.16 , pp. 1951-1967
    • Cheshev, P.1    Morelli, L.2    Marchesi, M.3    Podlipnik, C.4    Bergstrom, M.5    Bernardi, A.6
  • 71
    • 0033585008 scopus 로고    scopus 로고
    • Using a galactose library for exploration of a novel hydrophobic pocket in the receptor binding site of the Escherichia coli heat-labile enterotoxin
    • Minke, W.E.; Hong, F.; Verlinde, C.L.M.J.; Hol, W.G.J.; Fan, E. Using a galactose library for exploration of a novel hydrophobic pocket in the receptor binding site of the Escherichia coli heat-labile enterotoxin. J. Biol. Chem., 1999, 274, 33469-33473.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33469-33473
    • Minke, W.E.1    Hong, F.2    Verlinde, C.L.M.J.3    Hol, W.G.J.4    Fan, E.5
  • 72
    • 0035667728 scopus 로고    scopus 로고
    • Synthesis of lactose dendrimers and multivalency effects in binding to the cholera toxin b subunit
    • Vrasidas, I.; De Mol, N.J.; Liskamp, R.M.J.; Pieters, R.J. Synthesis of lactose dendrimers and multivalency effects in binding to the cholera toxin b subunit. Eur. J. Org. Chem., 2001, 4685-4692.
    • (2001) Eur. J. Org. Chem. , pp. 4685-4692
    • Vrasidas, I.1    De Mol, N.J.2    Liskamp, R.M.J.3    Pieters, R.J.4
  • 73
    • 0037118356 scopus 로고    scopus 로고
    • Synthesis and cholera toxin binding properties of a lactose-2- aminothiazoline conjugate
    • Vrasidas, I.; Kemmink, J.; Liskamp, R.M.J.; Pieters, R.J. Synthesis and cholera toxin binding properties of a lactose-2- aminothiazoline conjugate. Org. Lett., 2002, 4, 1807-1808.
    • (2002) Org. Lett. , vol.4 , pp. 1807-1808
    • Vrasidas, I.1    Kemmink, J.2    Liskamp, R.M.J.3    Pieters, R.J.4
  • 74
    • 0033522424 scopus 로고    scopus 로고
    • Structure-based exploration of the ganglioside GM1 binding sites of escherichia coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonists
    • Minke, W.E.; Roach, C.; Hol, W.G.J.; Verlinde, C.L.M.J. Structure-based exploration of the ganglioside GM1 binding sites of escherichia coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonists. Biochemistry, 1999, 38, 5684-5692.
    • (1999) Biochemistry , vol.38 , pp. 5684-5692
    • Minke, W.E.1    Roach, C.2    Hol, W.G.J.3    Verlinde, C.L.M.J.4
  • 75
    • 0036008848 scopus 로고    scopus 로고
    • Anchor-based design of improved cholera toxin and E-coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes
    • Pickens, J.C.; Merritt, E.A.; Ahn, M.; Verlinde, C.; Hol, W.G.J.; Fan, E.K. Anchor-based design of improved cholera toxin and E-coli heat-labile enterotoxin receptor binding antagonists that display multiple binding modes. Chem. Biol., 2002, 9, 215-224.
    • (2002) Chem. Biol. , vol.9 , pp. 215-224
    • Pickens, J.C.1    Merritt, E.A.2    Ahn, M.3    Verlinde, C.4    Hol, W.G.J.5    Fan, E.K.6
  • 76
    • 35548998270 scopus 로고    scopus 로고
    • Design of a focused virtual library to explore cholera toxin b-site
    • Podlipnik, C.; Bernardi, A. Design of a focused virtual library to explore cholera toxin b-site. Acta Chim. Slov., 2007, 54, 425-436.
    • (2007) Acta Chim. Slov. , vol.54 , pp. 425-436
    • Podlipnik, C.1    Bernardi, A.2
  • 78
    • 15744377412 scopus 로고    scopus 로고
    • A synthetic divalent cholera toxin glycocalix[4]arene ligand having higher affinity than natural gm1 oligosaccharide
    • Arosio, D.; Fontanella, M.; Baldini, L.; Mauri, L.; Bernardi, A.; Casnati, A.; Sansone, F.; Ungaro, R. A synthetic divalent cholera toxin glycocalix[4]arene ligand having higher affinity than natural gm1 oligosaccharide. J. Am. Chem. Soc., 2005, 127, 3660-3661.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 3660-3661
    • Arosio, D.1    Fontanella, M.2    Baldini, L.3    Mauri, L.4    Bernardi, A.5    Casnati, A.6    Sansone, F.7    Ungaro, R.8
  • 79
    • 0034701264 scopus 로고    scopus 로고
    • High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design
    • Fan, E.; Zhang, Z.; Minke, W.E.; Hou, Z.; Verlinde, C.L.M.J.; Hol, W.G.J. High-affinity pentavalent ligands of Escherichia coli heat-labile enterotoxin by modular structure-based design. J. Am. Chem. Soc., 2000, 122, 2663-2664.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2663-2664
    • Fan, E.1    Zhang, Z.2    Minke, W.E.3    Hou, Z.4    Verlinde, C.L.M.J.5    Hol, W.G.J.6
  • 80
    • 0024351848 scopus 로고
    • Binding of vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to GM1, derivatives of GM1, and nonlipid oligosaccharide polyvalent ligands
    • Schengrund, C.L.; Ringler, N.J. Binding of vibrio cholera toxin and the heat-labile enterotoxin of Escherichia coli to GM1, derivatives of GM1, and nonlipid oligosaccharide polyvalent ligands. J. Biol. Chem., 1989, 264, 13233-13237.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13233-13237
    • Schengrund, C.L.1    Ringler, N.J.2
  • 81
    • 75749112873 scopus 로고    scopus 로고
    • Manipulation of electrostatic and saccharide linker interactions in the design of efficient glycopolypeptide-based cholera toxin inhibitors
    • Maheshwari, R.; Levenson, E.A.; Kiick, K.L. Manipulation of electrostatic and saccharide linker interactions in the design of efficient glycopolypeptide-based cholera toxin inhibitors. Macromol. Biosci., 2010, 10, 68-81.
    • (2010) Macromol. Biosci. , vol.10 , pp. 68-81
    • Maheshwari, R.1    Levenson, E.A.2    Kiick, K.L.3
  • 82
    • 0030732896 scopus 로고    scopus 로고
    • Oligosaccharide-derivatized dendrimers: Defined multivalent inhibitors of the adherence of the cholera toxin B subunit and the heat labile enterotoxin of E
    • Thompson, J.P.; Schengrund, C.-L. Oligosaccharide-derivatized dendrimers: Defined multivalent inhibitors of the adherence of the cholera toxin B subunit and the heat labile enterotoxin of E. coli to GM1. Glycoconjugate J. 1997, 14, 837-845.
    • (1997) coli to GM1. Glycoconjugate J. , vol.14 , pp. 837-845
    • Thompson, J.P.1    Schengrund, C.-L.2
  • 85
    • 0036816147 scopus 로고    scopus 로고
    • Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharidemediated cellular interactions
    • Brewer, C.F.; Miceli, M.C.; Baum, L.G. Clusters, bundles, arrays and lattices: Novel mechanisms for lectin-saccharidemediated cellular interactions. Curr. Opin. Struct. Biol., 2002, 12, 616-623.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 616-623
    • Brewer, C.F.1    Miceli, M.C.2    Baum, L.G.3
  • 86
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks, W.P. On the attribution and additivity of binding energies. Proc. Natl. Acad. Sci. USA, 1981, 78, 4046-4050.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4046-4050
    • Jencks, W.P.1
  • 87
    • 0347694971 scopus 로고    scopus 로고
    • On the nature of the multivalency effect: A thermodynamic model
    • Kitov, P.I.; Bundle, D.R. On the nature of the multivalency effect: A thermodynamic model. J. Am. Chem. Soc., 2003, 125, 16271-16284.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16271-16284
    • Kitov, P.I.1    Bundle, D.R.2
  • 88
    • 0036462602 scopus 로고    scopus 로고
    • The cluster glycoside effect
    • Lundquist, J.J.; Toone, E.J. The cluster glycoside effect. Chem. Rev., 2002, 102, 555-578.
    • (2002) Chem. Rev. , vol.102 , pp. 555-578
    • Lundquist, J.J.1    Toone, E.J.2
  • 89
    • 0032476812 scopus 로고    scopus 로고
    • Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors
    • Mammen, M.; Chio, S.-K.; Whitesides, G.M. Polyvalent interactions in biological systems: Implications for design and use of multivalent ligands and inhibitors. Angew. Chem., Int. Ed., 1998, 37, 2755-2794.
    • (1998) Angew. Chem., Int. Ed. , vol.37 , pp. 2755-2794
    • Mammen, M.1    Chio, S.-K.2    Whitesides, G.M.3
  • 90
    • 0032169625 scopus 로고    scopus 로고
    • Inhibition of the adherence of cholera toxin and the heat-labile enterotoxin of escherichia coli to cell-surface GM1 by oligosaccharide-derivatized dendrimers
    • Thompson, J.P.; Schengrund, C.-L. Inhibition of the adherence of cholera toxin and the heat-labile enterotoxin of escherichia coli to cell-surface GM1 by oligosaccharide-derivatized dendrimers. Biochem. Pharmacol., 1998, 56, 591-597.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 591-597
    • Thompson, J.P.1    Schengrund, C.-L.2
  • 92
    • 0037032293 scopus 로고    scopus 로고
    • Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin
    • Zhang, Z.; Merritt, E.A.; Ahn, M.; Roach, C.; Hou, Z.; Verlinde, C.L.M.J.; Hol, W.G.J.; Fan, E. Solution and crystallographic studies of branched multivalent ligands that inhibit the receptor-binding of cholera toxin. J. Am. Chem. Soc., 2002, 124, 12991-12998.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12991-12998
    • Zhang, Z.1    Merritt, E.A.2    Ahn, M.3    Roach, C.4    Hou, Z.5    Verlinde, C.L.M.J.6    Hol, W.G.J.7    Fan, E.8
  • 93
    • 0037205935 scopus 로고    scopus 로고
    • Characterization and crystal structure of a highaffinity pentavalent receptor-binding inhibitor for cholera toxin and E
    • Merritt, E.A.; Zhang, Z.; Pickens, J.C.; Ahn, M.; Hol, W.G.J.; Fan, E. Characterization and crystal structure of a highaffinity pentavalent receptor-binding inhibitor for cholera toxin and E. coli heat-labile enterotoxin. J. Am. Chem. Soc., 2002, 124, 8818-8824.
    • (2002) coli heat-labile enterotoxin. J. Am. Chem. Soc. , vol.124 , pp. 8818-8824
    • Merritt, E.A.1    Zhang, Z.2    Pickens, J.C.3    Ahn, M.4    Hol, W.G.J.5    Fan, E.6
  • 94
    • 2442547627 scopus 로고    scopus 로고
    • Solution- and solid-phase syntheses of guanidine-bridged, water-soluble linkers for multivalent ligand design
    • Zhang, Z.; Pickens, J.C.; Hol, W.G.J.; Fan, E. Solution- and solid-phase syntheses of guanidine-bridged, water-soluble linkers for multivalent ligand design. Org. Lett., 2004, 6, 1377-1380.
    • (2004) Org. Lett. , vol.6 , pp. 1377-1380
    • Zhang, Z.1    Pickens, J.C.2    Hol, W.G.J.3    Fan, E.4
  • 99
    • 4644262461 scopus 로고    scopus 로고
    • Nonspanning bivalent ligands as improved surface receptor binding inhibitors of the cholera toxin B pentamer
    • Pickens, J.C.; Mitchell, D.D.; Liu, J.; Tan, X.; Zhang, Z.; Verlinde, C.L.M.J.; Hol, W.G.J.; Fan, E. Nonspanning bivalent ligands as improved surface receptor binding inhibitors of the cholera toxin B pentamer. Chem. Biol., 2004, 11, 1205-1215.
    • (2004) Chem. Biol. , vol.11 , pp. 1205-1215
    • Pickens, J.C.1    Mitchell, D.D.2    Liu, J.3    Tan, X.4    Zhang, Z.5    Verlinde, C.L.M.J.6    Hol, W.G.J.7    Fan, E.8
  • 100
    • 13944283259 scopus 로고    scopus 로고
    • Protein heterodimerization through ligand-bridged multivalent pre-organization: Enhancing ligand binding toward both protein targets
    • Liu, J.; Zhang, Z.; Tan, X.; Hol, W.G.J.; Verlinde, C.L.M.J.; Fan, E. Protein heterodimerization through ligand-bridged multivalent pre-organization: Enhancing ligand binding toward both protein targets. J. Am. Chem. Soc., 2005, 127, 2044-2045.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 2044-2045
    • Liu, J.1    Zhang, Z.2    Tan, X.3    Hol, W.G.J.4    Verlinde, C.L.M.J.5    Fan, E.6


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