메뉴 건너뛰기




Volumn 2, Issue 7, 2010, Pages 1612-1645

AB toxins: A paradigm switch from deadly to desirable

Author keywords

AB toxins; Adjuvants; Enterotoxins; Immunomodulation; Plants; Ricin; Vaccines

Indexed keywords

ANTHRAX TOXIN; ANTHRAX VACCINE; BACTERIAL TOXIN; CHOLERA TOXIN; CHOLERA VACCINE; ESCHERICHIA COLI ENTEROTOXIN; ESCHERICHIA COLI VACCINE; INFLUENZA VACCINE; PERTUSSIS TOXIN; PERTUSSIS VACCINE; PLANT TOXIN; RECOMBINANT VACCINE; RICIN; SHIGA TOXIN; VEROTOXIN;

EID: 79952078677     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins2071612     Document Type: Review
Times cited : (76)

References (201)
  • 1
    • 0014544827 scopus 로고
    • Pathogenesis of experimental cholera. Preparation and isolation of choleragen and choleragenoid
    • Finkelstein, R.A.; LoSpalluto,J.J. Pathogenesis of experimental cholera. Preparation and isolation of choleragen and choleragenoid. J. Exp. Med. 1969, 130, 185-202.
    • (1969) J. Exp. Med , vol.130 , pp. 185-202
    • Finkelstein, R.A.1    Lospalluto, J.J.2
  • 2
    • 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
  • 3
    • 0016794107 scopus 로고
    • Studies of the subunit structure of choleragen
    • Sattler, J.; Wiegandt, H. Studies of the subunit structure of choleragen. Eur. J. Biochem. 1975, 57, 309-316.
    • (1975) Eur. J. Biochem , vol.57 , pp. 309-316
    • Sattler, J.1    Wiegandt, H.2
  • 4
    • 0027174854 scopus 로고
    • Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin
    • Sixma, T.K.; Kalk, K.H.; van Zanten, B.A.; Dauter, Z.; Kingma, J.; Witholt, B.; Hol, W.G. Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. J. Mol. Biol. 1993, 230, 890-918.
    • (1993) J. Mol. Biol , vol.230 , pp. 890-918
    • Sixma, T.K.1    Kalk, K.H.2    van Zanten, B.A.3    Dauter, Z.4    Kingma, J.5    Witholt, B.6    Hol, W.G.7
  • 5
    • 0029644933 scopus 로고
    • Surprising leads for a cholera toxin receptor-binding antagonist: Crystallographic studies of CTB mutants
    • Merritt, E.A.; Sarfaty, S.; Chang, T.T.; Palmer, L.M.; Jobling, M.G.; Holmes, R.K.; Hol, W.G. Surprising leads for a cholera toxin receptor-binding antagonist: crystallographic studies of CTB mutants. Structure 1995, 3, 561-570.
    • (1995) Structure , vol.3 , pp. 561-570
    • Merritt, E.A.1    Sarfaty, S.2    Chang, T.T.3    Palmer, L.M.4    Jobling, M.G.5    Holmes, R.K.6    Hol, W.G.7
  • 6
    • 0015819081 scopus 로고
    • Tissue receptor for cholera exotoxin: Postulated structure from studies with GM1 ganglioside and related glycolipids
    • Holmgren, J.; Lonnroth, I.; Svennerholm, L. Tissue receptor for cholera exotoxin: postulated structure from studies with GM1 ganglioside and related glycolipids. Infect. Immun. 1973, 8, 208-214.
    • (1973) Infect. Immun , vol.8 , pp. 208-214
    • Holmgren, J.1    Lonnroth, I.2    Svennerholm, L.3
  • 7
  • 8
    • 0016915398 scopus 로고
    • The role of gangliosides in the action of cholera toxin
    • van Heyningen, W.E.; King, C.A. The role of gangliosides in the action of cholera toxin. Adv. Exp. Med. Biol. 1976, 71, 205-214.
    • (1976) Adv. Exp. Med. Biol , vol.71 , pp. 205-214
    • van Heyningen, W.E.1    King, C.A.2
  • 9
    • 0017274636 scopus 로고
    • The subunits of cholera toxin: Structure, stoichiometry, and function
    • van Heyningen, S. The subunits of cholera toxin: structure, stoichiometry, and function. J. Infect. Dis. 1976, 133 Suppl, 5-13.
    • (1976) J. Infect. Dis , vol.133 , Issue.Suppl. , pp. 5-13
    • Van Heyningen, S.1
  • 10
    • 0015970615 scopus 로고
    • Interaction of cholera toxin and toxin derivatives with lymphocytes. I. Binding properties and interference with lectin-induced cellular stimulation
    • Holmgren, J.; Lindholm, L.; Lonnroth, I. Interaction of cholera toxin and toxin derivatives with lymphocytes. I. Binding properties and interference with lectin-induced cellular stimulation. J. Exp. Med. 1974, 139, 801-819.
    • (1974) J. Exp. Med , vol.139 , pp. 801-819
    • Holmgren, J.1    Lindholm, L.2    Lonnroth, I.3
  • 11
    • 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
  • 12
    • 33846190237 scopus 로고    scopus 로고
    • Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids
    • Camberg, J.L.; Johnson, T.L.; Patrick, M.; Abendroth, J.; Hol, W.G.; Sandkvist, M. Synergistic stimulation of EpsE ATP hydrolysis by EpsL and acidic phospholipids. EMBO J. 2007, 26, 19-27.
    • (2007) EMBO J , vol.26 , pp. 19-27
    • Camberg, J.L.1    Johnson, T.L.2    Patrick, M.3    Abendroth, J.4    Hol, W.G.5    Sandkvist, M.6
  • 13
    • 11144271157 scopus 로고    scopus 로고
    • Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE
    • Camberg, J.L.; Sandkvist, M. Molecular analysis of the Vibrio cholerae type II secretion ATPase EpsE. J. Bacteriol. 2005, 187, 249-256.
    • (2005) J. Bacteriol , vol.187 , pp. 249-256
    • Camberg, J.L.1    Sandkvist, M.2
  • 14
    • 0034646722 scopus 로고    scopus 로고
    • Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXphi
    • Davis, B.M.; Lawson, E.H.; Sandkvist, M.; Ali, A.; Sozhamannan, S.; Waldor, M.K. Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXphi. Science 2000, 288, 333-335.
    • (2000) Science , vol.288 , pp. 333-335
    • davis, B.M.1    Lawson, E.H.2    Sandkvist, M.3    Ali, A.4    Sozhamannan, S.5    Waldor, M.K.6
  • 15
    • 0021749239 scopus 로고
    • Mechanism of toxin secretion by Vibrio cholerae investigated in strains harboring plasmids that encode heat-labile enterotoxins of Escherichia coli
    • USA
    • Hirst, T.R.; Sanchez, J.; Kaper, J.B.; Hardy, S.J.; Holmgren, J. Mechanism of toxin secretion by Vibrio cholerae investigated in strains harboring plasmids that encode heat-labile enterotoxins of Escherichia coli. Proc. Natl. Acad. Sci. USA 1984, 81, 7752-7756.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7752-7756
    • Hirst, T.R.1    Sanchez, J.2    Kaper, J.B.3    Hardy, S.J.4    Holmgren, J.5
  • 16
    • 0002588630 scopus 로고
    • Coordinated assembly of multisubunit proteins: Oligomerization of bacterial enterotoxins in vivo and in vitro
    • Hardy, S.J.; Holmgren, J.; Johansson, S.; Sanchez, J.; Hirst, T.R. Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro. Proc. Natl. Acad. Sci. USA 1988, 85, 7109-7113.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7109-7113
    • Hardy, S.J.1    Holmgren, J.2    Johansson, S.3    Sanchez, J.4    Hirst, T.R.5
  • 18
    • 0036181920 scopus 로고    scopus 로고
    • Mutational analysis of ganglioside GM(1)-binding ability, pentamer formation, and epitopes of cholera toxin B (CTB) subunits and CTB/heat-labile enterotoxin B subunit chimeras
    • Jobling, M.G.; Holmes, R.K. Mutational analysis of ganglioside GM(1)-binding ability, pentamer formation, and epitopes of cholera toxin B (CTB) subunits and CTB/heat-labile enterotoxin B subunit chimeras. Infect. Immun. 2002, 70, 1260-1271.
    • (2002) Infect. Immun , vol.70 , pp. 1260-1271
    • Jobling, M.G.1    Holmes, R.K.2
  • 20
    • 33845614097 scopus 로고    scopus 로고
    • Rafting with cholera toxin: Endocytosis and trafficking from plasma membrane to ER
    • Chinnapen, D.J.; Chinnapen, H.; Saslowsky, D.; Lencer, W.I. Rafting with cholera toxin: Endocytosis and trafficking from plasma membrane to ER. FEMS Microbiol. Lett. 2007, 266, 129-137.
    • (2007) FEMS Microbiol. Lett , vol.266 , pp. 129-137
    • Chinnapen, D.J.1    Chinnapen, H.2    Saslowsky, D.3    Lencer, W.I.4
  • 21
    • 3343011405 scopus 로고    scopus 로고
    • Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent Endocytic pathways
    • Massol, R.H.; Larsen, J.E.; Fujinaga, Y.; Lencer, W.I.; Kirchhausen, T. Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent Endocytic pathways. Mol. Biol. Cell. 2004, 15, 3631-3641.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3631-3641
    • Massol, R.H.1    Larsen, J.E.2    Fujinaga, Y.3    Lencer, W.I.4    Kirchhausen, T.5
  • 22
    • 0037010141 scopus 로고    scopus 로고
    • Transport of protein toxins into cells: Pathways used by ricin, cholera toxin and Shiga toxin
    • Sandvig, K.; van Deurs, B. Transport of protein toxins into cells: pathways used by ricin, cholera toxin and Shiga toxin. FEBS Lett. 2002, 529, 49-53.
    • (2002) FEBS Lett , vol.529 , pp. 49-53
    • Sandvig, K.1    Van Deurs, B.2
  • 23
    • 33746758880 scopus 로고    scopus 로고
    • Retrograde transport pathways utilised by viruses and protein toxins
    • Spooner, R.A.; Smith, D.C.; Easton, A.J.; Roberts, L.M.; Lord, J.M. Retrograde transport pathways utilised by viruses and protein toxins. Virol. J. 2006, 3, 26.
    • (2006) Virol. J , vol.3 , pp. 26
    • Spooner, R.A.1    Smith, D.C.2    Easton, A.J.3    Roberts, L.M.4    Lord, J.M.5
  • 24
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human ARF6-GTP
    • O'Neal, C.J.; Jobling, M.G.; Holmes, R.K.; Hol, W.G. Structural basis for the activation of cholera toxin by human ARF6-GTP. Science 2005, 309, 1093-1096.
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.G.4
  • 25
    • 1842289249 scopus 로고    scopus 로고
    • Role of receptor binding in toxicity, immunogenicity, and adjuvanticity of Escherichia coli heat-labile enterotoxin
    • Guidry, J.J.; Cardenas, L.; Cheng, E.; Clements, J.D. Role of receptor binding in toxicity, immunogenicity, and adjuvanticity of Escherichia coli heat-labile enterotoxin. Infect. Immun. 1997, 65, 4943-4950.
    • (1997) Infect. Immun , vol.65 , pp. 4943-4950
    • Guidry, J.J.1    Cardenas, L.2    Cheng, E.3    Clements, J.D.4
  • 26
    • 0031741198 scopus 로고    scopus 로고
    • Intranasal immunization with cytotoxic T-lymphocyte epitope peptide and mucosal adjuvant cholera toxin: Selective augmentation of peptide-presenting dendritic cells in nasal mucosa-associated lymphoid tissue
    • Porgador, A.; Staats, H.F.; Itoh, Y.; Kelsall, B.L. Intranasal immunization with cytotoxic T-lymphocyte epitope peptide and mucosal adjuvant cholera toxin: selective augmentation of peptide-presenting dendritic cells in nasal mucosa-associated lymphoid tissue. Infect. Immun. 1998, 66, 5876-5881.
    • (1998) Infect. Immun , vol.66 , pp. 5876-5881
    • Porgador, A.1    Staats, H.F.2    Itoh, Y.3    Kelsall, B.L.4
  • 27
    • 0028007467 scopus 로고
    • Cholera toxin B subunit: An efficient transmucosal carrier-delivery system for induction of peripheral immunological tolerance
    • Sun, J.B.; Holmgren, J.; Czerkinsky, C. Cholera toxin B subunit: an efficient transmucosal carrier-delivery system for induction of peripheral immunological tolerance. Proc. Natl. Acad. Sci. USA 1994, 91, 10795-10799.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10795-10799
    • Sun, J.B.1    Holmgren, J.2    Czerkinsky, C.3
  • 28
    • 0029983190 scopus 로고    scopus 로고
    • Cholera toxin B subunit as transmucosal carrier-delivery and immunomodulating system for induction of antiinfectious and antipathological immunity
    • Czerkinsky, C.; Sun, J.B.; Lebens, M.; Li, B.L.; Rask, C.; Lindblad, M.; Holmgren, J. Cholera toxin B subunit as transmucosal carrier-delivery and immunomodulating system for induction of antiinfectious and antipathological immunity. Ann. N. Y. Acad. Sci. 1996, 778, 185-193.
    • (1996) Ann. N. Y. Acad. Sci , vol.778 , pp. 185-193
    • Czerkinsky, C.1    Sun, J.B.2    Lebens, M.3    Li, B.L.4    Rask, C.5    Lindblad, M.6    Holmgren, J.7
  • 29
    • 0033815173 scopus 로고    scopus 로고
    • Oral administration of cholera toxin B subunit conjugated to myelin basic protein protects against experimental autoimmune encephalomyelitis by inducing transforming growth factor-beta- secreting cells and suppressing chemokine expression
    • Sun, J.B.; Xiao, B.G.; Lindblad, M.; Li, B.L.; Link, H.; Czerkinsky, C.; Holmgren, J. Oral administration of cholera toxin B subunit conjugated to myelin basic protein protects against experimental autoimmune encephalomyelitis by inducing transforming growth factor-beta- secreting cells and suppressing chemokine expression. Int. Immunol. 2000, 12, 1449-1457.
    • (2000) Int. Immunol , vol.12 , pp. 1449-1457
    • Sun, J.B.1    Xiao, B.G.2    Lindblad, M.3    Li, B.L.4    Link, H.5    Czerkinsky, C.6    Holmgren, J.7
  • 30
    • 0036774999 scopus 로고    scopus 로고
    • Recent advances in mucosal vaccines and adjuvants
    • Eriksson, K.; Holmgren, J. Recent advances in mucosal vaccines and adjuvants. Curr. Opin. Immunol. 2002, 14, 666-672.
    • (2002) Curr. Opin. Immunol , vol.14 , pp. 666-672
    • Eriksson, K.1    Holmgren, J.2
  • 32
    • 0034873558 scopus 로고    scopus 로고
    • Cholera toxin B subunit as a carrier molecule promotes antigen presentation and increases CD40 and CD86 expression on antigen-presenting cells
    • George-Chandy, A.; Eriksson, K.; Lebens, M.; Nordstrom, I.; Schon, E.; Holmgren, J. Cholera toxin B subunit as a carrier molecule promotes antigen presentation and increases CD40 and CD86 expression on antigen-presenting cells. Infect. Immun. 2001, 69, 5716-5725.
    • (2001) Infect. Immun , vol.69 , pp. 5716-5725
    • George-Chandy, A.1    Eriksson, K.2    Lebens, M.3    Nordstrom, I.4    Schon, E.5    Holmgren, J.6
  • 33
    • 50849121427 scopus 로고    scopus 로고
    • Cholera toxin B subunit promotes the induction of regulatory T cells by preventing human dendritic cell maturation
    • D'Ambrosio, A.; Colucci, M.; Pugliese, O.; Quintieri, F.; Boirivant, M. Cholera toxin B subunit promotes the induction of regulatory T cells by preventing human dendritic cell maturation. J. Leukoc. Biol. 2008, 84, 661-668.
    • (2008) J. Leukoc. Biol , vol.84 , pp. 661-668
    • D'ambrosio, A.1    Colucci, M.2    Pugliese, O.3    Quintieri, F.4    Boirivant, M.5
  • 34
    • 0034939162 scopus 로고    scopus 로고
    • Oral administration of collagen conjugated with cholera toxin induces tolerance to type II collagen and suppresses chondritis in an animal model of autoimmune ear disease
    • Kim, N.; Cheng, K.C.; Kwon, S.S.; Mora, R.; Barbieri, M.; Yoo, T.J. Oral administration of collagen conjugated with cholera toxin induces tolerance to type II collagen and suppresses chondritis in an animal model of autoimmune ear disease. Ann. Otol. Rhinol. Laryngol. 2001, 110, 646-654.
    • (2001) Ann. Otol. Rhinol. Laryngol , vol.110 , pp. 646-654
    • Kim, N.1    Cheng, K.C.2    Kwon, S.S.3    Mora, R.4    Barbieri, M.5    Yoo, T.J.6
  • 37
    • 0031762753 scopus 로고    scopus 로고
    • A plant-based cholera toxin B subunit-insulin fusion protein protects against the development of autoimmune diabetes
    • Arakawa, T.; Yu, J.; Chong, D.K.; Hough, J.; Engen, P.C.;Langridge, W.H. A plant-based cholera toxin B subunit-insulin fusion protein protects against the development of autoimmune diabetes. Nat. Biotechnol. 1998, 16, 934-938.
    • (1998) Nat. Biotechnol , vol.16 , pp. 934-938
    • Arakawa, T.1    Yu, J.2    Chong, D.K.3    Hough, J.4    Engen, P.C.5    Langridge, W.H.6
  • 38
    • 0036408394 scopus 로고    scopus 로고
    • Nasal administration of CTB-insulin induces active tolerance against autoimmune diabetes in non-obese diabetic (NOD) mice
    • Aspord, C.; Thivolet, C. Nasal administration of CTB-insulin induces active tolerance against autoimmune diabetes in non-obese diabetic (NOD) mice. Clin. Exp. Immunol. 2002, 130, 204-211.
    • (2002) Clin. Exp. Immunol , vol.130 , pp. 204-211
    • Aspord, C.1    Thivolet, C.2
  • 39
    • 0035862336 scopus 로고    scopus 로고
    • Differentiation of T regulatory cells by immature dendritic cells
    • Roncarolo, M.G.; Levings, M.K.; Traversari, C. Differentiation of T regulatory cells by immature dendritic cells. J. Exp. Med. 2001, 193, F5-F9.
    • (2001) J. Exp. Med , vol.193
    • Roncarolo, M.G.1    Levings, M.K.2    Traversari, C.3
  • 40
    • 0031935290 scopus 로고    scopus 로고
    • Efficacy of a food plant-based oral cholera toxin B subunit vaccine
    • Arakawa, T.; Chong, D.K.; Langridge, W.H. Efficacy of a food plant-based oral cholera toxin B subunit vaccine. Nat. Biotechnol. 1998, 16, 292-297.
    • (1998) Nat. Biotechnol , vol.16 , pp. 292-297
    • Arakawa, T.1    Chong, D.K.2    Langridge, W.H.3
  • 42
  • 43
    • 0042430426 scopus 로고    scopus 로고
    • Cholera toxin promotes the induction of regulatory T cells specific for bystander antigens by modulating dendritic cell activation
    • Lavelle, E.C.; McNeela, E.; Armstrong, M.E.; Leavy, O.; Higgins, S.C.; Mills, K.H. Cholera toxin promotes the induction of regulatory T cells specific for bystander antigens by modulating dendritic cell activation. J. Immunol. 2003, 171, 2384-2392.
    • (2003) J. Immunol , vol.171 , pp. 2384-2392
    • Lavelle, E.C.1    McNeela, E.2    Armstrong, M.E.3    Leavy, O.4    Higgins, S.C.5    Mills, K.H.6
  • 44
    • 14644407495 scopus 로고    scopus 로고
    • Recombinant cholera toxin B subunit activates dendritic cells and enhances antitumor immunity
    • Isomura, I.; Yasuda, Y.; Tsujimura, K.; Takahashi, T.; Tochikubo, K.; Morita, A. Recombinant cholera toxin B subunit activates dendritic cells and enhances antitumor immunity. Microbiol. Immunol. 2005, 49, 79-87.
    • (2005) Microbiol. Immunol , vol.49 , pp. 79-87
    • Isomura, I.1    Yasuda, Y.2    Tsujimura, K.3    Takahashi, T.4    Tochikubo, K.5    Morita, A.6
  • 45
    • 0032758223 scopus 로고    scopus 로고
    • Oral administration of cholera toxin B-insulin conjugates protects NOD mice from autoimmune diabetes by inducing CD4+ regulatory T-cells
    • Ploix, C.; Bergerot, I.; Durand, A.; Czerkinsky, C.; Holmgren, J.; Thivolet, C. Oral administration of cholera toxin B-insulin conjugates protects NOD mice from autoimmune diabetes by inducing CD4+ regulatory T-cells. Diabetes 1999, 48, 2150-2156.
    • (1999) Diabetes , vol.48 , pp. 2150-2156
    • Ploix, C.1    Bergerot, I.2    Durand, A.3    Czerkinsky, C.4    Holmgren, J.5    Thivolet, C.6
  • 46
    • 72349096793 scopus 로고    scopus 로고
    • Mucosally induced immunological tolerance, regulatory T cells and the adjuvant effect by cholera toxin B subunit
    • Sun, J.B.; Czerkinsky, C.; Holmgren, J. Mucosally induced immunological tolerance, regulatory T cells and the adjuvant effect by cholera toxin B subunit. Scand. J. Immunol. 2010, 71,1-11.
    • (2010) Scand. J. Immunol , vol.71 , pp. 1-11
    • Sun, J.B.1    Czerkinsky, C.2    Holmgren, J.3
  • 50
    • 36049042664 scopus 로고    scopus 로고
    • Deletion mutations in N-terminal alpha1 helix render heat labile enterotoxin B subunit susceptible to degradation
    • USA
    • Alone, P.V.; Malik, G.; Krishnan, A.; Garg, L.C. Deletion mutations in N-terminal alpha1 helix render heat labile enterotoxin B subunit susceptible to degradation. Proc. Natl. Acad. Sci. USA 2007, 104, 16056-16061.
    • (2007) Proc. Natl. Acad. Sci , vol.104 , pp. 16056-16061
    • Alone, P.V.1    Malik, G.2    Krishnan, A.3    Garg, L.C.4
  • 51
    • 53649107423 scopus 로고    scopus 로고
    • Secretory and GM1 receptor binding role of N-terminal region of LTB in Vibrio cholerae
    • Alone, P.V.; Garg, L.C. Secretory and GM1 receptor binding role of N-terminal region of LTB in Vibrio cholerae. Biochem. Biophys. Res. Commun. 2008, 376, 770-774.
    • (2008) Biochem. Biophys. Res. Commun , vol.376 , pp. 770-774
    • Alone, P.V.1    Garg, L.C.2
  • 52
    • 33845988064 scopus 로고    scopus 로고
    • Inhibition of Escherichia coli heat-labile enterotoxin B subunit pentamer (EtxB5) assembly in vitro using monoclonal antibodies
    • Chung, W.Y.; Carter, R.; Hardy, T.; Sack, M.; Hirst, T.R.; James, R.F. Inhibition of Escherichia coli heat-labile enterotoxin B subunit pentamer (EtxB5) assembly in vitro using monoclonal antibodies. J. Biol. Chem. 2006, 281, 39465-39470.
    • (2006) J. Biol. Chem , vol.281 , pp. 39465-39470
    • Chung, W.Y.1    Carter, R.2    Hardy, T.3    Sack, M.4    Hirst, T.R.5    James, R.F.6
  • 53
    • 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
  • 54
    • 0026598947 scopus 로고
    • Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography
    • Sixma, T.K.; Pronk, S.E.; Kalk, K.H.; van Zanten, B.A.; Berghuis, A.M.; Hol, W.G. Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature 1992, 355, 561-564.
    • (1992) Nature , vol.355 , pp. 561-564
    • Sixma, T.K.1    Pronk, S.E.2    Kalk, K.H.3    van Zanten, B.A.4    Berghuis, A.M.5    Hol, W.G.6
  • 55
    • 0030294870 scopus 로고    scopus 로고
    • Unexpected carbohydrate cross-binding by Escherichia coli heat-labile enterotoxin. Recognition of human and rabbit target cell glycoconjugates in comparison with cholera toxin
    • Karlsson, K.A.; Teneberg, S.; Angstrom, J.; Kjellberg, A.; Hirst, T.R.; Berstrom, J.; Miller-Podraza, H. Unexpected carbohydrate cross-binding by Escherichia coli heat-labile enterotoxin. Recognition of human and rabbit target cell glycoconjugates in comparison with cholera toxin. Bioorg. Med. Chem. 1996, 4, 1919-1928.
    • (1996) Bioorg. Med. Chem , vol.4 , pp. 1919-1928
    • Karlsson, K.A.1    Teneberg, S.2    Angstrom, J.3    Kjellberg, A.4    Hirst, T.R.5    Berstrom, J.6    Miller-Podraza, H.7
  • 56
    • 0019868369 scopus 로고
    • Interaction of cholera toxin with rat intestinal brush border membranes. Relative roles of gangliosides and galactoproteins as toxin receptors
    • Critchley, D.R.; Magnani, J.L.; Fishman, P.H. Interaction of cholera toxin with rat intestinal brush border membranes. Relative roles of gangliosides and galactoproteins as toxin receptors. J. Biol. Chem. 1981, 256, 8724-8731.
    • (1981) J. Biol. Chem , vol.256 , pp. 8724-8731
    • Critchley, D.R.1    Magnani, J.L.2    Fishman, P.H.3
  • 57
    • 0027959631 scopus 로고
    • The heat-labile enterotoxin of Escherichia coli binds to polylactosaminoglycan-containing receptors in CaCo-2 human intestinal epithelial cells
    • Orlandi, P.A.; Critchley, D.R.; Fishman, P.H. The heat-labile enterotoxin of Escherichia coli binds to polylactosaminoglycan-containing receptors in CaCo-2 human intestinal epithelial cells. Biochemistry 1994, 33, 12886-12895.
    • (1994) Biochemistry , vol.33 , pp. 12886-12895
    • Orlandi, P.A.1    Critchley, D.R.2    Fishman, P.H.3
  • 58
    • 0023916532 scopus 로고
    • Comparison of the carbohydrate-binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxins LTh-I, LT-IIa, and LT-IIb
    • Fukuta, S.; Magnani, J.L.; Twiddy, E.M.; Holmes, R.K.; Ginsburg, V. Comparison of the carbohydrate-binding specificities of cholera toxin and Escherichia coli heat-labile enterotoxins LTh-I, LT-IIa, and LT-IIb. Infect. Immun. 1988, 56, 1748-1753.
    • (1988) Infect. Immun , vol.56 , pp. 1748-1753
    • Fukuta, S.1    Magnani, J.L.2    Twiddy, E.M.3    Holmes, R.K.4    Ginsburg, V.5
  • 60
    • 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. Mol. Biol. Rev. 1992, 56, 622-647.
    • (1992) Microbiol. Mol. Biol. Rev , vol.56 , pp. 622-647
    • Spangler, B.D.1
  • 61
    • 1342268107 scopus 로고    scopus 로고
    • Nasal vaccination, Escherichia coli enterotoxin, and Bell's palsy
    • Couch, R.B. Nasal vaccination, Escherichia coli enterotoxin, and Bell's palsy. N. Engl. J. Med. 2004, 350, 860-861.
    • (2004) N. Engl. J. Med , vol.350 , pp. 860-861
    • Couch, R.B.1
  • 62
    • 0034444401 scopus 로고    scopus 로고
    • Inhibition of T-cell response by Escherichia coli heat-labile enterotoxin-treated epithelial cells
    • Lopes, L.M.; Maroof, A.; Dougan, G.; Chain, B.M. Inhibition of T-cell response by Escherichia coli heat-labile enterotoxin-treated epithelial cells. Infect. Immun. 2000, 68, 6891-6895.
    • (2000) Infect. Immun , vol.68 , pp. 6891-6895
    • Lopes, L.M.1    Maroof, A.2    Dougan, G.3    Chain, B.M.4
  • 63
    • 65449133249 scopus 로고    scopus 로고
    • Cholera toxin and Escherichia coli heat-labile enterotoxin, but not their nontoxic counterparts, improve the antigen-presenting cell function of human B lymphocytes
    • Negri, D.R.; Pinto, D.; Vendetti, S.; Patrizio, M.; Sanchez, M.; Riccomi, A.; Ruggiero, P.; Del Giudice, G.; De Magistris, M.T. Cholera toxin and Escherichia coli heat-labile enterotoxin, but not their nontoxic counterparts, improve the antigen-presenting cell function of human B lymphocytes. Infect. Immun. 2009, 77, 1924-1935.
    • (2009) Infect. Immun , vol.77 , pp. 1924-1935
    • Negri, D.R.1    Pinto, D.2    Vendetti, S.3    Patrizio, M.4    Sanchez, M.5    Riccomi, A.6    Ruggiero, P.7    Del Giudice, G.8    de Magistris, M.T.9
  • 64
    • 7044245896 scopus 로고    scopus 로고
    • The type II heat-labile enterotoxins LT-IIa and LT-IIb and their respective B pentamers differentially induce and regulate cytokine production in human monocytic cells
    • Hajishengallis, G.; Nawar, H.; Tapping, R.I.; Russell, M.W.; Connell, T.D. The Type II heat-labile enterotoxins LT-IIa and LT-IIb and their respective B pentamers differentially induce and regulate cytokine production in human monocytic cells. Infect. Immun. 2004, 72, 6351-6358.
    • (2004) Infect. Immun , vol.72 , pp. 6351-6358
    • Hajishengallis, G.1    Nawar, H.2    Tapping, R.I.3    Russell, M.W.4    Connell, T.D.5
  • 65
    • 61449235221 scopus 로고    scopus 로고
    • Influence of the A and B subunits of cholera toxin (CT) and Escherichia coli toxin (LT) on TNFalpha release from macrophages
    • Domingos, M.O.; Andrade, R.G.; Barbaro, K.C.; Borges, M.M.; Lewis, D.J.; New, R.R. Influence of the A and B subunits of cholera toxin (CT) and Escherichia coli toxin (LT) on TNF-alpha release from macrophages. Toxicon 2009, 53, 570-577.
    • (2009) Toxicon , vol.53 , pp. 570-577
    • Domingos, M.O.1    Andrade, R.G.2    Barbaro, K.C.3    Borges, M.M.4    Lewis, D.J.5    New, R.R.6
  • 66
    • 77953131126 scopus 로고    scopus 로고
    • Enhanced antigen uptake by dendritic cells induced by the B pentamer of the type II heat-labile enterotoxin LT-IIa requires engagement of TLR2
    • Lee, C.H.; Nawar, H.F.; Mandell, L.; Liang, S.; Hajishengallis, G.; Connell, T.D. Enhanced antigen uptake by dendritic cells induced by the B pentamer of the type II heat-labile enterotoxin LT-IIa requires engagement of TLR2. Vaccine 2010, 28, 3696-3705.
    • (2010) Vaccine , vol.28 , pp. 3696-3705
    • Lee, C.H.1    Nawar, H.F.2    Mandell, L.3    Liang, S.4    Hajishengallis, G.5    Connell, T.D.6
  • 67
    • 67649518029 scopus 로고    scopus 로고
    • In vivo and in vitro adjuvant activities of the B subunit of Type IIb heat-labile enterotoxin (LT-IIb-B5) from Escherichia coli
    • Liang, S.; Hosur, K.B.; Nawar, H.F.; Russell, M.W.; Connell, T.D.; Hajishengallis, G. In vivo and in vitro adjuvant activities of the B subunit of Type IIb heat-labile enterotoxin (LT-IIb-B5) from Escherichia coli. Vaccine 2009, 27, 4302-4308.
    • (2009) Vaccine , vol.27 , pp. 4302-4308
    • Liang, S.1    Hosur, K.B.2    Nawar, H.F.3    Russell, M.W.4    Connell, T.D.5    Hajishengallis, G.6
  • 68
    • 44849126376 scopus 로고    scopus 로고
    • Cholera toxin, E coli heat-labile toxin, and non-toxic derivatives induce dendritic cell migration into the follicle-associated epithelium of Peyer's patches
    • Anosova, N.G.; Chabot, S.; Shreedhar, V.; Borawski, J.A.; Dickinson, B.L.; Neutra, M.R. Cholera toxin, E. coli heat-labile toxin, and non-toxic derivatives induce dendritic cell migration into the follicle-associated epithelium of Peyer's patches. Mucosal. Immunol. 2008, 1, 59-67.
    • (2008) Mucosal. Immunol , vol.1 , pp. 59-67
    • Anosova, N.G.1    Chabot, S.2    Shreedhar, V.3    Borawski, J.A.4    Dickinson, B.L.5    Neutra, M.R.6
  • 69
    • 72049128598 scopus 로고    scopus 로고
    • Safety and immunogenicity of an influenza vaccine A/H5N1 (A/Vietnam/1194/2004) when coadministered with a heat-labile enterotoxin (LT) adjuvant patch
    • Glenn, G.M.; Thomas, D.N.; Poffenberger, K.L.; Flyer, D.C.; Ellingsworth, L.R.; Andersen, B.H.; Frech, S.A. Safety and immunogenicity of an influenza vaccine A/H5N1 (A/Vietnam/1194/2004) when coadministered with a heat-labile enterotoxin (LT) adjuvant patch. Vaccine 2009, 27 (Suppl. 6), G60-G66.
    • (2009) Vaccine , vol.27 , Issue.SUPPL.6
    • Glenn, G.M.1    Thomas, D.N.2    Poffenberger, K.L.3    Flyer, D.C.4    Ellingsworth, L.R.5    Andersen, B.H.6    Frech, S.A.7
  • 70
    • 22944434537 scopus 로고    scopus 로고
    • Bacterial toxins: Potential weapons against HIV infection
    • Alfano, M.; Rizzi, C.; Corti, D.; Adduce, L.; Poli, G. Bacterial toxins: potential weapons against HIV infection. Curr. Pharm. Des. 2005, 11, 2909-2926.
    • (2005) Curr. Pharm. Des , vol.11 , pp. 2909-2926
    • Alfano, M.1    Rizzi, C.2    Corti, D.3    Adduce, L.4    Poli, G.5
  • 71
    • 67650467717 scopus 로고    scopus 로고
    • Therapeutic efficacy of a multi-epitope vaccine against Helicobacter pylori infection in BALB/c mice model
    • Zhou, W.Y.; Shi, Y.; Wu, C.; Zhang, W.J.; Mao, X.H.; Guo, G.; Li, H.X.; Zou, Q.M. Therapeutic efficacy of a multi-epitope vaccine against Helicobacter pylori infection in BALB/c mice model. Vaccine 2009, 27, 5013-5019.
    • (2009) Vaccine , vol.27 , pp. 5013-5019
    • Zhou, W.Y.1    Shi, Y.2    Wu, C.3    Zhang, W.J.4    Mao, X.H.5    Guo, G.6    Li, H.X.7    Zou, Q.M.8
  • 72
    • 36749040951 scopus 로고    scopus 로고
    • Vectors encoding carcinoembryonic antigen fused to the B subunit of heat-labile enterotoxin elicit antigen-specific immune responses and antitumor effects
    • Facciabene, A.; Aurisicchio, L.; Elia, L.; Palombo, F.; Mennuni, C.; Ciliberto, G.; La Monica, N. Vectors encoding carcinoembryonic antigen fused to the B subunit of heat-labile enterotoxin elicit antigen-specific immune responses and antitumor effects. Vaccine 2007, 26, 47-58.
    • (2007) Vaccine , vol.26 , pp. 47-58
    • Facciabene, A.1    Aurisicchio, L.2    Elia, L.3    Palombo, F.4    Mennuni, C.5    Ciliberto, G.6    la Monica, N.7
  • 73
    • 67849130968 scopus 로고    scopus 로고
    • Developing novel immunogens for a safe and effective Alzheimer's disease vaccine
    • Lemere, C.A. Developing novel immunogens for a safe and effective Alzheimer's disease vaccine. Prog. Brain Res. 2009, 175, 83-93.
    • (2009) Prog. Brain Res , vol.175 , pp. 83-93
    • Lemere, C.A.1
  • 74
    • 0034670024 scopus 로고    scopus 로고
    • Modulation of innate and acquired immune responses by Escherichia coli heat-labile toxin: Distinct pro- and antiinflammatory effects of the nontoxic AB complex and the enzyme activity
    • Ryan, E.J.; McNeela, E.; Pizza, M.; Rappuoli, R.; O'Neill, L.; Mills, K.H. Modulation of innate and acquired immune responses by Escherichia coli heat-labile toxin: distinct pro- and antiinflammatory effects of the nontoxic AB complex and the enzyme activity. J. Immunol. 2000, 165, 5750-5759.
    • (2000) J. Immunol , vol.165 , pp. 5750-5759
    • Ryan, E.J.1    McNeela, E.2    Pizza, M.3    Rappuoli, R.4    O'Neill, L.5    Mills, K.H.6
  • 76
    • 69249206886 scopus 로고    scopus 로고
    • Protective effect of a synapsin peptide genetically fused to the B subunit of Escherichia coli heat-labile enterotoxin in rat autoimmune encephalomyelitis
    • Scerbo, M.J.; Rupil, L.L.; Bibolini, M.J.; Roth, G.A.; Monferran, C.G. Protective effect of a synapsin peptide genetically fused to the B subunit of Escherichia coli heat-labile enterotoxin in rat autoimmune encephalomyelitis. J. Neurosci. Res. 2009, 87, 2273-2281.
    • (2009) J. Neurosci. Res , vol.87 , pp. 2273-2281
    • Scerbo, M.J.1    Rupil, L.L.2    Bibolini, M.J.3    Roth, G.A.4    Monferran, C.G.5
  • 77
    • 29644440579 scopus 로고    scopus 로고
    • Bacterial and plant enterotoxin B subunit-autoantigen fusion proteins suppress diabetes insulitis
    • Carter, J.E., III; Yu, J.; Choi, N.W.; Hough, J.; Henderson, D.; He, D.; Langridge, W.H. Bacterial and plant enterotoxin B subunit-autoantigen fusion proteins suppress diabetes insulitis. Mol. Biotechnol. 2006, 32, 1-15.
    • (2006) Mol. Biotechnol , vol.32 , pp. 1-15
    • Carter, J.E.1    Yu, J.2    Choi, N.W.3    Hough, J.4    Henderson, D.5    He, D.6    Langridge, W.H.7
  • 78
  • 79
    • 0036774095 scopus 로고    scopus 로고
    • A functional antigen in a practical crop: LT-B producing maize protects mice against Escherichia coli heat labile enterotoxin (LT) and cholera toxin (CT)
    • Chikwamba, R.; Cunnick, J.; Hathaway, D.; McMurray, J.; Mason, H.; Wang, K. A functional antigen in a practical crop: LT-B producing maize protects mice against Escherichia coli heat labile enterotoxin (LT) and cholera toxin (CT). Transgenic Res. 2002, 11, 479-493.
    • (2002) Transgenic Res , vol.11 , pp. 479-493
    • Chikwamba, R.1    Cunnick, J.2    Hathaway, D.3    McMurray, J.4    Mason, H.5    Wang, K.6
  • 80
    • 33751419198 scopus 로고    scopus 로고
    • Synthesis and assembly of Escherichia coli heat-labile enterotoxin B subunit in transgenic lettuce (Lactuca sativa)
    • Kim, T.G.; Kim, M.Y.; Kim, B.G.; Kang, T.J.; Kim, Y.S.; Jang, Y.S.; Arntzen, C.J.; Yang, M.S. Synthesis and assembly of Escherichia coli heat-labile enterotoxin B subunit in transgenic lettuce (Lactuca sativa). Protein Expr. Purif. 2007, 51, 22-27.
    • (2007) Protein Expr. Purif , vol.51 , pp. 22-27
    • Kim, T.G.1    Kim, M.Y.2    Kim, B.G.3    Kang, T.J.4    Kim, Y.S.5    Jang, Y.S.6    Arntzen, C.J.7    Yang, M.S.8
  • 81
    • 36949021571 scopus 로고    scopus 로고
    • Ingestion of transgenic carrots expressing the Escherichia coli heat-labile enterotoxin B subunit protects mice against cholera toxin challenge
    • Rosales-MEndoza, S.; Soria-Guerra, R.E.; Lopez-Revilla, R.; Moreno-Fierros, L.; Alpuche-Solis, A.G. Ingestion of transgenic carrots expressing the Escherichia coli heat-labile enterotoxin B subunit protects mice against cholera toxin challenge. Plant Cell Rep. 2008, 27, 79-84.
    • (2008) Plant Cell Rep , vol.27 , pp. 79-84
    • Rosales-Mendoza, S.1    Soria-Guerra, R.E.2    Lopez-Revilla, R.3    Moreno-Fierros, L.4    Alpuche-Solis, A.G.5
  • 82
    • 60349091875 scopus 로고    scopus 로고
    • Mucosal immunity in mice induced by orally administered transgenic rice
    • Zhang, X.; Yuan, Z.; Duan, Q.; Zhu, H.; Yu, H.; Wang, Q. Mucosal immunity in mice induced by orally administered transgenic rice. Vaccine 2009, 27, 1596-1600.
    • (2009) Vaccine , vol.27 , pp. 1596-1600
    • Zhang, X.1    Yuan, Z.2    Duan, Q.3    Zhu, H.4    Yu, H.5    Wang, Q.6
  • 83
  • 85
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins-from cell biology to biomedical applications
    • Johannes, L.; Romer, W. Shiga toxins-from cell biology to biomedical applications. Nat. Rev. Microbiol. 2010, 8, 105-116.
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 105-116
    • Johannes, L.1    Romer, W.2
  • 86
    • 0034877295 scopus 로고    scopus 로고
    • Shiga toxins
    • Sandvig, K. Shiga toxins. Toxicon 2001, 39, 1629-1635.
    • (2001) Toxicon , vol.39 , pp. 1629-1635
    • Sandvig, K.1
  • 87
    • 58849092225 scopus 로고    scopus 로고
    • Epigenetic control of T-helper-cell differentiation
    • Wilson, C.B.; Rowell, E.; Sekimata, M. Epigenetic control of T-helper-cell differentiation. Nat. Rev. Immunol. 2009, 9, 91-105.
    • (2009) Nat. Rev. Immunol , vol.9 , pp. 91-105
    • Wilson, C.B.1    Rowell, E.2    Sekimata, M.3
  • 88
    • 0029874043 scopus 로고    scopus 로고
    • Activation of Shiga-like toxins by mouse and human intestinal mucus correlates with virulence of enterohemorrhagic Escherichia coli O91:H21 isolates in orally infected, streptomycin-treated mice
    • Melton-Celsa, A.R.; Darnell, S.C.; O'Brien, A.D. Activation of Shiga-like toxins by mouse and human intestinal mucus correlates with virulence of enterohemorrhagic Escherichia coli O91:H21 isolates in orally infected, streptomycin-treated mice. Infect. Immun. 1996, 64, 1569-1576.
    • (1996) Infect. Immun , vol.64 , pp. 1569-1576
    • Melton-Celsa, A.R.1    Darnell, S.C.2    O'Brien, A.D.3
  • 89
    • 0028367338 scopus 로고
    • Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution
    • Fraser, M.E.; Chernaia, M.M.; Kozlov, Y.V.; James, M.N. Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution. Nat. Struct. Biol. 1994, 1, 59-64.
    • (1994) Nat. Struct. Biol , vol.1 , pp. 59-64
    • Fraser, M.E.1    Chernaia, M.M.2    Kozlov, Y.V.3    James, M.N.4
  • 90
    • 0034669117 scopus 로고    scopus 로고
    • Entry of ricin and Shiga toxin into cells: Molecular mechanisms and medical perspectives
    • Sandvig, K.; van Deurs, B. Entry of ricin and Shiga toxin into cells: molecular mechanisms and medical perspectives. EMBO J. 2000, 19, 5943-5950.
    • (2000) EMBO J , vol.19 , pp. 5943-5950
    • Sandvig, K.1    van Deurs, B.2
  • 92
    • 10744222365 scopus 로고    scopus 로고
    • The B subunit of Shiga toxin coupled to full-size antigenic protein elicits humoral and cell-mediated immune responses associated with a Th1-dominant polarization
    • Haicheur, N.; Benchetrit, F.; Amessou, M.; Leclerc, C.; Falguieres, T.; Fayolle, C.; Bismuth, E.; Fridman, W.H.; Johannes, L.; Tartour, E. The B subunit of Shiga toxin coupled to full-size antigenic protein elicits humoral and cell-mediated immune responses associated with a Th1-dominant polarization. Int. Immunol. 2003, 15, 1161-1171.
    • (2003) Int. Immunol , vol.15 , pp. 1161-1171
    • Haicheur, N.1    Benchetrit, F.2    Amessou, M.3    Leclerc, C.4    Falguieres, T.5    Fayolle, C.6    Bismuth, E.7    Fridman, W.H.8    Johannes, L.9    Tartour, E.10
  • 93
    • 21544452246 scopus 로고    scopus 로고
    • Nontoxic Shiga toxin derivatives from Escherichia coli possess adjuvant activity for the augmentation of antigen-specific immune responses via dendritic cell activation
    • Ohmura, M.; Yamamoto, M.; Tomiyama-Miyaji, C.; Yuki, Y.; Takeda, Y.; Kiyono, H. Nontoxic Shiga toxin derivatives from Escherichia coli possess adjuvant activity for the augmentation of antigen-specific immune responses via dendritic cell activation. Infect. Immun.2005, 73, 4088-4097.
    • (2005) Infect. Immun , vol.73 , pp. 4088-4097
    • Ohmura, M.1    Yamamoto, M.2    Tomiyama-Miyaji, C.3    Yuki, Y.4    Takeda, Y.5    Kiyono, H.6
  • 95
    • 70449527637 scopus 로고    scopus 로고
    • A recombinant hybrid peptide composed of AAF adhesin of enteroaggregative Escherichia coli and Shiga toxin B subunit elicits protective immune response in mice
    • Oloomi, M.; Bouzari, S.; Emami, S. A recombinant hybrid peptide composed of AAF adhesin of enteroaggregative Escherichia coli and Shiga toxin B subunit elicits protective immune response in mice. Eur. J. Clin. Microbiol. Infect. Dis. 2009, 28, 1311-1316.
    • (2009) Eur. J. Clin. Microbiol. Infect. Dis , vol.28 , pp. 1311-1316
    • Oloomi, M.1    Bouzari, S.2    Emami, S.3
  • 96
    • 0028181737 scopus 로고
    • Cytotoxicity of a shiga toxin A subunit-CD4 fusion protein to human immunodeficiency virus-infected cells
    • al-Jaufy, A.Y.; Haddad, J.E.; King, S.R.; McPhee, R.A.; Jackson, M.P. Cytotoxicity of a shiga toxin A subunit-CD4 fusion protein to human immunodeficiency virus-infected cells. Infect. Immun. 1994, 62, 956-960.
    • (1994) Infect. Immun , vol.62 , pp. 956-960
    • Al-Jaufy, A.Y.1    Haddad, J.E.2    King, S.R.3    McPhee, R.A.4    Jackson, M.P.5
  • 98
    • 42149089255 scopus 로고    scopus 로고
    • Retrograde transport of pertussis toxin in the mammalian cell
    • Plaut, R.D.; Carbonetti, N.H. Retrograde transport of pertussis toxin in the mammalian cell. Cell Microbiol. 2008, 10, 1130-1139.
    • (2008) Cell Microbiol , vol.10 , pp. 1130-1139
    • Plaut, R.D.1    Carbonetti, N.H.2
  • 99
    • 79952090567 scopus 로고
    • Jules Jean Baptiste Vincent Bordet. 1870-1961
    • Oakley, C.L. Jules Jean Baptiste Vincent Bordet. 1870-1961. Biogr. Mem. Fellows R. Soc. 1962, 19-25.
    • (1962) Biogr. Mem. Fellows RSoc , pp. 19-25
    • Oakley, C.L.1
  • 100
    • 80052662534 scopus 로고    scopus 로고
    • Center for Diseases Control and Prevention (CDC). Available online, Accessed on 21 June 2010
    • Center for Diseases Control and Prevention (CDC). Pertussis (Whooping Cough) Vaccination. Available online: http://www.cdc.gov/vaccines/vpd-vac/pertussis/default.htm (Accessed on 21 June 2010).
    • Pertussis (Whooping Cough) Vaccination
  • 101
    • 0036855441 scopus 로고    scopus 로고
    • Pertussis toxin and the adenylate cyclase toxin from Bordetella pertussis activate human monocyte-derived dendritic cells and dominantly inhibit cytokine production through a cAMP-dependent pathway
    • Bagley, K.C.; Abdelwahab, S.F.; Tuskan, R.G.; Fouts, T.R.; Lewis, G.K. Pertussis toxin and the adenylate cyclase toxin from Bordetella pertussis activate human monocyte-derived dendritic cells and dominantly inhibit cytokine production through a cAMP-dependent pathway. J. Leukoc. Biol. 2002, 72, 962-969.
    • (2002) J. Leukoc. Biol , vol.72 , pp. 962-969
    • Bagley, K.C.1    Abdelwahab, S.F.2    Tuskan, R.G.3    Fouts, T.R.4    Lewis, G.K.5
  • 102
    • 34249885064 scopus 로고    scopus 로고
    • Evading the proteasome: Absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation
    • Worthington, Z.E.; Carbonetti, N.H. Evading the proteasome: absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation. Infect. Immun. 2007, 75, 2946-2953.
    • (2007) Infect. Immun , vol.75 , pp. 2946-2953
    • Worthington, Z.E.1    Carbonetti, N.H.2
  • 103
    • 0027389529 scopus 로고
    • Binding of pertussis toxin to lipid vesicles containing glycolipids
    • Hausman, S.Z.; Burns, D.L. Binding of pertussis toxin to lipid vesicles containing glycolipids. Infect. Immun. 1993, 61, 335-337.
    • (1993) Infect. Immun , vol.61 , pp. 335-337
    • Hausman, S.Z.1    Burns, D.L.2
  • 104
    • 0030974747 scopus 로고    scopus 로고
    • Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a prerequisite for cellular intoxication
    • el Baya, A.; Linnemann, R.; von Olleschik-Elbheim, L.; Robenek, H.; Schmidt, M.A. Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a prerequisite for cellular intoxication. Eur. J. Cell Biol. 1997, 73, 40-48.
    • (1997) Eur. J. Cell Biol , vol.73 , pp. 40-48
    • El baya, A.1    Linnemann, R.2    von Olleschik-Elbheim, L.3    Robenek, H.4    Schmidt, M.A.5
  • 105
    • 0028905448 scopus 로고
    • Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism
    • Xu, Y.; Barbieri, J.T. Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism. Infect. Immun. 1995, 63, 825-832.
    • (1995) Infect. Immun , vol.63 , pp. 825-832
    • Xu, Y.1    Barbieri, J.T.2
  • 106
    • 33746035677 scopus 로고    scopus 로고
    • Induction of dendritic cell maturation by pertussis toxin and its B subunit differentially initiate Toll-like receptor 4-dependent signal transduction pathways
    • Wang, Z.Y.; Yang, D.; Chen, Q.; Leifer, C.A.; Segal, D.M.; Su, S.B.; Caspi, R.R.; Howard, Z.O.; Oppenheim, J.J. Induction of dendritic cell maturation by pertussis toxin and its B subunit differentially initiate Toll-like receptor 4-dependent signal transduction pathways. Exp. Hematol. 2006, 34, 1115-1124.
    • (2006) Exp. Hematol , vol.34 , pp. 1115-1124
    • Wang, Z.Y.1    Yang, D.2    Chen, Q.3    Leifer, C.A.4    Segal, D.M.5    Su, S.B.6    Caspi, R.R.7    Howard, Z.O.8    Oppenheim, J.J.9
  • 107
    • 33750803442 scopus 로고    scopus 로고
    • Pertussis toxin is superior to TLR ligands in enhancing pathogenic autoimmunity, targeted at a neo-self antigen, by triggering robust expansion of Th1 cells and their cytokine production
    • Fujimoto, C.; Yu, C.R.; Shi, G.; Vistica, B.P.; Wawrousek, E.F.; Klinman, D.M.; Chan, C.C.; Egwuagu, C.E.; Gery, I. Pertussis toxin is superior to TLR ligands in enhancing pathogenic autoimmunity, targeted at a neo-self antigen, by triggering robust expansion of Th1 cells and their cytokine production. J. Immunol. 2006, 177, 6896-6903.
    • (2006) J. Immunol , vol.177 , pp. 6896-6903
    • Fujimoto, C.1    Yu, C.R.2    Shi, G.3    Vistica, B.P.4    Wawrousek, E.F.5    Klinman, D.M.6    Chan, C.C.7    Egwuagu, C.E.8    Gery, I.9
  • 108
    • 0037442014 scopus 로고    scopus 로고
    • Pertussis toxin enhances Th1 responses by stimulation of dendritic cells
    • Hou, W.; Wu, Y.; Sun, S.; Shi, M.; Sun, Y.; Yang, C.; Pei, G.; Gu, Y.; Zhong, C.; Sun, B. Pertussis toxin enhances Th1 responses by stimulation of dendritic cells. J. Immunol. 2003, 170, 1728-1736.
    • (2003) J. Immunol , vol.170 , pp. 1728-1736
    • Hou, W.1    Wu, Y.2    Sun, S.3    Shi, M.4    Sun, Y.5    Yang, C.6    Pei, G.7    Gu, Y.8    Zhong, C.9    Sun, B.10
  • 110
    • 0032821914 scopus 로고    scopus 로고
    • The B-oligomer of pertussis toxin deactivates CC chemokine receptor 5 and blocks entry of M-tropic HIV-1 strains
    • Alfano, M.; Schmidtmayerova, H.; Amella, C.A.; Pushkarsky, T.; Bukrinsky, M. The B-oligomer of pertussis toxin deactivates CC chemokine receptor 5 and blocks entry of M-tropic HIV-1 strains. J. Exp. Med. 1999, 190, 597-605.
    • (1999) J. Exp. Med , vol.190 , pp. 597-605
    • Alfano, M.1    Schmidtmayerova, H.2    Amella, C.A.3    Pushkarsky, T.4    Bukrinsky, M.5
  • 111
    • 0033858616 scopus 로고    scopus 로고
    • The B-oligomer of pertussis toxin inhibits human immunodeficiency virus type 1 replication at multiple stages
    • Alfano, M.; Pushkarsky, T.; Poli, G.; Bukrinsky, M. The B-oligomer of pertussis toxin inhibits human immunodeficiency virus type 1 replication at multiple stages. J. Virol. 2000, 74, 8767-8770.
    • (2000) J. Virol , vol.74 , pp. 8767-8770
    • Alfano, M.1    Pushkarsky, T.2    Poli, G.3    Bukrinsky, M.4
  • 112
    • 30744471901 scopus 로고    scopus 로고
    • Pertussis toxin B-oligomer suppresses IL-6 induced HIV-1 and chemokine expression in chronically infected U1 cells via inhibition of activator protein 1
    • Rizzi, C.; Crippa, M.P.; Jeeninga, R.E.; Berkhout, B.; Blasi, F.; Poli, G.; Alfano, M. Pertussis toxin B-oligomer suppresses IL-6 induced HIV-1 and chemokine expression in chronically infected U1 cells via inhibition of activator protein 1. J. Immunol. 2006, 176, 999-1006.
    • (2006) J. Immunol , vol.176 , pp. 999-1006
    • Rizzi, C.1    Crippa, M.P.2    Jeeninga, R.E.3    Berkhout, B.4    Blasi, F.5    Poli, G.6    Alfano, M.7
  • 113
    • 70350728404 scopus 로고    scopus 로고
    • Receptors of anthrax toxin and cell entry
    • van der Goot, G.; Young, J.A. Receptors of anthrax toxin and cell entry. Mol. Aspects Med. 2009, 30, 406-412.
    • (2009) Mol. Aspects Med , vol.30 , pp. 406-412
    • Van der Goot, G.1    Young, J.A.2
  • 115
    • 4444267311 scopus 로고    scopus 로고
    • Structure of heptameric protective antigen bound to an anthrax toxin receptor: A role for receptor in pH-dependent pore formation
    • USA
    • Lacy, D.B.; Wigelsworth, D.J.; Melnyk, R.A.; Harrison, S.C.; Collier, R.J. Structure of heptameric protective antigen bound to an anthrax toxin receptor: a role for receptor in pH-dependent pore formation. Proc. Natl. Acad. Sci. USA 2004, 101, 13147-13151.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 13147-13151
    • Lacy, D.B.1    Wigelsworth, D.J.2    Melnyk, R.A.3    Harrison, S.C.4    Collier, R.J.5
  • 116
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers Endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami, L.; Liu, S.; Cosson, P.; Leppla, S.H.; van der Goot, F.G. Anthrax toxin triggers Endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 2003, 160, 321-328.
    • (2003) J. Cell Biol , vol.160 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    Van Der, G.F.G.5
  • 117
  • 118
    • 76549104967 scopus 로고    scopus 로고
    • Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake
    • USA
    • Abrami, L.; Kunz, B.; van der Goot, F.G. Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake. Proc. Natl. Acad. Sci. USA 2010, 107, 1420-1424.
    • (2010) Proc. Natl. Acad. Sci , vol.107 , pp. 1420-1424
    • Abrami, L.1    Kunz, B.2    Van der, G.F.G.3
  • 119
    • 33748211202 scopus 로고    scopus 로고
    • Model of the toxic complex of anthrax: Responsive conformational changes in both the lethal factor and the protective antigen heptamer
    • Tama, F.; Ren, G.; Brooks, C.L., III; Mitra, A.K. Model of the toxic complex of anthrax: responsive conformational changes in both the lethal factor and the protective antigen heptamer. Protein Sci. 2006, 15, 2190-2200.
    • (2006) Protein Sci , vol.15 , pp. 2190-2200
    • Tama, F.1    Ren, G.2    Brooks, C.L.3    Mitra, A.K.4
  • 120
    • 77950407292 scopus 로고    scopus 로고
    • Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors
    • Abrami, L.; Bischofberger, M.; Kunz, B.; Groux, R.; van der Goot, F.G. Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathog. 2010, 6, e1000792.
    • (2010) PLoS Pathog , vol.6
    • Abrami, L.1    Bischofberger, M.2    Kunz, B.3    Groux, R.4    van der, G.F.G.5
  • 121
    • 33646132042 scopus 로고    scopus 로고
    • Onset of anthrax toxin pore formation
    • Gao, M.; Schulten, K. Onset of anthrax toxin pore formation. Biophys. J. 2006, 90, 3267-3279.
    • (2006) Biophys. J , vol.90 , pp. 3267-3279
    • Gao, M.1    Schulten, K.2
  • 122
    • 64549164100 scopus 로고    scopus 로고
    • Evidence for a proton-protein symport mechanism in the anthrax toxin channel
    • Basilio, D.; Juris, S.J.; Collier, R.J.; Finkelstein, A. Evidence for a proton-protein symport mechanism in the anthrax toxin channel. J. Gen. Physiol. 2009, 133, 307-314.
    • (2009) J. Gen. Physiol , vol.133 , pp. 307-314
    • Basilio, D.1    Juris, S.J.2    Collier, R.J.3    Finkelstein, A.4
  • 123
    • 0032506245 scopus 로고    scopus 로고
    • Characterization of membrane translocation by anthrax protective antigen
    • Wesche, J.; Elliott, J.L.; Falnes, P.O.; Olsnes, S.; Collier, R.J. Characterization of membrane translocation by anthrax protective antigen. Biochemistry 1998, 37, 15737-15746.
    • (1998) Biochemistry , vol.37 , pp. 15737-15746
    • Wesche, J.1    Elliott, J.L.2    Falnes, P.O.3    Olsnes, S.4    Collier, R.J.5
  • 124
    • 76049107424 scopus 로고    scopus 로고
    • Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation
    • USA
    • Thoren, K.L.; Worden, E.J.; Yassif, J.M.; Krantz, B.A. Lethal factor unfolding is the most force-dependent step of anthrax toxin translocation. Proc. Natl. Acad. Sci. USA 2009, 106, 21555-21560.
    • (2009) Proc. Natl. Acad. Sci , vol.106 , pp. 21555-21560
    • Thoren, K.L.1    Worden, E.J.2    Yassif, J.M.3    Krantz, B.A.4
  • 125
    • 77950880249 scopus 로고    scopus 로고
    • Effects of introducing a single charged residue into the phenylalanine clamp of multimeric anthrax protective antigen
    • Janowiak, B.E.; Fischer, A.; Collier, R.J. Effects of introducing a single charged residue into the phenylalanine clamp of multimeric anthrax protective antigen. J. Biol. Chem. 2010, 285, 8130-8137.
    • (2010) J. Biol. Chem , vol.285 , pp. 8130-8137
    • Janowiak, B.E.1    Fischer, A.2    Collier, R.J.3
  • 126
    • 10044247127 scopus 로고    scopus 로고
    • Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel
    • USA
    • Zhang, S.; Finkelstein, A.; Collier, R.J. Evidence that translocation of anthrax toxin's lethal factor is initiated by entry of its N terminus into the protective antigen channel. Proc. Natl. Acad. Sci. USA 2004, 101, 16756-16761.
    • (2004) Proc. Natl. Acad. Sci , vol.101 , pp. 16756-16761
    • Zhang, S.1    Finkelstein, A.2    Collier, R.J.3
  • 129
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale, G.; Pellizzari, R.; Recchi, C.; Napolitani, G.; Mock, M.; Montecucco, C. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 1998, 248, 706-711.
    • (1998) Biochem. Biophys. Res. Commun , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 131
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • Vitale, G.; Bernardi, L.; Napolitani, G.; Mock, M.; Montecucco, C. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 2000, 352 (Pt 3), 739-745.
    • (2000) Biochem. J , vol.352 , Issue.Pt 3 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 132
    • 16344384729 scopus 로고    scopus 로고
    • Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor
    • Shen, Y.; Zhukovskaya, N.L.; Guo, Q.; Florian, J.; Tang, W.J. Calcium-independent calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. EMBO J. 2005, 24, 929-941.
    • (2005) EMBO J , vol.24 , pp. 929-941
    • Shen, Y.1    Zhukovskaya, N.L.2    Guo, Q.3    Florian, J.4    Tang, W.J.5
  • 133
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla, S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. USA 1982, 79, 3162-3166.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 137
    • 70349510543 scopus 로고    scopus 로고
    • Anthrax edema toxin inhibits Nox1-mediated formation of reactive oxygen species by colon epithelial cells
    • Kim, J.S.; Bokoch, G.M. Anthrax edema toxin inhibits Nox1-mediated formation of reactive oxygen species by colon epithelial cells. J. Innate Immun. 2009, 1, 145-152.
    • (2009) J. Innate Immun , vol.1 , pp. 145-152
    • Kim, J.S.1    Bokoch, G.M.2
  • 138
    • 0033965158 scopus 로고    scopus 로고
    • The p38 signal transduction pathway: Activation and function
    • Ono, K.; Han, J. The p38 signal transduction pathway: activation and function. Cell. Signal. 2000, 12, 1-13.
    • (2000) Cell. Signal , vol.12 , pp. 1-13
    • Ono, K.1    Han, J.2
  • 139
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park, J.M.; Greten, F.R.; Li, Z.W.; Karin, M. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 2002, 297, 2048-2051.
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3    Karin, M.4
  • 142
    • 77951211617 scopus 로고    scopus 로고
    • Anthrax Lethal Toxin Impairs CD1d-Mediated Antigen Presentation by Targeting the ERK1/2 MAPK Pathway
    • doi:10.1128/IAI.01307-09
    • Khan, M.A.; Gallo, R.M.; Brutkiewicz, R.R. Anthrax Lethal Toxin Impairs CD1d-Mediated Antigen Presentation by Targeting the ERK1/2 MAPK Pathway. Infect. Immun.2010, doi:10.1128/IAI.01307-09.
    • (2010) Infect. Immun
    • Khan, M.A.1    Gallo, R.M.2    Brutkiewicz, R.R.3
  • 143
    • 70349579031 scopus 로고    scopus 로고
    • Bacillus anthracis lethal toxin attenuates lipoteichoic acid-induced maturation and activation of dendritic cells through a unique mechanism
    • Yang, J.; Woo, S.S.; Ryu, Y.H.; Yun, C.H.; Cho, M.H.; Rhie, G.E.; Kim, B.S.; Oh, H.B.; Han, S.H. Bacillus anthracis lethal toxin attenuates lipoteichoic acid-induced maturation and activation of dendritic cells through a unique mechanism. Mol. Immunol. 2009, 46, 3261-3268.
    • (2009) Mol. Immunol , vol.46 , pp. 3261-3268
    • Yang, J.1    Woo, S.S.2    Ryu, Y.H.3    Yun, C.H.4    Cho, M.H.5    Rhie, G.E.6    Kim, B.S.7    Oh, H.B.8    Han, S.H.9
  • 145
    • 65449172044 scopus 로고    scopus 로고
    • Anthrax edema toxin induces maturation of dendritic cells and enhances chemotaxis towards macrophage inflammatory protein 3beta
    • Maldonado-Arocho, F.J.; Bradley, K.A. Anthrax edema toxin induces maturation of dendritic cells and enhances chemotaxis towards macrophage inflammatory protein 3beta. Infect. Immun. 2009, 77, 2036-2042.
    • (2009) Infect. Immun , vol.77 , pp. 2036-2042
    • Maldonado-Arocho, F.J.1    Bradley, K.A.2
  • 146
    • 33748506107 scopus 로고    scopus 로고
    • Anthrax oedema toxin induces anthrax toxin receptor expression in monocyte-derived cells
    • Maldonado-Arocho, F.J.; Fulcher, J.A.; Lee, B.; Bradley, K.A. Anthrax oedema toxin induces anthrax toxin receptor expression in monocyte-derived cells. Mol. Microbiol. 2006, 61, 324-337.
    • (2006) Mol. Microbiol , vol.61 , pp. 324-337
    • Maldonado-Arocho, F.J.1    Fulcher, J.A.2    Lee, B.3    Bradley, K.A.4
  • 147
    • 36749009663 scopus 로고    scopus 로고
    • Anthrax lethal toxin- mediated killing of human and murine dendritic cells impairs the adaptive immune response
    • Alileche, A.; Serfass, E.R.; Muehlbauer, S.M.; Porcelli, S.A.; Brojatsch, J. Anthrax lethal toxin- mediated killing of human and murine dendritic cells impairs the adaptive immune response. PLoS Pathog. 2005, 1, e19.
    • (2005) PLoS Pathog , vol.1
    • Alileche, A.1    Serfass, E.R.2    Muehlbauer, S.M.3    Porcelli, S.A.4    Brojatsch, J.5
  • 148
    • 28444498350 scopus 로고    scopus 로고
    • Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo
    • Comer, J.E.; Chopra, A.K.; Peterson, J.W.; Konig, R. Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo. Infect. Immun. 2005, 73, 8275-8281.
    • (2005) Infect. Immun , vol.73 , pp. 8275-8281
    • Comer, J.E.1    Chopra, A.K.2    Peterson, J.W.3    Konig, R.4
  • 149
    • 17044378194 scopus 로고    scopus 로고
    • Anthrax lethal toxin blocks MAPK kinase-dependent IL-2 production in CD4+ T cells
    • Fang, H.; Cordoba-Rodriguez, R.; Lankford, C.S.; Frucht, D.M. Anthrax lethal toxin blocks MAPK kinase-dependent IL-2 production in CD4+ T cells. J. Immunol. 2005, 174, 4966-4971.
    • (2005) J. Immunol , vol.174 , pp. 4966-4971
    • Fang, H.1    Cordoba-Rodriguez, R.2    Lankford, C.S.3    Frucht, D.M.4
  • 151
    • 33646484203 scopus 로고    scopus 로고
    • Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production
    • Fang, H.; Xu, L.; Chen, T.Y.; Cyr, J.M.; Frucht, D.M. Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production. J. Immunol. 2006, 176, 6155-6161.
    • (2006) J. Immunol , vol.176 , pp. 6155-6161
    • Fang, H.1    Xu, L.2    Chen, T.Y.3    Cyr, J.M.4    Frucht, D.M.5
  • 152
    • 70349655453 scopus 로고    scopus 로고
    • Poly-gamma-d-glutamic acid and protective antigen conjugate vaccines induce functional antibodies against the protective antigen and capsule of Bacillus anthracis in guinea-pigs and rabbits
    • Lee, D.Y.; Chun, J.H.; Ha, H.J.; Park, J.; Kim, B.S.; Oh, H.B.; Rhie, G.E. Poly-gamma-d-glutamic acid and protective antigen conjugate vaccines induce functional antibodies against the protective antigen and capsule of Bacillus anthracis in guinea-pigs and rabbits. FEMS Immunol. Med. Microbiol. 2009, 57, 165-172.
    • (2009) FEMS Immunol. Med. Microbiol , vol.57 , pp. 165-172
    • Lee, D.Y.1    Chun, J.H.2    Ha, H.J.3    Park, J.4    Kim, B.S.5    Oh, H.B.6    Rhie, G.E.7
  • 153
    • 33747229123 scopus 로고    scopus 로고
    • Ribosome-inactivating proteins: Progress and problems
    • Stirpe, F.; Battelli, M.G. Ribosome-inactivating proteins: progress and problems. Cell. Mol. Life Sci. 2006, 63, 1850-1866.
    • (2006) Cell. Mol. Life Sci , vol.63 , pp. 1850-1866
    • Stirpe, F.1    Battelli, M.G.2
  • 154
    • 33745969531 scopus 로고    scopus 로고
    • Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay
    • Lubelli, C.; Chatgilialoglu, A.; Bolognesi, A.; Strocchi, P.; Colombatti, M.; Stirpe, F. Detection of ricin and other ribosome-inactivating proteins by an immuno-polymerase chain reaction assay. Anal. Biochem. 2006, 355, 102-109.
    • (2006) Anal. Biochem , vol.355 , pp. 102-109
    • Lubelli, C.1    Chatgilialoglu, A.2    Bolognesi, A.3    Strocchi, P.4    Colombatti, M.5    Stirpe, F.6
  • 155
    • 0026594370 scopus 로고
    • Biological activity of recombinant Ricinus communis agglutinin A chain produced in Escherichia coli
    • O'Hare, M.; Roberts, L.M.; Lord, J.M. Biological activity of recombinant Ricinus communis agglutinin A chain produced in Escherichia coli. FEBS Lett. 1992, 299, 209-212.
    • (1992) FEBS Lett , vol.299 , pp. 209-212
    • O'hare, M.1    Roberts, L.M.2    Lord, J.M.3
  • 157
    • 0023947126 scopus 로고
    • The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA
    • Endo, Y.; Tsurugi, K. The RNA N-glycosidase activity of ricin A-chain. The characteristics of the enzymatic activity of ricin A-chain with ribosomes and with rRNA. J. Biol. Chem. 1988, 263, 8735-8739.
    • (1988) J. Biol. Chem , vol.263 , pp. 8735-8739
    • Endo, Y.1    Tsurugi, K.2
  • 158
    • 56749154533 scopus 로고    scopus 로고
    • The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae
    • Chiou, J.C.; Li, X.P.; Remacha, M.; Ballesta, J.P.; Tumer, N.E. The ribosomal stalk is required for ribosome binding, depurination of the rRNA and cytotoxicity of ricin A chain in Saccharomyces cerevisiae. Mol. Microbiol. 2008, 70, 1441-1452.
    • (2008) Mol. Microbiol , vol.70 , pp. 1441-1452
    • Chiou, J.C.1    Li, X.P.2    Remacha, M.3    Ballesta, J.P.4    Tumer, N.E.5
  • 159
    • 0033570907 scopus 로고    scopus 로고
    • A new class of enzyme acting on damaged ribosomes: Ribosomal RNA apurinic site specific lyase found in wheat germ
    • Ogasawara, T.; Sawasaki, T.; Morishita, R.; Ozawa, A.; Madin, K.; Endo, Y. A new class of enzyme acting on damaged ribosomes: ribosomal RNA apurinic site specific lyase found in wheat germ. EMBO J. 1999, 18, 6522-6531.
    • (1999) EMBO J , vol.18 , pp. 6522-6531
    • Ogasawara, T.1    Sawasaki, T.2    Morishita, R.3    Ozawa, A.4    Madin, K.5    Endo, Y.6
  • 160
    • 0019309042 scopus 로고
    • Entry of lethal doses of abrin, ricin and modeccin into the cytosol of HeLa cells
    • Eiklid, K.; Olsnes, S.; Pihl, A. Entry of lethal doses of abrin, ricin and modeccin into the cytosol of HeLa cells. Exp. Cell Res. 1980, 126, 321-326.
    • (1980) Exp. Cell Res , vol.126 , pp. 321-326
    • Eiklid, K.1    Olsnes, S.2    Pihl, A.3
  • 161
    • 1642539986 scopus 로고    scopus 로고
    • The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain
    • Marsden, C.J.; Fulop, V.; Day, P.J.; Lord, J.M. The effect of mutations surrounding and within the active site on the catalytic activity of ricin A chain. Eur. J. Biochem. 2004, 271, 153-162.
    • (2004) Eur. J. Biochem , vol.271 , pp. 153-162
    • Marsden, C.J.1    Fulop, V.2    Day, P.J.3    Lord, J.M.4
  • 162
    • 0024756611 scopus 로고
    • Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes
    • Schlossman, D.; Withers, D.; Welsh, P.; Alexander, A.; Robertus, J.; Frankel, A. Role of glutamic acid 177 of the ricin toxin A chain in enzymatic inactivation of ribosomes. Mol. Cell Biol. 1989, 9, 5012-5021.
    • (1989) Mol. Cell Biol , vol.9 , pp. 5012-5021
    • Schlossman, D.1    Withers, D.2    Welsh, P.3    Alexander, A.4    Robertus, J.5    Frankel, A.6
  • 163
    • 0042311010 scopus 로고    scopus 로고
    • Role of lipids in the retrograde pathway of ricin intoxication
    • Spilsberg, B.; Van Meer, G.; Sandvig, K. Role of lipids in the retrograde pathway of ricin intoxication. Traffic 2003, 4, 544-552.
    • (2003) Traffic , vol.4 , pp. 544-552
    • Spilsberg, B.1    van Meer, G.2    Sandvig, K.3
  • 164
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo, Y.; Mitsui, K.; Motizuki, M.; Tsurugi, K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem. 1987, 262, 5908-5912.
    • (1987) J. Biol. Chem , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 165
    • 0023219950 scopus 로고
    • N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes
    • Endo, Y.; Tsurugi, K. RNA N-glycosidase activity of ricin A-chain. Mechanism of action of the toxic lectin ricin on eukaryotic ribosomes. J. Biol. Chem. 1987, 262, 8128-8130.
    • (1987) J. Biol. Chem , vol.262 , pp. 8128-8130
    • Endo, Y.1    Tsurugi, K.R.N.A.2
  • 166
    • 0025695634 scopus 로고
    • Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate
    • Rothberg, K.G.; Ying, Y.S.; Kamen, B.A.; Anderson, R.G. Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate. J. Cell. Biol. 1990, 111, 2931-2938.
    • (1990) J. Cell. Biol , vol.111 , pp. 2931-2938
    • Rothberg, K.G.1    Ying, Y.S.2    Kamen, B.A.3    Anderson, R.G.4
  • 167
    • 0032931988 scopus 로고    scopus 로고
    • Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated Endocytic vesicles
    • Rodal, S.K.; Skretting, G.; Garred, O.; Vilhardt, F.; van Deurs, B.; Sandvig, K. Extraction of cholesterol with methyl-beta-cyclodextrin perturbs formation of clathrin-coated Endocytic vesicles. Mol. Biol. Cell. 1999, 10, 961-974.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 961-974
    • Rodal, S.K.1    Skretting, G.2    Garred, O.3    Vilhardt, F.4    van Deurs, B.5    Sandvig, K.6
  • 168
    • 0027398577 scopus 로고
    • Rab9 functions in transport between late Endosomes and the trans Golgi network
    • Lombardi, D.; Soldati, T.; Riederer, M.A.; Goda, Y.; Zerial, M.; Pfeffer, S.R. Rab9 functions in transport between late Endosomes and the trans Golgi network. EMBO J. 1993, 12, 677-682.
    • (1993) EMBO J , vol.12 , pp. 677-682
    • lombardi, D.1    Soldati, T.2    Riederer, M.A.3    Goda, Y.4    Zerial, M.5    Pfeffer, S.R.6
  • 169
    • 0035150144 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- and Rab11-GTPases
    • Iversen, T.G.; Skretting, G.; Llorente, A.; Nicoziani, P.; van Deurs, B.; Sandvig, K. Endosome to Golgi transport of ricin is independent of clathrin and of the Rab9- and Rab11-GTPases. Mol. Biol. Cell. 2001, 12, 2099-2107.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2099-2107
    • Iversen, T.G.1    Skretting, G.2    Llorente, A.3    Nicoziani, P.4    van Deurs, B.5    Sandvig, K.6
  • 170
    • 0033634889 scopus 로고    scopus 로고
    • Endosome to Golgi transport of ricin is regulated by cholesterol
    • Grimmer, S.; Iversen, T.G.; van Deurs, B.; Sandvig, K. Endosome to Golgi transport of ricin is regulated by cholesterol. Mol. Biol. Cell. 2000, 11, 4205-4216.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 4205-4216
    • Grimmer, S.1    Iversen, T.G.2    van Deurs, B.3    Sandvig, K.4
  • 172
    • 0035831558 scopus 로고    scopus 로고
    • An interaction between ricin and calreticulin that may have implications for toxin trafficking
    • Day, P.J.; Owens, S.R.; Wesche, J.; Olsnes, S.; Roberts, L.M.; Lord, J.M. An interaction between ricin and calreticulin that may have implications for toxin trafficking. J. Biol. Chem. 2001, 276, 7202-7208.
    • (2001) J. Biol. Chem , vol.276 , pp. 7202-7208
    • Day, P.J.1    Owens, S.R.2    Wesche, J.3    Olsnes, S.4    Roberts, L.M.5    Lord, J.M.6
  • 173
  • 174
    • 0029909329 scopus 로고    scopus 로고
    • Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin
    • Sandvig, K.; van Deurs, B. Endocytosis, intracellular transport, and cytotoxic action of Shiga toxin and ricin. Physiol. Rev. 1996, 76, 949-966.
    • (1996) Physiol. Rev , vol.76 , pp. 949-966
    • Sandvig, K.1    van Deurs, B.2
  • 177
    • 0037176821 scopus 로고    scopus 로고
    • Binding of ricin A-chain to negatively charged phospholipid vesicles leads to protein structural changes and destabilizes the lipid bilayer
    • Day, P.J.; Pinheiro, T.J.; Roberts, L.M.; Lord, J.M. Binding of ricin A-chain to negatively charged phospholipid vesicles leads to protein structural changes and destabilizes the lipid bilayer. Biochemistry 2002, 41, 2836-2843.
    • (2002) Biochemistry , vol.41 , pp. 2836-2843
    • Day, P.J.1    Pinheiro, T.J.2    Roberts, L.M.3    Lord, J.M.4
  • 179
    • 0027289275 scopus 로고
    • Protection of mice from inhaled ricin by vaccination with ricin or by passive treatment with heterologous antibody
    • Hewetson, J.F.; Rivera, V.R.; Creasia, D.A.; Lemley, P.V.; Rippy, M.K.; Poli, M.A. Protection of mice from inhaled ricin by vaccination with ricin or by passive treatment with heterologous antibody. Vaccine 1993, 11, 743-746.
    • (1993) Vaccine , vol.11 , pp. 743-746
    • Hewetson, J.F.1    Rivera, V.R.2    Creasia, D.A.3    Lemley, P.V.4    Rippy, M.K.5    Poli, M.A.6
  • 180
    • 0020600983 scopus 로고
    • Antibody formation against the cytotoxic proteins abrin and ricin in humans and mice
    • Godal, A.; Fodstad, O.; Pihl, A. Antibody formation against the cytotoxic proteins abrin and ricin in humans and mice. Int. J. Cancer 1983, 32, 515-521.
    • (1983) Int. J. Cancer , vol.32 , pp. 515-521
    • Godal, A.1    Fodstad, O.2    Pihl, A.3
  • 181
    • 0022428446 scopus 로고
    • The removal of carbohydrates from ricin with Endoglycosidases H, F and D and alpha-mannosidase
    • Foxwell, B.M.; Donovan, T.A.; Thorpe, P.E.; Wilson, G. The removal of carbohydrates from ricin with Endoglycosidases H, F and D and alpha-mannosidase. Biochim. Biophys. Acta 1985, 840, 193-203.
    • (1985) Biochim. Biophys. Acta , vol.840 , pp. 193-203
    • Foxwell, B.M.1    Donovan, T.A.2    Thorpe, P.E.3    Wilson, G.4
  • 182
    • 0021985323 scopus 로고
    • The use of anti-ricin antibodies to protect mice intoxicated with ricin
    • Foxwell, B.M.; Detre, S.I.; Donovan, T.A.; Thorpe, P.E. The use of anti-ricin antibodies to protect mice intoxicated with ricin. Toxicology 1985, 34, 79-88.
    • (1985) Toxicology , vol.34 , pp. 79-88
    • Foxwell, B.M.1    Detre, S.I.2    Donovan, T.A.3    Thorpe, P.E.4
  • 183
    • 0025986909 scopus 로고
    • Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action
    • Ready, M.P.; Kim, Y.; Robertus, J.D. Site-directed mutagenesis of ricin A-chain and implications for the mechanism of action. Proteins 1991, 10, 270-278.
    • (1991) Proteins , vol.10 , pp. 270-278
    • Ready, M.P.1    Kim, Y.2    Robertus, J.D.3
  • 184
    • 0028102678 scopus 로고
    • Identification and characterization of a monoclonal antibody that neutralizes ricin toxicity in vitro and in vivo
    • Lemley, P.V.; Amanatides, P.; Wright, D.C. Identification and characterization of a monoclonal antibody that neutralizes ricin toxicity in vitro and in vivo. Hybridoma 1994, 13, 417-421.
    • (1994) Hybridoma , vol.13 , pp. 417-421
    • Lemley, P.V.1    Amanatides, P.2    Wright, D.C.3
  • 185
    • 0023182792 scopus 로고
    • Identification and characterization of a monoclonal antibody recognizing a galactose-binding domain of the toxin ricin
    • Colombatti, M.; Johnson, V.G.; Skopicki, H.A.; Fendley, B.; Lewis, M.S.; Youle, R.J. Identification and characterization of a monoclonal antibody recognizing a galactose-binding domain of the toxin ricin. J. Immunol. 1987, 138, 3339-3344.
    • (1987) J. Immunol , vol.138 , pp. 3339-3344
    • Colombatti, M.1    Johnson, V.G.2    Skopicki, H.A.3    Fendley, B.4    Lewis, M.S.5    Youle, R.J.6
  • 186
    • 0032905566 scopus 로고    scopus 로고
    • Prediction of a conserved, neutralizing epitope in ribosome-inactivating proteins
    • Lebeda, F.J.; Olson, M.A. Prediction of a conserved, neutralizing epitope in ribosome-inactivating proteins. Int. J. Biol. Macromol. 1999, 24, 19-26.
    • (1999) Int. J. Biol. Macromol , vol.24 , pp. 19-26
    • Lebeda, F.J.1    Olson, M.A.2
  • 187
    • 2442626550 scopus 로고    scopus 로고
    • Immunological characteristics associated with the protective efficacy of antibodies to ricin
    • Maddaloni, M.; Cooke, C.; Wilkinson, R.; Stout, A.V.; Eng, L.; Pincus, S.H. Immunological characteristics associated with the protective efficacy of antibodies to ricin. J. Immunol. 2004, 172, 6221-6228.
    • (2004) J. Immunol , vol.172 , pp. 6221-6228
    • Maddaloni, M.1    Cooke, C.2    Wilkinson, R.3    Stout, A.V.4    Eng, L.5    Pincus, S.H.6
  • 188
    • 20344390272 scopus 로고    scopus 로고
    • Vaccines against the category B toxins: Staphylococcal enterotoxin B, epsilon toxin and ricin
    • Mantis, N.J. Vaccines against the category B toxins: Staphylococcal enterotoxin B, epsilon toxin and ricin. Adv. Drug Deliv. Rev. 2005, 57, 1424-1439.
    • (2005) Adv. Drug Deliv. Rev , vol.57 , pp. 1424-1439
    • Mantis, N.J.1
  • 189
    • 0022425552 scopus 로고
    • Modification of the carbohydrate in ricin with metaperiodate-cyanoborohydride mixtures. Effects on toxicity and in vivo distribution
    • Thorpe, P.E.; Detre, S.I.; Foxwell, B.M.; Brown, A.N.; Skilleter, D.N.; Wilson, G.; Forrester, J.A.; Stirpe, F. Modification of the carbohydrate in ricin with metaperiodate-cyanoborohydride mixtures. Effects on toxicity and in vivo distribution. Eur. J. Biochem. 1985, 147, 197-206.
    • (1985) Eur. J. Biochem , vol.147 , pp. 197-206
    • Thorpe, P.E.1    Detre, S.I.2    Foxwell, B.M.3    Brown, A.N.4    Skilleter, D.N.5    Wilson, G.6    Forrester, J.A.7    Stirpe, F.8
  • 190
    • 0030733914 scopus 로고    scopus 로고
    • Liposomally-encapsulated ricin toxoid vaccine delivered intratracheally elicits a good immune response and protects against a lethal pulmonary dose of ricin toxin
    • Griffiths, G.D.; Bailey, S.C.; Hambrook, J.L.; Keyte, M.; Jayasekera, P.; Miles, J.; Williamson, E. Liposomally-encapsulated ricin toxoid vaccine delivered intratracheally elicits a good immune response and protects against a lethal pulmonary dose of ricin toxin. Vaccine 1997, 15, 1933-1939.
    • (1997) Vaccine , vol.15 , pp. 1933-1939
    • Griffiths, G.D.1    Bailey, S.C.2    Hambrook, J.L.3    Keyte, M.4    Jayasekera, P.5    Miles, J.6    Williamson, E.7
  • 191
    • 0029058270 scopus 로고
    • Kende, M. Dependence of ricin toxoid vaccine efficacy on the structure of poly(lactide-co-glycolide) microparticle carriers
    • Yan, C.; Rill, W.L.; Malli, R.; Hewetson, J.; Tammariello, R.; Kende, M. Dependence of ricin toxoid vaccine efficacy on the structure of poly(lactide-co-glycolide) microparticle carriers. Vaccine 1995, 13, 645-651.
    • (1995) Vaccine , vol.13 , pp. 645-651
    • Yan, C.1    Rill, W.L.2    Malli, R.3    Hewetson, J.4    Tammariello, R.5
  • 192
    • 0037154847 scopus 로고    scopus 로고
    • Oral immunization of mice with ricin toxoid vaccine encapsulated in polymeric microspheres against aerosol challenge
    • Kende, M.; Yan, C.; Hewetson, J.; Frick, M.A.; Rill, W.L.; Tammariello, R. Oral immunization of mice with ricin toxoid vaccine encapsulated in polymeric microspheres against aerosol challenge. Vaccine 2002, 20, 1681-1691.
    • (2002) Vaccine , vol.20 , pp. 1681-1691
    • Kende, M.1    Yan, C.2    Hewetson, J.3    Frick, M.A.4    Rill, W.L.5    Tammariello, R.6
  • 193
    • 67650678448 scopus 로고    scopus 로고
    • Humanized immunotoxins: A new generation of immunotoxins for targeted cancer therapy
    • Mathew, M.; Verma, R.S. Humanized immunotoxins: a new generation of immunotoxins for targeted cancer therapy. Cancer Sci. 2009, 100, 1359-1365.
    • (2009) Cancer Sci , vol.100 , pp. 1359-1365
    • Mathew, M.1    Verma, R.S.2
  • 194
    • 0033162598 scopus 로고    scopus 로고
    • Approves fusion protein for treatment of lymphoma
    • Piascik, P. FDA approves fusion protein for treatment of lymphoma. J. Am. Pharm. Assoc. (Wash.) 1999, 39, 571-572.
    • (1999) J. Am. Pharm. Assoc. (Wash , vol.39 , pp. 571-572
    • Piascik, P.F.D.A.1
  • 195
    • 77649232515 scopus 로고    scopus 로고
    • Expression of a ricin toxin B subunit: Insulin fusion protein in edible plant tissues
    • Carter, J.E., III; Odumosu, O.; Langridge, W.H. Expression of a ricin toxin B subunit: insulin fusion protein in edible plant tissues. Mol. Biotechnol. 2009, 44, 90-100.
    • (2009) Mol. Biotechnol , vol.44 , pp. 90-100
    • Carter, J.E.1    Odumosu, O.2    Langridge, W.H.3
  • 196
  • 197
    • 0033280218 scopus 로고    scopus 로고
    • Food plant-delivered cholera toxin B subunit for vaccination and immunotolerization
    • Arakawa, T.; Yu, J.; Langridge, W.H. Food plant-delivered cholera toxin B subunit for vaccination and immunotolerization. Adv. Exp. Med. Biol. 1999, 464, 161-178.
    • (1999) Adv. Exp. Med. Biol , vol.464 , pp. 161-178
    • Arakawa, T.1    Yu, J.2    Langridge, W.H.3
  • 198
    • 77954961620 scopus 로고    scopus 로고
    • Autoantigen plus interleukin-10 suppress diabetes autoimmunity
    • submitted for publication
    • Denes, B.; Fodor. I.; Langridge, W. Autoantigen plus interleukin-10 suppress diabetes autoimmunity. Diabetes Technol. Ther. 2010, submitted for publication.
    • (2010) Diabetes Technol. Ther
    • Denes, B.1    Fodor, I.2    Langridge, W.3
  • 199
    • 38349037623 scopus 로고    scopus 로고
    • Cancer immunotherapy based on recombinant Salmonella enterica serovar Typhimurium aroA strains secreting prostate-specific antigen and cholera toxin subunit B
    • Fensterle, J.; Bergmann, B.; Yone, C.L.; Hotz, C.; Meyer, S.R.; Spreng, S.; Goebel, W.; Rapp, U.R.; Gentschev, I. Cancer immunotherapy based on recombinant Salmonella enterica serovar Typhimurium aroA strains secreting prostate-specific antigen and cholera toxin subunit B. Cancer Gene Ther. 2008, 15, 85-93.
    • (2008) Cancer Gene Ther , vol.15 , pp. 85-93
    • Fensterle, J.1    Bergmann, B.2    Yone, C.L.3    Hotz, C.4    Meyer, S.R.5    Spreng, S.6    Goebel, W.7    Rapp, U.R.8    Gentschev, I.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.