메뉴 건너뛰기




Volumn , Issue , 2008, Pages 141-158

Clostridium difficile Toxins

Author keywords

Anti actin antibodies; Clostridium difficile; Hemorrhagic fluid; Homogeneity; Pseudomembranous

Indexed keywords


EID: 84954214925     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527614615.ch12     Document Type: Chapter
Times cited : (7)

References (107)
  • 1
    • 0020692081 scopus 로고
    • Loss of surface fibronectin from human lung fibroblasts exposed to cytotoxin from Clostridium difficile
    • Ahlgren T, Florin I, Jarstrand C, et al. (1983): Loss of surface fibronectin from human lung fibroblasts exposed to cytotoxin from Clostridium difficile. In Infect. Immun. 39: 1470-1472.
    • (1983) In Infect. Immun , vol.39 , pp. 1470-1472
    • Ahlgren, T.1    Florin, I.2    Jarstrand, C.3
  • 2
    • 0022641097 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates actin
    • Aktories K, Barman M, Ohishi I, et al. (1986): Botulinum C2 toxin ADP-ribosylates actin. In Nature (London) 322: 390-392.
    • (1986) In Nature (London) , vol.322 , pp. 390-392
    • Aktories, K.1    Barman, M.2    Ohishi, I.3
  • 3
    • 0023110218 scopus 로고
    • Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from C2 toxin
    • Aktories K, Weller U, Chatwal GS (1987): Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from C2 toxin. In FEBS Lett. 212: 109-113.
    • (1987) In FEBS Lett , vol.212 , pp. 109-113
    • Aktories, K.1    Weller, U.2    Chatwal, G.S.3
  • 4
    • 0028790399 scopus 로고
    • Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins
    • Aktories K, Just I (1995): Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by clostridial cytotoxins. In Trends Cell Biol. 5: 441-443.
    • (1995) In Trends Cell Biol , vol.5 , pp. 441-443
    • Aktories, K.1    Just, I.2
  • 5
    • 0021344470 scopus 로고
    • Rapid death of infant rhesus monkeys injected with Clostridium difficile toxins A and B: Physiologic and pathologic basis
    • Arnon SS, Mills DC, Day PA, et al. (1984): Rapid death of infant rhesus monkeys injected with Clostridium difficile toxins A and B: Physiologic and pathologic basis. In J. Pediatr. 104: 34-40.
    • (1984) In J. Pediatr , vol.104 , pp. 34-40
    • Arnon, S.S.1    Mills, D.C.2    Day, P.A.3
  • 6
    • 0019797242 scopus 로고
    • Two toxins (D-1 and D-2) of Clostridium difficile causing antibiotic-associated colitis: Purification and some characterization
    • Banno Y, Kobayashi T, Watanabe K, et al. (1981): Two toxins (D-1 and D-2) of Clostridium difficile causing antibiotic-associated colitis: purification and some characterization. In Biochem. Int. 2: 629-635.
    • (1981) In Biochem. Int , vol.2 , pp. 629-635
    • Banno, Y.1    Kobayashi, T.2    Watanabe, K.3
  • 7
    • 0021403353 scopus 로고
    • Biochemical characterization and biologic actions of two toxins (D-1 and D-2) from Clostridium difficile
    • Banno Y, Kobayashi T, Kono H, et al. (1984): Biochemical characterization and biologic actions of two toxins (D-1 and D-2) from Clostridium difficile. In Rev. Infect. Dis. 6: S11-S20.
    • (1984) In Rev. Infect. Dis , vol.6 , pp. S11-S20
    • Banno, Y.1    Kobayashi, T.2    Kono, H.3
  • 8
    • 0025367326 scopus 로고
    • Nucleotide sequence of the Clostridium difficile toxin B gene
    • Barroso LA, Wang SZ, Phelps CJ, et al. (1990): Nucleotide sequence of the Clostridium difficile toxin B gene. In Nucl. Acids Res. 18: 4004.
    • (1990) In Nucl. Acids Res , vol.18 , pp. 4004
    • Barroso, L.A.1    Wang, S.Z.2    Phelps, C.J.3
  • 9
    • 0027998795 scopus 로고
    • Mutagenesis of the Clostridium difficile toxin B gene and effect on cytotoxic activity
    • Barroso LA, Moncrief JS, Lyerly DM, et al. (1994): Mutagenesis of the Clostridium difficile toxin B gene and effect on cytotoxic activity. In Microb. Pathogen. 16: 297-303.
    • (1994) In Microb. Pathogen , vol.16 , pp. 297-303
    • Barroso, L.A.1    Moncrief, J.S.2    Lyerly, D.M.3
  • 10
    • 0017757971 scopus 로고
    • Clindamycin-associated colitis due to a toxin-producing species of Clostridium in hamsters
    • Bartlett JG, Onderdonk AB, Cisneros RL, et al. (1977): Clindamycin-associated colitis due to a toxin-producing species of Clostridium in hamsters. In J. Inf. Dis. 136: 701-705.
    • (1977) In J. Inf. Dis , vol.136 , pp. 701-705
    • Bartlett, J.G.1    Onderdonk, A.B.2    Cisneros, R.L.3
  • 11
    • 0025093525 scopus 로고
    • Clostridium difficile: Clinical considerations
    • Bartlett JG (1990): Clostridium difficile: Clinical considerations. In Rev. Inf. Dis. 12: S243-S251.
    • (1990) In Rev. Inf. Dis , vol.12 , pp. S243-S251
    • Bartlett, J.G.1
  • 12
    • 0018942383 scopus 로고
    • Protein synthesis requires cell-surface contact while nuclear events respond to cell shape in anchorage-dependent fibroblasts
    • Ben-Ze'ev A, Farmer SR, Penman S (1980): Protein synthesis requires cell-surface contact while nuclear events respond to cell shape in anchorage-dependent fibroblasts. In Cell, 21: 365-372.
    • (1980) In Cell , vol.21 , pp. 365-372
    • Ben-Ze'ev, A.1    Farmer, S.R.2    Penman, S.3
  • 13
    • 0024401088 scopus 로고
    • Pharmacological and biochemical, studies of cytotoxicity of Clostridium novyi type A alpha-toxin
    • Bette P, Frevert J, Mauler F, et al. (1989): Pharmacological and biochemical, studies of cytotoxicity of Clostridium novyi type A alpha-toxin. In Infect. Immun. 57: 2507-2513.
    • (1989) In Infect. Immun , vol.57 , pp. 2507-2513
    • Bette, P.1    Frevert, J.2    Mauler, F.3
  • 14
    • 0025768198 scopus 로고
    • A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C.difficile toxin B and C.sordellii lethal toxin
    • Bette P, Oksche A, Mauler F, et al. (1991): A comparative biochemical, pharmacological and immunological study of Clostridium novyi alpha-toxin, C.difficile toxin B and C.sordellii lethal toxin. In Toxicon, 29: 877-887.
    • (1991) In Toxicon , vol.29 , pp. 877-887
    • Bette, P.1    Oksche, A.2    Mauler, F.3
  • 15
    • 0027985585 scopus 로고
    • Mini-review Role of toxins A and B in the pathogenesis of Clostridium difficile disease
    • Bongaerts GPA, Lyerly DM (1994): Mini-review Role of toxins A and B in the pathogenesis of Clostridium difficile disease. In Microb. Pathogen. 17: 1-12.
    • (1994) In Microb. Pathogen , vol.17 , pp. 1-12
    • Bongaerts, G.P.A.1    Lyerly, D.M.2
  • 16
    • 0023268812 scopus 로고
    • Calcium and calmodulin in cellular intoxication with Clostridium difficile toxin B
    • Caspar M, Florin I, Thelestam M (1987): Calcium and calmodulin in cellular intoxication with Clostridium difficile toxin B. In J. Cell. Physiol. 132: 168-172.
    • (1987) In J. Cell. Physiol , vol.132 , pp. 168-172
    • Caspar, M.1    Florin, I.2    Thelestam, M.3
  • 17
    • 0028129331 scopus 로고
    • Neuronal involvement in the intestinal effects of Clostridium difficile toxin A and Vibrio cholerae enterotoxin in rat ileum
    • Castagliuolo I, LaMont JT, Letourneau R, et al. (1994): Neuronal involvement in the intestinal effects of Clostridium difficile toxin A and Vibrio cholerae enterotoxin in rat ileum. In Gastroenterol. 107: 657-665.
    • (1994) In Gastroenterol , vol.107 , pp. 657-665
    • Castagliuolo, I.1    LaMont, J.T.2    Letourneau, R.3
  • 18
    • 0018098448 scopus 로고
    • Clindamycin-induced enterocolitis in hamsters as a model of pseudomembranous colitis in patients
    • Chang T-W Bartlett JG, Gorbach SL, et al. (1978): Clindamycin-induced enterocolitis in hamsters as a model of pseudomembranous colitis in patients. In Infect. Immun. 20: 526-529.
    • (1978) In Infect. Immun , vol.20 , pp. 526-529
    • Chang, T.-W.1    Bartlett, J.G.2    Gorbach, S.L.3
  • 19
    • 0024449589 scopus 로고
    • The mammalian G-protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects microfilaments in Vero cells
    • Chardin P, Boquet P, Madaule P, et al. (1989): The mammalian G-protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects microfilaments in Vero cells. In EMBO J. 8: 1087-1092.
    • (1989) In EMBO J , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3
  • 21
    • 0025953135 scopus 로고
    • Phosphorylation of cellular proteins in response to treatment with Clostridium difficile toxin B and Clostridium sordellii toxin L
    • Ciesielski-Treska J, Ulrich G, Baldacini O, et al. (1991): Phosphorylation of cellular proteins in response to treatment with Clostridium difficile toxin B and Clostridium sordellii toxin L. In Eur. J. Cell Biol. 56: 68-78.
    • (1991) In Eur. J. Cell Biol , vol.56 , pp. 68-78
    • Ciesielski-Treska, J.1    Ulrich, G.2    Baldacini, O.3
  • 22
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu J-C, et al. (1995): The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. In Cell, 81: 1137-1146.
    • (1995) In Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.-C.3
  • 23
    • 0025017490 scopus 로고
    • Molecular characterization of the Clostridium difficile toxin A gene
    • Dove CH, Wang SZ, Price SB, et al. (1990): Molecular characterization of the Clostridium difficile toxin A gene. In Infect. Immun. 58: 480-488.
    • (1990) In Infect. Immun , vol.58 , pp. 480-488
    • Dove, C.H.1    Wang, S.Z.2    Price, S.B.3
  • 24
    • 0023906622 scopus 로고
    • Clostridium difficile toxins A and B inhibit human immune response in vitro
    • Däubener W, Leiser E, von Eichel-Streiber Cv, et al. (1988): Clostridium difficile toxins A and B inhibit human immune response in vitro. In Infect. Immun. 56: 1107-1112.
    • (1988) In Infect. Immun , vol.56 , pp. 1107-1112
    • Däubener, W.1    Leiser, E.2    von Eichel-Streiber, C.V.3
  • 25
    • 0025667927 scopus 로고
    • Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases
    • Eichel-Streiber Cv, Sauerborn M (1990): Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases. In Gene, 96: 107-113.
    • (1990) In Gene , vol.96 , pp. 107-113
    • Eichel-Streiber, C.V.1    Sauerborn, M.2
  • 26
    • 0025624777 scopus 로고
    • Cloning of Clostridium difficile toxin B gene and demonstration of high N-terminal homology between toxin A and B
    • Eichel-Streiber Cv, Laufenberg-Feldmann R, Sartingen S, et al. (1990): Cloning of Clostridium difficile toxin B gene and demonstration of high N-terminal homology between toxin A and B. In Med. Microbiol. Immunol. 179: 271-279.
    • (1990) In Med. Microbiol. Immunol , vol.179 , pp. 271-279
    • Eichel-Streiber, C.V.1    Laufenberg-Feldmann, R.2    Sartingen, S.3
  • 27
    • 0026655261 scopus 로고
    • Comparative sequence analysis of the Clostridium difficile toxins A and B
    • Eichel-Streiber Cv, Laufenberg-Feldmann R, Sartingen S, et al. (1992): Comparative sequence analysis of the Clostridium difficile toxins A and B. In Mol Gen Genet, 233: 260-268.
    • (1992) In Mol Gen Genet , vol.233 , pp. 260-268
    • Eichel-Streiber, C.V.1    Laufenberg-Feldmann, R.2    Sartingen, S.3
  • 28
    • 0013459331 scopus 로고
    • Molecular biology of the Clostridium difficile toxins
    • (Sebald M, ed) New York: Springer Verlag
    • Eichel-Streiber Cv (1993): Molecular biology of the Clostridium difficile toxins. In Genetics and Molecular Biology of Anaerobic Bacteria (Sebald M, ed) pp 264-289, New York: Springer Verlag.
    • (1993) In Genetics and Molecular Biology of Anaerobic Bacteria , pp. 264-289
    • Eichel-Streiber, C.V.1
  • 29
    • 0029086528 scopus 로고
    • Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B
    • Eichel-Streiber CV, Meyer zu Heringdorf D, Habermann E, et al. (1995): Closing in on the toxic domain through analysis of a variant Clostridium difficile cytotoxin B. In Molec. Microbiol. 17: 313-321.
    • (1995) In Molec. Microbiol , vol.17 , pp. 313-321
    • Eichel-Streiber, C.V.1    Meyer zu Heringdorf, D.2    Habermann, E.3
  • 30
    • 0024472054 scopus 로고
    • Effects of Clostridium difficile toxins A and B on cytoskeleton organization in Hep-2 cells: A comparative morphological study
    • Fiorentini C, Arancia G, Paradisi S, et al. (1989): Effects of Clostridium difficile toxins A and B on cytoskeleton organization in Hep-2 cells: A comparative morphological study. In Toxicon, 27: 1209-1218.
    • (1989) In Toxicon , vol.27 , pp. 1209-1218
    • Fiorentini, C.1    Arancia, G.2    Paradisi, S.3
  • 31
    • 0025367873 scopus 로고
    • Interaction of Clostridium difficile toxin A with cultured cells: Cytoskeletal changes and nuclear polarization
    • Fiorentini C, Malorni W, Paradisi S, et al. (1990): Interaction of Clostridium difficile toxin A with cultured cells: cytoskeletal changes and nuclear polarization. In Infect. Immun. 58: 2329-2336.
    • (1990) In Infect. Immun , vol.58 , pp. 2329-2336
    • Fiorentini, C.1    Malorni, W.2    Paradisi, S.3
  • 32
    • 0025772090 scopus 로고
    • Review article Clostridium difficile toxin A and its effects on cells
    • Fiorentini C, Thelestam M (1991): Review article Clostridium difficile toxin A and its effects on cells. In Toxicon, 29: 543-567.
    • (1991) In Toxicon , vol.29 , pp. 543-567
    • Fiorentini, C.1    Thelestam, M.2
  • 33
    • 0026549946 scopus 로고
    • Clostridium difficile toxin A induces multinucleation in the human leukemic T cell line JURKAT
    • Fiorentini C, Chow SC, Mastrantonio P, et al. (1992): Clostridium difficile toxin A induces multinucleation in the human leukemic T cell line JURKAT. In Eur. J. Cell Biol. 57: 292-297.
    • (1992) In Eur. J. Cell Biol , vol.57 , pp. 292-297
    • Fiorentini, C.1    Chow, S.C.2    Mastrantonio, P.3
  • 34
    • 0027250397 scopus 로고
    • Clostridium difficile toxin A elicits Ca2+ -independent cytotoxic effects in cultured normal rat intestinal crypt cells
    • Fiorentini C, Donelli G, Nicotera P, et al. (1993): Clostridium difficile toxin A elicits Ca2+ -independent cytotoxic effects in cultured normal rat intestinal crypt cells. In Infect. Immun. 61: 3988-3993.
    • (1993) In Infect. Immun , vol.61 , pp. 3988-3993
    • Fiorentini, C.1    Donelli, G.2    Nicotera, P.3
  • 35
    • 0026047280 scopus 로고
    • Cytokine response by human monocytes to Clostridium difficile toxin A and toxin B
    • Flegel WA, Müller F, Däubener W, et al. (1991): Cytokine response by human monocytes to Clostridium difficile toxin A and toxin B. In Infect. Immun. 59: 3659-3666.
    • (1991) In Infect. Immun , vol.59 , pp. 3659-3666
    • Flegel, W.A.1    Müller, F.2    Däubener, W.3
  • 36
    • 0019454424 scopus 로고
    • Intoxication of cultured human lung fibroblasts with Clostridium difficile toxin
    • Florin I, Thelestam M (1981): Intoxication of cultured human lung fibroblasts with Clostridium difficile toxin. In Infect. Immun. 33: 67-74.
    • (1981) In Infect. Immun , vol.33 , pp. 67-74
    • Florin, I.1    Thelestam, M.2
  • 37
    • 0021108235 scopus 로고
    • Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts
    • Florin I, Thelestam M (1983): Internalization of Clostridium difficile cytotoxin into cultured human lung fibroblasts. In Biochim. Biophys. Acta, 763: 383-392.
    • (1983) In Biochim. Biophys. Acta , vol.763 , pp. 383-392
    • Florin, I.1    Thelestam, M.2
  • 38
    • 0022443783 scopus 로고
    • Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B
    • Florin I, Thelestam M (1986): Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B. In Microb. Pathogen. 1: 373-385.
    • (1986) In Microb. Pathogen , vol.1 , pp. 373-385
    • Florin, I.1    Thelestam, M.2
  • 39
    • 0026249159 scopus 로고
    • Isolation of a fibroblast mutant resistant to Clostridium difficile toxins A and B
    • Florin I (1991): Isolation of a fibroblast mutant resistant to Clostridium difficile toxins A and B. In Microb. Pathogen. 11: 337-346.
    • (1991) In Microb. Pathogen , vol.11 , pp. 337-346
    • Florin, I.1
  • 40
    • 0026057782 scopus 로고
    • ADP-ribosylation in Clostridium difficile toxin-treated cells is not related to cytopathogenicity of toxin B
    • Florin I, Thelestam M (1991): ADP-ribosylation in Clostridium difficile toxin-treated cells is not related to cytopathogenicity of toxin B. In Biochim. Biophys. Acta, 1091: 51-54.
    • (1991) In Biochim. Biophys. Acta , vol.1091 , pp. 51-54
    • Florin, I.1    Thelestam, M.2
  • 41
    • 0026764540 scopus 로고
    • Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A
    • Frey SM, Wilkins TD (1992): Localization of two epitopes recognized by monoclonal antibody PCG-4 on Clostridium difficile toxin A. In Infect. Immun. 60: 2488-2492.
    • (1992) In Infect. Immun , vol.60 , pp. 2488-2492
    • Frey, S.M.1    Wilkins, T.D.2
  • 42
  • 43
    • 0024599071 scopus 로고
    • Effect of purified Clostridium difficile toxins on intestinal smooth muscle
    • Gilbert RJ, Pothoulakis C, LaMont JT (1989b): Effect of purified Clostridium difficile toxins on intestinal smooth muscle. II. Toxin B. In Am. J. Physiol. 256: G767-G772.
    • (1989) II. Toxin B. In Am. J. Physiol , vol.256 , pp. G767-G772
    • Gilbert, R.J.1    Pothoulakis, C.2    LaMont, J.T.3
  • 44
    • 0028944568 scopus 로고
    • Clostridium difficile toxin B activates calcium influx required for actin disassembly during cytotoxicity
    • Gilbert RJ, Pothoulakis C, LaMont JT, et al. (1995): Clostridium difficile toxin B activates calcium influx required for actin disassembly during cytotoxicity. In Am. J. Physiol. 268: G487-G495.
    • (1995) In Am. J. Physiol , vol.268 , pp. G487-G495
    • Gilbert, R.J.1    Pothoulakis, C.2    LaMont, J.T.3
  • 45
    • 0029127708 scopus 로고
    • Transient expression of RhoA, -B, and -C GTPases in HeLa cells potentiates resistance to Clostridium difficile toxins A and B but not to Clostridium sordellii lethal toxin
    • Giry M, Popoff MR, Eichel-Streiber Cv, et al. (1995): Transient expression of RhoA, -B, and -C GTPases in HeLa cells potentiates resistance to Clostridium difficile toxins A and B but not to Clostridium sordellii lethal toxin. In Infect Immun. 63: 4063-4071.
    • (1995) In Infect Immun , vol.63 , pp. 4063-4071
    • Giry, M.1    Popoff, M.R.2    Eichel-Streiber, C.V.3
  • 46
    • 0029102111 scopus 로고
    • Cloning and characterization of the cytotoxin L-encoding gene of Clostridium sordellii: Homology with Clostridium difficile cytotoxin B
    • Green GA, Schué V, Monteil H (1995): Cloning and characterization of the cytotoxin L-encoding gene of Clostridium sordellii: homology with Clostridium difficile cytotoxin B. In Gene, 161: 57-61.
    • (1995) In Gene , vol.161 , pp. 57-61
    • Green, G.A.1    Schué, V.2    Monteil, H.3
  • 47
    • 0000795948 scopus 로고
    • Intestinal flora in new-born infants with a description of a new pathogenic anaerobe Bacillus difficilis
    • Hall JC, O'Toole E (1935): Intestinal flora in new-born infants with a description of a new pathogenic anaerobe Bacillus difficilis. In Am J. Dis. Child. 49: 390-402.
    • (1935) In Am J. Dis. Child , vol.49 , pp. 390-402
    • Hall, J.C.1    O'Toole, E.2
  • 48
    • 0024204607 scopus 로고
    • Clostridium difficile toxin A perturbs cytoskeletal structure and tight juncion permeability of cultured human intestinal epithelial monolayers
    • Hecht G, Pothoulakis C, LaMont JT, et al. (1988): Clostridium difficile toxin A perturbs cytoskeletal structure and tight juncion permeability of cultured human intestinal epithelial monolayers. In J. Clin. Invest. 82: 1516-1524.
    • (1988) In J. Clin. Invest , vol.82 , pp. 1516-1524
    • Hecht, G.1    Pothoulakis, C.2    LaMont, J.T.3
  • 49
    • 0026577118 scopus 로고
    • Clostridium difficile toxin B disrupts the barrier function of T84 monolayers
    • Hecht G, Koutsouris A, Pothoulakis C, et al. (1992): Clostridium difficile toxin B disrupts the barrier function of T84 monolayers. In Gastroenterology, 102: 416-423.
    • (1992) In Gastroenterology , vol.102 , pp. 416-423
    • Hecht, G.1    Koutsouris, A.2    Pothoulakis, C.3
  • 50
    • 0023269823 scopus 로고
    • Cellular internalization of Clostridium difficile toxin A
    • Henriques B, Florin I, Thelestam M (1987): Cellular internalization of Clostridium difficile toxin A. In Microb. Pathogen. 2: 455-463.
    • (1987) In Microb. Pathogen , vol.2 , pp. 455-463
    • Henriques, B.1    Florin, I.2    Thelestam, M.3
  • 51
    • 0029027683 scopus 로고
    • Sequencing and analysis of the gene encoding the alpha-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile
    • Hofmann F, Herrmann A, Habermann E, et al. (1995): Sequencing and analysis of the gene encoding the alpha-toxin of Clostridium novyi proves its homology to toxins A and B of Clostridium difficile. In Mol Gen Genet, 247: 670-679.
    • (1995) In Mol Gen Genet , vol.247 , pp. 670-679
    • Hofmann, F.1    Herrmann, A.2    Habermann, E.3
  • 52
    • 0028177598 scopus 로고
    • Clostridium difficile toxin B acts on the GTP-binding protein Rho
    • Just I, Fritz G, Aktories K, et al. (1994a): Clostridium difficile toxin B acts on the GTP-binding protein Rho. In J. Biol. Chem. 269: 10706-10712.
    • (1994) In J. Biol. Chem , vol.269 , pp. 10706-10712
    • Just, I.1    Fritz, G.2    Aktories, K.3
  • 53
    • 0028283571 scopus 로고
    • Probing the action of Clostridium difficile toxin B in Xenopus laevis oocytes
    • Just I, Richter H-P, Prepens U, et al. (1994b): Probing the action of Clostridium difficile toxin B in Xenopus laevis oocytes. In J. Cell Sci. 107: 1653-1659.
    • (1994) In J. Cell Sci , vol.107 , pp. 1653-1659
    • Just, I.1    Richter, H.-P.2    Prepens, U.3
  • 54
    • 0028948208 scopus 로고
    • The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile
    • Just I, Selzer J, Eichel-Streiber Cv, et al. (1995a): The low molecular mass GTP-binding protein Rho is affected by toxin A from Clostridium difficile. In J. Clin. Invest. 95: 1026-1031.
    • (1995) In J. Clin. Invest , vol.95 , pp. 1026-1031
    • Just, I.1    Selzer, J.2    Eichel-Streiber, C.V.3
  • 55
    • 0029054398 scopus 로고
    • Glucosylation of Rho proteins by Clostridium difficile toxin B
    • Just I, Selzer J, Wilm M, et al. (1995b): Glucosylation of Rho proteins by Clostridium difficile toxin B. In Nature, 375: 500-503.
    • (1995) In Nature , vol.375 , pp. 500-503
    • Just, I.1    Selzer, J.2    Wilm, M.3
  • 56
    • 0029011449 scopus 로고
    • The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
    • Just I, Wilm M, Selzer J, et al. (1995c): The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. In J. Biol. Chem. 270: 13932-13936.
    • (1995) In J. Biol. Chem , vol.270 , pp. 13932-13936
    • Just, I.1    Wilm, M.2    Selzer, J.3
  • 57
    • 0024440715 scopus 로고
    • Purification and characterisation of Clostridium difficile toxin A by bovine thyroglobulin affinity chromatography and dissociation in denaturing conditions with or without reduction
    • Kamiya S, Reed PJ, Borriello SP (1989): Purification and characterisation of Clostridium difficile toxin A by bovine thyroglobulin affinity chromatography and dissociation in denaturing conditions with or without reduction. In J. Med. Microbiol. 30: 69-77.
    • (1989) In J. Med. Microbiol , vol.30 , pp. 69-77
    • Kamiya, S.1    Reed, P.J.2    Borriello, S.P.3
  • 58
    • 0028787845 scopus 로고
    • Microbial recognition of target-cell glycoconjugates
    • Karlsson K-A (1995): Microbial recognition of target-cell glycoconjugates. In Curr. Opin. Struct. Biol. 5: 622-635.
    • (1995) In Curr. Opin. Struct. Biol , vol.5 , pp. 622-635
    • Karlsson, K.-A.1
  • 59
    • 0028316383 scopus 로고
    • Neutrophil recruitment in Clostridium difficile toxin A enteritis in the rabbit
    • Kelly CP, Becker S, Linevsky JK, et al. (1994): Neutrophil recruitment in Clostridium difficile toxin A enteritis in the rabbit. In J. Clin. Invest. 93: 1257-1265.
    • (1994) In J. Clin. Invest , vol.93 , pp. 1257-1265
    • Kelly, C.P.1    Becker, S.2    Linevsky, J.K.3
  • 60
    • 0022525082 scopus 로고
    • Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Galalpha1-3Galbeta1-4GlcNAc
    • Krivan HC, Clark GF, Smith DF, et al. (1986): Cell surface binding site for Clostridium difficile enterotoxin: Evidence for a glycoconjugate containing the sequence Galalpha1-3Galbeta1-4GlcNAc. In Infect. Immun. 53: 573-581.
    • (1986) In Infect. Immun , vol.53 , pp. 573-581
    • Krivan, H.C.1    Clark, G.F.2    Smith, D.F.3
  • 61
    • 0027943207 scopus 로고
    • Clostridium difficile toxin A-induced microvascular dysfunction. Role of histamine
    • Kurose I, Pothoulakis C, LaMont JT, et al. (1994): Clostridium difficile toxin A-induced microvascular dysfunction. Role of histamine, In J. Clin. Invest. 94: 1919-1926.
    • (1994) In J. Clin. Invest , vol.94 , pp. 1919-1926
    • Kurose, I.1    Pothoulakis, C.2    LaMont, J.T.3
  • 62
    • 0024366515 scopus 로고
    • Effect of Clostridium difficile enterotoxin A on ultrastructure of Chinese hamster ovary cells
    • Kushnaryov VM, Sedmak JJ (1989): Effect of Clostridium difficile enterotoxin A on ultrastructure of Chinese hamster ovary cells. In Infect. Immun. 57: 3914-3921.
    • (1989) In Infect. Immun , vol.57 , pp. 3914-3921
    • Kushnaryov, V.M.1    Sedmak, J.J.2
  • 63
    • 0026793251 scopus 로고
    • Cytotoxicity of Clostridium difficile toxin A for human colonic and pancreatic carcinoma cell lines
    • Kushnaryov VM, Redlich PN, Sedmak JJ, et al. (1992): Cytotoxicity of Clostridium difficile toxin A for human colonic and pancreatic carcinoma cell lines. In Cancer Res. 52: 5096-5099.
    • (1992) In Cancer Res , vol.52 , pp. 5096-5099
    • Kushnaryov, V.M.1    Redlich, P.N.2    Sedmak, J.J.3
  • 64
    • 0017744946 scopus 로고
    • Undescribed toxin in pseudomembranous colitis
    • Larson HE, Parry JV, Price AB, et al. (1977): Undescribed toxin in pseudomembranous colitis. In Brit. Med. J. 1: 1246-1248.
    • (1977) In Brit. Med. J , vol.1 , pp. 1246-1248
    • Larson, H.E.1    Parry, J.V.2    Price, A.B.3
  • 65
    • 0020066824 scopus 로고
    • Production of antitoxins to two toxins of Clostridium difficile and immunological comparison of the toxins by cross-neutralization studies
    • Libby JM, Wilkins TD (1982): Production of antitoxins to two toxins of Clostridium difficile and immunological comparison of the toxins by cross-neutralization studies. In Infect. Immun. 35: 374-376.
    • (1982) In Infect. Immun , vol.35 , pp. 374-376
    • Libby, J.M.1    Wilkins, T.D.2
  • 66
    • 0020029308 scopus 로고
    • Effects of the two toxins of Clostridium difficile in antibiotic-associated cecitis in hamsters
    • Libby JM, Jortner BS, Wilkins TD (1982): Effects of the two toxins of Clostridium difficile in antibiotic-associated cecitis in hamsters. In Infect. Immun. 36: 822-829.
    • (1982) In Infect. Immun , vol.36 , pp. 822-829
    • Libby, J.M.1    Jortner, B.S.2    Wilkins, T.D.3
  • 67
    • 0023852615 scopus 로고
    • Effects of Clostridium difficile toxins A and B in rabbit small and large intestine in vivo and on cultured cells in vitro
    • Lima AA, Lyerly DM, Wilkins TD, et al. (1988): Effects of Clostridium difficile toxins A and B in rabbit small and large intestine in vivo and on cultured cells in vitro. In Infect. Immun. 56: 582-588.
    • (1988) In Infect. Immun , vol.56 , pp. 582-588
    • Lima, A.A.1    Lyerly, D.M.2    Wilkins, T.D.3
  • 68
    • 0024427674 scopus 로고
    • Clostridium difficile toxin A. Interaction with mucus and early sequential histopathologic effects in rabbit small intestine
    • Lima AA, Innes DJ, Chadee K, et al. (1989): Clostridium difficile toxin A. Interaction with mucus and early sequential histopathologic effects in rabbit small intestine. In Lab. Invest. 61: 419-425.
    • (1989) In Lab. Invest , vol.61 , pp. 419-425
    • Lima, A.A.1    Innes, D.J.2    Chadee, K.3
  • 69
    • 0021995801 scopus 로고
    • Effects of Clostridium difficile toxins given intragastrically to animals
    • Lyerly DM, Saum KE, MacDonald DK, et al. (1985): Effects of Clostridium difficile toxins given intragastrically to animals. In Infect. Immun. 47: 349-352.
    • (1985) In Infect. Immun , vol.47 , pp. 349-352
    • Lyerly, D.M.1    Saum, K.E.2    MacDonald, D.K.3
  • 70
    • 0022655836 scopus 로고
    • Purification and properties of toxins A and B of Clostridium difficile
    • Lyerly DM, Roberts MD, Phelps CJ, et al. (1986): Purification and properties of toxins A and B of Clostridium difficile. In FEMS Microbiol. Lett. 33: 31-35.
    • (1986) In FEMS Microbiol. Lett , vol.33 , pp. 31-35
    • Lyerly, D.M.1    Roberts, M.D.2    Phelps, C.J.3
  • 72
    • 10544224329 scopus 로고
    • Susceptibility of Clostridium difficile toxins A and B to trypsin and chymotrypsin
    • Lyerly DM, Carrig PE, Wilkins TD (1989): Susceptibility of Clostridium difficile toxins A and B to trypsin and chymotrypsin. In Microb. Ecol. Health & Dis. 2: 219-221.
    • (1989) In Microb. Ecol. Health & Dis , vol.2 , pp. 219-221
    • Lyerly, D.M.1    Carrig, P.E.2    Wilkins, T.D.3
  • 73
    • 0002011582 scopus 로고
    • Clostridium difficile
    • (Blaser MJ, Smith PD, Ravdin JI, et al. eds) New York: Raven Press, Ltd
    • Lyerly DM, Wilkins TD (1995): Clostridium difficile. In Infections of the gastrointestinal tract (Blaser MJ, Smith PD, Ravdin JI, et al. eds) pp 867-891, New York: Raven Press, Ltd
    • (1995) In Infections of the gastrointestinal tract , pp. 867-891
    • Lyerly, D.M.1    Wilkins, T.D.2
  • 74
    • 0025307343 scopus 로고
    • Surface blebbing and cytoskeletal changes induced in vitro by toxin B from Clostridium difficile: An immunochemical and ultrastructural study
    • Malorni W, Fiorentini C, Paradisi S, et al. (1990): Surface blebbing and cytoskeletal changes induced in vitro by toxin B from Clostridium difficile: An immunochemical and ultrastructural study. In Exp. Molec. Pathol. 52: 340-356.
    • (1990) In Exp. Molec. Pathol , vol.52 , pp. 340-356
    • Malorni, W.1    Fiorentini, C.2    Paradisi, S.3
  • 75
    • 0026565693 scopus 로고
    • Comparison of Clostridium sordellii toxins HT and LT with toxins A and B of C.difficile
    • Martinez RD, Wilkins TD (1992): Comparison of Clostridium sordellii toxins HT and LT with toxins A and B of C.difficile. In J. Med. Microbiol. 36: 30-36.
    • (1992) In J. Med. Microbiol , vol.36 , pp. 30-36
    • Martinez, R.D.1    Wilkins, T.D.2
  • 76
    • 0023923499 scopus 로고
    • Purification and characterization of toxin B from Clostridium difficile
    • Meador III J, Tweten RK (1988): Purification and characterization of toxin B from Clostridium difficile. In Infect. Immun. 56: 1708-1714.
    • (1988) In Infect. Immun , vol.56 , pp. 1708-1714
    • Meador, J.1    Tweten, R.K.2
  • 77
    • 0025061557 scopus 로고
    • C.difficile toxin A increases intestinal permeability and induces CI- secretion
    • Moore R, Pothoulakis C, LaMont JT, et al. (1990): C.difficile toxin A increases intestinal permeability and induces CI- secretion. In Am. J. Physiol. 259: G165-G172.
    • (1990) In Am. J. Physiol , vol.259 , pp. G165-G172
    • Moore, R.1    Pothoulakis, C.2    LaMont, J.T.3
  • 78
    • 0026777744 scopus 로고
    • Morphological changes of cultured endothelial cells after microinjection of toxins that act on the cytoskeleton
    • Müller H, Eichel-Streiber Cv, Habermann E (1992): Morphological changes of cultured endothelial cells after microinjection of toxins that act on the cytoskeleton. In Infect. Immun. 60: 3007-3010.
    • (1992) In Infect. Immun , vol.60 , pp. 3007-3010
    • Müller, H.1    Eichel-Streiber, C.V.2    Habermann, E.3
  • 79
    • 0028258943 scopus 로고
    • Rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells
    • Nishiyama T, Sasaki T, Takaishi K, et al. (1994): rac p21 is involved in insulin-induced membrane ruffling and rho p21 is involved in hepatocyte growth factor- and 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced membrane ruffling in KB cells. In Mol. Cell. Biol. 14: 2447-2456.
    • (1994) In Mol. Cell. Biol , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3
  • 80
    • 0028786658 scopus 로고
    • Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia
    • Nusrat A, Giry M, Turner JR, et al. (1995): Rho protein regulates tight junctions and perijunctional actin organization in polarized epithelia. In Proc. Natl. Acad. Sci. 92: 10629-10633.
    • (1995) In Proc. Natl. Acad. Sci , vol.92 , pp. 10629-10633
    • Nusrat, A.1    Giry, M.2    Turner, J.R.3
  • 81
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson MF, Ashworth A, Hall A (1995): An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. In Science, 269: 1270-1272.
    • (1995) In Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 82
    • 0023857099 scopus 로고
    • Clostridium difficile toxin B induces reorganization of actin, vinculin, and talin in cultured cells
    • Ottlinger ME, Lin S (1988): Clostridium difficile toxin B induces reorganization of actin, vinculin, and talin in cultured cells. In Exptl Cell Res. 174: 215-229.
    • (1988) In Exptl Cell Res , vol.174 , pp. 215-229
    • Ottlinger, M.E.1    Lin, S.2
  • 83
    • 0023747353 scopus 로고
    • Actin-specific ADP-ribosyl-transferase produced by a Clostridium difficile strain
    • Popoff MR, Rubin EJ, Gill DM, et al. (1988): Actin-specific ADP-ribosyl-transferase produced by a Clostridium difficile strain. In Infect. Immun. 56, 2299-2306.
    • (1988) In Infect. Immun , vol.56 , pp. 2299-2306
    • Popoff, M.R.1    Rubin, E.J.2    Gill, D.M.3
  • 84
    • 15844415779 scopus 로고    scopus 로고
    • Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation
    • Popoff MR, Chaves-Olarte E, Lemichez E., et al. (1996): Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. In J. Biol. Chem. 271, 10217-10224.
    • (1996) In J. Biol. Chem , vol.271 , pp. 10217-10224
    • Popoff, M.R.1    Chaves-Olarte, E.2    Lemichez, E.3
  • 85
    • 0023928894 scopus 로고
    • Clostridium difficile toxin A stimulates intracellular calcium release and chemotactic response in human granulocytes
    • Pothoulakis C, Sullivan R, Melnick DA, et al. (1988): Clostridium difficile toxin A stimulates intracellular calcium release and chemotactic response in human granulocytes. In J. Clin. Invest. 81: 1741-1745.
    • (1988) In J. Clin. Invest , vol.81 , pp. 1741-1745
    • Pothoulakis, C.1    Sullivan, R.2    Melnick, D.A.3
  • 86
    • 0028013431 scopus 로고
    • CP-96,345, a substance P antagonist, inhibits rat intestinal responses to Clostridium difficile toxin A but not cholera toxin
    • Pothoulakis C, Castagliuolo I, LaMont JT, et al. (1994): CP-96,345, a substance P antagonist, inhibits rat intestinal responses to Clostridium difficile toxin A but not cholera toxin. In Proc. Natl. Acad. Sci. 91: 947-951.
    • (1994) In Proc. Natl. Acad. Sci , vol.91 , pp. 947-951
    • Pothoulakis, C.1    Castagliuolo, I.2    LaMont, J.T.3
  • 87
    • 0005513303 scopus 로고
    • Cloning of the carbohydrate-binding portion of the toxin A gene of Clostridium difficile
    • Price SB, Phelps CJ, Wilkins TD, et al. (1987): Cloning of the carbohydrate-binding portion of the toxin A gene of Clostridium difficile. In Curr. Microbiol. 16: 55-60.
    • (1987) In Curr. Microbiol , vol.16 , pp. 55-60
    • Price, S.B.1    Phelps, C.J.2    Wilkins, T.D.3
  • 88
    • 0023144930 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells
    • Reuner KH, Presek P, Boschek CB, et al. (1987): Botulinum C2 toxin ADP-ribosylates actin and disorganizes the microfilament network in intact cells. In Eur. J. Cell Biol. 43: 134-140.
    • (1987) In Eur. J. Cell Biol , vol.43 , pp. 134-140
    • Reuner, K.H.1    Presek, P.2    Boschek, C.B.3
  • 89
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesion and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A (1992): The small GTP-binding protein rho regulates the assembly of focal adhesion and actin stress fibers in response to growth factors. In Cell, 70: 389-399.
    • (1992) In Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 90
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HF, Johnston CL, et al. (1992): The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. In Cell, 70: 401-410.
    • (1992) In Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3
  • 91
    • 0028935286 scopus 로고
    • Clostridium difficile toxin B is more potent than toxin A in damaging human colonic epithelium in vitro
    • Riegler M, Sedivy R, Pothoulakis C, et al. (1995): Clostridium difficile toxin B is more potent than toxin A in damaging human colonic epithelium in vitro. In J. Clin. Invest. 95: 2004-2011.
    • (1995) In J. Clin. Invest , vol.95 , pp. 2004-2011
    • Riegler, M.1    Sedivy, R.2    Pothoulakis, C.3
  • 92
    • 0017784215 scopus 로고
    • Antibiotic-induced colitis implication of a toxin neutralised by Clostridium sordellii antitoxin
    • Rifkin GD, Fekety FR, Silva J, et al. (1977): Antibiotic-induced colitis implication of a toxin neutralised by Clostridium sordellii antitoxin. In Lancet, ii: 1103-1106.
    • (1977) In Lancet , vol.2 , pp. 1103-1106
    • Rifkin, G.D.1    Fekety, F.R.2    Silva, J.3
  • 93
    • 0025324520 scopus 로고
    • Nucleotide sequence of Clostridium difficile toxin A
    • Sauerborn M, Eichel-Streiber Cv (1990): Nucleotide sequence of Clostridium difficile toxin A. In Nucl. Acids Res. 18: 1629-1630.
    • (1990) In Nucl. Acids Res , vol.18 , pp. 1629-1630
    • Sauerborn, M.1    Eichel-Streiber, C.V.2
  • 94
    • 84904460193 scopus 로고
    • Monoclonal antibodies discriminating between Clostridium difficile toxins A and B
    • (Freer J, Aitken R, Alouf JE, et al. eds) Stuttgart Jena New York: Gustav Fischer Verlag
    • Sauerborn M, Hegenbarth S, Laufenberg-Feldmann R, et al. (1994): Monoclonal antibodies discriminating between Clostridium difficile toxins A and B. In Bacterial protein toxins (Freer J, Aitken R, Alouf JE, et al. eds) pp 510-511, Stuttgart Jena New York: Gustav Fischer Verlag.
    • (1994) In Bacterial protein toxins , pp. 510-511
    • Sauerborn, M.1    Hegenbarth, S.2    Laufenberg-Feldmann, R.3
  • 95
    • 0027930435 scopus 로고
    • Hyperphosphorylation of calnexin, a chaperone protein, induced by Clostridium difficile cytotoxin
    • Schué V, Green GA, Girardot R, et al. (1994): Hyperphosphorylation of calnexin, a chaperone protein, induced by Clostridium difficile cytotoxin. In Biochem. Biophys. Res. Commun. 203: 22-28.
    • (1994) In Biochem. Biophys. Res. Commun , vol.203 , pp. 22-28
    • Schué, V.1    Green, G.A.2    Girardot, R.3
  • 96
    • 0027470176 scopus 로고
    • Different structural organization of Ras and Rho effector domains
    • Self AJ, Paterson HF, Hall A (1993): Different structural organization of Ras and Rho effector domains. In Oncogene, 8: 655-661.
    • (1993) In Oncogene , vol.8 , pp. 655-661
    • Self, A.J.1    Paterson, H.F.2    Hall, A.3
  • 97
    • 0025614767 scopus 로고
    • Microfilament-disrupting Clostridium difficile toxin B causes multinucleation of transformed cells but does not block capping of membrane Ig
    • Shoshan MC, Åman P, Skog S, et al. (1990): Microfilament-disrupting Clostridium difficile toxin B causes multinucleation of transformed cells but does not block capping of membrane Ig. In Eur. J. Cell Biol. 53: 357-363.
    • (1990) In Eur. J. Cell Biol , vol.53 , pp. 357-363
    • Shoshan, M.C.1    Åman, P.2    Skog, S.3
  • 98
    • 0027256675 scopus 로고
    • Activation of cellular phospholipase A2 by Clostridium difficile toxin B
    • Shoshan MC, Florin I, Thelestam M (1993a): Activation of cellular phospholipase A2 by Clostridium difficile toxin B. In J. Cell. Biochem. 52: 116-124.
    • (1993) In J. Cell. Biochem , vol.52 , pp. 116-124
    • Shoshan, M.C.1    Florin, I.2    Thelestam, M.3
  • 99
    • 0027284494 scopus 로고
    • Dithiothreitol generates an activated 250,000 mol.wt form of Clostridium difficile toxin B
    • Shoshan MC, Bergman T, Thelestam M, et al. (1993b): Dithiothreitol generates an activated 250,000 mol.wt form of Clostridium difficile toxin B. In Toxicon, 31: 845-852.
    • (1993) In Toxicon , vol.31 , pp. 845-852
    • Shoshan, M.C.1    Bergman, T.2    Thelestam, M.3
  • 100
    • 0027450371 scopus 로고
    • Effects of Clostridium difficile toxin B on human monocytes and macrophages: Possible relationship with cytoskeletal rearrangement
    • Siffert J-C, Baldacini O, Kuhry J-G, et al. (1993): Effects of Clostridium difficile toxin B on human monocytes and macrophages: possible relationship with cytoskeletal rearrangement. In Infect. Immun. 61: 1082-1090.
    • (1993) In Infect. Immun , vol.61 , pp. 1082-1090
    • Siffert, J.-C.1    Baldacini, O.2    Kuhry, J.-G.3
  • 101
    • 0020003645 scopus 로고
    • Purification and characterization of toxins A and B of Clostridium difficile
    • Sullivan NM, Pellet S, Wilkins TD (1982): Purification and characterization of toxins A and B of Clostridium difficile. In Infect. Immun. 35: 1032-1040.
    • (1982) In Infect. Immun , vol.35 , pp. 1032-1040
    • Sullivan, N.M.1    Pellet, S.2    Wilkins, T.D.3
  • 102
    • 0019119783 scopus 로고
    • Interaction of cytopathogenic toxin from Clostridium difficile with cells in tissue culture
    • Thelestam M, Brönnegård M (1980): Interaction of cytopathogenic toxin from Clostridium difficile with cells in tissue culture. In Scand. J. Infect. Dis. Suppl. 22: 16-29.
    • (1980) In Scand. J. Infect. Dis. Suppl , vol.22 , pp. 16-29
    • Thelestam, M.1    Brönnegård, M.2
  • 103
    • 0021674871 scopus 로고
    • Cytopathogenic action of Clostridium difficile toxins
    • Thelestam M, Florin I (1984): Cytopathogenic action of Clostridium difficile toxins. In J. Toxicol. Toxin Rev. 3:139-180.
    • (1984) In J. Toxicol. Toxin Rev , vol.3 , pp. 139-180
    • Thelestam, M.1    Florin, I.2
  • 104
    • 84901958318 scopus 로고
    • Toxins acting on the cytoskeleton
    • (Shier WT, Mebs D, eds) New York and Basel: Marcel Dekker, Inc
    • Thelestam M, Gross R (1990): Toxins acting on the cytoskeleton. In Handbook of toxinology (Shier WT, Mebs D, eds) pp 423-492, New York and Basel: Marcel Dekker, Inc.
    • (1990) In Handbook of toxinology , pp. 423-492
    • Thelestam, M.1    Gross, R.2
  • 105
    • 0024428291 scopus 로고
    • Comparative study of Clostridium difficile toxin A and cholera toxin in rabbit ileum
    • Triadafilopoulos G, Pothoulakis C, Weiss R, et al. (1989): Comparative study of Clostridium difficile toxin A and cholera toxin in rabbit ileum. In Gastroenterol. 97: 1186-1192.
    • (1989) In Gastroenterol , vol.97 , pp. 1186-1192
    • Triadafilopoulos, G.1    Pothoulakis, C.2    Weiss, R.3
  • 106
    • 0026078094 scopus 로고
    • Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y
    • Tucker KD, Wilkins TD (1991): Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. In Infect. Immun. 59: 73-78.
    • (1991) In Infect. Immun , vol.59 , pp. 73-78
    • Tucker, K.D.1    Wilkins, T.D.2
  • 107
    • 0021071642 scopus 로고
    • Ultrastructural effects of Clostridium difficile toxin B on smooth muscle cells and fibroblasts
    • Wedel N, Toselli P, Pothoulakis C, et al. (1983): Ultrastructural effects of Clostridium difficile toxin B on smooth muscle cells and fibroblasts. In Exptl Cell Res. 148: 413-422.
    • (1983) In Exptl Cell Res , vol.148 , pp. 413-422
    • Wedel, N.1    Toselli, P.2    Pothoulakis, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.