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Volumn 2, Issue 3, 1999, Pages 185-194

Bacterial toxins modifying the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL TOXIN; BIOPOLYMER; BOTULINUM TOXIN; BOTULINUM TOXIN TYPE C; CADHERIN; CYTOTOXIC NECROTIZING FACTOR 1; CYTOTOXIC NECROTIZING FACTOR TYPE 2; CYTOTOXIN; ESCHERICHIA COLI PROTEIN; IOTA TOXIN, CLOSTRIDIUM PERFRINGENS; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0033187403     PISSN: 11396709     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (56)

References (58)
  • 1
    • 0030802038 scopus 로고    scopus 로고
    • Rhô proteins: Targets for bacterial toxins
    • Aktories K (1997) Rhô proteins: targets for bacterial toxins. Trends Microbiol 5:282-288
    • (1997) Trends Microbiol , vol.5 , pp. 282-288
    • Aktories, K.1
  • 2
    • 0032491480 scopus 로고    scopus 로고
    • Characterization of the catalytic site of the ADP-ribosyltransferase Closlridiwn bolulinwn C2 toxin by site-directed mutagenesis
    • Earth H, Preiss JC, Hofmann F, Aktories K (1998) Characterization of the catalytic site of the ADP-ribosyltransferase Closlridiwn bolulinwn C2 toxin by site-directed mutagenesis. J Biol Chem 273:29506-29511
    • (1998) J Biol Chem , vol.273 , pp. 29506-29511
    • Earth, H.1    Preiss, J.C.2    Hofmann, F.3    Aktories, K.4
  • 3
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherindependent cell-cell contacts
    • Braga VMM, Machesky LM, Hall A, Hotchin NA (1997) The small GTPases Rho and Rac are required for the establishment of cadherindependent cell-cell contacts. J Cell Biol 137:1421-1431
    • (1997) J Cell Biol , vol.137 , pp. 1421-1431
    • Vmm, B.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 4
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyllransferase is essential for the enzymatic activity of large clostridial cytotoxins
    • Busch C, Hofmann F, Selzer J, Munro S, Jeckel D, Aktories K (1998) A common motif of eukaryotic glycosyllransferase is essential for the enzymatic activity of large clostridial cytotoxins. J Biol Chem 273:19566-19572
    • (1998) J Biol Chem , vol.273 , pp. 19566-19572
    • Busch, C.1    Hofmann, F.2    Selzer, J.3    Munro, S.4    Jeckel, D.5    Aktories, K.6
  • 5
    • 0030921889 scopus 로고    scopus 로고
    • Bacteroides fragilis Toxin exhibits polar activity on monolayers of human intestinal epithelial cells (T84 cells) in vitro
    • Chambers FG, Koshy SS, Saidi RF, Clark DP, Moore R , Sears CL (1997) Bacteroides fragilis Toxin exhibits polar activity on monolayers of human intestinal epithelial cells (T84 cells) in vitro. Infect Immun 65:3561-3570
    • (1997) Infect Immun , vol.65 , pp. 3561-3570
    • Chambers, F.G.1    Koshy, S.S.2    Saidi, R.F.3    Clark, D.P.4    Moore, R.5    Sears, C.L.6
  • 6
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages
    • Domenighini M, Rappuoli R ( 1996) Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Mol Microbiol 21:667-674
    • (1996) Mol Microbiol , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 7
    • 0027363074 scopus 로고
    • Induction of phagocytic behaviour in human epithelial cells by Escherichia coli cytotoxic necrotizing factor type 1
    • Falzano L, Fiorentini C, Donelli G, Michel E, Kocks C, Cossart P, Oswald E, Boquet P (1993) Induction of phagocytic behaviour in human epithelial cells by Escherichia coli cytotoxic necrotizing factor type 1. Mol Microbiol 9:1247-1254
    • (1993) Mol Microbiol , vol.9 , pp. 1247-1254
    • Falzano, L.1    Fiorentini, C.2    Donelli, G.3    Michel, E.4    Kocks, C.5    Cossart, P.6    Oswald, E.7    Boquet, P.8
  • 10
    • 0031027277 scopus 로고    scopus 로고
    • Cloning and characterization of the Bacteroidesfragilis metalloprotease toxin gene
    • Franco AA, Mundy LM, Trucksis M, Wu S, Kaper JB, Sears CL (1997) Cloning and characterization of the Bacteroidesfragilis metalloprotease toxin gene. Infect Immun 65:1007-1013
    • (1997) Infect Immun , vol.65 , pp. 1007-1013
    • Franco, A.A.1    Mundy, L.M.2    Trucksis, M.3    Wu, S.4    Kaper, J.B.5    Sears, C.L.6
  • 11
    • 0030721443 scopus 로고    scopus 로고
    • Inhibition of RhoA translocation and calcium sensitization by in vivo ADP-ribosylation with the chimeric toxin DC3B
    • Fujihara H, Walker LA, Gong MC, Lemichez E, Boquet P, Somlyo AV, Somlyo AP (1997) Inhibition of RhoA translocation and calcium sensitization by in vivo ADP-ribosylation with the chimeric toxin DC3B. Mol Biol Cell 8:2437-2447
    • (1997) Mol Biol Cell , vol.8 , pp. 2437-2447
    • Fujihara, H.1    Walker, L.A.2    Gong, M.C.3    Lemichez, E.4    Boquet, P.5    Somlyo, A.V.6    Somlyo, A.P.7
  • 12
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localized at tight junctions with no sequence similarity to occludin
    • Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S (1998) Claudin-1 and -2: novel integral membrane proteins localized at tight junctions with no sequence similarity to occludin. J Cell Biol 7:1539-1550
    • (1998) J Cell Biol , vol.7 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 14
    • 0032412385 scopus 로고    scopus 로고
    • Activation of Rho GTPases by Escherichia coli cytotoxic necrotizing factor i increases intestinal permeability in CaCo-2 cells
    • Schmidt G, 1 lofmann F, Aktories K
    • Gerhard R, Schmidt G, 1 lofmann F, Aktories K ( 1998) Activation of Rho GTPases by Escherichia coli cytotoxic necrotizing factor I increases intestinal permeability in CaCo-2 cells. Infect Immun 66:5125-5131
    • (1998) Infect Immun , vol.66 , pp. 5125-5131
    • Gerhard, R.1
  • 15
    • 0030832145 scopus 로고    scopus 로고
    • Clostridium spiroforme toxin genes are related to C. pcrfringens iota toxin genes but have a different genomic localization
    • Gibert M, Perelle S, Daube G, Popoff MR (1997) Clostridium spiroforme toxin genes are related to C. pcrfringens iota toxin genes but have a different genomic localization. Syst Appl Microbiol 20:337-347
    • (1997) Syst Appl Microbiol , vol.20 , pp. 337-347
    • Gibert, M.1    Perelle, S.2    Daube, G.3    Popoff, M.R.4
  • 16
    • 0031695576 scopus 로고    scopus 로고
    • Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion
    • Gopalakrishhnan S, Raman N, AtMnson SJ, Marrs JA (1998) Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion. Am J Physiol 275:C798-C809
    • (1998) Am J Physiol , vol.275
    • Gopalakrishhnan, S.1    Raman, N.2    Atmnson, S.J.3    Marrs, J.A.4
  • 17
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A (1998) Rho GTPases and the actin cytoskeleton. Science 279:509-514
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 18
    • 0027521262 scopus 로고
    • Comparative analysis of C3 and botulinal neurotoxin genes and their environment in Closlridiiim boiulininn types C and D
    • Hauser D, Gibert M, Eklund MW, Boquet P, Popoff MR (1993) Comparative analysis of C3 and botulinal neurotoxin genes and their environment in Closlridiiim boiulininn types C and D. J Bacteriol 175:7260-7268
    • (1993) J Bacteriol , vol.175 , pp. 7260-7268
    • Hauser, D.1    Gibert, M.2    Eklund, M.W.3    Boquet, P.4    Popoff, M.R.5
  • 19
    • 0032568834 scopus 로고    scopus 로고
    • Functional consequences of monoglucosylation of Ha-Ras at effector domain amino acid threonine 35
    • Hermann C, Ahmadian MR, Hofmann F, Just I (1998) Functional consequences of monoglucosylation of Ha-Ras at effector domain amino acid threonine 35. J Biol Chem 273:16134-16139
    • (1998) J Biol Chem , vol.273 , pp. 16134-16139
    • Hermann, C.1    Ahmadian, M.R.2    Hofmann, F.3    Just, I.4
  • 20
    • 0031887901 scopus 로고    scopus 로고
    • Chimeric clostridial cytotoxins: Identification of the N-terminal region involved in protein substrate recognition
    • Hofmann F, Busch C, Aktories K (1998) Chimeric clostridial cytotoxins: identification of the N-terminal region involved in protein substrate recognition. Infect Immun 66:1076-1081
    • (1998) Infect Immun , vol.66 , pp. 1076-1081
    • Hofmann, F.1    Busch, C.2    Aktories, K.3
  • 21
    • 0030891386 scopus 로고    scopus 로고
    • Localization of the glucosyltransferase activity ot Clostridium difficile Toxin B to the N-terminal part of the holotoxin
    • Hofmann F, Busch C, Prepcns U, Just I, Aktories K (1997) Localization of the glucosyltransferase activity ot Clostridium difficile Toxin B to the N-terminal part of the holotoxin. J Biol Chem 272:11074-11078
    • (1997) J Biol Chem , vol.272 , pp. 11074-11078
    • Hofmann, F.1    Busch, C.2    Prepcns, U.3    Just, I.4    Aktories, K.5
  • 22
    • 0030611230 scopus 로고    scopus 로고
    • BorJctclla bronchisepiica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gin-63 of the GTP-binding protein Rho
    • Horiguchi Y, Inoue N, Masuda M, Kazshimoto T, Katahira J, Sugimoto N, Matsuda M (1997) BorJctclla bronchisepiica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gin-63 of the GTP-binding protein Rho. Proc Nail Acad Sei USA 94:11623-11626
    • (1997) Proc Nail Acad Sei USA , vol.94 , pp. 11623-11626
    • Horiguchi, Y.1    Inoue, N.2    Masuda, M.3    Kazshimoto, T.4    Katahira, J.5    Sugimoto, N.6    Matsuda, M.7
  • 23
    • 0031024431 scopus 로고    scopus 로고
    • Cloning and characterization of the gene for the metalloprotease enterotoxin of Bacteroidesfragilis
    • Kling JJ, Wright RL, Moncrief JS, Wilkins TD (1997) Cloning and characterization of the gene for the metalloprotease enterotoxin of Bacteroidesfragilis. FEMS Microbiol Lett 146:279-284
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 279-284
    • Kling, J.J.1    Wright, R.L.2    Moncrief, J.S.3    Wilkins, T.D.4
  • 24
    • 0029849199 scopus 로고    scopus 로고
    • Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroidesfragilis
    • Koshi SS, Montrose MH, Sears CL (1996) Human intestinal epithelial cells swell and demonstrate actin rearrangement in response to the metalloprotease toxin of Bacteroidesfragilis. Infect Immun 64:5022-5028
    • (1996) Infect Immun , vol.64 , pp. 5022-5028
    • Koshi, S.S.1    Montrose, M.H.2    Sears, C.L.3
  • 25
    • 0029947859 scopus 로고    scopus 로고
    • Regulation of receptor-mediated endocytosis by Rho and Rac
    • LamazeC, Chuang TH, Terlecky LJ, Bokoch GM, Schmid SL (1996) Regulation of receptor-mediated endocytosis by Rho and Rac. Nature 382:177-179
    • (1996) Nature , vol.382 , pp. 177-179
    • Chuang, T.H.1    Terlecky, L.J.2    Bokoch, G.M.3    Schmid, S.L.4
  • 26
    • 0030742773 scopus 로고    scopus 로고
    • Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains
    • Lemichez E, Flatau G, Bruzzone M, Boquet P, Gauthier M (1998) Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Mol Microbiol 24:1061-1070
    • (1998) Mol Microbiol , vol.24 , pp. 1061-1070
    • Lemichez, E.1    Flatau, G.2    Bruzzone, M.3    Boquet, P.4    Gauthier, M.5
  • 27
    • 0029089328 scopus 로고
    • Cytoskeletal regulation of Caco-2 intestinal monolayer paracellular permeability
    • Ma TY, Hollander D, Tran LT, Nguyen D, Hoa N, Bhalla D (1995) Cytoskeletal regulation of Caco-2 intestinal monolayer paracellular permeability. J Cell Physiol 164:533-545
    • (1995) J Cell Physiol , vol.164 , pp. 533-545
    • Ma, T.Y.1    Hollander, D.2    Tran, L.T.3    Nguyen, D.4    Hoa, N.5    Bhalla, D.6
  • 28
    • 0030222377 scopus 로고    scopus 로고
    • Rho: A connection between membrane receptor signaling and the cytoskeleton
    • Machesky LM, Hall A (1996) Rho: a connection between membrane receptor signaling and the cytoskeleton. Trends Cell Biol 6:304-310
    • (1996) Trends Cell Biol , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 30
    • 0032037637 scopus 로고    scopus 로고
    • Molecular characterization of the Fragilysin pathogenicity islet of enterotoxigenic Bacteroidesfragilis
    • Moncrief JS, Duncan AJ, Wright RL, Barroso LA, Wilkins TD (1998) Molecular characterization of the Fragilysin pathogenicity islet of enterotoxigenic Bacteroidesfragilis. Infect Immun 66:1735-1739
    • (1998) Infect Immun , vol.66 , pp. 1735-1739
    • Moncrief, J.S.1    Duncan, A.J.2    Wright, R.L.3    Barroso, L.A.4    Wilkins, T.D.5
  • 31
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya S (1996) The small GTPase Rho: cellular functions and signal transduction. J Biochem 120:215-228
    • (1996) J Biochem , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 34
    • 1842289171 scopus 로고    scopus 로고
    • The Bacteroidesfragilis toxin fragilysin disrupts the paracellular barrier of epithelial cells
    • Obiso RJ, Azghani AO, Wilkins TD (1997) The Bacteroidesfragilis toxin fragilysin disrupts the paracellular barrier of epithelial cells. Infect Immun 65:1431-1439
    • (1997) Infect Immun , vol.65 , pp. 1431-1439
    • Obiso, R.J.1    Azghani, A.O.2    Wilkins, T.D.3
  • 35
    • 0028231764 scopus 로고
    • Cylotoxic necrotizing factor type 2 produced by virulent Esclierichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers
    • Oswald E, Sugai M, Labigne A, Wu HC, Fiorcntini C, Boquet P, O'Brien AD (1994) Cylotoxic necrotizing factor type 2 produced by virulent Esclierichia coli modifies the small GTP-binding proteins Rho involved in assembly of actin stress fibers. Proc Nail Acad Sei (USA) 91:3814-3818
    • (1994) Proc Nail Acad Sei (USA) , vol.91 , pp. 3814-3818
    • Oswald, E.1    Sugai, M.2    Labigne, A.3    Wu, H.C.4    Fiorcntini, C.5    Boquet, P.6    O'Brien, A.D.7
  • 36
    • 0030597057 scopus 로고    scopus 로고
    • Evidence that Arg-295, Glu-378 and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin
    • Perelle S, Domenighini M, Popoff MR (1996) Evidence that Arg-295, Glu-378 and Glu-380 are active-site residues of the ADP-ribosyltransferase activity of iota toxin. FEES Lett 395:191-194
    • (1996) FEES Lett , vol.395 , pp. 191-194
    • Perelle, S.1    Domenighini, M.2    Popoff, M.R.3
  • 37
    • 0027365422 scopus 로고
    • Characterization of Clostridiiim perfringens Iota-toxin genes and expression in Esclierichia coli
    • Perelle S, Gibert M, Boquet P, Popoff MR (1993) Characterization of Clostridiiim perfringens Iota-toxin genes and expression in Esclierichia coli. Infect Immun 61:5147-5156 (Author's correction, 63:4967, 1995)
    • (1993) Infect Immun , vol.61 , pp. 5147-5156
    • Perelle, S.1    Gibert, M.2    Boquet, P.3    Popoff, M.R.4
  • 38
    • 0031004306 scopus 로고    scopus 로고
    • Production of a complete binary toxin (Actin-ADP-ribosylating toxin) by Clostridiiim difficile CD196
    • Perelle S, Gibert M, Bourlioux P, Corthier G, Popoff MR (1997) Production of a complete binary toxin (Actin-ADP-ribosylating toxin) by Clostridiiim difficile CD196. Infect Immun 65:1402-1407
    • (1997) Infect Immun , vol.65 , pp. 1402-1407
    • Perelle, S.1    Gibert, M.2    Bourlioux, P.3    Corthier, G.4    Popoff, M.R.5
  • 39
    • 0031016925 scopus 로고    scopus 로고
    • Immunological and functional comparison between Clostridiiim perfringens iota toxin, C. spiroforme toxin, and anthrax toxins
    • Perelle S, Scalzo S, Kochi S, Mock M, Popoff MR (1997) Immunological and functional comparison between Clostridiiim perfringens iota toxin, C. spiroforme toxin, and anthrax toxins. FEMS Microbiol Lett 146:117-121
    • (1997) FEMS Microbiol Lett , vol.146 , pp. 117-121
    • Perelle, S.1    Scalzo, S.2    Kochi, S.3    Mock, M.4    Popoff, M.R.5
  • 41
    • 0032496097 scopus 로고    scopus 로고
    • Interaction of bacterial toxins with intestinal cells
    • Popoff MR (1998) Interaction of bacterial toxins with intestinal cells. Toxicon 36:665-685
    • (1998) Toxicon , vol.36 , pp. 665-685
    • Popoff, M.R.1
  • 42
    • 15844415779 scopus 로고    scopus 로고
    • Ras, Rap, and Rac small GTPbinding proteins are targets for Clostridiiim sordellii lethal toxin glucosylation
    • Chaves-Olarte E, Lemichez E, Von Eichel-Streiber C, Thelestam M, Chardin P, Cussac D, Antonny B, Chavrier P, Flatau G, Giry M, de Gunzburg J, Boquet P
    • Popoff MR, Chaves-Olarte E, Lemichez E, Von Eichel-Streiber C, Thelestam M, Chardin P, Cussac D, Antonny B, Chavrier P, Flatau G, Giry M, de Gunzburg J, Boquet P (1996) Ras, Rap, and Rac small GTPbinding proteins are targets for Clostridiiim sordellii lethal toxin glucosylation. J Biol Chem 271:10217-10224
    • (1996) J Biol Chem , vol.271 , pp. 10217-10224
    • Popoff, M.R.1
  • 43
    • 0026044664 scopus 로고
    • Characterization of the C3 gene of Closlridiiim boliilinnm types C and D and its expression in Esclierichia coli
    • Hauser D, Boquet P, Eklund MW,.Gill DM
    • Popoff MR, Hauser D, Boquet P, Eklund MW,.Gill DM (1991) Characterization of the C3 gene of Closlridiiim boliilinnm types C and D and its expression in Esclierichia coli. Infect Immun 59:3673-3679
    • (1991) Infect Immun , vol.59 , pp. 3673-3679
    • Popoff, M.R.1
  • 45
    • 0032535359 scopus 로고    scopus 로고
    • Inhibition of small G proteins by Clostridiiim sordellii lethal toxin activates cdc2 and MAP kinase in Xcnopns oocytes
    • Rime H, Talbi N, Popoff MR, Suziedelis K, Fessus C, Ozon R (1998) Inhibition of small G proteins by Clostridiiim sordellii lethal toxin activates cdc2 and MAP kinase in Xcnopns oocytes. Dev Biol 204:592-602
    • (1998) Dev Biol , vol.204 , pp. 592-602
    • Rime, H.1    Talbi, N.2    Popoff, M.R.3    Suziedelis, K.4    Fessus, C.5    Ozon, R.6
  • 46
    • 0031004425 scopus 로고    scopus 로고
    • Bacteroides fragilis toxin rearranges the actin cytoskeleton of HT29/C1 cells without direct proteolysis of actin or decrease in F-actin content
    • Saidi RF, Jaeger K, Montrose MH, Wu S, Sears CL (1997) Bacteroides fragilis toxin rearranges the actin cytoskeleton of HT29/C1 cells without direct proteolysis of actin or decrease in F-actin content. Cell Mot Cytoskel 37:159-165
    • (1997) Cell Mot Cytoskel , vol.37 , pp. 159-165
    • Saidi, R.F.1    Jaeger, K.2    Montrose, M.H.3    Wu, S.4    Sears, C.L.5
  • 47
    • 0029809318 scopus 로고    scopus 로고
    • Bacteroides fragilis Toxin rapidly intoxicates human intestinal epithelial cells (HT29/C1) in vitro
    • Saidi RF, Sears CL (1996) Bacteroides fragilis Toxin rapidly intoxicates human intestinal epithelial cells (HT29/C1) in vitro. Infect Immun 64:5029-5034
    • (1996) Infect Immun , vol.64 , pp. 5029-5034
    • Saidi, R.F.1    Sears, C.L.2
  • 48
    • 0030610785 scopus 로고    scopus 로고
    • Gin 63 of Rho is deamidated by Eschcricliia coli cytotoxic necrotizing factor-1
    • Schmidt G, Sehr P, Wilm M, Selzer J, Mann M, Aktories K (1997) Gin 63 of Rho is deamidated by Eschcricliia coli cytotoxic necrotizing factor-1. Nature 387:725-729
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 51
    • 2642685577 scopus 로고    scopus 로고
    • Specific inhibition of phorbol ester-stimulated phospholipase D by Clostridiiim sordellii lethal toxin and Clostridiiim difficile toxin B-1470 in HEK-293 cells
    • Vos M.Thiel M, Bauer B, Grannas A, Tapp E, Cool RH, de Gunzburg J, von Eichel-Streiber C, Jakobs KH
    • Schmidt M, Vos M.Thiel M, Bauer B, Grannas A, Tapp E, Cool RH, de Gunzburg J, von Eichel-Streiber C, Jakobs KH (1998) Specific inhibition of phorbol ester-stimulated phospholipase D by Clostridiiim sordellii lethal toxin and Clostridiiim difficile toxin B-1470 in HEK-293 cells. J Biol Chem 273:7413-7422
    • (1998) J Biol Chem , vol.273 , pp. 7413-7422
    • Schmidt, M.1
  • 52
    • 0032515914 scopus 로고    scopus 로고
    • Glucosylation and ADP ribosylation of Rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • Sehr P, Gili J, Genth H, Just I, Pick E, Aklories K (1998) Glucosylation and ADP ribosylation of Rho proteins: effects on nucleotide binding, GTPase activity, and effector coupling. Biochemistry 37:5296-5304
    • (1998) Biochemistry , vol.37 , pp. 5296-5304
    • Sehr, P.1    Gili, J.2    Genth, H.3    Just, I.4    Pick, E.5    Aklories, K.6
  • 53
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H, Takai Y ( 1997) Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. JCellBiol 139:1047-1059
    • (1997) JCellBiol , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 54
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and CDC42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N, Hall A ( 1997) Rho, Rac and CDC42 GTPases regulate the organization of the actin cytoskeleton. Curr Biol 9:86-92
    • (1997) Curr Biol , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 55
    • 0030271882 scopus 로고    scopus 로고
    • Large clostridial cytotoxins-a family of glucosyltransferases modifying small GTP-binding proteins
    • von Eichel-Streiber C, Boquet P, Sauerborn M, Thelestam M (1996) Large clostridial cytotoxins-a family of glucosyltransferases modifying small GTP-binding proteins. Trends Microbiol 4:375-382
    • (1996) Trends Microbiol , vol.4 , pp. 375-382
    • Eichel-Streiber, C.1    Boquet, P.2    Sauerborn, M.3    Thelestam, M.4
  • 56
    • 0025896984 scopus 로고
    • A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences
    • Wren BW (1991) A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Mol Microbiol 5:797-803
    • (1991) Mol Microbiol , vol.5 , pp. 797-803
    • Wren, B.W.1
  • 57
    • 0032440487 scopus 로고    scopus 로고
    • Bactemidesfragilis entcrotoxin cleaves the zonula adherens protein, E-cadherin
    • Wu S, Urn KC, Huang J, Saidi RF, Sears CL ( 1998) Bactemidesfragilis entcrotoxin cleaves the zonula adherens protein, E-cadherin. Proc Nail Acad Sei USA 95:14979-14984
    • (1998) Proc Nail Acad Sei USA , vol.95 , pp. 14979-14984
    • Wu, S.1    Urn, K.C.2    Huang, J.3    Saidi, R.F.4    Sears, C.L.5
  • 58
    • 0030021649 scopus 로고    scopus 로고
    • Signal transduction and actin filament organization
    • Zigmond SH (1996) Signal transduction and actin filament organization. CurrOpn Cell Biol 8:66-73
    • (1996) CurrOpn Cell Biol , vol.8 , pp. 66-73
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.