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Volumn 18, Issue , 2002, Pages 315-344

Bacterial toxins that modify the actin cytoskeleton

Author keywords

ADP ribosylation; Deamidation; Glycosylation; GTPase activating proteins; Guanine nucleotide exchange factors

Indexed keywords

ACTIN; ADENYLATE CYCLASE; BACTERIAL TOXIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RHO FACTOR; ADENOSINE TRIPHOSPHATE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0036437349     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.18.012502.134748     Document Type: Review
Times cited : (137)

References (155)
  • 3
    • 0024584734 scopus 로고
    • The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3
    • Aktories K, Braun U, Rosener S, Just I, Hall A. 1989. The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3. Biochem. Biophys. Res. Commun. 158:209-13
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 209-213
    • Aktories, K.1    Braun, U.2    Rosener, S.3    Just, I.4    Hall, A.5
  • 4
    • 0024341897 scopus 로고
    • Botulinum ADP-ribosyltransferase C3: A new tool to study low molecular weight GTP-binding proteins
    • Aktories K, Hall A. 1989. Botulinum ADP-ribosyltransferase C3: A new tool to study low molecular weight GTP-binding proteins. Trends Pharmacol. Sci. 10:415-18
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 415-418
    • Aktories, K.1    Hall, A.2
  • 5
    • 0023882163 scopus 로고
    • Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes
    • Aktories K, Rosener S, Blaschke U, Chhatwal GS. 1988. Botulinum ADP-ribosyltransferase C3. Purification of the enzyme and characterization of the ADP-ribosylation reaction in platelet membranes. Eur. J. Biochem. 172:445-50
    • (1988) Eur. J. Biochem. , vol.172 , pp. 445-450
    • Aktories, K.1    Rosener, S.2    Blaschke, U.3    Chhatwal, G.S.4
  • 6
    • 0033924259 scopus 로고    scopus 로고
    • Rho GTPases as targets of bacterial protein toxins
    • Aktories K, Schmidt G, Just I. 2000. Rho GTPases as targets of bacterial protein toxins. Biol. Chem. 381:421-26
    • (2000) Biol. Chem. , vol.381 , pp. 421-426
    • Aktories, K.1    Schmidt, G.2    Just, I.3
  • 7
    • 0032527805 scopus 로고    scopus 로고
    • Activation of RhoA and SAPK/JNK signalling pathways by the RhoA-specific exchange factor mNET1
    • Alberts AS, Treisman R. 1998. Activation of RhoA and SAPK/JNK signalling pathways by the RhoA-specific exchange factor mNET1. EMBO J. 17:4075-85
    • (1998) EMBO J. , vol.17 , pp. 4075-4085
    • Alberts, A.S.1    Treisman, R.2
  • 8
    • 0030035043 scopus 로고    scopus 로고
    • Identification of a putative target for Rho as the serine-threonine kinase protein kinase N
    • Amano M, Mukai H, Ono Y, Chihara K, Matsui T, et al. 1996. Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 271:648-50
    • (1996) Science , vol.271 , pp. 648-650
    • Amano, M.1    Mukai, H.2    Ono, Y.3    Chihara, K.4    Matsui, T.5
  • 9
    • 0035035193 scopus 로고    scopus 로고
    • YopE of Yersinia, a GAP for Rho GTPases, selectively modulates Rac-dependent actin structures in endothelial cells
    • Andor A, Trulzsch K, Essler M, Roggenkamp A, Wiedemann A, et al. 2001. YopE of Yersinia, a GAP for Rho GTPases, selectively modulates Rac-dependent actin structures in endothelial cells. Cell Microbiol. 3:301-10
    • (2001) Cell Microbiol. , vol.3 , pp. 301-310
    • Andor, A.1    Trulzsch, K.2    Essler, M.3    Roggenkamp, A.4    Wiedemann, A.5
  • 10
    • 0033215148 scopus 로고    scopus 로고
    • ADP-ribosylation of rho by C3 ribosyltransferase inhibits IL-2 production and sustained calcium influx in activated T cells
    • Angkachatchai V, Finkel TH. 1999. ADP-ribosylation of rho by C3 ribosyltransferase inhibits IL-2 production and sustained calcium influx in activated T cells. J. Immunol. 163:3819-25
    • (1999) J. Immunol. , vol.163 , pp. 3819-3825
    • Angkachatchai, V.1    Finkel, T.H.2
  • 11
    • 0027400947 scopus 로고
    • A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly
    • Aullo P, Giry M, Olsnes S, Popoff MR, Kocks C, Boquet P. 1993. A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly. EMBO J. 12:921-31
    • (1993) EMBO J. , vol.12 , pp. 921-931
    • Aullo, P.1    Giry, M.2    Olsnes, S.3    Popoff, M.R.4    Kocks, C.5    Boquet, P.6
  • 12
    • 0034074961 scopus 로고    scopus 로고
    • Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells
    • Bakshi CS, Singh VP, Wood MW, Jones PW, Wallis TS, Galyov EE. 2000. Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells. J. Bacteriol. 182:2341-44
    • (2000) J. Bacteriol. , vol.182 , pp. 2341-2344
    • Bakshi, C.S.1    Singh, V.P.2    Wood, M.W.3    Jones, P.W.4    Wallis, T.S.5    Galyov, E.E.6
  • 14
    • 0039003839 scopus 로고    scopus 로고
    • Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification
    • Barth H, Blocker D, Behlke J, Bergsma-Schutter W, Brisson A, et al. 2000. Cellular uptake of Clostridium botulinum C2 toxin requires oligomerization and acidification. J. Biol. Chem. 275:18704-11
    • (2000) J. Biol. Chem. , vol.275 , pp. 18704-18711
    • Barth, H.1    Blocker, D.2    Behlke, J.3    Bergsma-Schutter, W.4    Brisson, A.5
  • 15
    • 0032036388 scopus 로고    scopus 로고
    • The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin
    • Barth H, Hofmann F, Olenik C, Just I, Aktories K. 1998. The N-terminal part of the enzyme component (C2I) of the binary Clostridium botulinum C2 toxin interacts with the binding component C2II and functions as a carrier system for a Rho ADP-ribosylating C3-like fusion toxin. Infect. Immun. 66:1364-69
    • (1998) Infect. Immun. , vol.66 , pp. 1364-1369
    • Barth, H.1    Hofmann, F.2    Olenik, C.3    Just, I.4    Aktories, K.5
  • 16
    • 0033600856 scopus 로고    scopus 로고
    • Neosynthesis and activation of Rho by Escherichia coli cytotoxic necrotizing factor (CNF1) reverse cytopathic effects of ADP-ribosylated Rho
    • Barth H, Olenik C, Sehr P, Schmidt G, Aktories K, Meyer DK. 1999. Neosynthesis and activation of Rho by Escherichia coli cytotoxic necrotizing factor (CNF1) reverse cytopathic effects of ADP-ribosylated Rho. J. Biol. Chem. 274:27407-14
    • (1999) J. Biol. Chem. , vol.274 , pp. 27407-27414
    • Barth, H.1    Olenik, C.2    Sehr, P.3    Schmidt, G.4    Aktories, K.5    Meyer, D.K.6
  • 18
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop AL, Hall A. 2000. Rho GTPases and their effector proteins. Biochem. J. 2:241-55
    • (2000) Biochem. J. , vol.2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 19
    • 0033861270 scopus 로고    scopus 로고
    • The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence
    • Black DS, Bliska JB. 2000. The RhoGAP activity of the Yersinia pseudotuberculosis cytotoxin YopE is required for antiphagocytic function and virulence. Mol. Microbiol. 37:515-27
    • (2000) Mol. Microbiol. , vol.37 , pp. 515-527
    • Black, D.S.1    Bliska, J.B.2
  • 20
    • 0033791898 scopus 로고    scopus 로고
    • The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages
    • Black DS, Marie-Cardine A, Schraven B, Bliska JB. 2000. The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages. Cell Microbiol. 2:401-14
    • (2000) Cell Microbiol. , vol.2 , pp. 401-414
    • Black, D.S.1    Marie-Cardine, A.2    Schraven, B.3    Bliska, J.B.4
  • 21
    • 0029989699 scopus 로고    scopus 로고
    • Virulence factors and O groups of Escherichia coli isolates from patients with acute pyelonephritis, cystitis and asymptomatic bacteriuria
    • Blanco M, Blanco JE, Alonso MP, Blanco J. 1996. Virulence factors and O groups of Escherichia coli isolates from patients with acute pyelonephritis, cystitis and asymptomatic bacteriuria. Eur. J. Epidemiol. 12:191-98
    • (1996) Eur. J. Epidemiol. , vol.12 , pp. 191-198
    • Blanco, M.1    Blanco, J.E.2    Alonso, M.P.3    Blanco, J.4
  • 22
    • 0034866672 scopus 로고    scopus 로고
    • The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli
    • Boquet P. 2001. The cytotoxic necrotizing factor 1 (CNF1) from Escherichia coli. Toxicon 39:1673-80
    • (2001) Toxicon , vol.39 , pp. 1673-1680
    • Boquet, P.1
  • 23
    • 0034953089 scopus 로고    scopus 로고
    • Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1
    • Buetow L, Flatau G, Chiu K, Boquet P, Ghosh P. 2001. Structure of the Rho-activating domain of Escherichia coli cytotoxic necrotizing factor 1. Nat. Struct. Biol. 8:584-88
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 584-588
    • Buetow, L.1    Flatau, G.2    Chiu, K.3    Boquet, P.4    Ghosh, P.5
  • 24
    • 0032584665 scopus 로고    scopus 로고
    • A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins
    • Busch C, Hofmann F, Selzer J, Munro S, Jeckel D, Aktories K. 1998. A common motif of eukaryotic glycosyltransferases is essential for the enzyme activity of large clostridial cytotoxins. J. Biol. Chem. 273:19566-72
    • (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
  • 25
    • 0020658988 scopus 로고
    • Partial purification and characterization of an Escherichia coli toxic factor that induces morphological cell alterations
    • Caprioli A, Falbo V, Roda LG, Ruggeri FM, Zona C. 1983. Partial purification and characterization of an Escherichia coli toxic factor that induces morphological cell alterations. Infect. Immun. 39:1300-6
    • (1983) Infect. Immun. , vol.39 , pp. 1300-1306
    • Caprioli, A.1    Falbo, V.2    Roda, L.G.3    Ruggeri, F.M.4    Zona, C.5
  • 26
    • 0024449589 scopus 로고
    • The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells
    • Chardin P, Boquet P, Madaule P, Popoff MR, Rubin EJ, Gill DM. 1989. The mammalian G protein rhoC is ADP-ribosylated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8:1087-92
    • (1989) EMBO J. , vol.8 , pp. 1087-1092
    • Chardin, P.1    Boquet, P.2    Madaule, P.3    Popoff, M.R.4    Rubin, E.J.5    Gill, D.M.6
  • 27
    • 0030931082 scopus 로고    scopus 로고
    • Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells
    • Chaves-Olarte E, Weidmann M, Eichel-Streiber C, Thelestam M. 1997. Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells. J. Clin. Invest. 100:1734-41
    • (1997) J. Clin. Invest. , vol.100 , pp. 1734-1741
    • Chaves-Olarte, E.1    Weidmann, M.2    Eichel-Streiber, C.3    Thelestam, M.4
  • 28
    • 0025925037 scopus 로고
    • ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S
    • Coburn J, Gill DM. 1991. ADP-ribosylation of p21ras and related proteins by Pseudomonas aeruginosa exoenzyme S. Infect. Immun. 59:4259-62
    • (1991) Infect. Immun. , vol.59 , pp. 4259-4262
    • Coburn, J.1    Gill, D.M.2
  • 30
    • 0018582949 scopus 로고
    • Intracellular localization of the dermonecrotic toxin of Bordetella pertussis
    • Cowell JL, Hewlett EL, Manclark CR. 1979. Intracellular localization of the dermonecrotic toxin of Bordetella pertussis. Infect. Immun. 25:896-901
    • (1979) Infect. Immun. , vol.25 , pp. 896-901
    • Cowell, J.L.1    Hewlett, E.L.2    Manclark, C.R.3
  • 31
    • 0035040115 scopus 로고    scopus 로고
    • The GTPase Rac1 selectively regulates Salmonella invasion at the apical plasma membrane of polarized epithelial cells
    • Criss AK, Ahlgren DM, Jou TS, McCormick BA, Casanova JE. 2001. The GTPase Rac1 selectively regulates Salmonella invasion at the apical plasma membrane of polarized epithelial cells. J. Cell Sci. 114:1331-41
    • (2001) J. Cell Sci. , vol.114 , pp. 1331-1341
    • Criss, A.K.1    Ahlgren, D.M.2    Jou, T.S.3    McCormick, B.A.4    Casanova, J.E.5
  • 33
    • 0027434988 scopus 로고
    • Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease
    • de Paiva A, Ashton AC, Foran P, Schiavo G, Montecucco C, Dolly JO. 1993. Botulinum A like type B and tetanus toxins fulfils criteria for being a zinc-dependent protease. J. Neurochem. 61:2338-41
    • (1993) J. Neurochem. , vol.61 , pp. 2338-2341
    • De Paiva, A.1    Ashton, A.C.2    Foran, P.3    Schiavo, G.4    Montecucco, C.5    Dolly, J.O.6
  • 34
    • 0032480888 scopus 로고    scopus 로고
    • Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP
    • de Rooij J, Zwartkruis FJ, Verheijen MH, Cool RH, Nijman SM, et al. 1998. Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 396:74-77
    • (1998) Nature , vol.396 , pp. 74-77
    • De Rooij, J.1    Zwartkruis, F.J.2    Verheijen, M.H.3    Cool, R.H.4    Nijman, S.M.5
  • 35
    • 0035004612 scopus 로고    scopus 로고
    • AKAP signaling complexes at the cytoskeleton
    • Diviani D, Scott JD. 2001. AKAP signaling complexes at the cytoskeleton. J. Cell Sci. 114:1431-37
    • (2001) J. Cell Sci. , vol.114 , pp. 1431-1437
    • Diviani, D.1    Scott, J.D.2
  • 37
    • 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, et al. 1993. Induction of phagocytic behaviour in human epithelial cells by Escherichia coli cytotoxic necrotizing factor type 1. Mol. Microbiol. 9:1247-54
    • (1993) Mol. Microbiol. , vol.9 , pp. 1247-1254
    • Falzano, L.1    Fiorentini, C.2    Donelli, G.3    Michel, E.4    Kocks, C.5
  • 39
    • 0030851464 scopus 로고    scopus 로고
    • Escherichia coli cytotoxic necrotizing factor 1 (CNF1), a toxin that activates the Rho GTPase
    • Fiorentini C, Fabbri A, Flatau G, Donelli G, Matarrese P, et al. 1997. Escherichia coli cytotoxic necrotizing factor 1 (CNF1), a toxin that activates the Rho GTPase. J. Biol. Chem. 272:19532-37
    • (1997) J. Biol. Chem. , vol.272 , pp. 19532-19537
    • Fiorentini, C.1    Fabbri, A.2    Flatau, G.3    Donelli, G.4    Matarrese, P.5
  • 40
    • 0031795253 scopus 로고    scopus 로고
    • Rho-dependent cell spreading activated by E. coli cytotoxic necrotizing factor 1 hinders apoptosis in epithelial cells
    • Fiorentini C, Matarrese P, Straface E, Falzano L, Donelli G, et al. 1998. Rho-dependent cell spreading activated by E. coli cytotoxic necrotizing factor 1 hinders apoptosis in epithelial cells. Cell Death Differ. 5:921-29
    • (1998) Cell Death Differ. , vol.5 , pp. 921-929
    • Fiorentini, C.1    Matarrese, P.2    Straface, E.3    Falzano, L.4    Donelli, G.5
  • 41
    • 0035823591 scopus 로고    scopus 로고
    • SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell
    • Friebel A, Ilchmann H, Aepfelbacher M, Ehrbar K, Machleidt W, Hardt WD. 2001. SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell. J. Biol. Chem. 276:34035-40
    • (2001) J. Biol. Chem. , vol.276 , pp. 34035-34040
    • Friebel, A.1    Ilchmann, H.2    Aepfelbacher, M.3    Ehrbar, K.4    Machleidt, W.5    Hardt, W.D.6
  • 42
    • 0035182168 scopus 로고    scopus 로고
    • Surfing pathogens and the lessons learned for actin polymerization
    • Frischknecht F, Way M. 2001. Surfing pathogens and the lessons learned for actin polymerization. Trends Cell Biol. 11:30-38
    • (2001) Trends Cell Biol. , vol.11 , pp. 30-38
    • Frischknecht, F.1    Way, M.2
  • 43
    • 0031983624 scopus 로고    scopus 로고
    • The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton
    • Fu Y, Galán JE. 1998. The Salmonella typhimurium tyrosine phosphatase SptP is translocated into host cells and disrupts the actin cytoskeleton. Mol. Microbiol. 27:359-68
    • (1998) Mol. Microbiol. , vol.27 , pp. 359-368
    • Fu, Y.1    Galán, J.E.2
  • 44
    • 0033575956 scopus 로고    scopus 로고
    • A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion
    • Fu Y, Galán JE. 1999. A Salmonella protein antagonizes Rac-1 and Cdc42 to mediate host-cell recovery after bacterial invasion. Nature 401:293-97
    • (1999) Nature , vol.401 , pp. 293-297
    • Fu, Y.1    Galán, J.E.2
  • 45
    • 0026443094 scopus 로고
    • A zinc-protease specific domain in botulinum and tetanus neurotoxins
    • Fujii N, Kimura K, Yokosawa N, Tsuzuki K, Oguma K. 1992. A zinc-protease specific domain in botulinum and tetanus neurotoxins. Toxicon 30:1486-88
    • (1992) Toxicon , vol.30 , pp. 1486-1488
    • Fujii, N.1    Kimura, K.2    Yokosawa, N.3    Tsuzuki, K.4    Oguma, K.5
  • 46
    • 0034676002 scopus 로고    scopus 로고
    • In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin
    • Fullner KJ, Mekalanos JJ. 2000. In vivo covalent cross-linking of cellular actin by the Vibrio cholerae RTX toxin. EMBO J. 19:5315-23
    • (2000) EMBO J. , vol.19 , pp. 5315-5323
    • Fullner, K.J.1    Mekalanos, J.J.2
  • 47
    • 0033618308 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa exoenzyme S disrupts Ras-mediated signal transduction by inhibiting guanine nucleotide exchange factor-catalyzed nucleotide exchange
    • Ganesan AK, Vincent TS, Olson JC, Barbieri JT. 1999. Pseudomonas aeruginosa exoenzyme S disrupts Ras-mediated signal transduction by inhibiting guanine nucleotide exchange factor-catalyzed nucleotide exchange. J. Biol. Chem. 274:21823-29
    • (1999) J. Biol. Chem. , vol.274 , pp. 21823-21829
    • Ganesan, A.K.1    Vincent, T.S.2    Olson, J.C.3    Barbieri, J.T.4
  • 48
    • 0034444645 scopus 로고    scopus 로고
    • The arginine finger domain of ExoT contributes to actin cytoskeleton disruption and inhibition of internalization of Pseudomonas aeruginosa by epithelial cells and macrophages
    • Garrity-Ryan L, Kazmierczak B, Kowal R, Comolli J, Hauser A, Engel JN. 2000. The arginine finger domain of ExoT contributes to actin cytoskeleton disruption and inhibition of internalization of Pseudomonas aeruginosa by epithelial cells and macrophages. Infect. Immun. 68:7100-13
    • (2000) Infect. Immun. , vol.68 , pp. 7100-7113
    • Garrity-Ryan, L.1    Kazmierczak, B.2    Kowal, R.3    Comolli, J.4    Hauser, A.5    Engel, J.N.6
  • 50
    • 0030582768 scopus 로고    scopus 로고
    • Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii
    • Genth H, Hofmann F, Selzer J, Rex G, Aktories K, Just I. 1996. Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii. Biochem. Biophys. Res. Commun. 229:370-74
    • (1996) Biochem. Biophys. Res. Commun. , vol.229 , pp. 370-374
    • Genth, H.1    Hofmann, F.2    Selzer, J.3    Rex, G.4    Aktories, K.5    Just, I.6
  • 51
    • 0019952195 scopus 로고
    • Clostridium difficile and cytotoxin in feces of patients with antimicrobial agent-associated pseudomembranous colitis
    • George WL, Rolfe RD, Harding GK, Klein R, Putnam CW, Finegold SM. 1982. Clostridium difficile and cytotoxin in feces of patients with antimicrobial agent-associated pseudomembranous colitis. Infection 10:205-8
    • (1982) Infection , vol.10 , pp. 205-208
    • George, W.L.1    Rolfe, R.D.2    Harding, G.K.3    Klein, R.4    Putnam, C.W.5    Finegold, S.M.6
  • 52
    • 1842384421 scopus 로고
    • ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase
    • Gill DM, Meren R. 1978. ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase. Proc. Natl. Acad. Sci. USA 75:3050-54
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3050-3054
    • Gill, D.M.1    Meren, R.2
  • 53
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa is a GTPase-activating protein for Rho GTPases
    • Goehring U-M, Schmidt G, Pederson KJ, Aktories K, Barbieri JT. 1999. The N-terminal domain of Pseudomonas aeruginosa is a GTPase-activating protein for Rho GTPases. J. Biol. Chem. 274:36369-72
    • (1999) J. Biol. Chem. , vol.274 , pp. 36369-36372
    • Goehring, U.-M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 54
    • 0035199154 scopus 로고    scopus 로고
    • Actin-based motility of intracellular microbial pathogens
    • Goldberg MB. 2001. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65:595-626
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 595-626
    • Goldberg, M.B.1
  • 55
    • 0029056825 scopus 로고
    • Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility
    • Goldberg MB, Theriot JA. 1995. Shigella flexneri surface protein IcsA is sufficient to direct actin-based motility. Proc. Natl. Acad. Sci. USA 92:6572-76
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6572-6576
    • Goldberg, M.B.1    Theriot, J.A.2
  • 58
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall A, Nobes CD. 2000. Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton. Philos. Trans. R. Soc. London Ser. B 355:965-70
    • (2000) Philos. Trans. R. Soc. London Ser. B , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 59
    • 0032876380 scopus 로고    scopus 로고
    • Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex
    • Han S, Craig JA, Putnam CD, Carozzi NB, Tainer JA. 1999. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nat. Struct. Biol. 6:932-36
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 932-936
    • Han, S.1    Craig, J.A.2    Putnam, C.D.3    Carozzi, N.B.4    Tainer, J.A.5
  • 60
    • 0032577563 scopus 로고    scopus 로고
    • S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells
    • Hardt WD, Chen LM, Schuebel KE, Bustelo XR, Galán JE. 1998. S. typhimurium encodes an activator of Rho GTPases that induces membrane ruffling and nuclear responses in host cells. Cell 93:815-26
    • (1998) Cell , vol.93 , pp. 815-826
    • Hardt, W.D.1    Chen, L.M.2    Schuebel, K.E.3    Bustelo, X.R.4    Galán, J.E.5
  • 61
    • 0032568868 scopus 로고    scopus 로고
    • Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13
    • Hart MJ, Jiang X, Kozasa T, Roscoe W, Singer WD, et al. 1998. Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13. Science 280:2112-14
    • (1998) Science , vol.280 , pp. 2112-2114
    • Hart, M.J.1    Jiang, X.2    Kozasa, T.3    Roscoe, W.4    Singer, W.D.5
  • 63
    • 0033567985 scopus 로고    scopus 로고
    • Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella
    • Hayward RD, Koronakis V. 1999. Direct nucleation and bundling of actin by the SipC protein of invasive Salmonella. EMBO J. 18:4926-34
    • (1999) EMBO J. , vol.18 , pp. 4926-4934
    • Hayward, R.D.1    Koronakis, V.2
  • 64
    • 0032568834 scopus 로고    scopus 로고
    • Functional consequences of monoglucosylation of Ha-Ras at effector domain amino acid threonine 35
    • Herrmann 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. 273:16134-39
    • (1998) J. Biol. Chem. , vol.273 , pp. 16134-16139
    • Herrmann, C.1    Ahmadian, M.R.2    Hofmann, F.3    Just, I.4
  • 65
    • 0020535877 scopus 로고
    • Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin
    • Hewlett EL, Saner KT, Myers GA, Cowell JL, Guerrant RL. 1983. Induction of a novel morphological response in Chinese hamster ovary cells by pertussis toxin. Infect. Immun. 40:1198-203
    • (1983) Infect. Immun. , vol.40 , pp. 1198-1203
    • Hewlett, E.L.1    Saner, K.T.2    Myers, G.A.3    Cowell, J.L.4    Guerrant, R.L.5
  • 68
    • 0345504899 scopus 로고
    • Pseudomonas aeruginosa exoenzyme S: An adenosine diphosphate ribosyl-transferase distinct from toxin A
    • Iglewski BH, Sadoff J, Bjorn MJ, Maxwell ES. 1978. Pseudomonas aeruginosa exoenzyme S: An adenosine diphosphate ribosyl-transferase distinct from toxin A. Proc. Natl. Acad. Sci. USA 75:3211-15
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 3211-3215
    • Iglewski, B.H.1    Sadoff, J.2    Bjorn, M.J.3    Maxwell, E.S.4
  • 69
    • 0026099636 scopus 로고
    • Molecular cloning and sequencing of the epidermal cell differentiation inhibitor gene from Staphylococcus aureus
    • Inoue S, Sugai M, Murooka Y, Paik SY, Hong YM, et al. 1991. Molecular cloning and sequencing of the epidermal cell differentiation inhibitor gene from Staphylococcus aureus. Biochem. Biophys. Res. Commun. 174:459-64
    • (1991) Biochem. Biophys. Res. Commun. , vol.174 , pp. 459-464
    • Inoue, S.1    Sugai, M.2    Murooka, Y.3    Paik, S.Y.4    Hong, Y.M.5
  • 70
    • 0018911425 scopus 로고
    • Evidence that botulinum C2 toxin has two dissimilar components
    • Iwasaki M, Ohishi I, Sakaguchi G. 1980. Evidence that botulinum C2 toxin has two dissimilar components. Infect. Immun. 29:390-94
    • (1980) Infect. Immun. , vol.29 , pp. 390-394
    • Iwasaki, M.1    Ohishi, I.2    Sakaguchi, G.3
  • 71
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho
    • Jalink K, van Corven EJ, Hengeveld T, Morii N, Narumiya S, Moolenaar WH. 1994. Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein Rho. J. Cell Biol. 126:801-10
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    Van Corven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 72
    • 0027519408 scopus 로고
    • NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum
    • Jung M, Just I, van Damme J, Vandekerckhove J, Aktories K. 1993. NAD-binding site of the C3-like ADP-ribosyltransferase from Clostridium limosum. J. Biol. Chem. 268:23215-18
    • (1993) J. Biol. Chem. , vol.268 , pp. 23215-23218
    • Jung, M.1    Just, I.2    Van Damme, J.3    Vandekerckhove, J.4    Aktories, K.5
  • 73
    • 0028177598 scopus 로고
    • Clostridium difficile toxin B acts on the GTP-binding protein Rho
    • Just I, Fritz G, Aktories K, Giry M, Popoff MR, et al. 1994. Clostridium difficile toxin B acts on the GTP-binding protein Rho. J. Biol. Chem. 269:10706-12
    • (1994) J. Biol. Chem. , vol.269 , pp. 10706-10712
    • Just, I.1    Fritz, G.2    Aktories, K.3    Giry, M.4    Popoff, M.R.5
  • 74
    • 0026773213 scopus 로고
    • ADP-ribosylation of small GTP-binding proteins by Bacillus cereus
    • Just I, Schallehn G, Aktories K. 1992. ADP-ribosylation of small GTP-binding proteins by Bacillus cereus. Biochem. Biophys. Res. Commun. 183:931-36
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 931-936
    • Just, I.1    Schallehn, G.2    Aktories, K.3
  • 75
    • 0029925007 scopus 로고    scopus 로고
    • Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation
    • Just I, Selzer J, Hofmann F, Green GA, Aktories K. 1996. Inactivation of Ras by Clostridium sordellii lethal toxin-catalyzed glucosylation. J. Biol. Chem. 271:10149-53
    • (1996) J. Biol. Chem. , vol.271 , pp. 10149-10153
    • Just, I.1    Selzer, J.2    Hofmann, F.3    Green, G.A.4    Aktories, K.5
  • 77
    • 0029011449 scopus 로고
    • The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins
    • Just I, Wilm M, Selzer J, Rex G, von Eichel-Streiber C, et al. 1995b. The enterotoxin from Clostridium difficile (ToxA) monoglucosylates the Rho proteins. J. Biol. Chem. 270:13932-36
    • (1995) J. Biol. Chem. , vol.270 , pp. 13932-13936
    • Just, I.1    Wilm, M.2    Selzer, J.3    Rex, G.4    Von Eichel-Streiber, C.5
  • 78
    • 0033203232 scopus 로고    scopus 로고
    • Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals
    • Kalman D, Weiner OD, Goosney DL, Sedat JW, Finlay BB, et al. 1999. Enteropathogenic E. coli acts through WASP and Arp2/3 complex to form actin pedestals. Nat. Cell Biol. 1:389-91
    • (1999) Nat. Cell Biol. , vol.1 , pp. 389-391
    • Kalman, D.1    Weiner, O.D.2    Goosney, D.L.3    Sedat, J.W.4    Finlay, B.B.5
  • 79
    • 0029839017 scopus 로고    scopus 로고
    • A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium
    • Kaniga K, Uralil J, Bliska JB, Galan JE. 1996. A secreted protein tyrosine phosphatase with modular effector domains in the bacterial pathogen Salmonella typhimurium. Mol. Microbiol. 21:633-41
    • (1996) Mol. Microbiol. , vol.21 , pp. 633-641
    • Kaniga, K.1    Uralil, J.2    Bliska, J.B.3    Galan, J.E.4
  • 81
    • 0026515440 scopus 로고
    • L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks C, Gouin E, Tabouret M, Berche P, Ohayon H, Cossart P. 1992. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68:521-31
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 82
    • 0032569051 scopus 로고    scopus 로고
    • p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13
    • Kozasa T, Jiang X, Hart MJ, Sternweis PM, Singer WD, et al. 1998. p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13. Science 280:2109-11
    • (1998) Science , vol.280 , pp. 2109-2111
    • Kozasa, T.1    Jiang, X.2    Hart, M.J.3    Sternweis, P.M.4    Singer, W.D.5
  • 83
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma R, Sarner S, Ahmed S, Lim L. 1997. Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell Biol. 17:1201-11
    • (1997) Mol. Cell Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 84
    • 0033796738 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa ExoT is a Rho GTPase-activating protein
    • Krall R, Schmidt G, Aktories K, Barbieri JT. 2000. Pseudomonas aeruginosa ExoT is a Rho GTPase-activating protein. Infect. Immun. 68:6066-48
    • (2000) Infect. Immun. , vol.68 , pp. 6066-6068
    • Krall, R.1    Schmidt, G.2    Aktories, K.3    Barbieri, J.T.4
  • 85
    • 0036137206 scopus 로고    scopus 로고
    • In vivo Rho GTPase-activating protein activity of Pseudomonas aeruginosa cytotoxin ExoS
    • Krall R, Sun JJ, Pederson KI, Barbieri JT. 2002. In vivo Rho GTPase-activating protein activity of Pseudomonas aeruginosa cytotoxin ExoS. Infect. Immun. 70:360-67
    • (2002) Infect. Immun. , vol.70 , pp. 360-367
    • Krall, R.1    Sun, J.J.2    Pederson, K.I.3    Barbieri, J.T.4
  • 86
    • 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. 1997. Molecular localization of the Escherichia coli cytotoxic necrotizing factor CNF1 cell-binding and catalytic domains. Mol. Microbiol. 24:1061-70
    • (1997) Mol. Microbiol. , vol.24 , pp. 1061-1070
    • Lemichez, E.1    Flatau, G.2    Bruzzone, M.3    Boquet, P.4    Gauthier, M.5
  • 87
    • 0033055636 scopus 로고    scopus 로고
    • Membrane traffic and the cellular uptake of cholera toxin
    • Lencer WI, Hirst TR, Holmes RK. 1999. Membrane traffic and the cellular uptake of cholera toxin. Biochim. Biophys. Acta 1450:177-90
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 177-190
    • Lencer, W.I.1    Hirst, T.R.2    Holmes, R.K.3
  • 88
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla SH. 1982. Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. USA 79:3162-66
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 89
    • 0021314377 scopus 로고
    • Bacillus anthracis calmodulin-dependent adenylate cyclase: Chemical and enzymatic properties and interactions with eucaryotic cells
    • Leppla SH. 1984. Bacillus anthracis calmodulin-dependent adenylate cyclase: Chemical and enzymatic properties and interactions with eucaryotic cells. Adv. Cycl. Nucleotide Protein Phosphorylation Res. 17:189-98
    • (1984) Adv. Cycl. Nucleotide Protein Phosphorylation Res. , vol.17 , pp. 189-198
    • Leppla, S.H.1
  • 90
    • 0032867338 scopus 로고    scopus 로고
    • Identification of the region of rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 (CNF1)
    • Lerm M, Schmidt G, Goehring UM, Schirmer J, Aktories K. 1999. Identification of the region of rho involved in substrate recognition by Escherichia coli cytotoxic necrotizing factor 1 (CNF1). J. Biol. Chem. 274:28999-9004
    • (1999) J. Biol. Chem. , vol.274 , pp. 28999-29004
    • Lerm, M.1    Schmidt, G.2    Goehring, U.M.3    Schirmer, J.4    Aktories, K.5
  • 91
    • 0035064654 scopus 로고    scopus 로고
    • The Salmonella spvB virulence gene encodes an enzyme that ADP-ribosylates actin and destabilizes the cytoskeleton of eukaryotic cells
    • Lesnick ML, Reiner NE, Fierer J, Guiney DG. 2001. The Salmonella spvB virulence gene encodes an enzyme that ADP-ribosylates actin and destabilizes the cytoskeleton of eukaryotic cells. Mol. Microbiol. 39:1464-70
    • (2001) Mol. Microbiol. , vol.39 , pp. 1464-1470
    • Lesnick, M.L.1    Reiner, N.E.2    Fierer, J.3    Guiney, D.G.4
  • 92
    • 0029147581 scopus 로고
    • A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit
    • Locht C, Antoine R. 1995. A proposed mechanism of ADP-ribosylation catalyzed by the pertussis toxin S1 subunit. Biochimie 77:333-40
    • (1995) Biochimie , vol.77 , pp. 333-340
    • Locht, C.1    Antoine, R.2
  • 94
    • 0035846909 scopus 로고    scopus 로고
    • Cytolysin-mediated translocation (CMT): A functional equivalent of type III secretion in gram-positive bacteria
    • Madden JC, Ruiz N, Caparon M. 2001. Cytolysin-mediated translocation (CMT): A functional equivalent of type III secretion in gram-positive bacteria. Cell 104: 143-52
    • (2001) Cell , vol.104 , pp. 143-152
    • Madden, J.C.1    Ruiz, N.2    Caparon, M.3
  • 95
    • 16844366239 scopus 로고    scopus 로고
    • Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme
    • Malcolm KC, Elliott CM, Exton JH. 1996. Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 271:13135-39
    • (1996) J. Biol. Chem. , vol.271 , pp. 13135-13139
    • Malcolm, K.C.1    Elliott, C.M.2    Exton, J.H.3
  • 96
    • 0034651790 scopus 로고    scopus 로고
    • Activation of rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin
    • Masuda M, Betancourt L, Matsuzawa T, Kashimoto T, Takao T, et al. 2000. Activation of rho through a cross-link with polyamines catalyzed by Bordetella dermonecrotizing toxin. EMBO J. 19:521-30
    • (2000) EMBO J. , vol.19 , pp. 521-530
    • Masuda, M.1    Betancourt, L.2    Matsuzawa, T.3    Kashimoto, T.4    Takao, T.5
  • 97
    • 0035341210 scopus 로고    scopus 로고
    • Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin
    • McGhie EJ, Hayward RD, Koronakis V. 2001. Cooperation between actin-binding proteins of invasive Salmonella: SipA potentiates SipC nucleation and bundling of actin. EMBO J. 20:2131-39
    • (2001) EMBO J. , vol.20 , pp. 2131-2139
    • McGhie, E.J.1    Hayward, R.D.2    Koronakis, V.3
  • 98
    • 0026503893 scopus 로고
    • ADP-ribosylation by Clostridium botulinum C3 exoenzyme increases steady-state GTPase activities of recombinant rhoA and rhoB proteins
    • Mohr C, Koch G, Just I, Aktories K. 1992. ADP-ribosylation by Clostridium botulinum C3 exoenzyme increases steady-state GTPase activities of recombinant rhoA and rhoB proteins. FEBS Lett. 297:95-99
    • (1992) FEBS Lett. , vol.297 , pp. 95-99
    • Mohr, C.1    Koch, G.2    Just, I.3    Aktories, K.4
  • 99
    • 0018289914 scopus 로고
    • NAD-dependent ADP-ribosylation of arginine and proteins by Escherichia coli heat-labile enterotoxin
    • Moss J, Garrison S, Oppenheimer NJ, Richardson SH. 1979. NAD-dependent ADP-ribosylation of arginine and proteins by Escherichia coli heat-labile enterotoxin. J. Biol. Chem. 254:6270-72
    • (1979) J. Biol. Chem. , vol.254 , pp. 6270-6272
    • Moss, J.1    Garrison, S.2    Oppenheimer, N.J.3    Richardson, S.H.4
  • 100
    • 0035968220 scopus 로고    scopus 로고
    • SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes
    • Mukherjee K, Parashuraman S, Raje M, Mukhopadhyay A. 2001. SopE acts as an Rab5-specific nucleotide exchange factor and recruits non-prenylated Rab5 on Salmonella-containing phagosomes to promote fusion with early endosomes. J. Biol. Chem. 276:23607-15
    • (2001) J. Biol. Chem. , vol.276 , pp. 23607-23615
    • Mukherjee, K.1    Parashuraman, S.2    Raje, M.3    Mukhopadhyay, A.4
  • 101
    • 0021004191 scopus 로고
    • Detection of Clostridium difficile cytotoxin in HEp-2 and CHO cell lines
    • Murray PR, Weber CJ. 1983. Detection of Clostridium difficile cytotoxin in HEp-2 and CHO cell lines. Diagn. Microbiol. Infect. Dis. 1:331-33
    • (1983) Diagn. Microbiol. Infect. Dis. , vol.1 , pp. 331-333
    • Murray, P.R.1    Weber, C.J.2
  • 102
    • 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, Kato M, Yaku H, 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. Mol. Cell Biol. 14:2447-56
    • (1994) Mol. Cell Biol. , vol.14 , pp. 2447-2456
    • Nishiyama, T.1    Sasaki, T.2    Takaishi, K.3    Kato, M.4    Yaku, H.5
  • 103
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multi-molecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multi-molecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 104
  • 105
    • 0018148047 scopus 로고
    • Assay method for Vibrio cholerae and Escherichia coli enterotoxins by automated counting of floating Chinese hamster ovary cells in culture medium
    • Nozawa RT, Yokota T, Kuwahara S. 1978. Assay method for Vibrio cholerae and Escherichia coli enterotoxins by automated counting of floating Chinese hamster ovary cells in culture medium. J. Clin. Microbiol. 7:479-85
    • (1978) J. Clin. Microbiol. , vol.7 , pp. 479-485
    • Nozawa, R.T.1    Yokota, T.2    Kuwahara, S.3
  • 106
    • 0023161694 scopus 로고
    • Activation of botulinum C2 toxin by trypsin
    • Ohishi I. 1987. Activation of botulinum C2 toxin by trypsin. Infect. Immun. 55:1461-65
    • (1987) Infect. Immun. , vol.55 , pp. 1461-1465
    • Ohishi, I.1
  • 107
    • 0022453775 scopus 로고
    • ADP-ribosylation of nonmuscle actin with component I of C2 toxin
    • Ohishi I, Tsuyama S. 1986. ADP-ribosylation of nonmuscle actin with component I of C2 toxin. Biochem. Biophys. Res. Commun. 136:802-6
    • (1986) Biochem. Biophys. Res. Commun. , vol.136 , pp. 802-806
    • Ohishi, I.1    Tsuyama, S.2
  • 108
    • 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. Science 269:1270-72
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 109
    • 0025195876 scopus 로고
    • Microinjection of recombinant p21rho induces rapid changes in cell morphology
    • Paterson Self AJ, Garrett MD, Just I, Aktories K, Hall A. 1990. Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111:1001-7
    • (1990) J. Cell Biol. , vol.111 , pp. 1001-1007
    • Paterson Self, A.J.1    Garrett, M.D.2    Just, I.3    Aktories, K.4    Hall, A.5
  • 110
    • 0032931551 scopus 로고    scopus 로고
    • The amino-terminal domain of Pseudomonas aeruginosa ExoS disrupts actin filaments via small-molecular-weight GTP-binding proteins
    • Pederson KJ, Vallis AJ, Aktories K, Frank DW, Barbieri JT. 1999. The amino-terminal domain of Pseudomonas aeruginosa ExoS disrupts actin filaments via small-molecular-weight GTP-binding proteins. Mol. Microbiol. 32:393-401
    • (1999) Mol. Microbiol. , vol.32 , pp. 393-401
    • Pederson, K.J.1    Vallis, A.J.2    Aktories, K.3    Frank, D.W.4    Barbieri, J.T.5
  • 111
    • 0034792596 scopus 로고    scopus 로고
    • Mutation of specific acidic residues of the CNF1 T domain into lysine alters cell membrane translocation of the toxin
    • Pei S, Doye A, Boquet P. 2001. Mutation of specific acidic residues of the CNF1 T domain into lysine alters cell membrane translocation of the toxin. Mol. Microbiol. 41:1237-47
    • (2001) Mol. Microbiol. , vol.41 , pp. 1237-1247
    • Pei, S.1    Doye, A.2    Boquet, P.3
  • 112
    • 0028117139 scopus 로고
    • The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton
    • Pistor S, Chakraborty T, Niebuhr K, Domann E, Wehland J. 1994. The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton. EMBO J. 13:758-63
    • (1994) EMBO J. , vol.13 , pp. 758-763
    • Pistor, S.1    Chakraborty, T.2    Niebuhr, K.3    Domann, E.4    Wehland, J.5
  • 113
    • 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, von Eichel-Streiber C, Thelestam M, et al. 1996. Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. J. Biol. Chem. 271:10217-24
    • (1996) J. Biol. Chem. , vol.271 , pp. 10217-10224
    • Popoff, M.R.1    Chaves-Olarte, E.2    Lemichez, E.3    Von Eichel-Streiber, C.4    Thelestam, M.5
  • 114
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley AJ. 2001. Rho family proteins: Coordinating cell responses. Trends Cell Biol. 11:471-77
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 115
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions 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 adhesions and actin stress fibers in response to growth factors. Cell 70:389-99
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 116
    • 0035020562 scopus 로고    scopus 로고
    • Mutation of the gene encoding cytotoxic necrotizing factor type 1 (cnf(1)) attenuates the virulence of uropathogenic Escherichia coli
    • Rippere-Lampe KE, O'Brien AD, Conran R, Lockman HA. 2001. Mutation of the gene encoding cytotoxic necrotizing factor type 1 (cnf(1)) attenuates the virulence of uropathogenic Escherichia coli. Infect. Immun. 69:3954-64
    • (2001) Infect. Immun. , vol.69 , pp. 3954-3964
    • Rippere-Lampe, K.E.1    O'Brien, A.D.2    Conran, R.3    Lockman, H.A.4
  • 117
    • 0024259821 scopus 로고
    • Relationships between the calmodulin-dependent adenylate cyclases produced by Bacillus anthracis and Bordetella pertussis
    • Robertson DL. 1988. Relationships between the calmodulin-dependent adenylate cyclases produced by Bacillus anthracis and Bordetella pertussis. Biochem. Biophys. Res. Commun. 157:1027-32
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 1027-1032
    • Robertson, D.L.1
  • 119
    • 0026041195 scopus 로고
    • Microinjection of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption
    • Rosqvist R, Forsberg A, Wolf-Watz H. 1991. Microinjection of the Yersinia YopE cytotoxin in mammalian cells induces actin microfilament disruption. Biochem. Soc. Trans. 19:1131-32
    • (1991) Biochem. Soc. Trans. , vol.19 , pp. 1131-1132
    • Rosqvist, R.1    Forsberg, A.2    Wolf-Watz, H.3
  • 120
    • 0023779031 scopus 로고
    • Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin EJ, Gill DM, Boquet P, Popoff MR. 1988. Functional modification of a 21-kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell Biol. 8:418-26
    • (1988) Mol. Cell Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 121
    • 0032748576 scopus 로고    scopus 로고
    • Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases
    • Rudolph MG, Weise C, Mirold S, Hillenbrand B, Bader B, et al. 1999. Biochemical analysis of SopE from Salmonella typhimurium, a highly efficient guanosine nucleotide exchange factor for RhoGTPases. J. Biol. Chem. 274: 30501-9
    • (1999) J. Biol. Chem. , vol.274 , pp. 30501-30509
    • Rudolph, M.G.1    Weise, C.2    Mirold, S.3    Hillenbrand, B.4    Bader, B.5
  • 122
    • 0030757509 scopus 로고    scopus 로고
    • Rho proteins play a critical role in cell migration during the early phase of mucosal restitution
    • Santos MF, McCormack SA, Guo Z, Okolicany J, Zheng Y, et al. 1997. Rho proteins play a critical role in cell migration during the early phase of mucosal restitution. J. Clin. Invest. 100: 216-25
    • (1997) J. Clin. Invest. , vol.100 , pp. 216-225
    • Santos, M.F.1    McCormack, S.A.2    Guo, Z.3    Okolicany, J.4    Zheng, Y.5
  • 123
    • 0023830603 scopus 로고
    • ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin
    • Schering B, Barmann M, Chhatwal GS, Geipel U, Aktories K. 1988. ADP-ribosylation of skeletal muscle and non-muscle actin by Clostridium perfringens iota toxin. Eur. J. Biochem. 171: 225-29
    • (1988) Eur. J. Biochem. , vol.171 , pp. 225-229
    • Schering, B.1    Barmann, M.2    Chhatwal, G.S.3    Geipel, U.4    Aktories, K.5
  • 124
    • 0033527746 scopus 로고    scopus 로고
    • Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for rho GTPases
    • Schmidt G, Goehring UM, Schirmer J, Lerm M, Aktories K. 1999. Identification of the C-terminal part of Bordetella dermonecrotic toxin as a transglutaminase for rho GTPases. J. Biol. Chem. 274: 31875-81
    • (1999) J. Biol. Chem. , vol.274 , pp. 31875-31881
    • Schmidt, G.1    Goehring, U.M.2    Schirmer, J.3    Lerm, M.4    Aktories, K.5
  • 125
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt G, Sehr P, Wilm M, Selzer J, Mann M, Aktories K. 1997. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature 387: 725-29
    • (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
  • 126
    • 0034862657 scopus 로고    scopus 로고
    • The toxins of Bacteroides fragilis
    • Sears CL. 2001. The toxins of Bacteroides fragilis. Toxicon 39: 1737-46
    • (2001) Toxicon , vol.39 , pp. 1737-1746
    • Sears, C.L.1
  • 127
    • 0032515914 scopus 로고    scopus 로고
    • Glucosylation and ADP ribosylation of rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling
    • Sehr P, Joseph G, Genth H, Just I, Pick E, Aktories K. 1998. Glucosylation and ADP ribosylation of rho proteins: Effects on nucleotide binding, GTPase activity, and effector coupling. Biochemistry 37: 5296-304
    • (1998) Biochemistry , vol.37 , pp. 5296-5304
    • Sehr, P.1    Joseph, G.2    Genth, H.3    Just, I.4    Pick, E.5    Aktories, K.6
  • 128
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine A, Fujiwara M, Narumiya S. 1989. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264: 8602-5
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 129
    • 0029823945 scopus 로고    scopus 로고
    • Clostridium novyi alphatoxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins
    • Selzer J, Hofmann F, Rex G, Wilm M, Mann M, et al. 1996. Clostridium novyi alphatoxin-catalyzed incorporation of GlcNAc into Rho subfamily proteins. J. Biol. Chem. 271: 25173-77
    • (1996) J. Biol. Chem. , vol.271 , pp. 25173-25177
    • Selzer, J.1    Hofmann, F.2    Rex, G.3    Wilm, M.4    Mann, M.5
  • 130
    • 0024846136 scopus 로고
    • The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects
    • Simpson LI. 1989, The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects. J. Pharmacol. Exp. Ther. 251: 1223-28
    • (1989) J. Pharmacol. Exp. Ther. , vol.251 , pp. 1223-1228
    • Simpson, L.I.1
  • 131
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory MP, Cornelis GR. 1994. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14: 583-94
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 132
    • 0033923731 scopus 로고    scopus 로고
    • Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell
    • Stender S, Friebel A, Linder S, Rohde M, Mirold S, Hardt WD. 2000. Identification of SopE2 from Salmonella typhimurium, a conserved guanine nucleotide exchange factor for Cdc42 of the host cell. Mol. Microbiol. 36: 1206-21
    • (2000) Mol. Microbiol. , vol.36 , pp. 1206-1221
    • Stender, S.1    Friebel, A.2    Linder, S.3    Rohde, M.4    Mirold, S.5    Hardt, W.D.6
  • 133
    • 0022993253 scopus 로고
    • Clostridium perfringens iota toxin: Synergism between two proteins
    • Stiles BG, Wilkins TD. 1986. Clostridium perfringens iota toxin: Synergism between two proteins. Toxicon 24: 767-73
    • (1986) Toxicon , vol.24 , pp. 767-773
    • Stiles, B.G.1    Wilkins, T.D.2
  • 134
    • 0024517923 scopus 로고
    • Differential clearance and host-pathogen interactions of YopE- and YopK- YopL-Yersinia pestis in BALB/c mice
    • Straley SC, Cibull ML. 1989. Differential clearance and host-pathogen interactions of YopE- and YopK- YopL-Yersinia pestis in BALB/c mice. Infect. Immun. 57: 1200-10
    • (1989) Infect. Immun. , vol.57 , pp. 1200-1210
    • Straley, S.C.1    Cibull, M.L.2
  • 135
    • 0020362248 scopus 로고
    • Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura M, Nogimori K, Murai S, Yajima M, Ito K, et al. 1982. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry 21: 5516-22
    • (1982) Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1    Nogimori, K.2    Murai, S.3    Yajima, M.4    Ito, K.5
  • 137
    • 0345593392 scopus 로고    scopus 로고
    • IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells
    • Tran Van Nhieu G, Caron E, Hall A, Sansonetti PJ. 1999. IpaC induces actin polymerization and filopodia formation during Shigella entry into epithelial cells. EMBO J. 18: 3249-62
    • (1999) EMBO J. , vol.18 , pp. 3249-3262
    • Tran Van Nhieu, G.1    Caron, E.2    Hall, A.3    Sansonetti, P.J.4
  • 138
    • 0018075438 scopus 로고
    • Mechanism of action of choleragen
    • Vaughan M, Moss J. 1978. Mechanism of action of choleragen. J. Supramol. Struct. 8: 473-88
    • (1978) J. Supramol. Struct. , vol.8 , pp. 473-488
    • Vaughan, M.1    Moss, J.2
  • 139
    • 0030993268 scopus 로고    scopus 로고
    • ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and shape changes of T-lymphoma cells
    • Verschueren H, De Baetselier P, De Braekeleer J, Dewit J, Aktories K, Just I. 1997. ADP-ribosylation of Rho-proteins with botulinum C3 exoenzyme inhibits invasion and shape changes of T-lymphoma cells. Eur. J. Cell Biol. 73: 182-87
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 182-187
    • Verschueren, H.1    De Baetselier, P.2    De Braekeleer, J.3    Dewit, J.4    Aktories, K.5    Just, I.6
  • 140
    • 0034283341 scopus 로고    scopus 로고
    • Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin
    • Vetter IR, Hofmann F, Wohlgemuth S, Herrmann C, Just I. 2000. Structural consequences of mono-glucosylation of Ha-Ras by Clostridium sordellii lethal toxin. J. Mol. Biol. 301: 1091-95
    • (2000) J. Mol. Biol. , vol.301 , pp. 1091-1095
    • Vetter, I.R.1    Hofmann, F.2    Wohlgemuth, S.3    Herrmann, C.4    Just, I.5
  • 142
    • 0034097414 scopus 로고    scopus 로고
    • GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: A mechanism for disruption of actin microfilament structure
    • Von Pawel-Rammingen U, Telepnev MV, Schmidt G, Aktories K, Wolf-Watz H, Rosqvist R. 2000. GAP activity of the Yersinia YopE cytotoxin specifically targets the Rho pathway: A mechanism for disruption of actin microfilament structure. Mol. Microbiol. 36: 737-48
    • (2000) Mol. Microbiol. , vol.36 , pp. 737-748
    • Von Pawel-Rammingen, U.1    Telepnev, M.V.2    Schmidt, G.3    Aktories, K.4    Wolf-Watz, H.5    Rosqvist, R.6
  • 143
    • 0023708116 scopus 로고
    • ADP-ribosylated actin caps the barbed ends of actin filaments
    • Wegner A, Aktories K. 1988. ADP-ribosylated actin caps the barbed ends of actin filaments. J. Biol. Chem. 263: 13739-42
    • (1988) J. Biol. Chem. , vol.263 , pp. 13739-13742
    • Wegner, A.1    Aktories, K.2
  • 144
    • 0031226057 scopus 로고    scopus 로고
    • Crystal structure of RhoA-GDP and its functional implications
    • Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, et al. 1997. Crystal structure of RhoA-GDP and its functional implications. Nat. Struct. Biol. 4: 699-703
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 699-703
    • Wei, Y.1    Zhang, Y.2    Derewenda, U.3    Liu, X.4    Minor, W.5
  • 145
    • 0033956166 scopus 로고    scopus 로고
    • Bordetella pertussis virulence factors affect phagocytosis by human neutrophils
    • Weingart CL, Weiss AA. 2000. Bordetella pertussis virulence factors affect phagocytosis by human neutrophils. Infect. Immun. 68: 1735-39
    • (2000) Infect. Immun. , vol.68 , pp. 1735-1739
    • Weingart, C.L.1    Weiss, A.A.2
  • 147
    • 0032493440 scopus 로고    scopus 로고
    • Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases
    • Wiggins CA, Munro S. 1998. Activity of the yeast MNN1 alpha-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. USA 95: 7945-50
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7945-7950
    • Wiggins, C.A.1    Munro, S.2
  • 148
    • 0035937815 scopus 로고    scopus 로고
    • A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3
    • Wilde C, Chhatwal GS, Schmalzing G, Aktories K, Just I. 2001. A novel C3-like ADP-ribosyltransferase from Staphylococcus aureus modifying RhoE and Rnd3. J. Biol. Chem. 276: 9537-42
    • (2001) J. Biol. Chem. , vol.276 , pp. 9537-9542
    • Wilde, C.1    Chhatwal, G.S.2    Schmalzing, G.3    Aktories, K.4    Just, I.5
  • 149
    • 0026584952 scopus 로고
    • ADP-ribosylation of gelsolin-actin complexes by clostridial toxins
    • Wille M, Just I, Wegner A, Aktories K. 1992. ADP-ribosylation of gelsolin-actin complexes by clostridial toxins. J. Biol. Chem. 267: 50-55
    • (1992) J. Biol. Chem. , vol.267 , pp. 50-55
    • Wille, M.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 150
    • 0029806327 scopus 로고    scopus 로고
    • SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a sip-dependent mechanism and promotes bacterial entry
    • Wood MW, Rosqvist R, Mullan PB, Edwards MH, Galyov EE. 1996. SopE, a secreted protein of Salmonella dublin, is translocated into the target eukaryotic cell via a sip-dependent mechanism and promotes bacterial entry. Mol. Microbiol. 22: 327-38
    • (1996) Mol. Microbiol. , vol.22 , pp. 327-338
    • Wood, M.W.1    Rosqvist, R.2    Mullan, P.B.3    Edwards, M.H.4    Galyov, E.E.5
  • 151
    • 0032440487 scopus 로고    scopus 로고
    • Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, Ecadherin
    • Wu S, Lim KC, Huang J, Saidi RF, Sears CL. 1998. Bacteroides fragilis enterotoxin cleaves the zonula adherens protein, Ecadherin. Proc. Natl. Acad. Sci. USA 95: 14979-84
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14979-14984
    • Wu, S.1    Lim, K.C.2    Huang, J.3    Saidi, R.F.4    Sears, C.L.5
  • 154
    • 0035147455 scopus 로고    scopus 로고
    • A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
    • Zhou D, Chen LM, Hernandez L, Shears SB, Galán JE. 2001. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Mol. Microbiol. 39: 248-59
    • (2001) Mol. Microbiol. , vol.39 , pp. 248-259
    • Zhou, D.1    Chen, L.M.2    Hernandez, L.3    Shears, S.B.4    Galán, J.E.5
  • 155
    • 0033605618 scopus 로고    scopus 로고
    • Role of the S. typhimurium actin-binding protein SipA in bacterial internalization
    • Zhou D, Mooseker MS, Galán JE. 1999. Role of the S. typhimurium actin-binding protein SipA in bacterial internalization. Science 283: 2092-95
    • (1999) Science , vol.283 , pp. 2092-2095
    • Zhou, D.1    Mooseker, M.S.2    Galán, J.E.3


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