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Volumn 12, Issue 9, 2014, Pages 599-611

Novel bacterial ADP-ribosylating toxins: Structure and function

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ADP RIBOSYLTRANSFERASE TOXIN; BACTERIAL TOXIN; BOTULINUM TOXIN; CHOLIX TOXIN; CYCLIC AMP; DIPHTHERIA TOXIN; EXOENZYME C3; PERTUSSIS TOXIN; RHO FACTOR; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

EID: 84906320189     PISSN: 17401526     EISSN: 17401534     Source Type: Journal    
DOI: 10.1038/nrmicro3310     Document Type: Review
Times cited : (177)

References (204)
  • 1
    • 0024584734 scopus 로고
    • The rho gene product expressed in E coli is a substrate of botulinum ADP-ribosyltransferase C3
    • Aktories, K., Braun, U., Rösener, S., Just, I. & Hall, A. The rho gene product expressed in E. coli is a substrate of botulinum ADP-ribosyltransferase C3. Biochem. Biophys. Res. Commun. 158, 209-213 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.158 , pp. 209-213
    • Aktories, K.1    Braun, U.2    Rösener, S.3    Just, I.4    Hall, A.5
  • 2
    • 0024529240 scopus 로고
    • Purification of the 22 kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene product
    • Braun, U., Habermann, B., Just, I., Aktories, K. & Vandekerckhove, J. Purification of the 22 kDa protein substrate of botulinum ADP- ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene product. FEBS Lett. 243, 70-76 (1989).
    • (1989) FEBS Lett. , vol.243 , pp. 70-76
    • Braun, U.1    Habermann, B.2    Just, I.3    Aktories, K.4    Vandekerckhove, J.5
  • 3
    • 0008614480 scopus 로고
    • Mechanism of adenylate cyclase activation by cholera toxin: Inhibition of GTP hydrolysis at the regulatory site
    • Cassel, D. & Selinger, Z. Mechanism of adenylate cyclase activation by cholera toxin: Inhibition of GTP hydrolysis at the regulatory site. Proc. Natl Acad. Sci. USA 74, 3307-3311 (1977).
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 3307-3311
    • Cassel, D.1    Selinger, Z.2
  • 4
    • 1842384421 scopus 로고
    • ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase
    • Gill, D. M. & Meren, R. ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase. Proc. Natl Acad. Sci. USA 75, 3050-3054 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3050-3054
    • Gill, D.M.1    Meren, R.2
  • 5
    • 0022347238 scopus 로고
    • Pertussis toxin-catalyzed ADP-ribosylation of transducin Cysteine 347 is the ADP-ribose acceptor site
    • West, R. E., Moss, J., Vaughan, M., Liu, T. & Liu, T. Y. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. J. Biol. Chem. 260, 14428-14430 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 14428-14430
    • West, R.E.1    Moss, J.2    Vaughan, M.3    Liu, T.4    Liu, T.Y.5
  • 6
    • 0022641097 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates actin
    • Aktories, K. et al. Botulinum C2 toxin ADP-ribosylates actin. Nature 322, 390-392 (1986).
    • (1986) Nature , vol.322 , pp. 390-392
    • Aktories, K.1
  • 9
    • 44949212841 scopus 로고    scopus 로고
    • Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ? Toxin
    • Tsuge, H. et al. Structural basis of actin recognition and arginine ADP-ribosylation by Clostridium perfringens ? toxin. Proc. Natl Acad. Sci. USA 105, 7399-7404 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7399-7404
    • Tsuge, H.1
  • 10
    • 84875045406 scopus 로고    scopus 로고
    • Arginine ADP-ribosylation mechanism based on structural snapshots of iota-Toxin and actin complex
    • Tsurumura, T. et al. Arginine ADP-ribosylation mechanism based on structural snapshots of iota-Toxin and actin complex. Proc. Natl Acad. Sci. USA 110, 4267-4272 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4267-4272
    • Tsurumura, T.1
  • 11
    • 84875029636 scopus 로고    scopus 로고
    • Strain-Alleviation model of ADP-ribosylation
    • Jank, T. & Aktories, K. Strain-Alleviation model of ADP-ribosylation. Proc. Natl Acad. Sci. USA 110, 4163-4164 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4163-4164
    • Jank, T.1    Aktories, K.2
  • 12
    • 80051924025 scopus 로고    scopus 로고
    • New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin
    • Barth, H. & Aktories, K. New insights into the mode of action of the actin ADP-ribosylating virulence factors Salmonella enterica SpvB and Clostridium botulinum C2 toxin. Eur. J. Cell Biol. 90, 944-950 (2011).
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 944-950
    • Barth, H.1    Aktories, K.2
  • 13
    • 4544264417 scopus 로고    scopus 로고
    • Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • Barth, H., Aktories, K., Popoff, M. R. & Stiles, B. G. Binary bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol. Mol. Biol. Rev. 68, 373-402 (2004).
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 14
    • 33846814964 scopus 로고    scopus 로고
    • C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins
    • Vogelsgesang, M., Pautsch, A. & Aktories, K. C3 exoenzymes, novel insights into structure and action of Rho-ADP-ribosylating toxins. Naunyn Schmiedebergs Arch. Pharmacol. 374, 347-360 (2007).
    • (2007) Naunyn Schmiedebergs Arch. Pharmacol. , vol.374 , pp. 347-360
    • Vogelsgesang, M.1    Pautsch, A.2    Aktories, K.3
  • 15
    • 84871181408 scopus 로고    scopus 로고
    • Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure
    • Dueholm, M. S., Albertsen, M., Otzen, D. & Nielsen, P. H. Curli functional amyloid systems are phylogenetically widespread and display large diversity in operon and protein structure. PLoS ONE 7, e51274 (2012).
    • (2012) PLoS ONE , vol.7
    • Dueholm, M.S.1    Albertsen, M.2    Otzen, D.3    Nielsen, P.H.4
  • 16
    • 84883696561 scopus 로고    scopus 로고
    • Prediction of molecular mimicry candidates in human pathogenic bacteria
    • Doxey, A. C. & McConkey, B. J. Prediction of molecular mimicry candidates in human pathogenic bacteria. Virulence 4, 453-466 (2013).
    • (2013) Virulence , vol.4 , pp. 453-466
    • Doxey, A.C.1    McConkey, B.J.2
  • 17
    • 84867800804 scopus 로고    scopus 로고
    • From genotype to phenotype: Can systems biology be used to predict Staphylococcus aureus virulence?
    • Priest, N. K. et al. From genotype to phenotype: Can systems biology be used to predict Staphylococcus aureus virulence? Nature Rev. Microbiol. 10, 791-797 (2012).
    • (2012) Nature Rev. Microbiol. , vol.10 , pp. 791-797
    • Priest, N.K.1
  • 18
    • 2442711527 scopus 로고    scopus 로고
    • In silico identification of novel bacterial ADP-ribosyltransferases
    • Masignani, V. et al. In silico identification of novel bacterial ADP-ribosyltransferases. Int. J. Med. Microbiol. 293, 471-478 (2004).
    • (2004) Int. J. Med. Microbiol. , vol.293 , pp. 471-478
    • Masignani, V.1
  • 19
    • 78651239716 scopus 로고    scopus 로고
    • Cholera-And anthrax-like toxins are among several new ADP-ribosyltransferases
    • Fieldhouse, R. J., Turgeon, Z., White, D. & Merrill, A. R. Cholera-And anthrax-like toxins are among several new ADP-ribosyltransferases. PLoS Comput. Biol. 6, e1001029 (2010).
    • (2010) PLoS Comput. Biol. , vol.6
    • Fieldhouse, R.J.1    Turgeon, Z.2    White, D.3    Merrill, A.R.4
  • 20
    • 0026552246 scopus 로고
    • The crystal structure of diphtheria toxin
    • Choe, S. et al. The crystal structure of diphtheria toxin. Nature 357, 216-222 (1992).
    • (1992) Nature , vol.357 , pp. 216-222
    • Choe, S.1
  • 21
    • 0015217293 scopus 로고
    • Observations on the structure of diphtheria toxin
    • Gill, D. M. & Dinius, L. L. Observations on the structure of diphtheria toxin. J. Biol. Chem. 246, 1485-1491 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 1485-1491
    • Gill, D.M.1    Dinius, L.L.2
  • 22
    • 0015217337 scopus 로고
    • Structure and activity of diphtheria toxin I Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments
    • Collier, R. J. & Kandel, J. Structure and activity of diphtheria toxin. I. Thiol-dependent dissociation of a fraction of toxin into enzymically active and inactive fragments. J. Biol. Chem. 246, 1496-1503 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 1496-1503
    • Collier, R.J.1    Kandel, J.2
  • 23
    • 0015217224 scopus 로고
    • Structure-Activity relationships in diphtheria toxin
    • Gill, D. M. & Pappenheimer, A. M. Jr. Structure-Activity relationships in diphtheria toxin. J. Biol. Chem. 246, 1492-1495 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 1492-1495
    • Gill, D.M.1    Pappenheimer Jr., A.M.2
  • 24
    • 0029161099 scopus 로고
    • The three-dimensional crystal structure of cholera toxin
    • Zhang, R. G. et al. The three-dimensional crystal structure of cholera toxin. J. Mol. Biol. 251, 563-573 (1995).
    • (1995) J. Mol. Biol. , vol.251 , pp. 563-573
    • Zhang, R.G.1
  • 25
    • 0027174854 scopus 로고
    • Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin
    • Sixma, T. K. et al. Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. J. Mol. Biol. 230, 890-918 (1993).
    • (1993) J. Mol. Biol. , vol.230 , pp. 890-918
    • Sixma, T.K.1
  • 26
    • 0038208865 scopus 로고    scopus 로고
    • The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding
    • Blöcker, D. et al. The C terminus of component C2II of Clostridium botulinum C2 toxin is essential for receptor binding. Infect. Immun. 68, 4566-4573 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 4566-4573
    • Blöcker, D.1
  • 27
    • 33751070013 scopus 로고    scopus 로고
    • Structure and action of the binary C2 toxin from Clostridium botulinum
    • Schleberger, C., Hochmann, H., Barth, H., Aktories, K. & Schulz, G. E. Structure and action of the binary C2 toxin from Clostridium botulinum. J. Mol. Biol. 364, 705-715 (2006).
    • (2006) J. Mol. Biol. , vol.364 , pp. 705-715
    • Schleberger, C.1    Hochmann, H.2    Barth, H.3    Aktories, K.4    Schulz, G.E.5
  • 28
    • 0023110218 scopus 로고
    • Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin
    • Aktories, K., Weller, U. & Chhatwal, G. S. Clostridium botulinum type C produces a novel ADP-ribosyltransferase distinct from botulinum C2 toxin. FEBS Lett. 212, 109-113 (1987).
    • (1987) FEBS Lett. , vol.212 , pp. 109-113
    • Aktories, K.1    Weller, U.2    Chhatwal, G.S.3
  • 29
    • 0035808303 scopus 로고    scopus 로고
    • Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: Structural insights for recognition specificity and catalysis
    • Han, S., Arvai, A. S., Clancy, S. B. & Tainer, J. A. Crystal structure and novel recognition motif of Rho ADP-ribosylating C3 exoenzyme from Clostridium botulinum: Structural insights for recognition specificity and catalysis. J. Mol. Biol. 305, 95-107 (2001).
    • (2001) J. Mol. Biol. , vol.305 , pp. 95-107
    • Han, S.1    Arvai, A.S.2    Clancy, S.B.3    Tainer, J.A.4
  • 30
    • 84880511936 scopus 로고    scopus 로고
    • Structure and function of the Salmonella Typhi chimaeric A2B5 typhoid toxin
    • Song, J., Gao, X. & Galan, J. E. Structure and function of the Salmonella Typhi chimaeric A2B5 typhoid toxin. Nature 499, 350-354 (2013).
    • (2013) Nature , vol.499 , pp. 350-354
    • Song, J.1    Gao, X.2    Galan, J.E.3
  • 31
    • 77649193972 scopus 로고    scopus 로고
    • Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering
    • Lang, A. E. et al. Photorhabdus luminescens toxins ADP-ribosylate actin and RhoA to force actin clustering. Science 327, 1139-1142 (2010).
    • (2010) Science , vol.327 , pp. 1139-1142
    • Lang, A.E.1
  • 32
    • 0031904402 scopus 로고    scopus 로고
    • Novel insecticidal toxin from photorhabdus luminescens, toxin complex a (tca), and its histopathological effects on the midgut of manduca sexta
    • Blackburn, M., Golubeva, E., Bowen, D. & Ffrench-Constant, R. H. A. Novel insecticidal toxin from Photorhabdus luminescens, toxin complex a (Tca), and its histopathological effects on the midgut of Manduca sexta. Appl. Environ. Microbiol. 64, 3036-3041 (1998).
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3036-3041
    • Blackburn, M.1    Golubeva, E.2    Bowen, D.3    Ffrench-Constant, R.H.A.4
  • 33
    • 0036196923 scopus 로고    scopus 로고
    • The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases
    • Han, S. & Tainer, J. The ARTT motif and a unified structural understanding of substrate recognition in ADP-ribosylating bacterial toxins and eukaryotic ADP-ribosyltransferases. Int. J. Med. Microbiol. 291, 523-529 (2002).
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 523-529
    • Han, S.1    Tainer, J.2
  • 34
    • 0025076421 scopus 로고
    • Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid 148 with aspartic acid, glutamine, or serine
    • Wilson, B. A., Reich, K. A., Weinstein, B. R. & Collier, R. J. Active-site mutations of diphtheria toxin: Effects of replacing glutamic acid 148 with aspartic acid, glutamine, or serine. Biochemistry 29, 8643-8651 (1990).
    • (1990) Biochemistry , vol.29 , pp. 8643-8651
    • Wilson, B.A.1    Reich, K.A.2    Weinstein, B.R.3    Collier, R.J.4
  • 35
    • 0021280847 scopus 로고
    • NAD binding site of diphtheria toxin: Identification of a residue within the nicotinamide subsite by photochemical modification with NAD
    • Carroll, S. F. & Collier, R. J. NAD binding site of diphtheria toxin: Identification of a residue within the nicotinamide subsite by photochemical modification with NAD. Proc. Natl Acad. Sci. USA 81, 3307-3311 (1984).
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 3307-3311
    • Carroll, S.F.1    Collier, R.J.2
  • 36
    • 0023664604 scopus 로고
    • Active site of Pseudomonas aeruginosa exotoxin A Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin
    • Carroll, S. F. & Collier, R. J. Active site of Pseudomonas aeruginosa exotoxin A. Glutamic acid 553 is photolabeled by NAD and shows functional homology with glutamic acid 148 of diphtheria toxin. J. Biol. Chem. 262, 8707-8711 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 8707-8711
    • Carroll, S.F.1    Collier, R.J.2
  • 37
    • 0023449908 scopus 로고
    • Exotoxin A of Pseudomonas aeruginosa: Substitution of glutamic acid 553 with aspartic acid drastically reduces toxicity and enzymatic activity
    • Douglas, D. & Collier, R. Exotoxin A of Pseudomonas aeruginosa: Substitution of glutamic acid 553 with aspartic acid drastically reduces toxicity and enzymatic activity. J. Bacteriol. 169, 4967-4971 (1987).
    • (1987) J. Bacteriol. , vol.169 , pp. 4967-4971
    • Douglas, D.1    Collier, R.2
  • 38
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell, C. E. & Eisenberg, D. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochemistry 35, 1137-1149 (1996).
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 39
    • 1342286058 scopus 로고    scopus 로고
    • Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2
    • Oliver, A. W. et al. Crystal structure of the catalytic fragment of murine poly(ADP-ribose) polymerase-2. Nucleic Acids Res. 32, 456-464 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 456-464
    • Oliver, A.W.1
  • 41
    • 0037225397 scopus 로고    scopus 로고
    • Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-Toxin
    • Tsuge, H. et al. Crystal structure and site-directed mutagenesis of enzymatic components from Clostridium perfringens iota-Toxin. J. Mol. Biol. 325, 471-483 (2003).
    • (2003) J. Mol. Biol. , vol.325 , pp. 471-483
    • Tsuge, H.1
  • 42
    • 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. 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).
    • (1996) Mol. Microbiol. , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 43
    • 0000078012 scopus 로고
    • Contribution a luetude de la diphtherie
    • Roux Jr., E. & Yersin, A. Contribution a luetude de la diphtherie. Ann. Inst. Pasteur 2, 620-629 (1888).
    • (1888) Ann. Inst. Pasteur , vol.2 , pp. 620-629
    • Roux Jr., E.1    Yersin, A.2
  • 44
    • 0001079281 scopus 로고
    • The purification and concentration of diphtheria toxin
    • Eaton, M. D. The purification and concentration of diphtheria toxin. J. Bacteriol. 31, 347 (1936).
    • (1936) J. Bacteriol. , vol.31 , pp. 347
    • Eaton, M.D.1
  • 45
    • 0000674879 scopus 로고
    • Diphtheria toxin: I isolation and characterization of a toxic protein from C diphtheriae filtrates
    • Pappenheimer, A. M. Jr. Diphtheria toxin: I. isolation and characterization of a toxic protein from C. diphtheriae filtrates. J. Biol. Chem. 125, 543-553 (1937).
    • (1937) J. Biol. Chem. , vol.125 , pp. 543-553
    • Pappenheimer Jr., A.M.1
  • 46
    • 0001396162 scopus 로고
    • Studies on the virulence of bacteriophage infected strains of C diphtheriae
    • Freeman, V. J. Studies on the virulence of bacteriophage infected strains of C. diphtheriae. J. Bacteriol. 61, 675-688 (1951).
    • (1951) J. Bacteriol. , vol.61 , pp. 675-688
    • Freeman, V.J.1
  • 47
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor
    • Naglich, J. G., Metherall, J. E., Russell, D. W. & Eidels, L. Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor. Cell 69, 1051-1061 (1992).
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 48
    • 0031305240 scopus 로고    scopus 로고
    • Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor
    • Louie, G. V., Yang, W., Bowman, M. E. & Choe, S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor. Mol. Cell 1, 67-78 (1997).
    • (1997) Mol. Cell , vol.1 , pp. 67-78
    • Louie, G.V.1    Yang, W.2    Bowman, M.E.3    Choe, S.4
  • 49
    • 0031031848 scopus 로고    scopus 로고
    • Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery
    • Lemichez, E. et al. Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery. Mol. Microbiol. 23, 445-457 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 445-457
    • Lemichez, E.1
  • 50
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon, V. M., Klimpel, K. R., Arora, N., Henderson, M. A. & Leppla, S. H. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 63, 82-87 (1995).
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 51
    • 0019271816 scopus 로고
    • Diphtheria toxin entry into cells is facilitated by low pH
    • Sandvig, K. & Olsnes, S. Diphtheria toxin entry into cells is facilitated by low pH. J. Cell Biol. 87, 828-832 (1980).
    • (1980) J. Cell Biol. , vol.87 , pp. 828-832
    • Sandvig, K.1    Olsnes, S.2
  • 52
    • 0019287379 scopus 로고
    • The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement
    • Draper, R. K. & Simon, M. I. The entry of diphtheria toxin into the mammalian cell cytoplasm: Evidence for lysosomal involvement. J. Cell Biol. 87, 849-854 (1980).
    • (1980) J. Cell Biol. , vol.87 , pp. 849-854
    • Draper, R.K.1    Simon, M.I.2
  • 53
    • 0014202360 scopus 로고
    • Effect of diphtheria toxin on protein syn thesis: Inactivation of one of the transfer factors
    • Collier, R. J. Effect of diphtheria toxin on protein synthesis: Inactivation of one of the transfer factors. J. Mol. Biol. 25, 83-98 (1967).
    • (1967) J. Mol. Biol. , vol.25 , pp. 83-98
    • Collier, R.J.1
  • 54
    • 0014429772 scopus 로고
    • Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis
    • Honjo, T., Nishizuka, Y., Hayaishi, O. & Kato, I. Diphtheria toxin-dependent adenosine diphosphate ribosylation of aminoacyl transferase II and inhibition of protein synthesis. J. Biol. Chem. 243, 3553-3555 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 3553-3555
    • Honjo, T.1    Nishizuka, Y.2    Hayaishi, O.3    Kato, I.4
  • 55
    • 0019333247 scopus 로고
    • ADP-ribosylation of elongation factor 2 by diphtheria toxin Isolation and properties of the novel ribosyl-Amino acid and its hydrolysis products
    • Van Ness, B. G., Howard, J. B. & Bodley, J. W. ADP-ribosylation of elongation factor 2 by diphtheria toxin. Isolation and properties of the novel ribosyl-Amino acid and its hydrolysis products. J. Biol. Chem. 255, 10717-10720 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 10717-10720
    • Van Ness, B.G.1    Howard, J.B.2    Bodley, J.W.3
  • 56
    • 84888624530 scopus 로고    scopus 로고
    • The biosynthesis and biological function of diphthamide
    • Su, X., Lin, Z. & Lin, H. The biosynthesis and biological function of diphthamide. Crit. Rev. Biochem. Mol. Biol. 48, 515-521 (2013).
    • (2013) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 515-521
    • Su, X.1    Lin, Z.2    Lin, H.3
  • 57
    • 0000774551 scopus 로고
    • The effect of diphtheria toxin on the metabolism of HeLa cells
    • Strauss, N. & Hendee, E. D. The effect of diphtheria toxin on the metabolism of HeLa cells. J. Exp. Med. 109, 145-163 (1959).
    • (1959) J. Exp. Med. , vol.109 , pp. 145-163
    • Strauss, N.1    Hendee, E.D.2
  • 58
    • 84906320707 scopus 로고    scopus 로고
    • Critical movements of a single diphthamide residue of eukaryotic elongation factor 2 monitored by cryo EM
    • Taylor, D. et al. Critical movements of a single diphthamide residue of eukaryotic elongation factor 2 monitored by cryo EM. Microsc. Microanalysis 13, 388-389 (2007).
    • (2007) Microsc. Microanalysis , vol.13 , pp. 388-389
    • Taylor, D.1
  • 59
    • 84865282692 scopus 로고    scopus 로고
    • Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development
    • Liu, S. et al. Diphthamide modification on eukaryotic elongation factor 2 is needed to assure fidelity of mRNA translation and mouse development. Proc. Natl Acad. Sci. USA 109, 13817-13822 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 13817-13822
    • Liu, S.1
  • 60
    • 47549095879 scopus 로고    scopus 로고
    • The diphthamide modification on elongation factor 2 renders mammalian cells resistant to ricin
    • Gupta, P. K., Liu, S., Batavia, M. P. & Leppla, S. H. The diphthamide modification on elongation factor 2 renders mammalian cells resistant to ricin. Cell. Microbiol. 10, 1687-1694 (2008).
    • (2008) Cell. Microbiol. , vol.10 , pp. 1687-1694
    • Gupta, P.K.1    Liu, S.2    Batavia, M.P.3    Leppla, S.H.4
  • 61
    • 0020073392 scopus 로고
    • Bacterial toxins: A table of lethal amounts
    • Gill, D. M. Bacterial toxins: A table of lethal amounts. Microbiol. Rev. 46, 86-94 (1982).
    • (1982) Microbiol. Rev. , vol.46 , pp. 86-94
    • Gill, D.M.1
  • 62
    • 0023968573 scopus 로고
    • Amino acid sequence homology between the enzymic domains of diphtheria toxin and Pseudomonas aeruginosa exotoxin A
    • Carroll, S. F. & Collier, R. J. Amino acid sequence homology between the enzymic domains of diphtheria toxin and Pseudomonas aeruginosa exotoxin A. Mol. Microbiol. 2, 293-296 (1988).
    • (1988) Mol. Microbiol. , vol.2 , pp. 293-296
    • Carroll, S.F.1    Collier, R.J.2
  • 63
    • 0020483229 scopus 로고
    • Crystallization of exotoxin A from Pseudomonas aeruginosa
    • Collier, R. J. & McKay, D. B. Crystallization of exotoxin A from Pseudomonas aeruginosa. J. Mol. Biol. 157, 413-415 (1982).
    • (1982) J. Mol. Biol. , vol.157 , pp. 413-415
    • Collier, R.J.1    McKay, D.B.2
  • 64
    • 0022540281 scopus 로고
    • Structure of exotoxin A of Pseudomonas aeruginosa at 3.0 Angstrom resolution
    • Allured, V. S., Collier, R. J., Carroll, S. F. & McKay, D. B. Structure of exotoxin A of Pseudomonas aeruginosa at 3.0 Angstrom resolution. Proc. Natl Acad. Sci. USA 83, 1320-1324 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 1320-1324
    • Allured, V.S.1    Collier, R.J.2    Carroll, S.F.3    McKay, D.B.4
  • 65
    • 0026690341 scopus 로고
    • The α2 macroglobulin receptor/ low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A
    • Kounnas, M. Z. et al. The α2 macroglobulin receptor/ low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A. J. Biol. Chem. 267, 12420-12423 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 12420-12423
    • Kounnas, M.Z.1
  • 66
    • 0026455183 scopus 로고
    • Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol
    • Ogata, M., Fryling, C. M., Pastan, I. & FitzGerald, D. J. Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol. J. Biol. Chem. 267, 25396-25401 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25396-25401
    • Ogata, M.1    Fryling, C.M.2    Pastan, I.3    FitzGerald, D.J.4
  • 67
    • 0018967650 scopus 로고
    • Receptor-mediated internalization of Pseudomonas toxin by mouse fibroblasts
    • Fitzgerald, D., Morris, R. E. & Saelinger, C. B. Receptor-mediated internalization of Pseudomonas toxin by mouse fibroblasts. Cell 21, 867-873 (1980).
    • (1980) Cell , vol.21 , pp. 867-873
    • Fitzgerald, D.1    Morris, R.E.2    Saelinger, C.B.3
  • 68
    • 81555214408 scopus 로고    scopus 로고
    • A guide to taming a toxin-recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer
    • Weldon, J. E. & Pastan, I. A guide to taming a toxin-recombinant immunotoxins constructed from Pseudomonas exotoxin A for the treatment of cancer. FEBS J. 278, 4683-4700 (2011).
    • (2011) FEBS J. , vol.278 , pp. 4683-4700
    • Weldon, J.E.1    Pastan, I.2
  • 69
    • 0033554871 scopus 로고    scopus 로고
    • Reduction of furin-nicked Pseudomonas exotoxin A: An unfolding story
    • McKee, M. L. & FitzGerald, D. J. Reduction of furin-nicked Pseudomonas exotoxin A: An unfolding story. Biochemistry 38, 16507-16513 (1999).
    • (1999) Biochemistry , vol.38 , pp. 16507-16513
    • McKee, M.L.1    FitzGerald, D.J.2
  • 70
    • 0017362294 scopus 로고
    • Mechanism of action of Pseudomonas aeruginosa exotoxin A: Adenosine diphosphate ribosylation of mammalian elongation factor 2 in vitro and in vivo
    • Iglewski, B. H., Liu, P. V. & Kabat, D. Mechanism of action of Pseudomonas aeruginosa exotoxin A: Adenosine diphosphate ribosylation of mammalian elongation factor 2 in vitro and in vivo. Infection Immun. 15, 138-144 (1977).
    • (1977) Infection Immun. , vol.15 , pp. 138-144
    • Iglewski, B.H.1    Liu, P.V.2    Kabat, D.3
  • 71
    • 1242274354 scopus 로고    scopus 로고
    • Genetic diversity and virulence potential of environmental Vibrio cholerae population in a cholera-endemic area
    • Faruque, S. M. et al. Genetic diversity and virulence potential of environmental Vibrio cholerae population in a cholera-endemic area. Proc. Natl Acad. Sci. USA 101, 2123-2128 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2123-2128
    • Faruque, S.M.1
  • 72
    • 0030446912 scopus 로고    scopus 로고
    • Global climate and infectious disease: The cholera paradigm
    • Colwell, R. R. Global climate and infectious disease: The cholera paradigm. Science 274, 2025-2031 (1996).
    • (1996) Science , vol.274 , pp. 2025-2031
    • Colwell, R.R.1
  • 73
    • 77957275335 scopus 로고    scopus 로고
    • Diversity and distribution of cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae
    • Purdy, A. E. et al. Diversity and distribution of cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae. Environ. Microbiol. Rep. 2, 198-207 (2010).
    • (2010) Environ. Microbiol. Rep. , vol.2 , pp. 198-207
    • Purdy, A.E.1
  • 74
    • 34047252768 scopus 로고    scopus 로고
    • The genome of non O1 Vibrio cholerae NRT36S demonstrates the presence of pathogenic mechanisms that are distinct from those of O1 Vibrio cholerae
    • Chen, Y., Johnson, J. A., Pusch, G. D., Morris, J. G. & Stine, O. C. The genome of non O1 Vibrio cholerae NRT36S demonstrates the presence of pathogenic mechanisms that are distinct from those of O1 Vibrio cholerae. Infection Immun. 75, 2645-2647 (2007).
    • (2007) Infection Immun. , vol.75 , pp. 2645-2647
    • Chen, Y.1    Johnson, J.A.2    Pusch, G.D.3    Morris, J.G.4    Stine, O.C.5
  • 75
    • 84873049877 scopus 로고    scopus 로고
    • Novel cholix toxin variants ADP-ribosylating toxins in Vibrio cholerae non O1/ non O139 strains, and their pathogenicity
    • Awasthi, S. P. et al. Novel cholix toxin variants, ADP-ribosylating toxins in Vibrio cholerae non O1/ non O139 strains, and their pathogenicity. Infect. Immun. 81, 531-541 (2013).
    • (2013) Infect. Immun. , vol.81 , pp. 531-541
    • Awasthi, S.P.1
  • 76
    • 44849084557 scopus 로고    scopus 로고
    • Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae
    • Jørgensen, R. et al. Cholix toxin, a novel ADP-ribosylating factor from Vibrio cholerae. J. Biol. Chem. 283, 10671-10678 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 10671-10678
    • Jørgensen, R.1
  • 78
    • 0034739007 scopus 로고    scopus 로고
    • Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen
    • Stover, C. K. et al. Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen. Nature 406, 959-964 (2000).
    • (2000) Nature , vol.406 , pp. 959-964
    • Stover, C.K.1
  • 79
    • 33748441571 scopus 로고
    • Sechster bericht der deutschen wissenschaftlichen commission zur enforschung der cholera
    • in German)
    • Koch, R. Sechster Bericht der deutschen Wissenschaftlichen Commission zur Enforschung der Cholera. Dtsch Med Wochenschr 10, 191-192 (in German) (1884).
    • (1884) Dtsch Med Wochenschr , vol.10 , pp. 191-192
    • Koch, R.1
  • 80
    • 0021754748 scopus 로고
    • Robert Koch and the cholera vibrio: A centenary
    • Howard-Jones, N. Robert Koch and the cholera vibrio: A centenary. BMJ 288, 379-381 (1984).
    • (1984) BMJ , vol.288 , pp. 379-381
    • Howard-Jones, N.1
  • 81
    • 34247146685 scopus 로고
    • Enterotoxicity of bacteria-free culture-filtrate of Vibrio cholerae
    • De, S. N. Enterotoxicity of bacteria-free culture-filtrate of Vibrio cholerae. Nature 183, 1533-1534 (1959).
    • (1959) Nature , vol.183 , pp. 1533-1534
    • De, S.N.1
  • 82
    • 0033055636 scopus 로고    scopus 로고
    • Membrane traffic and the cellular uptake of cholera toxin
    • Lencer, W. I., Hirst, T. R. & Holmes, R. K. Membrane traffic and the cellular uptake of cholera toxin. Biochim. Biophys. Acta 1450, 177-190 (1999).
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 177-190
    • Lencer, W.I.1    Hirst, T.R.2    Holmes, R.K.3
  • 83
    • 0021015433 scopus 로고
    • Membrane receptors for bacterial toxins
    • Eidels, L., Proia, R. & Hart, D. Membrane receptors for bacterial toxins. Microbiol. Rev. 47, 596-620 (1983).
    • (1983) Microbiol. Rev. , vol.47 , pp. 596-620
    • Eidels, L.1    Proia, R.2    Hart, D.3
  • 85
    • 0025073256 scopus 로고
    • Mechanism of activation of cholera toxin by ADP-ribosylation factor (ARF): Both low-And high-Affinity interactions of ARF with guanine nucleotides promote toxin activation
    • Bobak, D. et al. Mechanism of activation of cholera toxin by ADP-ribosylation factor (ARF): Both low-And high-Affinity interactions of ARF with guanine nucleotides promote toxin activation. Biochemistry 29, 855-861 (1990).
    • (1990) Biochemistry , vol.29 , pp. 855-861
    • Bobak, D.1
  • 86
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human ARF6 GTP
    • O'Neal, C. J., Jobling, M. G., Holmes, R. K. & Hol, W. G. J. Structural basis for the activation of cholera toxin by human ARF6 GTP. Science 309, 1093-1096 (2005).
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'Neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.G.J.4
  • 87
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein
    • Kahn, R. A. & Gilman, A. G. The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem. 261, 7906-7911 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 88
    • 1842384421 scopus 로고
    • ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase
    • Gill, D. M. & Meren, R. ADP-ribosylation of membrane proteins catalyzed by cholera toxin: Basis of the activation of adenylate cyclase. Proc. Natl Acad. Sci. USA 75, 3050-3054 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3050-3054
    • Gill, D.M.1    Meren, R.2
  • 89
    • 0347349553 scopus 로고
    • Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system
    • Cassel, D. & Pfeuffer, T. Mechanism of cholera toxin action: Covalent modification of the guanyl nucleotide-binding protein of the adenylate cyclase system. Proc. Natl Acad. Sci. USA 75, 2669-2673 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 2669-2673
    • Cassel, D.1    Pfeuffer, T.2
  • 90
    • 0018140316 scopus 로고
    • Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin: Evidence for ADP ribosyl transferase activity similar to that of choleragen
    • Moss, J. Activation of adenylate cyclase by heat-labile Escherichia coli enterotoxin: Evidence for ADP ribosyl transferase activity similar to that of choleragen. J. Clin. Invest. 62, 281-285 (1978).
    • (1978) J. Clin. Invest. , vol.62 , pp. 281-285
    • Moss, J.1
  • 91
    • 0023388301 scopus 로고
    • Type II heat-labile enterotoxin of Escherichia coli activates adenylate cyclase in human fibroblasts by ADP ribosylation
    • Chang, P. P., Moss, J., Twiddy, E. M. & Holmes, R. K. Type II heat-labile enterotoxin of Escherichia coli activates adenylate cyclase in human fibroblasts by ADP ribosylation. Infect. Immun. 55, 1854-1858 (1987).
    • (1987) Infect. Immun. , vol.55 , pp. 1854-1858
    • Chang, P.P.1    Moss, J.2    Twiddy, E.M.3    Holmes, R.K.4
  • 92
    • 0016206523 scopus 로고
    • Action of Escherichia coli enterotoxin: Adenylate cyclase behavior of intestinal epithelial cells in culture
    • Kantor, H. S., Tao, P. & Wisdom, C. Action of Escherichia coli enterotoxin: Adenylate cyclase behavior of intestinal epithelial cells in culture. Infecti. Immun. 9, 1003-1010 (1974).
    • (1974) Infecti. Immun. , vol.9 , pp. 1003-1010
    • Kantor, H.S.1    Tao, P.2    Wisdom, C.3
  • 93
    • 33846079723 scopus 로고    scopus 로고
    • World Health Organization [online] (WHO, 2011
    • World Health Organization. Immunization, Vaccines and Biologicals: Pertussis [online], http://www.who.int/ immunization/topics/pertussis/en/ (WHO, 2011).
    • Immunization, Vaccines and Biologicals: Pertussis
  • 94
    • 0020362248 scopus 로고
    • Subunit structure of islet-Activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura, M. et al. Subunit structure of islet-Activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry 21, 5516-5522 (1982).
    • (1982) Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1
  • 95
    • 0028177724 scopus 로고
    • The crystal structure of pertussis toxin
    • Stein, P. E. et al. The crystal structure of pertussis toxin. Structure 2, 45-57 (1994).
    • (1994) Structure , vol.2 , pp. 45-57
    • Stein, P.E.1
  • 96
    • 0023884187 scopus 로고
    • Use of glycosyltransferases to restore pertussis toxin receptor activity to asialoagalactofetuin
    • Armstrong, G. D., Howard, L. A. & Peppler, M. S. Use of glycosyltransferases to restore pertussis toxin receptor activity to asialoagalactofetuin. J. Biol. Chem. 263, 8677-8684 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 8677-8684
    • Armstrong, G.D.1    Howard, L.A.2    Peppler, M.S.3
  • 97
    • 0028500699 scopus 로고
    • Structure of a pertussis toxin-sugar complex as a model for receptor binding
    • Stein, P. et al. Structure of a pertussis toxin-sugar complex as a model for receptor binding. Nature Struct. Biol. 1, 591-596 (1994).
    • (1994) Nature Struct. Biol. , vol.1 , pp. 591-596
    • Stein, P.1
  • 98
    • 0023877979 scopus 로고
    • Lectin-like binding of pertussis toxin to a 165 kilodalton Chinese hamster ovary cell glycoprotein
    • Brennan, M. J., David, J. L., Kenimer, J. G. & Manclark, C. R. Lectin-like binding of pertussis toxin to a 165 kilodalton Chinese hamster ovary cell glycoprotein. J. Biol. Chem. 263, 4895-4899 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 4895-4899
    • Brennan, M.J.1    David, J.L.2    Kenimer, J.G.3    Manclark, C.R.4
  • 99
    • 0030974747 scopus 로고    scopus 로고
    • Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a prerequisite for cellular intoxication
    • el Bayâ, A., Linnemann, R., von Olleschik-Elbheim, L., Robenek, H. & Schmidt, M. Endocytosis and retrograde transport of pertussis toxin to the Golgi complex as a prerequisite for cellular intoxication. Eur. J. Cell Biol. 73, 40-48 (1997).
    • (1997) Eur. J. Cell Biol. , vol.73 , pp. 40-48
    • El Bayâ, A.1    Linnemann, R.2    Von Olleschik-Elbheim, L.3    Robenek, H.4    Schmidt, M.5
  • 100
    • 0024576163 scopus 로고
    • Role of cysteine 41 of the A subunit of pertussis toxin
    • Burns, D. L. & Manclark, C. R. Role of cysteine 41 of the A subunit of pertussis toxin. J. Biol. Chem. 264, 564-568 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 564-568
    • Burns, D.L.1    Manclark, C.R.2
  • 101
    • 0025338668 scopus 로고
    • Roles of the disulfide bond and the carboxy-Terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin
    • Antoine, R. & Locht, C. Roles of the disulfide bond and the carboxy-Terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin. Infection Immun. 58, 1518-1526 (1990).
    • (1990) Infection Immun. , vol.58 , pp. 1518-1526
    • Antoine, R.1    Locht, C.2
  • 102
    • 0021111692 scopus 로고
    • Identification of the predominant substrate for ADP-ribosylation by islet activating protein
    • Bokoch, G. M., Katada, T., Northup, J. K., Hewlett, E. L. & Gilman, A. G. Identification of the predominant substrate for ADP-ribosylation by islet activating protein. J. Biol. Chem. 258, 2072-2075 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 2072-2075
    • Bokoch, G.M.1    Katada, T.2    Northup, J.K.3    Hewlett, E.L.4    Gilman, A.G.5
  • 103
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by islet-Activating protein due to ADP-ribosylation of a membrane protein
    • Katada, T. & Ui, M. Direct modification of the membrane adenylate cyclase system by islet-Activating protein due to ADP-ribosylation of a membrane protein. Proc. Natl Acad. Sci. USA 79, 3129-3133 (1982).
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 104
    • 0020541131 scopus 로고
    • Specific uncoupling by islet-Activating protein, pertussis toxin, of negative signal transduction via α-Adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells
    • Kurose, H., Katada, T., Amano, T. & Ui, M. Specific uncoupling by islet-Activating protein, pertussis toxin, of negative signal transduction via α-Adrenergic, cholinergic, and opiate receptors in neuroblastoma x glioma hybrid cells. J. Biol. Chem. 258, 4870-4875 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 4870-4875
    • Kurose, H.1    Katada, T.2    Amano, T.3    Ui, M.4
  • 105
    • 0023074774 scopus 로고
    • Molecular basis for the pathological actions of Clostridium perfringens iota toxin
    • Simpson, L. L., Stiles, B. G., Zepeda, H. H. & Wilkins, T. D. Molecular basis for the pathological actions of Clostridium perfringens iota toxin. Infect. Immun. 55, 118-122 (1987).
    • (1987) Infect. Immun. , vol.55 , pp. 118-122
    • Simpson, L.L.1    Stiles, B.G.2    Zepeda, H.H.3    Wilkins, T.D.4
  • 106
    • 0031004306 scopus 로고    scopus 로고
    • Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196
    • Perelle, S., Gibert, M., Bourlioux, P., Corthier, G. & Popoff, M. R. Production of a complete binary toxin (actin-specific ADP-ribosyltransferase) by Clostridium difficile CD196. Infect. Immun. 65, 1402-1407 (1997).
    • (1997) Infect. Immun. , vol.65 , pp. 1402-1407
    • Perelle, S.1    Gibert, M.2    Bourlioux, P.3    Corthier, G.4    Popoff, M.R.5
  • 107
    • 0024505395 scopus 로고
    • Production by Clostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity: Identification of a novel class of ADP-ribosyltransferases
    • Simpson, L. L., Stiles, B. G., Zepeda, H. & Wilkins, T. D. Production by Clostridium spiroforme of an iotalike toxin that possesses mono(ADP-ribosyl)transferase activity: Identification of a novel class of ADP-ribosyltransferases. Infect. Immun. 57, 255-261 (1989).
    • (1989) Infect. Immun. , vol.57 , pp. 255-261
    • Simpson, L.L.1    Stiles, B.G.2    Zepeda, H.3    Wilkins, T.D.4
  • 108
    • 80051693604 scopus 로고    scopus 로고
    • Actin as target for modification by bacterial protein toxins
    • Aktories, K., Lang, A. E., Schwan, C. & Mannherz, H. G. Actin as target for modification by bacterial protein toxins. FEBS J. 278, 4526-4543 (2011).
    • (2011) FEBS J. , vol.278 , pp. 4526-4543
    • Aktories, K.1    Lang, A.E.2    Schwan, C.3    Mannherz, H.G.4
  • 109
    • 34447291354 scopus 로고    scopus 로고
    • Anthrax toxin: Receptor binding, internalization, pore formation, and translocation
    • Young, J. A. T. & Collier, R. J. Anthrax toxin: Receptor binding, internalization, pore formation, and translocation. Annu. Rev. Biochem. 76, 243-265 (2007).
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 243-265
    • Young, J.A.T.1    Collier, R.J.2
  • 110
    • 80053636077 scopus 로고    scopus 로고
    • Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT)
    • Papatheodorou, P. et al. Lipolysis-stimulated lipoprotein receptor (LSR) is the host receptor for the binary toxin Clostridium difficile transferase (CDT). Proc. Natl Acad. Sci. USA 108, 16422-16427 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 16422-16427
    • Papatheodorou, P.1
  • 111
    • 0032876380 scopus 로고    scopus 로고
    • Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex
    • Han, S., Craig, J. A., Putnam, C. D., Carozzi, N. B. & Tainer, J. A. Evolution and mechanism from structures of an ADP-ribosylating toxin and NAD complex. Nature Struct. Biol. 6, 932-936 (1999).
    • (1999) Nature 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
  • 112
    • 0023612455 scopus 로고
    • Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg 177
    • Vandekerckhove, J., Schering, B., Bärmann, M. & Aktories, K. Clostridium perfringens iota toxin ADP-ribosylates skeletal muscle actin in Arg 177. FEBS Lett. 225, 48-52 (1987).
    • (1987) FEBS Lett. , vol.225 , pp. 48-52
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 113
    • 0023848539 scopus 로고
    • Botulinum C2 toxin ADP-ribosylates cytoplasmic β/γ-Actin in arginine 177
    • Vandekerckhove, J., Schering, B., Bärmann, M. & Aktories, K. Botulinum C2 toxin ADP-ribosylates cytoplasmic β/γ-Actin in arginine 177. J. Biol. Chem. 263, 696-700 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 696-700
    • Vandekerckhove, J.1    Schering, B.2    Bärmann, M.3    Aktories, K.4
  • 114
    • 0034819726 scopus 로고    scopus 로고
    • Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile
    • Gülke, I. et al. Characterization of the enzymatic component of the ADP-ribosyltransferase toxin CDTa from Clostridium difficile. Infect. Immun. 69, 6004-6011 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 6004-6011
    • Gülke, I.1
  • 115
    • 84891773348 scopus 로고    scopus 로고
    • Clostridium difficile binary toxin CDT: Mechanism, epidemiology, and potential clinical importance
    • Gerding, D. N., Johnson, S., Rupnik, M. & Aktories, K. Clostridium difficile binary toxin CDT: Mechanism, epidemiology, and potential clinical importance. Gut Microbes 5, 6-18 (2014).
    • (2014) Gut Microbes , vol.5 , pp. 6-18
    • Gerding, D.N.1    Johnson, S.2    Rupnik, M.3    Aktories, K.4
  • 116
    • 73449097193 scopus 로고    scopus 로고
    • Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria
    • Schwan, C. et al. Clostridium difficile toxin CDT induces formation of microtubule-based protrusions and increases adherence of bacteria. PLoS Pathog. 5, e1000626 (2009).
    • (2009) PLoS Pathog. , vol.5
    • Schwan, C.1
  • 117
    • 84893871106 scopus 로고    scopus 로고
    • Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence
    • Schwan, C. et al. Clostridium difficile toxin CDT hijacks microtubule organization and reroutes vesicle traffic to increase pathogen adherence. Proc. Natl Acad. Sci. USA 111, 2313-2318 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 2313-2318
    • Schwan, C.1
  • 118
    • 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, M. L., Reiner, N. E., Fierer, J. & Guiney, D. G. The Salmonella spvB virulence gene encodes an enzyme that ADP-ribosylates actin and destabilizes the cytoskeleton of eukaryotic cells. Mol. Microbiol. 39, 1464-1470 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 1464-1470
    • Lesnick, M.L.1    Reiner, N.E.2    Fierer, J.3    Guiney, D.G.4
  • 119
    • 0033812602 scopus 로고    scopus 로고
    • The spvB gene-product of the Salmonella enterica virulence plasmid is a mono(ADP-ribosyl)transferase
    • Otto, H. et al. The spvB gene-product of the Salmonella enterica virulence plasmid is a mono(ADP-ribosyl)transferase. Mol. Microbiol. 37, 1106-1115 (2000).
    • (2000) Mol. Microbiol. , vol.37 , pp. 1106-1115
    • Otto, H.1
  • 120
    • 0036208813 scopus 로고    scopus 로고
    • Characterization of an ADP-ribosyltransferase toxin (AexT) from Aeromonas salmonicida subsp. Salmonicida
    • Braun, M. et al. Characterization of an ADP-ribosyltransferase toxin (AexT) from Aeromonas salmonicida subsp. salmonicida. J. Bacteriol. 184, 1851-1858 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 1851-1858
    • Braun, M.1
  • 121
    • 35348947419 scopus 로고    scopus 로고
    • Aeromonas exoenzyme T of Aeromonas salmonicida is a bifunctional protein that targets the host cytoskeleton
    • Fehr, D. et al. Aeromonas exoenzyme T of Aeromonas salmonicida is a bifunctional protein that targets the host cytoskeleton. J. Biol. Chem. 282, 28843-28852 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 28843-28852
    • Fehr, D.1
  • 122
    • 77951600828 scopus 로고    scopus 로고
    • Photox, a novel actin-Targeting mono-ADP-ribosyltransferase from Photorhabdus luminescens
    • Visschedyk, D. D. et al. Photox, a novel actin-Targeting mono-ADP-ribosyltransferase from Photorhabdus luminescens. J. Biol. Chem. 285, 13525-13534 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 13525-13534
    • Visschedyk, D.D.1
  • 123
    • 31544444417 scopus 로고    scopus 로고
    • Salmonella enterica SpvB ADP-ribosylates actin at position arginine-177 Characterization of the catalytic domain within the SpvB protein and a comparison to binary clostridial actin-ADP-ribosylating toxins
    • Hochmann, H., Pust, S., von Figura, G., Aktories, K. & Barth, H. Salmonella enterica SpvB ADP-ribosylates actin at position arginine-177. Characterization of the catalytic domain within the SpvB protein and a comparison to binary clostridial actin-ADP-ribosylating toxins. Biochemistry 45, 1271-1277 (2006).
    • (2006) Biochemistry , vol.45 , pp. 1271-1277
    • Hochmann, H.1    Pust, S.2    Von Figura, G.3    Aktories, K.4    Barth, H.5
  • 124
    • 36849042170 scopus 로고    scopus 로고
    • Aeromonas hydrophila AH 3 AexT is an ADP-ribosylating toxin secreted through the type III secretion system
    • Vilches, S. et al. Aeromonas hydrophila AH 3 AexT is an ADP-ribosylating toxin secreted through the type III secretion system. Microb. Pathog. 44, 1-12 (2008).
    • (2008) Microb. Pathog. , vol.44 , pp. 1-12
    • Vilches, S.1
  • 126
    • 0024510722 scopus 로고
    • Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin
    • Coburn, J., Dillon, S. T., Iglewski, B. H. & Gill, D. M. Exoenzyme S of Pseudomonas aeruginosa ADP-ribosylates the intermediate filament protein vimentin. Infection Immun. 57, 996-998 (1989).
    • (1989) Infection Immun. , vol.57 , pp. 996-998
    • Coburn, J.1    Dillon, S.T.2    Iglewski, B.H.3    Gill, D.M.4
  • 127
    • 0024356764 scopus 로고
    • Several GTP-binding proteins, including p21c H ras, are preferred substrates of Pseudomonas aeruginosa exoenzyme S
    • Coburn, J., Wyatt, R. T., Iglewski, B. H. & Gill, D. M. Several GTP-binding proteins, including p21c H ras, are preferred substrates of Pseudomonas aeruginosa exoenzyme S. J. Biol. Chem. 264, 9004-9008 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 9004-9008
    • Coburn, J.1    Wyatt, R.T.2    Iglewski, B.H.3    Gill, D.M.4
  • 128
    • 33947173091 scopus 로고    scopus 로고
    • Aeromonas salmonicida toxin AexT has a Rho family GTPase-Activating protein domain
    • Litvak, Y. & Selinger, Z. Aeromonas salmonicida toxin AexT has a Rho family GTPase-Activating protein domain. J. Bacteriol. 189, 2558-2560 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 2558-2560
    • Litvak, Y.1    Selinger, Z.2
  • 129
    • 0023779031 scopus 로고
    • Functional modification of a 21 kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum
    • Rubin, E. J., Gill, D. M., Boquet, P. & Popoff, M. R. Functional modification of a 21 kilodalton G protein when ADP-ribosylated by exoenzyme C3 of Clostridium botulinum. Mol. Cell. Biol. 8, 418-426 (1988).
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 418-426
    • Rubin, E.J.1    Gill, D.M.2    Boquet, P.3    Popoff, M.R.4
  • 130
    • 0042026577 scopus 로고    scopus 로고
    • Rho-specific Bacillus cereus ADP-ribosyltransferase C3cer cloning and characterization
    • Wilde, C., Vogelsgesang, M. & Aktories, K. Rho-specific Bacillus cereus ADP-ribosyltransferase C3cer cloning and characterization. Biochemistry 42, 9694-9702 (2003).
    • (2003) Biochemistry , vol.42 , pp. 9694-9702
    • Wilde, C.1    Vogelsgesang, M.2    Aktories, K.3
  • 131
    • 84880162772 scopus 로고    scopus 로고
    • Signaling networks of Rho GTPases in cell motility
    • Hanna, S. & El Sibai, M. Signaling networks of Rho GTPases in cell motility. Cell Signall. 25, 1955-1961 (2013).
    • (2013) Cell Signall. , vol.25 , pp. 1955-1961
    • Hanna, S.1    El Sibai, M.2
  • 132
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • Heasman, S. J. & Ridley, A. J. Mammalian Rho GTPases: New insights into their functions from in vivo studies. Nature Rev. Mol. Cell Biol. 9, 690-701 (2008).
    • (2008) Nature Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 133
    • 0024353843 scopus 로고
    • Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase
    • Sekine, A., Fujiwara, M. & Narumiya, S. Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 8602-8605
    • Sekine, A.1    Fujiwara, M.2    Narumiya, S.3
  • 135
    • 0041707712 scopus 로고    scopus 로고
    • Entrapment of rho adp-ribosylated by clostridium botulinum c3 exoenzyme in the rho-guanine nucleotide dissociation inhibitor 1 complex
    • Genth, H. et al. Entrapment of Rho ADP-ribosylated by Clostridium botulinum C3 exoenzyme in the Rho-guanine nucleotide dissociation inhibitor 1 complex. J. Biol. Chem. 278, 28523-28527 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 28523-28527
    • Genth, H.1
  • 136
    • 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. et al. Neosynthesis and activation of Rho by Escherichia coli cytotoxic necrotizing factor (CNF1) reverse cytopathic effects of ADP-ribosylated Rho. J. Biol. Chem. 274, 27407-27414 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 27407-27414
    • Barth, H.1
  • 137
    • 27144457720 scopus 로고    scopus 로고
    • Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme
    • Pautsch, A., Vogelsgesang, M., Tränkle, J., Herrmann, C. & Aktories, K. Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. EMBO J. 24, 3670-3680 (2005).
    • (2005) EMBO J. , vol.24 , pp. 3670-3680
    • Pautsch, A.1    Vogelsgesang, M.2    Tränkle, J.3    Herrmann, C.4    Aktories, K.5
  • 138
    • 0035937815 scopus 로고    scopus 로고
    • Novel c3 like adp-ribosyltransferase from staphylococcus aureus modifying rhoe and rnd3
    • Wilde, C., Chhatwal, G. S., Schmalzing, G., Aktories, K. & Just, I. A. Novel C3 like ADP-ribosyltransferase from Staphylococcus aureus. Modifying RhoE and Rnd3. J. Biol. Chem. 276, 9537-9542 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 9537-9542
    • Wilde, C.1    Chhatwal, G.S.2    Schmalzing, G.3    Aktories, K.4    Just, I.A.5
  • 139
    • 33646905907 scopus 로고    scopus 로고
    • Localization of the C3 Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells
    • Molinari, G. et al. Localization of the C3 Like ADP-ribosyltransferase from Staphylococcus aureus during bacterial invasion of mammalian cells. Infect. Immun. 74, 3673-3677 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 3673-3677
    • Molinari, G.1
  • 140
    • 77649216057 scopus 로고    scopus 로고
    • Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes
    • Fahrer, J. et al. Selective and specific internalization of clostridial C3 ADP-ribosyltransferases into macrophages and monocytes. Cell. Microbiol. 12, 233-247 (2010).
    • (2010) Cell. Microbiol. , vol.12 , pp. 233-247
    • Fahrer, J.1
  • 141
    • 84891372332 scopus 로고    scopus 로고
    • To harm or not to harm? On the evolution and expression of virulence in group A streptococci
    • Wollein Waldetoft, K. & Råberg, L. To harm or not to harm? On the evolution and expression of virulence in group A streptococci. Trends Microbiol. 22, 7-13 (2014).
    • (2014) Trends Microbiol. , vol.22 , pp. 7-13
    • Wollein Waldetoft, K.1    Råberg, L.2
  • 142
    • 0035836659 scopus 로고    scopus 로고
    • Complete genome sequence of an M1 strain of Streptococcus pyogenes
    • Ferretti, J. J. et al. Complete genome sequence of an M1 strain of Streptococcus pyogenes. Proc. Natl Acad. Sci. USA 98, 4658-4663 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4658-4663
    • Ferretti, J.J.1
  • 143
    • 4744346611 scopus 로고    scopus 로고
    • Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes
    • Coye, L. H. & Collins, C. M. Identification of SpyA, a novel ADP-ribosyltransferase of Streptococcus pyogenes. Mol. Microbiol. 54, 89-98 (2004).
    • (2004) Mol. Microbiol. , vol.54 , pp. 89-98
    • Coye, L.H.1    Collins, C.M.2
  • 144
    • 84857356903 scopus 로고    scopus 로고
    • SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide
    • Korotkova, N. et al. SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide, SpyB. Mol. Microbiol. 83, 936-952 (2012).
    • (2012) SpyB. Mol. Microbiol. , vol.83 , pp. 936-952
    • Korotkova, N.1
  • 145
    • 34249682108 scopus 로고    scopus 로고
    • Novel functions of vimentin in cell adhesion, migration, and signaling
    • Ivaska, J., Pallari, H. M., Nevo, J. & Eriksson, J. E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp. Cell Res. 313, 2050-2062 (2007).
    • (2007) Exp. Cell Res. , vol.313 , pp. 2050-2062
    • Ivaska, J.1    Pallari, H.M.2    Nevo, J.3    Eriksson, J.E.4
  • 146
    • 0033859762 scopus 로고    scopus 로고
    • Impaired wound healing in embryonic and adult mice lacking vimentin
    • Eckes, B. et al. Impaired wound healing in embryonic and adult mice lacking vimentin. J. Cell Sci. 113, 2455-2462 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 2455-2462
    • Eckes, B.1
  • 147
    • 84862303967 scopus 로고    scopus 로고
    • Molecular and biological characterization of streptococcal SpyA-mediated ADP-ribosylation of intermediate filament protein vimentin
    • Icenogle, L. M. et al. Molecular and biological characterization of streptococcal SpyA-mediated ADP-ribosylation of intermediate filament protein vimentin. J. Biol. Chem. 287, 21481-21491 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 21481-21491
    • Icenogle, L.M.1
  • 148
    • 0035793427 scopus 로고    scopus 로고
    • Phosphorylation of vimentin head domain inhibits interaction with the carboxyl-Terminal end of α helical rod domain studied by surface plasmon resonance measurements
    • Gohara, R. et al. Phosphorylation of vimentin head domain inhibits interaction with the carboxyl-Terminal end of α helical rod domain studied by surface plasmon resonance measurements. FEBS Lett. 489, 182-186 (2001).
    • (2001) FEBS Lett. , vol.489 , pp. 182-186
    • Gohara, R.1
  • 149
    • 79959412072 scopus 로고    scopus 로고
    • SpyA a C3 Like ADP-ribosyltransferase, contributes to virulence in a mouse subcutaneous model of Streptococcus pyogenes infection
    • Hoff, J. S., DeWald, M., Moseley, S. L., Collins, C. M. & Voyich, J. M. SpyA, a C3 Like ADP-ribosyltransferase, contributes to virulence in a mouse subcutaneous model of Streptococcus pyogenes infection. Infection Immun. 79, 2404-2411 (2011).
    • (2011) Infection Immun. , vol.79 , pp. 2404-2411
    • Hoff, J.S.1    DeWald, M.2    Moseley, S.L.3    Collins, C.M.4    Voyich, J.M.5
  • 150
    • 0036500995 scopus 로고    scopus 로고
    • A functional screen for the type III (Hrp) secretome of the plant pathogen Pseudomonas syringae
    • Guttman, D. S. et al. A functional screen for the type III (Hrp) secretome of the plant pathogen Pseudomonas syringae. Science 295, 1722-1726 (2002).
    • (2002) Science , vol.295 , pp. 1722-1726
    • Guttman, D.S.1
  • 151
    • 0037188539 scopus 로고    scopus 로고
    • Genomewide identification of proteins secreted by the Hrp type III protein secretion system of Pseudomonas syringae pv tomato DC3000
    • Petnicki-Ocwieja, T. et al. Genomewide identification of proteins secreted by the Hrp type III protein secretion system of Pseudomonas syringae pv. tomato DC3000. Proc. Natl Acad. Sci. USA 99, 7652-7657 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7652-7657
    • Petnicki-Ocwieja, T.1
  • 152
    • 33750213711 scopus 로고    scopus 로고
    • Closing the circle on the discovery of genes encoding Hrp regulon members and type III secretion system effectors in the genomes of three model Pseudomonas syringae strains
    • Lindeberg, M. et al. Closing the circle on the discovery of genes encoding Hrp regulon members and type III secretion system effectors in the genomes of three model Pseudomonas syringae strains. Mol. Plant Microbe Interact. 19, 1151-1158 (2006).
    • (2006) Mol. Plant Microbe Interact. , vol.19 , pp. 1151-1158
    • Lindeberg, M.1
  • 153
    • 0037133169 scopus 로고    scopus 로고
    • Genomewide identification of Pseudomonas syringae pv tomato DC3000 promoters controlled by the HrpL alternative sigma factor
    • Fouts, D. E. et al. Genomewide identification of Pseudomonas syringae pv. tomato DC3000 promoters controlled by the HrpL alternative sigma factor. Proc. Natl Acad. Sci. USA 99, 2275-2280 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 2275-2280
    • Fouts, D.E.1
  • 154
    • 0041335630 scopus 로고    scopus 로고
    • The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv tomato DC3000
    • Buell, C. R. et al. The complete genome sequence of the Arabidopsis and tomato pathogen Pseudomonas syringae pv. tomato DC3000. Proc. Natl Acad. Sci. USA 100, 10181-10186 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 10181-10186
    • Buell, C.R.1
  • 155
    • 34249064705 scopus 로고    scopus 로고
    • A type III effector ADP-ribosylates RNA-binding proteins and quells plant immunity
    • Fu, Z. Q. et al. A type III effector ADP-ribosylates RNA-binding proteins and quells plant immunity. Nature 447, 284-288 (2007).
    • (2007) Nature , vol.447 , pp. 284-288
    • Fu, Z.Q.1
  • 156
    • 83355169694 scopus 로고    scopus 로고
    • Structure function analysis of an ADP-ribosyltransferase type III effector and its RNA-binding target in plant immunity
    • Jeong, B.R. et al. Structure function analysis of an ADP- ribosyltransferase type III effector and its RNA-binding target in plant immunity. J. Biol. Chem. 286, 43272-43281 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 43272-43281
    • Jeong, B.R.1
  • 157
    • 0041355556 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa ExoT ADP-ribosylates CT10 regulator of kinase (Crk) proteins
    • Sun, J. & Barbieri, J. T. Pseudomonas aeruginosa ExoT ADP-ribosylates CT10 regulator of kinase (Crk) proteins. J. Biol. Chem. 278, 32794-32800 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 32794-32800
    • Sun, J.1    Barbieri, J.T.2
  • 159
    • 0030873319 scopus 로고    scopus 로고
    • AtGRP7, a nuclear RNA-binding protein as a component of a circadian-regulated negative feedback loop in Arabidopsis thaliana
    • Heintzen, C., Nater, M., Apel, K. & Staiger, D. AtGRP7, a nuclear RNA-binding protein as a component of a circadian-regulated negative feedback loop in Arabidopsis thaliana. Proc. Natl Acad. Sci. USA 94, 8515-8520 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 8515-8520
    • Heintzen, C.1    Nater, M.2    Apel, K.3    Staiger, D.4
  • 160
    • 84875222858 scopus 로고    scopus 로고
    • Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7
    • Nicaise, V. et al. Pseudomonas HopU1 modulates plant immune receptor levels by blocking the interaction of their mRNAs with GRP7. EMBO J. 32, 701-712 (2013).
    • (2013) EMBO J. , vol.32 , pp. 701-712
    • Nicaise, V.1
  • 161
    • 0025938601 scopus 로고
    • Identification of molecular contacts between the U1, a small nuclear ribonucleoprotein and U1 RNA
    • Jessen, T. H., Oubridge, C., Teo, C. H., Pritchard, C. & Nagai, K. Identification of molecular contacts between the U1, a small nuclear ribonucleoprotein and U1 RNA. EMBO J. 10, 3447-3456 (1991).
    • (1991) EMBO J. , vol.10 , pp. 3447-3456
    • Jessen, T.H.1    Oubridge, C.2    Teo, C.H.3    Pritchard, C.4    Nagai, K.5
  • 162
    • 0028129989 scopus 로고
    • Conserved structures and diversity of functions of RNA-binding proteins
    • Burd, C. & Dreyfuss, G. Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621 (1994).
    • (1994) Science , vol.265 , pp. 615-621
    • Burd, C.1    Dreyfuss, G.2
  • 163
    • 0025221731 scopus 로고
    • Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A
    • Nagai, K., Oubridge, C., Jessen, T H., Li, J. & Evans, P. R. Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A. Nature 348, 515-520 (1990).
    • (1990) Nature , vol.348 , pp. 515-520
    • Nagai, K.1    Oubridge, C.2    Jessen, T.H.3    Li, J.4    Evans, P.R.5
  • 164
    • 0030671070 scopus 로고    scopus 로고
    • Chemical shift mapping of the RNA-binding interface of the multiple-RBD protein sex-lethal
    • Lee, A. L. et al. Chemical shift mapping of the RNA-binding interface of the multiple-RBD protein sex-lethal. Biochemistry 36, 14306-14317 (1997).
    • (1997) Biochemistry , vol.36 , pp. 14306-14317
    • Lee, A.L.1
  • 165
    • 36849007471 scopus 로고    scopus 로고
    • Auto-regulation of the circadian slave oscillator component AtGRP7 and regulation of its targets is impaired by a single RNA recognition motif point mutation
    • Schfning, J. C. et al. Auto-regulation of the circadian slave oscillator component AtGRP7 and regulation of its targets is impaired by a single RNA recognition motif point mutation. Plant J. 52, 1119-1130 (2007).
    • (2007) Plant J. , vol.52 , pp. 1119-1130
    • Schfning, J.C.1
  • 166
    • 65649123807 scopus 로고    scopus 로고
    • Innate immunity in plants: An arms race between pattern recognition receptors in plants and effectors in microbial pathogens
    • Boller, T. & He, S. Y. Innate immunity in plants: An arms race between pattern recognition receptors in plants and effectors in microbial pathogens. Science 324, 742-744 (2009).
    • (2009) Science , vol.324 , pp. 742-744
    • Boller, T.1    He, S.Y.2
  • 167
    • 77954763024 scopus 로고    scopus 로고
    • Plant immunity: Towards an integrated view of plant-pathogen interactions
    • Dodds, P. N. & Rathjen, J. P. Plant immunity: Towards an integrated view of plant-pathogen interactions. Nature Rev. Genet. 11, 539-548 (2010).
    • (2010) Nature Rev. Genet. , vol.11 , pp. 539-548
    • Dodds, P.N.1    Rathjen, J.P.2
  • 168
    • 79551682471 scopus 로고    scopus 로고
    • Activation of plant pattern-recognition receptors by bacteria
    • Segonzac, C. & Zipfel, C. Activation of plant pattern-recognition receptors by bacteria. Curr. Opin. Microbiol. 14, 54-61 (2011).
    • (2011) Curr. Opin. Microbiol. , vol.14 , pp. 54-61
    • Segonzac, C.1    Zipfel, C.2
  • 169
    • 84857512851 scopus 로고    scopus 로고
    • A first step in bringing typhoid fever out of the closet
    • Maurice, J. A first step in bringing typhoid fever out of the closet. Lancet 379, 699-700 (2012).
    • (2012) Lancet , vol.379 , pp. 699-700
    • Maurice, J.1
  • 170
    • 1842585488 scopus 로고    scopus 로고
    • Salmonella Typhi encodes a functional cytolethal distending toxin that is delivered into host cells by a bacterial-internalization pathway
    • Haghjoo, E. & Galán, J. E. Salmonella Typhi encodes a functional cytolethal distending toxin that is delivered into host cells by a bacterial-internalization pathway. Proc. Natl Acad. Sci. USA 101, 4614-4619 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4614-4619
    • Haghjoo, E.1    Galán, J.E.2
  • 171
    • 38049046618 scopus 로고    scopus 로고
    • Delivery of a Salmonella Typhi exotoxin from a host intracellular compartment
    • Spanò, S., Ugalde, J. E. & Gal án, J. E. Delivery of a Salmonella Typhi exotoxin from a host intracellular compartment. Cell Host Microbe 3, 30-38 (2008).
    • (2008) Cell Host Microbe , vol.3 , pp. 30-38
    • Spanò, S.1    Ugalde, J.E.2    Galán, J.E.3
  • 172
    • 84887617040 scopus 로고    scopus 로고
    • Salmonella enterica delivers its genotoxin through outer membrane vesicles secreted from infected cells
    • Guidi, R. et al. Salmonella enterica delivers its genotoxin through outer membrane vesicles secreted from infected cells. Cell. Microbiol. 15, 2034-2050 (2013).
    • (2013) Cell. Microbiol. , vol.15 , pp. 2034-2050
    • Guidi, R.1
  • 177
    • 33644928093 scopus 로고    scopus 로고
    • eds Laskin A. I. Bennett J. W. Gadd G. M. & Sariaslani S.) Academic Press
    • Ffrench-Constant, R. & Waterfield, N. in Advances in Applied Microbiology (eds Laskin, A. I., Bennett, J. W., Gadd, G. M. & Sariaslani, S.) 169-183 (Academic Press, 2005).
    • (2005) Advances in Applied Microbiology , pp. 169-183
    • Ffrench-Constant, R.1    Waterfield, N.2
  • 178
    • 84875620662 scopus 로고    scopus 로고
    • A syringe-like injection mechanism in Photorhabdus luminescens toxins
    • Gatsogiannis, C. et al. A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature 495, 520-523 (2013).
    • (2013) Nature , vol.495 , pp. 520-523
    • Gatsogiannis, C.1
  • 179
    • 0037268543 scopus 로고    scopus 로고
    • Photorhabdus: Towards a functional genomic analysis of a symbiont and pathogen
    • Ffrench-Constant, R. et al. Photorhabdus: Towards a functional genomic analysis of a symbiont and pathogen. FEMS Microbiol. Rev. 26, 433-456 (2003).
    • (2003) FEMS Microbiol. Rev. , vol.26 , pp. 433-456
    • Ffrench-Constant, R.1
  • 180
    • 0026439926 scopus 로고
    • Thymosin β4 sequesters the majority of G actin in resting human polymorphonuclear leukocytes
    • Cassimeris, L., Safer, D., Nachmias, V. T. & Zigmond, S. H. Thymosin β4 sequesters the majority of G actin in resting human polymorphonuclear leukocytes. J. Cell Biol. 119, 1261-1270 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 1261-1270
    • Cassimeris, L.1    Safer, D.2    Nachmias, V.T.3    Zigmond, S.H.4
  • 181
    • 70349413077 scopus 로고    scopus 로고
    • The β thymosins: Intracellular and extracellular activities of a versatile actin binding protein family
    • Mannherz, H. G. & Hannappel, E. The β thymosins: Intracellular and extracellular activities of a versatile actin binding protein family. Cell. Motil. Cytoskeleton 66, 839-851 (2009).
    • (2009) Cell. Motil. Cytoskeleton , vol.66 , pp. 839-851
    • Mannherz, H.G.1    Hannappel, E.2
  • 182
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter, I. R. & Wittinghofer, A. The guanine nucleotide-binding switch in three dimensions. Science 294, 1299-1304 (2001).
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 183
    • 84897574368 scopus 로고    scopus 로고
    • Mechanism of Tc toxin action revealed in molecular detail
    • Meusch, D. et al. Mechanism of Tc toxin action revealed in molecular detail. Nature 508, 61-65 (2014).
    • (2014) Nature , vol.508 , pp. 61-65
    • Meusch, D.1
  • 184
    • 0024041593 scopus 로고
    • Molecular Koch's postulates applied to microbial pathogenicity
    • Falkow, S. Molecular Koch's postulates applied to microbial pathogenicity. Rev. Infect. Dis. 10 (Suppl. 2) 274-276 (1988).
    • (1988) Rev. Infect. Dis. , vol.10 , Issue.SUPPL. 2 , pp. 274-276
    • Falkow, S.1
  • 185
    • 1842434337 scopus 로고    scopus 로고
    • Molecular Koch's postulates applied to bacterial pathogenicity-A personal recollection 15 years later
    • Falkow, S. Molecular Koch's postulates applied to bacterial pathogenicity-A personal recollection 15 years later. Nature Rev. Microbiol. 2, 67-72 (2004).
    • (2004) Nature Rev. Microbiol. , vol.2 , pp. 67-72
    • Falkow, S.1
  • 186
    • 84864544419 scopus 로고    scopus 로고
    • A comparison of computational methods for identifying virulence factors
    • Zheng, L. L. et al. A comparison of computational methods for identifying virulence factors. PLoS ONE 7, e42517 (2012).
    • (2012) PLoS ONE , vol.7
    • Zheng, L.L.1
  • 188
    • 35348932100 scopus 로고    scopus 로고
    • A comprehensive system for evaluation of remote sequence similarity detection
    • Qi, Y., Sadreyev, R. I., Wang, Y., Kim, B. H. & Grishin, N. V. A comprehensive system for evaluation of remote sequence similarity detection. BMC Bioinformatics 8, 314 (2007).
    • (2007) BMC Bioinformatics , vol.8 , pp. 314
    • Qi, Y.1    Sadreyev, R.I.2    Wang, Y.3    Kim, B.H.4    Grishin, N.V.5
  • 189
    • 0023669148 scopus 로고
    • Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene
    • Palmiter, R. D. et al. Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene. Cell 50, 435-443 (1987).
    • (1987) Cell , vol.50 , pp. 435-443
    • Palmiter, R.D.1
  • 190
    • 0034899321 scopus 로고    scopus 로고
    • Diphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice
    • Saito, M. et al. Diphtheria toxin receptor-mediated conditional and targeted cell ablation in transgenic mice. Nature Biotech. 19, 746-750 (2001).
    • (2001) Nature Biotech. , vol.19 , pp. 746-750
    • Saito, M.1
  • 191
    • 21444454735 scopus 로고    scopus 로고
    • A Cre-inducible diphtheria toxin receptor mediates cell lineage ablation after toxin administration
    • Buch, T. et al. A Cre-inducible diphtheria toxin receptor mediates cell lineage ablation after toxin administration. Nature Meth. 2, 419-426 (2005).
    • (2005) Nature Meth. , vol.2 , pp. 419-426
    • Buch, T.1
  • 192
    • 0024349836 scopus 로고
    • A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin
    • Chaudhary, V. K. et al. A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature 339, 394-397 (1989).
    • (1989) Nature , vol.339 , pp. 394-397
    • Chaudhary, V.K.1
  • 193
    • 0038290547 scopus 로고    scopus 로고
    • Immunotoxins containing Pseudomonas exotoxin A: A short history
    • Pastan, I. Immunotoxins containing Pseudomonas exotoxin A: A short history. Cancer Immunol. Immunother. 52, 338-341 (2003).
    • (2003) Cancer Immunol. Immunother. , vol.52 , pp. 338-341
    • Pastan, I.1
  • 194
    • 80054118081 scopus 로고    scopus 로고
    • Antibody fusion proteins: Anti CD22 recombinant immunotoxin moxetumomab pasudotox
    • Kreitman, R. J. & Pastan, I. Antibody fusion proteins: Anti CD22 recombinant immunotoxin moxetumomab pasudotox. Clin. Cancer Res. 17, 6398-6405 (2011).
    • (2011) Clin. Cancer Res. , vol.17 , pp. 6398-6405
    • Kreitman, R.J.1    Pastan, I.2
  • 195
    • 0035954624 scopus 로고    scopus 로고
    • Efficacy of the anti CD22 recombinant immunotoxin BL22 in chemotherapy-resistant hairy-cell leukemia
    • Kreitman, R. J. et al. Efficacy of the anti CD22 recombinant immunotoxin BL22 in chemotherapy-resistant hairy-cell leukemia. New Engl. J. Med. 345, 241-247 (2001).
    • (2001) New Engl. J. Med. , vol.345 , pp. 241-247
    • Kreitman, R.J.1
  • 196
    • 0023784225 scopus 로고
    • Selective killing of HIV-infected cells by recombinant human CD4 Pseudomonas exotoxin hybrid protein
    • Chaudhary, V. K. et al. Selective killing of HIV-infected cells by recombinant human CD4 Pseudomonas exotoxin hybrid protein. Nature 335, 369-372 (1988).
    • (1988) Nature , vol.335 , pp. 369-372
    • Chaudhary, V.K.1
  • 197
    • 77954685640 scopus 로고    scopus 로고
    • Immunotoxin complementation of HAART to deplete persisting HIV-infected cell reservoirs
    • Berger, E. A. & Pastan, I. Immunotoxin complementation of HAART to deplete persisting HIV-infected cell reservoirs. PLoS Pathog. 6, e1000803 (2010).
    • (2010) PLoS Pathog. , vol.6
    • Berger, E.A.1    Pastan, I.2
  • 198
    • 77950473461 scopus 로고    scopus 로고
    • Initial characterization of an immunotoxin constructed from domains II and III of cholera exotoxin
    • Sarnovsky, R. et al. Initial characterization of an immunotoxin constructed from domains II and III of cholera exotoxin. Cancer Immunol. Immunother. 59, 737-746 (2010).
    • (2010) Cancer Immunol. Immunother. , vol.59 , pp. 737-746
    • Sarnovsky, R.1
  • 199
    • 0034073932 scopus 로고    scopus 로고
    • Enhancement of diphtheria toxin potency by replacement of the receptor binding domain with tetanus toxin C fragment
    • Francis, J. W. et al. Enhancement of diphtheria toxin potency by replacement of the receptor binding domain with tetanus toxin C fragment. J. Neurochem. 74, 2528-2536 (2000).
    • (2000) J. Neurochem. , vol.74 , pp. 2528-2536
    • Francis, J.W.1
  • 200
    • 3042770615 scopus 로고    scopus 로고
    • Differential effects of Rho GTPases on axonal and dendritic development in hippocampal neurones
    • Ahnert-Hilger, G. et al. Differential effects of Rho GTPases on axonal and dendritic development in hippocampal neurones. J. Neurochem. 90, 9-18 (2004).
    • (2004) J. Neurochem. , vol.90 , pp. 9-18
    • Ahnert-Hilger, G.1
  • 201
    • 33751178359 scopus 로고    scopus 로고
    • Enhanced survival and regeneration of axotomized retinal neurons by repeated delivery of cell-permeable C3 like Rho antagonists
    • Bertrand, J., Di Polo, A. & McKerracher, L. Enhanced survival and regeneration of axotomized retinal neurons by repeated delivery of cell-permeable C3 like Rho antagonists. Neurobiol. Dis. 25, 65-72 (2007).
    • (2007) Neurobiol. Dis. , vol.25 , pp. 65-72
    • Bertrand, J.1    Di Polo, A.2    McKerracher, L.3
  • 202
    • 65349128735 scopus 로고    scopus 로고
    • A 29 amino acid fragment of Clostridium botulinum C3 protein enhances neuronal outgrowth, connectivity, and reinnervation
    • Hfltje, M. et al. A 29 amino acid fragment of Clostridium botulinum C3 protein enhances neuronal outgrowth, connectivity, and reinnervation. FASEB J. 23, 1115-1126 (2009).
    • (2009) FASEB J. , vol.23 , pp. 1115-1126
    • Hfltje, M.1
  • 203
    • 13944274451 scopus 로고    scopus 로고
    • Application of Rho antagonist to neuronal cell bodies promotes neurite growth in compartmented cultures and regeneration of retinal ganglion cell axons in the optic nerve of adult rats
    • Bertrand, J., Winton, M. J., Rodriguez-Hernandez, N., Campenot, R. B. & McKerracher, L. Application of Rho antagonist to neuronal cell bodies promotes neurite growth in compartmented cultures and regeneration of retinal ganglion cell axons in the optic nerve of adult rats. J. Neurosci. 25, 1113-1121 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 1113-1121
    • Bertrand, J.1    Winton, M.J.2    Rodriguez-Hernandez, N.3    Campenot, R.B.4    McKerracher, L.5
  • 204
    • 77952368484 scopus 로고    scopus 로고
    • C3 peptide enhances recovery from spinal cord injury by improved regenerative growth of descending fiber tracts
    • Boato, F. et al. C3 peptide enhances recovery from spinal cord injury by improved regenerative growth of descending fiber tracts. J. Cell Sci. 123, 1652-1662 (2010)..
    • (2010) J. Cell Sci. , vol.123 , pp. 1652-1662
    • Boato, F.1


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