메뉴 건너뛰기




Volumn , Issue , 2008, Pages 33-45

Pertussis Toxin

Author keywords

ADP ribosyltransferase; Agrobacterium tumefaciens; Dermonecrotic toxin; Pertussis toxin; Pharmacological

Indexed keywords


EID: 0010881981     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527614615.ch3     Document Type: Chapter
Times cited : (4)

References (58)
  • 1
    • 84954248263 scopus 로고    scopus 로고
    • Bacterial Toxins. © Chapman & Hall, Weinheim
    • K. Aktories (Ed.), Bacterial Toxins. © Chapman & Hall, Weinheim, 1997. ISBN 3-8261-0080-8
    • (1997)
    • Aktories, K.1
  • 2
    • 84920205236 scopus 로고
    • Placebo-controlled trial of two acellular pertussis vaccines in Sweden - protective efficacy and adverse events
    • Ad hoc group for the study of pertussis vaccines (1988): Placebo-controlled trial of two acellular pertussis vaccines in Sweden - protective efficacy and adverse events. In Lancet ii: 955-960.
    • (1988) In Lancet , vol.2 , pp. 955-960
  • 3
    • 0022540281 scopus 로고
    • Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Ångstrom resolution
    • Allured VS, Collier RJ, Carroll SF, et al. (1986): Structure of exotoxin A of Pseudomonas aeruginosa at 3.0-Ångstrom resolution. In Proc. Natl. Acad. Sci. USA 83: 1320-1324.
    • (1986) In Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1320-1324
    • Allured, V.S.1    Collier, R.J.2    Carroll, S.F.3
  • 4
    • 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 (1990): Roles of the disulfide bond and the carboxy-terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin. In Infect. Immun. 58: 1518-1526.
    • (1990) In Infect. Immun , vol.58 , pp. 1518-1526
    • Antoine, R.1    Locht, C.2
  • 5
    • 0028231026 scopus 로고
    • The NAD-glycohydrolase activity of the pertussis toxin S1 subunit: Involvement of the catalytic His-35 residue
    • Antoine R, Locht C (1994): The NAD-glycohydrolase activity of the pertussis toxin S1 subunit: involvement of the catalytic His-35 residue. In J. Biol. Chem. 269: 6450-6457.
    • (1994) In J. Biol. Chem , vol.269 , pp. 6450-6457
    • Antoine, R.1    Locht, C.2
  • 6
    • 84954231622 scopus 로고
    • Genetic organization of the pertussis toxin locus
    • Antoine R, Raze D, Locht C. (1995): Genetic organization of the pertussis toxin locus. In Zbl. Bakteriol. Suppl. 28: 44-45.
    • (1995) In Zbl. Bakteriol. Suppl , vol.28 , pp. 44-45
    • Antoine, R.1    Raze, D.2    Locht, C.3
  • 7
    • 0027484158 scopus 로고
    • Evidence for a catalytic role of glutamic acid 129 in the NAD-glycohydrolase activity of the pertussis toxin S1 subunit
    • Antoine R, Tallett A, van Heyningen S, et al. (1993): Evidence for a catalytic role of glutamic acid 129 in the NAD-glycohydrolase activity of the pertussis toxin S1 subunit. In J. Biol. Chem. 268: 24149-24155.
    • (1993) In J. Biol. Chem , vol.268 , pp. 24149-24155
    • Antoine, R.1    Tallett, A.2    van Heyningen, S.3
  • 8
    • 0023228057 scopus 로고
    • Bordetella parapertussis and Bordetella bronchiseptica contain transcriptionnally silent pertussis toxin genes
    • Arico B, Rappuoli R (1987): Bordetella parapertussis and Bordetella bronchiseptica contain transcriptionnally silent pertussis toxin genes. In J. Bacteriol. 169: 2847-2853.
    • (1987) In J. Bacteriol , vol.169 , pp. 2847-2853
    • Arico, B.1    Rappuoli, R.2
  • 9
    • 0023884187 scopus 로고
    • Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin
    • Armstrong GD, Howard LA, Peppier MS (1988): Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin. In J. Biol. Chem. 263: 8677-8684.
    • (1988) In J. Biol. Chem , vol.263 , pp. 8677-8684
    • Armstrong, G.D.1    Howard, L.A.2    Peppier, M.S.3
  • 10
    • 0029127696 scopus 로고
    • Pertussis toxin export genes are regulated by the ptx promoter and may be required for efficient translation of ptx mRNA in Bordetella pertussis
    • Baker SM, Masi A, Liu D-F, et al. (1995): Pertussis toxin export genes are regulated by the ptx promoter and may be required for efficient translation of ptx mRNA in Bordetella pertussis. In Infect. Immun. 63: 3920-3926.
    • (1995) In Infect. Immun , vol.63 , pp. 3920-3926
    • Baker, S.M.1    Masi, A.2    Liu, D.-F.3
  • 11
    • 0027956705 scopus 로고
    • The modular architecture of bacterial response regulators: Insights into the activation mechanism of the BvgA transactivator of Bordetella pertussis
    • Boucher PE, Menozzi FD, Locht C (1994): The modular architecture of bacterial response regulators: insights into the activation mechanism of the BvgA transactivator of Bordetella pertussis. In J. Mol. Biol. 241: 363-377.
    • (1994) In J. Mol. Biol , vol.241 , pp. 363-377
    • Boucher, P.E.1    Menozzi, F.D.2    Locht, C.3
  • 12
    • 0028855911 scopus 로고
    • Synergistic binding of RNA polymerase and BvgA phosphate to the pertussis toxin promoter of Bordetella pertussis
    • Boucher PE, Stibitz S (1995): Synergistic binding of RNA polymerase and BvgA phosphate to the pertussis toxin promoter of Bordetella pertussis. In J. Bacteriol. 177: 6486-6491.
    • (1995) In J. Bacteriol , vol.177 , pp. 6486-6491
    • Boucher, P.E.1    Stibitz, S.2
  • 13
    • 0023877979 scopus 로고
    • Binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein
    • Brennan MJ, David JL, Kenimer JG, et al. (1988): Binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. In J. Biol. Chem. 263: 4895-4899.
    • (1988) In J. Biol. Chem , vol.263 , pp. 4895-4899
    • Brennan, M.J.1    David, J.L.2    Kenimer, J.G.3
  • 14
    • 0026552246 scopus 로고
    • The crystal structure of diphtheria toxin
    • Choe S, Bennett MJ, Fujii G, et al. (1992): The crystal structure of diphtheria toxin. In Nature 357: 216-222.
    • (1992) In Nature , vol.357 , pp. 216-222
    • Choe, S.1    Bennett, M.J.2    Fujii, G.3
  • 15
    • 0025690256 scopus 로고
    • Lymphocyte receptors for pertussis toxin
    • Clark CG, Armstrong GD (1990): Lymphocyte receptors for pertussis toxin. In Infect Immun. 58: 3840-3846.
    • (1990) In Infect Immun , vol.58 , pp. 3840-3846
    • Clark, C.G.1    Armstrong, G.D.2
  • 16
    • 0026344820 scopus 로고
    • The carboxyl terminus of the S1 subunit of pertussis toxin confers high affinity binding to transducin
    • Cortina G, Krueger KM, Barbieri JT (1991): The carboxyl terminus of the S1 subunit of pertussis toxin confers high affinity binding to transducin. In J. Biol. Chem. 266: 23810-23814.
    • (1991) In J. Biol. Chem , vol.266 , pp. 23810-23814
    • Cortina, G.1    Krueger, K.M.2    Barbieri, J.T.3
  • 17
    • 0029053826 scopus 로고
    • Identification of a Bordetella pertussis regulatory factor required for transcription of the pertussis toxin operon in Escherichia coli
    • DeShazer D, Wood GE, Friedman RL (1995): Identification of a Bordetella pertussis regulatory factor required for transcription of the pertussis toxin operon in Escherichia coli. In J. Bacteriol. 177: 3801 -3807.
    • (1995) In J. Bacteriol , vol.177 , pp. 3801-3807
    • DeShazer, D.1    Wood, G.E.2    Friedman, R.L.3
  • 18
    • 0027054186 scopus 로고
    • Peptide inhibitors of ADP-ribosylation by pertussis toxin are substrates with affinities comparable to those of the trimeric GTP-binding proteins
    • Graf R, Codina J, Birnbaumer L (1992): Peptide inhibitors of ADP-ribosylation by pertussis toxin are substrates with affinities comparable to those of the trimeric GTP-binding proteins. In Mol. Pharmacol. 42: 760-764.
    • (1992) In Mol. Pharmacol , vol.42 , pp. 760-764
    • Graf, R.1    Codina, J.2    Birnbaumer, L.3
  • 19
    • 0026642586 scopus 로고
    • Interaction of pertussis toxin with cells and model membranes
    • Hausman SZ, Burns DL (1992): Interaction of pertussis toxin with cells and model membranes. In J. Biol. Chem. 267: 13735-13739.
    • (1992) In J. Biol. Chem , vol.267 , pp. 13735-13739
    • Hausman, S.Z.1    Burns, D.L.2
  • 20
    • 0027933633 scopus 로고
    • Detection and subcellular localization of three Ptl proteins involved in the secretion of pertussis toxin from Bordetella pertussis
    • Johnson FD, Burns DL (1994): Detection and subcellular localization of three Ptl proteins involved in the secretion of pertussis toxin from Bordetella pertussis. In J. Bacteriol. 176: 5350-5356.
    • (1994) In J. Bacteriol , vol.176 , pp. 5350-5356
    • Johnson, F.D.1    Burns, D.L.2
  • 21
    • 0023131742 scopus 로고
    • Structure-activity analysis of the activation of pertussis toxin
    • Kaslow HR, Lim LK, Moss J, et al. (1987): Structure-activity analysis of the activation of pertussis toxin. In Biochemistry 26: 123-127.
    • (1987) In Biochemistry , vol.26 , pp. 123-127
    • Kaslow, H.R.1    Lim, L.K.2    Moss, J.3
  • 22
    • 0022969324 scopus 로고
    • Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. Interaction of the α-subunits with βγ-subunits in development of their biological activities
    • Katada T, Oinuma M, Ui M (1986): Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. Interaction of the α-subunits with βγ-subunits in development of their biological activities. In J. Biol. Chem. 261: 8182-8191.
    • (1986) In J. Biol. Chem , vol.261 , pp. 8182-8191
    • Katada, T.1    Oinuma, M.2    Ui, M.3
  • 23
    • 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 (1982): Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. In Proc. Natl. Acad. Sci. USA 79: 3129-3133.
    • (1982) In Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 24
    • 0029113743 scopus 로고
    • Localization of the promoter for the ptl genes in Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin
    • Kotob SI, Hausman SZ, Burns DL (1995): Localization of the promoter for the ptl genes in Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin. In infect. Immun. 63: 3227-3230.
    • (1995) In infect. Immun , vol.63 , pp. 3227-3230
    • Kotob, S.I.1    Hausman, S.Z.2    Burns, D.L.3
  • 25
    • 0001207804 scopus 로고
    • Antigenic modulation of Bordetella pertussis
    • Lacey BW (1960): Antigenic modulation of Bordetella pertussis. In J. Hyg. 58: 57-93.
    • (1960) In J. Hyg , vol.58 , pp. 57-93
    • Lacey, B.W.1
  • 26
    • 0024524499 scopus 로고
    • Expression of pertussis toxin in Bordetella bronchiseptica and Bordetella parapertussis carrying recombinant plasmids
    • Lee CK, Roberts A, Perrin S (1989): Expression of pertussis toxin in Bordetella bronchiseptica and Bordetella parapertussis carrying recombinant plasmids. In Infect. Immun. 57: 1413-1418.
    • (1989) In Infect. Immun , vol.57 , pp. 1413-1418
    • Lee, C.K.1    Roberts, A.2    Perrin, S.3
  • 27
    • 0027514682 scopus 로고
    • Site-specific alterations in the B-oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin
    • Lobet Y, Feron C, Dequesne G, et al. (1993): Site-specific alterations in the B-oligomer that affect receptor-binding activities and mitogenicity of pertussis toxin. In J. Exp. Med. 177: 79-87.
    • (1993) In J. Exp. Med , vol.177 , pp. 79-87
    • Lobet, Y.1    Feron, C.2    Dequesne, G.3
  • 28
    • 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. In Biochimie 77: 333-340.
    • (1995) In Biochimie , vol.77 , pp. 333-340
    • Locht, C.1    Antoine, R.2
  • 29
  • 30
    • 0022492403 scopus 로고
    • Pertussis toxin gene: Nucleotide sequence and genetic organization
    • Locht C, Keith JM (1986): Pertussis toxin gene: nucleotide sequence and genetic organization. In Science 232: 1258-1264.
    • (1986) In Science , vol.232 , pp. 1258-1264
    • Locht, C.1    Keith, J.M.2
  • 31
    • 0025249932 scopus 로고
    • The role of cysteine 41 in the enzymatic activities of the pertussis toxin S1 subunit as investigated by site-directed mutagenesis
    • Locht C, Lobet Y, Feron C, et al. (1990): The role of cysteine 41 in the enzymatic activities of the pertussis toxin S1 subunit as investigated by site-directed mutagenesis. In J. Biol. Chem. 265: 4552-4559.
    • (1990) In J. Biol. Chem , vol.265 , pp. 4552-4559
    • Locht, C.1    Lobet, Y.2    Feron, C.3
  • 32
    • 0023123539 scopus 로고
    • Nucleotide sequence homology to pertussis toxin gene in B. bronchiseptica and B. parapertussis
    • Marchitto KS, Smith SG, Locht C, et al. (1987): Nucleotide sequence homology to pertussis toxin gene in B. bronchiseptica and B. parapertussis. In Infect. Immun. 55: 497-501.
    • (1987) In Infect. Immun , vol.55 , pp. 497-501
    • Marchitto, K.S.1    Smith, S.G.2    Locht, C.3
  • 33
    • 0028267231 scopus 로고
    • Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide
    • Merritt EA, Sarfaty S, van den Akker F., et al. (1994): Crystal structure of cholera toxin B-pentamer bound to receptor GM1 pentasaccharide. In Prot. Sci. 3: 166-175.
    • (1994) In Prot. Sci , vol.3 , pp. 166-175
    • Merritt, E.A.1    Sarfaty, S.2    van den Akker, F.3
  • 34
    • 0021100134 scopus 로고
    • Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (Islet activating protein)
    • Moss J, Stanley SJ, Burns DL, et al. (1983): Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (Islet activating protein). In J. Biol. Chem. 258: 11879-11882.
    • (1983) In J. Biol. Chem , vol.258 , pp. 11879-11882
    • Moss, J.1    Stanley, S.J.2    Burns, D.L.3
  • 35
    • 0002892384 scopus 로고
    • Biological activities of pertussigen (pertussis toxin)
    • (Sekura RD, Moss J, Vaughn M, eds) Orlando, FL: Academic Press
    • Munoz JJ (1985): Biological activities of pertussigen (pertussis toxin). In Pertussis toxin (Sekura RD, Moss J, Vaughn M, eds) pp 1-18, Orlando, FL: Academic Press.
    • (1985) In Pertussis toxin , pp. 1-18
    • Munoz, J.J.1
  • 36
    • 0019518133 scopus 로고
    • Biological activities of crystalline pertussigen from Bordetella pertussis
    • Munoz JJ, Arai H, Bergman RK, et al. (1981): Biological activities of crystalline pertussigen from Bordetella pertussis. In Infect. Immun. 33: 820-826.
    • (1981) In Infect. Immun , vol.33 , pp. 820-826
    • Munoz, J.J.1    Arai, H.2    Bergman, R.K.3
  • 37
    • 0013439365 scopus 로고
    • Bordetella pertussis: Immunological and other biological activities
    • New York: Marcel Dekker
    • Munoz JJ, Bergman RK (1977): Bordetella pertussis: Immunological and other biological activities. Immunological Series, Vol. 4, pp 1-235, New York: Marcel Dekker.
    • (1977) Immunological Series , vol.4 , pp. 1-235
    • Munoz, J.J.1    Bergman, R.K.2
  • 38
    • 0020526730 scopus 로고
    • Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP-ribosylation by islet-activating protein, pertussis toxin, in adipocyte membrane
    • Murayama T, Ui M (1983): Loss of the inhibitory function of the guanine nucleotide regulatory component of adenylate cyclase due to its ADP-ribosylation by islet-activating protein, pertussis toxin, in adipocyte membrane. In J. Biol. Chem. 258: 381-390.
    • (1983) In J. Biol. Chem , vol.258 , pp. 381-390
    • Murayama, T.1    Ui, M.2
  • 39
    • 0345197348 scopus 로고
    • Cloning and sequencing of the pertussis toxin gene: Operon structure and gene duplication
    • Nicosia A, Perugini M, Franzini C, et al. (1986): Cloning and sequencing of the pertussis toxin gene: Operon structure and gene duplication. In Proc. Natl. Acad. Sci. USA 83: 4631-4635.
    • (1986) In Proc. Natl. Acad. Sci. USA , vol.83 , pp. 4631-4635
    • Nicosia, A.1    Perugini, M.2    Franzini, C.3
  • 40
    • 0013588384 scopus 로고
    • Histamine shock in mice sensitized with Hemophilus pertussis vaccine
    • Parfentjev IA, Goodline MA (1948): Histamine shock in mice sensitized with Hemophilus pertussis vaccine. In J. Pharmacol. Exp. Ther. 92: 411-413.
    • (1948) In J. Pharmacol. Exp. Ther , vol.92 , pp. 411-413
    • Parfentjev, I.A.1    Goodline, M.A.2
  • 41
    • 0021182482 scopus 로고
    • The concept of pertussis as a toxin mediated disease
    • Pittman M (1984): The concept of pertussis as a toxin mediated disease. In Pediatr. Infect. Dis. 3: 467-486.
    • (1984) In Pediatr. Infect. Dis , vol.3 , pp. 467-486
    • Pittman, M.1
  • 42
    • 0026586142 scopus 로고
    • Pertussis toxin has eukaryotic-like carbohydrate recognition domains
    • Saukkonen K, Burnette WN, Mar VL, et al. (1992): Pertussis toxin has eukaryotic-like carbohydrate recognition domains. In Proc. Natl. Acad. Sci. USA 89: 118-122.
    • (1992) In Proc. Natl. Acad. Sci. USA , vol.89 , pp. 118-122
    • Saukkonen, K.1    Burnette, W.N.2    Mar, V.L.3
  • 43
    • 0027237519 scopus 로고
    • DNA topology affects transcriptional regulation of the pertussis toxin gene of Bordetella pertussis in Escherichia coli in vitro
    • Scarlato V, Arico B, Rappuoli R (1993): DNA topology affects transcriptional regulation of the pertussis toxin gene of Bordetella pertussis in Escherichia coli in vitro. In J. Bacteriol. 175: 4764-4771.
    • (1993) In J. Bacteriol , vol.175 , pp. 4764-4771
    • Scarlato, V.1    Arico, B.2    Rappuoli, R.3
  • 44
    • 0025052257 scopus 로고
    • Positive transcriptional feedback at the bvg locus controls expression of virulence factors in Bordetella pertussis
    • Scarlato V, Prugnola A, Arico B., et al. (1990): Positive transcriptional feedback at the bvg locus controls expression of virulence factors in Bordetella pertussis. In Proc. Natl. Acad. Sci. USA 87: 6753-6757.
    • (1990) In Proc. Natl. Acad. Sci. USA , vol.87 , pp. 6753-6757
    • Scarlato, V.1    Prugnola, A.2    Arico, B.3
  • 45
    • 0021100514 scopus 로고
    • Pertussis toxin, affinity purification of a new ADP-ribosyltransferase
    • Sekura RD, Fish F, Manclark CR, et al. (1983): Pertussis toxin, affinity purification of a new ADP-ribosyltransferase. In J. Biol. Chem. 258: 14647-14651.
    • (1983) In J. Biol. Chem , vol.258 , pp. 14647-14651
    • Sekura, R.D.1    Fish, F.2    Manclark, C.R.3
  • 46
  • 47
    • 0028500699 scopus 로고
    • Structure of a pertussis toxin - sugar complex as a model for receptor binding
    • Stein PE, Boodhoo A, Armstrong GD, et al. (1994b): Structure of a pertussis toxin - sugar complex as a model for receptor binding. In Structural Biology 1: 591-596.
    • (1994) In Structural Biology , vol.1 , pp. 591-596
    • Stein, P.E.1    Boodhoo, A.2    Armstrong, G.D.3
  • 48
    • 0024539059 scopus 로고
    • Phase variation in Bordetella pertussis by frameshift mutation in a gene for a novel two-component system
    • Stibitz S, Aaronson W, Monack D, et al. (1989): Phase variation in Bordetella pertussis by frameshift mutation in a gene for a novel two-component system. In Nature 338: 266-269.
    • (1989) In Nature , vol.338 , pp. 266-269
    • Stibitz, S.1    Aaronson, W.2    Monack, D.3
  • 49
    • 0026050868 scopus 로고
    • A heterotrimeric G protein Gαi-3, on Golgi membranes regulates the secretion of a heparan sulfate proteoglycan in LLC-PK1 epithelial cells
    • Stow JL, de Almeida JB, Narula N, et al. (1991): A heterotrimeric G protein Gαi-3, on Golgi membranes regulates the secretion of a heparan sulfate proteoglycan in LLC-PK1 epithelial cells. In J. Cell Biol. 114: 1113-1124.
    • (1991) In J. Cell Biol , vol.114 , pp. 1113-1124
    • Stow, J.L.1    de Almeida, J.B.2    Narula, N.3
  • 50
    • 0020362248 scopus 로고
    • Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura M, Nogimori K, Murai S, et al. (1982): Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. In Biochemistry 21: 5516-5522.
    • (1982) In Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1    Nogimori, K.2    Murai, S.3
  • 51
    • 0002318350 scopus 로고
    • Bordetella pertussis BvgAS virulence control system
    • (Hoch J, Silhavy T, eds) Washington DC: American Society for Microbiology
    • Uhl MA, Miller JF (1995): Bordetella pertussis BvgAS virulence control system. In two-component signal transduction. (Hoch J, Silhavy T, eds) pp 333-349, Washington DC: American Society for Microbiology.
    • (1995) In two-component signal transduction , pp. 333-349
    • Uhl, M.A.1    Miller, J.F.2
  • 52
    • 0028785432 scopus 로고
    • BvgAS is sufficient for activation of the Bordetella pertussis ptx locus in Escherichia coli
    • Uhl MA, Miller JF (1995): BvgAS is sufficient for activation of the Bordetella pertussis ptx locus in Escherichia coli. In J. Bacteriol. 177: 6477-6485.
    • (1995) In J. Bacteriol , vol.177 , pp. 6477-6485
    • Uhl, M.A.1    Miller, J.F.2
  • 53
    • 0002885931 scopus 로고
    • The multiple biological activities of pertussis toxin
    • (Wardlaw AC, Parton R, eds) Chichester: John Wiley and Sons
    • Ui M (1988): The multiple biological activities of pertussis toxin. In Pathogenesis and Immunity in Pertussis (Wardlaw AC, Parton R, eds) pp 121-145, Chichester: John Wiley and Sons.
    • (1988) In Pathogenesis and Immunity in Pertussis , pp. 121-145
    • Ui, M.1
  • 54
    • 0003085965 scopus 로고
    • Pertussis toxin as a valuable probe for G-protein involvement in signal transduction. In ADP-ribosylating toxins and G proteins
    • (Moss J, Vaughan M, eds)
    • Ui M (1990): Pertussis toxin as a valuable probe for G-protein involvement in signal transduction. In ADP-ribosylating toxins and G proteins. Insights into signal transduction (Moss J, Vaughan M, eds) pp 45-77.
    • (1990) Insights into signal transduction , pp. 45-77
    • Ui, M.1
  • 55
    • 0026059027 scopus 로고
    • Activity of the Agrobacterium T-DNA transfer machinery is affected by virB gene products
    • Ward JE, Dale EM, Binns AN (1991): Activity of the Agrobacterium T-DNA transfer machinery is affected by virB gene products. In Proc. Natl. Acad. Sci. USA 88: 9350-9354.
    • (1991) In Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9350-9354
    • Ward, J.E.1    Dale, E.M.2    Binns, A.N.3
  • 56
    • 0024388753 scopus 로고
    • Lethal infection by Bordetella pertussis mutants in the infant mouse model
    • Weiss AA, Goodwin M (1989): Lethal infection by Bordetella pertussis mutants in the infant mouse model. In Infect. Immun. 57: 3757-3764.
    • (1989) In Infect. Immun , vol.57 , pp. 3757-3764
    • Weiss, A.A.1    Goodwin, M.2
  • 57
    • 0027518747 scopus 로고
    • Molecular characterization of an operon required for pertussis toxin secretion
    • Weiss AA, Johnson FD, Burns DL (1993): Molecular characterization of an operon required for pertussis toxin secretion. In Proc. Natl. Acad. Sci. USA 90: 2970-2974.
    • (1993) In Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2970-2974
    • Weiss, A.A.1    Johnson, F.D.2    Burns, D.L.3
  • 58
    • 0028905448 scopus 로고
    • Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism
    • Xu Y, Barbieri JT (1995): Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism. In Infect. Immun. 63: 825-832.
    • (1995) In Infect. Immun , vol.63 , pp. 825-832
    • Xu, Y.1    Barbieri, J.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.