메뉴 건너뛰기




Volumn 258, Issue 4, 1996, Pages 661-671

Crystal structure of the pertussis toxin-ATP complex: A molecular sensor

Author keywords

ATP binding; Crystal structure; Endoplasmic reticulum; Pertussis toxin; Retrograde transport

Indexed keywords

ADENOSINE TRIPHOSPHATE; PERTUSSIS TOXIN;

EID: 0029867135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0277     Document Type: Article
Times cited : (59)

References (54)
  • 1
    • 0023884187 scopus 로고
    • Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin
    • Armstrong, G. D., Howard, L. A. & Peppler, M. S. (1988). Use of glycosyltransferases to restore pertussis toxin receptor activity to asialogalactofetuin. J. Biol. Chem. 263, 8677-8684.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8677-8684
    • Armstrong, G.D.1    Howard, L.A.2    Peppler, M.S.3
  • 2
    • 0028485286 scopus 로고
    • MINIMAGE: A program for plotting electron density maps
    • Arnez, J. G. (1994). MINIMAGE: a program for plotting electron density maps. J. Appl. Crystallog. 27, 649-653.
    • (1994) J. Appl. Crystallog. , vol.27 , pp. 649-653
    • Arnez, J.G.1
  • 3
    • 0026508087 scopus 로고
    • Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum
    • Braakman, I., Helenius, J. & Helenius, A. (1992). Role of ATP and disulphide bonds during protein folding in the endoplasmic reticulum. Nature, 356, 260-262.
    • (1992) Nature , vol.356 , pp. 260-262
    • Braakman, I.1    Helenius, J.2    Helenius, A.3
  • 4
    • 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. (1988). Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. J. Biol. Chem. 263, 4895-4899.
    • (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
  • 6
    • 0026597444 scopus 로고
    • Free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger, A. T. (1992b). Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature, 355, 472-475.
    • (1992) Nature , vol.355 , pp. 472-475
    • Brünger, A.T.1
  • 7
    • 0023019139 scopus 로고
    • Adenine nucleotides promote dissociation of pertussis toxin subunits
    • Burns, D. L. & Manclark, C. R. (1986). Adenine nucleotides promote dissociation of pertussis toxin subunits. J. Biol. Chem. 261, 4324-4327.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4324-4327
    • Burns, D.L.1    Manclark, C.R.2
  • 8
    • 0025012987 scopus 로고
    • Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity
    • Chaudhary, V. K., Jinno, Y., Fitzgerald, D. & Pastan, I. (1990). Pseudomonas exotoxin contains a specific sequence at the carboxyl terminus that is required for cytotoxicity Proc. Natl Acad. Sci. USA, 87, 308-312.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 308-312
    • Chaudhary, V.K.1    Jinno, Y.2    Fitzgerald, D.3    Pastan, I.4
  • 9
    • 0000436770 scopus 로고
    • Exploitation of crystalline architecture and solution data in the rational preparation of novel mixed-metal ATP complexes
    • Cini, R. & Marzilli, L. G. (1988). Exploitation of crystalline architecture and solution data in the rational preparation of novel mixed-metal ATP complexes. Inorg. Chem. 27, 1855-1856.
    • (1988) Inorg. Chem. , vol.27 , pp. 1855-1856
    • Cini, R.1    Marzilli, L.G.2
  • 10
    • 84967850703 scopus 로고
    • Translocation of ATP into the lumen of rat liver and canine pancreas rough endoplasmic reticulum derived vesicles and its binding to lumenal glucose regulated proteins
    • Clairmont, C., Demaio, A. & Hirschberg, C. (1991). Translocation of ATP into the lumen of rat liver and canine pancreas rough endoplasmic reticulum derived vesicles and its binding to lumenal glucose regulated proteins. J. Cell. Biol. 115, 255a.
    • (1991) J. Cell. Biol. , vol.115
    • Clairmont, C.1    Demaio, A.2    Hirschberg, C.3
  • 11
    • 0027301156 scopus 로고
    • Inhibition of heat-labile cholera and Escherichia coli enterotoxins by brefeldin A
    • Donta, S. T., Beristain, S. & Tomicic, T. K. (1993). Inhibition of heat-labile cholera and Escherichia coli enterotoxins by brefeldin A. Infect. Immun. 61, 3282-3286.
    • (1993) Infect. Immun. , vol.61 , pp. 3282-3286
    • Donta, S.T.1    Beristain, S.2    Tomicic, T.K.3
  • 12
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: Building bridges in protein folding
    • Freedman, R. B., Hirst, T. R. & Tuite, M. F. (1994). Protein disulphide isomerase: building bridges in protein folding. Trends Biochem. Sci. 19, 331-336.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 13
    • 0026499117 scopus 로고
    • Control of pertussis in the world
    • Galazka, A. (1992). Control of pertussis in the world. World Health Stat. Quart. 45, 238-247.
    • (1992) World Health Stat. Quart. , vol.45 , pp. 238-247
    • Galazka, A.1
  • 14
    • 0001983754 scopus 로고
    • Jeljaszewica, J. & Wadstrom, T., eds, Academic Press, New York
    • Gill, D. M. (1978). In Bacterial Toxins and Cell Membranes (Jeljaszewica, J. & Wadstrom, T., eds), pp. 291-332, Academic Press, New York.
    • (1978) Bacterial Toxins and Cell Membranes , pp. 291-332
    • Gill, D.M.1
  • 15
    • 0028089159 scopus 로고
    • Proteolytic activation of bacterial toxins: Role of bacterial and host cell proteases
    • Gordon, V. M. & Leppla, S. H. (1994). Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases. Infect. Immun. 62, 333-340.
    • (1994) Infect. Immun. , vol.62 , pp. 333-340
    • Gordon, V.M.1    Leppla, S.H.2
  • 16
    • 0028128355 scopus 로고
    • Role of trypsin-like cleavage at arginine 192 in the enzymatic and cytotonic activities of escherichia coli heat-labile enterotoxin
    • Grant, C. C. R., Messner, R. J. & Cieplak, W., Jr (1994). Role of trypsin-like cleavage at arginine 192 in the enzymatic and cytotonic activities of Escherichia coli heat-labile enterotoxin. Infect. Immun. 62, 4270-4278.
    • (1994) Infect. Immun. , vol.62 , pp. 4270-4278
    • Grant, C.C.R.1    Messner, R.J.2    Cieplak W., Jr.3
  • 17
    • 0026642586 scopus 로고
    • Interaction of pertussis toxin with cells and model membranes
    • Hausman, S. Z. & Burns, D. L. (1992). Interaction of pertussis toxin with cells and model membranes. J. Biol. Chem. 267, 13735-13739.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13735-13739
    • Hausman, S.Z.1    Burns, D.L.2
  • 18
    • 0025315201 scopus 로고
    • Binding of ATP by pertussis toxin and isolated toxin subunits
    • Hausman, S. Z., Manclark, C. R. & Burns, D. L. (1990). Binding of ATP by pertussis toxin and isolated toxin subunits. Biochemistry, 29, 6128-6131.
    • (1990) Biochemistry , vol.29 , pp. 6128-6131
    • Hausman, S.Z.1    Manclark, C.R.2    Burns, D.L.3
  • 19
    • 0002193613 scopus 로고
    • The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography
    • Higashi, T. (1989). The processing of diffraction data taken on a screenless Weissenberg camera for macromolecular crystallography J. Appl. Crystallog. 22, 9-18.
    • (1989) J. Appl. Crystallog. , vol.22 , pp. 9-18
    • Higashi, T.1
  • 21
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J.-Y, Cowan, S. W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A, 47, 110-119.
    • (1991) Acta Crystallog. Sect. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 22
    • 0023131742 scopus 로고
    • Structure-activity analysis of the activation of pertussis toxin
    • Kaslow, H. R., Lim, L.-K., Moss, J. & Lesikar, D. D. (1987). Structure-activity analysis of the activation of pertussis toxin. Biochemistry, 26, 123-127.
    • (1987) Biochemistry , vol.26 , pp. 123-127
    • Kaslow, H.R.1    Lim, L.-K.2    Moss, J.3    Lesikar, D.D.4
  • 23
    • 0020490738 scopus 로고
    • ADP ribosylation of the specific membrane protein of C6 cells by isletactivating protein associated with modification of adenylate cyclase activity
    • Katada, T. & Ui, M. (1982a). ADP ribosylation of the specific membrane protein of C6 cells by isletactivating protein associated with modification of adenylate cyclase activity J. Biol. Chem. 257, 7210-7216.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7210-7216
    • Katada, T.1    Ui, M.2
  • 24
    • 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. (1982b). Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc. Nat Acad. Sci. USA, 79, 3129-3133.
    • (1982) Proc. Nat Acad. Sci. USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 25
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 26
    • 0027233731 scopus 로고
    • Molecular characterization of the in vitro activation of pertussis toxin by ATP
    • Krueger, K. M. & Barbieri, J. T. (1993). Molecular characterization of the in vitro activation of pertussis toxin by ATP. J. Biol. Chem. 268, 12570-12578.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12570-12578
    • Krueger, K.M.1    Barbieri, J.T.2
  • 27
    • 0028230250 scopus 로고
    • Assignment of functional domains involved in ADP-ribosylation and B-oligomer binding within the carboxyl terminus of the S1 subunit of pertussis toxin
    • Krueger, K. M. & Barbieri, J. T. (1994). Assignment of functional domains involved in ADP-ribosylation and B-oligomer binding within the carboxyl terminus of the S1 subunit of pertussis toxin. Infect. Immun. 62, 2071-2078.
    • (1994) Infect. Immun. , vol.62 , pp. 2071-2078
    • Krueger, K.M.1    Barbieri, J.T.2
  • 28
    • 0025807970 scopus 로고
    • Protease treatment of pertussis toxin identifies the preferential cleavage of the s1 subunit
    • Krueger, K. M., Mende-Mueller, L. M. & Barbieri, J. T. (1991). Protease treatment of pertussis toxin identifies the preferential cleavage of the S1 subunit. J. Biol. Chem. 266, 8122-8128.
    • (1991) J. Biol. Chem. , vol.266 , pp. 8122-8128
    • Krueger, K.M.1    Mende-Mueller, L.M.2    Barbieri, J.T.3
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    Macarthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0021912437 scopus 로고
    • Adenine nucleotides directly stimulate pertussis toxin
    • Lim, L.-K., Sekura, D. D. & Kaslow, H. R. (1985). Adenine nucleotides directly stimulate pertussis toxin. J. Biol. Chem. 260, 2585-2588.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2585-2588
    • Lim, L.-K.1    Sekura, D.D.2    Kaslow, H.R.3
  • 31
    • 0024402268 scopus 로고
    • Effects of eliminating a disulfide bridge within domain II of pseudomonas aeruginosa exotoxin A
    • Madshus, I. G. & Collier, R. J. (1989). Effects of eliminating a disulfide bridge within domain II of Pseudomonas aeruginosa exotoxin A. Infect. Immun. 57, 1873-1878.
    • (1989) Infect. Immun. , vol.57 , pp. 1873-1878
    • Madshus, I.G.1    Collier, R.J.2
  • 32
    • 0027312063 scopus 로고
    • Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase
    • Mandel, R., Ryser, H. J., Ghani, F., Wu, M. & Peak, D. (1993). Inhibition of a reductive function of the plasma membrane by bacitracin and antibodies against protein disulfide-isomerase. Proc. Natl Acad. Sci. USA, 90, 4112-4116.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 4112-4116
    • Mandel, R.1    Ryser, H.J.2    Ghani, F.3    Wu, M.4    Peak, D.5
  • 33
    • 0023033093 scopus 로고
    • The interaction of nucleotides with pertussis toxin
    • Mattera, R., Codina, J., Sekura, R. D. & Bimbaumer, L. (1986). The interaction of nucleotides with pertussis toxin. J. Biol. Chem. 261, 11173-11179.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11173-11179
    • Mattera, R.1    Codina, J.2    Sekura, R.D.3    Bimbaumer, L.4
  • 34
    • 0028057108 scopus 로고
    • Raster3D version 2.0: A program for photorealistic molecular graphics
    • Merritt, E. A. & Murphy, M. E. P. (1994). Raster3D version 2.0: a program for photorealistic molecular graphics. Acta Crystallog. sect. D, 50, 869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 35
    • 0003345237 scopus 로고
    • Pertussis vaccine
    • Plotkin, S. A. & Mortimer, E. A., Jr, eds, W. B. Saunders Company, Philadelphia
    • Mortimer, E. A., Jr (1994). Pertussis vaccine. In Vaccines (Plotkin, S. A. & Mortimer, E. A., Jr, eds), pp. 91-135, W. B. Saunders Company, Philadelphia.
    • (1994) Vaccines , pp. 91-135
    • Mortimer E.A., Jr.1
  • 36
    • 0025737882 scopus 로고
    • Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH: Characterization and topology of inserted regions
    • Moskaug, J. O., Stenmark, H. & Olsnes, S. (1991), Insertion of diphtheria toxin B-fragment into the plasma membrane at low pH: characterization and topology of inserted regions. J. Biol. Chem. 266, 2652-2659.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2652-2659
    • Moskaug, J.O.1    Stenmark, H.2    Olsnes, S.3
  • 37
    • 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, S. J., Burns, D. L., Hsia, J. A., Yost, D. A., Myers, G. A. & Hewlett, E. L. (1983). Activation by thiol of the latent NAD glycohydrolase and ADP-ribosyltransferase activities of Bordetella pertussis toxin (islet-activating protein). J. Biol. Chem. 258, 11879-11882.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11879-11882
    • Moss, J.1    Stanley, S.J.2    Burns, D.L.3    Hsia, J.A.4    Yost, D.A.5    Myers, G.A.6    Hewlett, E.L.7
  • 38
    • 0022495497 scopus 로고
    • Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergents
    • Moss, J., Stanley, S. J., Watkins, P. A., Burns, D. L., Manclark, C. R., Kaslow, H. R. & Hewlett, E. L. (1986). Stimulation of the thiol-dependent ADP-ribosyltransferase and NAD glycohydrolase activities of Bordetella pertussis toxin by adenine nucleotides, phospholipids, and detergents. Biochemistry, 25, 2720-2725.
    • (1986) Biochemistry , vol.25 , pp. 2720-2725
    • Moss, J.1    Stanley, S.J.2    Watkins, P.A.3    Burns, D.L.4    Manclark, C.R.5    Kaslow, H.R.6    Hewlett, E.L.7
  • 39
    • 0019513324 scopus 로고
    • Mouse-protective and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis
    • Munoz, J. J., Arai, H. & Cole, R. L. (1981a). Mouse-protective and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis. Infect. Immun. 32, 243-250.
    • (1981) Infect. Immun. , vol.32 , pp. 243-250
    • Munoz, J.J.1    Arai, H.2    Cole, R.L.3
  • 40
    • 0019518133 scopus 로고
    • Biological activities of crystalline pertussigen from Bordetella pertussis
    • Munoz, J. J., Arai, H., Bergman, R. K. & Sadowski, P. L. (1981b). Biological activities of crystalline pertussigen from Bordetella pertussis. Infect. Immun. 33, 820-826.
    • (1981) Infect. Immun. , vol.33 , pp. 820-826
    • Munoz, J.J.1    Arai, H.2    Bergman, R.K.3    Sadowski, P.L.4
  • 41
    • 0027468582 scopus 로고
    • Involvement of the Golgi region in the intracellular trafficking of cholera toxin
    • Nambiar, M. P., Oda, T., Chen, C., Kuwazuru, Y. & Wu, H. C. (1993). Involvement of the Golgi region in the intracellular trafficking of cholera toxin. J. Cell. Physiol. 154, 222-228.
    • (1993) J. Cell. Physiol. , vol.154 , pp. 222-228
    • Nambiar, M.P.1    Oda, T.2    Chen, C.3    Kuwazuru, Y.4    Wu, H.C.5
  • 42
    • 0027978637 scopus 로고
    • Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus
    • Nilsson, T. & Warren, G. (1994). Retention and retrieval in the endoplasmic reticulum and the Golgi apparatus. Curr. Opin. Cell Biol. 6, 517-521.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 517-521
    • Nilsson, T.1    Warren, G.2
  • 43
    • 0025243542 scopus 로고
    • Processing of pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol
    • Ogata, M., Chaudhary V. K., Pastan, I. & FitzGerald, D. J. (1990). Processing of Pseudomonas exotoxin by a cellular protease results in the generation of a 37,000-Da toxin fragment that is translocated to the cytosol. J. Biol. Chem. 265, 20678-20685.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20678-20685
    • Ogata, M.1    Chaudhary, V.K.2    Pastan, I.3    FitzGerald, D.J.4
  • 44
    • 0027314536 scopus 로고
    • Brefeldin A blocks the response of cultured cells to cholera toxin
    • Orlandi, P. A., Curran, P. K. & Fishman, P. H. (1993). Brefeldin A blocks the response of cultured cells to cholera toxin. J. Biol. Chem. 268, 12010-12016.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12010-12016
    • Orlandi, P.A.1    Curran, P.K.2    Fishman, P.H.3
  • 45
    • 0026741237 scopus 로고
    • Toxin entry: How reversible is the secretory pathway?
    • Pelham, H. R. B., Roberts, L. M. & Lord, J. M. (1992). Toxin entry: how reversible is the secretory pathway? Trends Cell Biol. 2, 183-185.
    • (1992) Trends Cell Biol. , vol.2 , pp. 183-185
    • Pelham, H.R.B.1    Roberts, L.M.2    Lord, J.M.3
  • 46
    • 84944812409 scopus 로고
    • Improved Fourier coefficients for maps using phases from partial structures with errors
    • Read, R. J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystdlog. sect. A, 42, 140-149.
    • (1986) Acta Crystdlog. Sect. A , vol.42 , pp. 140-149
    • Read, R.J.1
  • 47
    • 0000293676 scopus 로고
    • X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation
    • Sakabe, N. (1991). X-ray diffraction data collection system for modern protein crystallography with a Weissenberg camera and an imaging plate using synchrotron radiation. Nucl. Instr. Methods, sect. A, 303, 448-463.
    • (1991) Nucl. Instr. Methods, Sect. A , vol.303 , pp. 448-463
    • Sakabe, N.1
  • 48
    • 0028275814 scopus 로고
    • Endocytosis and intracellular sorting of ricin and shiga toxin
    • Sandvig, K. & van Deurs, B. (1994). Endocytosis and intracellular sorting of ricin and shiga toxin. FEBS Letters, 346, 99-102.
    • (1994) FEBS Letters , vol.346 , pp. 99-102
    • Sandvig, K.1    Van Deurs, B.2
  • 49
    • 0028352977 scopus 로고
    • Retrograde transport from the golgi complex to the ER of both shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP
    • Sandvig, K., Ryd, M., Garred, O., Schweda, E., Holm, P. K. & van Deurs, B. (1994). Retrograde transport from the Golgi complex to the ER of both Shiga toxin and the nontoxic Shiga B-fragment is regulated by butyric acid and cAMP. J. Cell. Biol. 126, 53-64.
    • (1994) J. Cell. Biol. , vol.126 , pp. 53-64
    • Sandvig, K.1    Ryd, M.2    Garred, O.3    Schweda, E.4    Holm, P.K.5    Van Deurs, B.6
  • 52
    • 0026465205 scopus 로고
    • Addition of an ER retention signal to the ricin A chain increases the cytotoxicity of the holotoxin
    • Wales, R., Chaddock, J. A., Roberts, L. M. & Lord, J. M. (1992). Addition of an ER retention signal to the ricin A chain increases the cytotoxicity of the holotoxin. Exp. Cell Res. 203, 1-4.
    • (1992) Exp. Cell Res. , vol.203 , pp. 1-4
    • Wales, R.1    Chaddock, J.A.2    Roberts, L.M.3    Lord, J.M.4
  • 53
    • 0028905448 scopus 로고
    • Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism
    • Xu, Y. & Barbieri, J. T. (1995). Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism. Infect. Immun. 63, 825-832.
    • (1995) Infect. Immun. , vol.63 , pp. 825-832
    • Xu, Y.1    Barbieri, J.T.2
  • 54
    • 0025975785 scopus 로고
    • Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin
    • Yoshida, T., Chen, C., Zhang, M. & Wu, H. C. (1991). Disruption of the Golgi apparatus by brefeldin A inhibits the cytotoxicity of ricin, modeccin, and Pseudomonas toxin. Exp. Cell Res. 192, 389-395.
    • (1991) Exp. Cell Res. , vol.192 , pp. 389-395
    • Yoshida, T.1    Chen, C.2    Zhang, M.3    Wu, H.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.