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Volumn 133, Issue 4, 1996, Pages 801-807

Oligomeric and subunit structure of the Helicobacter Pylori vacuolating cytotoxin

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CYTOTOXIN; PROTEIN SUBUNIT;

EID: 0029898566     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.133.4.801     Document Type: Article
Times cited : (160)

References (36)
  • 1
    • 0025787798 scopus 로고
    • Alpha-toxin of Staphylococcus aureus
    • Bahkdi, S., and J. Tranum-Jensen. 1991. Alpha-toxin of Staphylococcus aureus. Microbiol Rev. 55:733-751.
    • (1991) Microbiol Rev. , vol.55 , pp. 733-751
    • Bahkdi, S.1    Tranum-Jensen, J.2
  • 4
    • 0025180806 scopus 로고
    • POLCA, a library running in a modern environment, implements a protocol for averaging randomly oriented images
    • Bellon, P.L., and S. Lanzavechia. 1990. POLCA, a library running in a modern environment, implements a protocol for averaging randomly oriented images. Comput. Appl. Biosci. 6:271-277.
    • (1990) Comput. Appl. Biosci. , vol.6 , pp. 271-277
    • Bellon, P.L.1    Lanzavechia, S.2
  • 6
    • 0346074091 scopus 로고
    • Three-dimensional structure of Diphtheria toxin
    • J. Moss, B. Iglewski, M. Vaughan, and AT. Tu, editors. Marcel Dekker, Inc., New York
    • Collier, R.J. 1995. Three-dimensional structure of Diphtheria toxin. In Bacterial Toxins and Virulence Factors in Disease. J. Moss, B. Iglewski, M. Vaughan, and AT. Tu, editors. Marcel Dekker, Inc., New York. 81-93.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 81-93
    • Collier, R.J.1
  • 7
    • 0026739795 scopus 로고
    • Purification and characterization of the vacuolating toxin from Helicobacter pylori
    • Cover, T.L., and M.J. Blaser. 1992a. Purification and characterization of the vacuolating toxin from Helicobacter pylori. J Biol. Chem. 267:10570-10575.
    • (1992) J Biol. Chem. , vol.267 , pp. 10570-10575
    • Cover, T.L.1    Blaser, M.J.2
  • 8
    • 0026643058 scopus 로고
    • Helicobacter pylori and gastroduodenal disease
    • Cover, T.L., and M.J. Blaser. 1922b. Helicobacter pylori and gastroduodenal disease. Annu. Rev. Med. 43:135-145.
    • (1922) Annu. Rev. Med. , vol.43 , pp. 135-145
    • Cover, T.L.1    Blaser, M.J.2
  • 9
    • 0028308711 scopus 로고
    • Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains
    • Cover, T.L., M.K.R. Tummuru, P. Cao, S.A. Thompson, and M.J. Blaser. 1994. Divergence of genetic sequences for the vacuolating cytotoxin among Helicobacter pylori strains. J. Biol. Chem. 269:10566-10573.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10566-10573
    • Cover, T.L.1    Tummuru, M.K.R.2    Cao, P.3    Thompson, S.A.4    Blaser, M.J.5
  • 11
    • 0002090806 scopus 로고
    • Bacterial ADP-ribosyl-transferases
    • J. Moss, B. Iglewski, M. Vaughan, and A.T. Tu. editors. Marcel Dekker, Inc., New York
    • Domenighini, M., M. Pizza, and R. Rappuoli. 1995. Bacterial ADP-ribosyl-transferases. In Bacterial Toxins and Virulence Factors in Disease. J. Moss, B. Iglewski, M. Vaughan, and A.T. Tu. editors. Marcel Dekker, Inc., New York. 59-80.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 59-80
    • Domenighini, M.1    Pizza, M.2    Rappuoli, R.3
  • 12
    • 0028060680 scopus 로고
    • Diphtheria toxin at low pH depolarizes the membrane, increases the membrane conductance and induces a new type of ion channel in Vero cells
    • Eriksen, S., S. Olsnes, K. Sandvig, and O. Sand. 1994. Diphtheria toxin at low pH depolarizes the membrane, increases the membrane conductance and induces a new type of ion channel in Vero cells. EMBO (Eur. Mol. Biol. Organ.) J. 13:4433-4439.
    • (1994) EMBO (Eur. Mol. Biol. Organ.) J. , vol.13 , pp. 4433-4439
    • Eriksen, S.1    Olsnes, S.2    Sandvig, K.3    Sand, O.4
  • 13
    • 0025739648 scopus 로고
    • Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes
    • Harris, R.W., P.J. Sims, and R.K. Tweten. 1991. Kinetic aspects of the aggregation of Clostridium perfringens θ-toxin on erythrocyte membranes. J. Biol. Chem. 266:6936-6941.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6936-6941
    • Harris, R.W.1    Sims, P.J.2    Tweten, R.K.3
  • 14
    • 0021095633 scopus 로고
    • Procedure for freeze-drying molecules absorbed to mica Hakes
    • Heuser, J.E. 1983. Procedure for freeze-drying molecules absorbed to mica Hakes. J. Mol. Biol. 169:155-195.
    • (1983) J. Mol. Biol. , vol.169 , pp. 155-195
    • Heuser, J.E.1
  • 15
    • 0024416678 scopus 로고
    • Protocol for 3-D visualization of molecules on mica via the quick-freeze, deep etch technique
    • Heuser, J.E. 1989. Protocol for 3-D visualization of molecules on mica via the quick-freeze, deep etch technique. J. Electron Microsc. Tech. 13:244-263.
    • (1989) J. Electron Microsc. Tech. , vol.13 , pp. 244-263
    • Heuser, J.E.1
  • 16
    • 0345570658 scopus 로고
    • Channels formed by botulinum. tetanus and diptheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch, D.H., M. Romero-Mira, B.E. Ehrlich, A. Finkelstein, B.R. Dasgupta, and L.L. Simpson. 1985. Channels formed by botulinum. tetanus and diptheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA. 82:1692-1696.
    • (1985) Proc. Natl. Acad. Sci. USA. , vol.82 , pp. 1692-1696
    • Hoch, D.H.1    Romero-Mira, M.2    Ehrlich, B.E.3    Finkelstein, A.4    Dasgupta, B.R.5    Simpson, L.L.6
  • 17
    • 0028618715 scopus 로고
    • Three-dimensional reconstructions of accessory tubules observed in sperm axonemes of two insect species
    • Lanzavecchia, S., P.L. Bellon, R. Dallai, and B.A. Afzelius. 1994. Three-dimensional reconstructions of accessory tubules observed in sperm axonemes of two insect species. J. Struct. Biol. 113:225-237.
    • (1994) J. Struct. Biol. , vol.113 , pp. 225-237
    • Lanzavecchia, S.1    Bellon, P.L.2    Dallai, R.3    Afzelius, B.A.4
  • 18
    • 0001128658 scopus 로고
    • Anthrax toxins
    • J. Moss, B. Iglewski, M. Vaughan, and A.T. Tu, editors. Marcel Dekker Inc., New York
    • Leppla, S.H. 1995. Anthrax toxins. In Bacterial Toxins and Virulence Factors in Disease. J. Moss, B. Iglewski, M. Vaughan, and A.T. Tu, editors. Marcel Dekker Inc., New York. 543-572.
    • (1995) Bacterial Toxins and Virulence Factors in Disease , pp. 543-572
    • Leppla, S.H.1
  • 19
    • 0025880541 scopus 로고
    • Production of a cytotoxin by Helicobacter pylori
    • Leunk, R.D. 1991. Production of a cytotoxin by Helicobacter pylori. Rev. Infect. Dis. 13 (Suppl.):686-689.
    • (1991) Rev. Infect. Dis. , vol.13 , Issue.SUPPL. , pp. 686-689
    • Leunk, R.D.1
  • 22
    • 0018308483 scopus 로고
    • Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulphide bond reduction and subunit composition
    • Mekalanos, J.J.R., R.J. Collier, and W.R. Romig. 1979. Enzymic activity of cholera toxin. II. Relationships to proteolytic processing, disulphide bond reduction and subunit composition. J. Biol. Chem. 254:5855-5861.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5855-5861
    • Mekalanos, J.J.R.1    Collier, R.J.2    Romig, W.R.3
  • 23
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne, J.C., D. Furlong, P.C. Hanna, J.S. Wall, and R.J. Collier. 1994. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269:20607-20612.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20607-20612
    • Milne, J.C.1    Furlong, D.2    Hanna, P.C.3    Wall, J.S.4    Collier, R.J.5
  • 25
    • 0010800349 scopus 로고
    • Molecular models of toxin membrane translocation
    • J.E. Alouf, and J.H. Freer, editors. Academic Press, New York
    • Montecucco, C., E. Papini, and G. Schiavo. 1991. Molecular models of toxin membrane translocation. In Sourcebook of Bacterial Protein Toxins. J.E. Alouf, and J.H. Freer, editors. Academic Press, New York. 45-56.
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 45-56
    • Montecucco, C.1    Papini, E.2    Schiavo, G.3
  • 28
    • 0027524426 scopus 로고
    • Helicobacter pylori and gastric cancer
    • Parsonnet, J. 1993. Helicobacter pylori and gastric cancer. Gastroenterol. Clin. North Am. 22:89-104.
    • (1993) Gastroenterol. Clin. North Am. , vol.22 , pp. 89-104
    • Parsonnet, J.1
  • 29
    • 0028181355 scopus 로고
    • Toxin inactivation and antigen stabilization: Two different uses of formaldehyde
    • Rappuoli, R. 1994. Toxin inactivation and antigen stabilization: two different uses of formaldehyde. Vaccine. 12:579-581.
    • (1994) Vaccine. , vol.12 , pp. 579-581
    • Rappuoli, R.1
  • 30
    • 0028365481 scopus 로고
    • Genetic analysis of the Helicobacter pylori vacuolating cytotoxin: Structural similarities with the IgA protease type of exported protein
    • Schmitt, W., and R. Haas. 1994. Genetic analysis of the Helicobacter pylori vacuolating cytotoxin: structural similarities with the IgA protease type of exported protein. Mol. Microbiol. 12:307-319.
    • (1994) Mol. Microbiol. , vol.12 , pp. 307-319
    • Schmitt, W.1    Haas, R.2
  • 31
    • 0027169048 scopus 로고
    • A ring-shaped structure with a crown formed by streptolysin-O on the erythrocyte membrane
    • Sekiya, K., R. Satoh, H. Danbara, and Y. Futaesaku. 1993. A ring-shaped structure with a crown formed by streptolysin-O on the erythrocyte membrane. J. Bacteriol. 175:5953-5961.
    • (1993) J. Bacteriol. , vol.175 , pp. 5953-5961
    • Sekiya, K.1    Satoh, R.2    Danbara, H.3    Futaesaku, Y.4
  • 32
    • 0028519218 scopus 로고
    • Unravelling the pathogenic role of Helicobacter pylori in peptic ulcer: Potential for new therapies and vaccines
    • Telford, J.L., A. Covacci, P. Ghiara, C. Montecucco, and R. Rappuoli. 1994a. Unravelling the pathogenic role of Helicobacter pylori in peptic ulcer: potential for new therapies and vaccines. Trends Biotechnol. 12:420-426.
    • (1994) Trends Biotechnol. , vol.12 , pp. 420-426
    • Telford, J.L.1    Covacci, A.2    Ghiara, P.3    Montecucco, C.4    Rappuoli, R.5
  • 34
    • 0026745129 scopus 로고
    • Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: Identification of the site of proleolytic activation
    • van der Goot, F.G., J. Lakey, F. Pattus, C.M. Kay, O. Sorokine, A. Van Dorselaer, and J.T. Buckley. 1992. Spectroscopic study of the activation and oligomerization of the channel-forming toxin aerolysin: identification of the site of proleolytic activation. Biochemistry. 31:8566-8570.
    • (1992) Biochemistry. , vol.31 , pp. 8566-8570
    • Van der Goot, F.G.1    Lakey, J.2    Pattus, F.3    Kay, C.M.4    Sorokine, O.5    Van Dorselaer, A.6    Buckley, J.T.7
  • 35
    • 0028860071 scopus 로고
    • Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vaculating cytotoxin
    • Xiang, Z., S. Censini, P.F. Bayeli, J.L. Telford, N. Figura, R. Rappuoli, and A. Covacci. 1995. Analysis of expression of CagA and VacA virulence factors in 43 strains of Helicobacter pylori reveals that clinical isolates can be divided into two major types and that CagA is not necessary for expression of the vaculating cytotoxin. Infect. Immun. 63:94-98.
    • (1995) Infect. Immun. , vol.63 , pp. 94-98
    • Xiang, Z.1    Censini, S.2    Bayeli, P.F.3    Telford, J.L.4    Figura, N.5    Rappuoli, R.6    Covacci, A.7
  • 36
    • 0027640399 scopus 로고
    • Rab GTPases in vesicular transport
    • Zerial, M., and H. Stenmark. 1993. Rab GTPases in vesicular transport. Curr. Opin. Cell Biol. 5:613-620.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 613-620
    • Zerial, M.1    Stenmark, H.2


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