메뉴 건너뛰기




Volumn 288, Issue 38, 2013, Pages 27505-27516

Structural basis of subtilase cytotoxin SubAB assembly

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR DYSFUNCTION; ENDOPLASMIC RETICULUM CHAPERONE; FUNCTIONAL CHARACTERIZATION; HYDROPHOBIC PATCH; INTRACELLULAR TRAFFICKING; MOLECULAR TARGETS; PATHOGENIC STRAINS; SEQUENCE COMPARISONS;

EID: 84884539472     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.462622     Document Type: Article
Times cited : (19)

References (34)
  • 5
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao, R. V., Ellerby, H. M., and Bredesen, D. E. (2004) Coupling endoplasmic reticulum stress to the cell death program. Cell Death Differ. 11, 372-380
    • (2004) Cell Death Differ. , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 6
    • 7444240833 scopus 로고    scopus 로고
    • The ER function BiP is a master regulator of ER function
    • Hendershot, L. M. (2004) The ER function BiP is a master regulator of ER function. Mt. Sinai. J. Med. 71, 289-297
    • (2004) Mt. Sinai. J. Med. , vol.71 , pp. 289-297
    • Hendershot, L.M.1
  • 9
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 11
  • 18
    • 0038309664 scopus 로고    scopus 로고
    • Cholera holotoxin assembly requires a hydrophobic domain at the A-B5 interface: Mutational analysis and development of an in vitro assembly system
    • Tinker, J. K., Erbe, J. L., Hol, W. G. J., and Holmes, R. K. (2003) Cholera holotoxin assembly requires a hydrophobic domain at the A-B5 interface: mutational analysis and development of an in vitro assembly system. Infect. Immun. 71, 4093-4101
    • (2003) Infect. Immun. , vol.71 , pp. 4093-4101
    • Tinker, J.K.1    Erbe, J.L.2    Hol, W.G.J.3    Holmes, R.K.4
  • 21
    • 0031048978 scopus 로고    scopus 로고
    • Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line
    • Orlandi, P. A. (1997) Protein-disulfide isomerase-mediated reduction of the A subunit of cholera toxin in a human intestinal cell line. J. Biol. Chem. 272, 4591-4599
    • (1997) J. Biol. Chem. , vol.272 , pp. 4591-4599
    • Orlandi, P.A.1
  • 22
    • 0035937408 scopus 로고    scopus 로고
    • Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin
    • Tsai, B., Rodighiero, C., Lencer, W. I., and Rapoport, T. A. (2001) Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin. Cell 104, 937-948
    • (2001) Cell , vol.104 , pp. 937-948
    • Tsai, B.1    Rodighiero, C.2    Lencer, W.I.3    Rapoport, T.A.4
  • 23
    • 0031942258 scopus 로고    scopus 로고
    • Contribution of the disulfide bond of the A subunit to the action of Escherichia coli heat-labile enterotoxin
    • Okamoto, K., Nomura, T., Fujii, Y., and Yamanaka, H. (1998) Contribution of the disulfide bond of the A subunit to the action of Escherichia coli heat-labile enterotoxin. J. Bacteriol. 180, 1368-1374
    • (1998) J. Bacteriol. , vol.180 , pp. 1368-1374
    • Okamoto, K.1    Nomura, T.2    Fujii, Y.3    Yamanaka, H.4
  • 24
    • 0026576742 scopus 로고
    • Characterization of hybrid toxins produced in Escherichia coli by assembly of A and B polypeptides from type I and type II heat-labile enterotoxins
    • Connell, T. D., and Holmes, R. K. (1992) Characterization of hybrid toxins produced in Escherichia coli by assembly of A and B polypeptides from type I and type II heat-labile enterotoxins. Infect. Immun. 60, 1653-1661
    • (1992) Infect. Immun. , vol.60 , pp. 1653-1661
    • Connell, T.D.1    Holmes, R.K.2
  • 25
    • 0023698050 scopus 로고
    • Isolation and some properties of A and B subunits of Vero toxin 2 and in vitro formation of hybrid toxins between subunits of Vero toxin 1 and Vero toxin 2 from Escherichia coli O157: H7
    • Ito, H., Yutsudo, T., Hirayama, T., and Takeda, Y. (1988) Isolation and some properties of A and B subunits of Vero toxin 2 and in vitro formation of hybrid toxins between subunits of Vero toxin 1 and Vero toxin 2 from Escherichia coli O157:H7. Microb. Pathog. 5, 189-195
    • (1988) Microb. Pathog. , vol.5 , pp. 189-195
    • Ito, H.1    Yutsudo, T.2    Hirayama, T.3    Takeda, Y.4
  • 26
    • 0024350890 scopus 로고
    • In vivo formation of hybrid toxins comprising Shiga toxin and the Shiga-like toxins and role of the B subunit in localization and cytotoxic activity
    • Weinstein, D. L., Jackson, M. P., Perera, L. P., Holmes, R. K., and O'Brien, A. D. (1989) In vivo formation of hybrid toxins comprising Shiga toxin and the Shiga-like toxins and role of the B subunit in localization and cytotoxic activity. Infect. Immun. 57, 3743-3750
    • (1989) Infect. Immun. , vol.57 , pp. 3743-3750
    • Weinstein, D.L.1    Jackson, M.P.2    Perera, L.P.3    Holmes, R.K.4    O'Brien, A.D.5
  • 27
    • 0019776719 scopus 로고
    • In vitro formation of hybrid toxins between subunits of Escherichia coli heat-labile enterotoxin and those of cholera enterotoxin
    • Takeda, Y., Honda, T., Taga, S., and Miwatani, T. (1981) In vitro formation of hybrid toxins between subunits of Escherichia coli heat-labile enterotoxin and those of cholera enterotoxin. Infect. Immun. 34, 341-346
    • (1981) Infect. Immun. , vol.34 , pp. 341-346
    • Takeda, Y.1    Honda, T.2    Taga, S.3    Miwatani, T.4
  • 28
    • 0033548246 scopus 로고    scopus 로고
    • Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin: Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity
    • Rodighiero, C., Aman, A. T., Kenny, M. J., Moss, J., Lencer, W. I., and Hirst, T. R. (1999) Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin: construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity. J. Biol. Chem. 274, 3962-3969
    • (1999) J. Biol. Chem. , vol.274 , pp. 3962-3969
    • Rodighiero, C.1    Aman, A.T.2    Kenny, M.J.3    Moss, J.4    Lencer, W.I.5    Hirst, T.R.6
  • 31
    • 0000486193 scopus 로고    scopus 로고
    • Adaptive multilevel finite element solution of the Poisson-Boltzmann equation I: Algorithms and examples
    • Holst, M., Baker, N., and Wang, F. (2000) Adaptive multilevel finite element solution of the Poisson-Boltzmann equation I: Algorithms and examples. J. Comput. Chem. 21, 1319-1342
    • (2000) J. Comput. Chem. , vol.21 , pp. 1319-1342
    • Holst, M.1    Baker, N.2    Wang, F.3
  • 34
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.