메뉴 건너뛰기




Volumn 30, Issue 2, 2003, Pages 293-300

Production and proteolytic assay of lethal factor from Bacillus anthracis

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ANTHRAX; BACILLUS ANTHRACIS; ESCHERICHIA COLI;

EID: 0041568569     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00132-3     Document Type: Article
Times cited : (18)

References (35)
  • 1
    • 0034816420 scopus 로고    scopus 로고
    • Rapid purification of recombinant anthrax-protective antigen under nondenaturing conditions
    • N. Ahuja, P. Kumar, R. Bhatnagar, Rapid purification of recombinant anthrax-protective antigen under nondenaturing conditions, Biochem. Biophys. Res. Commun. 286 (2001) 6-11.
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 6-11
    • Ahuja, N.1    Kumar, P.2    Bhatnagar, R.3
  • 2
    • 0024327681 scopus 로고
    • Calcium is required for the expression of anthrax lethal toxin activity in the macrophage-like cell line J774A.1
    • R. Bhatnagar, Y. Singh, S.H. Leppla, A.M. Friedlander, Calcium is required for the expression of anthrax lethal toxin activity in the macrophage-like cell line J774A.1, Infect. Immun. 57 (1989) 2107-2117.
    • (1989) Infect. Immun. , vol.57 , pp. 2107-2117
    • Bhatnagar, R.1    Singh, Y.2    Leppla, S.H.3    Friedlander, A.M.4
  • 3
    • 0024523836 scopus 로고
    • Anthrax toxin: Channel-forming activity of protective antigen in planar phospholipid bilayers
    • R.O. Blaustein, T.M. Koehler, R.J. Collier, A. Finkelstein, Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers, Proc. Natl. Acad. Sci. USA 86 (1989) 2209-2213.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2209-2213
    • Blaustein, R.O.1    Koehler, T.M.2    Collier, R.J.3    Finkelstein, A.4
  • 4
    • 0038322024 scopus 로고    scopus 로고
    • Anthrax lethal factor proteolysis and inactivation of MAP-kinase-kinase
    • A.P. Chopra, S.A. Boone, X. Liang, N.S. Duesbery, Anthrax lethal factor proteolysis and inactivation of MAP-kinase-kinase, J. Biol. Chem. 278 (2003) 9402-9406.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9402-9406
    • Chopra, A.P.1    Boone, S.A.2    Liang, X.3    Duesbery, N.S.4
  • 6
    • 0035957358 scopus 로고    scopus 로고
    • Suppression if ras-mediated transformation and inhibition of tumor growth and angiogenesis by anthrax lethal factor, a proteolytic inhibitor of multiple MEK pathways
    • N.S. Duesbery, J. Resau, C.P. Webb, S. Koochekpour, H.M. Koo, S.H. Leppla, G.F. Vande Woude, Suppression if ras-mediated transformation and inhibition of tumor growth and angiogenesis by anthrax lethal factor, a proteolytic inhibitor of multiple MEK pathways, Proc. Natl. Acad. Sci. USA 98 (2001) 4089-4094.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4089-4094
    • Duesbery, N.S.1    Resau, J.2    Webb, C.P.3    Koochekpour, S.4    Koo, H.M.5    Leppla, S.H.6    Vande Woude, G.F.7
  • 8
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process
    • A.M. Friedlander, Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process, J. Biol. Chem. 261 (1986) 7123-7126.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 11
    • 0034809345 scopus 로고    scopus 로고
    • Effect of pH on stability of anthrax lethal factor: Correlation between denaturation and activity
    • P. Gupta, S. Singh, A. Tiwari, R. Bhat, R. Bhatnagar, Effect of pH on stability of anthrax lethal factor: correlation between denaturation and activity, Biochem. Biophys. Res. Commun. 284 (2001) 568-573.
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 568-573
    • Gupta, P.1    Singh, S.2    Tiwari, A.3    Bhat, R.4    Bhatnagar, R.5
  • 12
    • 0033179823 scopus 로고    scopus 로고
    • Expression and purification of the recombinant protective antigen of Bacillus anthracis
    • P. Gupta, S.M. Waheed, R. Bhatnagar, Expression and purification of the recombinant protective antigen of Bacillus anthracis, Protein Expr. Purif. 16 (1999) 369-376.
    • (1999) Protein Expr. Purif. , vol.16 , pp. 369-376
    • Gupta, P.1    Waheed, S.M.2    Bhatnagar, R.3
  • 13
    • 0031946979 scopus 로고    scopus 로고
    • Lethal factor active-site mutations affect catalytic activity in vitro
    • S.E. Hammond, P.C. Hanna, Lethal factor active-site mutations affect catalytic activity in vitro, Infect. Immun. 66 (1998) 2374-2378.
    • (1998) Infect. Immun. , vol.66 , pp. 2374-2378
    • Hammond, S.E.1    Hanna, P.C.2
  • 14
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • R.K. Klimpel, S.S. Molloy, G. Thomas, S.H. Leppla, Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin, Proc. Natl. Acad. Sci. USA 89 (1992) 10277-10281.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10277-10281
    • Klimpel, R.K.1    Molloy, S.S.2    Thomas, G.3    Leppla, S.H.4
  • 15
    • 0037022666 scopus 로고    scopus 로고
    • Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase
    • H.M. Koo, M. VanBrocklin, M.J. McWilliams, S.H. Leppla, N.S. Duesbery, G.F. Woude, Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase, Proc. Natl. Acad. Sci. USA 99 (2002) 3052-3057.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 3052-3057
    • Koo, H.M.1    VanBrocklin, M.2    McWilliams, M.J.3    Leppla, S.H.4    Duesbery, N.S.5    Woude, G.F.6
  • 16
    • 0024214705 scopus 로고
    • Production and purification of anthrax toxin
    • Academic Press, New York
    • S.H. Leppla, Production and purification of anthrax toxin, in: Methods in Enzymology, vol. 165, Academic Press, New York, 1988, pp. 103-116.
    • (1988) Methods in Enzymology , vol.165 , pp. 103-116
    • Leppla, S.H.1
  • 17
    • 0020681139 scopus 로고
    • Evidence for plasmid mediated toxin production in Bacillus anthracis
    • O.P. Mikesell, B.E. Ivins, J.D. Ristroph, T.M. Dreier, Evidence for plasmid mediated toxin production in Bacillus anthracis, Infect. Immun. 39 (1983) 371-376.
    • (1983) Infect. Immun. , vol.39 , pp. 371-376
    • Mikesell, O.P.1    Ivins, B.E.2    Ristroph, J.D.3    Dreier, T.M.4
  • 19
    • 0037076268 scopus 로고    scopus 로고
    • Progress in rapid screening of Bacillus anthracis lethal factor activity
    • M. Mock, B.P. Roques, Progress in rapid screening of Bacillus anthracis lethal factor activity, Proc. Natl. Acad. Sci. USA 99 (2002) 6527-6529.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6527-6529
    • Mock, M.1    Roques, B.P.2
  • 20
    • 0035969533 scopus 로고    scopus 로고
    • Recognition and management of anthrax
    • N. Morton, M.D. Swartz, Recognition and management of anthrax, N. Engl. J. Med. 345 (2001) 1621-1626.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 1621-1626
    • Morton, N.1    Swartz, M.D.2
  • 22
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • J.M. Park, F.R. Greten, Z.W. Li, M. Karin, Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition, Science 297 (2002) 2048-2051.
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3    Karin, M.4
  • 23
    • 0034049623 scopus 로고    scopus 로고
    • Optimized production and purification of Bacillus anthracis lethal factor
    • S. Park, S.H. Leppla, Optimized production and purification of Bacillus anthracis lethal factor, Protein Expr. Purif. 18 (2000) 293-302.
    • (2000) Protein Expr. Purif. , vol.18 , pp. 293-302
    • Park, S.1    Leppla, S.H.2
  • 24
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα
    • R. Pellizzari, C. Guidi-Rontani, G. Vitale, M. Mock, C. Montecucco, Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNFα, FEBS Lett. 462 (1999) 199-204.
    • (1999) FEBS Lett. , vol.462 , pp. 199-204
    • Pellizzari, R.1    Guidi-Rontani, C.2    Vitale, G.3    Mock, M.4    Montecucco, C.5
  • 27
    • 0030087551 scopus 로고    scopus 로고
    • Expression and purification of anthrax toxin protective antigen from Escherichia coli
    • M. Sharma, P.K. Swain, A.P. Chopra, V.K. Chaudhary, Y. Singh, Expression and purification of anthrax toxin protective antigen from Escherichia coli, Protein Expr. Purif. 7 (1996) 33-38.
    • (1996) Protein Expr. Purif. , vol.7 , pp. 33-38
    • Sharma, M.1    Swain, P.K.2    Chopra, A.P.3    Chaudhary, V.K.4    Singh, Y.5
  • 28
    • 0028075838 scopus 로고
    • Heat shock-induced phosphorylation of GroEL alters its binding and dissociation from unfolded proteins
    • M. Sherman, A.L. Goldberg, Heat shock-induced phosphorylation of GroEL alters its binding and dissociation from unfolded proteins, J. Biol. Chem. 50 (1994) 31479-31483.
    • (1994) J. Biol. Chem. , vol.50 , pp. 31479-31483
    • Sherman, M.1    Goldberg, A.L.2
  • 30
    • 0001731185 scopus 로고
    • Observations on experimental anthrax: Demonstration of a specific lethal factor produced in vivo by Bacillus anthracis
    • H. Smith, J. Keppie, Observations on experimental anthrax: demonstration of a specific lethal factor produced in vivo by Bacillus anthracis, Nature 173 (1954) 869-870.
    • (1954) Nature , vol.173 , pp. 869-870
    • Smith, H.1    Keppie, J.2
  • 31
    • 0033056295 scopus 로고    scopus 로고
    • Proteasome activity is requires for anthrax lethal toxin to kill macrophages
    • G. Tang, S.H. Leppla, Proteasome activity is requires for anthrax lethal toxin to kill macrophages, Infect. Immun. 67 (1999) 3055-3060.
    • (1999) Infect. Immun. , vol.67 , pp. 3055-3060
    • Tang, G.1    Leppla, S.H.2
  • 32
    • 0030158243 scopus 로고    scopus 로고
    • A method for the separation of GST fusion protein from co-purifying GroEL
    • A. Thain, K. Gaston, O. Jenkins, A.R. Clarke, A method for the separation of GST fusion protein from co-purifying GroEL, Trend Genet. 6 (1996) 209-210.
    • (1996) Trend Genet. , vol.6 , pp. 209-210
    • Thain, A.1    Gaston, K.2    Jenkins, O.3    Clarke, A.R.4
  • 34
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • G. Vitale, L. Bernardi, G. Napolitani, M. Mock, C. Montecucco, Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor, J. Biochem. 352 (2000) 739-745.
    • (2000) J. Biochem. , vol.352 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 35
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • G. Vitale, R. Pellizzari, C. Recchi, G. Napolitani, M. Mock, C. Montecucco, Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages, Biochem. Biophys. Res. Commun. 248 (1998) 706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.