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Volumn 72, Issue 1, 2004, Pages 602-605

Protection against Anthrax Toxemia by Hexa-D-Arginine In Vitro and In Vivo

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRAX TOXIN; ANTIGEN; DEXTRO ARGININE; FURIN; HEXA DEXTRO ARGININE; POLYPEPTIDE; UNCLASSIFIED DRUG;

EID: 0346881395     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.72.1.602-605.2004     Document Type: Article
Times cited : (76)

References (26)
  • 2
    • 0034862444 scopus 로고    scopus 로고
    • Toxins of Bacillus anthracis
    • Brossier, F., and M. Mock. 2001. Toxins of Bacillus anthracis. Toxicon 39:1747-1755.
    • (2001) Toxicon , vol.39 , pp. 1747-1755
    • Brossier, F.1    Mock, M.2
  • 3
    • 0034073579 scopus 로고    scopus 로고
    • Role of toxin functional domains in anthrax pathogenesis
    • Brossier, F., M. Weber-Levy, M. Mock, and J. C. Sirard. 2000. Role of toxin functional domains in anthrax pathogenesis. Infect. Immun. 68:1781-1786.
    • (2000) Infect. Immun. , vol.68 , pp. 1781-1786
    • Brossier, F.1    Weber-Levy, M.2    Mock, M.3    Sirard, J.C.4
  • 5
    • 0036468526 scopus 로고    scopus 로고
    • Quickening the pace of anthrax research: Three advances point to possible therapies
    • Chaudry, G. J., M. Moayeri, S. Liu, and S. H. Leppla. 2001. Quickening the pace of anthrax research: three advances point to possible therapies. Trends Microbiol. 10:58-62.
    • (2001) Trends Microbiol. , vol.10 , pp. 58-62
    • Chaudry, G.J.1    Moayeri, M.2    Liu, S.3    Leppla, S.H.4
  • 6
    • 0021285324 scopus 로고
    • Immunoelectrophoretic analysis, toxicity, and kinetics of in vitro production of the protective antigen and lethal factor components of Bacillus anthracis toxin
    • Ezzell, J. W., B. E. lvins, and S. H. Leppla. 1984. Immunoelectrophoretic analysis, toxicity, and kinetics of in vitro production of the protective antigen and lethal factor components of Bacillus anthracis toxin. Infect. Immun. 45:761-767.
    • (1984) Infect. Immun. , vol.45 , pp. 761-767
    • Ezzell, J.W.1    Lvins, B.E.2    Leppla, S.H.3
  • 8
    • 0028859127 scopus 로고
    • In vitro processing of anthrax toxin protective antigen by recombinant PC1 (SPC3) and bovine intermediate lobe secretory vesicle membranes
    • Friedman, T. C., V. M. Gordon, S. H. Leppla, K. R. Klimpel, N. P. Birch, and Y. P. Loh. 1995. In vitro processing of anthrax toxin protective antigen by recombinant PC1 (SPC3) and bovine intermediate lobe secretory vesicle membranes. Arch. Biochem. Biophys. 316:5-13.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 5-13
    • Friedman, T.C.1    Gordon, V.M.2    Leppla, S.H.3    Klimpel, K.R.4    Birch, N.P.5    Loh, Y.P.6
  • 9
    • 0030807070 scopus 로고    scopus 로고
    • A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen
    • Gordon, V. M., A. Rehemtulla, and S. H. Leppla. 1997. A role for PACE4 in the proteolytic activation of anthrax toxin protective antigen. Infect. Immun. 65:3370-3375.
    • (1997) Infect. Immun. , vol.65 , pp. 3370-3375
    • Gordon, V.M.1    Rehemtulla, A.2    Leppla, S.H.3
  • 11
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • Klimpel, K., S. Molloy, G. Thomas, and S. Leppla. 1992. 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 89:10277-10281.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10277-10281
    • Klimpel, K.1    Molloy, S.2    Thomas, G.3    Leppla, S.4
  • 13
    • 0002107879 scopus 로고    scopus 로고
    • J. A. Alouf and J. Freer (ed.). Academic Press, London, United Kingdom
    • Leppla, S. H. 1999. p. 243-263. In J. A. Alouf and J. Freer (ed.), Comprehensive sourcebook of bacterial protein toxins. Academic Press, London, United Kingdom.
    • (1999) Comprehensive Sourcebook of Bacterial Protein Toxins , pp. 243-263
    • Leppla, S.H.1
  • 14
    • 0034957451 scopus 로고    scopus 로고
    • A dominant-negative therapy for anthrax
    • Leppla, S. H. 2001. A dominant-negative therapy for anthrax. Nat. Med. 7:659-660.
    • (2001) Nat. Med. , vol.7 , pp. 659-660
    • Leppla, S.H.1
  • 15
    • 0001616921 scopus 로고    scopus 로고
    • Anthrax toxin fusion proteins for intracellular delivery of macromolecules
    • Leppla, S. H., N. Arora, and M. Varughese. 1999. Anthrax toxin fusion proteins for intracellular delivery of macromolecules. J. Appl. Microbiol. 87:284.
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 284
    • Leppla, S.H.1    Arora, N.2    Varughese, M.3
  • 18
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy, S. S., P. A. Bresnahan, S. H. Leppla, K. R. Klimpel, and G. Thomas. 1992. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen. J. Biol. Chem. 267:16396-16402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 21
    • 0036893450 scopus 로고    scopus 로고
    • The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo
    • Sarac, M. S., A. Cameron, and I. Lindberg. 2002. The furin inhibitor hexa-D-arginine blocks the activation of Pseudomonas aeruginosa exotoxin A in vivo. Infect. Immun. 70:7136-7139.
    • (2002) Infect. Immun. , vol.70 , pp. 7136-7139
    • Sarac, M.S.1    Cameron, A.2    Lindberg, I.3
  • 22
    • 0033066901 scopus 로고    scopus 로고
    • Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells
    • Singh, Y., K. R. Klimpel, S. Goel, P. K. Swain, and S. H. Leppla. 1999. Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells. Infect. Immun. 67:1853-1859.
    • (1999) Infect. Immun. , vol.67 , pp. 1853-1859
    • Singh, Y.1    Klimpel, K.R.2    Goel, S.3    Swain, P.K.4    Leppla, S.H.5
  • 23
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • Soelaiman, S., B. Q. Wei, P. Bergson, Y. S. Lee, Y. Shen, M. Mrksich, B. K. Scholchet, and W. J. Tang. 2003. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chcm. 278:25990-25997.
    • (2003) J. Biol. Chcm. , vol.278 , pp. 25990-25997
    • Soelaiman, S.1    Wei, B.Q.2    Bergson, P.3    Lee, Y.S.4    Shen, Y.5    Mrksich, M.6    Scholchet, B.K.7    Tang, W.J.8
  • 25
    • 0022599644 scopus 로고
    • Differences in susceptibility of inbred mice to Bacillus anthracis
    • Welkos, S. L., T. J. Keener, and P. H. Gibbs. 1986. Differences in susceptibility of inbred mice to Bacillus anthracis. Infect. Immun. 51:795-800.
    • (1986) Infect. Immun. , vol.51 , pp. 795-800
    • Welkos, S.L.1    Keener, T.J.2    Gibbs, P.H.3
  • 26
    • 0035110350 scopus 로고    scopus 로고
    • Role of furin in delivery of CTL epitope of an anthrax toxin-fusion protein
    • Zhang, Y., Y. Kida, K. Kuwano, Y. Misumi, Y. Ikehara, and S. Arai. 2001. Role of furin in delivery of CTL epitope of an anthrax toxin-fusion protein. Microbiol. Immunol. 45:119-125.
    • (2001) Microbiol. Immunol. , vol.45 , pp. 119-125
    • Zhang, Y.1    Kida, Y.2    Kuwano, K.3    Misumi, Y.4    Ikehara, Y.5    Arai, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.