메뉴 건너뛰기




Volumn 7, Issue 6, 2007, Pages 843-854

New insights into the pathogenesis and treatment of anthrax toxin-induced shock

Author keywords

Anthrax; Pathogenesis; Toxin; Treatment

Indexed keywords

ANTHRAX TOXIN; ANTIBIOTIC AGENT; CLINDAMYCIN; RIFAMPICIN;

EID: 34250737810     PISSN: 14712598     EISSN: None     Source Type: Journal    
DOI: 10.1517/14712598.7.6.843     Document Type: Review
Times cited : (15)

References (114)
  • 1
    • 33644897590 scopus 로고    scopus 로고
    • HOLTY JE, BRAVATA DM, LIU H et al.: Systematic review: a century of inhalational anthrax cases from 1900 to 2005. Ann. Intern. Med. (2006) 144:270-280. • An important review of all anthrax cases reported on in the US over the past 100 years.
    • HOLTY JE, BRAVATA DM, LIU H et al.: Systematic review: a century of inhalational anthrax cases from 1900 to 2005. Ann. Intern. Med. (2006) 144:270-280. • An important review of all anthrax cases reported on in the US over the past 100 years.
  • 2
    • 0035202697 scopus 로고    scopus 로고
    • JERNIGAN JA, STEPHENS DS, ASHFORD DA: Bioterrorrissm-related inhalational anthrax: the first 10 cases reported in the United States. Emerg. Infect. Dis. (2001) 7:933-944. • A comprehensive clinical review of 10 of the 11 inhalational anthrax cases presenting during the 2001 outbreak in the US.
    • JERNIGAN JA, STEPHENS DS, ASHFORD DA: Bioterrorrissm-related inhalational anthrax: the first 10 cases reported in the United States. Emerg. Infect. Dis. (2001) 7:933-944. • A comprehensive clinical review of 10 of the 11 inhalational anthrax cases presenting during the 2001 outbreak in the US.
  • 3
    • 33846842333 scopus 로고    scopus 로고
    • Lethal and edema toxins in the pathogenesis of Bacillus anthracis septic shock: Implications for therapy
    • SHERER K, LI Y, CUI X, EICHACKER PQ: Lethal and edema toxins in the pathogenesis of Bacillus anthracis septic shock: implications for therapy. Am. J. Respir. Crit. Care Med. (2007) 175:211-221.
    • (2007) Am. J. Respir. Crit. Care Med , vol.175 , pp. 211-221
    • SHERER, K.1    LI, Y.2    CUI, X.3    EICHACKER, P.Q.4
  • 4
    • 0001256478 scopus 로고    scopus 로고
    • Anthrax toxin
    • Aktories K, Just I Eds, New York, NY: Springer
    • LEPPLA SH: Anthrax toxin. In: Bacterial Proteins. Aktories K, Just I (Eds), New York, NY: Springer (2000):445-472.
    • (2000) Bacterial Proteins , pp. 445-472
    • LEPPLA, S.H.1
  • 6
    • 33750022662 scopus 로고    scopus 로고
    • Bacillus anthracis: A multi-faceted role for anthrax lethal toxin in thwarting host immune defenses
    • XU L, FRUCHT DM: Bacillus anthracis: a multi-faceted role for anthrax lethal toxin in thwarting host immune defenses. Int. J. Biochem. Cell Biol. (2007) 39:20-24.
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 20-24
    • XU, L.1    FRUCHT, D.M.2
  • 7
    • 4444317796 scopus 로고    scopus 로고
    • Antitoxins: Novel strategies to target agents of bioterrorism
    • RAINEY GJA, YOUNG JAT: Antitoxins: novel strategies to target agents of bioterrorism. Nat. Rev. Microbiol. (2004) 2:721-726.
    • (2004) Nat. Rev. Microbiol , vol.2 , pp. 721-726
    • GJA, R.1    JAT, Y.2
  • 8
    • 0031052342 scopus 로고    scopus 로고
    • Crystal structure of the anthrax toxin protective antigen
    • PETOSA C, COLLIER RJ, KLIMPEL KR et al.: Crystal structure of the anthrax toxin protective antigen. Nature (1997) 385:833-838.
    • (1997) Nature , vol.385 , pp. 833-838
    • PETOSA, C.1    COLLIER, R.J.2    KLIMPEL, K.R.3
  • 9
    • 0035829509 scopus 로고    scopus 로고
    • Identification of the cellular receptor for anthrax toxin
    • BRADLEY KA, MOGRIDGE J, MOUREZ M et al.: Identification of the cellular receptor for anthrax toxin. Nature (2001) 414:225-229.
    • (2001) Nature , vol.414 , pp. 225-229
    • BRADLEY, K.A.1    MOGRIDGE, J.2    MOUREZ, M.3
  • 10
    • 0038303163 scopus 로고    scopus 로고
    • Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor
    • SCOBIE HM, RAINEY GJ, BRADLEY KA, YOUNG JA: Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor. Proc. Natl. Acad. Sci. USA (2003) 100:5170-5174.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5170-5174
    • SCOBIE, H.M.1    RAINEY, G.J.2    BRADLEY, K.A.3    YOUNG, J.A.4
  • 11
    • 2342454381 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: An anthrax toxin receptor
    • LACY DB, WIGELSWORTH DJ, SCOBIE HM et al.: Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. Proc. Natl. Acad. Sci. USA (2004) 101:6367-6372.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6367-6372
    • LACY, D.B.1    WIGELSWORTH, D.J.2    SCOBIE, H.M.3
  • 12
    • 33750474061 scopus 로고    scopus 로고
    • SCOBIE HM, WIGELSWORTH DJ, MARLETT JM et al.: Anthrax toxin receptor 2-dependent lethal toxin killing in vivo. PLoS Pathog. (2006) 2(10):e111. • A report including references to other recent work directed at anthrax toxin and host cell receptor interactions.
    • SCOBIE HM, WIGELSWORTH DJ, MARLETT JM et al.: Anthrax toxin receptor 2-dependent lethal toxin killing in vivo. PLoS Pathog. (2006) 2(10):e111. • A report including references to other recent work directed at anthrax toxin and host cell receptor interactions.
  • 13
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • GORDON VM, KLIMPEL KR, ARORA N et al.: Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. (1995) 63:82-87.
    • (1995) Infect. Immun , vol.63 , pp. 82-87
    • GORDON, V.M.1    KLIMPEL, K.R.2    ARORA, N.3
  • 14
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • ABRAMI L, LIU S, COSSON P et al.: Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. (2003) 160:321-328.
    • (2003) J. Cell Biol , vol.160 , pp. 321-328
    • ABRAMI, L.1    LIU, S.2    COSSON, P.3
  • 15
    • 31544434936 scopus 로고    scopus 로고
    • Both PA63 and PA83 are endocytosed within an anthrax protective antigen mixed heptamer: A putative mechanism to overcome a furin deficiency
    • CHEKANOV AV, REMACLE AG, GOLUBKOV VS et al.: Both PA63 and PA83 are endocytosed within an anthrax protective antigen mixed heptamer: a putative mechanism to overcome a furin deficiency. Arch. Biochem. Biophys. (2006) 446:52-59.
    • (2006) Arch. Biochem. Biophys , vol.446 , pp. 52-59
    • CHEKANOV, A.V.1    REMACLE, A.G.2    GOLUBKOV, V.S.3
  • 16
    • 0037076364 scopus 로고    scopus 로고
    • The lethal and edema factors of anthrax toxin bind only to oligometic forms of the protective antigen
    • MOGRIDGE J, CUNNINGHAM K, LACY DB et al.: The lethal and edema factors of anthrax toxin bind only to oligometic forms of the protective antigen. Proc. Natl. Acad. Sci. USA (2002) 99:7045-7048.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7045-7048
    • MOGRIDGE, J.1    CUNNINGHAM, K.2    LACY, D.B.3
  • 18
    • 33646019842 scopus 로고    scopus 로고
    • The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin
    • WEI W, LU Q, CHAUDRY GJ et al.: The LDL receptor-related protein LRP6 mediates internalization and lethality of anthrax toxin. Cell (2006) 124:1141-1154.
    • (2006) Cell , vol.124 , pp. 1141-1154
    • WEI, W.1    LU, Q.2    CHAUDRY, G.J.3
  • 19
    • 34047224102 scopus 로고    scopus 로고
    • LRP5 and LRP6 are not required for protective antigen-mediated internalization or lethality from anthrax lethal toxin
    • YOUNG JJ, BROMBERG-WHITE JL, ZYLSTRA C et al.: LRP5 and LRP6 are not required for protective antigen-mediated internalization or lethality from anthrax lethal toxin. PLoS Pathog. (2007) 3(3):e27.
    • (2007) PLoS Pathog , vol.3 , Issue.3
    • YOUNG, J.J.1    BROMBERG-WHITE, J.L.2    ZYLSTRA, C.3
  • 21
    • 0035829518 scopus 로고    scopus 로고
    • Crystal structure of the anthrax lethal factor
    • PANNIFER AD, WONG TY, SCHWARZENBACHER R et al.: Crystal structure of the anthrax lethal factor Nature (2001) 414:229-233.
    • (2001) Nature , vol.414 , pp. 229-233
    • PANNIFER, A.D.1    WONG, T.Y.2    SCHWARZENBACHER, R.3
  • 22
    • 18244414803 scopus 로고    scopus 로고
    • DUESBERY NS, WEBB CP, LEPPLA SH et al.: Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science (1998) 280:734-737. • An early work identifying lethal factor's actions and intracellular target.
    • DUESBERY NS, WEBB CP, LEPPLA SH et al.: Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science (1998) 280:734-737. • An early work identifying lethal factor's actions and intracellular target.
  • 23
    • 0000823104 scopus 로고
    • The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. Anthracis in vivo
    • SMITH H, KEPPIE J, STANLEY JL: The chemical basis of the virulence of Bacillus anthracis. V. The specific toxin produced by B. Anthracis in vivo. Br. J. Exp. Pathol. (1955) 36:460-472.
    • (1955) Br. J. Exp. Pathol , vol.36 , pp. 460-472
    • SMITH, H.1    KEPPIE, J.2    STANLEY, J.L.3
  • 24
    • 73049164375 scopus 로고
    • Purification of Factor I and recognition of a third factor of the anthrax toxin
    • STANLEY JL, SMITH H: Purification of Factor I and recognition of a third factor of the anthrax toxin. J. Gen. Microbiol. (1961) 26:49-63.
    • (1961) J. Gen. Microbiol , vol.26 , pp. 49-63
    • STANLEY, J.L.1    SMITH, H.2
  • 25
    • 0345504971 scopus 로고
    • In vivo effects of B. anthracis culture filtrates
    • ECKERT NJ, BONVENTRE PF: In vivo effects of B. anthracis culture filtrates. J. Infect. Dis. (1963) 112:226-232.
    • (1963) J. Infect. Dis , vol.112 , pp. 226-232
    • ECKERT, N.J.1    BONVENTRE, P.F.2
  • 26
    • 0013922581 scopus 로고
    • The pathogenesis of the lethal effect of anthrax toxin in the rat
    • BEALL FA, DALLDORF FG: The pathogenesis of the lethal effect of anthrax toxin in the rat. J. Infect. Dis. (1966) 116:377-389.
    • (1966) J. Infect. Dis , vol.116 , pp. 377-389
    • BEALL, F.A.1    DALLDORF, F.G.2
  • 27
    • 0014252017 scopus 로고
    • Pathophysiological changes in the rat associated with anthrax toxin
    • FISH DC, KLEIN F, LINCOLN RE et al.: Pathophysiological changes in the rat associated with anthrax toxin. J. Infect. Dis. (1968) 118:114-124.
    • (1968) J. Infect. Dis , vol.118 , pp. 114-124
    • FISH, D.C.1    KLEIN, F.2    LINCOLN, R.E.3
  • 28
    • 0014252491 scopus 로고
    • Neurological and physiological responses of the primate to anthrax toxin
    • VICK JA, LINCOLN RE, KLEIN F et al.: Neurological and physiological responses of the primate to anthrax toxin. J. Infect. Dis. (1968) 118(1):85-96.
    • (1968) J. Infect. Dis , vol.118 , Issue.1 , pp. 85-96
    • VICK, J.A.1    LINCOLN, R.E.2    KLEIN, F.3
  • 29
    • 12144288811 scopus 로고    scopus 로고
    • Lethality during continuous anthrax lethal toxin infusion is associated with circulatory shock but not inflammatory cytokine or nitric oxide release in rats
    • CUI X, MOAYERI M, LI Y et al.: Lethality during continuous anthrax lethal toxin infusion is associated with circulatory shock but not inflammatory cytokine or nitric oxide release in rats. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2004) 286:R699-R709.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.286
    • CUI, X.1    MOAYERI, M.2    LI, Y.3
  • 30
    • 19944433149 scopus 로고    scopus 로고
    • Late treatment with a protective antigen derived monoclonal antibody improves hemodynamic function and survival in a lethal toxin-infused rat model of anthrax sepsis
    • CUI X, LI Y, MOAYERI M et al.: Late treatment with a protective antigen derived monoclonal antibody improves hemodynamic function and survival in a lethal toxin-infused rat model of anthrax sepsis. J. Infect. Dis. (2005) 191:422-434.
    • (2005) J. Infect. Dis , vol.191 , pp. 422-434
    • CUI, X.1    LI, Y.2    MOAYERI, M.3
  • 32
    • 33747066785 scopus 로고    scopus 로고
    • BALDARI CT, TONELLO F, PACCANI SR, MONTECUUCO C: Anthrax toxins: a paradigm of bacterial immune suppression. Trends Immunol. (2006) 27(9):434-440. • A review summarizing recent work on the potential immunosuppressive effects of anthrax toxins.
    • BALDARI CT, TONELLO F, PACCANI SR, MONTECUUCO C: Anthrax toxins: a paradigm of bacterial immune suppression. Trends Immunol. (2006) 27(9):434-440. • A review summarizing recent work on the potential immunosuppressive effects of anthrax toxins.
  • 33
    • 0032755353 scopus 로고    scopus 로고
    • PELLIZZARI R, GUIDI-RONTANI C, VTTALE G et al.: Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNF. FEBS Lett. (1999) 462:199-204. • One of the first in vitro suides to show that lethal factor can suppress elements of the host innate immune response.
    • PELLIZZARI R, GUIDI-RONTANI C, VTTALE G et al.: Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNγ-induced release of NO and TNF. FEBS Lett. (1999) 462:199-204. • One of the first in vitro suides to show that lethal factor can suppress elements of the host innate immune response.
  • 34
    • 0035142005 scopus 로고    scopus 로고
    • Macrophage-derived cell lines do not express proinflammatory cytokines after exposure to Bacillus anthracis lethal toxin
    • ERWIN JL, DASILVA LM, BAVARI S et al.: Macrophage-derived cell lines do not express proinflammatory cytokines after exposure to Bacillus anthracis lethal toxin. Infect. Immun. (2001) 69:1175-1177.
    • (2001) Infect. Immun , vol.69 , pp. 1175-1177
    • ERWIN, J.L.1    DASILVA, L.M.2    BAVARI, S.3
  • 35
    • 1642577137 scopus 로고    scopus 로고
    • Cutting edge: Anthrax lethal toxin inhibits activation of IFN-regulatory factor 3 by lipopolysaccharide
    • DANG O, NAVARRO L, ANDERSON K, DAVID M: Cutting edge: anthrax lethal toxin inhibits activation of IFN-regulatory factor 3 by lipopolysaccharide. J. Immunol. (2004) 172:747-751.
    • (2004) J. Immunol , vol.172 , pp. 747-751
    • DANG, O.1    NAVARRO, L.2    ANDERSON, K.3    DAVID, M.4
  • 37
    • 0042964832 scopus 로고    scopus 로고
    • Impairment of dendritic cells and adaptive immunity by anthrax lethal toxin
    • AGRAWAL A, LINGAPPA J, LEPPLA SH et al.: Impairment of dendritic cells and adaptive immunity by anthrax lethal toxin. Nature (2003) 424:329-334.
    • (2003) Nature , vol.424 , pp. 329-334
    • AGRAWAL, A.1    LINGAPPA, J.2    LEPPLA, S.H.3
  • 38
    • 85047692288 scopus 로고    scopus 로고
    • MOAYERI M, HAINES D, YOUNG HA, LEPPLA SH: Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice. J. Clin. Invest. (2003) 112:670-682. • The first in vivo studies demonstrating that lethality associated with anthrax lethal toxin is not associated with excessive inflammatory cytokine release.
    • MOAYERI M, HAINES D, YOUNG HA, LEPPLA SH: Bacillus anthracis lethal toxin induces TNF-α-independent hypoxia-mediated toxicity in mice. J. Clin. Invest. (2003) 112:670-682. • The first in vivo studies demonstrating that lethality associated with anthrax lethal toxin is not associated with excessive inflammatory cytokine release.
  • 39
    • 33644880791 scopus 로고    scopus 로고
    • CUI X, LI Y, LI X et al.: Sublethal doses of Bacillus anthracis lethal toxin inhibit inflammation with lipopolysaccharide and Escherichia coli challenge but have opposite effects on survival. J. Infect. Dis. (2006) 193(6):829-840. • The initial in vivo study showing that anthrax lethal toxin can inhibit the host inflammatory response to both noninfectious and infectious stimuli.
    • CUI X, LI Y, LI X et al.: Sublethal doses of Bacillus anthracis lethal toxin inhibit inflammation with lipopolysaccharide and Escherichia coli challenge but have opposite effects on survival. J. Infect. Dis. (2006) 193(6):829-840. • The initial in vivo study showing that anthrax lethal toxin can inhibit the host inflammatory response to both noninfectious and infectious stimuli.
  • 40
    • 0346251030 scopus 로고    scopus 로고
    • KIRBY JE: Anthrax lethal toxin induces human endothelial cell apoptosis. Infect. Immun. (2004) 72:430-439. • One of the first studies to demonstrate the direct effects lethal toxin might have on endothelial cells.
    • KIRBY JE: Anthrax lethal toxin induces human endothelial cell apoptosis. Infect. Immun. (2004) 72:430-439. • One of the first studies to demonstrate the direct effects lethal toxin might have on endothelial cells.
  • 41
    • 19544371576 scopus 로고    scopus 로고
    • Anthrax lethal toxin induces endothelial barrier dysfunction
    • WARFEL JM, STEELE AD, D'AGNILLO F: Anthrax lethal toxin induces endothelial barrier dysfunction. Am. J. Pathol. (2005) 166:1871-1881.
    • (2005) Am. J. Pathol , vol.166 , pp. 1871-1881
    • WARFEL, J.M.1    STEELE, A.D.2    D'AGNILLO, F.3
  • 42
    • 31844441582 scopus 로고    scopus 로고
    • Anthrax lethal toxin induces ketotifen-sensitive intradermal vascular leakage in certain inbred mice
    • GOZES Y, MOAYERI M, WIGGINS JF, LEPPLA SH: Anthrax lethal toxin induces ketotifen-sensitive intradermal vascular leakage in certain inbred mice. Infect. Immun. (2006) 74:1266-1272.
    • (2006) Infect. Immun , vol.74 , pp. 1266-1272
    • GOZES, Y.1    MOAYERI, M.2    WIGGINS, J.F.3    LEPPLA, S.H.4
  • 43
    • 25444447355 scopus 로고    scopus 로고
    • Pathological manifestations in mice exposed to anthrax lethal toxin
    • CULLEY NC, PINSON DM, CHAKRABARTY A et al.: Pathological manifestations in mice exposed to anthrax lethal toxin. Infect. Immun. (2005) 73:7006-7010.
    • (2005) Infect. Immun , vol.73 , pp. 7006-7010
    • CULLEY, N.C.1    PINSON, D.M.2    CHAKRABARTY, A.3
  • 44
    • 21544472343 scopus 로고    scopus 로고
    • Endocrine perturbation increases susceptibility to anthrax lethal toxin
    • MOAYERI M, WEBSTER JI, WIGGINS JF et al.: Endocrine perturbation increases susceptibility to anthrax lethal toxin. Infect. Immun. (2005) 73:4238-4244.
    • (2005) Infect. Immun , vol.73 , pp. 4238-4244
    • MOAYERI, M.1    WEBSTER, J.I.2    WIGGINS, J.F.3
  • 45
    • 31744441475 scopus 로고    scopus 로고
    • Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin
    • BOYDEN ED, DIETRICH WF: Nalp1b controls mouse macrophage susceptibility to anthrax lethal toxin. Nat. Genet. (2006) 38:240-244.
    • (2006) Nat. Genet , vol.38 , pp. 240-244
    • BOYDEN, E.D.1    DIETRICH, W.F.2
  • 46
    • 0036295213 scopus 로고    scopus 로고
    • Lethal toxin of Bacillus anthracis causes apoptosis of macrophages
    • POPOV SG, VILLASMIL R, BERNARDI J et al.: Lethal toxin of Bacillus anthracis causes apoptosis of macrophages. Biochem. Biophys. Res. Commun. (2002) 293:349-355.
    • (2002) Biochem. Biophys. Res. Commun , vol.293 , pp. 349-355
    • POPOV, S.G.1    VILLASMIL, R.2    BERNARDI, J.3
  • 47
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 inhibition
    • PARK JM, GRETEN FR, LI Z, KARIN M: Macrophage apoptosis by anthrax lethal factor through p38 inhibition. Science (2002) 297:2048-2051.
    • (2002) Science , vol.297 , pp. 2048-2051
    • PARK, J.M.1    GRETEN, F.R.2    LI, Z.3    KARIN, M.4
  • 48
    • 0022973265 scopus 로고
    • Anthrax toxin blocks priming of neutrophils by lipopolysaccharide and by muramyl dipeptide
    • WRIGHT GC, MANDELL GI: Anthrax toxin blocks priming of neutrophils by lipopolysaccharide and by muramyl dipeptide. J. Exp. Med. (1986) 164:1700-1709.
    • (1986) J. Exp. Med , vol.164 , pp. 1700-1709
    • WRIGHT, G.C.1    MANDELL, G.I.2
  • 49
    • 23944507581 scopus 로고    scopus 로고
    • Anthrax lethal toxin paralyzes neutrophil actin-based motility
    • DURING RL, LI W, HAO B et al.: Anthrax lethal toxin paralyzes neutrophil actin-based motility. J. Infect. Dis. (2005) 192:837-845.
    • (2005) J. Infect. Dis , vol.192 , pp. 837-845
    • DURING, R.L.1    LI, W.2    HAO, B.3
  • 50
    • 33744914838 scopus 로고    scopus 로고
    • Bacillus anthracis toxins inhibit human neutrophil NADPH oxidase activity
    • CRAWFORD MA, AYLOTT CV, BOURDEAU RW, BOKOCH GM: Bacillus anthracis toxins inhibit human neutrophil NADPH oxidase activity. J. Immunol. (2006) 176:7557-7565.
    • (2006) J. Immunol , vol.176 , pp. 7557-7565
    • CRAWFORD, M.A.1    AYLOTT, C.V.2    BOURDEAU, R.W.3    BOKOCH, G.M.4
  • 51
    • 13644268542 scopus 로고    scopus 로고
    • Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signaling
    • PACCANI SR, TONELLO F, GHITTONI R et al.: Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signaling. J. Exp. Med. (2005) 201:325-331.
    • (2005) J. Exp. Med , vol.201 , pp. 325-331
    • PACCANI, S.R.1    TONELLO, F.2    GHITTONI, R.3
  • 52
    • 28444498350 scopus 로고    scopus 로고
    • Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo
    • COMER JE, CHOPRA AK, PETERSON JW, KONIG R: Direct inhibition of T-lymphocyte activation by anthrax toxins in vivo. Infect. Immun. (2005) 73:8275-8281.
    • (2005) Infect. Immun , vol.73 , pp. 8275-8281
    • COMER, J.E.1    CHOPRA, A.K.2    PETERSON, J.W.3    KONIG, R.4
  • 53
    • 34250762455 scopus 로고    scopus 로고
    • Anthrax toxins inhibit immune cell chemotaxis by perturbing chemokine receptor signalling
    • Epub ahead of print
    • ROSSI PACCANI S, TONELLO F, PATRUSSI L et al.: Anthrax toxins inhibit immune cell chemotaxis by perturbing chemokine receptor signalling. Cell. Microbiol. (2006) Epub ahead of print.
    • (2006) Cell. Microbiol
    • ROSSI PACCANI, S.1    TONELLO, F.2    PATRUSSI, L.3
  • 54
    • 33646484203 scopus 로고    scopus 로고
    • Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production
    • FANG H, XU L, CHEN TY et al.: Anthrax lethal toxin has direct and potent inhibitory effects on B cell proliferation and immunoglobulin production. J. Immunol. (2006) 176:6155-6161.
    • (2006) J. Immunol , vol.176 , pp. 6155-6161
    • FANG, H.1    XU, L.2    CHEN, T.Y.3
  • 55
    • 0033866471 scopus 로고    scopus 로고
    • Translocation on B. anthracis lethal and oedema factors across endosome membranes
    • GUIDI-RONTANI C, WEBER-LEVY M, MOCK M, CABIAUX V: Translocation on B. anthracis lethal and oedema factors across endosome membranes. Cell Microbiol. (2000) 2:259-264.
    • (2000) Cell Microbiol , vol.2 , pp. 259-264
    • GUIDI-RONTANI, C.1    WEBER-LEVY, M.2    MOCK, M.3    CABIAUX, V.4
  • 56
    • 33845941401 scopus 로고    scopus 로고
    • Anthrax edema factor, voltage-dependent binding to the protective antigen ion channel and comparison to LF binding
    • NEUMEYER T, TONELLO F, DAL MOLIN F et al.: Anthrax edema factor, voltage-dependent binding to the protective antigen ion channel and comparison to LF binding. J. Biol. Chem. (2006) 281(43):32335-32343.
    • (2006) J. Biol. Chem , vol.281 , Issue.43 , pp. 32335-32343
    • NEUMEYER, T.1    TONELLO, F.2    DAL MOLIN, F.3
  • 57
    • 0037169549 scopus 로고    scopus 로고
    • Mapping the anthrax protective antigen binding site on the lethal and edema factors
    • LACY DB, MOUREZ M, FOUASSIER A, COLLIERS RJ: Mapping the anthrax protective antigen binding site on the lethal and edema factors. J. Biol. Chem. (2002) 277:3006-3010.
    • (2002) J. Biol. Chem , vol.277 , pp. 3006-3010
    • LACY, D.B.1    MOUREZ, M.2    FOUASSIER, A.3    COLLIERS, R.J.4
  • 58
    • 0000947082 scopus 로고    scopus 로고
    • LEPPLA SH: Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations in eukaryotic cells. Proc. Natl. Acad. Sci. USA (1982) 79:3162-3166. • The initial in vitro study demonstrating the adenyl cyclase activity of anthrax edema factor.
    • LEPPLA SH: Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations in eukaryotic cells. Proc. Natl. Acad. Sci. USA (1982) 79:3162-3166. • The initial in vitro study demonstrating the adenyl cyclase activity of anthrax edema factor.
  • 59
    • 33751119538 scopus 로고    scopus 로고
    • Cell entry and cAMP imaging of anthrax edema toxin
    • DAL MOLIN F, TONELLO F, LADANT D et al.: Cell entry and cAMP imaging of anthrax edema toxin. EMBO J. (2006) 25:5405-5413.
    • (2006) EMBO J , vol.25 , pp. 5405-5413
    • DAL MOLIN, F.1    TONELLO, F.2    LADANT, D.3
  • 60
    • 16344384729 scopus 로고    scopus 로고
    • Calcium-independant calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor
    • SHEN Y, ZHUKOVSKAYA NL, GUO Q et al.: Calcium-independant calmodulin binding and two-metal-ion catalytic mechanism of anthrax edema factor. EMBO J. (2005) 24:929-941.
    • (2005) EMBO J , vol.24 , pp. 929-941
    • SHEN, Y.1    ZHUKOVSKAYA, N.L.2    GUO, Q.3
  • 62
    • 0036719095 scopus 로고    scopus 로고
    • Anthrax edema toxin requires influx of calcium for inducing cyclic AMP Toxicity in target cells
    • KUMAR P, AJUJA N, BHATNAGAR R: Anthrax edema toxin requires influx of calcium for inducing cyclic AMP Toxicity in target cells. Infect. Immun. (2002) 70:4997-5007.
    • (2002) Infect. Immun , vol.70 , pp. 4997-5007
    • KUMAR, P.1    AJUJA, N.2    BHATNAGAR, R.3
  • 63
    • 33748506107 scopus 로고    scopus 로고
    • Anthrax edema toxin induces anthrax toxin receptor expression in moncyte-derived cells
    • MALDONADO-AROCHO FJ, FULCHER JA, BENHUR L, BRADLEY KA Anthrax edema toxin induces anthrax toxin receptor expression in moncyte-derived cells. Mol. Microbiol. (2006) 61:324-337.
    • (2006) Mol. Microbiol , vol.61 , pp. 324-337
    • MALDONADO-AROCHO, F.J.1    FULCHER, J.A.2    BENHUR, L.3    BRADLEY, K.A.4
  • 64
    • 0021205725 scopus 로고
    • Anthrax: The disease in relation to vaccines
    • HAMBLETON P, CARMAN JA, MELLING J: Anthrax: the disease in relation to vaccines. Vaccine (1984) 2:125-132.
    • (1984) Vaccine , vol.2 , pp. 125-132
    • HAMBLETON, P.1    CARMAN, J.A.2    MELLING, J.3
  • 65
    • 27544500820 scopus 로고    scopus 로고
    • FIROVED AM, MILLER GF, MOAYERI M et al.: Bacillus anthracis edema toxin causes extensive tissue lesions and rapid lethality in mice. Am. J. Pathol. (2005) 167:1309-1320. • The first study to investigate the in vivo effects of highly purified preparations of anthrax edema toxin.
    • FIROVED AM, MILLER GF, MOAYERI M et al.: Bacillus anthracis edema toxin causes extensive tissue lesions and rapid lethality in mice. Am. J. Pathol. (2005) 167:1309-1320. • The first study to investigate the in vivo effects of highly purified preparations of anthrax edema toxin.
  • 66
    • 33846811743 scopus 로고    scopus 로고
    • CUI X, LI Y, LI X et al.: B. Anthracis edema and lethal toxin have different hemodynamic effects but function together to worsen shock and outcome in a rat model. J. Infect. Dis. (2007) 195:572-580. • The first in vivo study to directly compare the hemodynamic effects of anthrax edema and lethal toxins alone and together.
    • CUI X, LI Y, LI X et al.: B. Anthracis edema and lethal toxin have different hemodynamic effects but function together to worsen shock and outcome in a rat model. J. Infect. Dis. (2007) 195:572-580. • The first in vivo study to directly compare the hemodynamic effects of anthrax edema and lethal toxins alone and together.
  • 67
    • 0024988252 scopus 로고
    • Cyclic AMP and mechanisms of vasodilation
    • MURRAY KJ: Cyclic AMP and mechanisms of vasodilation. Pharmacol. Ther. (1990) 47:329-345.
    • (1990) Pharmacol. Ther , vol.47 , pp. 329-345
    • MURRAY, K.J.1
  • 68
    • 33846784814 scopus 로고    scopus 로고
    • Signal transduction: Receptors, coupling proteins, and second messengers
    • Philadelphia: Lippincott, Williams and Wilkins
    • KATZ AM: Signal transduction: receptors, coupling proteins, and second messengers. In: Physiology of the Heart. Philadelphia: Lippincott, Williams and Wilkins (2001):255-286.
    • (2001) Physiology of the Heart , pp. 255-286
    • KATZ, A.M.1
  • 69
    • 17044400220 scopus 로고    scopus 로고
    • TOURNIER J, QUESNEL-HELLMANN A, MATHIEU J et al.: Anthrax edema toxin cooperated with lethal toxin to impair cytokine secretion during infection of dendritic cells. J. Immunol. (2005) 174:4934-4941. • An important in vitro study examining the the immunosuppressive effects of anthrax edema and lethal toxins together.
    • TOURNIER J, QUESNEL-HELLMANN A, MATHIEU J et al.: Anthrax edema toxin cooperated with lethal toxin to impair cytokine secretion during infection of dendritic cells. J. Immunol. (2005) 174:4934-4941. • An important in vitro study examining the the immunosuppressive effects of anthrax edema and lethal toxins together.
  • 70
    • 25444495497 scopus 로고    scopus 로고
    • Bacillus anthracis edema toxin inhibits Staphylococcus aures enterotoxin B effects in vitro: A potential protein therapeutic?
    • KRAKAUER T, LITTLE SF, STILES BG: Bacillus anthracis edema toxin inhibits Staphylococcus aures enterotoxin B effects in vitro: a potential protein therapeutic? Infect. Immun. (2005) 73:7069-7073.
    • (2005) Infect. Immun , vol.73 , pp. 7069-7073
    • KRAKAUER, T.1    LITTLE, S.F.2    STILES, B.G.3
  • 71
    • 0027930622 scopus 로고
    • Anthrax edema toxin differentially regulates lipopolysaccharide-induced monocyte production of tumor necrosis factor alpha and interleukin-6 by increasing intracellular cyclic AMP
    • HOOVER DL, FRIEDLANDER AM, ROGERS LC et al.: Anthrax edema toxin differentially regulates lipopolysaccharide-induced monocyte production of tumor necrosis factor alpha and interleukin-6 by increasing intracellular cyclic AMP. Infect. Immun. (1994) 62:4432-4439.
    • (1994) Infect. Immun , vol.62 , pp. 4432-4439
    • HOOVER, D.L.1    FRIEDLANDER, A.M.2    ROGERS, L.C.3
  • 72
    • 0021930758 scopus 로고
    • Effects of anthrax toxin components on human neutrophils
    • O'BRIEN J, FRIEDLANDER A, DREIER T et al.: Effects of anthrax toxin components on human neutrophils. Infect. Immun. (1985) 47:306-310.
    • (1985) Infect. Immun , vol.47 , pp. 306-310
    • O'BRIEN, J.1    FRIEDLANDER, A.2    DREIER, T.3
  • 73
    • 11244316719 scopus 로고    scopus 로고
    • Effect of antibiotics on Group A Streptococcus exoprotein production analyzed by two-dimensional gel electrophoresis
    • TANAKA M, HASEGAWA T, OKAMOTO A et al.: Effect of antibiotics on Group A Streptococcus exoprotein production analyzed by two-dimensional gel electrophoresis. Antimicrob. Agents Chemother. (2005) 49:88-96.
    • (2005) Antimicrob. Agents Chemother , vol.49 , pp. 88-96
    • TANAKA, M.1    HASEGAWA, T.2    OKAMOTO, A.3
  • 74
    • 34250773747 scopus 로고    scopus 로고
    • BEEB E, ZHONG J, CLAGETT M et al.: Protection against inhalation anthrax-induced lethality by a human monoclonal antibody to protective antigen in rabbits and cynomologous monkeys [abstract B-33]. In: Program and abstracts of the 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy (Chicago). Washington, DC: American Society for Microbiology (2003):47.
    • BEEB E, ZHONG J, CLAGETT M et al.: Protection against inhalation anthrax-induced lethality by a human monoclonal antibody to protective antigen in rabbits and cynomologous monkeys [abstract B-33]. In: Program and abstracts of the 43rd Interscience Conference on Antimicrobial Agents and Chemotherapy (Chicago). Washington, DC: American Society for Microbiology (2003):47.
  • 75
    • 33846791092 scopus 로고    scopus 로고
    • Fluids have opposing effects on survival comparing lipopolysaccharide (LPS) and Bacillus anthracis lethal toxin (LeTx) challenge in rats
    • LI Y, CUI X, HALEY M et al.: Fluids have opposing effects on survival comparing lipopolysaccharide (LPS) and Bacillus anthracis lethal toxin (LeTx) challenge in rats. Am. J. Resp. Crit. Care. Med. (2005) 2:A39.
    • (2005) Am. J. Resp. Crit. Care. Med , vol.2
    • LI, Y.1    CUI, X.2    HALEY, M.3
  • 76
    • 34250714309 scopus 로고    scopus 로고
    • Increases in blood pressure with norepinephrine improve survival with LPS but not lethal toxin challenge in rats
    • LI Y, CUI X, SU J et al.: Increases in blood pressure with norepinephrine improve survival with LPS but not lethal toxin challenge in rats. Am. J. Resp. Crit. Care Med. (2007) 4:A39.
    • (2007) Am. J. Resp. Crit. Care Med , vol.4
    • LI, Y.1    CUI, X.2    SU, J.3
  • 77
    • 19944432972 scopus 로고    scopus 로고
    • A high-affinity monoclonal antibody to anthrax protective antigen passively protects rabbits before and after aerosolized Bacillus anthracis spore challenge
    • MOHAMED N, CLAGETT M, LI J et al.: A high-affinity monoclonal antibody to anthrax protective antigen passively protects rabbits before and after aerosolized Bacillus anthracis spore challenge. Infect. Immun. (2005) 73:795-802.
    • (2005) Infect. Immun , vol.73 , pp. 795-802
    • MOHAMED, N.1    CLAGETT, M.2    LI, J.3
  • 78
    • 31844451680 scopus 로고    scopus 로고
    • Human monoclonal anti-protective antigen antibody completely protects rabbits and is synergistic with ciprofloxacin in protecting mice and guinea pigs against inhalation anthrax
    • PETERSON JW, COMER JE, NOFFSINGER DM et al.: Human monoclonal anti-protective antigen antibody completely protects rabbits and is synergistic with ciprofloxacin in protecting mice and guinea pigs against inhalation anthrax. Infect. Immun. (2006) 74:1016-1024.
    • (2006) Infect. Immun , vol.74 , pp. 1016-1024
    • PETERSON, J.W.1    COMER, J.E.2    NOFFSINGER, D.M.3
  • 79
    • 20844461166 scopus 로고    scopus 로고
    • A Phase I study of PAmAb, a fully human monoclonal antibody against Bacillus anthracis protective antigen, in healthy volunteers
    • SUBRAMANIAN GM, CRONIN PW, POLEY G et al.: A Phase I study of PAmAb, a fully human monoclonal antibody against Bacillus anthracis protective antigen, in healthy volunteers. Clin. Infect. Dis. (2005) 41:12-20.
    • (2005) Clin. Infect. Dis , vol.41 , pp. 12-20
    • SUBRAMANIAN, G.M.1    CRONIN, P.W.2    POLEY, G.3
  • 80
    • 0035984720 scopus 로고    scopus 로고
    • Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity
    • MAYNARD JA, MAASSEN CBM, LEPPLA SH et al.: Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity. Nat. Biotechnol. (2002) 20:597-601.
    • (2002) Nat. Biotechnol , vol.20 , pp. 597-601
    • MAYNARD, J.A.1    MAASSEN, C.B.M.2    LEPPLA, S.H.3
  • 81
    • 33144486286 scopus 로고    scopus 로고
    • Efficient neutralization of anthrax toxin by chimpanzee monoclonal antibodies against protective antigen
    • CHEN Z, MOAYERI M, ZHOU Y et al.: Efficient neutralization of anthrax toxin by chimpanzee monoclonal antibodies against protective antigen. J. Infect. Dis. (2006) 193:625-633.
    • (2006) J. Infect. Dis , vol.193 , pp. 625-633
    • CHEN, Z.1    MOAYERI, M.2    ZHOU, Y.3
  • 82
    • 28444435513 scopus 로고    scopus 로고
    • Passive protection against anthrax by using a high-affinity antitoxin antibody fragment lacking an fc region
    • MABRY R, RANI M, GEIGER R et al.: Passive protection against anthrax by using a high-affinity antitoxin antibody fragment lacking an fc region. Infect. Immun. (2005) 73:8362-8368.
    • (2005) Infect. Immun , vol.73 , pp. 8362-8368
    • MABRY, R.1    RANI, M.2    GEIGER, R.3
  • 83
    • 4243151610 scopus 로고    scopus 로고
    • Human anti-anthrax protective antigen neutralizing monoclonal antibodies derived from donors vaccinated with anthrax vaccine adsorbed
    • SAWADA-HIRAI R, JIANG I, WANG F et al.: Human anti-anthrax protective antigen neutralizing monoclonal antibodies derived from donors vaccinated with anthrax vaccine adsorbed. J. Immune Based Ther. Vaccines (2004) 2:5.
    • (2004) J. Immune Based Ther. Vaccines , vol.2 , pp. 5
    • SAWADA-HIRAI, R.1    JIANG, I.2    WANG, F.3
  • 84
    • 0242290931 scopus 로고    scopus 로고
    • Human antibodies from immunized donors are protective against anthrax toxin in vivo
    • WILD MA, XIN H, MARUYAMA T et al.: Human antibodies from immunized donors are protective against anthrax toxin in vivo. Nat. Biotechnol. (2003) 21:1305-1306.
    • (2003) Nat. Biotechnol , vol.21 , pp. 1305-1306
    • WILD, M.A.1    XIN, H.2    MARUYAMA, T.3
  • 85
    • 33749244808 scopus 로고    scopus 로고
    • Prophylaxis and therapy of inhalational anthrax by a novel monoclonal antibody to protective antigen that mimics vaccine-induced immunity
    • VITALE L, BLANSET D, LOWY I et al.: Prophylaxis and therapy of inhalational anthrax by a novel monoclonal antibody to protective antigen that mimics vaccine-induced immunity. Infect. Immun. (2006) 74:5840-5847.
    • (2006) Infect. Immun , vol.74 , pp. 5840-5847
    • VITALE, L.1    BLANSET, D.2    LOWY, I.3
  • 86
    • 0035933746 scopus 로고    scopus 로고
    • A dominant-negative mutant of Bacillus anthracis protective antigen inhibits anthrax toxin in vivo
    • SINGH Y, KHANNA H, CHOPRA AP, MEHRA V: A dominant-negative mutant of Bacillus anthracis protective antigen inhibits anthrax toxin in vivo. J. Biol. Chem. (2001) 276:22090-22094.
    • (2001) J. Biol. Chem , vol.276 , pp. 22090-22094
    • SINGH, Y.1    KHANNA, H.2    CHOPRA, A.P.3    MEHRA, V.4
  • 87
    • 0035957753 scopus 로고    scopus 로고
    • Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax
    • SELLMAN BR, MOUREZ M, COLLIER RJ: Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science (2001) 292:695-697.
    • (2001) Science , vol.292 , pp. 695-697
    • SELLMAN, B.R.1    MOUREZ, M.2    COLLIER, R.J.3
  • 88
    • 33750601159 scopus 로고    scopus 로고
    • Search for cyclodextrin-based inhibitors of anthrax toxins: Synthesis, structural features, and relative activities
    • KARGINOV VA, NESTOROVICH EM, YOHANNES A et al.: Search for cyclodextrin-based inhibitors of anthrax toxins: synthesis, structural features, and relative activities. Antimicrob. Agents Chemother. (2006) 50:3740-3753.
    • (2006) Antimicrob. Agents Chemother , vol.50 , pp. 3740-3753
    • KARGINOV, V.A.1    NESTOROVICH, E.M.2    YOHANNES, A.3
  • 89
    • 33846026772 scopus 로고    scopus 로고
    • Inhibition of anthrax protective antigen outside and inside the cell
    • BACKER MV, PATEL V, JEHNING BT et al.: Inhibition of anthrax protective antigen outside and inside the cell. Antimicrob. Agents Chemother. (2007) 51:245-251.
    • (2007) Antimicrob. Agents Chemother , vol.51 , pp. 245-251
    • BACKER, M.V.1    PATEL, V.2    JEHNING, B.T.3
  • 90
    • 0346881395 scopus 로고    scopus 로고
    • Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo
    • SARAC MS, PEINADO JR, LEPPLA SH, LINDBERG I: Protection against anthrax toxemia by hexa-D-arginine in vitro and in vivo. Infect. Immun. (2004) 72:602-605.
    • (2004) Infect. Immun , vol.72 , pp. 602-605
    • SARAC, M.S.1    PEINADO, J.R.2    LEPPLA, S.H.3    LINDBERG, I.4
  • 91
    • 33845922116 scopus 로고    scopus 로고
    • Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine
    • JIAO GS, CREGAR L, WANG J et al.: Synthetic small molecule furin inhibitors derived from 2,5-dideoxystreptamine. Proc. Natl. Acad. Sci. USA (2006) 103:19707-19712.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19707-19712
    • JIAO, G.S.1    CREGAR, L.2    WANG, J.3
  • 93
    • 2442640131 scopus 로고    scopus 로고
    • Neutralizing monoclonal antibody against anthrax lethal factor inhibits intoxication in a mouse model
    • ZHAO P, LIANG X, KALBFLEISCH J et al.: Neutralizing monoclonal antibody against anthrax lethal factor inhibits intoxication in a mouse model. Hum. Antibodies (2003) 12:129-135.
    • (2003) Hum. Antibodies , vol.12 , pp. 129-135
    • ZHAO, P.1    LIANG, X.2    KALBFLEISCH, J.3
  • 94
    • 25444451322 scopus 로고    scopus 로고
    • An anthrax lethal factor-neutralizing monoclonal antibody protects rats before and after challenge with anthrax toxin
    • LIM N, KIM J, OH MS et al.: An anthrax lethal factor-neutralizing monoclonal antibody protects rats before and after challenge with anthrax toxin. Infect. Immun. (2005) 73:6547-6551.
    • (2005) Infect. Immun , vol.73 , pp. 6547-6551
    • LIM, N.1    KIM, J.2    OH, M.S.3
  • 95
    • 2542627454 scopus 로고    scopus 로고
    • Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor
    • MIN D, TANG W, MRKSICH M: Chemical screening by mass spectrometry to identify inhibitors of anthrax lethal factor. Nat. Biotechnol. (2004) 22:717-723.
    • (2004) Nat. Biotechnol , vol.22 , pp. 717-723
    • MIN, D.1    TANG, W.2    MRKSICH, M.3
  • 96
    • 10744223044 scopus 로고    scopus 로고
    • Identification of small molecule inhibitors of anthrax lethal factor
    • PANCHAL RG, HERMONE AR, NGUYEN TL et al.: Identification of small molecule inhibitors of anthrax lethal factor. Nat. Struct. Mol. Biol. (2004) 11:67-72.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 67-72
    • PANCHAL, R.G.1    HERMONE, A.R.2    NGUYEN, T.L.3
  • 97
    • 22144478634 scopus 로고    scopus 로고
    • Efficient synthetic inhibitors of anthrax lethal factor
    • FORINO M, JOHNSON S, WONG TY et al.: Efficient synthetic inhibitors of anthrax lethal factor. Proc. Natl. Acad. Sci. USA (2005) 102:9499-9504.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9499-9504
    • FORINO, M.1    JOHNSON, S.2    WONG, T.Y.3
  • 98
    • 2442478677 scopus 로고    scopus 로고
    • Potent inhibitors of anthrax lethal factor from green tea
    • DELLAICA I, DONA M, TONELLO F et al.: Potent inhibitors of anthrax lethal factor from green tea. EMBO Rep. (2004) 5:418-422.
    • (2004) EMBO Rep , vol.5 , pp. 418-422
    • DELLAICA, I.1    DONA, M.2    TONELLO, F.3
  • 99
    • 0034784582 scopus 로고    scopus 로고
    • Designing a polyvalent inhibitor of anthrax toxin
    • MOUREZ M, KANE RS, MOGRIDGE J et al.: Designing a polyvalent inhibitor of anthrax toxin. Nat. Biotechnol. (2001) 19:958-961.
    • (2001) Nat. Biotechnol , vol.19 , pp. 958-961
    • MOUREZ, M.1    KANE, R.S.2    MOGRIDGE, J.3
  • 100
    • 33748993435 scopus 로고    scopus 로고
    • Synthesis of potent inhibitors of anthrax toxin based on poly-L-glutamic acid
    • JOSHI A, SAARAPH A, POON V et al.: Synthesis of potent inhibitors of anthrax toxin based on poly-L-glutamic acid. Bioconjug. Chem. (2006) 17:1265-1269.
    • (2006) Bioconjug. Chem , vol.17 , pp. 1265-1269
    • JOSHI, A.1    SAARAPH, A.2    POON, V.3
  • 101
    • 33748601221 scopus 로고    scopus 로고
    • Polyvalent inhibitors of anthrax toxin that target host receptors
    • BASHA S, RAI P, POON V et al.: Polyvalent inhibitors of anthrax toxin that target host receptors. Proc. Natl. Acad. Sci. USA (2006) 103:13509-13513.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 13509-13513
    • BASHA, S.1    RAI, P.2    POON, V.3
  • 102
    • 33646593190 scopus 로고    scopus 로고
    • Statistical pattern matching facilitates the design of polyvalent inhibitors of anthrax and cholera toxins
    • RAI P, PADALA C, POON V et al.: Statistical pattern matching facilitates the design of polyvalent inhibitors of anthrax and cholera toxins. Nat. Biotechnol. (2006) 24:582-586.
    • (2006) Nat. Biotechnol , vol.24 , pp. 582-586
    • RAI, P.1    PADALA, C.2    POON, V.3
  • 103
    • 33745214233 scopus 로고    scopus 로고
    • Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides
    • KUZMIC P, CREGAR L, MILLIS SZ, GOLDMAN M: Mixed-type noncompetitive inhibition of anthrax lethal factor protease by aminoglycosides. FEBS J. (2006) 273:3054-3062.
    • (2006) FEBS J , vol.273 , pp. 3054-3062
    • KUZMIC, P.1    CREGAR, L.2    MILLIS, S.Z.3    GOLDMAN, M.4
  • 104
    • 33746411959 scopus 로고    scopus 로고
    • Cationic polyamines inhibit anthrax lethal factor protease
    • GOLDMAN ME, CREGAR L, NGUYEN D et al.: Cationic polyamines inhibit anthrax lethal factor protease. BMC Pharmacol. (2006) 6:8.
    • (2006) BMC Pharmacol , vol.6 , pp. 8
    • GOLDMAN, M.E.1    CREGAR, L.2    NGUYEN, D.3
  • 105
    • 33746434654 scopus 로고    scopus 로고
    • Selectively guanidinylated derivatives of neamine. Syntheses and inhibition of anthrax lethal factor protease
    • JIAO GS, SIMO O, NAGATA M et al.: Selectively guanidinylated derivatives of neamine. Syntheses and inhibition of anthrax lethal factor protease. Bioorg. Med. Chem. Lett. (2006) 16(19):5183-5189.
    • (2006) Bioorg. Med. Chem. Lett , vol.16 , Issue.19 , pp. 5183-5189
    • JIAO, G.S.1    SIMO, O.2    NAGATA, M.3
  • 107
    • 34250750569 scopus 로고    scopus 로고
    • Ultrastructural features of lymphocyte suppression induced by anthrax lethal toxin and treated with chloroquine
    • Dec 18: Epub ahead of print
    • HIRSH MI, MANOV I, COHEN-KAPLAN V, IANCU TC: Ultrastructural features of lymphocyte suppression induced by anthrax lethal toxin and treated with chloroquine. Lab. Invest. (2006) Dec 18: Epub ahead of print.
    • (2006) Lab. Invest
    • HIRSH, M.I.1    MANOV, I.2    COHEN-KAPLAN, V.3    IANCU, T.C.4
  • 108
    • 0037173617 scopus 로고    scopus 로고
    • Screening inhibitors of anthrax lethal factor
    • TONELLO F, SEVESO M, MARIN O et al.: Screening inhibitors of anthrax lethal factor. Nature (2002) 418:386.
    • (2002) Nature , vol.418 , pp. 386
    • TONELLO, F.1    SEVESO, M.2    MARIN, O.3
  • 109
    • 0347192782 scopus 로고    scopus 로고
    • The sttuctural basis for substrate and inhibitor selectivity of the anthrax lethal factor
    • TURK BE, WONG TY, SCHWARZENBACHER R et al.: The sttuctural basis for substrate and inhibitor selectivity of the anthrax lethal factor. Nat. Struct. Mol. Biol. (2004) 11:60-66.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 60-66
    • TURK, B.E.1    WONG, T.Y.2    SCHWARZENBACHER, R.3
  • 110
    • 1542327666 scopus 로고    scopus 로고
    • Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection
    • SHEN Y, ZHUKOVSKAYA NL, ZIMMER MI et al.: Selective inhibition of anthrax edema factor by adefovir, a drug for chronic hepatitis B virus infection. Proc. Natl. Acad. Sci. USA (2004) 101:3242-3247.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3242-3247
    • SHEN, Y.1    ZHUKOVSKAYA, N.L.2    ZIMMER, M.I.3
  • 111
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • SOELAIMAN S, WEI BQ, BERGSON P et al.: Structure-based inhibitor discovery against adenyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J. Biol. Chem. (2003) 278:25990-25997.
    • (2003) J. Biol. Chem , vol.278 , pp. 25990-25997
    • SOELAIMAN, S.1    WEI, B.Q.2    BERGSON, P.3
  • 112
    • 33947390946 scopus 로고    scopus 로고
    • A case of naturally acquired inhalation anthrax: Clinical care and analyses of anti-protective antigen immunoglobulin G and lethal factor
    • WALSH JL, PESIK N, QUINN CP et al.: A case of naturally acquired inhalation anthrax: clinical care and analyses of anti-protective antigen immunoglobulin G and lethal factor. CID (2007) 44:968-971.
    • (2007) CID , vol.44 , pp. 968-971
    • WALSH, J.L.1    PESIK, N.2    QUINN, C.P.3
  • 113
    • 34250757425 scopus 로고    scopus 로고
    • www.washingtonpost.com/wp-dyn/content/article/2006/06/19/ AR2006061901135_pf.html. Accessed August 10 (2006). ROSENWALD MS: US to buy anthrax treatment from HGS. Washington Post. June 20 (2006).
    • www.washingtonpost.com/wp-dyn/content/article/2006/06/19/ AR2006061901135_pf.html. Accessed August 10 (2006). ROSENWALD MS: US to buy anthrax treatment from HGS. Washington Post. June 20 (2006).
  • 114
    • 34250733779 scopus 로고    scopus 로고
    • Cangene Corp. Winnipeg, Manitoba
    • www.hhs.gov/news/press/2006pres/20060728.html-9k. Cangene Corp. Winnipeg, Manitoba.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.