메뉴 건너뛰기




Volumn 19, Issue , 2003, Pages 45-70

Anthrax Toxin

Author keywords

Endocytosis; Oligomer; Pore; Receptor; Translocation

Indexed keywords

ANTHRAX TOXIN; ANTIGEN;

EID: 0344825036     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.19.111301.140655     Document Type: Conference Paper
Times cited : (497)

References (123)
  • 1
    • 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, Leppla SH, Van Der Goot FG. 2003. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 160:321-28
    • (2003) J. Cell Biol. , vol.160 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    Van Der Goot, F.G.5
  • 2
    • 0021803919 scopus 로고
    • Crystallization of the protective antigen protein of Bacillus anthracis
    • Allured VS, Case LM, Leppla SH, McKay DB. 1985. Crystallization of the protective antigen protein of Bacillus anthracis. J. Biol. Chem. 260:5012-13
    • (1985) J. Biol. Chem. , vol.260 , pp. 5012-5013
    • Allured, V.S.1    Case, L.M.2    Leppla, S.H.3    McKay, D.B.4
  • 3
    • 0026741811 scopus 로고
    • Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells
    • Arora N, Klimpel KR, Singh Y, Leppla SH. 1992. Fusions of anthrax toxin lethal factor to the ADP-ribosylation domain of Pseudomonas exotoxin A are potent cytotoxins which are translocated to the cytosol of mammalian cells. J. Biol. Chem. 267:15542-48
    • (1992) J. Biol. Chem. , vol.267 , pp. 15542-15548
    • Arora, N.1    Klimpel, K.R.2    Singh, Y.3    Leppla, S.H.4
  • 4
    • 0027403919 scopus 로고
    • Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides
    • Arora N, Leppla SH. 1993. Residues 1-254 of anthrax toxin lethal factor are sufficient to cause cellular uptake of fused polypeptides. J. Biol. Chem. 268:3334-41
    • (1993) J. Biol. Chem. , vol.268 , pp. 3334-3341
    • Arora, N.1    Leppla, S.H.2
  • 5
    • 0027973442 scopus 로고
    • Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells
    • Arora N, Williamson LC, Leppla SH, Halpern JL. 1994. Cytotoxic effects of a chimeric protein consisting of tetanus toxin light chain and anthrax toxin lethal factor in non-neuronal cells. J. Biol. Chem. 269:26165-71
    • (1994) J. Biol. Chem. , vol.269 , pp. 26165-26171
    • Arora, N.1    Williamson, L.C.2    Leppla, S.H.3    Halpern, J.L.4
  • 7
    • 0029914034 scopus 로고    scopus 로고
    • Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo
    • Ballard JD, Collier RJ, Starnbach MN. 1996. Anthrax toxin-mediated delivery of a cytotoxic T-cell epitope in vivo. Proc. Natl. Acad. Sci. USA 93:12531-34
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12531-12534
    • Ballard, J.D.1    Collier, R.J.2    Starnbach, M.N.3
  • 8
    • 3543121118 scopus 로고    scopus 로고
    • Anthrax toxin as a molecular tool for stimulation of cytotoxic T lymphocytes: Disulfide-linked epitopes, multiple injections, and role of CD4(+) cells
    • Ballard JD, Collier RJ, Starnbach MN. 1998a. Anthrax toxin as a molecular tool for stimulation of cytotoxic T lymphocytes: disulfide-linked epitopes, multiple injections, and role of CD4(+) cells. Infect. Immun. 66:4696-99
    • (1998) Infect. Immun. , vol.66 , pp. 4696-4699
    • Ballard, J.D.1    Collier, R.J.2    Starnbach, M.N.3
  • 9
    • 0031932474 scopus 로고    scopus 로고
    • Anthrax toxin-mediated delivery in vivo and in vitro of a cytotoxic T-lymphocyte epitope from ovalbumin
    • Ballard JD, Doling AM, Beauregard K, Collier RJ, Starnbach MN. 1998b. Anthrax toxin-mediated delivery in vivo and in vitro of a cytotoxic T-lymphocyte epitope from ovalbumin. Infect. Immun. 66:615-19
    • (1998) Infect. Immun. , vol.66 , pp. 615-619
    • Ballard, J.D.1    Doling, A.M.2    Beauregard, K.3    Collier, R.J.4    Starnbach, M.N.5
  • 10
    • 0033868243 scopus 로고    scopus 로고
    • Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization
    • Beauregard KE, Collier RJ, Swanson JA. 2000. Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization. Cell. Microbiol. 2:251-58
    • (2000) Cell. Microbiol. , vol.2 , pp. 251-258
    • Beauregard, K.E.1    Collier, R.J.2    Swanson, J.A.3
  • 12
    • 0034870220 scopus 로고    scopus 로고
    • Differential gene expression during capillary morphogenesis in 3D collagen matrices: Regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling
    • Bell SE, Mavila A, Salazar R, Bayless KJ, Kanagala S, et al. 2001. Differential gene expression during capillary morphogenesis in 3D collagen matrices: regulated expression of genes involved in basement membrane matrix assembly, cell cycle progression, cellular differentiation and G-protein signaling. J. Cell Sci. 114:2755-73
    • (2001) J. Cell Sci. , vol.114 , pp. 2755-2773
    • Bell, S.E.1    Mavila, A.2    Salazar, R.3    Bayless, K.J.4    Kanagala, S.5
  • 13
    • 0032539990 scopus 로고    scopus 로고
    • Identification of residues lining the anthrax protective antigen channel
    • Benson EL, Huynh PD, Finkelstein A, Collier RJ. 1998. Identification of residues lining the anthrax protective antigen channel. Biochemistry 37:3941-48
    • (1998) Biochemistry , vol.37 , pp. 3941-3948
    • Benson, E.L.1    Huynh, P.D.2    Finkelstein, A.3    Collier, R.J.4
  • 14
    • 0028335856 scopus 로고
    • Protein synthesis is required for expression of anthrax lethal toxin cytotoxicity
    • Bhatnagar R, Friedlander AM. 1994. Protein synthesis is required for expression of anthrax lethal toxin cytotoxicity. Infect. Immun. 62:2958-62
    • (1994) Infect. Immun. , vol.62 , pp. 2958-2962
    • Bhatnagar, R.1    Friedlander, A.M.2
  • 15
    • 0029758834 scopus 로고    scopus 로고
    • Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen
    • Blanke SR, Milne JC, Benson EL, Collier RJ. 1996. Fused polycationic peptide mediates delivery of diphtheria toxin A chain to the cytosol in the presence of anthrax protective antigen. Proc. Natl. Acad. Sci. USA 93:8437-42
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8437-8442
    • Blanke, S.R.1    Milne, J.C.2    Benson, E.L.3    Collier, R.J.4
  • 16
    • 0025201667 scopus 로고
    • Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Effects on macroscopic conductance
    • Blaustein RO, Finkelstein A. 1990. Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Effects on macroscopic conductance. J. Gen. Physiol. 96:905-19
    • (1990) J. Gen. Physiol. , vol.96 , pp. 905-919
    • Blaustein, R.O.1    Finkelstein, A.2
  • 17
    • 0024523836 scopus 로고
    • Anthrax toxin: Channel-forming activity of protective antigen in planar phospholipid bilayers
    • Blaustein RO, Koehler TM, Collier RJ, Finkelstein A. 1989. Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers. Proc. Natl. Acad. Sci. USA 86:2209-13
    • (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
  • 18
    • 0025225339 scopus 로고
    • Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis
    • Blaustein RO, Lea EJ, Finkelstein A. 1990. Voltage-dependent block of anthrax toxin channels in planar phospholipid bilayer membranes by symmetric tetraalkylammonium ions. Single-channel analysis. J. Gen. Physiol. 96:921-42
    • (1990) J. Gen. Physiol. , vol.96 , pp. 921-942
    • Blaustein, R.O.1    Lea, E.J.2    Finkelstein, A.3
  • 20
    • 0032940151 scopus 로고    scopus 로고
    • Functional analysis of the carboxy-terminal domain of Bacillus anthracis protective antigen
    • Brossier F, Sirard JC, Guidi-Rontani C, Duflot E, Mock M. 1999. Functional analysis of the carboxy-terminal domain of Bacillus anthracis protective antigen. Infect. Immun. 67:964-67
    • (1999) Infect. Immun. , vol.67 , pp. 964-967
    • Brossier, F.1    Sirard, J.C.2    Guidi-Rontani, C.3    Duflot, E.4    Mock, M.5
  • 22
    • 0035206185 scopus 로고    scopus 로고
    • ADP-ribosylating binary toxin genes of Clostridium difficile strain CCUG 20309
    • Chang SY, Song KP. 2001. ADP-ribosylating binary toxin genes of Clostridium difficile strain CCUG 20309. DNA Seq. 12:115-20
    • (2001) DNA Seq. , vol.12 , pp. 115-120
    • Chang, S.Y.1    Song, K.P.2
  • 23
    • 0025913370 scopus 로고
    • Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity
    • Considine RV, Simpson LL. 1991. Cellular and molecular actions of binary toxins possessing ADP-ribosyltransferase activity. Toxicon 29:913-36
    • (1991) Toxicon , vol.29 , pp. 913-936
    • Considine, R.V.1    Simpson, L.L.2
  • 24
    • 0037076304 scopus 로고    scopus 로고
    • Mapping the lethal factor and edema factor binding sites on oligomeric anthrax protective antigen
    • Cunningham K, Lacy DB, Mogridge J, Collier RJ. 2002. Mapping the lethal factor and edema factor binding sites on oligomeric anthrax protective antigen. Proc. Natl. Acad. Sci. USA 99:7049-53
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7049-7053
    • Cunningham, K.1    Lacy, D.B.2    Mogridge, J.3    Collier, R.J.4
  • 25
    • 0037076271 scopus 로고    scopus 로고
    • A peptide-based fluorescence resonance energy transfer assay for Bacillus anthracis lethal factor protease
    • Cummings RT, Salowe SP, Cunningham BR, Wiltsie J, Park YW, et al. 2002. A peptide-based fluorescence resonance energy transfer assay for Bacillus anthracis lethal factor protease. Proc. Natl. Acad. Sci. USA 99:6603-6
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6603-6606
    • Cummings, R.T.1    Salowe, S.P.2    Cunningham, B.R.3    Wiltsie, J.4    Park, Y.W.5
  • 26
    • 0033041377 scopus 로고    scopus 로고
    • Cytotoxic T-lymphocyte epitopes fused to anthrax toxin induce protective antiviral immunity
    • Doling AM, Ballard JD, Shen H, Krishna KM, Ahmed R, et al. 1999. Cytotoxic T-lymphocyte epitopes fused to anthrax toxin induce protective antiviral immunity. Infect. Immun. 67:3290-96
    • (1999) Infect. Immun. , vol.67 , pp. 3290-3296
    • Doling, A.M.1    Ballard, J.D.2    Shen, H.3    Krishna, K.M.4    Ahmed, R.5
  • 27
    • 0037165139 scopus 로고    scopus 로고
    • Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin
    • Drum CL, Yan SZ, Bard J, Shen YQ, Lu D, et al. 2002. Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415:396-402
    • (2002) Nature , vol.415 , pp. 396-402
    • Drum, C.L.1    Yan, S.Z.2    Bard, J.3    Shen, Y.Q.4    Lu, D.5
  • 28
    • 0035957358 scopus 로고    scopus 로고
    • Suppression of ras-mediated transformation and inhibition of tumor growth and angiogenesis by anthrax lethal factor, a proteolytic inhibitor of multiple MEK pathways
    • Duesbery NS, Webb CP, Koochekpour S, Koo HM, et al. 2001. Suppression of 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 98:4089-94
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4089-4094
    • Duesbery, N.S.1    Webb, C.P.2    Koochekpour, S.3    Koo, H.M.4
  • 29
    • 18244414803 scopus 로고    scopus 로고
    • Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
    • Duesbery NS, Webb CP, Leppla SH, Gordon VM, Klimpel KR, et al. 1998. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280:734-37
    • (1998) Science , vol.280 , pp. 734-737
    • Duesbery, N.S.1    Webb, C.P.2    Leppla, S.H.3    Gordon, V.M.4    Klimpel, K.R.5
  • 30
    • 0034612326 scopus 로고    scopus 로고
    • A quantitative study of the interactions of Bacillus anthracis edema factor and lethal factor with activated protective antigen
    • Elliott JL, Mogridge J, Collier RJ. 2000. A quantitative study of the interactions of Bacillus anthracis edema factor and lethal factor with activated protective antigen. Biochemistry 39:6706-13
    • (2000) Biochemistry , vol.39 , pp. 6706-6713
    • Elliott, J.L.1    Mogridge, J.2    Collier, R.J.3
  • 31
    • 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, Little SF, Friedlander AM, Chanh TC. 2001. Macrophage-derived cell lines do not express proinflammatory cytokines after exposure to Bacillus anthracis lethal toxin. Infect. Immun. 69:1175-77
    • (2001) Infect. Immun. , vol.69 , pp. 1175-1177
    • Erwin, J.L.1    DaSilva, L.M.2    Bavari, S.3    Little, S.F.4    Friedlander, A.M.5    Chanh, T.C.6
  • 32
    • 0026587409 scopus 로고
    • Serum protease cleavage of Bacillus anthracis protective antigen
    • Ezzell JW Jr, Abshire TG. 1992. Serum protease cleavage of Bacillus anthracis protective antigen. J. Gen. Microbiol. 138 (Pt 3): 543-49
    • (1992) J. Gen. Microbiol. , vol.138 , Issue.3 PART , pp. 543-549
    • Ezzell Jr., J.W.1    Abshire, T.G.2
  • 34
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process
    • Friedlander AM. 1986. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261:7123-26
    • (1986) J. Biol. Chem. , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 36
  • 38
    • 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, Henderson MA, Leppla SH. 1995. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 63:82-87
    • (1995) Infect. Immun. , vol.63 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3    Henderson, M.A.4    Leppla, S.H.5
  • 39
    • 0023932170 scopus 로고
    • Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetellapertussis adenylate cyclase toxin
    • Gordon VM, Leppla SH, Hewlett EL. 1988. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetellapertussis adenylate cyclase toxin. Infect. Immun. 56:1066-69
    • (1988) Infect. Immun. , vol.56 , pp. 1066-1069
    • Gordon, V.M.1    Leppla, S.H.2    Hewlett, E.L.3
  • 42
    • 0033866471 scopus 로고    scopus 로고
    • Translocation of Bacillus anthracis lethal and oedema factors across endosome membranes
    • Guidi-Rontani C, Weber-Levy M, Mock M, Cabiaux V. 2000. Translocation of Bacillus anthracis lethal and oedema factors across endosome membranes. Cell. Microbiol. 2:259-64
    • (2000) Cell. Microbiol. , vol.2 , pp. 259-264
    • Guidi-Rontani, C.1    Weber-Levy, M.2    Mock, M.3    Cabiaux, V.4
  • 44
    • 0027097608 scopus 로고
    • Biochemical and physiological changes induced by anthrax lethal toxin in J774 macrophage-like cells
    • Hanna PC, Kochi S, Collier RJ. 1992. Biochemical and physiological changes induced by anthrax lethal toxin in J774 macrophage-like cells. Mol. Biol. Cell 3:1269-77
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1269-1277
    • Hanna, P.C.1    Kochi, S.2    Collier, R.J.3
  • 46
    • 0345570658 scopus 로고
    • Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: Relevance to translocation of proteins across membranes
    • Hoch DH, Romero Mira M, Ehrlich BE, Finkelstein A, DasGupta BR, Simpson LL. 1985. Channels formed by botulinum, tetanus, and diphtheria toxins in planar lipid bilayers: relevance to translocation of proteins across membranes. Proc. Natl. Acad. Sci. USA 82: 1692-96
    • (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
  • 47
    • 0019819794 scopus 로고
    • Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes
    • Kagan BL, Finkelstein A, Colombini M. 1981. Diphtheria toxin fragment forms large pores in phospholipid bilayer membranes. Proc. Natl. Acad. Sci. USA 78:4950-54
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4950-4954
    • Kagan, B.L.1    Finkelstein, A.2    Colombini, M.3
  • 48
  • 49
    • 85025049366 scopus 로고
    • Anthrax toxin lethal factor has homology to the thermolysin-like proteases and displays protease activity
    • Klimpel KR, Arora N, Leppla SH. 1993. Anthrax toxin lethal factor has homology to the thermolysin-like proteases and displays protease activity. Abstr. Am. Soc. Microbiol. Annu. Meet. p. 45
    • (1993) Abstr. Am. Soc. Microbiol. Annu. Meet. , pp. 45
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 50
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • Klimpel KR, Molloy SS, Thomas G, Leppla SH. 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 89:10277-81
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10277-10281
    • Klimpel, K.R.1    Molloy, S.S.2    Thomas, G.3    Leppla, S.H.4
  • 51
    • 0028334918 scopus 로고
    • The effects of pH on the interaction of anthrax toxin lethal and edema factors with phospholipid vesicles
    • Kochi SK, Martin I, Schiavo G, Mock M, Cabiaux V. 1994. The effects of pH on the interaction of anthrax toxin lethal and edema factors with phospholipid vesicles. Biochemistry 33:2604-9
    • (1994) Biochemistry , vol.33 , pp. 2604-2609
    • Kochi, S.K.1    Martin, I.2    Schiavo, G.3    Mock, M.4    Cabiaux, V.5
  • 52
    • 0345582809 scopus 로고    scopus 로고
    • New York: Springer
    • Koehler TM, ed. 2002. Anthrax. New York: Springer. Vol. 271
    • (2002) Anthrax , vol.271
    • Koehler, T.M.1
  • 53
    • 0025771545 scopus 로고
    • Anthrax toxin protective antigen: Low-pH-induced hydrophobicity and channel formation in liposomes
    • Koehler TM, Collier RJ. 1991. Anthrax toxin protective antigen: low-pH-induced hydrophobicity and channel formation in liposomes. Mol. Microbiol. 5:1501-6
    • (1991) Mol. Microbiol. , vol.5 , pp. 1501-1506
    • Koehler, T.M.1    Collier, R.J.2
  • 54
    • 0037022666 scopus 로고    scopus 로고
    • Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase
    • Koo HM, VanBrocklin M, McWilliams MJ, Leppla SH, Duesbery NS, Woude GF. 2002. Apoptosis and melanogenesis in human melanoma cells induced by anthrax lethal factor inactivation of mitogen-activated protein kinase kinase. Proc. Natl. Acad. Sci. USA 99:3052-57
    • (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
  • 56
    • 0037169549 scopus 로고    scopus 로고
    • Mapping the anthrax protective antigen binding site on the lethal and edema factors
    • Lacy DB, Mourez M, Fouassier A, Collier RJ. 2002. Mapping the anthrax protective antigen binding site on the lethal and edema factors. J. Biol. Chem. 277:3006-10
    • (2002) J. Biol. Chem. , vol.277 , pp. 3006-3010
    • Lacy, D.B.1    Mourez, M.2    Fouassier, A.3    Collier, R.J.4
  • 58
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla SH. 1982. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. USA 79:3162-66
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 59
    • 0021314377 scopus 로고
    • Bacillus anthracis calmodulin-dependent adenylate cyclase: Chemical and enzymatic properties and interactions with eucaryotic cells
    • Leppla SH. 1984. Bacillus anthracis calmodulin-dependent adenylate cyclase: chemical and enzymatic properties and interactions with eucaryotic cells. Adv. Cyclic Nucleotide Protein Phosphorylation Res. 17:189-98
    • (1984) Adv. Cyclic Nucleotide Protein Phosphorylation Res. , vol.17 , pp. 189-198
    • Leppla, S.H.1
  • 60
    • 0002661972 scopus 로고
    • The anthrax toxin complex
    • ed. J Alouf, New York: Academic
    • Leppla SH. 1991. The anthrax toxin complex. In Sourcebook of Bacterial Protein Toxins, ed. J Alouf, pp. 277-302. New York: Academic
    • (1991) Sourcebook of Bacterial Protein Toxins , pp. 277-302
    • Leppla, S.H.1
  • 61
    • 0001256478 scopus 로고    scopus 로고
    • Anthrax toxin
    • ed. K Aktories, I Just, Berlin: Springer
    • Leppla SH. 2000. Anthrax toxin. In Bacterial Protein Toxins, ed. K Aktories, I Just, pp. 445-72. Berlin: Springer
    • (2000) Bacterial Protein Toxins , pp. 445-472
    • Leppla, S.H.1
  • 63
    • 0023895994 scopus 로고
    • Production and characterization of monoclonal antibodies to the protective antigen component of Bacillus anthracis toxin
    • Little SF, Leppla SH, Cora E. 1988. Production and characterization of monoclonal antibodies to the protective antigen component of Bacillus anthracis toxin. Infect. Immun. 56:1807-13
    • (1988) Infect. Immun. , vol.56 , pp. 1807-1813
    • Little, S.F.1    Leppla, S.H.2    Cora, E.3
  • 64
    • 0025290784 scopus 로고
    • Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin
    • Little SF, Leppla SH, Friedlander AM. 1990. Production and characterization of monoclonal antibodies against the lethal factor component of Bacillus anthracis lethal toxin. Infect. Immun. 58:1606-13
    • (1990) Infect. Immun. , vol.58 , pp. 1606-1613
    • Little, S.F.1    Leppla, S.H.2    Friedlander, A.M.3
  • 65
    • 0029958827 scopus 로고    scopus 로고
    • Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies
    • Little SF, Novak JM, Lowe JR, Leppla SH, Singh Y, et al. 1996. Characterization of lethal factor binding and cell receptor binding domains of protective antigen of Bacillus anthracis using monoclonal antibodies. Microbiology 142:707-15
    • (1996) Microbiology , vol.142 , pp. 707-715
    • Little, S.F.1    Novak, J.M.2    Lowe, J.R.3    Leppla, S.H.4    Singh, Y.5
  • 66
    • 0013159236 scopus 로고    scopus 로고
    • Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization
    • Liu S, Leppla SH. 2002. Cell surface tumor endothelium marker 8 cytoplasmic tail-independent anthrax toxin binding, proteolytic processing, oligomer formation, and internalization. J. Biol. Chem. 278:5227-34
    • (2002) J. Biol. Chem. , vol.278 , pp. 5227-5234
    • Liu, S.1    Leppla, S.H.2
  • 67
    • 0034608874 scopus 로고    scopus 로고
    • Genetically modified anthrax lethal toxin safely delivers whole HIV protein antigens into the cytosol to induce T cell immunity
    • Lu Y, Friedman R, Kushner N, Doling A, Thomas L, et al. 2000. Genetically modified anthrax lethal toxin safely delivers whole HIV protein antigens into the cytosol to induce T cell immunity. Proc. Natl. Acad. Sci. USA 97:8027-32
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8027-8032
    • Lu, Y.1    Friedman, R.2    Kushner, N.3    Doling, A.4    Thomas, L.5
  • 68
    • 0035984720 scopus 로고    scopus 로고
    • Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity
    • Maynard JA, Maassen CB, Leppla SH, Brasky K, Patterson JL, et al. 2002. Protection against anthrax toxin by recombinant antibody fragments correlates with antigen affinity. Nat. Biotechnol. 20:597-601
    • (2002) Nat. Biotechnol. , vol.20 , pp. 597-601
    • Maynard, J.A.1    Maassen, C.B.2    Leppla, S.H.3    Brasky, K.4    Patterson, J.L.5
  • 69
    • 2542509040 scopus 로고    scopus 로고
    • The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin
    • Menard A, Altendorf K, Breves D, Mock M, Montecucco C. 1996. The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin. FEBS Lett. 386:161-64
    • (1996) FEBS Lett. , vol.386 , pp. 161-164
    • Menard, A.1    Altendorf, K.2    Breves, D.3    Mock, M.4    Montecucco, C.5
  • 70
    • 0033543208 scopus 로고    scopus 로고
    • Anthrax protective antigen: Prepore-to-pore conversion
    • Miller CJ, Elliott JL, Collier RJ. 1999. Anthrax protective antigen: prepore-to-pore conversion. Biochemistry 38:10432-41
    • (1999) Biochemistry , vol.38 , pp. 10432-10441
    • Miller, C.J.1    Elliott, J.L.2    Collier, R.J.3
  • 71
    • 0027443262 scopus 로고
    • pH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen
    • Milne JC, Collier RJ. 1993. pH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen. Mol. Microbiol. 10:647-53
    • (1993) Mol. Microbiol. , vol.10 , pp. 647-653
    • Milne, J.C.1    Collier, R.J.2
  • 72
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne JC, Furlong D, Hanna PC, Wall JS, Collier RJ. 1994. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269:20607-12
    • (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
  • 75
    • 0037076364 scopus 로고    scopus 로고
    • The lethal and edema factors of anthrax toxin bind only to oligomeric forms of the protective antigen
    • Mogridge J, Cunningham K, Lacy DB, Mourez M, Collier RJ. 2002b. The lethal and edema factors of anthrax toxin bind only to oligomeric forms of the protective antigen. Proc. Natl. Acad. Sci. USA 99:7045-48
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7045-7048
    • Mogridge, J.1    Cunningham, K.2    Lacy, D.B.3    Mourez, M.4    Collier, R.J.5
  • 76
    • 0035097284 scopus 로고    scopus 로고
    • Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin
    • Mogridge J, Mourez M, Collier RJ. 2001. Involvement of domain 3 in oligomerization by the protective antigen moiety of anthrax toxin. J. Bacteriol. 183:2111-16
    • (2001) J. Bacteriol. , vol.183 , pp. 2111-2116
    • Mogridge, J.1    Mourez, M.2    Collier, R.J.3
  • 77
    • 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 SS, Bresnahan PA, Leppla SH, Klimpel KR, Thomas G. 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. 267:16396-402
    • (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
  • 78
    • 0035852316 scopus 로고    scopus 로고
    • Induction of hepatitis C virus-specific cytotoxic T lymphocytes in mice by immunization with dendritic cells treated with an anthrax toxin fusion protein
    • Moriya O, Matsui M, Osorio M, Miyazawa H, Rice CM, et al. 2001. Induction of hepatitis C virus-specific cytotoxic T lymphocytes in mice by immunization with dendritic cells treated with an anthrax toxin fusion protein. Vaccine 20:789-96
    • (2001) Vaccine , vol.20 , pp. 789-796
    • Moriya, O.1    Matsui, M.2    Osorio, M.3    Miyazawa, H.4    Rice, C.M.5
  • 81
    • 0037022118 scopus 로고    scopus 로고
    • PA63 channel of anthrax toxin: An extended beta-barrel
    • Nassi S, Collier RJ, Finkelstein A. 2002. PA63 channel of anthrax toxin: an extended beta-barrel. Biochemistry 41:1445-50
    • (2002) Biochemistry , vol.41 , pp. 1445-1450
    • Nassi, S.1    Collier, R.J.2    Finkelstein, A.3
  • 82
    • 0026794750 scopus 로고
    • Functional characterization of protease-treated Bacillus anthracis protective antigen
    • Novak JM, Stein MP, Little SF, Leppla SH, Friedlander AM. 1992. Functional characterization of protease-treated Bacillus anthracis protective antigen. J. Biol. Chem. 267:17186-93
    • (1992) J. Biol. Chem. , vol.267 , pp. 17186-17193
    • Novak, J.M.1    Stein, M.P.2    Little, S.F.3    Leppla, S.H.4    Friedlander, A.M.5
  • 83
    • 0029937852 scopus 로고    scopus 로고
    • Hybrid proteins between Pseudomonas aeruginosa exotoxin A and poliovirus 2Apro cleave p220 in HeLa cells
    • Novoa I, Cotten M, Carrasco L. 1996. Hybrid proteins between Pseudomonas aeruginosa exotoxin A and poliovirus 2Apro cleave p220 in HeLa cells. J. Virol. 70:3319-24
    • (1996) J. Virol. , vol.70 , pp. 3319-3324
    • Novoa, I.1    Cotten, M.2    Carrasco, L.3
  • 85
    • 0026721947 scopus 로고
    • pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349-Lys
    • O'Keefe DO, Cabiaux V, Choe S, Eisenberg D, Collier RJ. 1992. pH-dependent insertion of proteins into membranes: B-chain mutation of diphtheria toxin that inhibits membrane translocation, Glu-349-Lys. Proc. Natl. Acad. Sci. USA 89:6202-6
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6202-6206
    • O'Keefe, D.O.1    Cabiaux, V.2    Choe, S.3    Eisenberg, D.4    Collier, R.J.5
  • 86
    • 0032717290 scopus 로고    scopus 로고
    • Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes
    • Okinaka RT, Cloud K, Hampton O, Hoffmaster AR, Hill KK, et al. 1999. Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes. J. Bacteriol. 181:6509-15
    • (1999) J. Bacteriol. , vol.181 , pp. 6509-6515
    • Okinaka, R.T.1    Cloud, K.2    Hampton, O.3    Hoffmaster, A.R.4    Hill, K.K.5
  • 88
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park JM, Greten FR, Li ZW, Karin M. 2002. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297:2048-51
    • (2002) Science , vol.297 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3    Karin, M.4
  • 89
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNFalpha
    • Pellizzari R, Guidi-Rontani C, Vitale G, Mock M, Montecucco C. 1999. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFNgamma-induced release of NO and TNFalpha. FEBS Lett. 462:199-204
    • (1999) FEBS Lett. , vol.462 , pp. 199-204
    • Pellizzari, R.1    Guidi-Rontani, C.2    Vitale, G.3    Mock, M.4    Montecucco, C.5
  • 91
    • 0023942902 scopus 로고
    • Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin
    • Popoff MR, Boquet P. 1988. Clostridium spiroforme toxin is a binary toxin which ADP-ribosylates cellular actin. Biochem. Biophys. Res. Commun. 152:1361-68
    • (1988) Biochem. Biophys. Res. Commun. , vol.152 , pp. 1361-1368
    • Popoff, M.R.1    Boquet, P.2
  • 92
    • 0345668477 scopus 로고    scopus 로고
    • The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex
    • Ratts R, Zeng H, Berg EA, Blue C, McComb ME, et al. 2003. The cytosolic entry of diphtheria toxin catalytic domain requires a host cell cytosolic translocation factor complex. J. Cell. Biol. 160:1139-50
    • (2003) J. Cell. Biol. , vol.160 , pp. 1139-1150
    • Ratts, R.1    Zeng, H.2    Berg, E.A.3    Blue, C.4    McComb, M.E.5
  • 93
    • 0031875676 scopus 로고    scopus 로고
    • Ltx1, a mouse locus that influences the susceptibility of macrophages to cytolysis caused by intoxication with Bacillus anthracis lethal factor, maps to chromosome 11
    • Roberts JE, Watters JW, Ballard JD, Dietrich WF. 1998. Ltx1, a mouse locus that influences the susceptibility of macrophages to cytolysis caused by intoxication with Bacillus anthracis lethal factor, maps to chromosome 11. Mol. Microbiol. 29:581-91
    • (1998) Mol. Microbiol. , vol.29 , pp. 581-591
    • Roberts, J.E.1    Watters, J.W.2    Ballard, J.D.3    Dietrich, W.F.4
  • 96
    • 0035957753 scopus 로고    scopus 로고
    • Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax
    • Sellman BR, Mourez M, Collier RJ. 2001a. Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science 292:695-97
    • (2001) Science , vol.292 , pp. 695-697
    • Sellman, B.R.1    Mourez, M.2    Collier, R.J.3
  • 97
    • 0035896616 scopus 로고    scopus 로고
    • Point mutations in anthrax protective antigen that block translocation
    • Sellman BR, Nassi S, Collier RJ. 2001b. Point mutations in anthrax protective antigen that block translocation. J. Biol. Chem. 276:8371-76
    • (2001) J. Biol. Chem. , vol.276 , pp. 8371-8376
    • Sellman, B.R.1    Nassi, S.2    Collier, R.J.3
  • 98
    • 12244306922 scopus 로고    scopus 로고
    • Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins
    • Shen Y, Lee YS, Soelaiman S, Bergson P, Lu D, et al. 2002. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. EMBO J. 21:6721-32
    • (2002) EMBO J. , vol.21 , pp. 6721-6732
    • Shen, Y.1    Lee, Y.S.2    Soelaiman, S.3    Bergson, P.4    Lu, D.5
  • 100
    • 0027989890 scopus 로고
    • Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain
    • Silverman JA, Mindell JA, Finkelstein A, Shen WH, Collier RJ. 1994. Mutational analysis of the helical hairpin region of diphtheria toxin transmembrane domain. J. Biol. Chem. 269:22542-32
    • (1994) J. Biol. Chem. , vol.269 , pp. 22542-22632
    • Silverman, J.A.1    Mindell, J.A.2    Finkelstein, A.3    Shen, W.H.4    Collier, R.J.5
  • 101
    • 0024846136 scopus 로고
    • The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects
    • Simpson LI. 1989. The binary toxin produced by Clostridium botulinum enters cells by receptor-mediated endocytosis to exert its pharmacologic effects. J. Pharmacol. Exp. Ther. 251:1223-28
    • (1989) J. Pharmacol. Exp. Ther. , vol.251 , pp. 1223-1228
    • Simpson, L.I.1
  • 102
    • 0035933746 scopus 로고    scopus 로고
    • A dominant negative mutant of Bacillus anthracis protective antigen inhibits anthrax toxin action in vivo
    • Singh Y, Khanna H, Chopra AP, Mehra V. 2001. A dominant negative mutant of Bacillus anthracis protective antigen inhibits anthrax toxin action in vivo. J. Biol. Chem. 276:22090-94
    • (2001) J. Biol. Chem. , vol.276 , pp. 22090-22094
    • Singh, Y.1    Khanna, H.2    Chopra, A.P.3    Mehra, V.4
  • 103
    • 0028172211 scopus 로고
    • The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective antigen is required for translocation of lethal factor
    • Singh Y, Klimpel KR, Arora N, Sharma M, Leppla SH. 1994. The chymotrypsin-sensitive site, FFD315, in anthrax toxin protective antigen is required for translocation of lethal factor. J. Biol. Chem. 269:29039-46
    • (1994) J. Biol. Chem. , vol.269 , pp. 29039-29046
    • Singh, Y.1    Klimpel, K.R.2    Arora, N.3    Sharma, M.4    Leppla, S.H.5
  • 104
    • 0033066901 scopus 로고    scopus 로고
    • Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells
    • Singh Y, Klimpel KR, Goel S, Swain PK, Leppla SH. 1999. Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells. Infect. Immun. 67:1853-59
    • (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
  • 105
    • 0025858389 scopus 로고
    • The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity
    • Singh Y, Klimpel KR, Quinn CP, Chaudhary VK, Leppla SH. 1991. The carboxyl-terminal end of protective antigen is required for receptor binding and anthrax toxin activity. J. Biol Chem. 266:15493-97
    • (1991) J. Biol Chem. , vol.266 , pp. 15493-15497
    • Singh, Y.1    Klimpel, K.R.2    Quinn, C.P.3    Chaudhary, V.K.4    Leppla, S.H.5
  • 106
    • 0034193183 scopus 로고    scopus 로고
    • Discovery of the anthrax toxin: The beginning of in vivo studies on pathogenic bacteria
    • Smith H. 2000. Discovery of the anthrax toxin: the beginning of in vivo studies on pathogenic bacteria. Trends Microbiol. 8: 199-200
    • (2000) Trends Microbiol. , vol.8 , pp. 199-200
    • Smith, H.1
  • 107
    • 0014127332 scopus 로고
    • Anthrax toxic complex
    • Smith H, Stoner HB. 1967. Anthrax toxic complex. Fed. Proc. 26:1554-57
    • (1967) Fed. Proc. , vol.26 , pp. 1554-1557
    • Smith, H.1    Stoner, H.B.2
  • 108
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L, Hobaugh MR, Shustak C, Cheley S, Bayley H, Gouaux JE. 1996. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 274: 1859-66
    • (1996) Science , vol.274 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 110
    • 0033056295 scopus 로고    scopus 로고
    • Proteasome activity is required for anthrax lethal toxin to kill macrophages
    • Tang G, Leppla SH. 1999. Proteasome activity is required for anthrax lethal toxin to kill macrophages. Infect. Immun. 67:3055-60
    • (1999) Infect. Immun. , vol.67 , pp. 3055-3060
    • Tang, G.1    Leppla, S.H.2
  • 112
    • 0036022854 scopus 로고    scopus 로고
    • Introduction: Anthrax history, disease and ecology
    • Turnbull PC. 2002. Introduction: anthrax history, disease and ecology. Curr. Top. Microbiol. Immunol. 271:1-19
    • (2002) Curr. Top. Microbiol. Immunol. , vol.271 , pp. 1-19
    • Turnbull, P.C.1
  • 113
    • 0030632048 scopus 로고    scopus 로고
    • The N-end rule pathway of protein degradation
    • Varshavsky A. 1997. The N-end rule pathway of protein degradation. Genes Cells 2:13-28
    • (1997) Genes Cells , vol.2 , pp. 13-28
    • Varshavsky, A.1
  • 114
    • 0033064418 scopus 로고    scopus 로고
    • Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin
    • Varughese M, Teixeira AV, Liu S, Leppla SH. 1999. Identification of a receptor-binding region within domain 4 of the protective antigen component of anthrax toxin. Infect. Immun. 67:1860-65
    • (1999) Infect. Immun. , vol.67 , pp. 1860-1865
    • Varughese, M.1    Teixeira, A.V.2    Liu, S.3    Leppla, S.H.4
  • 115
    • 0032581369 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages
    • Vitale G, Pellizzari R, Recchi C, Napolitani G, Mock M, Montecucco C. 1998. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:706-11
    • (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
  • 116
    • 0029125825 scopus 로고
    • Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification
    • Walker B, Bayley H. 1995. Key residues for membrane binding, oligomerization, and pore forming activity of staphylococcal alpha-hemolysin identified by cysteine scanning mutagenesis and targeted chemical modification. J. Biol. Chem. 270:23065-71
    • (1995) J. Biol. Chem. , vol.270 , pp. 23065-23071
    • Walker, B.1    Bayley, H.2
  • 117
    • 0030458792 scopus 로고    scopus 로고
    • Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: A Fourier-transform infrared spectroscopy approach
    • Wang XM, Mock M, Ruysschaert JM, Cabiaux V. 1996. Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: a Fourier-transform infrared spectroscopy approach. Biochemistry 35:14939-46
    • (1996) Biochemistry , vol.35 , pp. 14939-14946
    • Wang, X.M.1    Mock, M.2    Ruysschaert, J.M.3    Cabiaux, V.4
  • 118
    • 0035797887 scopus 로고    scopus 로고
    • Kif1C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor
    • Watters JW, Dewar K, Lehoczky J, Boyartchuk V, Dietrich WF. 2001. Kif1C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor. Curr. Biol. 11:1503-11
    • (2001) Curr. Biol. , vol.11 , pp. 1503-1511
    • Watters, J.W.1    Dewar, K.2    Lehoczky, J.3    Boyartchuk, V.4    Dietrich, W.F.5
  • 119
    • 0035870628 scopus 로고    scopus 로고
    • Genetic, physical, and transcript map of the Ltxs1 region of mouse chromosome 11
    • Watters JW, Dietrich WF. 2001. Genetic, physical, and transcript map of the Ltxs1 region of mouse chromosome 11. Genomics 73:223-31
    • (2001) Genomics , vol.73 , pp. 223-231
    • Watters, J.W.1    Dietrich, W.F.2
  • 120
    • 0032506245 scopus 로고    scopus 로고
    • Characterization of membrane translocation by anthrax protective antigen
    • Wesche J, Elliott JL, Falnes PO, Olsnes S, Collier RJ. 1998. Characterization of membrane translocation by anthrax protective antigen. Biochemistry 37:15737-46
    • (1998) Biochemistry , vol.37 , pp. 15737-15746
    • Wesche, J.1    Elliott, J.L.2    Falnes, P.O.3    Olsnes, S.4    Collier, R.J.5
  • 121
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin a domains: Widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker CA, Hynes RO. 2002. Distribution and evolution of von Willebrand/integrin a domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 13:3369-87
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 122
    • 0037868151 scopus 로고    scopus 로고
    • Characterization of dominant-negative forms of anthrax protective antigen
    • Yan M, Collier RJ. 2003. Characterization of dominant-negative forms of anthrax protective antigen. Mol. Med. 9:46-51
    • (2003) Mol. Med. , vol.9 , pp. 46-51
    • Yan, M.1    Collier, R.J.2
  • 123
    • 0029162979 scopus 로고
    • Effect of anthrax toxin's lethal factor on ion channels formed by the protective antigen
    • Zhao J, Milne JC, Collier RJ. 1995. Effect of anthrax toxin's lethal factor on ion channels formed by the protective antigen. J. Biol. Chem. 270:18626-30
    • (1995) J. Biol. Chem. , vol.270 , pp. 18626-18630
    • Zhao, J.1    Milne, J.C.2    Collier, R.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.