메뉴 건너뛰기




Volumn 65, Issue 3, 2003, Pages 309-314

Anthrax toxin receptor proteins

Author keywords

Angiogenesis; Anthrax toxin; Antitoxin; ATR; Receptor; TEM8

Indexed keywords

ANTHRAX TOXIN; ANTIBIOTIC AGENT; ANTITOXIN; CELL RECEPTOR; INTEGRIN; MEMBRANE PROTEIN; RECEPTOR PROTEIN; RECEPTOR SUBUNIT; TUMOR MARKER; VIRULENCE FACTOR;

EID: 0037300719     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(02)01455-7     Document Type: Note
Times cited : (58)

References (55)
  • 2
    • 0000059218 scopus 로고
    • The chemical basis of the virulence of Bacillus anthracis. II: Some biological properties of bacterial products
    • Keppie J., Smith H., Harris-Smith P.W. The chemical basis of the virulence of Bacillus anthracis. II: some biological properties of bacterial products. Br. J. Exp. Pathol. 34:1953;486-496.
    • (1953) Br. J. Exp. Pathol. , vol.34 , pp. 486-496
    • Keppie, J.1    Smith, H.2    Harris-Smith, P.W.3
  • 4
    • 0020681139 scopus 로고
    • Evidence for plasmid-mediated toxin production in Bacillus anthracis
    • Mikesell P., Ivins B.E., Ristroph J.D., Dreier T.M. Evidence for plasmid-mediated toxin production in Bacillus anthracis. Infect Immun. 39:1983;371-376.
    • (1983) Infect Immun. , vol.39 , pp. 371-376
    • Mikesell, P.1    Ivins, B.E.2    Ristroph, J.D.3    Dreier, T.M.4
  • 5
    • 0021967604 scopus 로고
    • Association of the encapsulation of Bacillus anthracis with a 60 megadalton plasmid
    • Uchida I., Sekizaki T., Hashimoto K., Terakado N. Association of the encapsulation of Bacillus anthracis with a 60 megadalton plasmid. J. Gen. Microbiol. 131(Pt 2):1985;363-367.
    • (1985) J. Gen. Microbiol. , vol.131 , Issue.PART 2 , pp. 363-367
    • Uchida, I.1    Sekizaki, T.2    Hashimoto, K.3    Terakado, N.4
  • 6
    • 0000947082 scopus 로고
    • Anthrax toxin edema factor: A bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells
    • Leppla S.H. Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. U.S.A. 79:1982;3162-3166.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 3162-3166
    • Leppla, S.H.1
  • 9
    • 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. Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages. Biochem. Biophys. Res. Commun. 248:1998;706-711.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 706-711
    • Vitale, G.1    Pellizzari, R.2    Recchi, C.3    Napolitani, G.4    Mock, M.5    Montecucco, C.6
  • 10
    • 0034672216 scopus 로고    scopus 로고
    • Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor
    • Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C. Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor. Biochem. J. 352(Pt 3):2000;739-745.
    • (2000) Biochem. J. , vol.352 , Issue.PART 3 , pp. 739-745
    • Vitale, G.1    Bernardi, L.2    Napolitani, G.3    Mock, M.4    Montecucco, C.5
  • 13
    • 0035797887 scopus 로고    scopus 로고
    • Kif1C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor
    • Watters J.W., Dewar K., Lehoczky J., Boyartchuk V., Dietrich W.F. Kif1C, a kinesin-like motor protein, mediates mouse macrophage resistance to anthrax lethal factor. Curr. Biol. 11:2001;1503-1511.
    • (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
  • 14
    • 0033056295 scopus 로고    scopus 로고
    • Proteasome activity is required for anthrax lethal toxin to kill macrophages
    • Tang G., Leppla S.H. Proteasome activity is required for anthrax lethal toxin to kill macrophages. Infect. Immun. 67:1999;3055-3060.
    • (1999) Infect. Immun. , vol.67 , pp. 3055-3060
    • Tang, G.1    Leppla, S.H.2
  • 15
    • 0028872463 scopus 로고
    • Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases
    • Gordon V.M., Klimpel K.R., Arora N., Henderson M.A., Leppla S.H. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect. Immun. 63:1995;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
  • 16
    • 0028018856 scopus 로고
    • Anthrax protective antigen forms oligomers during intoxication of mammalian cells
    • Milne J.C., Furlong D., Hanna P.C., Wall J.S., Collier R.J. Anthrax protective antigen forms oligomers during intoxication of mammalian cells. J. Biol. Chem. 269:1994;20607-20612.
    • (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
  • 18
    • 0022891493 scopus 로고
    • Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process
    • Friedlander A.M. Macrophages are sensitive to anthrax lethal toxin through an acid-dependent process. J. Biol. Chem. 261:1986;7123-7126.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7123-7126
    • Friedlander, A.M.1
  • 19
    • 0027443262 scopus 로고
    • PH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen
    • Milne J.C., Collier R.J. pH-dependent permeabilization of the plasma membrane of mammalian cells by anthrax protective antigen. Mol. Microbiol. 10:1993;647-653.
    • (1993) Mol. Microbiol. , vol.10 , pp. 647-653
    • Milne, J.C.1    Collier, R.J.2
  • 20
    • 0026044658 scopus 로고
    • Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells
    • Escuyer V., Collier R.J. Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells. Infect. Immun. 59:1991;3381-3386.
    • (1991) Infect. Immun. , vol.59 , pp. 3381-3386
    • Escuyer, V.1    Collier, R.J.2
  • 21
    • 0012550671 scopus 로고
    • Anthrax protective antigen receptor: Identification of a protective antigen binding protein by chemical cross-linking
    • Withholdt B, editor. New York: Gustav Fischer
    • Friedlander AM, Raziuddin A. Anthrax protective antigen receptor: identification of a protective antigen binding protein by chemical cross-linking. In: Withholdt B, editor. Bacterial protein toxins. New York: Gustav Fischer; 1992, p. 365-6.
    • (1992) Bacterial Protein Toxins , pp. 365-366
    • Friedlander, A.M.1    Raziuddin, A.2
  • 24
    • 0031866394 scopus 로고    scopus 로고
    • Ligand recognition by the I domain-containing integrins
    • Dickeson S.K., Santoro S.A. Ligand recognition by the I domain-containing integrins. Cell Mol. Life Sci. 54:1998;556-566.
    • (1998) Cell Mol. Life Sci. , vol.54 , pp. 556-566
    • Dickeson, S.K.1    Santoro, S.A.2
  • 25
    • 0001731185 scopus 로고
    • Observations on experimental anthrax: Demonstration of a specific lethal factor produced in vivo by Bacillus anthracis
    • Smith H., Keppie J. Observations on experimental anthrax: demonstration of a specific lethal factor produced in vivo by Bacillus anthracis. Nature. 173:1954;869-870.
    • (1954) Nature , vol.173 , pp. 869-870
    • Smith, H.1    Keppie, J.2
  • 26
    • 0036151303 scopus 로고    scopus 로고
    • Anthrax spores make an essential contribution to vaccine efficacy
    • Brossier F., Levy M., Mock M. Anthrax spores make an essential contribution to vaccine efficacy. Infect. Immun. 70:2002;661-664.
    • (2002) Infect. Immun. , vol.70 , pp. 661-664
    • Brossier, F.1    Levy, M.2    Mock, M.3
  • 27
    • 0036151173 scopus 로고    scopus 로고
    • Efficiency of protection of guinea pigs against infection with Bacillus anthracis spores by passive immunization
    • Kobiler D., Gozes Y., Rosenberg H., Marcus D., Reuveny S., Altboum Z. Efficiency of protection of guinea pigs against infection with Bacillus anthracis spores by passive immunization. Infect. Immun. 70:2002;544-560.
    • (2002) Infect. Immun. , vol.70 , pp. 544-560
    • Kobiler, D.1    Gozes, Y.2    Rosenberg, H.3    Marcus, D.4    Reuveny, S.5    Altboum, Z.6
  • 29
    • 0035957753 scopus 로고    scopus 로고
    • Dominant-negative mutants of a toxin subunit: An approach to therapy of anthrax
    • Sellman B.R., Mourez M., Collier R.J. Dominant-negative mutants of a toxin subunit: an approach to therapy of anthrax. Science. 292:2001;695-697.
    • (2001) Science , vol.292 , pp. 695-697
    • Sellman, B.R.1    Mourez, M.2    Collier, R.J.3
  • 30
    • 0023932170 scopus 로고
    • Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin
    • Gordon V.M., Leppla S.H., Hewlett E.L. Inhibitors of receptor-mediated endocytosis block the entry of Bacillus anthracis adenylate cyclase toxin but not that of Bordetella pertussis adenylate cyclase toxin. Infect. Immun. 56:1988;1066-1069.
    • (1988) Infect. Immun. , vol.56 , pp. 1066-1069
    • Gordon, V.M.1    Leppla, S.H.2    Hewlett, E.L.3
  • 31
    • 0025771545 scopus 로고
    • Anthrax toxin protective antigen: Low-pH-induced hydrophobicity and channel formation in liposomes
    • Koehler T.M., Collier R.J. Anthrax toxin protective antigen: low-pH-induced hydrophobicity and channel formation in liposomes. Mol. Microbiol. 5:1991;1501-1506.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1501-1506
    • Koehler, T.M.1    Collier, R.J.2
  • 32
    • 2542509040 scopus 로고    scopus 로고
    • The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin
    • Ménard A., Altendorf K., Breves D., Mock M., Montecucco C. The vacuolar ATPase proton pump is required for the cytotoxicity of Bacillus anthracis lethal toxin. FEBS Lett. 386:1996;161-164.
    • (1996) FEBS Lett. , vol.386 , pp. 161-164
    • Ménard, A.1    Altendorf, K.2    Breves, D.3    Mock, M.4    Montecucco, C.5
  • 33
    • 0024523836 scopus 로고
    • Anthrax toxin: Channel-forming activity of protective antigen in planar phospholipid bilayers
    • Blaustein R.O., Koehler T.M., Collier R.J., Finkelstein A. Anthrax toxin: channel-forming activity of protective antigen in planar phospholipid bilayers. Proc. Natl. Acad. Sci. U.S.A. 86:1989;2209-2213.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 2209-2213
    • Blaustein, R.O.1    Koehler, T.M.2    Collier, R.J.3    Finkelstein, A.4
  • 34
    • 0028281986 scopus 로고
    • The channel formed in planar lipid bilayers by the protective antigen component of anthrax toxin
    • Finkelstein A. The channel formed in planar lipid bilayers by the protective antigen component of anthrax toxin. Toxicology. 87:1994;29-41.
    • (1994) Toxicology , vol.87 , pp. 29-41
    • Finkelstein, A.1
  • 36
    • 0033868243 scopus 로고    scopus 로고
    • Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization
    • Beauregard K.E., Collier R.J., Swanson J.A. Proteolytic activation of receptor-bound anthrax protective antigen on macrophages promotes its internalization. Cell Microbiol. 2:2000;251-258.
    • (2000) Cell Microbiol. , vol.2 , pp. 251-258
    • Beauregard, K.E.1    Collier, R.J.2    Swanson, J.A.3
  • 37
    • 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 K.R., Goel S., Swain P.K., Leppla S.H. Oligomerization of anthrax toxin protective antigen and binding of lethal factor during endocytic uptake into mammalian cells. Infect. Immun. 67:1999;1853-1859.
    • (1999) Infect. Immun. , vol.67 , pp. 1853-1859
    • Singh, Y.1    Klimpel, K.R.2    Goel, S.3    Swain, P.K.4    Leppla, S.H.5
  • 38
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor: Identity with a heparin-binding EGF-like growth factor precursor
    • Naglich J.G., Metherall J.E., Russell D.W., Eidels L. Expression cloning of a diphtheria toxin receptor: identity with a heparin-binding EGF-like growth factor precursor. Cell. 69:1992;1051-1061.
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 39
    • 0028171066 scopus 로고
    • The cytoplasmic domain of the diphtheria toxin receptor (HB-EGF precursor) is not required for receptor-mediated endocytosis
    • Almond B.D., Eidels L. The cytoplasmic domain of the diphtheria toxin receptor (HB-EGF precursor) is not required for receptor-mediated endocytosis. J. Biol. Chem. 269:1994;26635-26641.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26635-26641
    • Almond, B.D.1    Eidels, L.2
  • 40
    • 0026794750 scopus 로고
    • Functional characterization of protease-treated Bacillus anthracis protective antigen
    • Novak J.M., Stein M.-P., Little S.F., Leppla S.H., Friedlander A.M. Functional characterization of protease-treated Bacillus anthracis protective antigen. J. Biol. Chem. 267:1992;17186-17193.
    • (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
  • 42
    • 0033059994 scopus 로고    scopus 로고
    • Bi-cycling the furin pathway: From TGN localization to pathogen activation and embryogenesis
    • Molloy S.S., Anderson E.D., Jean F., Thomas G. Bi-cycling the furin pathway: from TGN localization to pathogen activation and embryogenesis. Trends Cell Biol. 9:1999;28-35.
    • (1999) Trends Cell Biol. , vol.9 , pp. 28-35
    • Molloy, S.S.1    Anderson, E.D.2    Jean, F.3    Thomas, G.4
  • 43
    • 0026498189 scopus 로고
    • Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin
    • Klimpel K.R., Molloy S.S., Thomas G., Leppla S.H. Anthrax toxin protective antigen is activated by a cell surface protease with the sequence specificity and catalytic properties of furin. Proc. Natl. Acad. Sci. U.S.A. 89:1992;10277-10281.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 10277-10281
    • Klimpel, K.R.1    Molloy, S.S.2    Thomas, G.3    Leppla, S.H.4
  • 44
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy S.S., Bresnahan P.A., Leppla S.H., Klimpel K.R., Thomas G. 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. 267:1992;16396-16402.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 45
    • 0001256478 scopus 로고    scopus 로고
    • Anthrax toxin
    • Aktories K, Just I, editors. Berlin: Springer
    • Leppla SH. Anthrax toxin. In: Aktories K, Just I, editors. Handbook of experimental pharmacology. Berlin: Springer; 2000, p. 447-72.
    • (2000) Handbook of Experimental Pharmacology , pp. 447-472
    • Leppla, S.H.1
  • 46
    • 0029071726 scopus 로고
    • Isolation and characterization of a Clostridium botulinum C2 toxin-resistant cell line: Evidence for possible involvement of the cellular C2II receptor in growth regulation
    • Fritz G., Schroeder P., Aktories K. Isolation and characterization of a Clostridium botulinum C2 toxin-resistant cell line: evidence for possible involvement of the cellular C2II receptor in growth regulation. Infect. Immun. 63:1995;2334-2340.
    • (1995) Infect. Immun. , vol.63 , pp. 2334-2340
    • Fritz, G.1    Schroeder, P.2    Aktories, K.3
  • 47
    • 0034723205 scopus 로고    scopus 로고
    • Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates
    • Eckhardt M., Barth H., Blocker D., Aktories K. Binding of Clostridium botulinum C2 toxin to asparagine-linked complex and hybrid carbohydrates. J. Biol. Chem. 275:2000;2328-2334.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2328-2334
    • Eckhardt, M.1    Barth, H.2    Blocker, D.3    Aktories, K.4
  • 49
    • 0026496886 scopus 로고
    • The three-dimensional structure of the tenth type III module of fibronectin: An insight into RGD-mediated interactions
    • Main A.L., Harvey T.S., Baron M., Boyd J., Campbell I.D. The three-dimensional structure of the tenth type III module of fibronectin: an insight into RGD-mediated interactions. Cell. 71:1992;671-678.
    • (1992) Cell , vol.71 , pp. 671-678
    • Main, A.L.1    Harvey, T.S.2    Baron, M.3    Boyd, J.4    Campbell, I.D.5
  • 51
    • 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 S.E., Mavila A., Salazar R., Bayless K.J., Kanagala S., Maxwell S.A., Davis G.E. 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. 114:2001;2755-2773.
    • (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    Maxwell, S.A.6    Davis, G.E.7
  • 52
    • 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 N.S., Resau J., Webb C.P., Koochekpour S., Koo H.M., Leppla S.H., Vande Woude G.F. 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. U.S.A. 98:2001;4089-4094.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 4089-4094
    • Duesbery, N.S.1    Resau, J.2    Webb, C.P.3    Koochekpour, S.4    Koo, H.M.5    Leppla, S.H.6    Vande Woude, G.F.7
  • 53
    • 0035947634 scopus 로고    scopus 로고
    • Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin
    • Liu S., Bugge T.H., Leppla S.H. Targeting of tumor cells by cell surface urokinase plasminogen activator-dependent anthrax toxin. J. Biol. Chem. 276:2001;17976-17984.
    • (2001) J. Biol. Chem. , vol.276 , pp. 17976-17984
    • Liu, S.1    Bugge, T.H.2    Leppla, S.H.3
  • 54
    • 0034326255 scopus 로고    scopus 로고
    • Tumor cell-selective cytotoxicity of matrix metalloproteinase-activated anthrax toxin
    • Liu S., Netzel-Arnett S., Birkedal-Hansen H., Leppla S.H. Tumor cell-selective cytotoxicity of matrix metalloproteinase-activated anthrax toxin. Cancer Res. 60:2000;6061-6067.
    • (2000) Cancer Res. , vol.60 , pp. 6061-6067
    • Liu, S.1    Netzel-Arnett, S.2    Birkedal-Hansen, H.3    Leppla, S.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.