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Volumn 26, Issue 2, 2006, Pages 397-419

Toxins: Bacterial and Marine Toxins

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ADRENERGIC RECEPTOR BLOCKING AGENT; ANTHRAX TOXIN; ANTIBIOTIC AGENT; ANTIINFECTIVE AGENT; BACTERIAL TOXIN; BACTERIAL VACCINE; BETA ADRENERGIC RECEPTOR BLOCKING AGENT; BOTULINUM ANTISERUM; BOTULINUM TOXIN; CHOLERA TOXIN; CHOLERA VACCINE; CIPROFLOXACIN; COTRIMOXAZOLE; DIAZEPAM; DOXYCYCLINE; ERYTHROMYCIN; GONYAUTOXIN; IMMUNOGLOBULIN; LETHAL FACTOR INHIBITOR; MAGNESIUM SULFATE; MARINE TOXIN; METRONIDAZOLE; PENICILLIN G; QUINOLINE DERIVED ANTIINFECTIVE AGENT; TETANUS TOXIN; TETANUS TOXOID; TETRODOTOXIN; TRIMETHOPRIM; UNCLASSIFIED DRUG; UNINDEXED DRUG; VEROTOXIN;

EID: 33745426024     PISSN: 02722712     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cll.2006.04.003     Document Type: Review
Times cited : (17)

References (136)
  • 1
    • 0034838167 scopus 로고    scopus 로고
    • Toxins as weapons of mass destruction. A comparison and contrast with biological warfare and chemical warfare agents
    • Madsen J. Toxins as weapons of mass destruction. A comparison and contrast with biological warfare and chemical warfare agents. Clin Lab Med 21 3 (2001) 593-605
    • (2001) Clin Lab Med , vol.21 , Issue.3 , pp. 593-605
    • Madsen, J.1
  • 2
    • 33745356523 scopus 로고    scopus 로고
    • Shapiro DS WA. Sentinel laboratory guidelines for suspected agents of bioterrorism. Botulinum. Available at: http://www.asm.org/ASM/files/LEFTMARGINHEADERLIST/downloadfilename/0000000522/BotulismFinalVersion73003.pdf. Accessed January 6, 2006.
  • 4
    • 2442686741 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin-new insights into the cellular up-take of the actin-ADP-ribosylating toxin
    • Aktories K., and Barth H. Clostridium botulinum C2 toxin-new insights into the cellular up-take of the actin-ADP-ribosylating toxin. Int J Med Microbiol 293 7-8 (2004) 557-564
    • (2004) Int J Med Microbiol , vol.293 , Issue.7-8 , pp. 557-564
    • Aktories, K.1    Barth, H.2
  • 5
    • 4844230030 scopus 로고    scopus 로고
    • Clostridium botulinum and the clinical laboratorian: a detailed review of botulism, including biological warfare ramifications of botulinum toxin
    • Caya J.G., Agni R., and Miller J.E. Clostridium botulinum and the clinical laboratorian: a detailed review of botulism, including biological warfare ramifications of botulinum toxin. Arch Pathol Lab Med 128 6 (2004) 653-662
    • (2004) Arch Pathol Lab Med , vol.128 , Issue.6 , pp. 653-662
    • Caya, J.G.1    Agni, R.2    Miller, J.E.3
  • 6
    • 23744474333 scopus 로고    scopus 로고
    • First case of infant botulism caused by Clostridium baratii type F in California
    • Barash J.R., Tang T.W., and Arnon S.S. First case of infant botulism caused by Clostridium baratii type F in California. J Clin Microbiol 43 8 (2005) 4280-4282
    • (2005) J Clin Microbiol , vol.43 , Issue.8 , pp. 4280-4282
    • Barash, J.R.1    Tang, T.W.2    Arnon, S.S.3
  • 7
    • 0035903265 scopus 로고    scopus 로고
    • Botulism outbreak associated with eating fermented foods-Alaska, 2001
    • Centers for Disease Control and Prevention. Botulism outbreak associated with eating fermented foods-Alaska, 2001. MMWR Morb Mortal Wkly Rep 50 32 (2001) 680-682
    • (2001) MMWR Morb Mortal Wkly Rep , vol.50 , Issue.32 , pp. 680-682
    • Centers for Disease Control and Prevention1
  • 8
    • 0345686575 scopus 로고    scopus 로고
    • Botulinum toxin type B micromechanosensor
    • Liu W., Montana V., Chapman E.R., et al. Botulinum toxin type B micromechanosensor. Proc Natl Acad Sci USA 100 23 (2003) 13621-13625
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.23 , pp. 13621-13625
    • Liu, W.1    Montana, V.2    Chapman, E.R.3
  • 9
    • 24344504150 scopus 로고    scopus 로고
    • Detection of botulinum toxins: micromechanical and fluorescence-based sensors
    • Parpura V., and Chapman E.R. Detection of botulinum toxins: micromechanical and fluorescence-based sensors. Croat Med J 46 4 (2005) 491-497
    • (2005) Croat Med J , vol.46 , Issue.4 , pp. 491-497
    • Parpura, V.1    Chapman, E.R.2
  • 11
    • 0033867839 scopus 로고    scopus 로고
    • Selected classic examples of neurotoxic disorders-biological neurotoxins
    • Goetz C.G., and Meisel E. Selected classic examples of neurotoxic disorders-biological neurotoxins. Neurol Clin 18 3 (2000) 719-740
    • (2000) Neurol Clin , vol.18 , Issue.3 , pp. 719-740
    • Goetz, C.G.1    Meisel, E.2
  • 12
    • 4344715045 scopus 로고    scopus 로고
    • Medical aspects of biologic toxins
    • vii
    • Marks J.D. Medical aspects of biologic toxins. Anesthesiol Clin North America 22 3 (2004) 509-532 vii
    • (2004) Anesthesiol Clin North America , vol.22 , Issue.3 , pp. 509-532
    • Marks, J.D.1
  • 13
    • 33745383402 scopus 로고    scopus 로고
    • Bioterriorism Agents/Diseases by Category. Available at: http://www.bt.cdc.gov/agent/agentlist-category.asp. Accessed January 3, 2006.
  • 14
    • 33745395477 scopus 로고    scopus 로고
    • Darling RG WJ. USAMRIID's medical management of biological casualties handbook. 5th edition. Frederick (MD): US Army Medical Research Institute; 2004.
  • 15
    • 2942511921 scopus 로고    scopus 로고
    • Ganglioside-liposome immunoassay for the detection of botulinum toxin
    • Ahn-Yoon S., DeCory T.R., and Durst R.A. Ganglioside-liposome immunoassay for the detection of botulinum toxin. Anal Bioanal Chem 378 1 (2004) 68-75
    • (2004) Anal Bioanal Chem , vol.378 , Issue.1 , pp. 68-75
    • Ahn-Yoon, S.1    DeCory, T.R.2    Durst, R.A.3
  • 16
    • 0035961566 scopus 로고    scopus 로고
    • Botulinum toxin as a biological weapon: medical and public health management
    • Arnon S.S., Schechter R., Inglesby T.V., et al. Botulinum toxin as a biological weapon: medical and public health management. JAMA 285 8 (2001) 1059-1070
    • (2001) JAMA , vol.285 , Issue.8 , pp. 1059-1070
    • Arnon, S.S.1    Schechter, R.2    Inglesby, T.V.3
  • 17
    • 0026497466 scopus 로고
    • Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin
    • Schiavo G., Benfenati F., Poulain B., et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 359 6398 (1992) 832-835
    • (1992) Nature , vol.359 , Issue.6398 , pp. 832-835
    • Schiavo, G.1    Benfenati, F.2    Poulain, B.3
  • 18
    • 0027241009 scopus 로고
    • Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin
    • Schiavo G., Shone C.C., Rossetto O., et al. Botulinum neurotoxin serotype F is a zinc endopeptidase specific for VAMP/synaptobrevin. J Biol Chem 268 16 (1993) 11516-11519
    • (1993) J Biol Chem , vol.268 , Issue.16 , pp. 11516-11519
    • Schiavo, G.1    Shone, C.C.2    Rossetto, O.3
  • 19
    • 17444371599 scopus 로고    scopus 로고
    • Botulinum toxin: mechanisms of action
    • Dressler D., Saberi F.A., and Barbosa E.R. Botulinum toxin: mechanisms of action. Eur Neurol 63 1 (2005) 180-185
    • (2005) Eur Neurol , vol.63 , Issue.1 , pp. 180-185
    • Dressler, D.1    Saberi, F.A.2    Barbosa, E.R.3
  • 20
    • 18744410709 scopus 로고    scopus 로고
    • Botulinal neurotoxins: revival of an old killer
    • Montecucco C., and Molgo J. Botulinal neurotoxins: revival of an old killer. Curr Opin Pharmacol 5 3 (2005) 274-279
    • (2005) Curr Opin Pharmacol , vol.5 , Issue.3 , pp. 274-279
    • Montecucco, C.1    Molgo, J.2
  • 21
    • 3042856483 scopus 로고    scopus 로고
    • Microfluidic tectonics platform: a colorimetric, disposable botulinum toxin enzyme-linked immunosorbent assay system
    • Moorthy J., Mensing G.A., Kim D., et al. Microfluidic tectonics platform: a colorimetric, disposable botulinum toxin enzyme-linked immunosorbent assay system. Electrophoresis 25 10-11 (2004) 1705-1713
    • (2004) Electrophoresis , vol.25 , Issue.10-11 , pp. 1705-1713
    • Moorthy, J.1    Mensing, G.A.2    Kim, D.3
  • 22
    • 3242884957 scopus 로고    scopus 로고
    • Colloidal gold-based immunochromatographic assay for detection of botulinum neurotoxin type B
    • Chiao D.J., Shyu R.H., Hu C.S., et al. Colloidal gold-based immunochromatographic assay for detection of botulinum neurotoxin type B. J Chromatogr B Analyt Technol Biomed Life Sci 809 1 (2004) 37-41
    • (2004) J Chromatogr B Analyt Technol Biomed Life Sci , vol.809 , Issue.1 , pp. 37-41
    • Chiao, D.J.1    Shyu, R.H.2    Hu, C.S.3
  • 23
    • 25644432095 scopus 로고    scopus 로고
    • Botulinum neurotoxin detection and differentiation by mass spectrometry
    • Barr J.R., Moura H., Boyer A.E., et al. Botulinum neurotoxin detection and differentiation by mass spectrometry. Emerg Infect Dis 11 10 (2005) 1578-1583
    • (2005) Emerg Infect Dis , vol.11 , Issue.10 , pp. 1578-1583
    • Barr, J.R.1    Moura, H.2    Boyer, A.E.3
  • 24
    • 33745428977 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention. Epidemiology and prevention of vaccine-preventable diseases. The Pink Book. 8th edition. Available at: http://www.cdc.gov/nip/publications/pink. Accessed January 4, 2006.
  • 25
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco C., and Schiavo G. Mechanism of action of tetanus and botulinum neurotoxins. Mol Microbiol 13 1 (1994) 1-8
    • (1994) Mol Microbiol , vol.13 , Issue.1 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 27
    • 0038341615 scopus 로고    scopus 로고
    • Pascual FB ME, Zanardi LR, Cortese MM, et al. Tetanus surveillance-United States 1998-2000. MMWR CDC Surveill Summ 2003;52(SS03):1-8.
  • 28
    • 0037452242 scopus 로고    scopus 로고
    • Preventing and treating tetanus
    • Thwaites C.L., and Farrar J.J. Preventing and treating tetanus. BMJ 326 7381 (2003) 117-118
    • (2003) BMJ , vol.326 , Issue.7381 , pp. 117-118
    • Thwaites, C.L.1    Farrar, J.J.2
  • 29
    • 24744454624 scopus 로고    scopus 로고
    • Improvement in laboratory diagnosis of wound botulism and tetanus among injecting illicit-drug users by use of real-time PCR assays for neurotoxin gene fragments
    • Akbulut D., Grant K.A., and McLauchlin J. Improvement in laboratory diagnosis of wound botulism and tetanus among injecting illicit-drug users by use of real-time PCR assays for neurotoxin gene fragments. J Clin Microbiol 43 9 (2005) 4342-4348
    • (2005) J Clin Microbiol , vol.43 , Issue.9 , pp. 4342-4348
    • Akbulut, D.1    Grant, K.A.2    McLauchlin, J.3
  • 30
  • 32
    • 0034862444 scopus 로고    scopus 로고
    • Toxins of Bacillus anthracis
    • Brossier F., and Mock M. Toxins of Bacillus anthracis. Toxicon 39 11 (2001) 1747-1755
    • (2001) Toxicon , vol.39 , Issue.11 , pp. 1747-1755
    • Brossier, F.1    Mock, M.2
  • 33
    • 0031052342 scopus 로고    scopus 로고
    • Crystal structure of the anthrax toxin protective antigen
    • Petosa C., Collier R.J., Klimpel K.R., et al. Crystal structure of the anthrax toxin protective antigen. Nature 385 6619 (1997) 833-838
    • (1997) Nature , vol.385 , Issue.6619 , pp. 833-838
    • Petosa, C.1    Collier, R.J.2    Klimpel, K.R.3
  • 34
    • 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., et al. Proteolytic activation of bacterial toxins by eukaryotic cells is performed by furin and by additional cellular proteases. Infect Immun 63 1 (1995) 82-87
    • (1995) Infect Immun , vol.63 , Issue.1 , pp. 82-87
    • Gordon, V.M.1    Klimpel, K.R.2    Arora, N.3
  • 35
    • 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 USA 79 10 (1982) 3162-3166
    • (1982) Proc Natl Acad Sci USA , vol.79 , Issue.10 , pp. 3162-3166
    • Leppla, S.H.1
  • 36
    • 17044400220 scopus 로고    scopus 로고
    • Anthrax edema toxin cooperates with lethal toxin to impair cytokine secretion during infection of dendritic cells
    • Tournier J.N., Quesnel-Hellmann A., Mathieu J., et al. Anthrax edema toxin cooperates with lethal toxin to impair cytokine secretion during infection of dendritic cells. J Immunol 174 8 (2005) 4934-4941
    • (2005) J Immunol , vol.174 , Issue.8 , pp. 4934-4941
    • Tournier, J.N.1    Quesnel-Hellmann, A.2    Mathieu, J.3
  • 37
    • 13644268542 scopus 로고    scopus 로고
    • Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signaling
    • Paccani S.R., Tonello F., Ghittoni R., et al. Anthrax toxins suppress T lymphocyte activation by disrupting antigen receptor signaling. J Exp Med 201 3 (2005) 325-331
    • (2005) J Exp Med , vol.201 , Issue.3 , pp. 325-331
    • Paccani, S.R.1    Tonello, F.2    Ghittoni, R.3
  • 38
    • 0028088404 scopus 로고
    • Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity
    • Klimpel K.R., Arora N., and Leppla S.H. Anthrax toxin lethal factor contains a zinc metalloprotease consensus sequence which is required for lethal toxin activity. Mol Microbiol 13 6 (1994) 1093-1100
    • (1994) Mol Microbiol , vol.13 , Issue.6 , pp. 1093-1100
    • Klimpel, K.R.1    Arora, N.2    Leppla, S.H.3
  • 39
    • 18244414803 scopus 로고    scopus 로고
    • Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor
    • Duesbery N.S., Webb C.P., Leppla S.H., et al. Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal factor. Science 280 5364 (1998) 734-737
    • (1998) Science , vol.280 , Issue.5364 , pp. 734-737
    • Duesbery, N.S.1    Webb, C.P.2    Leppla, S.H.3
  • 40
    • 0037144590 scopus 로고    scopus 로고
    • Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition
    • Park J.M., Greten F.R., Li Z.W., et al. Macrophage apoptosis by anthrax lethal factor through p38 MAP kinase inhibition. Science 297 5589 (2002) 2048-2051
    • (2002) Science , vol.297 , Issue.5589 , pp. 2048-2051
    • Park, J.M.1    Greten, F.R.2    Li, Z.W.3
  • 41
    • 0346251030 scopus 로고    scopus 로고
    • Anthrax lethal toxin induces human endothelial cell apoptosis
    • Kirby J.E. Anthrax lethal toxin induces human endothelial cell apoptosis. Infect Immun 72 1 (2004) 430-439
    • (2004) Infect Immun , vol.72 , Issue.1 , pp. 430-439
    • Kirby, J.E.1
  • 42
    • 33745355474 scopus 로고    scopus 로고
    • Questions and answer about anthrax. Available at: http://www.bt.cdc.gov/agent/anthrax/faq. Accessed December 10, 2005.
  • 43
    • 0036569530 scopus 로고    scopus 로고
    • Anthrax as a biological weapon, 2002: updated recommendations for management
    • Inglesby T.V., O'Toole T., Henderson D.A., et al. Anthrax as a biological weapon, 2002: updated recommendations for management. JAMA 287 17 (2002) 2236-2252
    • (2002) JAMA , vol.287 , Issue.17 , pp. 2236-2252
    • Inglesby, T.V.1    O'Toole, T.2    Henderson, D.A.3
  • 44
    • 33745371891 scopus 로고    scopus 로고
    • Approved tests for the detection of Bacillus anthracis in the laboratory response network. Available at: http://www.bt.cdc.gov/agent/anthrax/lab-testing/approvedlrntests.asp. Accessed January 3, 2006.
  • 45
    • 0035955707 scopus 로고    scopus 로고
    • Update: investigation of bioterrorism-related anthrax and interim guidelines for exposure management and antimicrobial therapy, October 2001
    • Centers for Disease Control and Prevention. Update: investigation of bioterrorism-related anthrax and interim guidelines for exposure management and antimicrobial therapy, October 2001. MMWR Morb Mortal Wkly Rep 50 42 (2001) 909-919
    • (2001) MMWR Morb Mortal Wkly Rep , vol.50 , Issue.42 , pp. 909-919
    • Centers for Disease Control and Prevention1
  • 46
    • 0034759189 scopus 로고    scopus 로고
    • Clinical and environmental isolates of Vibrio cholerae serogroup O141 carry the CTX phage and the genes encoding the toxin-coregulated pili
    • Dalsgaard A., Serichantalergs O., Forslund A., et al. Clinical and environmental isolates of Vibrio cholerae serogroup O141 carry the CTX phage and the genes encoding the toxin-coregulated pili. J Clin Microbiol 39 11 (2001) 4086-4092
    • (2001) J Clin Microbiol , vol.39 , Issue.11 , pp. 4086-4092
    • Dalsgaard, A.1    Serichantalergs, O.2    Forslund, A.3
  • 47
    • 0027174854 scopus 로고
    • Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin
    • Sixma T.K., Kalk K.H., van Zanten B.A., et al. Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin. J Mol Biol 230 3 (1993) 890-918
    • (1993) J Mol Biol , vol.230 , Issue.3 , pp. 890-918
    • Sixma, T.K.1    Kalk, K.H.2    van Zanten, B.A.3
  • 48
    • 0029161099 scopus 로고
    • The three-dimensional crystal structure of cholera toxin
    • Zhang R.G., Scott D.L., Westbrook M.L., et al. The three-dimensional crystal structure of cholera toxin. J Mol Biol 251 4 (1995) 563-573
    • (1995) J Mol Biol , vol.251 , Issue.4 , pp. 563-573
    • Zhang, R.G.1    Scott, D.L.2    Westbrook, M.L.3
  • 49
    • 0011644189 scopus 로고
    • Interaction of cholera toxin and membrane GM1 ganglioside of small intestine
    • Holmgren J., Lonnroth I., Mansson J., et al. Interaction of cholera toxin and membrane GM1 ganglioside of small intestine. Proc Natl Acad Sci USA 72 7 (1975) 2520-2524
    • (1975) Proc Natl Acad Sci USA , vol.72 , Issue.7 , pp. 2520-2524
    • Holmgren, J.1    Lonnroth, I.2    Mansson, J.3
  • 50
    • 10744224620 scopus 로고    scopus 로고
    • Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulum
    • Fujinaga Y., Wolf A.A., Rodighiero C., et al. Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulum. Mol Biol Cell 14 12 (2003) 4783-4793
    • (2003) Mol Biol Cell , vol.14 , Issue.12 , pp. 4783-4793
    • Fujinaga, Y.1    Wolf, A.A.2    Rodighiero, C.3
  • 51
    • 2442714018 scopus 로고    scopus 로고
    • Retrograde transport of cholera toxin into the ER of host cells
    • Lencer W.I. Retrograde transport of cholera toxin into the ER of host cells. Int J Med Microbiol 293 7-8 (2004) 491-494
    • (2004) Int J Med Microbiol , vol.293 , Issue.7-8 , pp. 491-494
    • Lencer, W.I.1
  • 52
    • 0008614480 scopus 로고
    • Mechanism of adenylate cyclase activation by cholera toxin: inhibition of GTP hydrolysis at the regulatory site
    • Cassel D., and Selinger Z. Mechanism of adenylate cyclase activation by cholera toxin: inhibition of GTP hydrolysis at the regulatory site. Proc Natl Acad Sci USA 74 8 (1977) 3307-3311
    • (1977) Proc Natl Acad Sci USA , vol.74 , Issue.8 , pp. 3307-3311
    • Cassel, D.1    Selinger, Z.2
  • 53
    • 0033548246 scopus 로고    scopus 로고
    • Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity
    • Rodighiero C., Aman A.T., Kenny M.J., et al. Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity. J Biol Chem 274 7 (1999) 3962-3969
    • (1999) J Biol Chem , vol.274 , Issue.7 , pp. 3962-3969
    • Rodighiero, C.1    Aman, A.T.2    Kenny, M.J.3
  • 54
    • 0043172637 scopus 로고    scopus 로고
    • Development of microbial-human enterocyte interaction: cholera toxin
    • Lu L., Baldeon M.E., Savidge T., et al. Development of microbial-human enterocyte interaction: cholera toxin. Pediatr Res 54 2 (2003) 212-218
    • (2003) Pediatr Res , vol.54 , Issue.2 , pp. 212-218
    • Lu, L.1    Baldeon, M.E.2    Savidge, T.3
  • 55
    • 33745405466 scopus 로고    scopus 로고
    • Bopp CA RA, Wells JG. Laboratory methods for the diagnosis of epidemic dysentery and cholera. Atlanta (GA): Centers for Disease Control and Prevention; 1999.
  • 56
    • 0026426469 scopus 로고
    • Current trends update: cholera-Western Hemisphere, and recommendations for treatment of cholera
    • Centers for Disease Control and Prevention. Current trends update: cholera-Western Hemisphere, and recommendations for treatment of cholera. MMWR Morb Mortal Wkly Rep 40 32 (1991) 562-565
    • (1991) MMWR Morb Mortal Wkly Rep , vol.40 , Issue.32 , pp. 562-565
    • Centers for Disease Control and Prevention1
  • 57
    • 33745400857 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention. Update on cholera vaccine. Available at: http://www.cdc.gov/travel/other/cholera-vaccine.htm. Accessed January 4, 2006.
  • 58
    • 0034978873 scopus 로고    scopus 로고
    • The role of virulence factors in enterohemorrhagic Escherichia coli (EHEC)-associated hemolytic-uremic syndrome
    • Karch H. The role of virulence factors in enterohemorrhagic Escherichia coli (EHEC)-associated hemolytic-uremic syndrome. Semin Thromb Hemost 27 3 (2001) 207-213
    • (2001) Semin Thromb Hemost , vol.27 , Issue.3 , pp. 207-213
    • Karch, H.1
  • 59
    • 10744227433 scopus 로고    scopus 로고
    • Oral therapeutic agents with highly clustered globotriose for treatment of Shiga toxigenic Escherichia coli infections
    • Watanabe M., Matsuoka K., Kita E., et al. Oral therapeutic agents with highly clustered globotriose for treatment of Shiga toxigenic Escherichia coli infections. J Infect Dis 189 3 (2004) 360-368
    • (2004) J Infect Dis , vol.189 , Issue.3 , pp. 360-368
    • Watanabe, M.1    Matsuoka, K.2    Kita, E.3
  • 60
    • 0027185787 scopus 로고
    • Endothelial heterogeneity in Shiga toxin receptors and responses
    • Obrig T.G., Louise C.B., Lingwood C.A., et al. Endothelial heterogeneity in Shiga toxin receptors and responses. J Biol Chem 268 21 (1993) 15484-15488
    • (1993) J Biol Chem , vol.268 , Issue.21 , pp. 15484-15488
    • Obrig, T.G.1    Louise, C.B.2    Lingwood, C.A.3
  • 61
    • 0023930327 scopus 로고
    • Attaching and effacing adherence of Vero cytotoxin-producing Escherichia coli to rabbit intestinal epithelium in vivo
    • Sherman P., Soni R., and Karmali M. Attaching and effacing adherence of Vero cytotoxin-producing Escherichia coli to rabbit intestinal epithelium in vivo. Infect Immun 56 4 (1988) 756-761
    • (1988) Infect Immun , vol.56 , Issue.4 , pp. 756-761
    • Sherman, P.1    Soni, R.2    Karmali, M.3
  • 63
    • 0023854742 scopus 로고
    • Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins
    • Endo Y., Tsurugi K., Yutsudo T., et al. Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. Eur J Biochem 171 1-2 (1988) 45-50
    • (1988) Eur J Biochem , vol.171 , Issue.1-2 , pp. 45-50
    • Endo, Y.1    Tsurugi, K.2    Yutsudo, T.3
  • 64
    • 0023268257 scopus 로고
    • The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis
    • Obrig T.G., Moran T.P., and Brown J.E. The mode of action of Shiga toxin on peptide elongation of eukaryotic protein synthesis. Biochem J 244 2 (1987) 287-294
    • (1987) Biochem J , vol.244 , Issue.2 , pp. 287-294
    • Obrig, T.G.1    Moran, T.P.2    Brown, J.E.3
  • 65
    • 0036033409 scopus 로고    scopus 로고
    • A novel caspase dependent pathway is involved in apoptosis of human endothelial cells by Shiga toxins
    • Yoshida T., Koide N., Sugiyama T., et al. A novel caspase dependent pathway is involved in apoptosis of human endothelial cells by Shiga toxins. Microbiol Immunol 46 10 (2002) 697-700
    • (2002) Microbiol Immunol , vol.46 , Issue.10 , pp. 697-700
    • Yoshida, T.1    Koide, N.2    Sugiyama, T.3
  • 66
    • 14844365246 scopus 로고    scopus 로고
    • Shiga toxins activate translational regulation pathways in intestinal epithelial cells
    • Colpoys W.E., Cochran B.H., Carducci T.M., et al. Shiga toxins activate translational regulation pathways in intestinal epithelial cells. Cell Signal 17 7 (2005) 891-899
    • (2005) Cell Signal , vol.17 , Issue.7 , pp. 891-899
    • Colpoys, W.E.1    Cochran, B.H.2    Carducci, T.M.3
  • 67
    • 2342618145 scopus 로고    scopus 로고
    • Shiga toxin-producing Escherichia coli infection
    • Thorpe C.M. Shiga toxin-producing Escherichia coli infection. Clin Infect Dis 38 9 (2004) 1298-1303
    • (2004) Clin Infect Dis , vol.38 , Issue.9 , pp. 1298-1303
    • Thorpe, C.M.1
  • 68
    • 0028410120 scopus 로고
    • Escherichia coli O157:H7 outbreak linked to home-cooked hamburger-California, July 1993
    • Centers for Disease Control and Prevention. Escherichia coli O157:H7 outbreak linked to home-cooked hamburger-California, July 1993. MMWR Morb Mortal Wkly Rep 43 12 (1994) 213-216
    • (1994) MMWR Morb Mortal Wkly Rep , vol.43 , Issue.12 , pp. 213-216
    • Centers for Disease Control and Prevention1
  • 69
    • 0001250157 scopus 로고
    • Central nervous system involvement in the hemolytic uremic syndrome
    • Kaplan B.S., Trompeter R.S., and Moake J.L. (Eds), Marcel Dekker, New York
    • Siegler R. Central nervous system involvement in the hemolytic uremic syndrome. In: Kaplan B.S., Trompeter R.S., and Moake J.L. (Eds). Hemolytic uremic syndrome and thrombotic thrombocytopenic purpura (1992), Marcel Dekker, New York
    • (1992) Hemolytic uremic syndrome and thrombotic thrombocytopenic purpura
    • Siegler, R.1
  • 70
    • 0034729744 scopus 로고    scopus 로고
    • The risk of the hemolytic-uremic syndrome after antibiotic treatment of Escherichia coli O157:H7 infections
    • Wong C.S., Jelacic S., Habeeb R.L., et al. The risk of the hemolytic-uremic syndrome after antibiotic treatment of Escherichia coli O157:H7 infections. N Engl J Med 342 26 (2000) 1930-1936
    • (2000) N Engl J Med , vol.342 , Issue.26 , pp. 1930-1936
    • Wong, C.S.1    Jelacic, S.2    Habeeb, R.L.3
  • 71
    • 0033772641 scopus 로고    scopus 로고
    • Toxin gene expression by shiga toxin-producing Escherichia coli: the role of antibiotics and the bacterial SOS response
    • Kimmitt P.T., Harwood C.R., and Barer M.R. Toxin gene expression by shiga toxin-producing Escherichia coli: the role of antibiotics and the bacterial SOS response. Emerg Infect Dis 6 5 (2000) 458-465
    • (2000) Emerg Infect Dis , vol.6 , Issue.5 , pp. 458-465
    • Kimmitt, P.T.1    Harwood, C.R.2    Barer, M.R.3
  • 72
    • 0035877769 scopus 로고    scopus 로고
    • University outbreak of calicivirus infection mistakenly attributed to shiga toxin-producing Escherichia coli O157:H7-Virginia, 2000
    • Centers for Disease Control and Prevention. University outbreak of calicivirus infection mistakenly attributed to shiga toxin-producing Escherichia coli O157:H7-Virginia, 2000. MMWR Morb Mortal Wkly Rep 50 23 (2001) 489-491
    • (2001) MMWR Morb Mortal Wkly Rep , vol.50 , Issue.23 , pp. 489-491
    • Centers for Disease Control and Prevention1
  • 73
    • 33745425526 scopus 로고    scopus 로고
    • Braden CLJ, Boothe E, Vugia D, et al. Testing to identify shiga toxin-producing E. coli in HUS patients: FoodNet 1997-2001. Presented at the International Conference on Emerging Infectious Diseases. Atlanta (GA), March 2002.
  • 74
    • 15044364883 scopus 로고    scopus 로고
    • Neurotoxic marine poisoning
    • Isbister G.K., and Kiernan M.C. Neurotoxic marine poisoning. Lancet Neurol 4 4 (2005) 219-228
    • (2005) Lancet Neurol , vol.4 , Issue.4 , pp. 219-228
    • Isbister, G.K.1    Kiernan, M.C.2
  • 75
    • 0024439443 scopus 로고
    • Can ciguatera be a sexually transmitted disease?
    • Lange W.R., Lipkin K.M., and Yang G.C. Can ciguatera be a sexually transmitted disease?. J Toxicol Clin Toxicol 27 3 (1989) 193-197
    • (1989) J Toxicol Clin Toxicol , vol.27 , Issue.3 , pp. 193-197
    • Lange, W.R.1    Lipkin, K.M.2    Yang, G.C.3
  • 76
    • 1342293386 scopus 로고    scopus 로고
    • National Office of Animal and Plant Health, Agriculture, Fisheries and Forestry, Canberra (Australia)
    • Lehane L. Ciguatera fish poisoning: a review in a risk-assessment framework (1999), National Office of Animal and Plant Health, Agriculture, Fisheries and Forestry, Canberra (Australia)
    • (1999) Ciguatera fish poisoning: a review in a risk-assessment framework
    • Lehane, L.1
  • 77
    • 0032753635 scopus 로고    scopus 로고
    • Hyperosmolar D-mannitol reverses the increased membrane excitability and the nodal swelling caused by Caribbean ciguatoxin-1 in single frog myelinated axons
    • Mattei C., Molgo J., Marquais M., et al. Hyperosmolar D-mannitol reverses the increased membrane excitability and the nodal swelling caused by Caribbean ciguatoxin-1 in single frog myelinated axons. Brain Res 847 1 (1999) 50-58
    • (1999) Brain Res , vol.847 , Issue.1 , pp. 50-58
    • Mattei, C.1    Molgo, J.2    Marquais, M.3
  • 78
    • 0034332886 scopus 로고    scopus 로고
    • Ciguatera: recent advances but the risk remains
    • Lehane L., and Lewis R.J. Ciguatera: recent advances but the risk remains. Int J Food Microbiol 61 2-3 (2000) 91-125
    • (2000) Int J Food Microbiol , vol.61 , Issue.2-3 , pp. 91-125
    • Lehane, L.1    Lewis, R.J.2
  • 79
    • 33745384152 scopus 로고    scopus 로고
    • International Programme on Chemical Safety. Environmental health criteria 37. Aquatic (marine and freshwater) biotoxins. Available at: http://www.inchem.org/documents/ehc/ehc/ehc37.htm. Accessed January 4, 2006.
  • 81
    • 0035239230 scopus 로고    scopus 로고
    • The changing face of ciguatera
    • Lewis R.J. The changing face of ciguatera. Toxicon 39 1 (2001) 97-106
    • (2001) Toxicon , vol.39 , Issue.1 , pp. 97-106
    • Lewis, R.J.1
  • 82
    • 33745405709 scopus 로고    scopus 로고
    • Oliver L. Recommendations for use of the Cigua-check test kit. Presented at the Fourth Workshop of the Australian Research Network for Algal Toxins (ARNAT). Townsville, Queensland, Australia. The Australian Institute of Marine Science, July 14, 2002.
  • 83
    • 0036230634 scopus 로고    scopus 로고
    • A pilot study for the detection of acute ciguatera intoxication in human blood
    • Matta J., Navas J., Milad M., et al. A pilot study for the detection of acute ciguatera intoxication in human blood. J Toxicol Clin Toxicol 40 1 (2002) 49-57
    • (2002) J Toxicol Clin Toxicol , vol.40 , Issue.1 , pp. 49-57
    • Matta, J.1    Navas, J.2    Milad, M.3
  • 84
    • 0023906061 scopus 로고
    • Successful treatment of ciguatera fish poisoning with intravenous mannitol
    • Palafox N.A., Jain L.G., Pinano A.Z., et al. Successful treatment of ciguatera fish poisoning with intravenous mannitol. JAMA 259 18 (1988) 2740-2742
    • (1988) JAMA , vol.259 , Issue.18 , pp. 2740-2742
    • Palafox, N.A.1    Jain, L.G.2    Pinano, A.Z.3
  • 85
    • 0037177075 scopus 로고    scopus 로고
    • Ciguatera fish poisoning: a double-blind randomized trial of mannitol therapy
    • Schnorf H., Taurarii M., and Cundy T. Ciguatera fish poisoning: a double-blind randomized trial of mannitol therapy. Neurology 58 6 (2002) 873-880
    • (2002) Neurology , vol.58 , Issue.6 , pp. 873-880
    • Schnorf, H.1    Taurarii, M.2    Cundy, T.3
  • 87
    • 0028841852 scopus 로고
    • The release of glutamate and aspartate from rat brain synaptosomes in response to domoic acid (amnesic shellfish toxin) and kainic acid
    • Brown J.A., and Nijjar M.S. The release of glutamate and aspartate from rat brain synaptosomes in response to domoic acid (amnesic shellfish toxin) and kainic acid. Mol Cell Biochem 151 1 (1995) 49-54
    • (1995) Mol Cell Biochem , vol.151 , Issue.1 , pp. 49-54
    • Brown, J.A.1    Nijjar, M.S.2
  • 88
    • 0025007340 scopus 로고
    • Domoic acid: a dementia-inducing excitotoxic food poison with kainic acid receptor specificity
    • Stewart G.R., Zorumski C.F., Price M.T., et al. Domoic acid: a dementia-inducing excitotoxic food poison with kainic acid receptor specificity. Exp Neurol 110 1 (1990) 127-138
    • (1990) Exp Neurol , vol.110 , Issue.1 , pp. 127-138
    • Stewart, G.R.1    Zorumski, C.F.2    Price, M.T.3
  • 89
    • 33745412448 scopus 로고    scopus 로고
    • Ravn H YT, Ramsdell T. Amnestic shellfish poisoning (ASP). Intergovernmental Oceanographic Commission HAB publication series 1995;1(31).
  • 90
    • 0028181030 scopus 로고
    • Neuroexcitatory and neurotoxic actions of the amnesic shellfish poison, domoic acid
    • Peng Y.G., Taylor T.B., Finch R.E., et al. Neuroexcitatory and neurotoxic actions of the amnesic shellfish poison, domoic acid. Neuroreport 5 8 (1994) 981-985
    • (1994) Neuroreport , vol.5 , Issue.8 , pp. 981-985
    • Peng, Y.G.1    Taylor, T.B.2    Finch, R.E.3
  • 91
    • 0028022567 scopus 로고
    • Domoic acid poisoning
    • Kizer K.W. Domoic acid poisoning. West J Med 161 1 (1994) 59-60
    • (1994) West J Med , vol.161 , Issue.1 , pp. 59-60
    • Kizer, K.W.1
  • 92
    • 0033231633 scopus 로고    scopus 로고
    • Production and characterization of a monoclonal antibody against domoic acid and its application to enzyme immunoassay
    • Kawatsu K., Hamano Y., and Noguchi T. Production and characterization of a monoclonal antibody against domoic acid and its application to enzyme immunoassay. Toxicon 37 11 (1999) 1579-1589
    • (1999) Toxicon , vol.37 , Issue.11 , pp. 1579-1589
    • Kawatsu, K.1    Hamano, Y.2    Noguchi, T.3
  • 93
    • 0025366777 scopus 로고
    • An outbreak of toxic encephalopathy caused by eating mussels contaminated with domoic acid
    • Perl T.M., Bedard L., Kosatsky T., et al. An outbreak of toxic encephalopathy caused by eating mussels contaminated with domoic acid. N Engl J Med 322 25 (1990) 1775-1780
    • (1990) N Engl J Med , vol.322 , Issue.25 , pp. 1775-1780
    • Perl, T.M.1    Bedard, L.2    Kosatsky, T.3
  • 94
    • 0025194683 scopus 로고
    • Neurologic sequelae of domoic acid intoxication due to the ingestion of contaminated mussels
    • Teitelbaum J.S., Zatorre R.J., Carpenter S., et al. Neurologic sequelae of domoic acid intoxication due to the ingestion of contaminated mussels. N Engl J Med 322 25 (1990) 1781-1787
    • (1990) N Engl J Med , vol.322 , Issue.25 , pp. 1781-1787
    • Teitelbaum, J.S.1    Zatorre, R.J.2    Carpenter, S.3
  • 95
    • 0028897258 scopus 로고
    • Temporal lobe epilepsy caused by domoic acid intoxication: evidence for glutamate receptor-mediated excitotoxicity in humans
    • Cendes F., Andermann F., Carpenter S., et al. Temporal lobe epilepsy caused by domoic acid intoxication: evidence for glutamate receptor-mediated excitotoxicity in humans. Ann Neurol 37 1 (1995) 123-126
    • (1995) Ann Neurol , vol.37 , Issue.1 , pp. 123-126
    • Cendes, F.1    Andermann, F.2    Carpenter, S.3
  • 96
    • 0028584267 scopus 로고
    • A competitive enzyme-linked immunoassay for domoic acid determination in human body fluids
    • Smith D.S., and Kitts D.D. A competitive enzyme-linked immunoassay for domoic acid determination in human body fluids. Food Chem Toxicol 32 12 (1994) 1147-1154
    • (1994) Food Chem Toxicol , vol.32 , Issue.12 , pp. 1147-1154
    • Smith, D.S.1    Kitts, D.D.2
  • 97
    • 33745398016 scopus 로고    scopus 로고
    • International Programme on Chemical Safety. Poisons information monograph 67. Available at: http://www.inchem.org/documents/pims/chemical/pim670.htm. Accessed January 4, 2006.
  • 98
    • 0024401174 scopus 로고
    • Kynurenic acid protects against neurotoxicity and lethality of toxic extracts from contaminated Atlantic coast mussels
    • Pinsky C., Glavin G.B., and Bose R. Kynurenic acid protects against neurotoxicity and lethality of toxic extracts from contaminated Atlantic coast mussels. Prog Neuropsychopharmacol Biol Psychiatry 13 3-4 (1989) 595-598
    • (1989) Prog Neuropsychopharmacol Biol Psychiatry , vol.13 , Issue.3-4 , pp. 595-598
    • Pinsky, C.1    Glavin, G.B.2    Bose, R.3
  • 99
    • 0036175222 scopus 로고    scopus 로고
    • A competitive ELISA to detect brevetoxins from Karenia brevis (formerly Gymnodinium breve) in seawater, shellfish, and mammalian body fluid
    • Naar J., Bourdelais A., Tomas C., et al. A competitive ELISA to detect brevetoxins from Karenia brevis (formerly Gymnodinium breve) in seawater, shellfish, and mammalian body fluid. Environ Health Perspect 110 2 (2002) 179-185
    • (2002) Environ Health Perspect , vol.110 , Issue.2 , pp. 179-185
    • Naar, J.1    Bourdelais, A.2    Tomas, C.3
  • 100
    • 21044433427 scopus 로고    scopus 로고
    • Concentration and particle size of airborne toxic algae (brevetoxin) derived from ocean red tide events
    • Cheng Y.S., McDonald J.D., Kracko D., et al. Concentration and particle size of airborne toxic algae (brevetoxin) derived from ocean red tide events. Environ Sci Technol 39 10 (2005) 3443-3449
    • (2005) Environ Sci Technol , vol.39 , Issue.10 , pp. 3443-3449
    • Cheng, Y.S.1    McDonald, J.D.2    Kracko, D.3
  • 101
    • 19044370182 scopus 로고    scopus 로고
    • Natural and derivative brevetoxins: historical background, multiplicity, and effects
    • Baden D.G., Bourdelais A.J., Jacocks H., et al. Natural and derivative brevetoxins: historical background, multiplicity, and effects. Environ Health Perspect 113 5 (2005) 621-625
    • (2005) Environ Health Perspect , vol.113 , Issue.5 , pp. 621-625
    • Baden, D.G.1    Bourdelais, A.J.2    Jacocks, H.3
  • 102
    • 0038358133 scopus 로고    scopus 로고
    • Type B brevetoxins show tissue selectivity for voltage-gated sodium channels: comparison of brain, skeletal muscle and cardiac sodium channels
    • Bottein Dechraoui M.Y., and Ramsdell J.S. Type B brevetoxins show tissue selectivity for voltage-gated sodium channels: comparison of brain, skeletal muscle and cardiac sodium channels. Toxicon 41 7 (2003) 919-927
    • (2003) Toxicon , vol.41 , Issue.7 , pp. 919-927
    • Bottein Dechraoui, M.Y.1    Ramsdell, J.S.2
  • 103
    • 0022901519 scopus 로고
    • Brevetoxins, unique activators of voltage-sensitive sodium channels, bind to specific sites in rat brain synaptosomes
    • Poli M.A., Mende T.J., and Baden D.G. Brevetoxins, unique activators of voltage-sensitive sodium channels, bind to specific sites in rat brain synaptosomes. Mol Pharmacol 30 2 (1986) 129-135
    • (1986) Mol Pharmacol , vol.30 , Issue.2 , pp. 129-135
    • Poli, M.A.1    Mende, T.J.2    Baden, D.G.3
  • 104
    • 0024544737 scopus 로고
    • Brevetoxins: unique polyether dinoflagellate toxins
    • Baden D.G. Brevetoxins: unique polyether dinoflagellate toxins. FASEB J 3 7 (1989) 1807-1817
    • (1989) FASEB J , vol.3 , Issue.7 , pp. 1807-1817
    • Baden, D.G.1
  • 105
    • 0020025693 scopus 로고
    • Toxicity of two toxins from the Florida red tide marine dinoflagellate, Ptychodiscus brevis
    • Baden D.G., and Mende T.J. Toxicity of two toxins from the Florida red tide marine dinoflagellate, Ptychodiscus brevis. Toxicon 20 2 (1982) 457-461
    • (1982) Toxicon , vol.20 , Issue.2 , pp. 457-461
    • Baden, D.G.1    Mende, T.J.2
  • 106
    • 0020432791 scopus 로고
    • Bronchoconstriction caused by Florida red tide toxins
    • Baden D.G., Mende T.J., Bikhazi G., et al. Bronchoconstriction caused by Florida red tide toxins. Toxicon 20 5 (1982) 929-932
    • (1982) Toxicon , vol.20 , Issue.5 , pp. 929-932
    • Baden, D.G.1    Mende, T.J.2    Bikhazi, G.3
  • 107
    • 0142124282 scopus 로고    scopus 로고
    • Measurement of brevetoxin levels by radioimmunoassay of blood collection cards after acute, long-term, and low-dose exposure in mice
    • Woofter R., Dechraoui M.Y., Garthwaite I., et al. Measurement of brevetoxin levels by radioimmunoassay of blood collection cards after acute, long-term, and low-dose exposure in mice. Environ Health Perspect 111 13 (2003) 1595-1600
    • (2003) Environ Health Perspect , vol.111 , Issue.13 , pp. 1595-1600
    • Woofter, R.1    Dechraoui, M.Y.2    Garthwaite, I.3
  • 108
    • 0025997963 scopus 로고
    • An enzyme immunoassay for the detection of Florida red tide brevetoxins
    • Trainer V.L., and Baden D.G. An enzyme immunoassay for the detection of Florida red tide brevetoxins. Toxicon 29 11 (1991) 1387-1394
    • (1991) Toxicon , vol.29 , Issue.11 , pp. 1387-1394
    • Trainer, V.L.1    Baden, D.G.2
  • 109
    • 0033953294 scopus 로고    scopus 로고
    • Neurotoxic shellfish poisoning and brevetoxin metabolites: a case study from Florida
    • Poli M.A., Musser S.M., Dickey R.W., et al. Neurotoxic shellfish poisoning and brevetoxin metabolites: a case study from Florida. Toxicon 38 7 (2000) 981-993
    • (2000) Toxicon , vol.38 , Issue.7 , pp. 981-993
    • Poli, M.A.1    Musser, S.M.2    Dickey, R.W.3
  • 110
    • 33745349104 scopus 로고    scopus 로고
    • Australia New Zealand Food Authority. Shellfish toxins in food. A toxicological review and risk assessment. Technical report series number 14. p. 13-5. Available at: http://www.anzfa.gov. Accessed January 3, 2005.
  • 111
    • 0015921666 scopus 로고
    • Puffer fish poisoning
    • Sorokin M. Puffer fish poisoning. Med J Aust 1 19 (1973) 957
    • (1973) Med J Aust , vol.1 , Issue.19 , pp. 957
    • Sorokin, M.1
  • 112
    • 1842762939 scopus 로고    scopus 로고
    • Paralytic complications of puffer fish (tetrodotoxin) poisoning
    • Ahasan H.A., Mamun A.A., Karim S.R., et al. Paralytic complications of puffer fish (tetrodotoxin) poisoning. Singapore Med J 45 2 (2004) 73-74
    • (2004) Singapore Med J , vol.45 , Issue.2 , pp. 73-74
    • Ahasan, H.A.1    Mamun, A.A.2    Karim, S.R.3
  • 113
    • 33745379744 scopus 로고    scopus 로고
    • Tetrodotoxin. Available at: http://www.pufferfish.co.uk/aquaria.species/general/tetro.htm. Accessed January 3, 2005.
  • 114
    • 0023377591 scopus 로고
    • Marine bacteria which produce tetrodotoxin
    • Simidu U., Noguchi T., Hwang D.F., et al. Marine bacteria which produce tetrodotoxin. Appl Environ Microbiol 53 7 (1987) 1714-1715
    • (1987) Appl Environ Microbiol , vol.53 , Issue.7 , pp. 1714-1715
    • Simidu, U.1    Noguchi, T.2    Hwang, D.F.3
  • 115
    • 14244266197 scopus 로고    scopus 로고
    • Two novel species of tetrodotoxin-producing bacteria isolated from toxic marine puffer fishes
    • Yu C.F., Yu P.H., Chan P.L., et al. Two novel species of tetrodotoxin-producing bacteria isolated from toxic marine puffer fishes. Toxicon 44 6 (2004) 641-647
    • (2004) Toxicon , vol.44 , Issue.6 , pp. 641-647
    • Yu, C.F.1    Yu, P.H.2    Chan, P.L.3
  • 116
    • 33745375582 scopus 로고    scopus 로고
    • Tetrodotoxin: essentail data. Available at: http://www.cbwinfo.com/Biological/Toxins/TTX.html. Accessed January 3, 2006.
  • 117
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele S., and Catterall W.A. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie 82 9-10 (2000) 883-892
    • (2000) Biochimie , vol.82 , Issue.9-10 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 118
    • 14844318086 scopus 로고    scopus 로고
    • Acute tetrodotoxin-induced neurotoxicity after ingestion of puffer fish
    • Kiernan M.C., Isbister G.K., Lin C.S., et al. Acute tetrodotoxin-induced neurotoxicity after ingestion of puffer fish. Ann Neurol 57 3 (2005) 339-348
    • (2005) Ann Neurol , vol.57 , Issue.3 , pp. 339-348
    • Kiernan, M.C.1    Isbister, G.K.2    Lin, C.S.3
  • 119
    • 0033067902 scopus 로고    scopus 로고
    • Tetrodotoxin intoxication in a uraemic patient
    • Lan M.Y., Lai S.L., Chen S.S., et al. Tetrodotoxin intoxication in a uraemic patient. J Neurol Neurosurg Psychiatry 67 1 (1999) 127-128
    • (1999) J Neurol Neurosurg Psychiatry , vol.67 , Issue.1 , pp. 127-128
    • Lan, M.Y.1    Lai, S.L.2    Chen, S.S.3
  • 120
    • 33745392828 scopus 로고    scopus 로고
    • Toxnet. Available at: http://toxnet.nlm.nih.gov/cgi-bin/sis/search/f?./temp/∼DPklSV:1. Accessed January 5, 2006.
  • 122
    • 4644282978 scopus 로고    scopus 로고
    • Use of high performance liquid chromatography to measure tetrodotoxin in serum and urine of poisoned patients
    • O'Leary M.A., Schneider J.J., and Isbister G.K. Use of high performance liquid chromatography to measure tetrodotoxin in serum and urine of poisoned patients. Toxicon 44 5 (2004) 549-553
    • (2004) Toxicon , vol.44 , Issue.5 , pp. 549-553
    • O'Leary, M.A.1    Schneider, J.J.2    Isbister, G.K.3
  • 123
    • 33745390565 scopus 로고    scopus 로고
    • Saxitoxins. Available at: http://www.aims.gov.au/arnat/arnat-0008.htm. Accessed January 9, 2006.
  • 124
    • 20444439621 scopus 로고    scopus 로고
    • A rapid detection method for paralytic shellfish poisoning toxins by cell bioassay
    • Okumura M., Tsuzuki H., and Tomita B. A rapid detection method for paralytic shellfish poisoning toxins by cell bioassay. Toxicon 46 1 (2005) 93-98
    • (2005) Toxicon , vol.46 , Issue.1 , pp. 93-98
    • Okumura, M.1    Tsuzuki, H.2    Tomita, B.3
  • 125
    • 20544437789 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography-mass spectrometry for the analysis of paralytic shellfish poisoning (PSP) toxins
    • Dell'Aversano C., Hess P., and Quilliam M.A. Hydrophilic interaction liquid chromatography-mass spectrometry for the analysis of paralytic shellfish poisoning (PSP) toxins. J Chromatogr A 1081 2 (2005) 190-201
    • (2005) J Chromatogr A , vol.1081 , Issue.2 , pp. 190-201
    • Dell'Aversano, C.1    Hess, P.2    Quilliam, M.A.3
  • 126
    • 20244383475 scopus 로고    scopus 로고
    • Gonyautoxin: new treatment for healing acute and chronic anal fissures
    • Garrido R., Lagos N., Lattes K., et al. Gonyautoxin: new treatment for healing acute and chronic anal fissures. Dis Colon Rectum 48 2 (2005) 335-340
    • (2005) Dis Colon Rectum , vol.48 , Issue.2 , pp. 335-340
    • Garrido, R.1    Lagos, N.2    Lattes, K.3
  • 127
    • 0347758398 scopus 로고    scopus 로고
    • Saxitoxin blocks L-type ICa
    • Su Z., Sheets M., Ishida H., et al. Saxitoxin blocks L-type ICa. J Pharmacol Exp Ther 308 1 (2004) 324-329
    • (2004) J Pharmacol Exp Ther , vol.308 , Issue.1 , pp. 324-329
    • Su, Z.1    Sheets, M.2    Ishida, H.3
  • 128
    • 0038580639 scopus 로고    scopus 로고
    • Saxitoxin is a gating modifier of HERG K+ channels
    • Wang J., Salata J.J., and Bennett P.B. Saxitoxin is a gating modifier of HERG K+ channels. J Gen Physiol 121 6 (2003) 583-598
    • (2003) J Gen Physiol , vol.121 , Issue.6 , pp. 583-598
    • Wang, J.1    Salata, J.J.2    Bennett, P.B.3
  • 129
    • 33745424490 scopus 로고    scopus 로고
    • Flemming LE. Paralytic shellfish poisoning. Available at: http://www.whoi.edu/redtide/illness/psp.html. Accessed January 10, 2006.
  • 130
    • 33745342940 scopus 로고    scopus 로고
    • Saxitoxin. In: Robinson J, editor. Public health response to biological and chemical weapons. WHO guidance. 2nd edition. Geneva (Switzerland): World Health Organization.
  • 131
    • 0037736040 scopus 로고    scopus 로고
    • National Office of Animal and Plant Health, Agriculture, Fisheries, and Forestry, Canberra (Australia)
    • Lehane L. Paralytic shellfish poisoning: a review (2000), National Office of Animal and Plant Health, Agriculture, Fisheries, and Forestry, Canberra (Australia)
    • (2000) Paralytic shellfish poisoning: a review
    • Lehane, L.1
  • 132
    • 0030958245 scopus 로고    scopus 로고
    • Hypertension and identification of toxin in human urine and serum following a cluster of mussel-associated paralytic shellfish poisoning outbreaks
    • Gessner B.D., Bell P., Doucette G.J., et al. Hypertension and identification of toxin in human urine and serum following a cluster of mussel-associated paralytic shellfish poisoning outbreaks. Toxicon 35 5 (1997) 711-722
    • (1997) Toxicon , vol.35 , Issue.5 , pp. 711-722
    • Gessner, B.D.1    Bell, P.2    Doucette, G.J.3
  • 133
    • 33745409522 scopus 로고    scopus 로고
    • Vangelova L. Botulinum toxin: a poison that can heal. 1998. Available at: www.fda.gov/fdac/features/095_bot.html. Accessed January 3, 2006.
  • 135
    • 2342450639 scopus 로고    scopus 로고
    • Effects of cholera toxin on innate and adaptive immunity and its application as an immunomodulatory agent
    • Lavelle E.C., Jarnicki A., McNeela E., et al. Effects of cholera toxin on innate and adaptive immunity and its application as an immunomodulatory agent. J Leukoc Biol 75 5 (2004) 756-763
    • (2004) J Leukoc Biol , vol.75 , Issue.5 , pp. 756-763
    • Lavelle, E.C.1    Jarnicki, A.2    McNeela, E.3
  • 136
    • 0030859151 scopus 로고    scopus 로고
    • Modulation of B-cell activation by the B subunit of Escherichia coli enterotoxin: receptor interaction up-regulates MHC class II, B7, CD40, CD25 and ICAM-1
    • Nashar T.O., Hirst T.R., and Williams N.A. Modulation of B-cell activation by the B subunit of Escherichia coli enterotoxin: receptor interaction up-regulates MHC class II, B7, CD40, CD25 and ICAM-1. Immunology 91 4 (1997) 572-578
    • (1997) Immunology , vol.91 , Issue.4 , pp. 572-578
    • Nashar, T.O.1    Hirst, T.R.2    Williams, N.A.3


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