메뉴 건너뛰기




Volumn 2, Issue 10, 2010, Pages 2359-2410

Diversity and impact of prokaryotic toxins on aquatic environments: A review

Author keywords

Aquatic; Diversity of toxins; Impact of toxins; Molecular mechanisms; Prokaryotes

Indexed keywords

ACT TOXIN; ANATOXIN A; ANATOXIN A(S); ANTILLATOXIN; BACTERIAL TOXIN; BACTERIUM LIPOPOLYSACCHARIDE; BARBAMIDE; CHOLERA TOXIN; CHOLIX TOXIN; CURACIN A; CYANOTOXIN; CYLINDROSPERMOPSIN; CYTOTOXIN; DIPHTHERIA TOXIN; EXOA TOXIN; EXOTOXIN; HEPATOTOXIN; HOMOANATOXIN A; JAMAICAMIDE A; JAMAICAMIDE B; KALKITOXIN; LIPOPEPTIDE; MICROCYSTIN; NEUROTOXIN; NODULARIN; REPEATS IN TOXIN EXOPROTEIN; RTXA1 TOXIN; SAXITOXIN; UNCLASSIFIED DRUG; UNINDEXED DRUG; VEROTOXIN;

EID: 79952097439     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins2102359     Document Type: Review
Times cited : (73)

References (247)
  • 1
    • 0003584718 scopus 로고    scopus 로고
    • Rappuoli, R., Montecucco, C., Eds.; Sambrook & Tooze Publications at Oxford University Press: New York, NY, USA
    • Guidebook to Protein Toxins and Their Use in Cell Biology; Rappuoli, R., Montecucco, C., Eds.; Sambrook & Tooze Publications at Oxford University Press: New York, NY, USA, 1997.
    • (1997) Guidebook to Protein Toxins and Their Use In Cell Biology
  • 3
    • 46349102898 scopus 로고    scopus 로고
    • Neurotoxins from marine dinoflagellates: A brief review
    • Wang, D. Neurotoxins from marine dinoflagellates: A brief review. Mar. Drugs 2008, 6, 349-371.
    • (2008) Mar. Drugs , vol.6 , pp. 349-371
    • Wang, D.1
  • 5
    • 51549107755 scopus 로고    scopus 로고
    • A review of fungal phytotoxins: From basic studies to practical use
    • Berestetskiy, A.O. A review of fungal phytotoxins: from basic studies to practical use. Appl. Biochem. Microbiol. 2008, 44, 453-465.
    • (2008) Appl. Biochem. Microbiol , vol.44 , pp. 453-465
    • Berestetskiy, A.O.1
  • 6
    • 0030900285 scopus 로고    scopus 로고
    • Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells
    • Zitzer, A.; Wassenaar, T.; Walev, I.; Bhakdi, S. Potent membrane-permeabilizing and cytocidal action of Vibrio cholerae cytolysin on human intestinal cells. Infect. Immun. 1997, 65, 1293-1298.
    • (1997) Infect. Immun , vol.65 , pp. 1293-1298
    • Zitzer, A.1    Wassenaar, T.2    Walev, I.3    Bhakdi, S.4
  • 7
    • 0034657922 scopus 로고    scopus 로고
    • Role of tetanus neurotoxin insensitive vesicle-associated membrane protein (ti-vamp) in vesicular transport mediating neurite outgrowth
    • Martinez-Arca, S.; Alberts, P.; Zahraoui, A.; Louvard, D.; Galli, T. Role of tetanus neurotoxin insensitive vesicle-associated membrane protein (TI-VAMP) in vesicular transport mediating neurite outgrowth. J. Cell Biol. 2000, 149, 889-900.
    • (2000) J. Cell Biol , vol.149 , pp. 889-900
    • Martinez-Arca, S.1    Alberts, P.2    Zahraoui, A.3    Louvard, D.4    Galli, T.5
  • 8
    • 67249103849 scopus 로고    scopus 로고
    • Engineering botulinum neurotoxin to extend therapeutic intervention
    • Chen, S.; Barbieri, J.T. Engineering botulinum neurotoxin to extend therapeutic intervention. Proc. Natl. Acad. Sci. USA 2009, 106, 9180-9184.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 9180-9184
    • Chen, S.1    Barbieri, J.T.2
  • 10
    • 33646457879 scopus 로고    scopus 로고
    • Shiga toxin 1-induced cytokine production is mediated by map kinase pathways and translation initiation factor eif4e in the macrophage-likethp-1 cell line
    • Cherla, R.P.; Lee, S.-Y.; Mees, P.L.; Tesh, V.L. Shiga toxin 1-induced cytokine production is mediated by MAP kinase pathways and translation initiation factor eIF4E in the macrophage-likeTHP-1 cell line. J. Leukoc. Biol. 2006, 79, 397-407.
    • (2006) J. Leukoc. Biol , vol.79 , pp. 397-407
    • Cherla, R.P.1    Lee, S.-Y.2    Mees, P.L.3    Tesh, V.L.4
  • 11
    • 0026333997 scopus 로고
    • Lipid interaction of pseudomonas aeruginosa exotoxin a. acid-triggered permeabilization and aggregation of lipid vesicles
    • Menestrina, G.; Pederzolli, C.; Forti, S.; Gambale, F. Lipid interaction of Pseudomonas aeruginosa exotoxin A. Acid-triggered permeabilization and aggregation of lipid vesicles. Biophys. J. 1991, 60, 1388-1400.
    • (1991) Biophys. J , vol.60 , pp. 1388-1400
    • Menestrina, G.1    Pederzolli, C.2    Forti, S.3    Gambale, F.4
  • 12
    • 0025893128 scopus 로고
    • Characterization of rabbit lleal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G protein
    • Pothoulakis, C.; LaMont, J.T.; Eglow, R.; Gao, N.; Rubins, J.B.; Theoharides, T.C.; Dickey, B.F. Characterization of rabbit lleal receptors for Clostridium difficile toxin A. Evidence for a receptor-coupled G protein. J. Clin. Invest. 1991, 88, 119-125.
    • (1991) J. Clin. Invest , vol.88 , pp. 119-125
    • Pothoulakis, C.1    Lamont, J.T.2    Eglow, R.3    Gao, N.4    Rubins, J.B.5    Theoharides, T.C.6    Dickey, B.F.7
  • 13
    • 0024244214 scopus 로고
    • Cytoskeletal changes induced in HEp-2 cells by the cytotoxic necrotizing factor of Escherichia coli
    • Fiorentini, C.; Arancia, G.; Caprioli, A.; Falbo, V.; Ruggeri, F.M.; Donelli, G. Cytoskeletal changes induced in HEp-2 cells by the cytotoxic necrotizing factor of Escherichia coli. Toxicon 1988, 26, 1047-1056.
    • (1988) Toxicon , vol.26 , pp. 1047-1056
    • Fiorentini, C.1    Arancia, G.2    Caprioli, A.3    Falbo, V.4    Ruggeri, F.M.5    Donelli, G.6
  • 14
    • 77955843274 scopus 로고    scopus 로고
    • Neurotoxic cyanobacterial toxins
    • DOI: 10.1016/j.toxicon.2009.07.036
    • Aráoz, R.; Molgó, J.; Tandeau de Marsac, N. Neurotoxic cyanobacterial toxins. Toxicon 2010,56, 813-828, DOI: 10.1016/j.toxicon.2009.07.036.
    • (2010) Toxicon , vol.56 , pp. 813-828
    • Aráoz, R.1    Molgó, J.2    de Marsac, T.N.3
  • 15
    • 84989617497 scopus 로고
    • Species usage, concept, and evolution in the cyanobacteria (blue-green algae)
    • Castenholz, R.W. Species usage, concept, and evolution in the cyanobacteria (blue-green algae). J. Phycol. 1992, 28, 737-745.
    • (1992) J. Phycol , vol.28 , pp. 737-745
    • Castenholz, R.W.1
  • 16
    • 0000642932 scopus 로고    scopus 로고
    • The fossil record: Tracing the roots of the cyanobacterial lineage
    • Whintton, B.A., Potts, M., Eds.; Kluwer: Dordrecht, the Netherlands
    • Schopf, J.W. The fossil record: tracing the roots of the cyanobacterial lineage. In The Ecology of Cyanobacteria; Whintton, B.A., Potts, M., Eds.; Kluwer: Dordrecht, the Netherlands, 2000; pp. 13-35.
    • (2000) The Ecology of Cyanobacteria , pp. 13-35
    • Schopf, J.W.1
  • 17
    • 0000102730 scopus 로고
    • Group i. cyanobacteria
    • Krieg, N.R., Holt, J.G., Eds.; Williams & Wilkins: Baltimore, MD, USA
    • Castenholz, R.W.; Waterbury, J.B. Group I. Cyanobacteria. In Bergey's Manual of Systematic Bacteriology; Krieg, N.R., Holt, J.G., Eds.; Williams & Wilkins: Baltimore, MD, USA, 1989; Volume 3, pp. 1710-1728.
    • (1989) Bergey's Manual of Systematic Bacteriology , vol.3 , pp. 1710-1728
    • Castenholz, R.W.1    Waterbury, J.B.2
  • 19
    • 79952086660 scopus 로고
    • Prokaryotic algae (cyanophyta, prochlorophyta)
    • 2nd ed.; WCB Publishers: Boston, MA, USA
    • Sze, P. Prokaryotic algae (Cyanophyta, Prochlorophyta). In A Biology of the Algae, 2nd ed.; WCB Publishers: Boston, MA, USA, 1986; pp. 19-34.
    • (1986) A Biology of the Algae , pp. 19-34
    • Sze, P.1
  • 23
    • 14644411765 scopus 로고    scopus 로고
    • Cyanobacterial toxins: Risk management for health protection
    • Codd, G.A.; Morrison, L.F.; Metcalf, J.S. Cyanobacterial toxins: risk management for health protection. Toxicol. Appl. Pharmacol. 2005, 203, 264-272.
    • (2005) Toxicol. Appl. Pharmacol , vol.203 , pp. 264-272
    • Codd, G.A.1    Morrison, L.F.2    Metcalf, J.S.3
  • 24
    • 51149149298 scopus 로고
    • Poisonous Australian lake
    • Francis, G. Poisonous Australian lake. Nature 1878, 18, 11-12.
    • (1878) Nature , vol.18 , pp. 11-12
    • Francis, G.1
  • 25
    • 0023998873 scopus 로고
    • Anticholinesterase poisonings in dogs from a cyanobacterial (blue-green algae) bloom dominated by Anabaena flos-aquae
    • Mahmood, N.A.; Carmichael, W.W.; Pfahler, D. Anticholinesterase poisonings in dogs from a cyanobacterial (blue-green algae) bloom dominated by Anabaena flos-aquae. Am. J. Vet. Res.1988, 49, 500-503.
    • (1988) Am. J. Vet. Res , vol.49 , pp. 500-503
    • Mahmood, N.A.1    Carmichael, W.W.2    Pfahler, D.3
  • 27
    • 0026651340 scopus 로고
    • Cyanobacterial secondary metabolites-the cyanotoxins
    • Carmichael, W.W. Cyanobacterial secondary metabolites-the cyanotoxins. J. Appl. Bacteriol.1992, 72, 445-459.
    • (1992) J. Appl. Bacteriol , vol.72 , pp. 445-459
    • Carmichael, W.W.1
  • 28
    • 0028884107 scopus 로고
    • Sheep mortality associated with paralytic shellfish poisons from the cyanobacterium Anabaena circinalis
    • Negri, A.P.; Jones, G.J.; Hindmarsh, M. Sheep mortality associated with paralytic shellfish poisons from the cyanobacterium Anabaena circinalis. Toxicon 1995, 33, 1321-1329.
    • (1995) Toxicon , vol.33 , pp. 1321-1329
    • Negri, A.P.1    Jones, G.J.2    Hindmarsh, M.3
  • 29
    • 0031172833 scopus 로고    scopus 로고
    • Detection of an anatoxin-a(s)-like anticholinesterase in natural blooms and cultures of cyanobacteria/blue-green algae from Danish lakes and in the stomach contents of poisoned birds
    • Henriksen, P.; Carmichael, W.W.; An, J.; Moestrup, Ø. Detection of an anatoxin-a(s)-like anticholinesterase in natural blooms and cultures of cyanobacteria/blue-green algae from Danish lakes and in the stomach contents of poisoned birds. Toxicon 1997, 35, 901-913.
    • (1997) Toxicon , vol.35 , pp. 901-913
    • Henriksen, P.1    Carmichael, W.W.2    An, J.3    Moestrup, O.4
  • 30
    • 0032881298 scopus 로고    scopus 로고
    • Possible cause of unnatural mass death of wild birds in a pond in Nishinomiya, Japan: Sudden appearance of toxic cyanobacteria
    • Matsunaga, H.; Harada, K.-I.; Senma, M.; Ito, Y.; Yasuda, N.; Ushida, S.; Kimura, Y. Possible cause of unnatural mass death of wild birds in a pond in Nishinomiya, Japan: sudden appearance of toxic cyanobacteria. Nat. Toxins 1999, 7, 81-84.
    • (1999) Nat. Toxins , vol.7 , pp. 81-84
    • Matsunaga, H.1    Harada, K.-I.2    Senma, M.3    Ito, Y.4    Yasuda, N.5    Ushida, S.6    Kimura, Y.7
  • 37
    • 0029035276 scopus 로고
    • Uptake and depuration of the heptapeptide toxin microcystin-LR in Mytilus galloprovincialis
    • Vasconcelos, V.M. Uptake and depuration of the heptapeptide toxin microcystin-LR in Mytilus galloprovincialis. Aquat. Toxicol. 1995, 32, 227-237.
    • (1995) Aquat. Toxicol , vol.32 , pp. 227-237
    • Vasconcelos, V.M.1
  • 38
    • 0032961714 scopus 로고    scopus 로고
    • Dynamic of microcystins in the mussel Mytilus galloprovincialis
    • Amorim, A.; Vasconcelos, V. Dynamic of microcystins in the mussel Mytilus galloprovincialis. Toxicon 1999, 37, 1041-1052.
    • (1999) Toxicon , vol.37 , pp. 1041-1052
    • Amorim, A.1    Vasconcelos, V.2
  • 39
    • 14644425290 scopus 로고    scopus 로고
    • Ecotoxicological effects of selected cyanobacterial secondary metabolites a short review
    • Wiegand, C.; Pflugmacher, S. Ecotoxicological effects of selected cyanobacterial secondary metabolites a short review. Toxicol. Appl. Pharmacol. 2005, 203, 201-218.
    • (2005) Toxicol. Appl. Pharmacol , vol.203 , pp. 201-218
    • Wiegand, C.1    Pflugmacher, S.2
  • 40
  • 41
    • 0034908990 scopus 로고    scopus 로고
    • Impact of a toxic and a non-toxic strain of microcystis aeruginosa on the crayfish procambarus clarkii
    • Vasconcelos, V.; Oliveira, S.; Teles, F.O. Impact of a toxic and a non-toxic strain of Microcystis aeruginosa on the crayfish Procambarus clarkii. Toxicon 2001, 39, 1461-1470.
    • (2001) Toxicon , vol.39 , pp. 1461-1470
    • Vasconcelos, V.1    Oliveira, S.2    Teles, F.O.3
  • 42
    • 34347382759 scopus 로고    scopus 로고
    • Phytotoxic effects of cyanobacteria extract on the aquatic plant Lemna gibba: Microcystin accumulation, detoxication and oxidative stress induction
    • Saqrane, S.; El ghzali, I.; Ouahid, Y.; El Hassni, M.; El Hadrami, I.; Bouarab, L.; del Campo, F.F.; Oudra, B.; Vasconcelos, V. Phytotoxic effects of cyanobacteria extract on the aquatic plant Lemna gibba: Microcystin accumulation, detoxication and oxidative stress induction. Aquat. Toxicol. 2007, 83, 284-294.
    • (2007) Aquat. Toxicol , vol.83 , pp. 284-294
    • Saqrane, S.1    El ghzali, I.2    Ouahid, Y.3    El Hassni, M.4    El Hadrami, I.5    Bouarab, L.6    del Campo, F.F.7    Oudra, B.8    Vasconcelos, V.9
  • 43
    • 6944239771 scopus 로고    scopus 로고
    • Accumulation of paralytic shellfish toxins (pst) from the cyanobacterium aphanizomenon issatschenkoi by the cladoceran daphnia magna
    • Nogueira, I.C.G.; Pereira, P.; Dias, E.; Pflugmacher, S.; Wiegand, C.; Franca, S.; Vasconcelos, V.M. Accumulation of paralytic shellfish toxins (PST) from the cyanobacterium Aphanizomenon issatschenkoi by the cladoceran Daphnia magna. Toxicon 2004, 44, 773-780.
    • (2004) Toxicon , vol.44 , pp. 773-780
    • Nogueira, I.C.G.1    Pereira, P.2    Dias, E.3    Pflugmacher, S.4    Wiegand, C.5    Franca, S.6    Vasconcelos, V.M.7
  • 44
    • 0029015858 scopus 로고
    • Bioaccumulation of paralytic shellfish poisoning (psp) toxins from the cyanobacterium Anabaena circinalis by the freshwater mussel Alathyria condola
    • Negri, A.P.; Jones, G.J. Bioaccumulation of paralytic shellfish poisoning (PSP) toxins from the cyanobacterium Anabaena circinalis by the freshwater mussel Alathyria condola. Toxicon 1995, 33, 667-678.
    • (1995) Toxicon , vol.33 , pp. 667-678
    • Negri, A.P.1    Jones, G.J.2
  • 45
    • 2642567509 scopus 로고    scopus 로고
    • Accumulation and depuration of cyanobacterial paralytic shellfish toxins by the freshwater mussel Anodonta cygnea
    • Pereira, P.; Dias, E.; Franca, S.; Pereira, E.; Carolino, M.; Vasconcelos, V. Accumulation and depuration of cyanobacterial paralytic shellfish toxins by the freshwater mussel Anodonta cygnea. Aquat. Toxicol. 2004, 68, 339-350.
    • (2004) Aquat. Toxicol , vol.68 , pp. 339-350
    • Pereira, P.1    Dias, E.2    Franca, S.3    Pereira, E.4    Carolino, M.5    Vasconcelos, V.6
  • 46
    • 1442335375 scopus 로고    scopus 로고
    • Accumulation and depuration of the cyanobacterial toxin cylindrospermopsin in the freshwater mussel Anodonta cygnea
    • Saker, M.L.; Metcalf, J.S.; Codd, G.A.; Vasconcelos, V.M. Accumulation and depuration of the cyanobacterial toxin cylindrospermopsin in the freshwater mussel Anodonta cygnea. Toxicon 2004, 43, 185-194.
    • (2004) Toxicon , vol.43 , pp. 185-194
    • Saker, M.L.1    Metcalf, J.S.2    Codd, G.A.3    Vasconcelos, V.M.4
  • 47
    • 31544477132 scopus 로고    scopus 로고
    • Cyanobacterial toxins-occurrence, biosynthesis and impact on human affairs
    • Dittmann, E.; Wiegand, C. Cyanobacterial toxins-occurrence, biosynthesis and impact on human affairs. Mol. Nutr. Food Res. 2006, 50, 7-17.
    • (2006) Mol. Nutr. Food Res , vol.50 , pp. 7-17
    • Dittmann, E.1    Wiegand, C.2
  • 48
    • 33745795644 scopus 로고    scopus 로고
    • Recreational and occupational field exposure to freshwater cyanobacteria-a review of anecdotal and case reports, epidemiological studies and the challenges for epidemiologic assessment
    • Stewart, I.; Webb, P.; Schluter, P.; Shaw, G. Recreational and occupational field exposure to freshwater cyanobacteria-a review of anecdotal and case reports, epidemiological studies and the challenges for epidemiologic assessment. Environ. Health 2006, 5, 6.
    • (2006) Environ. Health , vol.5 , pp. 6
    • Stewart, I.1    Webb, P.2    Schluter, P.3    Shaw, G.4
  • 49
    • 38949089033 scopus 로고    scopus 로고
    • Heterocycles from cyanobacteria
    • Okino, T. Heterocycles from Cyanobacteria. Top. Heterocycl. Chem. 2006, 5, 1-19.
    • (2006) Top. Heterocycl. Chem , vol.5 , pp. 1-19
    • Okino, T.1
  • 50
    • 46349086410 scopus 로고    scopus 로고
    • Cyanobacterial toxins as allelochemicals with potential applications as algaecides, herbicides and insecticides
    • Berry, J.P.; Gantar, M.; Perez, M.H.; Berry, G.; Noriega, F.G. Cyanobacterial toxins as allelochemicals with potential applications as algaecides, herbicides and insecticides. Mar. Drugs 2008, 6, 117-146.
    • (2008) Mar. Drugs , vol.6 , pp. 117-146
    • Berry, J.P.1    Gantar, M.2    Perez, M.H.3    Berry, G.4    Noriega, F.G.5
  • 51
    • 59649115168 scopus 로고    scopus 로고
    • Bioactive compounds produced by cyanobacteria
    • Herrero, A., Flores, E., Eds.; Caister Academic Press: Norfolk, UV, USA
    • Sivonen, K.; Börner, T. Bioactive compounds produced by cyanobacteria. In The Cyanobacteria: Molecular Biology, Genomics and Evolution; Herrero, A., Flores, E., Eds.; Caister Academic Press: Norfolk, UV, USA, 2008; pp. 159-197.
    • (2008) The Cyanobacteria: Molecular Biology, Genomics and Evolution , pp. 159-197
    • Sivonen, K.1    Börner, T.2
  • 52
    • 33744965454 scopus 로고    scopus 로고
    • Cyanobacterial peptides-Nature's own combinatorial biosynthesis
    • Welker, M.; von Döhren, H. Cyanobacterial peptides-Nature's own combinatorial biosynthesis. FEMS Microbiol. Rev. 2006, 30, 530-563.
    • (2006) FEMS Microbiol. Rev , vol.30 , pp. 530-563
    • Welker, M.1    von Döhren, H.2
  • 53
    • 0030994088 scopus 로고    scopus 로고
    • Variation of microcystins, cyanobacterial hepatotoxins, in Anabaena spp. as a function of growth stimuli
    • Rapala, J.; Sivonen, K.; Lyra, C.; Niemelä, S.I. Variation of microcystins, cyanobacterial hepatotoxins, in Anabaena spp. as a function of growth stimuli. Appl. Environ. Microbiol. 1997, 63, 2206-2212.
    • (1997) Appl. Environ. Microbiol , vol.63 , pp. 2206-2212
    • Rapala, J.1    Sivonen, K.2    Lyra, C.3    Niemelä, S.I.4
  • 54
    • 3142757234 scopus 로고    scopus 로고
    • Diversity and distribution of Microcystis (Cyanobacteria) oligopeptide chemotypes from natural communities studied by single-colony mass spectrometry
    • Welker, M.; Brunke, M.; Preussel, K.; Lippert, I.; von Döhren, H. Diversity and distribution of Microcystis (Cyanobacteria) oligopeptide chemotypes from natural communities studied by single-colony mass spectrometry. Microbiology 2004, 150, 1785-1796.
    • (2004) Microbiology , vol.150 , pp. 1785-1796
    • Welker, M.1    Brunke, M.2    Preussel, K.3    Lippert, I.4    von Döhren, H.5
  • 55
    • 1242274446 scopus 로고    scopus 로고
    • Characteristics of microcystin production cell cycle of Microcystis viridis
    • Kameyama, K.; Sugiura, N.; Inamori, Y.; Maekawa, T. Characteristics of microcystin production cell cycle of Microcystis viridis. Environ. Toxicol. 2004, 19, 20-25.
    • (2004) Environ. Toxicol , vol.19 , pp. 20-25
    • Kameyama, K.1    Sugiura, N.2    Inamori, Y.3    Maekawa, T.4
  • 56
    • 25844501507 scopus 로고    scopus 로고
    • Variation between strains of the cyanobacterium Microcystis aeruginosa isolated from a Portuguese river
    • Saker, M.L.; Fastner, J.; Dittmann, E.; Christiansen, G.; Vasconcelos, V.M. Variation between strains of the cyanobacterium Microcystis aeruginosa isolated from a Portuguese river. J. Appl. Microbiol. 2005, 99, 749-757.
    • (2005) J. Appl. Microbiol , vol.99 , pp. 749-757
    • Saker, M.L.1    Fastner, J.2    Dittmann, E.3    Christiansen, G.4    Vasconcelos, V.M.5
  • 57
    • 0242349148 scopus 로고    scopus 로고
    • Cylindrospermopsin occurrence in two German lakes and preliminary assessment of toxicity and toxin production of Cylindrospermopsis raciborskii (cyanobacteria) isolates
    • Fastner, J.; Heinze, R.; Humpage, A.R.; Mischke, U.; Eaglesham, G.K.; Chorus, I. Cylindrospermopsin occurrence in two German lakes and preliminary assessment of toxicity and toxin production of Cylindrospermopsis raciborskii (cyanobacteria) isolates. Toxicon 2003, 42, 313-321.
    • (2003) Toxicon , vol.42 , pp. 313-321
    • Fastner, J.1    Heinze, R.2    Humpage, A.R.3    Mischke, U.4    Eaglesham, G.K.5    Chorus, I.6
  • 58
    • 0038706470 scopus 로고    scopus 로고
    • First report and toxicological assessment of the cyanobacterium Cylindrospermopsis raciborskii from Portuguese freshwaters
    • Saker, M.L.; Nogueira, I.C.G.; Vasconcelos, V.M.; Neilan, B.A.; Eaglesham, G.H.; Pereira, P. First report and toxicological assessment of the cyanobacterium Cylindrospermopsis raciborskii from Portuguese freshwaters. Ecotoxicol. Environ. Saf. 2003, 55, 243-250.
    • (2003) Ecotoxicol. Environ. Saf , vol.55 , pp. 243-250
    • Saker, M.L.1    Nogueira, I.C.G.2    Vasconcelos, V.M.3    Neilan, B.A.4    Eaglesham, G.H.5    Pereira, P.6
  • 59
    • 0027368295 scopus 로고
    • Hepatotoxin (microcystin) and neurotoxin (anatoxin-a) contained in natural blooms and strains of cyanobacteria from Japanese freshwaters
    • Park, H.-D.; Watanabe, M.F.; Harada, K.-I.; Nagai, H.; Suzuki, M.; Watanabe, M.; Hayashi, H. Hepatotoxin (microcystin) and neurotoxin (anatoxin-a) contained in natural blooms and strains of cyanobacteria from Japanese freshwaters. Nat. Toxins 1993, 1, 353-360.
    • (1993) Nat. Toxins , vol.1 , pp. 353-360
    • Park, H.-D.1    Watanabe, M.F.2    Harada, K.-I.3    Nagai, H.4    Suzuki, M.5    Watanabe, M.6    Hayashi, H.7
  • 60
    • 0035295956 scopus 로고    scopus 로고
    • The relationship between cyanotoxin (microcystin, MC) in pond-ditch water and primary liver cancer in China
    • Yu, S.; Zhao, N.; Zi, X. The relationship between cyanotoxin (microcystin, MC) in pond-ditch water and primary liver cancer in China. Zhonghua Zhong Liu Za Zhi 2001, 23, 96-99.
    • (2001) Zhonghua Zhong Liu Za Zhi , vol.23 , pp. 96-99
    • Yu, S.1    Zhao, N.2    Zi, X.3
  • 62
    • 34547222433 scopus 로고    scopus 로고
    • Molecular characterization of potential microcystin-producing cyanobacteria in lake ontario embayments and nearshore waters
    • Hotto, A.M.; Satchwell, M.F.; Boyer, G.L. Molecular characterization of potential microcystin-producing cyanobacteria in Lake Ontario embayments and nearshore waters. Appl. Environ. Microbiol. 2007, 73, 4570-4578.
    • (2007) Appl. Environ. Microbiol , vol.73 , pp. 4570-4578
    • Hotto, A.M.1    Satchwell, M.F.2    Boyer, G.L.3
  • 63
    • 0042929500 scopus 로고    scopus 로고
    • Microcystin-LR causes the collapse of actin filaments in primary human hepatocytes
    • Batista, T.; de Sousa, G.; Suput, J.S.; Rahmani, R.; Suput, D. Microcystin-LR causes the collapse of actin filaments in primary human hepatocytes. Aquat. Toxicol. 2003, 65, 85-91.
    • (2003) Aquat. Toxicol , vol.65 , pp. 85-91
    • Batista, T.1    de Sousa, G.2    Suput, J.S.3    Rahmani, R.4    Suput, D.5
  • 64
    • 75349086483 scopus 로고    scopus 로고
    • Molecular mechanisms of microcystin toxicity in animal cells
    • Campos, A.; Vasconcelos, V. Molecular mechanisms of Microcystin toxicity in animal cells. Int. J. Mol. Sci. 2010, 11, 268-287.
    • (2010) Int. J. Mol. Sci , vol.11 , pp. 268-287
    • Campos, A.1    Vasconcelos, V.2
  • 65
    • 42149140039 scopus 로고    scopus 로고
    • Chronic microcystin exposure induces hepatocyte proliferation with increased expression of mitotic and cyclin-associated genes in P53-deficient mice
    • Clark, S.P.; Ryan, T.P.; Searfoss, G.H.; Davis, M.A.; Hooser, S.B. Chronic microcystin exposure induces hepatocyte proliferation with increased expression of mitotic and cyclin-associated genes in P53-deficient mice. Toxicol. Pathol. 2008, 36, 190-203.
    • (2008) Toxicol. Pathol , vol.36 , pp. 190-203
    • Clark, S.P.1    Ryan, T.P.2    Searfoss, G.H.3    Davis, M.A.4    Hooser, S.B.5
  • 66
    • 33745209195 scopus 로고    scopus 로고
    • CaM-kinaseII-dependent commitment to microcystin-induced apoptosis is coupled to cell budding, but not to shrinkage or chromatin hypercondensation
    • Krakstad, C.; Herfindal, L.; Gjertsen, B.T.; Boe, R.; Vintermyr, O.K.; Fladmark, K.E.; Doskeland, S.O. CaM-kinaseII-dependent commitment to microcystin-induced apoptosis is coupled to cell budding, but not to shrinkage or chromatin hypercondensation. Cell Death Differ. 2005, 13, 1191-1202.
    • (2005) Cell Death Differ , vol.13 , pp. 1191-1202
    • Krakstad, C.1    Herfindal, L.2    Gjertsen, B.T.3    Boe, R.4    Vintermyr, O.K.5    Fladmark, K.E.6    Doskeland, S.O.7
  • 67
    • 33847671760 scopus 로고    scopus 로고
    • Phosphorylation and functions of inhibitor-2 family of proteins
    • Li, M.; Satinover, D.L.; Brautigan, D.L. Phosphorylation and functions of inhibitor-2 family of proteins. Biochemistry 2007, 46, 2380-2389.
    • (2007) Biochemistry , vol.46 , pp. 2380-2389
    • Li, M.1    Satinover, D.L.2    Brautigan, D.L.3
  • 68
    • 1642559254 scopus 로고    scopus 로고
    • Microcystin-LR and okadaic acid-induced cellular effects: A dualistic response
    • Gehringer, M.M. Microcystin-LR and okadaic acid-induced cellular effects: a dualistic response. FEBS Lett. 2004, 557, 1-8.
    • (2004) FEBS Lett , vol.557 , pp. 1-8
    • Gehringer, M.M.1
  • 69
    • 0038696373 scopus 로고    scopus 로고
    • Inhibition of nuclear protein phosphatase activity in mouse hepatocytes by the cyanobacterial toxin microcystin-LR
    • Guzman, R.E.; Solter, P.F.; Runnegar, M.T. Inhibition of nuclear protein phosphatase activity in mouse hepatocytes by the cyanobacterial toxin microcystin-LR. Toxicon 2003, 41, 773-781.
    • (2003) Toxicon , vol.41 , pp. 773-781
    • Guzman, R.E.1    Solter, P.F.2    Runnegar, M.T.3
  • 70
    • 33847147603 scopus 로고    scopus 로고
    • The role of ROS in microcystin-LR-induced hepatocyte apoptosis and liver injury in mice
    • Weng, D.; Lu, Y.; Wei, Y.; Liu, Y.; Shen, P. The role of ROS in microcystin-LR-induced hepatocyte apoptosis and liver injury in mice. Toxicology 2007, 232, 15-23.
    • (2007) Toxicology , vol.232 , pp. 15-23
    • Weng, D.1    Lu, Y.2    Wei, Y.3    Liu, Y.4    Shen, P.5
  • 71
    • 0033780306 scopus 로고    scopus 로고
    • Structural organization of microcystin biosynthesis in Microcystis aeruginosa pcc 7806: An integrated peptide-polyketide synthetase system
    • Tillett, D.; Dittmann, E.; Erhard, M.; von Döhren, H.; Börner, T.; Neilan, B.A. Structural organization of microcystin biosynthesis in Microcystis aeruginosa PCC 7806: an integrated peptide-polyketide synthetase system. Chem. Biol. 2000, 7, 753-764.
    • (2000) Chem. Biol , vol.7 , pp. 753-764
    • Tillett, D.1    Dittmann, E.2    Erhard, M.3    von Döhren, H.4    Börner, T.5    Neilan, B.A.6
  • 72
    • 0037226538 scopus 로고    scopus 로고
    • Microcystin biosynthesis in Planktothrix: Genes, evolution, and manipulation
    • Christiansen, G.; Fastner, J.; Erhard, M.; Börner, T.; Dittmann, E. Microcystin biosynthesis in Planktothrix: genes, evolution, and manipulation. J. Bacteriol. 2003, 185, 564-572.
    • (2003) J. Bacteriol , vol.185 , pp. 564-572
    • Christiansen, G.1    Fastner, J.2    Erhard, M.3    Börner, T.4    Dittmann, E.5
  • 74
    • 70349549298 scopus 로고    scopus 로고
    • The genetic basis of toxin production in cyanobacteria
    • Kurmayer, R.; Christiansen, G. The genetic basis of toxin production in Cyanobacteria. Freshwater Rev. 2009, 2, 31-50.
    • (2009) Freshwater Rev , vol.2 , pp. 31-50
    • Kurmayer, R.1    Christiansen, G.2
  • 75
    • 8744220572 scopus 로고    scopus 로고
    • Inactivation of an abc transporter gene, mcyH, results in loss of microcystin production in the cyanobacterium Microcystis aeruginosa PCC 7806
    • Pearson, L.A.; Hisbergues, M.; Börner, T.; Dittmann, E.; Neilan, B.A. Inactivation of an ABC transporter gene, mcyH, results in loss of microcystin production in the cyanobacterium Microcystis aeruginosa PCC 7806. Appl. Environ. Microbiol. 2004, 70, 6370-6378.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6370-6378
    • Pearson, L.A.1    Hisbergues, M.2    Börner, T.3    Dittmann, E.4    Neilan, B.A.5
  • 76
    • 0028847766 scopus 로고
    • Immuno-gold localization of hepatotoxins in cyanobacterial cells
    • Shi, L.; Carmichael, W.W.; Miller, I. Immuno-gold localization of hepatotoxins in cyanobacterial cells. Arch. Microbiol. 1995, 163, 7-15.
    • (1995) Arch. Microbiol , vol.163 , pp. 7-15
    • Shi, L.1    Carmichael, W.W.2    Miller, I.3
  • 77
    • 23044509179 scopus 로고    scopus 로고
    • Immunogold localisation of microcystins in cryosectioned cells of microcystis
    • Young, F.M.; Thomson, C.; Metcalf, J.S.; Lucocq, J.M.; Codd, G.A. Immunogold localisation of microcystins in cryosectioned cells of Microcystis. J. Struct. Biol. 2005, 151, 208-214.
    • (2005) J. Struct. Biol , vol.151 , pp. 208-214
    • Young, F.M.1    Thomson, C.2    Metcalf, J.S.3    Lucocq, J.M.4    Codd, G.A.5
  • 78
    • 0033856746 scopus 로고    scopus 로고
    • Light and the transcriptional response of the microcystin biosynthesis gene cluster
    • Kaebernick, M.; Neilan, B.; Borner, T.; Dittmann, E. Light and the transcriptional response of the microcystin biosynthesis gene cluster. Appl. Environ. Microbiol. 2000, 66, 3387-3392.
    • (2000) Appl. Environ. Microbiol , vol.66 , pp. 3387-3392
    • Kaebernick, M.1    Neilan, B.2    Borner, T.3    Dittmann, E.4
  • 79
    • 0031040256 scopus 로고    scopus 로고
    • A molecular basis for different interactions of marine toxins with protein phosphatase-1
    • Bagu, J.R.; Sykes, B.D.; Craig, M.M.; Holmes, C.F.B. A molecular basis for different interactions of marine toxins with protein phosphatase-1. J. Biol. Chem. 1997, 272, 5087-5097.
    • (1997) J. Biol. Chem , vol.272 , pp. 5087-5097
    • Bagu, J.R.1    Sykes, B.D.2    Craig, M.M.3    Holmes, C.F.B.4
  • 80
    • 8744313964 scopus 로고    scopus 로고
    • Characterization of the nodularin synthetase gene cluster and proposed theory of the evolution of cyanobacterial hepatotoxins
    • Moffitt, M.C.; Neilan, B.A. Characterization of the Nodularin synthetase gene cluster and proposed theory of the evolution of cyanobacterial hepatotoxins. Appl. Environ. Microbiol. 2004, 70, 6353-6362.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6353-6362
    • Moffitt, M.C.1    Neilan, B.A.2
  • 81
    • 56449124825 scopus 로고    scopus 로고
    • The molecular genetics and regulation of cyanobacterial peptide hepatotoxin biosynthesis
    • Pearson, L.A.; Moffitt, M.C.; Ginn, H.P.; Neilan, B.A. The molecular genetics and regulation of cyanobacterial peptide hepatotoxin biosynthesis. Crit. Rev. Toxicol. 2008, 38, 847-856.
    • (2008) Crit. Rev. Toxicol , vol.38 , pp. 847-856
    • Pearson, L.A.1    Moffitt, M.C.2    Ginn, H.P.3    Neilan, B.A.4
  • 82
    • 0022402504 scopus 로고
    • Severe hepatotoxicity caused by the tropical cyanobacterium (blue-green alga) cylindrospermopsis raciborskii (woloszynska) seenaya and subba raju isolated from a domestic water supply reservoir
    • Hawkins, P.R.; Runnegar, M.T.C.; Jackson, A.R.B.; Falconer, I.R. Severe hepatotoxicity caused by the tropical cyanobacterium (blue-green Alga) Cylindrospermopsis raciborskii (Woloszynska) Seenaya and Subba Raju isolated from a domestic water supply reservoir. Appl. Environ. Microbiol. 1985, 50, 1292-1295.
    • (1985) Appl. Environ. Microbiol , vol.50 , pp. 1292-1295
    • Hawkins, P.R.1    Runnegar, M.T.C.2    Jackson, A.R.B.3    Falconer, I.R.4
  • 83
    • 80052850108 scopus 로고
    • Cylindrospermopsin: A potent hepatotoxin from the blue-green alga Cylindrospermopsis raciborskii
    • Ohtani, I.; Moore, R.E.; Runnegar, M.T.C. Cylindrospermopsin: A potent hepatotoxin from the blue-green alga Cylindrospermopsis raciborskii. J. Am. Chem. Soc. 1992, 114, 7941-7942.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 7941-7942
    • Ohtani, I.1    Moore, R.E.2    Runnegar, M.T.C.3
  • 84
    • 0035401348 scopus 로고    scopus 로고
    • Isolation and identification of the cyanotoxin cylindrospermopsin and deoxy-cylindrospermopsin from a Thailand strain of cylindrospermopsis raciborskii (cyanobacteria)
    • Li, R.; Carmichael, W.W.; Brittain, S.; Eaglesham, G.K.; Shaw, G.R.; Mahakhant, A.; Noparatnaraporn, N.; Yongmanitchai, W.; Kaya, K.; Watanabe, M.M. Isolation and identification of the cyanotoxin cylindrospermopsin and deoxy-cylindrospermopsin from a Thailand strain of Cylindrospermopsis raciborskii (Cyanobacteria). Toxicon 2001, 39, 973-980.
    • (2001) Toxicon , vol.39 , pp. 973-980
    • Li, R.1    Carmichael, W.W.2    Brittain, S.3    Eaglesham, G.K.4    Shaw, G.R.5    Mahakhant, A.6    Noparatnaraporn, N.7    Yongmanitchai, W.8    Kaya, K.9    Watanabe, M.M.10
  • 85
    • 0028158344 scopus 로고
    • Isolation of cylindrospermopsin from a cyanobacterium Umezakia natans and its screening method
    • Harada, K.-I.; Ohtani, I.; Iwamoto, K.; Suzuki, M.; Watanabe, M.F.; Watanabe, M.; Terao, K. Isolation of cylindrospermopsin from a cyanobacterium Umezakia natans and its screening method. Toxicon 1994, 32, 73-84.
    • (1994) Toxicon , vol.32 , pp. 73-84
    • Harada, K.-I.1    Ohtani, I.2    Iwamoto, K.3    Suzuki, M.4    Watanabe, M.F.5    Watanabe, M.6    Terao, K.7
  • 86
    • 0030869941 scopus 로고    scopus 로고
    • Identification of cylindrospermopsin in the cyanobacterium Aphanizomenon ovalisporum (Cyanophyceae) isolated from lake Kinneret, Israel
    • Banker, R.; Carmeli, S.; Hadas, O.; Teltsch, B.; Porat, R.; Skenik, A. Identification of cylindrospermopsin in the cyanobacterium Aphanizomenon ovalisporum (Cyanophyceae) isolated from lake Kinneret, Israel. J. Phycol. 1997, 33, 613-616.
    • (1997) J. Phycol , vol.33 , pp. 613-616
    • Banker, R.1    Carmeli, S.2    Hadas, O.3    Teltsch, B.4    Porat, R.5    Skenik, A.6
  • 87
    • 0035686147 scopus 로고    scopus 로고
    • First report of the cyanotoxins cylindrospermopsin and deoxycylindrospermopsin from Raphidiopsis curvata (cyanobacteria)
    • Li, R.; Carmichael, W.W.; Brittain, S.; Eaglesham, G.K.; Shaw, G.R.; Yongding, L.; Watanabe, M.M. First report of the cyanotoxins cylindrospermopsin and deoxycylindrospermopsin from Raphidiopsis curvata (cyanobacteria). J. Phycol. 2001, 37, 1121-1126.
    • (2001) J. Phycol , vol.37 , pp. 1121-1126
    • Li, R.1    Carmichael, W.W.2    Brittain, S.3    Eaglesham, G.K.4    Shaw, G.R.5    Yongding, L.6    Watanabe, M.M.7
  • 88
    • 0034754774 scopus 로고    scopus 로고
    • Identification of genes implicated in toxin production in the cyanobacterium Cylindrospermopsis raciborskii
    • Schembri, M.A.; Neilan, B.A.; Saint, C.P. Identification of genes implicated in toxin production in the cyanobacterium Cylindrospermopsis raciborskii. Environ. Toxicol. 2001, 16, 413-421.
    • (2001) Environ. Toxicol , vol.16 , pp. 413-421
    • Schembri, M.A.1    Neilan, B.A.2    Saint, C.P.3
  • 89
    • 31344460347 scopus 로고    scopus 로고
    • First report on cylindrospermopsin producing aphanizomenon flos-aquae (cyanobacteria) isolated from two german lakes
    • Preubel, K.; Stüken, A.; Wiedner, C.; Chorus, I.; Fastner, J. First report on cylindrospermopsin producing Aphanizomenon flos-aquae (Cyanobacteria) isolated from two German lakes. Toxicon 2006, 47, 156-162.
    • (2006) Toxicon , vol.47 , pp. 156-162
    • Preubel, K.1    Stüken, A.2    Wiedner, C.3    Chorus, I.4    Fastner, J.5
  • 90
    • 33845950858 scopus 로고    scopus 로고
    • First evidence for the production of cylindrospermopsin and deoxy-cylindrospermopsin by the freshwater benthic cyanobacterium, Lyngbya wollei (Farlow ex Gomont) Speziale and Dyck
    • Seifert, M.; McGregor, G.; Eaglesham, G.; Wickramasinghe, W.; Shaw, G. First evidence for the production of cylindrospermopsin and deoxy-cylindrospermopsin by the freshwater benthic cyanobacterium, Lyngbya wollei (Farlow ex Gomont) Speziale and Dyck. Harmful Algae 2007, 6, 73-80.
    • (2007) Harmful Algae , vol.6 , pp. 73-80
    • Seifert, M.1    McGregor, G.2    Eaglesham, G.3    Wickramasinghe, W.4    Shaw, G.5
  • 91
    • 0028200062 scopus 로고
    • Electron microscopic studies on experimental poisoning in mice induced by cylindrospermopsin isolated from blue-green alga Umezakia natans
    • Terao, K.; Ohmori, S.; Igarashi, K.; Ohtani, I.; Watanabe, M.F.; Harada, K.I.; Ito, E.; Watanabe, M. Electron microscopic studies on experimental poisoning in mice induced by cylindrospermopsin isolated from blue-green alga Umezakia natans. Toxicon 1994, 32, 833-843.
    • (1994) Toxicon , vol.32 , pp. 833-843
    • Terao, K.1    Ohmori, S.2    Igarashi, K.3    Ohtani, I.4    Watanabe, M.F.5    Harada, K.I.6    Ito, E.7    Watanabe, M.8
  • 92
    • 0024892099 scopus 로고
    • A new procedure for the analysis and purification of naturally occurring anatoxin-a from the blue-green alga Anabaena flos-aquae
    • Harada, K.-I.; Kimura, Y.; Ogawa, K.; Suzuki, M.; Dahlem, A.M.; Beasley, V.R.; Carmichael, W.W. A new procedure for the analysis and purification of naturally occurring anatoxin-a from the blue-green alga Anabaena flos-aquae. Toxicon 1989, 27, 1289-1296.
    • (1989) Toxicon , vol.27 , pp. 1289-1296
    • Harada, K.-I.1    Kimura, Y.2    Ogawa, K.3    Suzuki, M.4    Dahlem, A.M.5    Beasley, V.R.6    Carmichael, W.W.7
  • 93
    • 0033034115 scopus 로고    scopus 로고
    • Hepatic and renal toxicity of the blue-green alga (cyanobacterium) Cylindrospermopsis raciborskii in male Swiss albino mice
    • Falconer, I.R.; Hardy, S.J.; Humpage, A.R.; Froscio, S.M.; Tozer, G.J.; Hawkins, P.R. Hepatic and renal toxicity of the blue-green alga (cyanobacterium) Cylindrospermopsis raciborskii in male Swiss albino mice. Environ. Toxicol. 1999, 14, 143-150.
    • (1999) Environ. Toxicol , vol.14 , pp. 143-150
    • Falconer, I.R.1    Hardy, S.J.2    Humpage, A.R.3    Froscio, S.M.4    Tozer, G.J.5    Hawkins, P.R.6
  • 95
    • 0035072467 scopus 로고    scopus 로고
    • Preliminary evidence for in vivo tumour initiation by oral administration of extracts of the blue-green alga Cylindrospermopsis raciborskii containing the toxin cylindrospermopsin
    • Falconer, I.R.; Humpage, A.R. Preliminary evidence for in vivo tumour initiation by oral administration of extracts of the blue-green alga Cylindrospermopsis raciborskii containing the toxin cylindrospermopsin. Environ. Toxicol. 2001, 16, 192-195.
    • (2001) Environ. Toxicol , vol.16 , pp. 192-195
    • Falconer, I.R.1    Humpage, A.R.2
  • 96
    • 0028853288 scopus 로고
    • Inhibition of reduced glutathione synthesis by cyanobacterial alkaloid cylindrospermopsin in cultured rat hepatocytes
    • Runnegar, M.T.; Kong, S.-M.; Zhong, Y.-Z.; Lu, S.C. Inhibition of reduced glutathione synthesis by cyanobacterial alkaloid cylindrospermopsin in cultured rat hepatocytes. Biochem. Pharmacol.1995, 49, 219-225.
    • (1995) Biochem. Pharmacol , vol.49 , pp. 219-225
    • Runnegar, M.T.1    Kong, S.-M.2    Zhong, Y.-Z.3    Lu, S.C.4
  • 97
    • 0036802862 scopus 로고    scopus 로고
    • Genotoxicity investigation of a cyanobacterial toxin, cylindrospermopsin
    • Shen, X.; Lam, P.K.S.; Shaw, G.R.; Wickramasinghe, W. Genotoxicity investigation of a cyanobacterial toxin, cylindrospermopsin. Toxicon 2002, 40, 1499-1501.
    • (2002) Toxicon , vol.40 , pp. 1499-1501
    • Shen, X.1    Lam, P.K.S.2    Shaw, G.R.3    Wickramasinghe, W.4
  • 98
    • 0037133743 scopus 로고    scopus 로고
    • A novel gene encoding amidinotransferase in the cylindrospermopsin producing cyanobacterium Aphanizomenon ovalisporum
    • Shalev-Alon, G.; Sukenik, A.; Livnah, O.; Schwarz, R.; Kaplan, A. A novel gene encoding amidinotransferase in the cylindrospermopsin producing cyanobacterium Aphanizomenon ovalisporum. FEMS Microbiol. Lett. 2002, 209, 87-91.
    • (2002) FEMS Microbiol. Lett , vol.209 , pp. 87-91
    • Shalev-Alon, G.1    Sukenik, A.2    Livnah, O.3    Schwarz, R.4    Kaplan, A.5
  • 99
    • 33644903798 scopus 로고    scopus 로고
    • Functional modeling and phylogenetic distribution of putative cylindrospermopsin biosynthesis enzymes
    • Kellmann, R.; Mills, T.; Neilan, B. Functional modeling and phylogenetic distribution of putative cylindrospermopsin biosynthesis enzymes. J. Mol. Evol. 2006, 62, 267-280.
    • (2006) J. Mol. Evol , vol.62 , pp. 267-280
    • Kellmann, R.1    Mills, T.2    Neilan, B.3
  • 100
    • 0024403199 scopus 로고
    • Preliminary characterization of neurotoxic cyanobacteria blooms and strains from Finland
    • Sivonen, K.; Himberg, K.; Luukkainen, R.; Niemelä, S.I.; Poon, G.K.; Codd, G.A. Preliminary characterization of neurotoxic cyanobacteria blooms and strains from Finland. Toxic. Assess. 1989, 4, 339-352.
    • (1989) Toxic. Assess , vol.4 , pp. 339-352
    • Sivonen, K.1    Himberg, K.2    Luukkainen, R.3    Niemelä, S.I.4    Poon, G.K.5    Codd, G.A.6
  • 101
    • 1542496610 scopus 로고    scopus 로고
    • Simultaneous production of homoanatoxin-a, anatoxin-a, and a new non-toxic 4-hydroxyhomoanatoxin-a by the cyanobacterium Raphidiopsis mediterranea Skuja
    • Namikoshi, M.; Murakami, T.; Watanabe, M.F.; Oda, T.; Yamada, J.; Tsujimura, S.; Nagai, H.; Oishi, S. Simultaneous production of homoanatoxin-a, anatoxin-a, and a new non-toxic 4-hydroxyhomoanatoxin-a by the cyanobacterium Raphidiopsis mediterranea Skuja. Toxicon 2003, 42, 533-538.
    • (2003) Toxicon , vol.42 , pp. 533-538
    • Namikoshi, M.1    Murakami, T.2    Watanabe, M.F.3    Oda, T.4    Yamada, J.5    Tsujimura, S.6    Nagai, H.7    Oishi, S.8
  • 103
    • 33846198729 scopus 로고    scopus 로고
    • Production of Anatoxin-a and a novel biosynthetic precursor by the cyanobacterium Aphanizomenon issatschenkoi
    • Selwood, A.I.; Holland, P.T.; Wood, S.A.; Smith, K.F.; McNabb, P.S. Production of Anatoxin-a and a novel biosynthetic precursor by the cyanobacterium Aphanizomenon issatschenkoi. Environ. Sci. Technol. 2006, 41, 506-510.
    • (2006) Environ. Sci. Technol , vol.41 , pp. 506-510
    • Selwood, A.I.1    Holland, P.T.2    Wood, S.A.3    Smith, K.F.4    McNabb, P.S.5
  • 104
    • 0026577946 scopus 로고
    • Investigations of a neurotoxic oscillatorialean strain (Cyanophyceae) and its toxin. Isolation and characterization of homoanatoxin-a
    • Skulberg, O.M.; Skulberg, R.; Carmichael, W.W.; Andersen, R.A.; Matsunaga, S.; Moore, R.E. Investigations of a neurotoxic oscillatorialean strain (Cyanophyceae) and its toxin. Isolation and characterization of homoanatoxin-a. Environ. Toxicol. Chem. 1992, 11, 321-329.
    • (1992) Environ. Toxicol. Chem , vol.11 , pp. 321-329
    • Skulberg, O.M.1    Skulberg, R.2    Carmichael, W.W.3    Andersen, R.A.4    Matsunaga, S.5    Moore, R.E.6
  • 105
    • 0037355049 scopus 로고    scopus 로고
    • The first identification of the rare cyanobacterial toxin, homoanatoxin-a, in Ireland
    • Furey, A.; Crowley, J.; Shuilleabhain, A.N.; Skulberg, O.M.; James, K.J. The first identification of the rare cyanobacterial toxin, homoanatoxin-a, in Ireland. Toxicon 2003, 41, 297-303.
    • (2003) Toxicon , vol.41 , pp. 297-303
    • Furey, A.1    Crowley, J.2    Shuilleabhain, A.N.3    Skulberg, O.M.4    James, K.J.5
  • 106
    • 17644409017 scopus 로고    scopus 로고
    • Neurotoxins in axenic oscillatorian cyanobacteria: Coexistence of anatoxin-a and homoanatoxin-a determined by ligand-binding assay and GC/MS
    • Aráoz, R.; Nghiem, H.-O.; Rippka, R.; Palibroda, N.; de Marsac, N.T.; Herdman, M. Neurotoxins in axenic oscillatorian cyanobacteria: coexistence of anatoxin-a and homoanatoxin-a determined by ligand-binding assay and GC/MS. Microbiology 2005, 151, 1263-1273.
    • (2005) Microbiology , vol.151 , pp. 1263-1273
    • Aráoz, R.1    Nghiem, H.-O.2    Rippka, R.3    Palibroda, N.4    de Marsac, N.T.5    Herdman, M.6
  • 107
    • 67650497679 scopus 로고    scopus 로고
    • Identification of a polyketide synthase coding sequence specific for anatoxin-a-producing Oscillatoria cyanobacteria
    • Cadel-Six, S.; Iteman, I.; Peyraud-Thomas, C.; Mann, S.; Ploux, O.; Mejean, A. Identification of a polyketide synthase coding sequence specific for anatoxin-a-producing Oscillatoria cyanobacteria. Appl. Environ. Microbiol. 2009, 75, 4909-4912.
    • (2009) Appl. Environ. Microbiol , vol.75 , pp. 4909-4912
    • Cadel-Six, S.1    Iteman, I.2    Peyraud-Thomas, C.3    Mann, S.4    Ploux, O.5    Mejean, A.6
  • 108
    • 67650519382 scopus 로고    scopus 로고
    • Evidence that biosynthesis of the neurotoxic alkaloids anatoxin-a and homoanatoxin-a in the cyanobacterium oscillatoria pcc 6506 occurs on a modular polyketide synthase initiated by l-proline
    • Méjean, A.; Mann, S.; Maldiney, T.; Vassiliadis, G.; Lequin, O.; Ploux, O. Evidence that biosynthesis of the neurotoxic alkaloids anatoxin-a and homoanatoxin-a in the cyanobacterium Oscillatoria PCC 6506 occurs on a modular polyketide synthase initiated by L-proline. J. Am. Chem. Soc. 2009, 131, 7512-7513.
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 7512-7513
    • Méjean, A.1    Mann, S.2    Maldiney, T.3    Vassiliadis, G.4    Lequin, O.5    Ploux, O.6
  • 109
    • 0022539538 scopus 로고
    • The pharmacology of anatoxin-a(s), a neurotoxin produced by the freshwater cyanobacterium Anabaena flos-aquae NRC 525-17
    • Mahmood, N.A.; Carmichael, W.W. The pharmacology of anatoxin-a(s), a neurotoxin produced by the freshwater cyanobacterium Anabaena flos-aquae NRC 525-17. Toxicon 1986, 24, 425-434.
    • (1986) Toxicon , vol.24 , pp. 425-434
    • Mahmood, N.A.1    Carmichael, W.W.2
  • 110
  • 111
    • 0023714073 scopus 로고
    • Comparison of effects of anatoxin-a(s) and paraoxon, physostigmine and pyridostigmine on mouse brain cholinesterase activity
    • Cook, W.O.; Beasley, V.R.; Dahlem, A.M.; Dellinger, J.A.; Harlin, K.S.; Carmichael, W.W Comparison of effects of anatoxin-a(s) and paraoxon, physostigmine and pyridostigmine on mouse brain cholinesterase activity. Toxicon 1988, 26, 750-753.
    • (1988) Toxicon , vol.26 , pp. 750-753
    • Cook, W.O.1    Beasley, V.R.2    Dahlem, A.M.3    Dellinger, J.A.4    Harlin, K.S.5    Carmichael, W.W.6
  • 112
    • 0242467774 scopus 로고    scopus 로고
    • Neurotoxins with anticholinesterase activity and their possible use as warfare agents
    • Pita, R.; Anadón, A.; Martínez-Larrañaga, M.R. Neurotoxins with anticholinesterase activity and their possible use as warfare agents. Med. Clin. (Barc.) 2003, 121, 511-517.
    • (2003) Med. Clin. (Barc.) , vol.121 , pp. 511-517
    • Pita, R.1    Anadón, A.2    Martínez-Larrañaga, M.R.3
  • 113
    • 34249009177 scopus 로고    scopus 로고
    • Biochemical characterization of paralytic shellfish toxin biosynthesis in vitro
    • Kellmann, R.; Neilan, B.A. Biochemical characterization of paralytic shellfish toxin biosynthesis in vitro. J. Phycol. 2007, 43, 497-508.
    • (2007) J. Phycol , vol.43 , pp. 497-508
    • Kellmann, R.1    Neilan, B.A.2
  • 114
    • 65549101737 scopus 로고    scopus 로고
    • Characterisation of the paralytic shellfish toxin biosynthesis gene clusters in Anabaena circinalis AWQC131C and Aphanizomenon sp. NH-5
    • DOI:10.1186/1471-2091-10-8
    • Mihali, T.K.; Kellmann, R.; Neilan, B.A. Characterisation of the paralytic shellfish toxin biosynthesis gene clusters in Anabaena circinalis AWQC131C and Aphanizomenon sp. NH-5. BMC Biochem. 2009, 10, 8, DOI:10.1186/1471-2091-10-8.
    • (2009) BMC Biochem , vol.10 , pp. 8
    • Mihali, T.K.1    Kellmann, R.2    Neilan, B.A.3
  • 115
    • 0022930560 scopus 로고
    • Structure-activity relations of tetrodotoxin, saxitoxin, and analogues
    • Kao, C.Y. Structure-activity relations of tetrodotoxin, saxitoxin, and analogues. Ann. N. Y. Acad. Sci. 1986, 479, 52-67.
    • (1986) Ann. N. Y. Acad. Sci , vol.479 , pp. 52-67
    • Kao, C.Y.1
  • 116
    • 4344645019 scopus 로고    scopus 로고
    • Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula
    • Chang, Z.; Sitachitta, N.; Rossi, J.V.; Roberts, M.A.; Flatt, P.M.; Jia, J.; Sherman, D.H.; Gerwick, W.H. Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula. J. Nat. Prod. 2004, 67, 1356-1367.
    • (2004) J. Nat. Prod , vol.67 , pp. 1356-1367
    • Chang, Z.1    Sitachitta, N.2    Rossi, J.V.3    Roberts, M.A.4    Flatt, P.M.5    Jia, J.6    Sherman, D.H.7    Gerwick, W.H.8
  • 117
    • 0002800142 scopus 로고
    • A bacterial source of tetrodotoxins and saxitoxins
    • Hall, S., Strichartz, G., Eds.; American Chemical Society: Washington, DC, USA
    • Tamplin, M.L. A bacterial source of tetrodotoxins and saxitoxins. In Marine Toxins: Origin, Structure, and Molecular Pharmacology; Hall, S., Strichartz, G., Eds.; American Chemical Society: Washington, DC, USA, 1990; Volume 418, pp. 78-86.
    • (1990) Marine Toxins: Origin, Structure, and Molecular Pharmacology , vol.418 , pp. 78-86
    • Tamplin, M.L.1
  • 118
    • 33645393913 scopus 로고    scopus 로고
    • Saxitoxin, a toxic marine natural product that targets a multitude of receptors
    • Llewellyn, L.E. Saxitoxin, a toxic marine natural product that targets a multitude of receptors. Nat. Prod. Rep. 2006, 23, 200-222.
    • (2006) Nat. Prod. Rep , vol.23 , pp. 200-222
    • Llewellyn, L.E.1
  • 119
    • 84878187534 scopus 로고    scopus 로고
    • Toxins: Potential chemical weapons from living organisms. Available online, accessed on 24 June
    • Toxins: Potential chemical weapons from living organisms. Available online: http://www.opcw.org/about-chemical-weapons/types-of-chemical-agent/toxins/ (accessed on 24 June 2010).
    • (2010)
  • 120
    • 46949108154 scopus 로고    scopus 로고
    • Biosynthetic intermediate analysis and functional homology reveal a saxitoxin gene cluster in cyanobacteria
    • Kellmann, R.; Mihali, T.K.; Jeon, Y.J.; Pickford, R.; Pomati, F.; Neilan, B.A. Biosynthetic intermediate analysis and functional homology reveal a saxitoxin gene cluster in cyanobacteria. Appl. Environ. Microbiol. 2008, 74, 4044-4053.
    • (2008) Appl. Environ. Microbiol , vol.74 , pp. 4044-4053
    • Kellmann, R.1    Mihali, T.K.2    Jeon, Y.J.3    Pickford, R.4    Pomati, F.5    Neilan, B.A.6
  • 121
    • 3042551455 scopus 로고    scopus 로고
    • Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula
    • Edwards, D.J.; Marquez, B.L.; Nogle, L.M.; McPhail, K.; Goeger, D.E.; Roberts, M.A.; Gerwick, W.H. Structure and biosynthesis of the jamaicamides, new mixed polyketide-peptide neurotoxins from the marine cyanobacterium Lyngbya majuscula. Chem. Biol. 2004, 11, 817-833.
    • (2004) Chem. Biol , vol.11 , pp. 817-833
    • Edwards, D.J.1    Marquez, B.L.2    Nogle, L.M.3    McPhail, K.4    Goeger, D.E.5    Roberts, M.A.6    Gerwick, W.H.7
  • 122
    • 22544467754 scopus 로고    scopus 로고
    • The neurotoxic lipopeptide kalkitoxin interacts with voltage-sensitive sodium channels in cerebellar granule neurons
    • LePage, K.T.; Goeger, D.; Yokokawa, F.; Asano, T.; Shioiri, T.; Gerwick, W.H.; Murray, T.F. The neurotoxic lipopeptide kalkitoxin interacts with voltage-sensitive sodium channels in cerebellar granule neurons. Toxicol. Lett. 2005, 158, 133-139.
    • (2005) Toxicol. Lett , vol.158 , pp. 133-139
    • Lepage, K.T.1    Goeger, D.2    Yokokawa, F.3    Asano, T.4    Shioiri, T.5    Gerwick, W.H.6    Murray, T.F.7
  • 124
    • 0029096389 scopus 로고
    • Antillatoxin: An exceptionally ichthyotoxic cyclic lipopeptide from the tropical cyanobacterium Lyngbya majuscula
    • Orjala, J.; Nagle, D.G.; Hsu, V.; Gerwick, W.H. Antillatoxin: an exceptionally ichthyotoxic cyclic lipopeptide from the tropical cyanobacterium Lyngbya majuscula. J. Am. Chem. Soc. 1995, 117, 8281-8282.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 8281-8282
    • Orjala, J.1    Nagle, D.G.2    Hsu, V.3    Gerwick, W.H.4
  • 126
    • 0033231630 scopus 로고    scopus 로고
    • Antillatoxin and kalkitoxin, ichthyotoxins from the tropical cyanobacterium Lyngbya majuscula, induce distinct temporal patterns of NMDA receptor-mediated neurotoxicity
    • Berman, F.W.; Gerwick, W.H.; Murray, T.F. Antillatoxin and kalkitoxin, ichthyotoxins from the tropical cyanobacterium Lyngbya majuscula, induce distinct temporal patterns of NMDA receptor-mediated neurotoxicity. Toxicon 1999, 37, 1645-1648.
    • (1999) Toxicon , vol.37 , pp. 1645-1648
    • Berman, F.W.1    Gerwick, W.H.2    Murray, T.F.3
  • 127
    • 0002401080 scopus 로고    scopus 로고
    • Chemotherapy of neoplastic diseases
    • 9th ed.; Hardman, J.G., Limbird, L.E., Molinoff, P.B., Ruddin, R.W., Guilman, A.G., Eds.; Pergamon Press: New York, NY, USA
    • Calabresi, P.; Chabner, B. Chemotherapy of neoplastic diseases. In The Pharmacological Basis of Therapeutics, 9th ed.; Hardman, J.G., Limbird, L.E., Molinoff, P.B., Ruddin, R.W., Guilman, A.G., Eds.; Pergamon Press: New York, NY, USA, 1996; pp. 1225-1287.
    • (1996) The Pharmacological Basis of Therapeutics , pp. 1225-1287
    • Calabresi, P.1    Chabner, B.2
  • 128
    • 4344645019 scopus 로고    scopus 로고
    • Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula
    • Chang, Z.; Sitachitta, N.; Rossi, J.V.; Roberts, M.A.; Flatt, P.M.; Jia, J.; Sherman, D.H.; Gerwick, W.H. Biosynthetic pathway and gene cluster analysis of curacin A, an antitubulin natural product from the tropical marine cyanobacterium Lyngbya majuscula. J. Nat. Prod. 2004, 67, 1356-1367.
    • (2004) J. Nat. Prod , vol.67 , pp. 1356-1367
    • Chang, Z.1    Sitachitta, N.2    Rossi, J.V.3    Roberts, M.A.4    Flatt, P.M.5    Jia, J.6    Sherman, D.H.7    Gerwick, W.H.8
  • 129
    • 0029969534 scopus 로고    scopus 로고
    • Barbamide, a chlorinated metabolite with molluscicidal activity from the Caribbean cyanobacterium Lyngbya majuscula
    • Orjala, J., Gerwick, W.H. Barbamide, a chlorinated metabolite with molluscicidal activity from the Caribbean cyanobacterium Lyngbya majuscula. J. Nat. Prod. 1996, 59, 427-430.
    • (1996) J. Nat. Prod , vol.59 , pp. 427-430
    • Orjala, J.1    Gerwick, W.H.2
  • 130
    • 0037151788 scopus 로고    scopus 로고
    • The barbamide biosynthetic gene cluster: A novel cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (nrps) origin involving an unusual trichloroleucyl starter unit
    • Chang, Z.; Flatt, P.; Gerwick, W.H.; Nguyen, V.-A.; Willis, C.L.; Sherman, D.H. The barbamide biosynthetic gene cluster: A novel cyanobacterial system of mixed polyketide synthase (PKS)-non-ribosomal peptide synthetase (NRPS) origin involving an unusual trichloroleucyl starter unit. Gene 2002, 296, 235-247.
    • (2002) Gene , vol.296 , pp. 235-247
    • Chang, Z.1    Flatt, P.2    Gerwick, W.H.3    Nguyen, V.-A.4    Willis, C.L.5    Sherman, D.H.6
  • 131
    • 0034800552 scopus 로고    scopus 로고
    • Biosynthesis of natural products on modular peptide synthetases
    • Doekel, S.; Marahiel, M.A. Biosynthesis of natural products on modular peptide synthetases. Metab. Eng. 2001, 3, 64-77.
    • (2001) Metab. Eng , vol.3 , pp. 64-77
    • Doekel, S.1    Marahiel, M.A.2
  • 132
    • 24744433982 scopus 로고    scopus 로고
    • Evolutionary implications of bacterial polyketide synthases
    • Jenke-Kodama, H.; Sandmann, A.; Muller, R.; Dittmann, E. Evolutionary implications of bacterial polyketide synthases. Mol. Biol. Evol. 2005, 22, 2027-2039.
    • (2005) Mol. Biol. Evol , vol.22 , pp. 2027-2039
    • Jenke-Kodama, H.1    Sandmann, A.2    Muller, R.3    Dittmann, E.4
  • 133
    • 0031768868 scopus 로고    scopus 로고
    • Lipopolysaccharide inhibition of rat hepatic microsomal epoxide hydrolase and glutathione S-transferase gene expression irrespective of nuclear factor-[k]B activation
    • Choi, S.H.; Kim, S.G. Lipopolysaccharide inhibition of rat hepatic microsomal epoxide hydrolase and glutathione S-transferase gene expression irrespective of nuclear factor-[k]B activation. Biochem. Pharmacol. 1998, 56, 1427-1436.
    • (1998) Biochem. Pharmacol , vol.56 , pp. 1427-1436
    • Choi, S.H.1    Kim, S.G.2
  • 134
    • 0037178217 scopus 로고    scopus 로고
    • The occurrence of Aeromonas hydrophila strains in Italian mineral and thermal waters
    • Biscardi, D.; Castaldo, A.; Gualillo, O.; Fusco, R. The occurrence of Aeromonas hydrophila strains in Italian mineral and thermal waters. Sci. Total Environ. 2002, 292, 255-263.
    • (2002) Sci. Total Environ , vol.292 , pp. 255-263
    • Biscardi, D.1    Castaldo, A.2    Gualillo, O.3    Fusco, R.4
  • 138
    • 0024791970 scopus 로고
    • Vibrio species in seawater and mussels: Abundance and numerical taxonomy
    • Ortigosa, M.; Esteve, C.; Pujalte, M.J. Vibrio species in seawater and mussels: abundance and numerical taxonomy. Syst. Appl. Microbiol. 1989, 12, 316-325.
    • (1989) Syst. Appl. Microbiol , vol.12 , pp. 316-325
    • Ortigosa, M.1    Esteve, C.2    Pujalte, M.J.3
  • 139
    • 0027965478 scopus 로고
    • Numerical taxonomy of vibrionaceae isolated from oysters and seawater along an annual cycle
    • Ortigosa, M.; Garay, E.; Pujalte, M.J. Numerical taxonomy of Vibrionaceae isolated from oysters and seawater along an annual cycle. Syst. Appl. Microbiol. 1994, 17, 216-225.
    • (1994) Syst. Appl. Microbiol , vol.17 , pp. 216-225
    • Ortigosa, M.1    Garay, E.2    Pujalte, M.J.3
  • 140
    • 0029080587 scopus 로고
    • Nested PCR method for rapid and sensitive detection of Vibrio vulnificus in fish, sediments, and water
    • Arias, C.R.; Garay, E.; Aznar, R. Nested PCR method for rapid and sensitive detection of Vibrio vulnificus in fish, sediments, and water. Appl. Environ. Microbiol. 1995, 61, 3476-3478.
    • (1995) Appl. Environ. Microbiol , vol.61 , pp. 3476-3478
    • Arias, C.R.1    Garay, E.2    Aznar, R.3
  • 141
    • 0030690158 scopus 로고    scopus 로고
    • Dominant intestinal microflora of sea bream and sea bass larvae from two hatcheries, during larval development
    • Grisez, L.; Reyniers J.; Verdonck, L.; Swings, J.; Ollevier, F. Dominant intestinal microflora of sea bream and sea bass larvae from two hatcheries, during larval development. Aquaculture 1997, 155, 387-399.
    • (1997) Aquaculture , vol.155 , pp. 387-399
    • Grisez, L.1    Reyniers, J.2    Verdonck, L.3    Swings, J.4    Ollevier, F.5
  • 142
    • 33646118500 scopus 로고    scopus 로고
    • Occurrence of vibrio parahaemolyticus, v. cholerae, and v. vulnificus in norwegian blue mussels (mytilus edulis
    • Bauer, A.; Østensvik, Ø.; Florvåg, M.; Ørmen, Ø.; Rørvik, L.M. Occurrence of Vibrio parahaemolyticus, V. cholerae, and V. vulnificus in Norwegian blue mussels (Mytilus edulis). Appl. Environ. Microbiol. 2006, 72, 3058-3061.
    • (2006) Appl. Environ. Microbiol , vol.72 , pp. 3058-3061
    • Bauer, A.1    Østensvik, O.2    Florvåg, M.3    Ørmen, O.4    Rørvik, L.M.5
  • 144
    • 0032052066 scopus 로고    scopus 로고
    • Species of Vibrio isolated from hepatopancreas, haemolymph and digestive tract of a population of healthy juvenile Penaeus vannamei
    • Gomez-Gil, B.; Roque, A.; Turnbull, J.F.; Tron-Mayen, L. Species of Vibrio isolated from hepatopancreas, haemolymph and digestive tract of a population of healthy juvenile Penaeus vannamei. Aquaculture 1998, 163, 1-9.
    • (1998) Aquaculture , vol.163 , pp. 1-9
    • Gomez-Gil, B.1    Roque, A.2    Turnbull, J.F.3    Tron-Mayen, L.4
  • 145
    • 0032213745 scopus 로고    scopus 로고
    • Vibrios associated with Penaeus chinensis (Crustacea: Decapoda) larvae in Chinese shrimp hatcheries
    • Vandenberghe, J.; Li, Y.; Verdonck, L.; Sorgeloos, P.; Xu, H.S.; Swings, J. Vibrios associated with Penaeus chinensis (Crustacea: Decapoda) larvae in Chinese shrimp hatcheries. Aquaculture 1998, 169, 121-132.
    • (1998) Aquaculture , vol.169 , pp. 121-132
    • Vandenberghe, J.1    Li, Y.2    Verdonck, L.3    Sorgeloos, P.4    Xu, H.S.5    Swings, J.6
  • 146
    • 0032754143 scopus 로고    scopus 로고
    • How Vibrio cholerae survive during starvation
    • Wai, S.N.; Mizunoe, Y.; Yoshida, S. How Vibrio cholerae survive during starvation. FEMS Microbiol. Lett. 1999, 180, 123-131.
    • (1999) FEMS Microbiol. Lett , vol.180 , pp. 123-131
    • Wai, S.N.1    Mizunoe, Y.2    Yoshida, S.3
  • 147
    • 0032079041 scopus 로고    scopus 로고
    • Shrimp diseases and currentdiagnostic methods
    • Lightner, D.V.; Redman, R.M. Shrimp diseases and currentdiagnostic methods. Aquaculture 1998, 164, 201-220.
    • (1998) Aquaculture , vol.164 , pp. 201-220
    • Lightner, D.V.1    Redman, R.M.2
  • 148
    • 0035923978 scopus 로고    scopus 로고
    • Diseases, prophylaxis and treatment of the Atlantic halibut Hippoglossus hippoglossus: A review
    • Bergh, O.; Nilsen F.; Samuelsen, O.B. Diseases, prophylaxis and treatment of the Atlantic halibut Hippoglossus hippoglossus: a review. Dis. Aquat. Org. 2001, 48, 57-74.
    • (2001) Dis. Aquat. Org , vol.48 , pp. 57-74
    • Bergh, O.1    Nilsen, F.2    Samuelsen, O.B.3
  • 149
    • 0034159990 scopus 로고    scopus 로고
    • Vibrio species associated with mortalities in hatchery-reared turbot (Colistium nudipinnis) and brill (C. guntheri) in New Zealand
    • Diggles, B.K.; Carson, J.; Hine, P.M.; Hickman, R.W.; Tait, M.J. Vibrio species associated with mortalities in hatchery-reared turbot (Colistium nudipinnis) and brill (C. guntheri) in New Zealand. Aquaculture 2000, 183, 1-12.
    • (2000) Aquaculture , vol.183 , pp. 1-12
    • Diggles, B.K.1    Carson, J.2    Hine, P.M.3    Hickman, R.W.4    Tait, M.J.5
  • 150
    • 0032794513 scopus 로고    scopus 로고
    • Bacterial interactions in early life stages of marine cold water fish
    • Hansen, G.H.; Olafsen, J.A. Bacterial interactions in early life stages of marine cold water fish. Microb. Ecol. 1999, 38, 1-26.
    • (1999) Microb. Ecol , vol.38 , pp. 1-26
    • Hansen, G.H.1    Olafsen, J.A.2
  • 151
    • 36749079251 scopus 로고    scopus 로고
    • Regulatory networks controlling Vibrio cholerae virulence gene expression
    • Matson, J.S.; Withey, J.H.; DiRita, V.J. Regulatory networks controlling Vibrio cholerae virulence gene expression. Infect. Immun. 2007, 75, 5542-5549.
    • (2007) Infect. Immun , vol.75 , pp. 5542-5549
    • Matson, J.S.1    Withey, J.H.2    Dirita, V.J.3
  • 154
    • 0034454681 scopus 로고    scopus 로고
    • Ctx prophages in classical biotype Vibrio cholerae: Functional phage genes but dysfunctional phage genomes
    • Davis, B.M.; Moyer, K.E.; Boyd, E.F.; Waldor, M.K. CTX prophages in classical biotype Vibrio cholerae: functional phage genes but dysfunctional phage genomes. J. Bacteriol. 2000, 182, 6992-6998.
    • (2000) J. Bacteriol , vol.182 , pp. 6992-6998
    • Davis, B.M.1    Moyer, K.E.2    Boyd, E.F.3    Waldor, M.K.4
  • 155
    • 0026663115 scopus 로고
    • The virulence gene activator ToxT from Vibrio cholerae is a member of the AraC family of transcriptional activators
    • Higgins, D.; Nazareno, E.; DiRita, V.J. The virulence gene activator ToxT from Vibrio cholerae is a member of the AraC family of transcriptional activators. J. Bacteriol. 1992, 174, 6974-6980.
    • (1992) J. Bacteriol , vol.174 , pp. 6974-6980
    • Higgins, D.1    Nazareno, E.2    Dirita, V.J.3
  • 156
    • 0032987096 scopus 로고    scopus 로고
    • Environmental signals modulate ToxT-dependent virulence factor expression in Vibrio cholerae
    • Schuhmacher, D.A.; Klose, K.E. Environmental signals modulate ToxT-dependent virulence factor expression in Vibrio cholerae. J. Bacteriol. 1999, 181, 1508-1514.
    • (1999) J. Bacteriol , vol.181 , pp. 1508-1514
    • Schuhmacher, D.A.1    Klose, K.E.2
  • 157
    • 27944462141 scopus 로고    scopus 로고
    • Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT
    • Prouty, M.G.; Osorio, C.R.; Klose, K.E. Characterization of functional domains of the Vibrio cholerae virulence regulator ToxT. Mol. Microbiol. 2005, 58, 1143-1156.
    • (2005) Mol. Microbiol , vol.58 , pp. 1143-1156
    • Prouty, M.G.1    Osorio, C.R.2    Klose, K.E.3
  • 158
    • 33645471024 scopus 로고    scopus 로고
    • The toxbox: Specific dna sequence requirements for activation of Vibrio cholerae virulence genes by ToxT
    • Withey, J.H.; DiRita, V.J. The toxbox: specific DNA sequence requirements for activation of Vibrio cholerae virulence genes by ToxT. Mol. Microbiol. 2006, 59, 1779-1789.
    • (2006) Mol. Microbiol , vol.59 , pp. 1779-1789
    • Withey, J.H.1    Dirita, V.J.2
  • 159
    • 0036195527 scopus 로고    scopus 로고
    • Regulation of gene expression in vibrio cholerae by toxt involves both antirepression and rna polymerase stimulation
    • Yu, R.R.; DiRita, V.J. Regulation of gene expression in Vibrio cholerae by ToxT involves both antirepression and RNA polymerase stimulation. Mol. Microbiol. 2002, 43, 119-134.
    • (2002) Mol. Microbiol , vol.43 , pp. 119-134
    • Yu, R.R.1    Dirita, V.J.2
  • 160
    • 0033544713 scopus 로고    scopus 로고
    • Regulation and temporal expression patterns of Vibrio cholerae virulence genes during infection
    • Lee, S.H.; Hava, D.L.; Waldor, M.K.; Camilli, A. Regulation and temporal expression patterns of Vibrio cholerae virulence genes during infection. Cell 1999, 99, 625-634.
    • (1999) Cell , vol.99 , pp. 625-634
    • Lee, S.H.1    Hava, D.L.2    Waldor, M.K.3    Camilli, A.4
  • 161
    • 0035026929 scopus 로고    scopus 로고
    • Microbes and microbial toxins: Paradigms for microbial-mucosal interactions V. Cholera: Invasion of the intestinal epithelial barrier by a stably folded protein toxin
    • Lencer, W.I. Microbes and microbial toxins: paradigms for microbial-mucosal interactions V. Cholera: invasion of the intestinal epithelial barrier by a stably folded protein toxin. Am. J. Physiol. Gastrointest. Liver Physiol. 2001, 280, 781-786.
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol , vol.280 , pp. 781-786
    • Lencer, W.I.1
  • 162
    • 0033055636 scopus 로고    scopus 로고
    • Membrane traffic and cellular uptake of cholera toxin
    • Lencer, W.I.; Hirst, T.R.; Holmes, R.K. Membrane traffic and cellular uptake of cholera toxin. Biochim. Biophys. Acta 1999, 1450, 177-190.
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 177-190
    • Lencer, W.I.1    Hirst, T.R.2    Holmes, R.K.3
  • 164
    • 0032903930 scopus 로고    scopus 로고
    • Cellular microbiology: Can we learn cell physiology from microorganisms
    • Fasano, A. Cellular microbiology: can we learn cell physiology from microorganisms? Am. J. Physiol., Cell Physiol. 1999, 276, 765-776.
    • (1999) Am. J. Physiol., Cell Physiol , vol.276 , pp. 765-776
    • Fasano, A.1
  • 165
    • 35648975533 scopus 로고    scopus 로고
    • Martx, multifuntional autoprocessing repeats-in-toxin toxins
    • Satchell, K.J.F. MARTX, multifuntional autoprocessing repeats-in-toxin toxins. Infect. Immun. 2007, 75, 5079-5084.
    • (2007) Infect. Immun , vol.75 , pp. 5079-5084
    • Satchell, K.J.F.1
  • 167
    • 0028165393 scopus 로고
    • Densities of vibrio vulnificus in the intestines of fish from the u.s. gulf coast
    • DePaola, A.; Capers, G.M.; Alexander, D. Densities of Vibrio vulnificus in the intestines of fish from the U.S. Gulf Coast. Appl. Environ. Microbiol. 1994, 60, 984-988.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 984-988
    • Depaola, A.1    Capers, G.M.2    Alexander, D.3
  • 169
    • 33745126986 scopus 로고    scopus 로고
    • Detection of free-living and plankton-bound vibrios in coastal waters of the adriatic sea (italy) and study of their pathogenicity associated properties
    • Baffone, W.; Tarsi, R.; Pane, L.; Campana, R.; Repetto, B.; Mariottini, G.L.; Pruzzo, C. Detection of free-living and plankton-bound vibrios in coastal waters of the Adriatic Sea (Italy) and study of their pathogenicity associated properties. Environ. Microbiol. 2006, 8, 1299-1305.
    • (2006) Environ. Microbiol , vol.8 , pp. 1299-1305
    • Baffone, W.1    Tarsi, R.2    Pane, L.3    Campana, R.4    Repetto, B.5    Mariottini, G.L.6    Pruzzo, C.7
  • 170
    • 65449185894 scopus 로고    scopus 로고
    • Vibrio vulnificus: Disease and pathogenesis
    • Jones, K.J.; Oliver, J.D. Vibrio vulnificus: disease and pathogenesis. Infect. Immun. 2009, 77, 1723-1733.
    • (2009) Infect. Immun , vol.77 , pp. 1723-1733
    • Jones, K.J.1    Oliver, J.D.2
  • 171
    • 0026632549 scopus 로고
    • Vibrio vulnificus infection in taiwan: Report of 28 cases and review of clinical manifestations and treatment
    • Chuang, Y.C.; Yuan, C.Y.; Liu, C.Y.; Lan, C.K.; Huang, A.H. Vibrio vulnificus infection in Taiwan: report of 28 cases and review of clinical manifestations and treatment. Clin. Infect. Dis. 1992, 15, 271-276.
    • (1992) Clin. Infect. Dis , vol.15 , pp. 271-276
    • Chuang, Y.C.1    Yuan, C.Y.2    Liu, C.Y.3    Lan, C.K.4    Huang, A.H.5
  • 172
    • 20844455738 scopus 로고    scopus 로고
    • Wound infections caused by Vibrio vulnificus and other marine bacteria
    • Oliver, J.D. Wound infections caused by Vibrio vulnificus and other marine bacteria. Epidemiol. Infect. 2005, 133, 383-391.
    • (2005) Epidemiol Infect , vol.133 , pp. 383-391
    • Oliver, J.D.1
  • 173
    • 0021928232 scopus 로고
    • Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus
    • Gray, L.D.; Kreger, A.S. Purification and characterization of an extracellular cytolysin produced by Vibrio vulnificus. Infect. Immun. 1985, 48, 62-72.
    • (1985) Infect. Immun , vol.48 , pp. 62-72
    • Gray, L.D.1    Kreger, A.S.2
  • 174
    • 0023241504 scopus 로고
    • Purification and characterization of an elastolytic protease of Vibrio vulnificus
    • Kothary, M.H.; Kreger, A.S. Purification and characterization of an elastolytic protease of Vibrio vulnificus. J. Gen. Microbiol. 1987, 133, 1783-1791.
    • (1987) J. Gen. Microbiol , vol.133 , pp. 1783-1791
    • Kothary, M.H.1    Kreger, A.S.2
  • 175
    • 0034118185 scopus 로고    scopus 로고
    • Metalloprotease is not essential for vibrio vulnificus virulence in mice
    • Shao, C.P.; Hor, L.I. Metalloprotease is not essential for Vibrio vulnificus virulence in mice. Infect. Immun. 2000, 68, 3569-3573.
    • (2000) Infect. Immun , vol.68 , pp. 3569-3573
    • Shao, C.P.1    Hor, L.I.2
  • 176
    • 40749157602 scopus 로고    scopus 로고
    • Vibrio vulnificus rtx toxin kills host cells only after contact of the bacteria with host cells
    • Kim, Y.R.; Lee, S.E.; Kook, H.; Yeom, J.A.; Na, H.S.; Kim, S.Y.; Chung, S.S.;. Choy, H.E.; Rhee, J.H. Vibrio vulnificus RTX toxin kills host cells only after contact of the bacteria with host cells. Cell. Microbiol. 2008, 10, 848-862.
    • (2008) Cell. Microbiol , vol.10 , pp. 848-862
    • Kim, Y.R.1    Lee, S.E.2    Kook, H.3    Yeom, J.A.4    Na, H.S.5    Kim, S.Y.6    Chung, S.S.7    Choy, H.E.8
  • 177
    • 15944429289 scopus 로고    scopus 로고
    • Molecular pathogenesis of vibrio vulnificus
    • Gulig, P.A.; Bourdage, K.L.; Starks, A.M. Molecular pathogenesis of Vibrio vulnificus. J. Microbiol. 2005, 43, 118-131.
    • (2005) J. Microbiol , vol.43 , pp. 118-131
    • Gulig, P.A.1    Bourdage, K.L.2    Starks, A.M.3
  • 178
    • 42149186570 scopus 로고    scopus 로고
    • Vibrio vulnificus rtxe is important for virulence and its expression is induced by exposure to host cells
    • Lee, B.C.; Lee, J.H.; Kim, M.W.; Kim, B.S.; Oh, M.H.; Kim, K.S.; Kim, T.S.; Choi, S.H. Vibrio vulnificus rtxE is important for virulence and its expression is induced by exposure to host cells. Infect. Immun. 2008, 76, 1509-1517.
    • (2008) Infect. Immun , vol.76 , pp. 1509-1517
    • Lee, B.C.1    Lee, J.H.2    Kim, M.W.3    Kim, B.S.4    Oh, M.H.5    Kim, K.S.6    Kim, T.S.7    Choi, S.H.8
  • 179
    • 0030862053 scopus 로고    scopus 로고
    • Hyper production, purification, and mechanism of action of the cytotoxic enterotoxin produced by Aeromonas hydrophila
    • Chopra, A.K. Hyper production, purification, and mechanism of action of the cytotoxic enterotoxin produced by Aeromonas hydrophila. Infect. Immun. 1997, 65, 4299-4308.
    • (1997) Infect. Immun , vol.65 , pp. 4299-4308
    • Chopra, A.K.1
  • 180
    • 0030716756 scopus 로고    scopus 로고
    • Incidence and clinical symptoms of Aeromonas-associated traveller's diarrhoea in Tokyo
    • Yamada, S.; Matsushita, S.; Dejsirilet, S.; Kudoh, Y. Incidence and clinical symptoms of Aeromonas-associated traveller's diarrhoea in Tokyo. Epidemiol. Infect. 1997, 119, 121-126.
    • (1997) Epidemiol. Infect , vol.119 , pp. 121-126
    • Yamada, S.1    Matsushita, S.2    Dejsirilet, S.3    Kudoh, Y.4
  • 181
    • 0036129793 scopus 로고    scopus 로고
    • Role of various enterotoxins in Aeromonas hyrophila-induced gastroenteritis: Generation of enterotoxin gene-deficient mutants and evaluation of their enterotoxin activity
    • Sha, J.; Kozlova, E.V.; Chopra, K. Role of various enterotoxins in Aeromonas hyrophila-induced gastroenteritis: generation of enterotoxin gene-deficient mutants and evaluation of their enterotoxin activity. Infect. Immun. 2002, 70, 1924-1935.
    • (2002) Infect. Immun , vol.70 , pp. 1924-1935
    • Sha, J.1    Kozlova, E.V.2    Chopra, K.3
  • 182
    • 0034058065 scopus 로고    scopus 로고
    • The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages
    • Chopra, A.K.; Xu, X.J.; Ribardo, D.; Gonzalez, M.; Kuhl, K.; Peterson, J.W.; Houston, C.W. The cytotoxic enterotoxin of Aeromonas hydrophila induces proinflammatory cytokine production and activates arachidonic acid metabolism in macrophages. Infect. Immun. 2000, 68, 2808-2818.
    • (2000) Infect. Immun , vol.68 , pp. 2808-2818
    • Chopra, A.K.1    Xu, X.J.2    Ribardo, D.3    Gonzalez, M.4    Kuhl, K.5    Peterson, J.W.6    Houston, C.W.7
  • 183
    • 0033565425 scopus 로고    scopus 로고
    • Mechanisms of lung neutrophil activation after hemorrhage or endotoxemia: Roles of reactive oxygen intermediates, nf-kB, and cyclic amp response element binding protein
    • Shenkar, R.; Abraham, E. Mechanisms of lung neutrophil activation after hemorrhage or endotoxemia: roles of reactive oxygen intermediates, NF-kB, and cyclic AMP response element binding protein. J. Immunol. 1999, 163, 954-962.
    • (1999) J. Immunol , vol.163 , pp. 954-962
    • Shenkar, R.1    Abraham, E.2
  • 184
    • 0023238632 scopus 로고
    • Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila
    • Howard, S.P.; Garland, W.J.; Green, M.J.; Buckley, J.T. Nucleotide sequence of the gene for the hole-forming toxin aerolysin of Aeromonas hydrophila. J. Bacteriol. 1987, 169, 2869-2871.
    • (1987) J. Bacteriol , vol.169 , pp. 2869-2871
    • Howard, S.P.1    Garland, W.J.2    Green, M.J.3    Buckley, J.T.4
  • 185
    • 0026129021 scopus 로고
    • Genetic variation in related cytolytic toxins produced by different species of Aeromonas
    • Ashok, K.C.; Houston, C.W.; Kurosky, A. Genetic variation in related cytolytic toxins produced by different species of Aeromonas. FEMS Microbiol. Lett. 1991, 78, 231-238.
    • (1991) FEMS Microbiol. Lett , vol.78 , pp. 231-238
    • Ashok, K.C.1    Houston, C.W.2    Kurosky, A.3
  • 186
    • 34248680659 scopus 로고    scopus 로고
    • Shiga toxin-producing Escherichia coli: An overview
    • Gyles, C.L. Shiga toxin-producing Escherichia coli: an overview. J. Anim. Sci. 2007, 85, E45-E62.
    • (2007) J. Anim. Sci , vol.85
    • Gyles, C.L.1
  • 188
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins-from cell biology to biomedical applications
    • Johannes, L.; Romer, W. Shiga toxins-from cell biology to biomedical applications. Nat. Rev. Microbiol. 2010, 8, 105-116.
    • (2010) Nat. Rev. Microbiol , vol.8 , pp. 105-116
    • Johannes, L.1    Romer, W.2
  • 189
    • 4644358200 scopus 로고    scopus 로고
    • Shiga toxinencoding bacteriophages-genomes in motion
    • Herold, S.; Karch, H.; Schmidt, H. Shiga toxinencoding bacteriophages-genomes in motion. Int. J. Med. Microbiol. 2004, 294, 115-121.
    • (2004) Int. J. Med. Microbiol , vol.294 , pp. 115-121
    • Herold, S.1    Karch, H.2    Schmidt, H.3
  • 190
    • 0036211836 scopus 로고    scopus 로고
    • Identification, characterization, and distribution of a Shiga toxin 1 gene variant (stx(1c)) in escherichia coli strains isolated from humans
    • Zhang, W.; Bielaszewska, M.; Kuczius, T.; Karch, H. Identification, characterization, and distribution of a Shiga toxin 1 gene variant (stx(1c)) in Escherichia coli strains isolated from humans. J. Clin. Microbiol. 2002, 40, 1441-1446.
    • (2002) J. Clin. Microbiol , vol.40 , pp. 1441-1446
    • Zhang, W.1    Bielaszewska, M.2    Kuczius, T.3    Karch, H.4
  • 191
    • 0025028971 scopus 로고
    • Induction of verotoxin sensitivity in receptor-deficient cell lines using the receptor glycolipid globotriosylceramide
    • Waddell, T.; Cohen, A.; Lingwood, C.A. Induction of verotoxin sensitivity in receptor-deficient cell lines using the receptor glycolipid globotriosylceramide. Proc. Natl. Acad. Sci. USA 1990,87, 7898-7901.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7898-7901
    • Waddell, T.1    Cohen, A.2    Lingwood, C.A.3
  • 193
    • 0028301437 scopus 로고
    • Glycosphingolipid receptor function is modified by fatty acid content. verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues
    • Kiarash, A.; Boyd, B.; Lingwood, C.A. Glycosphingolipid receptor function is modified by fatty acid content. Verotoxin 1 and verotoxin 2c preferentially recognize different globotriaosyl ceramide fatty acid homologues. J. Biol. Chem. 1994, 269, 11138-11146.
    • (1994) J. Biol. Chem , vol.269 , pp. 11138-11146
    • Kiarash, A.1    Boyd, B.2    Lingwood, C.A.3
  • 195
    • 3042639390 scopus 로고    scopus 로고
    • Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin
    • Lauvrak, S.U.; Torgersen, M.L.; Sandvig, K. Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin. J. Cell Sci. 2004, 117, 2321-2331.
    • (2004) J. Cell Sci , vol.117 , pp. 2321-2331
    • Lauvrak, S.U.1    Torgersen, M.L.2    Sandvig, K.3
  • 197
    • 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. 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. 1988, 171, 45-50.
    • (1988) Eur. J. Biochem , vol.171 , pp. 45-50
    • Endo, Y.1
  • 198
    • 0030973162 scopus 로고    scopus 로고
    • Ribotoxic stress response: Activation of the stress-activated protein kinase jnk1 by inhibitors of the peptidyl transferase reaction and by sequence-specific rna damage to the α-sarcin/ricin loop in the 28s rrna
    • Iordanov, M.S.; Pribnow, D.; Magun, J.L.; Dinh, T.H.; Pearson, J.A.; Chen, S.L.; Magun, B.E. Ribotoxic stress response: activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the α-sarcin/ricin loop in the 28S rRNA. Mol. Cell Biol. 1997, 17, 3373-3381.
    • (1997) Mol. Cell Biol , vol.17 , pp. 3373-3381
    • Iordanov, M.S.1    Pribnow, D.2    Magun, J.L.3    Dinh, T.H.4    Pearson, J.A.5    Chen, S.L.6    Magun, B.E.7
  • 199
    • 0036141198 scopus 로고    scopus 로고
    • Shiga toxin 1-induced activation of c-Jun NH2-terminal kinase and p38 in the human monocytic cell line thp-1: Possible involvement in the production of TNF-α
    • Foster, G.H.; Tesh, V.L. Shiga toxin 1-induced activation of c-Jun NH2-terminal kinase and p38 in the human monocytic cell line THP-1: possible involvement in the production of TNF-α. J. Leukoc. Biol. 2002, 71, 107-114.
    • (2002) J. Leukoc. Biol , vol.71 , pp. 107-114
    • Foster, G.H.1    Tesh, V.L.2
  • 200
    • 0032961903 scopus 로고    scopus 로고
    • Induction of cytokines in a human colon epithelial cell line by Shiga toxin 1 (Stx1) and Stx2 but not by non-toxic mutant Stx1 which lacks N-glycosidase activity
    • Yamasaki, C.; Natori, Y.; Zeng, X.T.; Ohmura, M.; Yamasaki, S.; Takeda, Y.; Natori, Y. Induction of cytokines in a human colon epithelial cell line by Shiga toxin 1 (Stx1) and Stx2 but not by non-toxic mutant Stx1 which lacks N-glycosidase activity. FEBS Lett. 1999, 442, 231-234.
    • (1999) FEBS Lett , vol.442 , pp. 231-234
    • Yamasaki, C.1    Natori, Y.2    Zeng, X.T.3    Ohmura, M.4    Yamasaki, S.5    Takeda, Y.6    Natori, Y.7
  • 201
    • 0037373313 scopus 로고    scopus 로고
    • Shiga toxin 1 triggers a ribotoxic stress response leading to p38 and jnk activation and induction of apoptosis in intestinal epithelial cells
    • Smith, W.E.; Kane, A.V.; Campbell, S.T.; Acheson, D.W.; Cochran, B.H.; Thorpe, C.M. Shiga toxin 1 triggers a ribotoxic stress response leading to p38 and JNK activation and induction of apoptosis in intestinal epithelial cells. Infect. Immun. 2003, 71, 1497-1504.
    • (2003) Infect. Immun , vol.71 , pp. 1497-1504
    • Smith, W.E.1    Kane, A.V.2    Campbell, S.T.3    Acheson, D.W.4    Cochran, B.H.5    Thorpe, C.M.6
  • 202
    • 38849180895 scopus 로고    scopus 로고
    • Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells
    • Lee, S.Y.; Lee, M.S.; Cherla, R.P.; Tesh, V.L. Shiga toxin 1 induces apoptosis through the endoplasmic reticulum stress response in human monocytic cells. Cell. Microbiol. 2008, 10, 10770-10780.
    • (2008) Cell. Microbiol , vol.10 , pp. 10770-10780
    • Lee, S.Y.1    Lee, M.S.2    Cherla, R.P.3    Tesh, V.L.4
  • 203
    • 0032581041 scopus 로고    scopus 로고
    • Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes
    • Suh, J.K.; Hovde, C.J.; Robertus, J.D. Shiga toxin attacks bacterial ribosomes as effectively as eucaryotic ribosomes. Biochemistry 1998, 37, 9394-9398.
    • (1998) Biochemistry , vol.37 , pp. 9394-9398
    • Suh, J.K.1    Hovde, C.J.2    Robertus, J.D.3
  • 204
    • 0029992963 scopus 로고    scopus 로고
    • Coinoculation with Hartmannella vermiformis enhances replicative Legionella pneumophila lung infection in a murine model of Legionnaires' disease
    • Brieland, J.; McClain, M.; Heath, L.; Chrisp, C.; Huffnagle, G.; LeGendre, M.; Hurley, M.; Fantone, J.; Engleberg, C. Coinoculation with Hartmannella vermiformis enhances replicative Legionella pneumophila lung infection in a murine model of Legionnaires' disease. Infect. Immun. 1996, 64, 2449-2456.
    • (1996) Infect. Immun , vol.64 , pp. 2449-2456
    • Brieland, J.1    McClain, M.2    Heath, L.3    Chrisp, C.4    Huffnagle, G.5    Legendre, M.6    Hurley, M.7    Fantone, J.8    Engleberg, C.9
  • 206
    • 0020591330 scopus 로고
    • Formation of a novel phagosome by the Legionnaires disease bacterium (Legionella pneumophila) in human monocytes
    • Horwitz, M.A. Formation of a novel phagosome by the Legionnaires' disease bacterium (Legionella pneumophila) in human monocytes. J. Exp. Med. 1983, 158, 1319-1331.
    • (1983) J. Exp. Med , vol.158 , pp. 1319-1331
    • Horwitz, M.A.1
  • 208
    • 0032821428 scopus 로고    scopus 로고
    • The leukotoxin of Pasteurella haemolytica binds to b2 integrins on bovine leukocytes
    • Ambagala, T.C.; Ambagala, A.P.N.; Srikumaran, S. The leukotoxin of Pasteurella haemolytica binds to b2 integrins on bovine leukocytes. FEMS Microbiol. Lett. 1999, 179, 161-167.
    • (1999) FEMS Microbiol. Lett , vol.179 , pp. 161-167
    • Ambagala, T.C.1    Ambagala, A.P.N.2    Srikumaran, S.3
  • 209
    • 39849091484 scopus 로고    scopus 로고
    • Virulence factor rtx in Legionella pneumophila, evidence suggesting it is a modular multifunctional protein
    • DOI:10.1186/1471-2164-9-14
    • D'Auria, G.; Jimenez, N.; Peris-Bondia, F.; Pelaz, C.; Latorre, A.; Moya, A. Virulence factor rtx in Legionella pneumophila, evidence suggesting it is a modular multifunctional protein. BMC Genomics 2008, 9, 14, DOI:10.1186/1471-2164-9-14.
    • (2008) BMC Genomics , vol.9 , pp. 14
    • D'auria, G.1    Jimenez, N.2    Peris-Bondia, F.3    Pelaz, C.4    Latorre, A.5    Moya, A.6
  • 211
    • 0001930773 scopus 로고    scopus 로고
    • Campylobacter jejuni
    • 2nd ed.; Doyle, M.P., Beuchat, L.R., Montville, T.J., Eds.; ASM Press: Washington, DC, USA
    • Nachamkin, I. Campylobacter jejuni. In Food Microbiology, Fundamentals and Frontiers, 2nd ed.; Doyle, M.P., Beuchat, L.R., Montville, T.J., Eds.; ASM Press: Washington, DC, USA, 2001.
    • (2001) Food Microbiology, Fundamentals and Frontiers
    • Nachamkin, I.1
  • 212
    • 0002639660 scopus 로고    scopus 로고
    • Clinical aspects of Campylobacter infection
    • 2nd ed.; Nachamkin, I., Blaser, M.J., Eds.; ASM Press: Washington, DC, USA
    • Skirrow, M.B.; Blaser, M.J. Clinical aspects of Campylobacter infection. In Campylobacter, 2nd ed.; Nachamkin, I., Blaser, M.J., Eds.; ASM Press: Washington, DC, USA, 2000; pp. 69-88.
    • (2000) Campylobacter , pp. 69-88
    • Skirrow, M.B.1    Blaser, M.J.2
  • 214
    • 0029008918 scopus 로고
    • Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae
    • Okuda, J.; Kurazono, H.; Takeda, Y. Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio, and cloning and sequencing of the cdt gene from Shigella dysenteriae. Microb. Pathog. 1995, 18, 167-172.
    • (1995) Microb. Pathog , vol.18 , pp. 167-172
    • Okuda, J.1    Kurazono, H.2    Takeda, Y.3
  • 215
    • 0033957389 scopus 로고    scopus 로고
    • Cytolethal distending toxin sequence and activity in the enterohepatic pathogen Helicobacter hepaticus
    • Young, V.B.; Knox, K.A.; Schauer, D.B. Cytolethal distending toxin sequence and activity in the enterohepatic pathogen Helicobacter hepaticus. Infect. Immun. 2000, 68, 184-191.
    • (2000) Infect. Immun , vol.68 , pp. 184-191
    • Young, V.B.1    Knox, K.A.2    Schauer, D.B.3
  • 216
    • 53649091724 scopus 로고    scopus 로고
    • Campylobacter-induced interleukin-8 secretion in polarized human intestinal epithelial cells requires Campylobacter-secreted cytolethal distending toxin- and Toll-like receptor-mediated activation of NF-kB
    • Zheng, J.; Meng, J.; Zhao, S.; Singh, R.; Song, W. Campylobacter-induced interleukin-8 secretion in polarized human intestinal epithelial cells requires Campylobacter-secreted cytolethal distending toxin- and Toll-like receptor-mediated activation of NF-kB. Infect. Immun. 2008, 76, 4498-4508.
    • (2008) Infect. Immun , vol.76 , pp. 4498-4508
    • Zheng, J.1    Meng, J.2    Zhao, S.3    Singh, R.4    Song, W.5
  • 217
    • 0034644631 scopus 로고    scopus 로고
    • A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein
    • Tejero, L.M.; Galan, J.E. A bacterial toxin that controls cell cycle progression as a deoxyribonuclease I-like protein. Science 2000, 290, 354-357.
    • (2000) Science , vol.290 , pp. 354-357
    • Tejero, L.M.1    Galan, J.E.2
  • 218
    • 0034967972 scopus 로고    scopus 로고
    • CdtA CdtB, and CdtC form a tripartite complex required for cytolethal distending toxin
    • Tejero, L.M.; Galan, J.E. CdtA, CdtB, and CdtC form a tripartite complex required for cytolethal distending toxin. Infect. Immun. 2001, 69, 4358-4365.
    • (2001) Infect. Immun , vol.69 , pp. 4358-4365
    • Tejero, L.M.1    Galan, J.E.2
  • 219
    • 33749261083 scopus 로고    scopus 로고
    • Watershed issues associated with Clostridium botulinum: A literature review
    • Long, S.C.; Tauscher, T. Watershed issues associated with Clostridium botulinum: A literature review. J. Water Health 2006, 04.3, 277-288.
    • (2006) J. Water Health , vol.4 , Issue.3 , pp. 277-288
    • Long, S.C.1    Tauscher, T.2
  • 220
    • 0015502845 scopus 로고
    • A common subunit structure in Clostridium botulinum type A, B and E toxins
    • DasGupta, B.R.; Sugiyama, H. A common subunit structure in Clostridium botulinum type A, B and E toxins. Biochem. Biophys. Res. Commun. 1972, 48, 108-112.
    • (1972) Biochem. Biophys. Res. Commun , vol.48 , pp. 108-112
    • Dasgupta, B.R.1    Sugiyama, H.2
  • 221
    • 0025006842 scopus 로고
    • Cloning and complete nucleotide sequence of the gene for the main component of hemagglutinin produced by Clostridium botulinum type c
    • Tsuzuki, K.; Kimura, K.; Fujii, N.; Yokosawa, N.; Indoh, T.; Murakami, T.; Oguma, K. Cloning and complete nucleotide sequence of the gene for the main component of hemagglutinin produced by Clostridium botulinum type C. Infect. Immun. 1990, 58, 3173-3177.
    • (1990) Infect. Immun , vol.58 , pp. 3173-3177
    • Tsuzuki, K.1    Kimura, K.2    Fujii, N.3    Yokosawa, N.4    Indoh, T.5    Murakami, T.6    Oguma, K.7
  • 222
    • 0026718624 scopus 로고
    • The complete nucleotide sequence of the gene coding for the nontoxic-nonhemagglutinin component of Clostridium botulinum type C progenitor toxin
    • Tsuzuki, K.; Kimura, K.; Fujii, N.; Yokosawa, N.; Oguma, K. The complete nucleotide sequence of the gene coding for the nontoxic-nonhemagglutinin component of Clostridium botulinum type C progenitor toxin. Biochem. Biophys. Res. Commun. 1992, 183, 1273-1279.
    • (1992) Biochem. Biophys. Res. Commun , vol.183 , pp. 1273-1279
    • Tsuzuki, K.1    Kimura, K.2    Fujii, N.3    Yokosawa, N.4    Oguma, K.5
  • 223
    • 0032755353 scopus 로고    scopus 로고
    • Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the lps/ifn gamma-induced release of no and tnfalpha
    • Pellizzari, R.; Guidi-Rontani, C.; Vitale, G.; Mock, M.; Montecucco, C. Anthrax lethal factor cleaves MKK3 in macrophages and inhibits the LPS/IFN gamma-induced release of NO and TNFalpha. FEBS Lett. 1999, 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
  • 225
    • 0028310404 scopus 로고
    • Mechanism of action of tetanus and botulinum neurotoxins
    • Montecucco, C.; Schiavo, G. Mechanism of action of tetanus and botulinum neurotoxins. Mol.Microbiol. 1994, 13, 1-8.
    • (1994) Mol.Microbiol , vol.13 , pp. 1-8
    • Montecucco, C.1    Schiavo, G.2
  • 226
    • 0028303173 scopus 로고
    • Conserved structure of genes encoding components of botulinum neurotoxin complex M and the sequence of the gene coding for the nontoxic component in nonproteolytic Clostridium botulinum type
    • East, F.A.K.; Collins, M.D. Conserved structure of genes encoding components of botulinum neurotoxin complex M and the sequence of the gene coding for the nontoxic component in nonproteolytic Clostridium botulinum type. Curr. Microbiol. 1994, 29, 69-77.
    • (1994) Curr. Microbiol , vol.29 , pp. 69-77
    • East, F.A.K.1    Collins, M.D.2
  • 227
    • 0025314995 scopus 로고
    • The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins
    • Binz, T.; Kurazono, H.; Wille, M.; Frevert, J.; Wernars, K.; Niemann, H. The complete sequence of botulinum neurotoxin type A and comparison with other clostridial neurotoxins. J. Biol.Chem. 1990, 265, 9153-9158.
    • (1990) J. Biol.Chem , vol.265 , pp. 9153-9158
    • Binz, T.1    Kurazono, H.2    Wille, M.3    Frevert, J.4    Wernars, K.5    Niemann, H.6
  • 228
    • 0028283313 scopus 로고
    • Organization of the botulinum neurotoxin C1 gene and its associated non-toxic protein genes in Clostridium botulinum C 468
    • Hauser, D.; Eklund, M.W.; Boquet, P.; Popoff, M.R. Organization of the botulinum neurotoxin C1 gene and its associated non-toxic protein genes in Clostridium botulinum C 468. Mol. Gen. Genet. 1994, 243, 631-640.
    • (1994) Mol. Gen. Genet , vol.243 , pp. 631-640
    • Hauser, D.1    Eklund, M.W.2    Boquet, P.3    Popoff, M.R.4
  • 229
    • 0028948134 scopus 로고
    • The genes for the Clostridium botulinum type G toxin complex are on a plasmid
    • Zhou, Y.; Sugiyama, H.; Nakano, H.; Johnson, E.A. The genes for the Clostridium botulinum type G toxin complex are on a plasmid. Infect. Immun. 1995, 63, 2087-2091.
    • (1995) Infect. Immun , vol.63 , pp. 2087-2091
    • Zhou, Y.1    Sugiyama, H.2    Nakano, H.3    Johnson, E.A.4
  • 230
    • 0030221082 scopus 로고    scopus 로고
    • Genotyping of Clostridium perfringens by polymerase chain reaction isa useful adjunct to diagnosis of clostridial enteric disease in animals
    • Songer, J.G.; Meer, R.M. Genotyping of Clostridium perfringens by polymerase chain reaction isa useful adjunct to diagnosis of clostridial enteric disease in animals. Anaerobe 1996, 2, 197-203.
    • (1996) Anaerobe , vol.2 , pp. 197-203
    • Songer, J.G.1    Meer, R.M.2
  • 231
    • 0027214133 scopus 로고
    • Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus
    • Hunter, S.E.; Brown, J.E.; Oyston, P.C.; Sakurai, J., Titball, R.W. Molecular genetic analysis of beta-toxin of Clostridium perfringens reveals sequence homology with alpha-toxin, gamma-toxin, and leukocidin of Staphylococcus aureus. Infect. Immun. 1993, 61, 3958-3965.
    • (1993) Infect. Immun , vol.61 , pp. 3958-3965
    • Hunter, S.E.1    Brown, J.E.2    Oyston, P.C.3    Sakurai, J.4    Titball, R.W.5
  • 232
    • 0027164407 scopus 로고
    • Cloning nucleotidesequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli
    • Czeczulin, J.R.; Hanna, P.C.; McClane, B.A. Cloning, nucleotidesequencing, and expression of the Clostridium perfringens enterotoxin gene in Escherichia coli. Infect. Immun. 1993, 61, 3429-3439.
    • (1993) Infect. Immun , vol.61 , pp. 3429-3439
    • Czeczulin, J.R.1    Hanna, P.C.2    McClane, B.A.3
  • 233
    • 0028158676 scopus 로고
    • A complex array of Hpr consensus DNA recognition sequences proximal to the enterotoxin gene in Clostridium perfringens type a
    • Brynestad, S.; Iwanejko, L.A.; Stewart, G.S.A.B.; Granum, P.E. A complex array of Hpr consensus DNA recognition sequences proximal to the enterotoxin gene in Clostridium perfringens type A. Microbiology 1994, 140, 97-104.
    • (1994) Microbiology , vol.140 , pp. 97-104
    • Brynestad, S.1    Iwanejko, L.A.2    Stewart, G.S.A.B.3    Granum, P.E.4
  • 234
    • 0033865962 scopus 로고    scopus 로고
    • Phylogenetic affiliation of the pseudomonads based on 16S rRNA sequence
    • Anzai, Y.K.H.; Park, J.Y.; Wakabayashi, H. Phylogenetic affiliation of the pseudomonads based on 16S rRNA sequence. Int. J. Syst. Evol. Microbiol. 2000, 50, 1563-1589.
    • (2000) Int. J. Syst. Evol. Microbiol , vol.50 , pp. 1563-1589
    • Anzai, Y.K.H.1    Park, J.Y.2    Wakabayashi, H.3
  • 236
    • 0037326937 scopus 로고    scopus 로고
    • Multicentre surveillance of Pseudomonas aeruginosa susceptibility patterns in nosocomial infections
    • Van Eldere, J. Multicentre surveillance of Pseudomonas aeruginosa susceptibility patterns in nosocomial infections. J. Antimicrob. Chemother. 2003, 51, 347-352.
    • (2003) J. Antimicrob. Chemother , vol.51 , pp. 347-352
    • van Eldere, J.1
  • 237
    • 60849116672 scopus 로고    scopus 로고
    • Pseudomonas exotoxin A: From virulence actor toanti-cancera gent
    • Wolf, P.; Elsasser-Beile, Ú. Pseudomonas exotoxin A: From virulence actor toanti-cancera gent. Int. J. Med. Microbiol. 2009, 299, 161-176.
    • (2009) Int. J. Med. Microbiol , vol.299 , pp. 161-176
    • Wolf, P.1    Elsasser-Beile, U.2
  • 238
    • 0029746051 scopus 로고    scopus 로고
    • Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages
    • Domenighini, M.; Rappuoli, R. Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages. Microbiology 1996, 21, 667-674.
    • (1996) Microbiology , vol.21 , pp. 667-674
    • Domenighini, M.1    Rappuoli, R.2
  • 239
    • 0024384846 scopus 로고
    • Functional analysis of domains ii, ib, and iii of pseudomonas exotoxin
    • Siegall, C.B.; Chaudhary, V.K.; FitzGerald, D.J.; Pastan, I. Functional analysis of domains II, Ib, and III of Pseudomonas exotoxin. J. Biol. Chem. 1989, 264, 14256-14261.
    • (1989) J. Biol. Chem , vol.264 , pp. 14256-14261
    • Siegall, C.B.1    Chaudhary, V.K.2    Fitzgerald, D.J.3    Pastan, I.4
  • 240
    • 0026455183 scopus 로고
    • Cell-mediated cleavage of pseudomonas exotoxin between arg279 and gly280 generates the enzymatically active fragment which translocates to the cytosol
    • Ogata, M.; Fryling, C.M.; Pastan, I.; FitzGerald, D.J. Cell-mediated cleavage of Pseudomonas exotoxin between Arg279 and Gly280 generates the enzymatically active fragment which translocates to the cytosol. J. Biol. Chem. 1992, 267, 25396-25401.
    • (1992) J. Biol. Chem , vol.267 , pp. 25396-25401
    • Ogata, M.1    Fryling, C.M.2    Pastan, I.3    Fitzgerald, D.J.4
  • 241
    • 0027398577 scopus 로고
    • Rab9 functions in transport between late endosomes and the trans Golgi network
    • Lombardi, D.; Soldati, T.; Riederer, M.A.; Goda, Y.; Zerial, M.; Pfeffer, S.R. Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 1993, 12, 677-682.
    • (1993) EMBO J , vol.12 , pp. 677-682
    • Lombardi, D.1    Soldati, T.2    Riederer, M.A.3    Goda, Y.4    Zerial, M.5    Pfeffer, S.R.6
  • 242
    • 0032969203 scopus 로고    scopus 로고
    • The kdel retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum
    • Jackson, M.E.; Simpson, J.C.; Girod, A.; Pepperkok, R., Roberts, L.M.; Lord, J.M. The KDEL retrieval system is exploited by Pseudomonas exotoxin A, but not by Shiga-like toxin-1, during retrograde transport from the Golgi complex to the endoplasmic reticulum. J. Cell Sci. 1999, 112, 467-475.
    • (1999) J. Cell Sci , vol.112 , pp. 467-475
    • Jackson, M.E.1    Simpson, J.C.2    Girod, A.3    Pepperkok, R.4    Roberts, L.M.5    Lord, J.M.6
  • 243
    • 69749091726 scopus 로고    scopus 로고
    • Gene and antigen markers of Shiga-toxin producing E. coli from Michigan and Indiana river water: Occurrence and relation to recreational water quality criteria
    • Duris, J.W.; Haack, S.K.; Fogarty, L.R. Gene and antigen markers of Shiga-toxin producing E. coli from Michigan and Indiana river water: Occurrence and relation to recreational water quality criteria. J. Environ. Qual. 2009, 38, 1878-1886.
    • (2009) J. Environ. Qual , vol.38 , pp. 1878-1886
    • Duris, J.W.1    Haack, S.K.2    Fogarty, L.R.3
  • 245
    • 74249083008 scopus 로고    scopus 로고
    • The genus Aeromonas: Taxonomy, pathogenicity, and infection
    • Janda, J.M.; Abbott, S.L. The genus Aeromonas: taxonomy, pathogenicity, and infection. Clin. Microbiol. Rev. 2010, 23, 35-73.
    • (2010) Clin. Microbiol. Rev , vol.23 , pp. 35-73
    • Janda, J.M.1    Abbott, S.L.2
  • 246
    • 4544264417 scopus 로고    scopus 로고
    • Binary Bacterial toxins: Biochemistry, biology, and applications of common Clostridium and Bacillus proteins
    • Barth, H.; Aktories, K.; Popoff, M.R.; Stiles, B.G. Binary Bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins. Microbiol. Mol. Biol. Rev. 2004, 68, 373-402.
    • (2004) Microbiol. Mol. Biol. Rev , vol.68 , pp. 373-402
    • Barth, H.1    Aktories, K.2    Popoff, M.R.3    Stiles, B.G.4
  • 247
    • 72449165391 scopus 로고    scopus 로고
    • Toxin-mediated effects on the innate mucosal defenses: Implications for enteric vaccines
    • Glenn, G.M.; Francis, D.H.; Danielsen, E.M. Toxin-mediated effects on the innate mucosal defenses: implications for enteric vaccines. Infect. Immun. 2009, 77, 5206-5215.
    • (2009) Infect. Immun , vol.77 , pp. 5206-5215
    • Glenn, G.M.1    Francis, D.H.2    Danielsen, E.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.