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Volumn 11, Issue 4, 2013, Pages 991-1018

An overview on the marine neurotoxin, saxitoxin: Genetics, moleculartargets, methods of detection and ecological functions

Author keywords

Copper transporter; Ion channels; Neurotoxin; Paralytic shellfish toxin; Phytoplankton; Saxitoxin

Indexed keywords

CALCIUM CHANNEL; CARBAMIC ACID; DECARBAMOYLSAXITOXIN; ION CHANNEL; NEUROTOXIN; POTASSIUM CHANNEL; SAXITOXIN; SEA WATER; VOLTAGE GATED SODIUM CHANNEL;

EID: 84877004348     PISSN: None     EISSN: 16603397     Source Type: Journal    
DOI: 10.3390/md11040991     Document Type: Review
Times cited : (238)

References (137)
  • 1
    • 46349102898 scopus 로고    scopus 로고
    • Neurotoxins from marine dinoflagallates: A brief review
    • Wang, D.-Z. Neurotoxins from marine dinoflagallates: A brief review. Mar. Drugs 2008, 6, 349-371.
    • (2008) Mar. Drugs , vol.6 , pp. 349-371
    • Wang, D.-Z.1
  • 2
    • 0032849891 scopus 로고    scopus 로고
    • Polyketides from dinoflagellates: Origins, pharmacology and biosynthesis
    • Rein, K.S.; Borrone, J. Polyketides from dinoflagellates: Origins, pharmacology and biosynthesis. Comp. Biochem. Physiol. B 1999, 124, 117-131.
    • (1999) Comp. Biochem. Physiol. B , vol.124 , pp. 117-131
    • Rein, K.S.1    Borrone, J.2
  • 3
    • 84860132654 scopus 로고    scopus 로고
    • Bioterrorism: Toxins as weapons
    • Anderson, P.D. Bioterrorism: Toxins as weapons. J. Pharm. Pract. 2012, 25, 121-129.
    • (2012) J. Pharm. Pract. , vol.25 , pp. 121-129
    • Anderson, P.D.1
  • 4
    • 0020427649 scopus 로고
    • Studies on paralytic shellfish poisoning in tropical waters: 4. Structures of 2 paralytic shellfish toxins, gonyautoxin-V and gonyautoxin-VI isolated from a tropical dinoflagellate, Pyrodinium bahamense var. compressa
    • Harada, T.; Oshima, Y.; Yasumoto, T. Studies on paralytic shellfish poisoning in tropical waters: 4. Structures of 2 paralytic shellfish toxins, gonyautoxin-V and gonyautoxin-VI isolated from a tropical dinoflagellate, Pyrodinium bahamense var. compressa. Agric. Biol. Chem. 1982, 46, 1861-1864.
    • (1982) Agric. Biol. Chem. , vol.46 , pp. 1861-1864
    • Harada, T.1    Oshima, Y.2    Yasumoto, T.3
  • 5
    • 0023622488 scopus 로고
    • Dinoflagellate Gymnodinium catenatum as the source of paralytic shellfish toxins in Tasmanian shellfish
    • Oshima, Y.; Hasegawa, M.; Yasumoto, T.; Hallegraeff, G.; Blackburn, S. Dinoflagellate Gymnodinium catenatum as the source of paralytic shellfish toxins in Tasmanian shellfish. Toxicon 1987, 25, 1105-1111.
    • (1987) Toxicon , vol.25 , pp. 1105-1111
    • Oshima, Y.1    Hasegawa, M.2    Yasumoto, T.3    Hallegraeff, G.4    Blackburn, S.5
  • 6
    • 0023936669 scopus 로고
    • Three estuarine Australian dinoflagellates that can produce paralytic shellfish toxins
    • Hallegraeff, G.M.; Steffensen, D.A.; Wetherbee, R. Three estuarine Australian dinoflagellates that can produce paralytic shellfish toxins. J. Plankton Res. 1988, 10, 533-541.
    • (1988) J. Plankton Res. , vol.10 , pp. 533-541
    • Hallegraeff, G.M.1    Steffensen, D.A.2    Wetherbee, R.3
  • 7
    • 0025256419 scopus 로고
    • Dynamics and physiology of saxitoxin production by the dinoflagellates Alexandrium spp
    • Anderson, D.M.; Kulis, D.M.; Sullivan, J.J.; Hall, S.; Lee, C. Dynamics and physiology of saxitoxin production by the dinoflagellates Alexandrium spp. Mar. Biol. 1990, 104, 511-524.
    • (1990) Mar. Biol. , vol.104 , pp. 511-524
    • Anderson, D.M.1    Kulis, D.M.2    Sullivan, J.J.3    Hall, S.4    Lee, C.5
  • 8
    • 0030742175 scopus 로고    scopus 로고
    • Evidence for paralytic shellfish poisons in the freshwater cyanobacterium Lyngbya wollei (Farlow ex Gomont) comb. nov
    • Carmichael, W.W.; Evans, W.R.; Yin, Q.Q.; Bell, P.; Moczydlowski, E. Evidence for paralytic shellfish poisons in the freshwater cyanobacterium Lyngbya wollei (Farlow ex Gomont) comb. nov. Appl. Environ. Microbiol. 1997, 63, 3104-3110.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3104-3110
    • Carmichael, W.W.1    Evans, W.R.2    Yin, Q.Q.3    Bell, P.4    Moczydlowski, E.5
  • 9
    • 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
  • 10
    • 0033029115 scopus 로고    scopus 로고
    • The first evidence of paralytic shellfish toxins in the freshwater cyanobacterium Cylindrospermopsis raciborskii, isolated from Brazil
    • Lagos, N.; Onodera, H.; Zagatto, P.A.; Andrinolo, D.; Azevedo, S.M.; Oshima, Y. The first evidence of paralytic shellfish toxins in the freshwater cyanobacterium Cylindrospermopsis raciborskii, isolated from Brazil. Toxicon 1999, 37, 1359-1373.
    • (1999) Toxicon , vol.37 , pp. 1359-1373
    • Lagos, N.1    Onodera, H.2    Zagatto, P.A.3    Andrinolo, D.4    Azevedo, S.M.5    Oshima, Y.6
  • 11
    • 0033850893 scopus 로고    scopus 로고
    • The freshwater cyanobacterium Planktothrix sp. FP1: Molecular identification and detection of paralytic shellfish poisoning toxins
    • Pomati, F.; Sacchi, S.; Rossetti, C.; Giovannardi, S.; Onodera, H.; Oshima, Y.; Neilan, B.A. The freshwater cyanobacterium Planktothrix sp. FP1: Molecular identification and detection of paralytic shellfish poisoning toxins. J. Phycol. 2000, 36, 553-562.
    • (2000) J. Phycol. , vol.36 , pp. 553-562
    • Pomati, F.1    Sacchi, S.2    Rossetti, C.3    Giovannardi, S.4    Onodera, H.5    Oshima, Y.6    Neilan, B.A.7
  • 12
    • 0035179486 scopus 로고    scopus 로고
    • PSP toxins from Aphanizomenon flos-aquae (cyanobacteria) collected in the Crestuma-Lever reservoir (Douro river, northern Portugal)
    • Ferreira, F.M.B.; Soler, J.M.F.; Fidalgo, M.L.; Fernandez-Vila, P. PSP toxins from Aphanizomenon flos-aquae (cyanobacteria) collected in the Crestuma-Lever reservoir (Douro river, northern Portugal). Toxicon 2001, 39, 757-761.
    • (2001) Toxicon , vol.39 , pp. 757-761
    • Ferreira, F.M.B.1    Soler, J.M.F.2    Fidalgo, M.L.3    Fernandez-Vila, P.4
  • 13
    • 0001377493 scopus 로고
    • Microalgal metabolites
    • Shimizu, Y. Microalgal metabolites. Chem. Rev. 1993, 93, 1685-1698.
    • (1993) Chem. Rev. , vol.93 , pp. 1685-1698
    • Shimizu, Y.1
  • 14
    • 77952961827 scopus 로고    scopus 로고
    • On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin
    • Pearson, L.; Mihali, T.; Moffitt, M.; Kellmann, R.; Neilan, B. On the chemistry, toxicology and genetics of the cyanobacterial toxins, microcystin, nodularin, saxitoxin and cylindrospermopsin. Mar. Drugs 2010, 8, 1650-1680.
    • (2010) Mar. Drugs , vol.8 , pp. 1650-1680
    • Pearson, L.1    Mihali, T.2    Moffitt, M.3    Kellmann, R.4    Neilan, B.5
  • 18
    • 0019415171 scopus 로고
    • Structure of saxitoxin in solutions and stereochemistry of dihydrosaxitoxins
    • Shimizu, Y.; Hsu, C.P.; Genenah, A. Structure of saxitoxin in solutions and stereochemistry of dihydrosaxitoxins. J. Am. Chem. Soc. 1981, 103, 605-609.
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 605-609
    • Shimizu, Y.1    Hsu, C.P.2    Genenah, A.3
  • 19
    • 0013894170 scopus 로고
    • Purification and characterization of poison produced by Gonyaulax catenella in axenic culture
    • Schantz, E.J.; Lynch, J.M.; Vayvada, G.; Matsumot, K.; Rapoport, H. Purification and characterization of poison produced by Gonyaulax catenella in axenic culture. Biochemistry 1966, 5, 1191-1195.
    • (1966) Biochemistry , vol.5 , pp. 1191-1195
    • Schantz, E.J.1    Lynch, J.M.2    Vayvada, G.3    Matsumot, K.4    Rapoport, H.5
  • 20
    • 0021219849 scopus 로고
    • Structural determinants of the affinity of saxitoxin for neuronal sodium channels - Electrophysiological studies on frog peripheral nerve
    • Strichartz, G. Structural determinants of the affinity of saxitoxin for neuronal sodium channels - Electrophysiological studies on frog peripheral nerve. J. Gen. Physiol. 1984, 84, 281-305.
    • (1984) J. Gen. Physiol. , vol.84 , pp. 281-305
    • Strichartz, G.1
  • 21
    • 0019643267 scopus 로고
    • Specific toxicity of paralytic shellfish poisons
    • Genenah, A.A.; Shimizu, Y. Specific toxicity of paralytic shellfish poisons. J. Agric. Food Chem. 1981, 29, 1289-1291.
    • (1981) J. Agric. Food Chem. , vol.29 , pp. 1289-1291
    • Genenah, A.A.1    Shimizu, Y.2
  • 22
    • 0002507958 scopus 로고
    • The Saxitoxins: Sources, Chemistry, and Pharmacology
    • Marine Toxins: Origin, Structure, and Molecular Pharmacology; Hall, S., Strichartz, G., Eds; American Chemical Society: Washington, DC, USA
    • Hall, S.; Strichartz, G.; Moczydlowski, E.; Ravindran, A.; Reichardt, P.B. The Saxitoxins: Sources, Chemistry, and Pharmacology. In Marine Toxins: Origin, Structure, and Molecular Pharmacology; Hall, S., Strichartz, G., Eds; American Chemical Society Symposium Series 418; American Chemical Society: Washington, DC, USA, 1990; pp. 29-65.
    • (1990) American Chemical Society Symposium Series 418 , pp. 29-65
    • Hall, S.1    Strichartz, G.2    Moczydlowski, E.3    Ravindran, A.4    Reichardt, P.B.5
  • 23
    • 35648967000 scopus 로고    scopus 로고
    • Predicitive toxinology: An initial foray using calculated molecular descriptors to decribe toxicity using saxitoxin as a model
    • Llewellyn, L.E. Predicitive toxinology: An initial foray using calculated molecular descriptors to decribe toxicity using saxitoxin as a model. Toxicon 2007, 50, 901-913.
    • (2007) Toxicon , vol.50 , pp. 901-913
    • Llewellyn, L.E.1
  • 24
    • 0033731909 scopus 로고    scopus 로고
    • Molecular mechanisms of neurotoxin action on voltage-gated sodium channels
    • Cestele, S.; Catterall, W.A. Molecular mechanisms of neurotoxin action on voltage-gated sodium channels. Biochimie 2000, 82, 883-892.
    • (2000) Biochimie , vol.82 , pp. 883-892
    • Cestele, S.1    Catterall, W.A.2
  • 25
    • 0027497515 scopus 로고
    • Molecular evolution of voltage-sensitive ion channel genes: On the origins of electrical excitability
    • Strong, M.; Chandy, K.G.; Gutman, G.A. Molecular evolution of voltage-sensitive ion channel genes: On the origins of electrical excitability. Mol. Biol. Evol. 1993, 10, 221-242.
    • (1993) Mol. Biol. Evol. , vol.10 , pp. 221-242
    • Strong, M.1    Chandy, K.G.2    Gutman, G.A.3
  • 26
    • 80051495437 scopus 로고    scopus 로고
    • NaChBac: The long lost sodium channel ancestor
    • Charalambous, K.; Wallace, B.A. NaChBac: The long lost sodium channel ancestor. Biochemistry 2011, 50, 6742-6752.
    • (2011) Biochemistry , vol.50 , pp. 6742-6752
    • Charalambous, K.1    Wallace, B.A.2
  • 27
    • 84864851318 scopus 로고    scopus 로고
    • Neurotoxins and their binding areas on voltage-gated sodium channels
    • Stevens, M.; Peigneur, S.; Tytgat, J. Neurotoxins and their binding areas on voltage-gated sodium channels. Front. Pharmacol. 2011, 2, 1-13.
    • (2011) Front. Pharmacol. , vol.2 , pp. 1-13
    • Stevens, M.1    Peigneur, S.2    Tytgat, J.3
  • 29
    • 0001800671 scopus 로고
    • The Voltage Sensitive Sodium Channel: A Receptor for Multiple Neurotoxins
    • Anderson, D.M., White, A.W., Baden, D.G., Eds.; Elsevier Science Publishing Co., Inc.: New York, NY, USA
    • Catterall, W.A. The Voltage Sensitive Sodium Channel: A Receptor for Multiple Neurotoxins. In Toxic Dinoflagellates; Anderson, D.M., White, A.W., Baden, D.G., Eds.; Elsevier Science Publishing Co., Inc.: New York, NY, USA, 1985; pp. 329-342.
    • (1985) Toxic Dinoflagellates , pp. 329-342
    • Catterall, W.A.1
  • 30
    • 0024811092 scopus 로고
    • A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II
    • Noda, M.; Suzuki, H.; Numa, S.; Stuhmer, W. A single point mutation confers tetrodotoxin and saxitoxin insensitivity on the sodium channel II. FEBS Lett. 1989, 259, 213-216.
    • (1989) FEBS Lett. , vol.259 , pp. 213-216
    • Noda, M.1    Suzuki, H.2    Numa, S.3    Stuhmer, W.4
  • 32
    • 0021360647 scopus 로고
    • The sodium channel from rat brain - Purification and subunit composition
    • Hartshorne, R.P.; Catterall, W.A. The sodium channel from rat brain - Purification and subunit composition. J. Biol. Chem. 1984, 259, 1667-1675.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1667-1675
    • Hartshorne, R.P.1    Catterall, W.A.2
  • 33
    • 0020005052 scopus 로고
    • Active groups of saxitoxin and tetrodoxin as deduced from actions of saxitoxin analogs on frog muscle and squid axon
    • Kao, C.Y.; Walker, S.E. Active groups of saxitoxin and tetrodoxin as deduced from actions of saxitoxin analogs on frog muscle and squid axon. J. Physiol. 1982, 323, 619-637.
    • (1982) J. Physiol. , vol.323 , pp. 619-637
    • Kao, C.Y.1    Walker, S.E.2
  • 34
    • 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
  • 35
    • 0002751692 scopus 로고
    • The Mode and Action of Toxins and Seafood Poisoning
    • Falconer, I., Ed.; Academic Press: San Diego, CA, USA
    • Baden, D.G.; Trainer, V.L. The Mode and Action of Toxins and Seafood Poisoning. In Algal Toxins in Seafood and Drinking Water; Falconer, I., Ed.; Academic Press: San Diego, CA, USA, 1993.
    • (1993) Algal Toxins in Seafood and Drinking Water
    • Baden, D.G.1    Trainer, V.L.2
  • 36
    • 0038580639 scopus 로고    scopus 로고
    • Saxitoxin is a gating modifier of hERG K+ channels
    • Wang, J.X.; Salata, J.J.; Bennett, P.B. Saxitoxin is a gating modifier of hERG K+ channels. J. Gen. Physiol. 2003, 121, 583-598.
    • (2003) J. Gen. Physiol. , vol.121 , pp. 583-598
    • Wang, J.X.1    Salata, J.J.2    Bennett, P.B.3
  • 37
    • 79951831891 scopus 로고    scopus 로고
    • Extraordinary conservation, gene loss, and positive selection in the evolution of an ancient neurotoxin
    • Murray, S.A.; Mihali, T.K.; Neilan, B.A. Extraordinary conservation, gene loss, and positive selection in the evolution of an ancient neurotoxin. Mol. Biol. Evol. 2011, 28, 1173-1182.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 1173-1182
    • Murray, S.A.1    Mihali, T.K.2    Neilan, B.A.3
  • 39
    • 84866152524 scopus 로고    scopus 로고
    • Adaptive evolution of voltage-gated sodium channels: The first 800 million years
    • Zakon, H.H. Adaptive evolution of voltage-gated sodium channels: The first 800 million years. Proc. Natl. Acad. Sci. USA 2012, 109, 10619-10625.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 10619-10625
    • Zakon, H.H.1
  • 40
    • 0025961765 scopus 로고
    • Pharmacologiocal and biochemical properties of saxiphilin, a soluble saxitoxin-binding protein from the bullfrog (Rana catesbeiana)
    • Mahar, J.; Lukacs, G.L.; Li, Y.; Hall, S.; Moczydlowski, E. Pharmacologiocal and biochemical properties of saxiphilin, a soluble saxitoxin-binding protein from the bullfrog (Rana catesbeiana). Toxicon 1991, 29, 53-71.
    • (1991) Toxicon , vol.29 , pp. 53-71
    • Mahar, J.1    Lukacs, G.L.2    Li, Y.3    Hall, S.4    Moczydlowski, E.5
  • 41
    • 0028216288 scopus 로고
    • Molecular cloning of bullfrog saxiphilin - A unique relative of the transferrin family that binds saxitoxin
    • Morabito, M.A.; Moczydlowski, E. Molecular cloning of bullfrog saxiphilin - A unique relative of the transferrin family that binds saxitoxin. Proc. Natl. Acad. Sci. USA 1994, 91, 2478-2482.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2478-2482
    • Morabito, M.A.1    Moczydlowski, E.2
  • 42
    • 84857359712 scopus 로고    scopus 로고
    • Beyond bilobal: Transferrin homologs having unusual domain architectures
    • Gaffney, J.P.; Valentine, A.M. Beyond bilobal: Transferrin homologs having unusual domain architectures. Biochim. Biophys. Acta Gen. Subj. 2012, 1820, 212-217.
    • (2012) Biochim. Biophys. Acta Gen. Subj. , vol.1820 , pp. 212-217
    • Gaffney, J.P.1    Valentine, A.M.2
  • 43
    • 0028822129 scopus 로고
    • Expression of saxiphilin in insect cells and localization of the saxitoxin-binding site to the C-terminal domain homologous to the C-lobe of transferrins
    • Morabito, M.A.; Llewellyn, L.E.; Moczydlowski, E.G. Expression of saxiphilin in insect cells and localization of the saxitoxin-binding site to the C-terminal domain homologous to the C-lobe of transferrins. Biochemistry 1995, 34, 13027-13033.
    • (1995) Biochemistry , vol.34 , pp. 13027-13033
    • Morabito, M.A.1    Llewellyn, L.E.2    Moczydlowski, E.G.3
  • 44
    • 33751157517 scopus 로고
    • Characterization of saxitoxin binding to saxiphilin, a relative of the transferrin family that displays pH-dependent ligand-binding
    • Llewellyn, L.E.; Moczydlowski, E.G. Characterization of saxitoxin binding to saxiphilin, a relative of the transferrin family that displays pH-dependent ligand-binding. Biochemistry 1994, 33, 12312-12322.
    • (1994) Biochemistry , vol.33 , pp. 12312-12322
    • Llewellyn, L.E.1    Moczydlowski, E.G.2
  • 45
    • 84863249064 scopus 로고    scopus 로고
    • Inhibition of copper uptake in yeast reveals the copper transporter Ctr1p as a potential molecular target of saxitoxin
    • Cusick, K.D.; Minkin, S.C.; Dodani, S.C.; Chang, C.J.; Wilhelm, S.W.; Sayler, G.S. Inhibition of copper uptake in yeast reveals the copper transporter Ctr1p as a potential molecular target of saxitoxin. Environ. Sci. Technol. 2012, 46, 2959-2966.
    • (2012) Environ. Sci. Technol. , vol.46 , pp. 2959-2966
    • Cusick, K.D.1    Minkin, S.C.2    Dodani, S.C.3    Chang, C.J.4    Wilhelm, S.W.5    Sayler, G.S.6
  • 46
    • 0030266832 scopus 로고    scopus 로고
    • Regulated copper uptake in Chlamydomonas reinhardtii in response to copper availabilty
    • Hill, K.; Hassett, R.; Kosman, D.; Merchant, S. Regulated copper uptake in Chlamydomonas reinhardtii in response to copper availabilty. Plant. Physiol. 1996, 112, 697-704.
    • (1996) Plant. Physiol. , vol.112 , pp. 697-704
    • Hill, K.1    Hassett, R.2    Kosman, D.3    Merchant, S.4
  • 47
    • 0028152451 scopus 로고
    • The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake
    • Dancis, A.; Haile, D.; Yuan, D.S.; Klausner, R.D. The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J. Biol. Chem. 1994, 269, 25660-25667.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25660-25667
    • Dancis, A.1    Haile, D.2    Yuan, D.S.3    Klausner, R.D.4
  • 48
    • 0028010889 scopus 로고
    • Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport
    • Dancis, A.; Yuan, D.S.; Haile, D.; Askwith, C.; Eide, D.; Moehle, C.; Kaplan, J.; Klausner, R.D. Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport. Cell 1994, 76, 393-402.
    • (1994) Cell , vol.76 , pp. 393-402
    • Dancis, A.1    Yuan, D.S.2    Haile, D.3    Askwith, C.4    Eide, D.5    Moehle, C.6    Kaplan, J.7    Klausner, R.D.8
  • 49
    • 66449102468 scopus 로고    scopus 로고
    • Two Chlamydomonas CTR copper transporters with a novel Cys-Met motif are localized to the plasma membrane and function in copper assimilation
    • Page, M.D.; Kropat, J.; Hamel, P.P.; Merchant, S.S. Two Chlamydomonas CTR copper transporters with a novel Cys-Met motif are localized to the plasma membrane and function in copper assimilation. Plant Cell 2009, 21, 928-943.
    • (2009) Plant Cell , vol.21 , pp. 928-943
    • Page, M.D.1    Kropat, J.2    Hamel, P.P.3    Merchant, S.S.4
  • 50
    • 33644867700 scopus 로고    scopus 로고
    • Projection structure of the human copper transporter CTR1 at 6-Ã resolution reveals a compact trimer with a novel channel-like architecture
    • Aller, S.G.; Unger, V.M. Projection structure of the human copper transporter CTR1 at 6-Ã resolution reveals a compact trimer with a novel channel-like architecture. Proc. Natl. Acad. Sci. USA 2006, 103, 3627-3632.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 3627-3632
    • Aller, S.G.1    Unger, V.M.2
  • 51
    • 0016263666 scopus 로고
    • Evidence that tetrodotoxin and saxitoxin act at a metal cation binding site in sodium channels of nerve membrane
    • Henderson, R.; Ritchie, J.M.; Strichartz, G.R. Evidence that tetrodotoxin and saxitoxin act at a metal cation binding site in sodium channels of nerve membrane. Proc. Natl. Acad. Sci. USA 1974, 71, 3936-3940.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 3936-3940
    • Henderson, R.1    Ritchie, J.M.2    Strichartz, G.R.3
  • 52
    • 34248641973 scopus 로고    scopus 로고
    • A structural perspective on copper uptake in eukaryotes
    • De Feo, C.J.; Aller, S.G.; Unger, V.M. A structural perspective on copper uptake in eukaryotes. Biometals 2007, 20, 705-716.
    • (2007) Biometals , vol.20 , pp. 705-716
    • De Feo, C.J.1    Aller, S.G.2    Unger, V.M.3
  • 53
    • 0029843191 scopus 로고    scopus 로고
    • Microalgal metabolites: A new perspective
    • Shimizu, Y. Microalgal metabolites: A new perspective. Annu. Rev. Microbiol. 1996, 50, 431-465.
    • (1996) Annu. Rev. Microbiol. , vol.50 , pp. 431-465
    • Shimizu, Y.1
  • 54
    • 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. App. Environ. Microbiol. 2008, 74, 4044-4053.
    • (2008) App. 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
  • 55
    • 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
  • 56
    • 65549101737 scopus 로고    scopus 로고
    • Characterisation of the paralytic shellfish toxin biosynthesis gene clusters in Anabaena circinalis AWQC131C and Aphanizomenon sp. NH-5
    • 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.
    • (2009) BMC Biochem. , vol.10 , pp. 8
    • Mihali, T.K.1    Kellmann, R.2    Neilan, B.A.3
  • 57
    • 79951844818 scopus 로고    scopus 로고
    • A putative gene cluster from a Lyngbya wollei bloom that encodes paralytic shellfish toxin biosynthesis
    • Mihali, T.K.; Carmichael, W.W.; Neilan, B.A. A putative gene cluster from a Lyngbya wollei bloom that encodes paralytic shellfish toxin biosynthesis. PLoS One 2011, 6, e14657.
    • (2011) PLoS One , vol.6
    • Mihali, T.K.1    Carmichael, W.W.2    Neilan, B.A.3
  • 58
    • 79959953825 scopus 로고    scopus 로고
    • Genomic understanding of dinoflagellates
    • Lin, S.J. Genomic understanding of dinoflagellates. Res. Microbiol. 2011, 162, 551-569.
    • (2011) Res. Microbiol. , vol.162 , pp. 551-569
    • Lin, S.J.1
  • 59
    • 77950397835 scopus 로고    scopus 로고
    • Transcriptome profiling of a toxic dinoflagellate reveals a gene-rich protist and a potential impact on gene expression due to bacterial presence
    • Moustafa, A.; Evans, A.N.; Kulis, D.M.; Hackett, J.D.; Erdner, D.L.; Anderson, D.M.; Bhattacharya, D. Transcriptome profiling of a toxic dinoflagellate reveals a gene-rich protist and a potential impact on gene expression due to bacterial presence. PLoS One 2010, 5, e9688.
    • (2010) PLoS One , vol.5
    • Moustafa, A.1    Evans, A.N.2    Kulis, D.M.3    Hackett, J.D.4    Erdner, D.L.5    Anderson, D.M.6    Bhattacharya, D.7
  • 60
    • 70349202709 scopus 로고    scopus 로고
    • Distinct gene number-genome size relationships for eukaryotes and non-eukaryotes: Gene content estimation for dinoflagellate genomes
    • Hou, Y.; Lin, S. Distinct gene number-genome size relationships for eukaryotes and non-eukaryotes: Gene content estimation for dinoflagellate genomes. PLoS One 2009, 4, e6978.
    • (2009) PLoS One , vol.4
    • Hou, Y.1    Lin, S.2
  • 61
    • 33744788118 scopus 로고    scopus 로고
    • Global transcriptional profiling of the toxic dinoflagellate Alexandrium fundyense using massively parallel signature sequencing
    • Erdner, D.L.; Anderson, D.M. Global transcriptional profiling of the toxic dinoflagellate Alexandrium fundyense using massively parallel signature sequencing. BMC Genomics 2006, 7, 88.
    • (2006) BMC Genomics , vol.7 , pp. 88
    • Erdner, D.L.1    Anderson, D.M.2
  • 64
    • 51449120033 scopus 로고    scopus 로고
    • From stop to start: Tandem gene arrangement, copy number and trans-splicing sites in the dinoflagellate Amphidinium carterae
    • Bachvaroff, T.R.; Place, A.R. From stop to start: Tandem gene arrangement, copy number and trans-splicing sites in the dinoflagellate Amphidinium carterae. PLoS One 2008, 3, e2929.
    • (2008) PLoS One , vol.3
    • Bachvaroff, T.R.1    Place, A.R.2
  • 65
    • 0030832064 scopus 로고    scopus 로고
    • Structure and organization of the peridinin chlorophyll a binding protein gene in Gonyaulax polyedra
    • Le, Q.H.; Markovic, P.; Hastings, J.W.; Jovine, R.V.M.; Morse, D. Structure and organization of the peridinin chlorophyll a binding protein gene in Gonyaulax polyedra. Mol. Gen. Genet. 1997, 255, 595-604.
    • (1997) Mol. Gen. Genet. , vol.255 , pp. 595-604
    • Le, Q.H.1    Markovic, P.2    Hastings, J.W.3    Jovine, R.V.M.4    Morse, D.5
  • 67
    • 84861416517 scopus 로고    scopus 로고
    • Dozens of toxin-related genes are expressed in a nontoxic strain of the dinoflagellate Heterocapsa circularisquama
    • Salcedo, T.; Upadhyay, R.J.; Nagasaki, K.; Bhattacharya, D. Dozens of toxin-related genes are expressed in a nontoxic strain of the dinoflagellate Heterocapsa circularisquama. Mol. Biol. Evol. 2012, 29, 1503-1506.
    • (2012) Mol. Biol. Evol. , vol.29 , pp. 1503-1506
    • Salcedo, T.1    Upadhyay, R.J.2    Nagasaki, K.3    Bhattacharya, D.4
  • 68
    • 0036314609 scopus 로고    scopus 로고
    • Purification and characterization of sulfotransferase specific to O-22 of 11-hydroxy saxitoxin from the toxic dinoflagellate Gymnodinium catenatum (Dinophyceae)
    • Yoshida, T.; Sako, Y.; Uchida, A.; Kakutani, T.; Arakawa, O.; Noguchi, T.; Ishida, Y. Purification and characterization of sulfotransferase specific to O-22 of 11-hydroxy saxitoxin from the toxic dinoflagellate Gymnodinium catenatum (Dinophyceae). Fish. Sci. 2002, 68, 634-642.
    • (2002) Fish. Sci. , vol.68 , pp. 634-642
    • Yoshida, T.1    Sako, Y.2    Uchida, A.3    Kakutani, T.4    Arakawa, O.5    Noguchi, T.6    Ishida, Y.7
  • 69
    • 0035686195 scopus 로고    scopus 로고
    • Purification and characterization of a sulfotransferase specific to N-21 of saxitoxin and gonyautoxin 2 + 3 from the toxic dinoflagellate Gymnodinium catenatum (Dinophyceae)
    • Sako, Y.; Yoshida, T.; Uchida, A.; Arakawa, O.; Noguchi, T.; Ishida, Y. Purification and characterization of a sulfotransferase specific to N-21 of saxitoxin and gonyautoxin 2 + 3 from the toxic dinoflagellate Gymnodinium catenatum (Dinophyceae). J. Phycol. 2001, 37, 1044-1051.
    • (2001) J. Phycol. , vol.37 , pp. 1044-1051
    • Sako, Y.1    Yoshida, T.2    Uchida, A.3    Arakawa, O.4    Noguchi, T.5    Ishida, Y.6
  • 71
    • 77953293293 scopus 로고    scopus 로고
    • Paralytic shellfish poisoning: Seafood safety and human health perspectives
    • Etheridge, S.M. Paralytic shellfish poisoning: Seafood safety and human health perspectives. Toxicon 2010, 56, 108-122.
    • (2010) Toxicon , vol.56 , pp. 108-122
    • Etheridge, S.M.1
  • 73
    • 0034108055 scopus 로고    scopus 로고
    • Marine algal toxins: Origins, health effects, and their increased occurrence
    • Van Dolah, F.M. Marine algal toxins: Origins, health effects, and their increased occurrence. Environ. Health Perspect. 2000, 108, 133-141.
    • (2000) Environ. Health Perspect. , vol.108 , pp. 133-141
    • Van Dolah, F.M.1
  • 74
    • 23844494323 scopus 로고    scopus 로고
    • The effects of harmful algal blooms on aquatic organisms
    • Landsberg, J.H. The effects of harmful algal blooms on aquatic organisms. Rev. Fish. Sci. 2002, 10, 113-390.
    • (2002) Rev. Fish. Sci. , vol.10 , pp. 113-390
    • Landsberg, J.H.1
  • 75
    • 57649201291 scopus 로고    scopus 로고
    • Saxitoxin monitoring in three species of Florida puffer fish
    • Abbott, J.P.; Flewelling, L.J.; Landsberg, J.H. Saxitoxin monitoring in three species of Florida puffer fish. Harmful Algae 2009, 8, 343-348.
    • (2009) Harmful Algae , vol.8 , pp. 343-348
    • Abbott, J.P.1    Flewelling, L.J.2    Landsberg, J.H.3
  • 76
    • 0002800142 scopus 로고
    • A Bacterial Source of Tetrodotoxins and Saxitoxins
    • Hall, S.L., 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.L., Strichartz, G., Eds.; American Chemical Society: Washington, DC, USA, 1990; pp. 78-86.
    • (1990) Marine Toxins: Origin, Structure, and Molecular Pharmacology , pp. 78-86
    • Tamplin, M.L.1
  • 79
    • 84855222244 scopus 로고    scopus 로고
    • Investigations into matrix components affecting the performance of the official bioassay reference method for quantitation of paralytic shellfish poisoning toxins in oysters
    • Turner, A.D.; Dhanji-Rapkova, M.; Algoet, M.; Suarez-Isla, B.A.; Cordova, M.; Caceres, C.; Murphy, C.J.; Casey, M.; Lees, D.N. Investigations into matrix components affecting the performance of the official bioassay reference method for quantitation of paralytic shellfish poisoning toxins in oysters. Toxicon 2012, 59, 215-230.
    • (2012) Toxicon , vol.59 , pp. 215-230
    • Turner, A.D.1    Dhanji-Rapkova, M.2    Algoet, M.3    Suarez-Isla, B.A.4    Cordova, M.5    Caceres, C.6    Murphy, C.J.7    Casey, M.8    Lees, D.N.9
  • 80
    • 51049100398 scopus 로고    scopus 로고
    • Effect of mouse strain and gender on LD50 of yessotoxin
    • Aune, T.; Aasen, J.A.B.; Miles, C.O.; Larsen, S. Effect of mouse strain and gender on LD50 of yessotoxin. Toxicon 2008, 52, 535-540.
    • (2008) Toxicon , vol.52 , pp. 535-540
    • Aune, T.1    Aasen, J.A.B.2    Miles, C.O.3    Larsen, S.4
  • 81
    • 33749636606 scopus 로고    scopus 로고
    • Food and Agricultural Organization Food and Agricultural Organization of the United Nations: Rome, Italy
    • Food and Agricultural Organization. Marine Biotoxins FAO Food and Nutrition Paper 80; Food and Agricultural Organization of the United Nations: Rome, Italy, 2004.
    • (2004) Marine Biotoxins FAO Food and Nutrition Paper 80
  • 82
    • 77953807873 scopus 로고    scopus 로고
    • Comparison of analytical tools and biological assays for detection of paralytic shellfish poisoning toxins
    • Humpage, A.R.; Magalhaes, V.F.; Froscio, S.M. Comparison of analytical tools and biological assays for detection of paralytic shellfish poisoning toxins. Anal. Bioanal. Chem. 2010, 397, 1655-1671.
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 1655-1671
    • Humpage, A.R.1    Magalhaes, V.F.2    Froscio, S.M.3
  • 83
    • 0035865109 scopus 로고    scopus 로고
    • A fluorometric method based on changes in membrane potential for screening paralytic shellfish toxins in mussels
    • Louzao, M.C.; Vieytes, M.R.; Baptista de Sousa, J.M.V.; Leira, F.; Botana, L.M. A fluorometric method based on changes in membrane potential for screening paralytic shellfish toxins in mussels. Anal. Biochem. 2001, 289, 246-250.
    • (2001) Anal. Biochem. , vol.289 , pp. 246-250
    • Louzao, M.C.1    Vieytes, M.R.2    Baptista De Sousa, J.M.V.3    Leira, F.4    Botana, L.M.5
  • 85
    • 0002625573 scopus 로고
    • High-Performance Liquid Chromatographic Method Applied to Paralytic Shellfish Poisoning Research
    • Hall, S., Strichartz, G., Eds.; American Chemical Society: Washington, DC, USA
    • Sullivan, J.J. High-Performance Liquid Chromatographic Method Applied to Paralytic Shellfish Poisoning Research. In Marine Toxins: Origin, Structure, and Molecular Pharmacology; Hall, S., Strichartz, G., Eds.; American Chemical Society: Washington, DC, USA, 1990; pp. 66-77.
    • (1990) Marine Toxins: Origin, Structure, and Molecular Pharmacology , pp. 66-77
    • Sullivan, J.J.1
  • 86
    • 84860280579 scopus 로고    scopus 로고
    • Refinement of AOAC official method (SM) 2005.06 liquid chromatography-fluorescence detection method to improve performance characteristics for the determination of paralytic shellfish toxins in king and queen scallops
    • Turner, A.D.; Hatfield, R.C. Refinement of AOAC official method (SM) 2005.06 liquid chromatography-fluorescence detection method to improve performance characteristics for the determination of paralytic shellfish toxins in king and queen scallops. J. AOAC Int. 2012, 95, 129-142.
    • (2012) J. AOAC Int. , vol.95 , pp. 129-142
    • Turner, A.D.1    Hatfield, R.C.2
  • 87
    • 0347004525 scopus 로고    scopus 로고
    • Analysis of cyanobacterial toxins by hydrophilic interaction liquid chromatography-mass spectrometry
    • Dell'Aversano, C.; Eaglesham, G.K.; Quilliam, M.A. Analysis of cyanobacterial toxins by hydrophilic interaction liquid chromatography-mass spectrometry. J. Chromatogr. A 2004, 1028, 155-164.
    • (2004) J. Chromatogr. A , vol.1028 , pp. 155-164
    • Dell'Aversano, C.1    Eaglesham, G.K.2    Quilliam, M.A.3
  • 88
    • 20544437789 scopus 로고    scopus 로고
    • Hydrophilic interaction liquid chromatography-mass spectrometry for the analysis of paralytic shellfish poisoning (PSP) toxins
    • Dell'Aversano, C.; Hess, P.; Quilliam, M.A. Hydrophilic interaction liquid chromatography-mass spectrometry for the analysis of paralytic shellfish poisoning (PSP) toxins. J. Chromatogr. A 2005, 1081, 190-201.
    • (2005) J. Chromatogr. A , vol.1081 , pp. 190-201
    • Dell'Aversano, C.1    Hess, P.2    Quilliam, M.A.3
  • 89
    • 84855186685 scopus 로고    scopus 로고
    • Verification and quantification of saxitoxin from algal samples using fast and validated hydrophilic interaction liquid chromatography-tandem mass spectrometry method
    • Halme, M.; Rapinoja, M.L.; Karjalainen, M.; Vanninen, P. Verification and quantification of saxitoxin from algal samples using fast and validated hydrophilic interaction liquid chromatography-tandem mass spectrometry method. J. Chromatogr. B 2012, 880, 50-57.
    • (2012) J. Chromatogr. B , vol.880 , pp. 50-57
    • Halme, M.1    Rapinoja, M.L.2    Karjalainen, M.3    Vanninen, P.4
  • 90
    • 0021151286 scopus 로고
    • A competitive displacement assay to detect saxitoxin and tetrodotoxin
    • Davio, S.R.; Fontelo, P.A. A competitive displacement assay to detect saxitoxin and tetrodotoxin. Anal. Biochem. 1984, 141, 199-204.
    • (1984) Anal. Biochem. , vol.141 , pp. 199-204
    • Davio, S.R.1    Fontelo, P.A.2
  • 92
    • 0030908123 scopus 로고    scopus 로고
    • Development and preliminary validation of a microtiter plate-based receptor binding assay for paralytic shellfish poisoning toxins
    • Doucette, G.J.; Logan, M.M.; Ramsdell, J.S.; van Dolah, F.M. Development and preliminary validation of a microtiter plate-based receptor binding assay for paralytic shellfish poisoning toxins. Toxicon 1997, 35, 625-636.
    • (1997) Toxicon , vol.35 , pp. 625-636
    • Doucette, G.J.1    Logan, M.M.2    Ramsdell, J.S.3    Van Dolah, F.M.4
  • 93
    • 3042683314 scopus 로고    scopus 로고
    • Analysis of paralytic shellfish poisoning congeners by a sodium channel receptor binding assay
    • Usup, G.; Leaw, C.-P.; Cheah, M.-Y.; Ahmad, A.; Ng, B.-K. Analysis of paralytic shellfish poisoning congeners by a sodium channel receptor binding assay. Toxicon 2004, 44, 37-43.
    • (2004) Toxicon , vol.44 , pp. 37-43
    • Usup, G.1    Leaw, C.-P.2    Cheah, M.-Y.3    Ahmad, A.4    Ng, B.-K.5
  • 94
    • 85047687338 scopus 로고    scopus 로고
    • Determination of paralytic shellfish toxins in shellfish by Receptor Binding Assay: Collaborative study
    • Van Dolan, F.M.; Fire, S.E.; Leighfield, T.A.; Mikulski, C.M.; Doucette, G.J. Determination of paralytic shellfish toxins in shellfish by Receptor Binding Assay: Collaborative study. J. AOAC Int. 2012, 95, 795-812.
    • (2012) J. AOAC Int. , vol.95 , pp. 795-812
    • Van Dolan, F.M.1    Fire, S.E.2    Leighfield, T.A.3    Mikulski, C.M.4    Doucette, G.J.5
  • 95
    • 0023911188 scopus 로고
    • A tissue culture assay for tetrodotoxin, saxitoxin, and related toxins
    • Kogure, K.; Tamplin, M.L.; Simidu, U.; Colwell, R.R. A tissue culture assay for tetrodotoxin, saxitoxin, and related toxins. Toxicon 1988, 26, 191-197.
    • (1988) Toxicon , vol.26 , pp. 191-197
    • Kogure, K.1    Tamplin, M.L.2    Simidu, U.3    Colwell, R.R.4
  • 96
    • 0026799204 scopus 로고
    • Paralytic shellfish poison (saxitoxin family) bioassays: Automated endpoint determination and stadardization of the in vitro tissue culture bioassay, and comparison with the standard mouse bioassay
    • Jellett, J.F.; Marks, L.J.; Stewart, J.E.; Dorey, M.I.; Watson-Wright, W.; Lawrence, J.F. Paralytic shellfish poison (saxitoxin family) bioassays: Automated endpoint determination and stadardization of the in vitro tissue culture bioassay, and comparison with the standard mouse bioassay. Toxicon 1992, 30, 1143-1156.
    • (1992) Toxicon , vol.30 , pp. 1143-1156
    • Jellett, J.F.1    Marks, L.J.2    Stewart, J.E.3    Dorey, M.I.4    Watson-Wright, W.5    Lawrence, J.F.6
  • 97
    • 0026549496 scopus 로고
    • A tissue culture assay for direct detection of sodium channel blocking toxins in bacterial culture supernatents
    • Gallacher, S.; Birkbeck, T.H. A tissue culture assay for direct detection of sodium channel blocking toxins in bacterial culture supernatents. FEMS Microbiol. Lett. 1992, 92, 101-108.
    • (1992) FEMS Microbiol. Lett. , vol.92 , pp. 101-108
    • Gallacher, S.1    Birkbeck, T.H.2
  • 98
    • 0027521670 scopus 로고
    • Tetrazolium-based bioassay for neurotoxins active on voltage-sensitive sodium channels: Semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins
    • Manger, M.L.; Lega, L.S.; Lee, S.Y.; Hungerford, J.M.; Wekell, M.M. Tetrazolium-based bioassay for neurotoxins active on voltage-sensitive sodium channels: Semiautomated assay for saxitoxins, brevetoxins, and ciguatoxins. Anal. Biochem. 1993, 214, 190-194.
    • (1993) Anal. Biochem. , vol.214 , pp. 190-194
    • Manger, M.L.1    Lega, L.S.2    Lee, S.Y.3    Hungerford, J.M.4    Wekell, M.M.5
  • 99
    • 0032409230 scopus 로고    scopus 로고
    • The MIST (TM) shipable cell bioassay kits for PSP: An alternative to the mouse bioassay
    • Jellett, J.F.; Doucette, L.I.; Belland, E.R. The MIST (TM) shipable cell bioassay kits for PSP: An alternative to the mouse bioassay. J. Shellfish Res. 1998, 17, 1653-1655.
    • (1998) J. Shellfish Res. , vol.17 , pp. 1653-1655
    • Jellett, J.F.1    Doucette, L.I.2    Belland, E.R.3
  • 100
    • 0036236427 scopus 로고    scopus 로고
    • A rapid and sensitive assay for paralytic shellfish poison (PSP) toxins using mouse brain synaptoneurosomes
    • Nicholson, R.A.; Li, G.H.; Buenaventura, E.; Graham, D. A rapid and sensitive assay for paralytic shellfish poison (PSP) toxins using mouse brain synaptoneurosomes. Toxicon 2002, 40, 831-838.
    • (2002) Toxicon , vol.40 , pp. 831-838
    • Nicholson, R.A.1    Li, G.H.2    Buenaventura, E.3    Graham, D.4
  • 101
    • 0242417427 scopus 로고    scopus 로고
    • A fluorimetric microplate assay for detection and quantitation of toxins causing paralytic shellfish poisoning
    • Louzao, M.C.; Vieytes, M.R.; Cabado, A.G.; de Sousa, J.; Botana, L.M. A fluorimetric microplate assay for detection and quantitation of toxins causing paralytic shellfish poisoning. Chem. Res. Toxicol. 2003, 16, 433-438.
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 433-438
    • Louzao, M.C.1    Vieytes, M.R.2    Cabado, A.G.3    De Sousa, J.4    Botana, L.M.5
  • 102
    • 34250156728 scopus 로고    scopus 로고
    • Flow cytometric detection of saxitoxins using fluorescent voltage-sensitive dyes
    • Manger, R.; Woodle, D.; Berger, A.; Hungerford, J. Flow cytometric detection of saxitoxins using fluorescent voltage-sensitive dyes. Anal. Biochem. 2007, 366, 149-155.
    • (2007) Anal. Biochem. , vol.366 , pp. 149-155
    • Manger, R.1    Woodle, D.2    Berger, A.3    Hungerford, J.4
  • 103
    • 0026041714 scopus 로고
    • Direct enzyme immunoassay in microtitration plate and test strip format for the detection of saxitoxin in shellfish
    • Usleber, E.; Schneider, E.; Terplan, G. Direct enzyme immunoassay in microtitration plate and test strip format for the detection of saxitoxin in shellfish. Lett. Appl. Microbiol. 1991, 13, 275-277.
    • (1991) Lett. Appl. Microbiol. , vol.13 , pp. 275-277
    • Usleber, E.1    Schneider, E.2    Terplan, G.3
  • 104
    • 0000731247 scopus 로고
    • Production and characterization of antibodies against neosaxitoxin
    • Chu, F.S.; Huang, X.; Hall, S. Production and characterization of antibodies against neosaxitoxin. J. AOAC Int. 1992, 75, 341-345.
    • (1992) J. AOAC Int. , vol.75 , pp. 341-345
    • Chu, F.S.1    Huang, X.2    Hall, S.3
  • 105
    • 0029189883 scopus 로고
    • Production and characterization of antibodies against neosaxitoxin utilizing a novel immunogen synthesis procedure
    • Burk, C.; Usleber, E.; Dietrich, R.; Martlbauer, E. Production and characterization of antibodies against neosaxitoxin utilizing a novel immunogen synthesis procedure. Food Agric. Immunol. 1995, 7, 315-322.
    • (1995) Food Agric. Immunol. , vol.7 , pp. 315-322
    • Burk, C.1    Usleber, E.2    Dietrich, R.3    Martlbauer, E.4
  • 107
    • 0001250659 scopus 로고    scopus 로고
    • Direct competitive enzyme-linked immunosorbent assay for saxitoxin and neosaxitoxin
    • Huang, X.; Hsu, K.H.; Chu, F.S. Direct competitive enzyme-linked immunosorbent assay for saxitoxin and neosaxitoxin. J. Agric. Food Chem. 1996, 44, 1029-1035.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1029-1035
    • Huang, X.1    Hsu, K.H.2    Chu, F.S.3
  • 108
    • 0036324938 scopus 로고    scopus 로고
    • Development and application of an enzyme immunoassay based on a monoclonal antibody against gonyautoxin components of paralytic shellfish poisoning toxins
    • Kawatsu, K.; Hamano, Y.; Sugiyama, A.; Hashizume, K.; Noguchi, T. Development and application of an enzyme immunoassay based on a monoclonal antibody against gonyautoxin components of paralytic shellfish poisoning toxins. J. Food Prot. 2002, 65, 1304-1308.
    • (2002) J. Food Prot. , vol.65 , pp. 1304-1308
    • Kawatsu, K.1    Hamano, Y.2    Sugiyama, A.3    Hashizume, K.4    Noguchi, T.5
  • 109
    • 77952611311 scopus 로고    scopus 로고
    • Development of ELISAs for detecting domoic acid, okadaic acid, and saxitoxin and their applicability for the detection of marine toxins in samples collected in Belgium
    • Dubois, M.; Demoulin, L.; Charlier, C.; Singh, G.; Godefroy, S.B.; Campbell, K.; Elliott, C.T.; Delahaut, P. Development of ELISAs for detecting domoic acid, okadaic acid, and saxitoxin and their applicability for the detection of marine toxins in samples collected in Belgium. Food Addit. Contam. Part A 2010, 27, 859-868.
    • (2010) Food Addit. Contam. Part A , vol.27 , pp. 859-868
    • Dubois, M.1    Demoulin, L.2    Charlier, C.3    Singh, G.4    Godefroy, S.B.5    Campbell, K.6    Elliott, C.T.7    Delahaut, P.8
  • 110
    • 83155163695 scopus 로고    scopus 로고
    • Examination of the seasonal dynamics of the toxic dinoflagellate Alexandrium catenella at Redondo Beach, California, by quantitative PCR
    • Garneau, M.E.; Schnetzer, A.; Countway, P.D.; Jones, A.C.; Seubert, E.L.; Caron, D.A. Examination of the seasonal dynamics of the toxic dinoflagellate Alexandrium catenella at Redondo Beach, California, by quantitative PCR. Appl. Environ. Microbiol. 2011, 77, 7669-7680.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7669-7680
    • Garneau, M.E.1    Schnetzer, A.2    Countway, P.D.3    Jones, A.C.4    Seubert, E.L.5    Caron, D.A.6
  • 112
    • 84857363009 scopus 로고    scopus 로고
    • A multiplex qPCR targeting hepato- and neurotoxigenic cyanobacteria of global significance
    • Al-Tebrineh, J.; Pearson, L.A.; Yasar, S.A.; Neilan, B.A. A multiplex qPCR targeting hepato- and neurotoxigenic cyanobacteria of global significance. Harmful Algae 2012, 15, 19-25.
    • (2012) Harmful Algae , vol.15 , pp. 19-25
    • Al-Tebrineh, J.1    Pearson, L.A.2    Yasar, S.A.3    Neilan, B.A.4
  • 113
    • 84865189694 scopus 로고    scopus 로고
    • Specific detection of the toxic dinoflagellates Alexandrium tamarense and Alexandrium catenella from single vegetative cells by a loop-mediated isothermal amplification method
    • Nagai, S.; Itakura, S. Specific detection of the toxic dinoflagellates Alexandrium tamarense and Alexandrium catenella from single vegetative cells by a loop-mediated isothermal amplification method. Mar. Genomics 2012, 7, 43-49.
    • (2012) Mar. Genomics , vol.7 , pp. 43-49
    • Nagai, S.1    Itakura, S.2
  • 115
    • 0035940965 scopus 로고    scopus 로고
    • Detection of loop-mediated isothermal amplification reaction by turbidity derived from magnesium pyrophosphate formation
    • Mori, Y.; Nagamine, K.; Tomita, N.; Notomi, T. Detection of loop-mediated isothermal amplification reaction by turbidity derived from magnesium pyrophosphate formation. Biochem. Biophys. Res. Commun. 2001, 289, 150-154.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 150-154
    • Mori, Y.1    Nagamine, K.2    Tomita, N.3    Notomi, T.4
  • 116
    • 0042921125 scopus 로고    scopus 로고
    • Use of loop-mediated isothermal amplification of the IS900 sequence for rapid detection of cultured Mycobacterium avium subsp. paratuberculosi s
    • Enosawa, M.; Kageyama, S.; Sawai, K.; Watanabe, K.; Notomi, T.; Onoe, S.; Mori, Y.; Yokomizo, Y. Use of loop-mediated isothermal amplification of the IS900 sequence for rapid detection of cultured Mycobacterium avium subsp. paratuberculosi s. J. Clin. Microbiol. 2003, 41, 4359-4365.
    • (2003) J. Clin. Microbiol. , vol.41 , pp. 4359-4365
    • Enosawa, M.1    Kageyama, S.2    Sawai, K.3    Watanabe, K.4    Notomi, T.5    Onoe, S.6    Mori, Y.7    Yokomizo, Y.8
  • 117
    • 84864750483 scopus 로고    scopus 로고
    • Application of rRNA probes and fluorescence in situ hybridization for rapid detection of the toxic dinoflagellate Alexandrium minutum
    • Tang, X.H.; Yu, R.C.; Zhou, M.J.; Yu, Z.G. Application of rRNA probes and fluorescence in situ hybridization for rapid detection of the toxic dinoflagellate Alexandrium minutum. Chin. J. Ocean. Limnol. 2012, 30, 256-263.
    • (2012) Chin. J. Ocean. Limnol. , vol.30 , pp. 256-263
    • Tang, X.H.1    Yu, R.C.2    Zhou, M.J.3    Yu, Z.G.4
  • 118
    • 39049165870 scopus 로고    scopus 로고
    • DNA probes, targeting large sub-unit rRNA, for the rapid identification of the paralytic shellfish poison producing dinoflagellate, Gymnodinium catenatum
    • Rhodes, L.; Smith, K.; De Salas, M. DNA probes, targeting large sub-unit rRNA, for the rapid identification of the paralytic shellfish poison producing dinoflagellate, Gymnodinium catenatum. New Z. J. Mar. Freshw. Res. 2007, 41, 385-390.
    • (2007) New Z. J. Mar. Freshw. Res. , vol.41 , pp. 385-390
    • Rhodes, L.1    Smith, K.2    De Salas, M.3
  • 119
    • 0030617896 scopus 로고    scopus 로고
    • Notes on Alexandrium population dynamics
    • Wyatt, T.; Jenkinson, I.R. Notes on Alexandrium population dynamics. J. Plankton Res. 1997, 19, 551-575.
    • (1997) J. Plankton Res. , vol.19 , pp. 551-575
    • Wyatt, T.1    Jenkinson, I.R.2
  • 121
    • 0141684771 scopus 로고    scopus 로고
    • Chemical ecology of eukaryotic microalgae in marine ecosystems
    • Cembella, A.D. Chemical ecology of eukaryotic microalgae in marine ecosystems. Phycologia 2003, 42, 420-447.
    • (2003) Phycologia , vol.42 , pp. 420-447
    • Cembella, A.D.1
  • 122
    • 84986760537 scopus 로고
    • Intracellular localization of saxitoxins in the dinofllagellate Gonyaulax tamarensis
    • Anderson, D.M.; Cheng, T.P.-O. Intracellular localization of saxitoxins in the dinofllagellate Gonyaulax tamarensis. J. Phycol. 1988, 24, 17-22.
    • (1988) J. Phycol. , vol.24 , pp. 17-22
    • Anderson, D.M.1    Cheng, T.P.-O.2
  • 123
    • 0001565275 scopus 로고    scopus 로고
    • Ecophysiology and Metabolism of Paralytic Shellfish Toxins in Marine Microalgae
    • Anderson, D.M., Cembella, A.D., Hallegraeff, G., Eds.; Springer-Verlag: Berlin, Germany
    • Cembella, A.D. Ecophysiology and Metabolism of Paralytic Shellfish Toxins in Marine Microalgae. In Physiological Ecology of Harmful Algal Blooms; Anderson, D.M., Cembella, A.D., Hallegraeff, G., Eds.; Springer-Verlag: Berlin, Germany, 1998; pp. 381-403.
    • (1998) Physiological Ecology of Harmful Algal Blooms , pp. 381-403
    • Cembella, A.D.1
  • 124
    • 37549010308 scopus 로고    scopus 로고
    • Neuroecology, chemical defense, and the keystone species concept
    • Zimmer, R.K.; Ferrer, R.P. Neuroecology, chemical defense, and the keystone species concept. Biol. Bull. 2007, 213, 208-225.
    • (2007) Biol. Bull. , vol.213 , pp. 208-225
    • Zimmer, R.K.1    Ferrer, R.P.2
  • 125
    • 11144239326 scopus 로고    scopus 로고
    • Accumulation and depuration rates of paralytic shellfish poisoning toxins in the shore crab Telmessus acutidens by feeding toxic mussels under laboratory controlled conditions
    • Oikawa, H.; Satomi, M.; Watabe, S.; Yano, Y. Accumulation and depuration rates of paralytic shellfish poisoning toxins in the shore crab Telmessus acutidens by feeding toxic mussels under laboratory controlled conditions. Toxicon 2005, 45, 163-169.
    • (2005) Toxicon , vol.45 , pp. 163-169
    • Oikawa, H.1    Satomi, M.2    Watabe, S.3    Yano, Y.4
  • 126
    • 0001569269 scopus 로고
    • Potential impact of a toxic dinoflagellate (Alexandrium excavatum) bloom on survival of fish and crustacean larvae
    • Robineau, B.; Gagné, J.A.; Fortier, L.; Cembella, A.D. Potential impact of a toxic dinoflagellate (Alexandrium excavatum) bloom on survival of fish and crustacean larvae. Mar. Biol. 1991, 108, 293-301.
    • (1991) Mar. Biol. , vol.108 , pp. 293-301
    • Robineau, B.1    Gagné, J.A.2    Fortier, L.3    Cembella, A.D.4
  • 127
    • 33747194724 scopus 로고    scopus 로고
    • Copepods induce paralytic shellfish toxin production in marine dinoflagellates
    • Selander, E.; Thor, P.; Toth, G.; Pavia, H. Copepods induce paralytic shellfish toxin production in marine dinoflagellates. Proc. R. Soc. B 2006, 273, 1673-1680.
    • (2006) Proc. R. Soc. B , vol.273 , pp. 1673-1680
    • Selander, E.1    Thor, P.2    Toth, G.3    Pavia, H.4
  • 128
    • 42149085005 scopus 로고    scopus 로고
    • Induction of toxin production in dinoflagellates: The grazer makes a difference
    • Bergkvist, J.; Selander, E.; Pavia, H. Induction of toxin production in dinoflagellates: The grazer makes a difference. Oecologia 2008, 156, 147-154.
    • (2008) Oecologia , vol.156 , pp. 147-154
    • Bergkvist, J.1    Selander, E.2    Pavia, H.3
  • 129
    • 0033580619 scopus 로고    scopus 로고
    • Copepod grazing selection and particle discrimination on the basis of PSP toxin content
    • Teegarden, G.J. Copepod grazing selection and particle discrimination on the basis of PSP toxin content. Mar. Ecol. Prog. Ser. 1999, 181, 163-176.
    • (1999) Mar. Ecol. Prog. Ser. , vol.181 , pp. 163-176
    • Teegarden, G.J.1
  • 130
    • 24044552963 scopus 로고    scopus 로고
    • Toxin content and toxic effects of the dinoflagellate Gyrodinium corsicum (Paulmier) on the ingestion and survival rates of the copepods Acartia grani and Euterpina acutifrons
    • Da Costa, R.M.; Franco, J.; Cacho, E.; Fernandez, F. Toxin content and toxic effects of the dinoflagellate Gyrodinium corsicum (Paulmier) on the ingestion and survival rates of the copepods Acartia grani and Euterpina acutifrons . J. Exp. Mar. Biol. Ecol. 2005, 322, 177-183.
    • (2005) J. Exp. Mar. Biol. Ecol. , vol.322 , pp. 177-183
    • Da Costa, R.M.1    Franco, J.2    Cacho, E.3    Fernandez, F.4
  • 131
    • 0034683489 scopus 로고    scopus 로고
    • Short-term and long-term effects of the toxic dinoflagellate Alexandrium minutum on the copepod Acartia clausi
    • Frangoulos, M.; Guisande, C.; Maneiro, I.; Riveiro, I.; Franco, J. Short-term and long-term effects of the toxic dinoflagellate Alexandrium minutum on the copepod Acartia clausi. Mar. Ecol. Prog. Ser. 2000, 203, 161-169.
    • (2000) Mar. Ecol. Prog. Ser. , vol.203 , pp. 161-169
    • Frangoulos, M.1    Guisande, C.2    Maneiro, I.3    Riveiro, I.4    Franco, J.5
  • 133
    • 0001687194 scopus 로고    scopus 로고
    • Toxic marine phytoplankton, zooplankton grazers, and pelagic food webs
    • Turner, J.T.; Tester, P.A. Toxic marine phytoplankton, zooplankton grazers, and pelagic food webs. Limnol. Oceanogr. 1997, 42, 1203-1214.
    • (1997) Limnol. Oceanogr. , vol.42 , pp. 1203-1214
    • Turner, J.T.1    Tester, P.A.2
  • 134
    • 33646569539 scopus 로고    scopus 로고
    • Biological control of harmful algal blooms: A modelling study
    • Solé, J.; Estrada, M.; Garcia-Ladona, E. Biological control of harmful algal blooms: A modelling study. J. Mar. Syst. 2006, 61, 165-179.
    • (2006) J. Mar. Syst. , vol.61 , pp. 165-179
    • Solé, J.1    Estrada, M.2    Garcia-Ladona, E.3
  • 135
    • 0037023627 scopus 로고    scopus 로고
    • Toxic effects of Alexandrium spp. on heterotrophic dinoflagellates: An allelochemical defence mechanism independent of PSP-toxin content
    • Tillmann, U.; John, U. Toxic effects of Alexandrium spp. on heterotrophic dinoflagellates: An allelochemical defence mechanism independent of PSP-toxin content. Mar. Ecol. Prog. Ser. 2002, 230, 47-59.
    • (2002) Mar. Ecol. Prog. Ser. , vol.230 , pp. 47-59
    • Tillmann, U.1    John, U.2
  • 136
    • 45849154263 scopus 로고    scopus 로고
    • Toxicity of Alexandrium lusitanicum to gastropod larvae is not caused by paralytic-shellfish-poisoning toxins
    • Juhl, A.R.; Martins, C.A.; Anderson, D.M. Toxicity of Alexandrium lusitanicum to gastropod larvae is not caused by paralytic-shellfish-poisoning toxins. Harmful Algae 2008, 7, 567-573.
    • (2008) Harmful Algae , vol.7 , pp. 567-573
    • Juhl, A.R.1    Martins, C.A.2    Anderson, D.M.3


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