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Acute Hepatopancreatic Necrosis Disease (AHPND): virulence, pathogenesis and mitigation strategies in shrimp aquaculture. <i>Toxins 13(8)</i>: 524. <a href=\"https://dx.doi.org/10.3390/toxins13080524\" target=\"_blank\">https://dx.doi.org/10.3390/toxins13080524</a>","StandardTitle":"Acute Hepatopancreatic Necrosis Disease (AHPND): virulence, pathogenesis and mitigation strategies in shrimp aquaculture","AuthorsString":"Kumar, V. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":353036,"RR":"<b>Abdallah, M.F.; Van Hassel, W.H.R.; Andjelkovic, M.; Wilmotte, A.; Rajkovic, A.</b> (2021). Cyanotoxins and food contamination in developing countries: review of their types, toxicity, analysis, occurrence and mitigation strategies. <i>Toxins 13(11)</i>: 786. <a href=\"https://dx.doi.org/10.3390/toxins13110786\" target=\"_blank\">https://dx.doi.org/10.3390/toxins13110786</a>","StandardTitle":"Cyanotoxins and food contamination in developing countries: review of their types, toxicity, analysis, occurrence and mitigation strategies","AuthorsString":"Abdallah, M.F. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":347850,"RR":"<b>Katikou, P.</b> (2021). Digital technologies and open data sources in marine biotoxins’ risk analysis: the case of ciguatera fish poisoning. <i>Toxins 13(10)</i>: 692. <a href=\"https://dx.doi.org/10.3390/toxins13100692\" target=\"_blank\">https://dx.doi.org/10.3390/toxins13100692</a>","StandardTitle":"Digital technologies and open data sources in marine biotoxins’ risk analysis: the case of ciguatera fish poisoning","AuthorsString":"Katikou, P.","BibLvlCode":"AS"},{"BRefID":245577,"RR":"<b>Silva, M.; Pratheepa, V.K.; Botana, L.M.; Vasconcelos, V.</b> (2015). Emergent toxins in North Atlantic temperate waters: a challenge for monitoring programs and legislation. <i>Toxins 7(3)</i>: 859-885. <a href=\"http://dx.doi.org/10.3390/toxins7030859\" target=\"_blank\">http://dx.doi.org/10.3390/toxins7030859</a>","StandardTitle":"Emergent toxins in North Atlantic temperate waters: a challenge for monitoring programs and legislation","AuthorsString":"Silva, M. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":381479,"RR":"<b>Barroso, R.A.; Ramos, L.; Moreno, H.; Antunes, A.</b> (2024). Evolutionary analysis of Cnidaria Small Cysteine-Rich Proteins (SCRiPs), an enigmatic neurotoxin family from stony corals and sea anemones (Anthozoa: Hexacorallia). <i>Toxins 16(2)</i>: 75. <a href=\"https://dx.doi.org/10.3390/toxins16020075\" target=\"_blank\">https://dx.doi.org/10.3390/toxins16020075</a>","StandardTitle":"Evolutionary analysis of Cnidaria Small Cysteine-Rich Proteins (SCRiPs), an enigmatic neurotoxin family from stony corals and sea anemones (Anthozoa: Hexacorallia)","AuthorsString":"Barroso, R.A. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":409650,"RR":"<b>Tomaševic, T.; Arapov, J.; Ujevic, I.; Bonacic, T.; Bužancic, M.; Bulic, A.; Skejic, S.; Roje-Busatto, R.; Ninčević Gladan, Z</b> (2025). Growth dynamics and toxin production of <i>Pseudo-nitzschia</i> species isolated from the Central Adriatic Sea. <i>Toxins 17(6)</i>: 307. <a href=\"https://dx.doi.org/10.3390/toxins17060307\" target=\"_blank\">https://dx.doi.org/10.3390/toxins17060307</a>","StandardTitle":"Growth dynamics and toxin production of <i>Pseudo-nitzschia</i> species isolated from the Central Adriatic Sea","AuthorsString":"Tomaševic, T. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":394223,"RR":"<b>Asakawa, M.; Ito, K.; Kajihara, H.</b> (2013). Highly toxic ribbon worm <i>Cephalothrix simula</i> containing tetrodotoxin in Hiroshima Bay, Hiroshima Prefecture, Japan. <i>Toxins 5(2)</i>: 376-395. <a href=\"https://dx.doi.org/10.3390/toxins5020376\" target=\"_blank\">https://dx.doi.org/10.3390/toxins5020376</a>","StandardTitle":"Highly toxic ribbon worm <i>Cephalothrix simula</i> containing tetrodotoxin in Hiroshima Bay, Hiroshima Prefecture, Japan","AuthorsString":"Asakawa, M.; Ito, K.; Kajihara, H.","BibLvlCode":"AS"},{"BRefID":304809,"RR":"<b>Remigante, A.; Costa, R.; Morabito, R.; La Spada, G.; Marino, A.; Dossena, S.</b> (2018). Impact of scyphozoan venoms on human health and current first aid options for stings. <i>Toxins 10(4)</i>: 133. <a href=\"https://dx.doi.org/10.3390/toxins10040133\" target=\"_blank\">https://dx.doi.org/10.3390/toxins10040133</a>","StandardTitle":"Impact of scyphozoan venoms on human health and current first aid options for stings","AuthorsString":"Remigante, A. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":197335,"RR":"<b>Gerssen, A.; Pol-Hofstad, I.E.; Poelman, M.; Mulder, P.P.J.; van den Top, H.J.</b> (2010). Marine toxins: Chemistry, toxicity, occurrence and detection, with special reference to the Dutch situation. <i>Toxins 2(4)</i>: 878-904. <a href=\"http://dx.doi.org/10.3390/toxins2040878\" target=\"_blank\">http://dx.doi.org/10.3390/toxins2040878</a>","StandardTitle":"Marine toxins: Chemistry, toxicity, occurrence and detection, with special reference to the Dutch situation","AuthorsString":"Gerssen, A. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":347887,"RR":"<b>Coelho, G.R.; da Silva, D.L.; Beraldo-Neto, E.; Vigerelli, H.; de Oliveira, L.A.; Sciani, J.M.; Pimenta, D.C.</b> (2021). Neglected venomous animals and toxins: underrated biotechnological tools in drug development. <i>Toxins 13(12)</i>: 851. <a href=\"https://dx.doi.org/10.3390/toxins13120851\" target=\"_blank\">https://dx.doi.org/10.3390/toxins13120851</a>","StandardTitle":"Neglected venomous animals and toxins: underrated biotechnological tools in drug development","AuthorsString":"Coelho, G.R. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":338045,"RR":"<b>Kalina, R.S.; Peigneur, S.; Zelepuga, E.A.; Dmitrenok, P.S.; Kvetkina, A.N.; Kim, N.Y.; Leychenko, E.V.; Tytgat, J.; Kozlovskaya, E.P.; Monastyrnaya, M.M.; Gladkikh, I.N.</b> (2020). New insights into the type II toxins from the sea anemone <i>Heteractis crispa</i>. <i>Toxins 12(1)</i>: 44. <a href=\"https://hdl.handle.net/10.3390/toxins12010044\" target=\"_blank\">https://hdl.handle.net/10.3390/toxins12010044</a>","StandardTitle":"New insights into the type II toxins from the sea anemone <i>Heteractis crispa</i>","AuthorsString":"Kalina, R.S. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":359345,"RR":"<b>Dzhembekova, N.; Moncheva, S.; Slabakova, N.; Zlateva, I.; Nagai, S.; Wietkamp, S.; Wellkamp, M.; Tillmann, U.; Krock, B.</b> (2022). New knowledge on distribution and abundance of toxic microalgal species and related toxins in the Northwestern Black Sea. <i>Toxins 14(10)</i>: 685. <a href=\"https://dx.doi.org/10.3390/toxins14100685\" target=\"_blank\">https://dx.doi.org/10.3390/toxins14100685</a>","StandardTitle":"New knowledge on distribution and abundance of toxic microalgal species and related toxins in the Northwestern Black Sea","AuthorsString":"Dzhembekova, N. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":362446,"RR":"<b>Kalina, R.S.; Kasheverov, I.E.; Koshelev, S.G.; Sintsova, O.V.; Peigneur, S.; Pinheiro-Junior, E.L.; Popov, R.S.; Chausova, V.; Monastyrnaya, M.M.; Dmitrenok, P.S.; Isaeva, M.P.; Tytgat, J.; Kozlov, S.A.; Kozlovskaya, E.P.; Leychenko, E.V.; Gladkikh, I.N.</b> (2022). Nicotinic acetylcholine receptors are novel targets of APETx-like toxins from the sea anemone <i>Heteractis magnifica</i>. <i>Toxins 14(10)</i>: 697. <a href=\"https://dx.doi.org/10.3390/toxins14100697\" target=\"_blank\">https://dx.doi.org/10.3390/toxins14100697</a>","StandardTitle":"Nicotinic acetylcholine receptors are novel targets of APETx-like toxins from the sea anemone <i>Heteractis magnifica</i>","AuthorsString":"Kalina, R.S. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":308017,"RR":"<b>Rodríguez, A.A.; Garateix, A.; Salceda, E.; Peigneur, S.; Zaharenko, A.J.; Pons, T.; Santos, Y.; Arreguin, R.; Ständker, L.; Forssmann, W.-G.; Tytgat, J.; Vega, R.; Soto, E.</b> (2018). PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone <i>Phymanthus crucifer</i>. <i>Toxins 10(2)</i>: 72. <a href=\"https://dx.doi.org/10.3390/toxins10020072\" target=\"_blank\">https://dx.doi.org/10.3390/toxins10020072</a>","StandardTitle":"PhcrTx2, a new crab-paralyzing peptide toxin from the sea anemone <i>Phymanthus crucifer</i>","AuthorsString":"Rodríguez, A.A. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":322825,"RR":"<b>Kumar, V.; De Bels, L.; Couck, L.; Baruah, K.; Bossier, P.; Van Den Broeck, W.</b> (2019). PirAB<sup>VP</sup> toxin binds to epithelial cells of the digestive tract and produce pathognomonic AHPND lesions in germ-free brine shrimp. <i>Toxins 11(12)</i>: 717. <a href=\"https://dx.doi.org/10.3390/toxins11120717\" target=\"_blank\">https://dx.doi.org/10.3390/toxins11120717</a>","StandardTitle":"PirAB<sup>VP</sup> toxin binds to epithelial cells of the digestive tract and produce pathognomonic AHPND lesions in germ-free brine shrimp","AuthorsString":"Kumar, V. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":381544,"RR":"<b>Hoepner, C.M.; Stewart, Z.K.; Qiao, R.; Fobert, E.K.; Prentis, P.J.; Colella, A.; Chataway, T.; Burke da Silva, K.; Abbott, C.A.</b> (2024). Proteotransciptomics of the most popular host sea anemone <i>Entacmaea quadricolor</i> reveals not all toxin genes expressed by tentacles are recruited into its venom arsenal. <i>Toxins 16(2)</i>: 85. <a href=\"https://dx.doi.org/10.3390/toxins16020085\" target=\"_blank\">https://dx.doi.org/10.3390/toxins16020085</a>","StandardTitle":"Proteotransciptomics of the most popular host sea anemone <i>Entacmaea quadricolor</i> reveals not all toxin genes expressed by tentacles are recruited into its venom arsenal","AuthorsString":"Hoepner, C.M. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":362021,"RR":"<b>Kryuchkov, F.; Robertson, A.; Mudge, E.M.; Miles, C.O.; Van Gothem, S.; Uhlig, S.</b> (2022). Reductive amination for LC-MS signal enhancement and confirmation of the presence of Caribbean ciguatoxin-1 in fish. <i>Toxins 14(6)</i>: 399. <a href=\"https://dx.doi.org/10.3390/toxins14060399\" target=\"_blank\">https://dx.doi.org/10.3390/toxins14060399</a>","StandardTitle":"Reductive amination for LC-MS signal enhancement and confirmation of the presence of Caribbean ciguatoxin-1 in fish","AuthorsString":"Kryuchkov, F. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":395811,"RR":"<b>Melnikova, D.I.; Nijland, R.; Magarlamov, T.Y.</b> (2021). The first data on the complete genome of a tetrodotoxin-producing bacterium. <i>Toxins 13(6)</i>: 410. <a href=\"https://dx.doi.org/10.3390/toxins13060410\" target=\"_blank\">https://dx.doi.org/10.3390/toxins13060410</a>","StandardTitle":"The first data on the complete genome of a tetrodotoxin-producing bacterium","AuthorsString":"Melnikova, D.I.; Nijland, R.; Magarlamov, T.Y.","BibLvlCode":"AS"},{"BRefID":280628,"RR":"<b>García-Fernández, R.; Peigneur, S.; Pons, T.; Alvarez, C.; González, L.; Chávez, M.A.; Tytgat, J.</b> (2016). The Kunitz-type protein ShPI-1 inhibits serine proteases and voltage-gated potassium channels. <i>Toxins 8(4)</i>: 110. <a href=\"http://dx.doi.org/10.3390/toxins8040110\" target=\"_blank\">dx.doi.org/10.3390/toxins8040110</a>","StandardTitle":"The Kunitz-type protein ShPI-1 inhibits serine proteases and voltage-gated potassium channels","AuthorsString":"García-Fernández, R. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":310869,"RR":"<b>Goransson, U.; Jacobsson, E.; Strand, M.; Andersson, H.S.</b> (2019). The toxins of nemertean worms. <i>Toxins 11(2)</i>: 120. <a href=\"https://dx.doi.org/10.3390/toxins11020120\" target=\"_blank\">https://dx.doi.org/10.3390/toxins11020120</a>","StandardTitle":"The toxins of nemertean worms","AuthorsString":"Goransson, U. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":418973,"RR":"<b>Kwambai, C.S.; Ennaceri, H.; Lymbery, A.J.; Laird, D.W.; Cosgrove, J.; Moheimani, N.R.</b> (2025). Toxic <i>Alexandrium</i> treatment in Western Australia: Investigating the efficacy of modified nano clay. <i>Toxins 17(10)</i>: 495. <a href=\"https://dx.doi.org/10.3390/toxins17100495\" target=\"_blank\">https://dx.doi.org/10.3390/toxins17100495</a>","StandardTitle":"Toxic <i>Alexandrium</i> treatment in Western Australia: Investigating the efficacy of modified nano clay","AuthorsString":"Kwambai, C.S. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":317958,"RR":"<b>Fassio, G.; Modica, M.V.; Mary, L.; Zaharias, P.; Fedosov, A.E.; Gorson, J.; Kantor, Y.I.; Holford, M.; Puillandre, N.</b> (2019). Venom diversity and evolution in the most divergent cone snail genus <i>Profundiconus</i>. <i>Toxins 11(11)</i>: 623. <a href=\"https://dx.doi.org/10.3390/toxins11110623\" target=\"_blank\">https://dx.doi.org/10.3390/toxins11110623</a>","StandardTitle":"Venom diversity and evolution in the most divergent cone snail genus <i>Profundiconus</i>","AuthorsString":"Fassio, G. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":289047,"RR":"<b>Sousa, S.; Vetter, I.; Lewis, R.</b> (2013). Venom peptides as a rich source of Ca<sub>v</sub>2.2 channel blockers. <i>Toxins 5(2)</i>: 286-314. <a href=\"https://dx.doi.org/10.3390/toxins5020286\" target=\"_blank\">https://dx.doi.org/10.3390/toxins5020286</a>","StandardTitle":"Venom peptides as a rich source of Ca<sub>v</sub>2.2 channel blockers","AuthorsString":"Sousa, S. <i>et al.</i>","BibLvlCode":"AS"},{"BRefID":238277,"RR":"<b>Kendel, Y.; Melaun, C.; Kurz, A.; Nicke, A.; Peigneur, S.; Tytgat, J.; Wunder, C.; Mebs, D.; Kauferstein, S.</b> (2013). Venomous secretions from marine snails of the Terebridae family target acetylcholine receptors. <i>Toxins 5(5)</i>: 1043-1050. <a href=\"http://dx.doi.org/10.3390/toxins5051043\" target=\"_blank\">dx.doi.org/10.3390/toxins5051043</a>","StandardTitle":"Venomous secretions from marine snails of the Terebridae family target acetylcholine receptors","AuthorsString":"Kendel, Y. <i>et al.</i>","BibLvlCode":"AS"}],"BEntOpen":null,"BEntPrivate":null,"availability":null,"litstyles":null,"thespers":null,"arch2discl":null,"SERpubls":null,"MONpubls":null,"pictures":[],"thestermsPath":null,"thestermsASFA":null,"taxtermsASFA":null,"geotermsASFA":null,"collections":null,"conf":null,"proj":null,"Physdatasets":null,"spcols":null,"doi":null,"publs":[{"PublID":15325,"PublName":"Multidisciplinary Digital Publishing Institute (MDPI)","InsID":null,"PersID":null,"INBOID":null,"OrderNr":1}],"serparttypes":["A"],"monauthors":null,"MParts":null,"SParts":null,"hLibs":null,"langs":[{"BEntID":189743,"AbstractFlag":0,"LangID":15,"LangCode":"en","Lang":"English","DutchTerm":"Engels","LangCodeExtended":"eng"}],"urls":[{"URL":"http://www.mdpi.com/journal/toxins/","externalID":null,"URLTypeCode":null,"URLID":124835,"URLTypID":22,"URLType":"Journal home page","URLPrefix":null},{"URL":"https://doaj.org/toc/f056f0d9a3594cec869f8793e809bff2","externalID":null,"URLTypeCode":"DOAJ","URLID":127569,"URLTypID":48,"URLType":"DOAJ","URLPrefix":"https://doaj.org/"},{"URL":"www.mdpi.com/journal/toxins","externalID":null,"URLTypeCode":null,"URLID":122142,"URLTypID":null,"URLType":null,"URLPrefix":null}],"thesterms":null,"taxterms":null,"geoterms":null,"othterms":null,"asfacodes":null,"asfa2codes":null,"thestermsFRIS":null,"taxtermsFRIS":null,"geotermsFRIS":null,"othtermsFRIS":null,"resmessage":"","complete":1,"sessions":{"newSesName":"Chisala, Chilekwa, C.","newSesDate":{"date":"2010-07-13 11:50:14.667000","timezone_type":3,"timezone":"Europe/Brussels"},"updSesName":"Bouchti, Zohra, Z.","updSesDate":{"date":"2024-01-22 08:20:48.030000","timezone_type":3,"timezone":"Europe/Brussels"}}}