{"refrec":{"BRefID":238166,"RR":"<b>Orts, D.J.B.; Moran, Y.; Cologna, C.T.; Peigneur, S.; Madio, B.; Praher, D.; Quinton, L.; De Pauw, E.; Bicudo, J.E.P.W.; Tytgat, J.; de Freitas, J.C.</b> (2013). BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker. <i>The FEBS Journal 280(19)</i>: 4839-4852. <a href=\"http://dx.doi.org/10.1111/febs.12456\" target=\"_blank\">dx.doi.org/10.1111/febs.12456</a>","BEntID":229853,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>The FEBS Journal 280(19)</i>: 4839-4852. <a href=\"https://dx.doi.org/10.1111/febs.12456\" target=\"_blank\">https://dx.doi.org/10.1111/febs.12456</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Orts, D.J.B.; Moran, Y.; Cologna, C.T.; Peigneur, S.; Madio, B.; Praher, D.; Quinton, L.; De Pauw, E.; Bicudo, J.E.P.W.; Tytgat, J.; de Freitas, J.C.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Orts, D.J.B. <i>et al.</i>","Englishabstract":"Sea anemone venoms have become a rich source of peptide toxins which are invaluable tools for studying the structure and functions of ion channels. In this work, BcsTx3, a toxin found in the venom of a <em>Bunodosoma&nbsp;caissarum</em> (population captured at the Saint Peter and Saint Paul Archipelago, Brazil) was purified and biochemically and pharmacologically characterized. The pharmacological effects were studied on 12 different subtypes of voltage-gated potassium channels (K<sub>V</sub>1.1&ndash;K<sub>V</sub>1.6; K<sub>V</sub>2.1; K<sub>V</sub>3.1; K<sub>V</sub>4.2; K<sub>V</sub>4.3; <em>h</em>ERG and Shaker IR) and three cloned voltage-gated sodium channel isoforms (Na<sub>V</sub>1.2, Na<sub>V</sub>1.4 and BgNa<sub>V</sub>1.1) expressed in <em>Xenopus&nbsp;laevis</em> oocytes. BcsTx3 shows a high affinity for Drosophila Shaker IR channels over rKv1.2, hKv1.3 and rKv1.6, and is not active on Na<sub>V</sub> channels. Biochemical characterization reveals that BcsTx3 is a 50 amino acid peptide crosslinked by four disulfide bridges, and sequence comparison allowed BcsTx3 to be classified as a novel type of sea anemone toxin acting on K<sub>V</sub> channels. Moreover, putative toxins homologous to BcsTx3 from two additional actiniarian species suggest an ancient origin of this newly discovered toxin family.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"BcsTx3 is a founder of a novel sea anemone toxin family of potassium channel blocker","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2024-12-10 01:32:52.928458","timezone_type":1,"timezone":"+01:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"Bunodosomacaissarum; potassium channel toxin; Saint Peter and Saint PaulArchipelago; sea anemone; sequence alignment","OtherDescriptors":null,"Notes":null,"AnaPub":2013,"MonPub":null,"DateUpdate":"2014-05-26","DateCreate":"2014-05-18","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000327130600011","VABBcode":null,"OpenAcc":0,"DOI":"10.1111/febs.12456"},"refs":null,"anarec":{"AnaID":238166,"PubliDate":2013,"Pagination":"4839-4852","XtraPublOfAnaID":null,"ISBN":null,"Volume":"280","Issue":"19","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":235768,"SerRR":"The FEBS Journal. Wiley-Blackwell: Oxford.  ISSN 1742-464X; e-ISSN 1742-4658","StandardTitleSer":"The FEBS Journal","ISSN":"1742-464X","AbbrevSer":null,"StandardTitleMon":null,"StartPage":4839,"Pages":14,"ToPubliDate":null,"BRefBibLvlCode":"S","SerNotes":null},"monrec":null,"serrec":null,"relations":null,"relationsRev":null,"addrec":null,"othpubs":null,"ownerships":null,"authors":[{"AutName":"Orts","Firstname":null,"Initials":"D.J.B.","Affiliation":"Univ Sao Paulo, Inst Biosci, Dept Physiol, BR-05508 Sao Paulo,Brazil.","Discriminator":null,"CorporateFlag":0,"BEntID":229853,"AutID":178345,"OrderNr":1,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Moran","Firstname":null,"Initials":"Y.","Affiliation":"Univ Vienna, Fac Life Sci, Dept MolEvolut & Dev, A-1010 Vienna, Austria.","Discriminator":null,"CorporateFlag":0,"BEntID":229853,"AutID":178346,"OrderNr":2,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":null,"InsFSN":null,"ORCID":null,"PersID":null,"InsID":null},{"AutName":"Cologna","Firstname":"Camila","Initials":"C.T.","Affiliation":"Laboratory of Mass Spectrometry, Department of Chemistry, University of Liège","Discriminator":null,"CorporateFlag":0,"BEntID":229853,"AutID":178347,"OrderNr":3,"DegrID":null,"EditorFlag":0,"CorrespFlag":0,"IllustratorFlag":0,"ReviserFlag":0,"TranslatorFlag":0,"InsAcronym":"MSLAB","InsFSN":"Université de Liège; 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