{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,13]],"date-time":"2026-05-13T18:18:58Z","timestamp":1778696338834,"version":"3.51.4"},"reference-count":58,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,12,1]],"date-time":"2017-12-01T00:00:00Z","timestamp":1512086400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"Agency for Innovation by Science and Technology"},{"name":"IUAP"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Peptides"],"published-print":{"date-parts":[[2017,12]]},"DOI":"10.1016\/j.peptides.2016.08.008","type":"journal-article","created":{"date-parts":[[2016,9,3]],"date-time":"2016-09-03T05:41:24Z","timestamp":1472881284000},"page":"43-50","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":18,"special_numbering":"C","title":["Expanding the pharmacological profile of \u03ba-hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel Kv10.1"],"prefix":"10.1016","volume":"98","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7173-7195","authenticated-orcid":false,"given":"Lien","family":"Moreels","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Steve","family":"Peigneur","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoko","family":"Yamaguchi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kim","family":"Vriens","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Etienne","family":"Waelkens","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shunyi","family":"Zhu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karin","family":"Thevissen","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8087-4768","authenticated-orcid":false,"given":"Bruno P.A.","family":"Cammue","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kazuki","family":"Sato","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jan","family":"Tytgat","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.peptides.2016.08.008_bib0005","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.actatropica.2008.05.021","article-title":"Epidemiology of scorpionism: a global appraisal","volume":"107","author":"Chippaux","year":"2008","journal-title":"Acta Trop."},{"key":"10.1016\/j.peptides.2016.08.008_bib0010","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1177\/1535370213513991","article-title":"Scorpion venoms as a potential source of novel cancer therapeutic compounds","volume":"239","author":"Ding","year":"2014","journal-title":"Exp. Biol. Med. (Maywood)."},{"key":"10.1016\/j.peptides.2016.08.008_bib0015","doi-asserted-by":"crossref","first-page":"2137","DOI":"10.3390\/toxins6072137","article-title":"Scorpions: a presentation","volume":"6","author":"Goyffon","year":"2014","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.peptides.2016.08.008_bib0020","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.pediatrneurol.2007.09.007","article-title":"Channelopathies: a review","volume":"38","author":"Bernard","year":"2008","journal-title":"Pediatr. Neurol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0025","first-page":"4871","article-title":"Use of chlorotoxin for targeting of primary brain tumors","volume":"58","author":"Soroceanu","year":"1998","journal-title":"Cancer Res."},{"key":"10.1016\/j.peptides.2016.08.008_bib0030","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.3390\/toxins7041079","article-title":"Chlorotoxin: a helpful natural scorpion peptide to diagnose glioma and fight tumor invasion","volume":"7","author":"Dardevet","year":"2015","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.peptides.2016.08.008_bib0035","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1134\/S1068162014040013","article-title":"Chlorotoxin and related peptides. Short insect toxins from scorpion venom","volume":"40","author":"Arzamasov","year":"2014","journal-title":"Russ. J. Bioorg. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0040","doi-asserted-by":"crossref","first-page":"30040","DOI":"10.1074\/jbc.M111258200","article-title":"kappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function Importance of the functional diad in potassium channel selectivity","volume":"277","author":"Srinivasan","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0045","first-page":"289","article-title":"Diversity of potassium channel ligands: focus on scorpion toxins","volume":"55","author":"Kuzmenkov","year":"2015","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2016.08.008_bib0050","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/S0165-6147(99)01398-X","article-title":"A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies","volume":"20","author":"Tytgat","year":"1999","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.peptides.2016.08.008_bib0055","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.toxicon.2004.03.022","article-title":"Current views on scorpion toxins specific for K+-channels","volume":"43","author":"Rodr\u00edguez de la Vega","year":"2004","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0060","doi-asserted-by":"crossref","first-page":"e60201","DOI":"10.1371\/journal.pone.0060201","article-title":"Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins","volume":"8","author":"Chen","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.peptides.2016.08.008_bib0065","doi-asserted-by":"crossref","first-page":"2471","DOI":"10.1002\/pmic.200900763","article-title":"Molecular diversity of toxic components from the scorpion Heterometrus petersii venom revealed by proteomic and transcriptome analysis","volume":"10","author":"Ma","year":"2010","journal-title":"Proteomics"},{"key":"10.1016\/j.peptides.2016.08.008_bib0070","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1042\/BJ20041705","article-title":"An unusual fold for potassium channel blockers: NMR structure of three toxins from the scorpion Opisthacanthus madagascariensis","volume":"388","author":"Chagot","year":"2005","journal-title":"Biochem. J."},{"key":"10.1016\/j.peptides.2016.08.008_bib0075","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.toxicon.2009.04.010","article-title":"Cloning and characterization of cDNA sequences encoding for new venom peptides of the Brazilian scorpion Opisthacanthus cayaporum","volume":"54","author":"Silva","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0080","doi-asserted-by":"crossref","first-page":"1509","DOI":"10.1016\/j.peptides.2011.05.017","article-title":"The new kappa-KTx 2.5 from the scorpion Opisthacanthus cayaporum","volume":"32","author":"Camargos","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.peptides.2016.08.008_bib0085","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1016\/j.toxicon.2008.03.029","article-title":"Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum","volume":"51","author":"Schwartz","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0090","doi-asserted-by":"crossref","first-page":"e35154","DOI":"10.1371\/journal.pone.0035154","article-title":"Structural and functional diversity of acidic scorpion potassium channel toxins","volume":"7","author":"Chen","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.peptides.2016.08.008_bib0095","doi-asserted-by":"crossref","DOI":"10.1093\/database\/baw056","article-title":"Kalium: a database of potassium channel toxins from scorpion venom","author":"Kuzmenkov","year":"2016","journal-title":"Database (Oxford)"},{"key":"10.1016\/j.peptides.2016.08.008_bib0100","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1016\/j.toxicon.2012.03.010","article-title":"The UniProtKB\/Swiss-Prot Tox-Prot program: a central hub of integrated venom protein data","volume":"60","author":"Jungo","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0105","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/j.bcp.2012.01.021","article-title":"Purification, molecular cloning and functional characterization of HelaTx1 (Heterometrus laoticus): The first member of a new kappa-KTX subfamily","volume":"83","author":"Vandendriessche","year":"2012","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0110","doi-asserted-by":"crossref","first-page":"12321","DOI":"10.1074\/jbc.M111.329607","article-title":"New tricks of an old pattern: structural versatility of scorpion toxins with common cysteine spacing","volume":"287","author":"Saucedo","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0115","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.bcp.2004.10.018","article-title":"Assignment of voltage-gated potassium channel blocking activity to kappa-KTx1.3, a non-toxic homologue of kappa-hefutoxin-1, from Heterometrus spinifer venom","volume":"69","author":"Nirthanan","year":"2005","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0120","doi-asserted-by":"crossref","first-page":"13813","DOI":"10.1074\/jbc.M112.343996","article-title":"Hg1, novel peptide inhibitor specific for Kv1.3 channels from first scorpion Kunitz-type potassium channel toxin family","volume":"287","author":"Chen","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0125","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1002\/jbt.20382","article-title":"ImKTx1, a new Kv1.3 channel blocker with a unique primary structure","volume":"25","author":"Chen","year":"2011","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0130","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1042\/BSR20130052","article-title":"Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold","volume":"33","author":"Gao","year":"2013","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.peptides.2016.08.008_bib0135","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.toxicon.2013.05.010","article-title":"Synthesis and characterization of amino acid deletion analogs of \u03ba-hefutoxin 1, a scorpion toxin on potassium channels","volume":"71","author":"Peigneur","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0140","doi-asserted-by":"crossref","first-page":"4302","DOI":"10.1074\/jbc.272.7.4302","article-title":"On the convergent evolution of animal toxins","volume":"272","author":"Dauplais","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0145","doi-asserted-by":"crossref","first-page":"e00594","DOI":"10.7554\/eLife.00594","article-title":"Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K+ channel","volume":"2","author":"Banerjee","year":"2013","journal-title":"Elife"},{"key":"10.1016\/j.peptides.2016.08.008_bib0150","doi-asserted-by":"crossref","first-page":"5540","DOI":"10.1093\/emboj\/18.20.5540","article-title":"Oncogenic potential of EAG K(+) channels","volume":"18","author":"Pardo","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.peptides.2016.08.008_bib0155","doi-asserted-by":"crossref","first-page":"675","DOI":"10.2174\/092986712798992011","article-title":"Approaches targeting Kv10.1 open a novel window for cancer diagnosis and therapy","volume":"19","author":"Pardo","year":"2012","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0160","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1007\/s00424-015-1784-3","article-title":"Kv10.1 K+ channel: from physiology to cancer","volume":"468","author":"Ouadid-Ahidouch","year":"2016","journal-title":"Pfl\u00fcgers Arch.: Eur. J. Physiol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0165","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1083\/jcb.201404136","article-title":"Targeting potassium channels in cancer","volume":"206","author":"Huang","year":"2014","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0170","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1006\/mcne.2000.0851","article-title":"Cloning and functional expression of rat eag2, a new member of the ether-\u00e0-go-go family of potassium channels and comparison of its distribution with that of eag1","volume":"16","author":"Ludwig","year":"2000","journal-title":"Mol. Cell. Neurosci."},{"key":"10.1016\/j.peptides.2016.08.008_bib0175","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/j.neuroscience.2008.05.019","article-title":"Eag1 potassium channel immunohistochemistry in the CNS of adult rat and selected regions of human brain","volume":"155","author":"Martin","year":"2008","journal-title":"Neuroscience"},{"key":"10.1016\/j.peptides.2016.08.008_bib0180","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0014-5793(98)00973-9","article-title":"Cloning of a human ether-a-go-go potassium channel expressed in myoblasts at the onset of fusion","volume":"434","author":"Occhiodoro","year":"1998","journal-title":"FEBS Lett."},{"key":"10.1016\/j.peptides.2016.08.008_bib0185","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1186\/1476-4598-5-41","article-title":"Overexpression of Eag1 potassium channels in clinical tumours","volume":"5","author":"Hemmerlein","year":"2006","journal-title":"Mol. Cancer"},{"key":"10.1016\/j.peptides.2016.08.008_bib0190","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1476-4598-5-42","article-title":"Ether \u00e0 go-go potassium channel expression in soft tissue sarcoma patients","volume":"5","author":"Mello de Queiroz","year":"2006","journal-title":"Mol. Cancer"},{"key":"10.1016\/j.peptides.2016.08.008_bib0195","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1007\/s12032-007-0015-y","article-title":"Aberrant expression of Eag1 potassium channels in gastric cancer patients and cell lines","volume":"24","author":"Ding","year":"2007","journal-title":"Med. Oncol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0200","doi-asserted-by":"crossref","first-page":"2039","DOI":"10.1007\/s10620-007-0116-7","article-title":"Expression and prognostic roles of Eag1 in resected esophageal squamous cell carcinomas","volume":"53","author":"Ding","year":"2008","journal-title":"Dig. Dis. Sci."},{"key":"10.1016\/j.peptides.2016.08.008_bib0205","doi-asserted-by":"crossref","first-page":"1257","DOI":"10.3748\/wjg.v13.i8.1257","article-title":"Aberrant expression of ether \u00e0 go-go potassium channel in colorectal cancer patients and cell lines","volume":"13","author":"Ding","year":"2007","journal-title":"World J. Gastroenterol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0210","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s002329900563","article-title":"Identification of Ether \u00e0 go-go and calcium-activated potassium channels in human melanoma cells","volume":"171","author":"Meyer","year":"1999","journal-title":"J. Membr. Biol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0215","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1158\/1078-0432.CCR-06-1940","article-title":"Expression of voltage-gated potassium channels in human and mouse colonic carcinoma","volume":"13","author":"Ousingsawat","year":"2007","journal-title":"Clin. Cancer Res."},{"key":"10.1016\/j.peptides.2016.08.008_bib0220","doi-asserted-by":"crossref","first-page":"7421","DOI":"10.1074\/jbc.M703758200","article-title":"Eag1 and Bestrophin 1 are up-regulated in fast-growing colonic cancer cells","volume":"283","author":"Spitzner","year":"2008","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0225","doi-asserted-by":"crossref","first-page":"15986","DOI":"10.1021\/bi0511181","article-title":"A novel conotoxin framework with a helix-loop-helix (Cs \u03b1\/\u03b1) fold","volume":"44","author":"M\u00f6ller","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.peptides.2016.08.008_bib0230","doi-asserted-by":"crossref","first-page":"3594","DOI":"10.1111\/febs.12349","article-title":"Genes encoding 4-Cys antimicrobial peptides in wheat Triticum kiharae Dorof. et Migush: multimodular structural organization, instraspecific variability, distribution and role in defence","volume":"280","author":"Utkina","year":"2013","journal-title":"FEBS J."},{"key":"10.1016\/j.peptides.2016.08.008_bib0235","doi-asserted-by":"crossref","first-page":"14331","DOI":"10.1074\/jbc.M113.530477","article-title":"Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design","volume":"289","author":"Berkut","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0240","first-page":"1","article-title":"Reference method for broth dilution antifungal susceptibility testing of yeasts: approved standard \u2212 third edition","author":"Rex","year":"2008","journal-title":"Clin. Lab. Stand. Inst."},{"key":"10.1016\/j.peptides.2016.08.008_bib0245","article-title":"Reference method for broth dilution antifungal susceptibility testing of filamentous fungi: approved standard \u2212 second edition","author":"Rex","year":"2008","journal-title":"Clin. Lab. Stand. Inst."},{"key":"10.1016\/j.peptides.2016.08.008_bib0250","doi-asserted-by":"crossref","first-page":"15301","DOI":"10.1016\/S0021-9258(19)49534-3","article-title":"Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds","volume":"267","author":"Terras","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0255","doi-asserted-by":"crossref","first-page":"47","DOI":"10.3389\/fmicb.2011.00047","article-title":"The antifungal plant defensin HsAFP1 from Heuchera sanguinea induces apoptosis in Candida albicans","volume":"2","author":"Aerts","year":"2011","journal-title":"Front. Microbiol."},{"key":"10.1016\/j.peptides.2016.08.008_bib0260","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera \u2013 a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0265","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.toxicon.2014.02.010","article-title":"Functional and structural study comparing the C-terminal amidated \u03b2-neurotoxin Ts1 with its isoform Ts1-G isolated from Tityus serrulatus venom","volume":"83","author":"Coelho","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.peptides.2016.08.008_bib0270","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.peptides.2004.01.009","article-title":"Molecular cloning and functional expression of the alpha-scorpion toxin BotIII: Pivotal role of the C-terminal region for its interaction with voltage-dependent sodium channels","volume":"25","author":"Benkhadir","year":"2004","journal-title":"Peptides"},{"key":"10.1016\/j.peptides.2016.08.008_bib0275","doi-asserted-by":"crossref","first-page":"48849","DOI":"10.1074\/jbc.M208842200","article-title":"A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity","volume":"277","author":"Dutton","year":"2002","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.peptides.2016.08.008_bib0280","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.3390\/md12052970","article-title":"Conotoxins targeting nicotinic acetylcholine receptors: an overview","volume":"12","author":"Lebbe","year":"2014","journal-title":"Mar. Drugs"},{"key":"10.1016\/j.peptides.2016.08.008_bib0285","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1006\/abbi.1998.0815","article-title":"Disulfide isomerization within the C-terminus of cobrotoxin decelerates by thiol compounds and trinitrophenylation, but accelerates by modification of carboxyl groups","volume":"358","author":"Chang","year":"1998","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.peptides.2016.08.008_bib0290","doi-asserted-by":"crossref","first-page":"652","DOI":"10.1006\/bbrc.1999.1418","article-title":"Expression and mutagenesis studies of cobrotoxin from Taiwan cobra","volume":"263","author":"Chang","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."}],"container-title":["Peptides"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S019697811630167X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S019697811630167X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,6,19]],"date-time":"2022-06-19T21:06:18Z","timestamp":1655672778000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S019697811630167X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,12]]},"references-count":58,"alternative-id":["S019697811630167X"],"URL":"https:\/\/doi.org\/10.1016\/j.peptides.2016.08.008","relation":{},"ISSN":["0196-9781"],"issn-type":[{"value":"0196-9781","type":"print"}],"subject":[],"published":{"date-parts":[[2017,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Expanding the pharmacological profile of \u03ba-hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel Kv10.1","name":"articletitle","label":"Article Title"},{"value":"Peptides","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.peptides.2016.08.008","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2016 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}