{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T15:02:10Z","timestamp":1790694130764,"version":"4.1.0"},"reference-count":127,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2024,3,22]],"date-time":"2024-03-22T00:00:00Z","timestamp":1711065600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo (FAPESP)","doi-asserted-by":"publisher","award":["2017\/18398-1"],"award-info":[{"award-number":["2017\/18398-1"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo (FAPESP)","doi-asserted-by":"publisher","award":["313273\/2018-9"],"award-info":[{"award-number":["313273\/2018-9"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo (FAPESP)","doi-asserted-by":"publisher","award":["312901\/2022-4"],"award-info":[{"award-number":["312901\/2022-4"]}],"id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Funda\u00e7\u00e3o Butantan and Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico (CNPq)","doi-asserted-by":"publisher","award":["2017\/18398-1"],"award-info":[{"award-number":["2017\/18398-1"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Funda\u00e7\u00e3o Butantan and Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico (CNPq)","doi-asserted-by":"publisher","award":["313273\/2018-9"],"award-info":[{"award-number":["313273\/2018-9"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003593","name":"Funda\u00e7\u00e3o Butantan and Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico (CNPq)","doi-asserted-by":"publisher","award":["312901\/2022-4"],"award-info":[{"award-number":["312901\/2022-4"]}],"id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Coralsnakes (Micrurus spp.) are the only elapids found throughout the Americas. They are recognized for their highly neurotoxic venom, which is comprised of a wide variety of toxins, including the stable, low-mass toxins known as three-finger toxins (3FTx). Due to difficulties in venom extraction and availability, research on coralsnake venoms is still very limited when compared to that of other Elapidae snakes like cobras, kraits, and mambas. In this study, two previously described 3FTx from the venom of M. corallinus, NXH1 (3SOC1_MICCO), and NXH8 (3NO48_MICCO) were characterized. Using in silico, in vitro, and ex vivo experiments, the biological activities of these toxins were predicted and evaluated. The results showed that only NXH8 was capable of binding to skeletal muscle cells and modulating the activity of nAChRs in nerve\u2013diaphragm preparations. These effects were antagonized by anti-rNXH8 or antielapidic sera. Sequence analysis revealed that the NXH1 toxin possesses eight cysteine residues and four disulfide bonds, while the NXH8 toxin has a primary structure similar to that of non-conventional 3FTx, with an additional disulfide bond on the first loop. These findings add more information related to the structural diversity present within the 3FTx class, while expanding our understanding of the mechanisms of the toxicity of this coralsnake venom and opening new perspectives for developing more effective therapeutic interventions.<\/jats:p>","DOI":"10.3390\/toxins16040164","type":"journal-article","created":{"date-parts":[[2024,3,22]],"date-time":"2024-03-22T05:10:53Z","timestamp":1711084253000},"page":"164","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["The Cloning and Characterization of a Three-Finger Toxin Homolog (NXH8) from the Coralsnake Micrurus corallinus That Interacts with Skeletal Muscle Nicotinic Acetylcholine Receptors"],"prefix":"10.3390","volume":"16","author":[{"given":"Henrique","family":"Roman-Ramos","sequence":"first","affiliation":[{"name":"Laborat\u00f3rio de Biotecnologia, Programa de P\u00f3s-Gradua\u00e7\u00e3o em Medicina, Universidade Nove de Julho (UNINOVE), S\u00e3o Paulo 01504-001, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0289-9809","authenticated-orcid":false,"given":"\u00c1lvaro R. B.","family":"Prieto-da-Silva","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Gen\u00e9tica, Instituto Butantan, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Humberto","family":"Dell\u00ea","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biotecnologia, Programa de P\u00f3s-Gradua\u00e7\u00e3o em Medicina, Universidade Nove de Julho (UNINOVE), S\u00e3o Paulo 01504-001, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0759-5863","authenticated-orcid":false,"given":"Rafael S.","family":"Floriano","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Toxinologia e Estudos Cardiovasculares, Universidade do Oeste Paulista (UNOESTE), Presidente Prudente 19067-175, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lourdes","family":"Dias","sequence":"additional","affiliation":[{"name":"Departamento de Farmacologia, Faculdade de Ci\u00eancias M\u00e9dicas, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-887, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen","family":"Hyslop","sequence":"additional","affiliation":[{"name":"Departamento de Farmacologia, Faculdade de Ci\u00eancias M\u00e9dicas, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-887, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Raphael","family":"Schezaro-Ramos","sequence":"additional","affiliation":[{"name":"Departamento de Farmacologia, Faculdade de Ci\u00eancias M\u00e9dicas, Universidade Estadual de Campinas (UNICAMP), Campinas 13083-887, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0774-1691","authenticated-orcid":false,"given":"Denis","family":"Servent","sequence":"additional","affiliation":[{"name":"Service d\u2019Ing\u00e9nierie Mol\u00e9culaire pour la Sant\u00e9 (SIMoS), D\u00e9partement M\u00e9dicaments et Technologies pour la Sant\u00e9, Universit\u00e9 Paris Saclay, Commissariat \u00e0 l\u2019\u00e9nergie Atomique et aux \u00c9nergies Alternatives (CEA), F-91191 Gif sur Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gilles","family":"Mourier","sequence":"additional","affiliation":[{"name":"Service d\u2019Ing\u00e9nierie Mol\u00e9culaire pour la Sant\u00e9 (SIMoS), D\u00e9partement M\u00e9dicaments et Technologies pour la Sant\u00e9, Universit\u00e9 Paris Saclay, Commissariat \u00e0 l\u2019\u00e9nergie Atomique et aux \u00c9nergies Alternatives (CEA), F-91191 Gif sur Yvette, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"J\u00e9ssica Lopes","family":"de Oliveira","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biotecnologia, Programa de P\u00f3s-Gradua\u00e7\u00e3o em Medicina, Universidade Nove de Julho (UNINOVE), S\u00e3o Paulo 01504-001, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Douglas Edgard","family":"Lemes","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Biotecnologia, Programa de P\u00f3s-Gradua\u00e7\u00e3o em Medicina, Universidade Nove de Julho (UNINOVE), S\u00e3o Paulo 01504-001, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1861-5153","authenticated-orcid":false,"given":"Let\u00edcia V.","family":"Costa-Lotufo","sequence":"additional","affiliation":[{"name":"Departamento de Farmacologia, Instituto de Ci\u00eancias Biom\u00e9dicas, Universidade de S\u00e3o Paulo (USP), S\u00e3o Paulo 05508-000, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jane S.","family":"Oliveira","sequence":"additional","affiliation":[{"name":"Centro de Biotecnologia, Instituto Butantan, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Milene Cristina","family":"Menezes","sequence":"additional","affiliation":[{"name":"Centro Bioindustrial, Instituto Butantan, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4606-6120","authenticated-orcid":false,"given":"Regina P.","family":"Markus","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Cronofarmacologia, Instituto de Bioci\u00eancias, Universidade de S\u00e3o Paulo (USP), S\u00e3o Paulo 05508-090, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3652-241X","authenticated-orcid":false,"given":"Paulo Lee","family":"Ho","sequence":"additional","affiliation":[{"name":"Centro Bioindustrial, Instituto Butantan, S\u00e3o Paulo 05503-900, SP, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,3,22]]},"reference":[{"key":"ref_1","unstructured":"World Health Organization (2024, March 03). [FACT SHEET] Snakebite Envenoming. Available online: https:\/\/web.archive.org\/web\/20240303212634\/https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/snakebite-envenoming."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","article-title":"Snakebite envenoming","volume":"3","author":"Gutierrez","year":"2017","journal-title":"Nat. Rev. Dis. Primers"},{"key":"ref_3","unstructured":"Roze, J.A. (1996). Coral Snakes of the Americas: Biology, Identification and Venoms, Krieger."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"142","DOI":"10.15448\/1980-6108.2014.2.16119","article-title":"A study on venom yield of Brazilian coralsnakes and its use in the evaluation of antielapidic serum","volume":"2","author":"Carvalho","year":"2014","journal-title":"Sci. Medica"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"222","DOI":"10.3109\/15563650.2015.1135337","article-title":"Coral snake bites (Micrurus spp.) in Brazil: A review of literature reports","volume":"54","author":"Bucaretchi","year":"2016","journal-title":"Clin. Toxicol."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1590\/S0036-46652006000300005","article-title":"Bites by coral snakes (Micrurus spp.) in Campinas, State of Sao Paulo, Southeastern Brazil","volume":"48","author":"Bucaretchi","year":"2006","journal-title":"Rev. Inst. Med. Trop. Sao Paulo"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1193","DOI":"10.1016\/S0041-0101(97)00031-7","article-title":"Toxins isolated from the venom of the Brazilian coral snake (Micrurus frontalis frontalis) include hemorrhagic type phospholipases A2 and postsynaptic neurotoxins","volume":"35","author":"Francis","year":"1997","journal-title":"Toxicon"},{"key":"ref_8","unstructured":"Hessel, M.M., and McAninch, S.A. (2022). Coral Snake Toxicity, StatPearls."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1590\/S0036-46651987000300001","article-title":"Coral snake venoms: Mode of action and pathophysiology of experimental envenomation (1)","volume":"29","year":"1987","journal-title":"Rev. Inst. Med. Trop. Sao Paulo"},{"key":"ref_10","first-page":"13","article-title":"A\u00e7\u00f5es pr\u00e9-juncionais e p\u00f3s-juncionais da pe\u00e7onha da cobra coral Micrurus corallinus na jun\u00e7\u00e3o neuromuscular","volume":"47","author":"Fontana","year":"1983","journal-title":"Mem. Inst. Butantan"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.cbpb.2004.11.012","article-title":"Biological and enzymatic activities of Micrurus sp. (Coral) snake venoms","volume":"140","author":"Cecchini","year":"2005","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.toxicon.2014.07.010","article-title":"Intravascular hemolysis induced by the venom of the Eastern coral snake, Micrurus fulvius, in a mouse model: Identification of directly hemolytic phospholipases A2","volume":"90","author":"Lomonte","year":"2014","journal-title":"Toxicon"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1016\/0041-0101(92)90446-C","article-title":"Experimental myonecrosis induced by the venoms of South American Micrurus (coral snakes)","volume":"30","author":"Gutierrez","year":"1992","journal-title":"Toxicon"},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"356","DOI":"10.1016\/j.toxicon.2011.11.009","article-title":"Myotoxicity and nephrotoxicity by Micrurus venoms in experimental envenomation","volume":"59","author":"Lago","year":"2012","journal-title":"Toxicon"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1007\/s12012-021-09640-7","article-title":"Cardiotoxic Effects of Micrurus surinamensis (Cuvier, 1817) Snake Venom","volume":"21","author":"Reis","year":"2021","journal-title":"Cardiovasc. Toxicol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/s12012-021-09713-7","article-title":"In Vivo Cardiotoxic Potential of Micrurus frontalis Venom","volume":"22","author":"Lempek","year":"2022","journal-title":"Cardiovasc. Toxicol."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.toxicon.2009.01.032","article-title":"Death following coral snake bite in the United States\u2014First documented case (with ELISA confirmation of envenomation) in over 40 years","volume":"53","author":"Norris","year":"2009","journal-title":"Toxicon"},{"key":"ref_18","unstructured":"WHO Expert Committee on the Selection of Essential Drugs, and World Health Organization (1977, January 17\u201321). The Selection of Essential Drugs: Report of a WHO Expert Committee. Proceedings of the WHO Expert Committee on the Selection of Essential Drugs, Geneva, Switzerland."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1016\/j.toxicon.2012.04.253","article-title":"Coral Snake Antivenin\u2019s Deadly Deadline","volume":"60","author":"Mannel","year":"2012","journal-title":"Toxicon"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.toxicon.2012.04.251","article-title":"Critical Shortage of Coral Snake Antivenom is Impacting Patient Care","volume":"60","author":"Bernstein","year":"2012","journal-title":"Toxicon"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.1016\/S0041-0101(98)00119-6","article-title":"A study on the venom yield of venomous snake species from Argentina","volume":"36","author":"Dolab","year":"1998","journal-title":"Toxicon"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1590\/S0073-47212002000400013","article-title":"Varia\u00e7\u00e3o de peso e sobrevida de Micrurus corallinus sob diferentes condi\u00e7\u00f5es de alimenta\u00e7\u00e3o em biot\u00e9rio (Serpentes, Elapidae)","volume":"92","author":"Serapicos","year":"2002","journal-title":"Iheringia S\u00e9rie Zool."},{"key":"ref_23","unstructured":"Silva, N.J., Porras, L.W., Aird, S.D., and Prudente, A.L.C. (2021). Advances in Coralsnake Biology: With an Emphasis on South America, Eagle Mountain Publishing LC."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Leao, L.I., Ho, P.L., and Junqueira-de-Azevedo Ide, L. (2009). Transcriptomic basis for an antiserum against Micrurus corallinus (coral snake) venom. BMC Genom., 10.","DOI":"10.1186\/1471-2164-10-112"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1016\/j.jprot.2011.04.003","article-title":"Snake venomics and venom gland transcriptomic analysis of Brazilian coral snakes, Micrurus altirostris and M. corallinus","volume":"74","author":"Silva","year":"2011","journal-title":"J. Proteom."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1919","DOI":"10.1002\/pmic.200700668","article-title":"Proteomic analysis of the venom from the fish eating coral snake Micrurus surinamensis: Novel toxins, their function and phylogeny","volume":"8","author":"Batista","year":"2008","journal-title":"Proteomics"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1810","DOI":"10.1016\/j.jprot.2011.07.011","article-title":"Venomic analysis and evaluation of antivenom cross-reactivity of South American Micrurus species","volume":"74","author":"Ciscotto","year":"2011","journal-title":"J. Proteom."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/0305-0491(91)90043-D","article-title":"Comparative enzymatic composition of Brazilian coral snake (Micrurus) venoms","volume":"99","author":"Aird","year":"1991","journal-title":"Comp. Biochem. Physiol. B"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.toxicon.2016.09.008","article-title":"Venoms of Micrurus coral snakes: Evolutionary trends in compositional patterns emerging from proteomic analyses","volume":"122","author":"Lomonte","year":"2016","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Aird, S.D., da Silva, N.J., Qiu, L., Villar-Briones, A., Saddi, V.A., Pires de Campos Telles, M., Grau, M.L., and Mikheyev, A.S. (2017). Coralsnake Venomics: Analyses of Venom Gland Transcriptomes and Proteomes of Six Brazilian Taxa. Toxins, 9.","DOI":"10.3390\/toxins9060187"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.jprot.2019.03.014","article-title":"New insights into the phylogeographic distribution of the 3FTx\/PLA(2) venom dichotomy across genus Micrurus in South America","volume":"200","author":"Sanz","year":"2019","journal-title":"J. Proteom."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1017\/S0269727000013075","article-title":"Structural Basis for Functional Diversity of Animal Toxins","volume":"99","author":"Menez","year":"1992","journal-title":"Proc. R. Soc. Edinb. Sect. B Biol. Sci."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"17","DOI":"10.4331\/wjbc.v10.i1.17","article-title":"Last decade update for three-finger toxins: Newly emerging structures and biological activities","volume":"10","author":"Utkin","year":"2019","journal-title":"World J. Biol. Chem."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"855","DOI":"10.1016\/j.toxicon.2010.07.010","article-title":"Structure, function and evolution of three-finger toxins: Mini proteins with multiple targets","volume":"56","author":"Kini","year":"2010","journal-title":"Toxicon"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1046\/j.1432-1327.1999.00623.x","article-title":"Snake venom alpha-neurotoxins and other \u2018three-finger\u2019 proteins","volume":"264","author":"Tsetlin","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1007\/s00239-003-2461-2","article-title":"Molecular evolution and phylogeny of elapid snake venom three-finger toxins","volume":"57","author":"Fry","year":"2003","journal-title":"J. Mol. Evol."},{"key":"ref_37","doi-asserted-by":"crossref","unstructured":"Nirthanan, S. (2020). Snake three-finger alpha-neurotoxins and nicotinic acetylcholine receptors: Molecules, mechanisms and medicine. Biochem. Pharmacol., 181.","DOI":"10.1016\/j.bcp.2020.114168"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"11233","DOI":"10.1016\/S0021-9258(19)78115-0","article-title":"Site of fasciculin interaction with acetylcholinesterase","volume":"269","author":"Radic","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/0163-7258(87)90002-7","article-title":"Current view on the structure-function relationship of postsynaptic neurotoxins from snake venoms","volume":"34","author":"Endo","year":"1987","journal-title":"Pharmacol. Ther."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.toxicon.2013.01.019","article-title":"Alpha neurotoxins","volume":"66","author":"Barber","year":"2013","journal-title":"Toxicon"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"570","DOI":"10.2174\/138920312803582960","article-title":"Structure and dynamics of cardiotoxins","volume":"13","author":"Konshina","year":"2012","journal-title":"Curr. Protein Pept. Sci."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"638","DOI":"10.2174\/1568026615666150217113011","article-title":"Antiproliferative activity of cobra venom cytotoxins","volume":"15","author":"Dubovskii","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0163-7258(88)90111-8","article-title":"Structure and pharmacology of elapid cytotoxins","volume":"36","author":"Dufton","year":"1988","journal-title":"Pharmacol. Ther."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1016\/S0024-3205(97)00049-0","article-title":"Muscarinic receptor subtype selective toxins","volume":"60","author":"Adem","year":"1997","journal-title":"Life Sci."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/j.toxicon.2011.08.004","article-title":"Muscarinic toxins","volume":"58","author":"Servent","year":"2011","journal-title":"Toxicon"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"4766","DOI":"10.1021\/bi00135a004","article-title":"Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins","volume":"31","author":"McDowell","year":"1992","journal-title":"Biochemistry"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Yang, D.C., Deuis, J.R., Dashevsky, D., Dobson, J., Jackson, T.N., Brust, A., Xie, B., Koludarov, I., Debono, J., and Hendrikx, I. (2016). The Snake with the Scorpion\u2019s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus). Toxins, 8.","DOI":"10.3390\/toxins8100303"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"23904","DOI":"10.1038\/srep23904","article-title":"Discovery and characterisation of a novel toxin from Dendroaspis angusticeps, named Tx7335, that activates the potassium channel KcsA","volume":"6","author":"Jin","year":"2016","journal-title":"Sci. Rep."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1002\/anie.201308898","article-title":"Chemical synthesis, 3D structure, and ASIC binding site of the toxin mambalgin-2","volume":"53","author":"Schroeder","year":"2014","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1073\/pnas.88.6.2437","article-title":"Calciseptine, a peptide isolated from black mamba venom, is a specific blocker of the L-type calcium channel","volume":"88","author":"Schweitz","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"24279","DOI":"10.1074\/jbc.272.39.24279","article-title":"Only snake curaremimetic toxins with a fifth disulfide bond have high affinity for the neuronal alpha7 nicotinic receptor","volume":"272","author":"Servent","year":"1997","journal-title":"J. Biol. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1243","DOI":"10.1016\/S0041-0101(96)00110-9","article-title":"Binding of native kappa-neurotoxins and site-directed mutants to nicotinic acetylcholine receptors","volume":"34","author":"Chiappinelli","year":"1996","journal-title":"Toxicon"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"3353","DOI":"10.1021\/bi9629687","article-title":"Critical interactions at the dimer interface of kappa-bungarotoxin, a neuronal nicotinic acetylcholine receptor antagonist","volume":"36","author":"Grant","year":"1997","journal-title":"Biochemistry"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"310","DOI":"10.1016\/0005-2795(75)90186-5","article-title":"Snake venom toxins. The primary structure of protein S4C11. A neurotoxin homologue from the venom of forest cobra (Naja melanoleuca)","volume":"400","author":"Carlsson","year":"1975","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1515\/bchm2.1980.361.1.425","article-title":"Snake venoms. The amino acid sequences of two Melanoleuca-type toxins","volume":"361","author":"Joubert","year":"1980","journal-title":"Hoppe Seylers Z. Physiol. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/S0167-4781(98)00218-8","article-title":"cDNA sequence analysis and expression of four long neurotoxin homologues from Naja naja atra","volume":"1443","author":"Qian","year":"1998","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"15810","DOI":"10.1074\/jbc.M100788200","article-title":"\u201cWeak toxin\u201d from Naja kaouthia is a nontoxic antagonist of alpha 7 and muscle-type nicotinic acetylcholine receptors","volume":"276","author":"Utkin","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_58","first-page":"1211","article-title":"Characterization and cloning of long neurotoxin homolog from Naja naja atra","volume":"46","author":"Lin","year":"1998","journal-title":"Biochem. Mol. Biol. Int."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/0014-5793(91)80764-T","article-title":"Extensive multiplicity of the miscellaneous type of neurotoxins from the venom of the cobra Naja naja naja and structural characterization of major components","volume":"284","author":"Shafqat","year":"1991","journal-title":"FEBS Lett."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"832","DOI":"10.1038\/sj.bjp.0705299","article-title":"Neuromuscular effects of candoxin, a novel toxin from the venom of the Malayan krait (Bungarus candidus)","volume":"139","author":"Nirthanan","year":"2003","journal-title":"Br. J. Pharmacol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"17811","DOI":"10.1074\/jbc.M111152200","article-title":"Candoxin, a novel toxin from Bungarus candidus, is a reversible antagonist of muscle (alphabetagammadelta) but a poorly reversible antagonist of neuronal alpha 7 nicotinic acetylcholine receptors","volume":"277","author":"Nirthanan","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1002\/mrc.872","article-title":"Sequence-specific C-13 NMR assignments in a neurotoxin (candoxin) from Bungarus candidus","volume":"39","author":"Parvathy","year":"2001","journal-title":"Magn. Reson. Chem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1016\/S0041-0101(98)00199-8","article-title":"Primary structure of gamma-bungarotoxin, a new postsynaptic neurotoxin from venom of Bungarus multicinctus","volume":"37","author":"Aird","year":"1999","journal-title":"Toxicon"},{"key":"ref_64","first-page":"347","article-title":"cDNA sequence analysis of a novel neurotoxin homolog from Taiwan banded krait","volume":"43","author":"Chang","year":"1997","journal-title":"Biochem. Mol. Biol. Int."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1045","DOI":"10.1093\/nar\/18.4.1045","article-title":"A cDNA sequence encoding a neurotoxin-homolog from Bungarus multicinctus","volume":"18","author":"Danse","year":"1990","journal-title":"Nucleic Acids Res."},{"key":"ref_66","first-page":"241","article-title":"Isolation of Neurotoxins from the Venom of Bungarus Multicinctus and Their Modes of Neuromuscular Blocking Action","volume":"144","author":"Chang","year":"1963","journal-title":"Arch. Int. Pharmacodyn. Ther."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.lfs.2011.09.024","article-title":"Characterization of a new muscarinic toxin from the venom of the Brazilian coral snake Micrurus lemniscatus in rat hippocampus","volume":"89","author":"Pimenta","year":"2011","journal-title":"Life Sci."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1822","DOI":"10.1111\/bph.14954","article-title":"Fulditoxin, representing a new class of dimeric snake toxins, defines novel pharmacology at nicotinic ACh receptors","volume":"177","author":"Foo","year":"2020","journal-title":"Br. J. Pharmacol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/j.toxicon.2012.05.023","article-title":"Mipartoxin-I, a novel three-finger toxin, is the major neurotoxic component in the venom of the redtail coral snake Micrurus mipartitus (Elapidae)","volume":"60","author":"Floriano","year":"2012","journal-title":"Toxicon"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/0014-5793(95)01543-4","article-title":"Characterization of multiple nicotinic acetylcholine receptor-binding proteins and phospholipases A2 from the venom of the coral snake Micrurus nigrocinctus","volume":"380","author":"Stiles","year":"1996","journal-title":"FEBS Lett."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Kleiz-Ferreira, J.M., Bernaerts, H., Pinheiro-Junior, E.L., Peigneur, S., Zingali, R.B., and Tytgat, J. (2022). Pharmacological Screening of Venoms from Five Brazilian Micrurus Species on Different Ion Channels. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23147714"},{"key":"ref_72","doi-asserted-by":"crossref","unstructured":"Kleiz-Ferreira, J.M., Cirauqui, N., Trajano, E.A., Almeida, M.S., and Zingali, R.B. (2021). Three-Finger Toxins from Brazilian Coral Snakes: From Molecular Framework to Insights in Biological Function. Toxins, 13.","DOI":"10.3390\/toxins13050328"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.toxicon.2019.09.017","article-title":"Novel three-finger toxins from Micrurus dumerilii and Micrurus mipartitus coral snake venoms: Phylogenetic relationships and characterization of Clarkitoxin-I-Mdum","volume":"170","author":"Torres","year":"2019","journal-title":"Toxicon"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"327","DOI":"10.3109\/15569549509019467","article-title":"Reverse Biology Applied to Micrurus-Corallinus, a South-American Coral Snake","volume":"14","author":"Ho","year":"1995","journal-title":"J. Toxicol.-Toxin Rev."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1111\/j.1432-1033.1997.00144.x","article-title":"Cloning of an unusual natriuretic peptide from the South American coral snake Micrurus corallinus","volume":"250","author":"Ho","year":"1997","journal-title":"Eur. J. Biochem."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1006\/bbrc.1999.2033","article-title":"Cloning and characterization of an alpha-neurotoxin-type protein specific for the coral snake Micrurus corallinus","volume":"267","author":"Soares","year":"2000","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_77","doi-asserted-by":"crossref","unstructured":"Ramos, H.R., Junqueira-de-Azevedo Ide, L., Novo, J.B., Castro, K., Duarte, C.G., Machado-de-Avila, R.A., Chavez-Olortegui, C., and Ho, P.L. (2016). A Heterologous Multiepitope DNA Prime\/Recombinant Protein Boost Immunisation Strategy for the Development of an Antiserum against Micrurus corallinus (Coral Snake) Venom. PLoS Negl. Trop. Dis., 10.","DOI":"10.1371\/journal.pntd.0004484"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/S0021-9258(18)54020-5","article-title":"Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis","volume":"268","author":"Pillet","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_79","first-page":"9362","article-title":"Genetic engineering of snake toxins. The functional site of Erabutoxin a, as delineated by site-directed mutagenesis, includes variant residues","volume":"270","author":"Tremeau","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"10958","DOI":"10.1074\/jbc.273.18.10958","article-title":"Identification of pairwise interactions in the alpha-neurotoxin-nicotinic acetylcholine receptor complex through double mutant cycles","volume":"273","author":"Ackermann","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"9581","DOI":"10.1074\/jbc.274.14.9581","article-title":"Subunit interface selectivity of the alpha-neurotoxins for the nicotinic acetylcholine receptor","volume":"274","author":"Osaka","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"34851","DOI":"10.1074\/jbc.274.49.34851","article-title":"Variability among the sites by which curaremimetic toxins bind to torpedo acetylcholine receptor, as revealed by identification of the functional residues of alpha-cobratoxin","volume":"274","author":"Antil","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"29594","DOI":"10.1074\/jbc.M909746199","article-title":"Molecular determinants by which a long chain toxin from snake venom interacts with the neuronal alpha 7-nicotinic acetylcholine receptor","volume":"275","author":"Gaillard","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"12406","DOI":"10.1074\/jbc.M110320200","article-title":"NMR structural analysis of alpha-bungarotoxin and its complex with the principal alpha-neurotoxin-binding sequence on the alpha 7 subunit of a neuronal nicotinic acetylcholine receptor","volume":"277","author":"Moise","year":"2002","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"22930","DOI":"10.1074\/jbc.M102300200","article-title":"The solution structure of the complex formed between alpha-bungarotoxin and an 18-mer cognate peptide derived from the alpha 1 subunit of the nicotinic acetylcholine receptor from Torpedo californica","volume":"276","author":"Zeng","year":"2001","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"20","DOI":"10.2144\/98251bm02","article-title":"Nickel-induced oligomerization of proteins containing 10-histidine tags","volume":"25","author":"Sprules","year":"1998","journal-title":"Biotechniques"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/S0041-0101(00)00233-6","article-title":"Cross reactivity of different specific Micrurus antivenom sera with homologous and heterologous snake venoms","volume":"39","author":"Yamagushi","year":"2001","journal-title":"Toxicon"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.toxicon.2013.03.006","article-title":"Pharmacological study of a new Asp49 phospholipase A(2) (Bbil-TX) isolated from Bothriopsis bilineata smargadina (forest viper) venom in vertebrate neuromuscular preparations","volume":"69","author":"Floriano","year":"2013","journal-title":"Toxicon"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.toxlet.2015.11.020","article-title":"Neutralization of the neuromuscular inhibition of venom and taipoxin from the taipan (Oxyuranus scutellatus) by F(ab\u2019)2 and whole IgG antivenoms","volume":"241","author":"Herrera","year":"2016","journal-title":"Toxicol. Lett."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"2065","DOI":"10.1007\/s00204-019-02476-9","article-title":"Neurotoxicity of Micrurus lemniscatus lemniscatus (South American coralsnake) venom in vertebrate neuromuscular preparations in vitro and neutralization by antivenom","volume":"93","author":"Floriano","year":"2019","journal-title":"Arch. Toxicol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1080\/15563650.2016.1222615","article-title":"Cross neutralization of coral snake venoms by commercial Australian snake antivenoms","volume":"55","author":"Ramos","year":"2017","journal-title":"Clin. Toxicol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1016\/S0041-0101(00)00223-3","article-title":"First tryptophan-containing weak neurotoxin from cobra venom","volume":"39","author":"Utkin","year":"2001","journal-title":"Toxicon"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.neuropharm.2015.01.001","article-title":"Snake neurotoxin alpha-bungarotoxin is an antagonist at native GABA(A) receptors","volume":"93","author":"Hannan","year":"2015","journal-title":"Neuropharmacology"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"22747","DOI":"10.1074\/jbc.M115.648824","article-title":"Neurotoxins from snake venoms and alpha-conotoxin ImI inhibit functionally active ionotropic gamma-aminobutyric acid (GABA) receptors","volume":"290","author":"Kudryavtsev","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"E891","DOI":"10.1073\/pnas.1415488112","article-title":"MmTX1 and MmTX2 from coral snake venom potently modulate GABAA receptor activity","volume":"112","author":"Rosso","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1756-6606-4-2","article-title":"Directed evolution of a three-finger neurotoxin by using cDNA display yields antagonists as well as agonists of interleukin-6 receptor signaling","volume":"4","author":"Naimuddin","year":"2011","journal-title":"Mol. Brain"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"2623","DOI":"10.1021\/jm401904q","article-title":"Design of a truncated cardiotoxin-I analogue with potent insulinotropic activity","volume":"57","author":"Nguyen","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1805","DOI":"10.1002\/cbic.201200081","article-title":"Cardiotoxin-I: An unexpectedly potent insulinotropic agent","volume":"13","author":"Nguyen","year":"2012","journal-title":"Chembiochem"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/s40409-018-0140-4","article-title":"Actiflagelin, a new sperm activator isolated from Walterinnesia aegyptia venom using phenotypic screening","volume":"24","author":"Jaquillard","year":"2018","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_100","doi-asserted-by":"crossref","unstructured":"Kuhn, P., Deacon, A.M., Comsa, D.S., Rajaseger, G., Kini, R.M., Uson, I.I., and Kolatkar, P.R. (2000). The atomic resolution structure of bucandin, a novel toxin isolated from the malayan krait, determined by direct methods. erratum. Acta Crystallogr. D Biol. Crystallogr., 56.","DOI":"10.1107\/S090744490001739X"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1042\/bj3600539","article-title":"NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus)","volume":"360","author":"Torres","year":"2001","journal-title":"Biochem. J."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/S0167-4838(00)00082-0","article-title":"Structure-function studies on Taiwan cobra long neurotoxin homolog","volume":"1480","author":"Chang","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Nirthanan, S. (2002). Biochemical and Pharmacological Studies on Candoxin, a Novel Toxin from the Venom of the Malayan Krait Bungarus candidus, National University of Singapore.","DOI":"10.1038\/sj.bjp.0705299"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.compbiolchem.2007.02.011","article-title":"Computer modeling of binding of diverse weak toxins to nicotinic acetylcholine receptors","volume":"31","author":"Mordvitsev","year":"2007","journal-title":"Comput. Biol. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/S0041-0101(02)00388-4","article-title":"Non-conventional toxins from Elapid venoms","volume":"41","author":"Nirthanan","year":"2003","journal-title":"Toxicon"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1023\/A:1019760401692","article-title":"Characterization and gene organization of Taiwan banded krait (Bungarus multicinctus) gamma-bungarotoxin","volume":"21","author":"Chang","year":"2002","journal-title":"J. Protein Chem."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1111\/j.1432-1033.1978.tb12612.x","article-title":"Naja haje haje (Egyptian cobra) venom. Some properties and the complete primary structure of three toxins (CM-2, CM-11 and CM-12)","volume":"90","author":"Joubert","year":"1978","journal-title":"Eur. J. Biochem."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"4247","DOI":"10.1046\/j.1432-1033.2002.03113.x","article-title":"A synthetic weak neurotoxin binds with low affinity to Torpedo and chicken alpha7 nicotinic acetylcholine receptors","volume":"269","author":"Poh","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.toxicon.2004.09.014","article-title":"Weak neurotoxin from Naja kaouthia cobra venom affects haemodynamic regulation by acting on acetylcholine receptors","volume":"45","author":"Ogay","year":"2005","journal-title":"Toxicon"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"16458","DOI":"10.1016\/S0021-9258(19)85442-X","article-title":"Xenoxins, a family of peptides from dorsal gland secretion of Xenopus laevis related to snake venom cytotoxins and neurotoxins","volume":"268","author":"Kolbe","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"20046","DOI":"10.1074\/jbc.273.32.20046","article-title":"Isolation of a member of the neurotoxin\/cytotoxin peptide family from Xenopus laevis skin which activates dihydropyridine-sensitive Ca2+ channels in mammalian epithelial cells","volume":"273","author":"Macleod","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"4471","DOI":"10.1021\/bi00181a006","article-title":"Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins","volume":"33","author":"Kieffer","year":"1994","journal-title":"Biochemistry"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1038\/icb.1995.45","article-title":"Tissue expression, structure and function of the murine Ly-6 family of molecules","volume":"73","author":"Gumley","year":"1995","journal-title":"Immunol. Cell Biol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/0014-5793(94)00674-1","article-title":"Structure-function relationships in the receptor for urokinase-type plasminogen activator. Comparison to other members of the Ly-6 family and snake venom alpha-neurotoxins","volume":"349","author":"Ploug","year":"1994","journal-title":"FEBS Lett."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1093\/genetics\/157.1.211","article-title":"The Caenorhabditis elegans odr-2 gene encodes a novel Ly-6-related protein required for olfaction","volume":"157","author":"Chou","year":"2001","journal-title":"Genetics"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0896-6273(00)80757-6","article-title":"lynx1, an endogenous toxin-like modulator of nicotinic acetylcholine receptors in the mammalian CNS","volume":"23","author":"Miwa","year":"1999","journal-title":"Neuron"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1111\/jnc.13975","article-title":"The three-finger toxin fold: A multifunctional structural scaffold able to modulate cholinergic functions","volume":"142","author":"Kessler","year":"2017","journal-title":"J. Neurochem."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/S0014-2999(00)00095-9","article-title":"Molecular characterization of the specificity of interactions of various neurotoxins on two distinct nicotinic acetylcholine receptors","volume":"393","author":"Servent","year":"2000","journal-title":"Eur. J. Pharmacol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"4543","DOI":"10.1038\/s41467-022-32174-7","article-title":"The molecular mechanism of snake short-chain alpha-neurotoxin binding to muscle-type nicotinic acetylcholine receptors","volume":"13","author":"Nys","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_120","unstructured":"Tu, A.T. (1991). Handbook of Natural Toxins: Reptile Venoms and Toxins, Marcel Dekker Inc."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"5463","DOI":"10.1073\/pnas.74.12.5463","article-title":"DNA sequencing with chain-terminating inhibitors","volume":"74","author":"Sanger","year":"1977","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_122","unstructured":"Green, M.R., Sambrook, J., and Sambrook, J. (2012). Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press. [4th ed.]."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"3389","DOI":"10.1093\/nar\/25.17.3389","article-title":"Gapped BLAST and PSI-BLAST: A new generation of protein database search programs","volume":"25","author":"Altschul","year":"1997","journal-title":"Nucleic Acids Res."},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1002\/prot.340090304","article-title":"A workbench for multiple alignment construction and analysis","volume":"9","author":"Schuler","year":"1991","journal-title":"Proteins"},{"key":"ref_125","first-page":"164","article-title":"PHYLIP-Phylogeny Inference Package (Version 3.2)","volume":"5","author":"Felsenstein","year":"1989","journal-title":"Cladistics"},{"key":"ref_126","unstructured":"Harlow, E., and Lane, D. (1988). Antibodies: A Laboratory Manual, Cold Spring Harbor Laboratory."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.ejphar.2005.09.056","article-title":"Melatonin modulates rat myotube-acetylcholine receptors by inhibiting calmodulin","volume":"525","author":"Monteiro","year":"2005","journal-title":"Eur. J. Pharmacol."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/4\/164\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T14:17:50Z","timestamp":1760105870000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/16\/4\/164"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,3,22]]},"references-count":127,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2024,4]]}},"alternative-id":["toxins16040164"],"URL":"https:\/\/doi.org\/10.3390\/toxins16040164","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,3,22]]}}}