{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,17]],"date-time":"2026-08-17T22:07:48Z","timestamp":1787004468010,"version":"build-2736575974"},"reference-count":31,"publisher":"Portland Press Ltd.","issue":"10","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2019,5,31]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>Nicotinic acetylcholine receptors (nAChRs) are pentameric ligand-gated ion channels that play crucial roles in neurotransmission and regulate complex processes in brain functions, including anxiety, learning and memory, food intake, drug addiction, cognition and nociception. To perform these and other functions, a diverse array of nAChR subtypes are generated by homomeric or heteromeric assembly of 17 homologous nAChR subunits. Agonists, acetylcholine and nicotine, bind to the interface formed between two \u03b1 subunits and between \u03b1 and non-\u03b1 subunits to activate the nAChR and allow cation influx. The diversity of subunit interfaces determines the channel properties, the responses to different agonists\/antagonists, desensitization and downstream signaling and thus, define specialized properties and functions. Over the last several decades, snake venom neurotoxins have contributed to the purification, localization and characterization of molecular details of various nAChRs. Utkin et al. have described the purification and characterization of \u03b1\u03b4-bungarotoxins, a novel class of neurotoxins in a recent paper published in the Biochemical Journal [Biochem. J. (2019) 476, 1285\u20131302]. These toxins from Bungarus candidus venom preferably bind to \u03b1\u2013\u03b4 site with two orders of magnitude higher affinity compared with \u03b1\u2013\u03b3 or \u03b1\u2013\u03b5 sites. The subtle changes in the structure of \u03b1\u03b4-bungarotoxins led to variation in interface selectivity. Such new classes of antagonists will offer us great opportunity to delineate the pharmacophores and design new highly selective antagonists. Thus, their findings provide new impetus to re-evaluate molecular details of pharmacological properties of \u03b1-neurotoxins with careful consideration towards subtype-, interface- and species-selectivity.<\/jats:p>","DOI":"10.1042\/bcj20190255","type":"journal-article","created":{"date-parts":[[2019,5,28]],"date-time":"2019-05-28T12:35:17Z","timestamp":1559046917000},"page":"1515-1520","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":14,"title":["Toxins for decoding interface selectivity in nicotinic acetylcholine receptors"],"prefix":"10.1042","volume":"476","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-6100-3251","authenticated-orcid":false,"given":"R. 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