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Recently isolated from\n                      <jats:italic>Bungarus candidus<\/jats:italic>\n                      venom, \u03b1\u03b4\u2010bungarotoxins differ from \u03b1\u2010Bgt: they bind more reversibly and distinguish two binding sites in\n                      <jats:italic>Torpedo californica<\/jats:italic>\n                      nAChR.\n                      <jats:italic>Naja kaouthia<\/jats:italic>\n                      \u03b1\u2010cobratoxin, classical blocker of nAChRs, was shown to inhibit certain GABA\u2010A receptor subtypes, whereas \u03b1\u2010cobratoxin dimer with 2 intermolecular disulfides has a novel type of 3D structure. Non\u2010conventional toxin WTX has additional 5th disulfide not in the central loop, as \u03b1\u2010Bgt, but in the N\u2010terminal loop, like all Ly6\/uPAR proteins, and inhibits \u03b17 and Torpedo nAChRs. A water\u2010soluble form of Lynx1, ws\u2010Lynx1, was expressed in\n                      <jats:italic>E<\/jats:italic>\n                      .\n                      <jats:italic>coli<\/jats:italic>\n                      , its\n                      <jats:sup>1<\/jats:sup>\n                      H\u2010NMR structure and binding to several nAChRs determined. For SLURP\u20101, similar information was obtained with its recombinant analogue rSLURP\u20101. A common feature of ws\u2010Lynx1, rSLURP\u20101, and WTX is their activity against nAChRs and muscarinic acetylcholine receptors. Synthetic SLURP\u20101, identical to the natural protein, demonstrated some differences from rSLURP\u20101 in distinguishing nAChR subtypes. The loop II fragment of the Lynx1 was synthesized having the same \u00b5M affinity for the Torpedo nAChR as ws\u2010Lynx1. This review illustrates the productivity of parallel research of nAChR interactions with the two TFP groups.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:label\/>\n                    <jats:p>\n                      <jats:boxed-text content-type=\"graphic\" position=\"anchor\">\n                        <jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc15123-fig-0003-m.png\">\n                          <jats:alt-text>image<\/jats:alt-text>\n                        <\/jats:graphic>\n                      <\/jats:boxed-text>\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1111\/jnc.15123","type":"journal-article","created":{"date-parts":[[2020,7,10]],"date-time":"2020-07-10T09:25:00Z","timestamp":1594373100000},"page":"1223-1235","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["Three\u2010finger proteins from snakes and humans acting on nicotinic receptors: Old and new"],"prefix":"10.1111","volume":"158","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7980-6191","authenticated-orcid":false,"given":"Victor I.","family":"Tsetlin","sequence":"first","affiliation":[{"name":"Department of Molecular Neuroimmune Signalling Shemyakin\u2010Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russian Federation"},{"name":"PhysBio of MePhi Moscow Russian Federation"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7373-6524","authenticated-orcid":false,"given":"Igor E.","family":"Kasheverov","sequence":"additional","affiliation":[{"name":"Department of Molecular Neuroimmune Signalling Shemyakin\u2010Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russian Federation"},{"name":"Sechenov First Moscow State Medical University Institute of Molecular Medicine Moscow Russian Federation"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4609-970X","authenticated-orcid":false,"given":"Yuri N.","family":"Utkin","sequence":"additional","affiliation":[{"name":"Department of Molecular Neuroimmune Signalling Shemyakin\u2010Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russian Federation"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2020,7,26]]},"reference":[{"key":"e_1_2_11_2_1","doi-asserted-by":"publisher","DOI":"10.1110\/ps.8.4.810"},{"key":"e_1_2_11_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.neuint.2017.05.015"},{"key":"e_1_2_11_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/ijd.13850"},{"key":"e_1_2_11_5_1","doi-asserted-by":"publisher","DOI":"10.1038\/sj.emboj.7600620"},{"key":"e_1_2_11_6_1","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0217339"},{"key":"e_1_2_11_7_1","doi-asserted-by":"publisher","DOI":"10.3109\/10799893.2013.865747"},{"key":"e_1_2_11_8_1","doi-asserted-by":"publisher","DOI":"10.1096\/fba.1027"},{"key":"e_1_2_11_9_1","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 C. 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