{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,10]],"date-time":"2026-07-10T15:48:30Z","timestamp":1783698510072,"version":"3.55.0"},"reference-count":110,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2015,5,14]],"date-time":"2015-05-14T00:00:00Z","timestamp":1431561600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Nicotinic acetylcholine receptors (nAChRs) fulfill a variety of functions making identification and analysis of nAChR subtypes a challenging task. Traditional instruments for nAChR research are d-tubocurarine, snake venom protein \u03b1-bungarotoxin (\u03b1-Bgt), and \u03b1-conotoxins, neurotoxic peptides from Conus snails. Various new compounds of different structural classes also interacting with nAChRs have been recently identified. Among the low-molecular weight compounds are alkaloids pibocin, varacin and makaluvamines C and G. 6-Bromohypaphorine from the mollusk Hermissenda crassicornis does not bind to Torpedo nAChR but behaves as an agonist on human \u03b17 nAChR. To get more selective \u03b1-conotoxins, computer modeling of their complexes with acetylcholine-binding proteins and distinct nAChRs was used. Several novel three-finger neurotoxins targeting nAChRs were described and \u03b1-Bgt inhibition of GABA-A receptors was discovered. Information on the mechanisms of nAChR interactions with the three-finger proteins of the Ly6 family was found. Snake venom phospholipases A2 were recently found to inhibit different nAChR subtypes. Blocking of nAChRs in Lymnaea stagnalis neurons was shown for venom C-type lectin-like proteins, appearing to be the largest molecules capable to interact with the receptor. A huge nAChR molecule sensible to conformational rearrangements accommodates diverse binding sites recognizable by structurally very different compounds.<\/jats:p>","DOI":"10.3390\/toxins7051683","type":"journal-article","created":{"date-parts":[[2015,5,15]],"date-time":"2015-05-15T07:57:02Z","timestamp":1431676622000},"page":"1683-1701","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":33,"title":["Natural Compounds Interacting with Nicotinic Acetylcholine Receptors: From Low-Molecular Weight Ones to Peptides and Proteins"],"prefix":"10.3390","volume":"7","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0313-9193","authenticated-orcid":false,"given":"Denis","family":"Kudryavtsev","sequence":"first","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Irina","family":"Shelukhina","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Catherine","family":"Vulfius","sequence":"additional","affiliation":[{"name":"Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tatyana","family":"Makarieva","sequence":"additional","affiliation":[{"name":"Elyakov Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok 690022, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Valentin","family":"Stonik","sequence":"additional","affiliation":[{"name":"Elyakov Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok 690022, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maxim","family":"Zhmak","sequence":"additional","affiliation":[{"name":"SME Syneuro, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor","family":"Ivanov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor","family":"Kasheverov","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4609-970X","authenticated-orcid":false,"given":"Yuri","family":"Utkin","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victor","family":"Tsetlin","sequence":"additional","affiliation":[{"name":"Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2015,5,14]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"40207","DOI":"10.1074\/jbc.R112.407668","article-title":"The nicotinic acetylcholine receptor: The founding father of the pentameric ligand-gated ion channel superfamily","volume":"287","author":"Changeux","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1007\/s00424-012-1200-1","article-title":"Cholinergic receptors: Functional role of nicotinic ACh receptors in brain circuits and disease","volume":"465","author":"Yakel","year":"2013","journal-title":"Pflugers. Arch. Eur. J. Physiol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"941","DOI":"10.1016\/j.str.2012.05.003","article-title":"Structure and pharmacology of pentameric receptor channels: From bacteria to brain","volume":"20","author":"Corringer","year":"2012","journal-title":"Structure"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.tips.2014.12.002","article-title":"Nicotinic ACh receptors as therapeutic targets in CNS disorders","volume":"36","author":"Dineley","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_5","doi-asserted-by":"crossref","unstructured":"Lombardo, S., and Maskos, U. (2014). Role of the nicotinic acetylcholine receptor in Alzheimer\u2019s disease pathology and treatment. Neuropharmacology.","DOI":"10.1016\/j.neuropharm.2014.11.018"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1097\/WCO.0b013e32833cc968","article-title":"Autoimmune mediated neuromuscular junction defects","volume":"23","author":"Farrugia","year":"2010","journal-title":"Curr. Opin. Neurol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.jmb.2004.12.031","article-title":"Refined structure of the nicotinic acetylcholine receptor at 4A resolution","volume":"346","author":"Unwin","year":"2005","journal-title":"J. Mol. Biol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1017\/S0033583513000061","article-title":"Nicotinic acetylcholine receptor and the structural basis of neuromuscular transmission: Insights from Torpedo postsynaptic membranes","volume":"46","author":"Unwin","year":"2013","journal-title":"Q. Rev. Biophys."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1038\/35077011","article-title":"Crystal structure of an ACh-binding protein reveals the ligand-binding domain of nicotinic receptors","volume":"411","author":"Brejc","year":"2001","journal-title":"Nature"},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1038\/nsmb951","article-title":"Crystal structure of nicotinic acetylcholine receptor homolog AChBP in complex with an alpha-conotoxin PnIA variant","volume":"12","author":"Celie","year":"2005","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"907","DOI":"10.1016\/S0896-6273(04)00115-1","article-title":"Nicotine and carbamylcholine binding to nicotinic acetylcholine receptors as studied in AChBP crystal structures","volume":"41","author":"Celie","year":"2004","journal-title":"Neuron"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"3635","DOI":"10.1038\/sj.emboj.7600828","article-title":"Structures of Aplysia AChBP complexes with nicotinic agonists and antagonists reveal distinctive binding interfaces and conformations","volume":"24","author":"Hansen","year":"2005","journal-title":"EMBO J."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1038\/nn.2908","article-title":"Ligand-binding domain of an \u03b17-nicotinic receptor chimera and its complex with agonist","volume":"14","author":"Li","year":"2011","journal-title":"Nat. Neurosci."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"e1001034","DOI":"10.1371\/journal.pbio.1001034","article-title":"A structural and mutagenic blueprint for molecular recognition of strychnine and d-tubocurarine by different cys-loop receptors","volume":"9","author":"Brams","year":"2011","journal-title":"PLoS Biol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"1512","DOI":"10.1038\/sj.emboj.7600620","article-title":"Crystal structure of a Cbtx-AChBP complex reveals essential interactions between snake alpha-neurotoxins and nicotinic receptors","volume":"24","author":"Bourne","year":"2005","journal-title":"EMBO J."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1042\/BJ20130636","article-title":"Complex between \u03b1-bungarotoxin and an \u03b17 nicotinic receptor ligand-binding domain chimaera","volume":"454","author":"Huang","year":"2013","journal-title":"Biochem. J."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"3615","DOI":"10.1073\/pnas.0507889103","article-title":"Structural determinants of selective alpha-conotoxin binding to a nicotinic acetylcholine receptor homolog AChBP","volume":"103","author":"Ulens","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"3858","DOI":"10.1038\/sj.emboj.7601785","article-title":"AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity","volume":"26","author":"Dutertre","year":"2007","journal-title":"EMBO J."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1016\/j.bcp.2009.05.032","article-title":"Polypeptide and peptide toxins, magnifying lenses for binding sites in nicotinic acetylcholine receptors","volume":"78","author":"Tsetlin","year":"2009","journal-title":"Biochem. Pharmacol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.toxicon.2012.09.007","article-title":"Three-finger toxins, a deadly weapon of elapid venom--milestones of discovery","volume":"62","author":"Utkin","year":"2013","journal-title":"Toxicon"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1111\/j.1471-4159.2009.06033.x","article-title":"Presence of alpha7 nicotinic acetylcholine receptors on dorsal root ganglion neurons proved using knockout mice and selective alpha-neurotoxins in histochemistry","volume":"109","author":"Shelukhina","year":"2009","journal-title":"J. Neurochem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/j.neuron.2011.04.013","article-title":"Aversion to nicotine is regulated by the balanced activity of \u03b24 and \u03b15 nicotinic receptor subunits in the medial habenula","volume":"70","author":"Frahm","year":"2011","journal-title":"Neuron"},{"key":"ref_23","first-page":"31173","article-title":"Conus peptides: Biodiversity-Based discovery and exogenomics","volume":"281","author":"Olivera","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.2174\/138161209788682316","article-title":"Naturally occurring and synthetic peptides acting on nicotinic acetylcholine receptors","volume":"15","author":"Kasheverov","year":"2009","journal-title":"Curr. Pharm. Des."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1016\/j.toxicon.2012.04.340","article-title":"Towards an integrated venomics approach for accelerated conopeptide discovery","volume":"60","author":"Prashanth","year":"2012","journal-title":"Toxicon"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1817","DOI":"10.1021\/tx200182m","article-title":"Cyclic Imines: Chemistry and Mechanism of Action: A Review","volume":"24","author":"Otero","year":"2011","journal-title":"Chem. Res. Toxicol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"6076","DOI":"10.1073\/pnas.0912372107","article-title":"Structural determinants in phycotoxins and AChBP conferring high affinity binding and nicotinic AChR antagonism","volume":"107","author":"Bourne","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"1753","DOI":"10.1021\/tx100210a","article-title":"Human muscarinic acetylcholine receptors are a target of the marine toxin 13-desmethyl C spirolide","volume":"23","author":"Wandscheer","year":"2010","journal-title":"Chem. Res. Toxicol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/toxins4010001","article-title":"Investigations into the toxicology of spirolides, a group of marine phycotoxins","volume":"4","author":"Munday","year":"2012","journal-title":"Toxins (Basel)"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1859","DOI":"10.3390\/md12041859","article-title":"Marine natural products acting on the acetylcholine-binding protein and nicotinic receptors: From computer modeling to binding studies and electrophysiology","volume":"12","author":"Kudryavtsev","year":"2014","journal-title":"Mar. Drugs"},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1517\/17460441.2013.822365","article-title":"Physical and virtual screening methods for marine toxins and drug discovery targeting nicotinic acetylcholine receptors","volume":"8","author":"Benoit","year":"2013","journal-title":"Expert Opin. Drug Discov."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Philpot, R.M. (2015). Potential Use of Nicotinic Receptor Agonists for the Treatment of Chemotherapy-Induced Cognitive Deficits. Neurochem. Res.","DOI":"10.1007\/s11064-015-1528-y"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.clinthera.2014.09.013","article-title":"Pharmacodynamics, Pharmacokinetics, Safety, and Tolerability of Encenicline, a Selective \u03b17 Nicotinic Receptor Partial Agonist, in Single Ascending-dose and Bioavailability Studies","volume":"37","author":"Barbier","year":"2015","journal-title":"Clin. Ther."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1208\/s12248-012-9328-7","article-title":"Population analyses of efficacy and safety of ABT-594 in subjects with diabetic peripheral neuropathic pain","volume":"14","author":"Dutta","year":"2012","journal-title":"AAPS J."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.3390\/md13031255","article-title":"6-Bromohypaphorine from Marine Nudibranch Mollusk Hermissenda crassicornis is an Agonist of Human \u03b17 Nicotinic Acetylcholine Receptor","volume":"13","author":"Kasheverov","year":"2015","journal-title":"Mar. Drugs"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"4226","DOI":"10.2174\/138161211798999384","article-title":"Structure-activity studies on alpha-conotoxins","volume":"17","author":"Muttenthaler","year":"2011","journal-title":"Curr. Pharm. Des."},{"key":"ref_37","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":"ref_38","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.4155\/fmc.14.99","article-title":"Cone snail venomics: from novel biology to novel therapeutics","volume":"6","author":"Prashanth","year":"2014","journal-title":"Future Med. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"6042","DOI":"10.2174\/1381612820666140314150634","article-title":"Alpha9 alpha10 nicotinic acetylcholine receptors as target for the treatment of chronic pain","volume":"20","author":"Cesario","year":"2014","journal-title":"Curr. Pharm. Des."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.toxicon.2010.09.009","article-title":"Venomic study on cone snails (Conus spp.) from South Africa","volume":"57","author":"Kauferstein","year":"2011","journal-title":"Toxicon"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.peptides.2012.07.002","article-title":"Unraveling the peptidome of the South African cone snails Conus pictus and Conus natalis","volume":"41","author":"Peigneur","year":"2013","journal-title":"Peptides"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.1016\/j.peptides.2010.07.011","article-title":"A new subfamily of conotoxins belonging to the A-superfamily","volume":"31","author":"Peng","year":"2010","journal-title":"Peptides"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1074\/jbc.M112.427898","article-title":"Characterization of a novel \u03b1-conotoxin from conus textile that selectively targets \u03b16\/\u03b13\u03b22\u03b23 nicotinic acetylcholine receptors","volume":"288","author":"Luo","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1016\/j.toxicon.2012.06.011","article-title":"Diversity and evolution of conotoxins in Conus virgo, Conus eburneus, Conus imperialis and Conus marmoreus from the South China Sea","volume":"60","author":"Liu","year":"2012","journal-title":"Toxicon"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"791","DOI":"10.1016\/j.bcp.2013.07.016","article-title":"Isolation and characterization of \u03b1-conotoxin LsIA with potent activity at nicotinic acetylcholine receptors","volume":"86","author":"Inserra","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.toxicon.2014.08.074","article-title":"Discovery of a new subclass of \u03b1-conotoxins in the venom of Conus australis","volume":"91","author":"Lebbe","year":"2014","journal-title":"Toxicon"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.toxicon.2014.10.006","article-title":"Isolation, purification and functional characterization of alpha-BnIA from Conus bandanus venom","volume":"91","author":"Nguyen","year":"2014","journal-title":"Toxicon"},{"key":"ref_48","doi-asserted-by":"crossref","unstructured":"Morales-Gonz\u00e1lez, D., Flores-Mart\u00ednez, E., Zamora-Bustillos, R., Rivera-Reyes, R., Michel-Morf\u00edn, J.E., Landa-Jaime, V., Falc\u00f3n, A., and Aguilar, M.B. (2015). Diversity of A-conotoxins of three worm-hunting cone snails (Conus brunneus, Conus nux, and Conus princeps) from the Mexican Pacific coast. Peptides.","DOI":"10.1016\/j.peptides.2015.02.002"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"6628","DOI":"10.1021\/bi7004202","article-title":"Discovery, synthesis, and structure activity of a highly selective alpha7 nicotinic acetylcholine receptor antagonist","volume":"46","author":"Whiteaker","year":"2007","journal-title":"Biochemistry"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1074\/jbc.M109.071183","article-title":"A synthetic combinatorial strategy for developing alpha-conotoxin analogs as potent alpha7 nicotinic acetylcholine receptor antagonists","volume":"285","author":"Armishaw","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"3511","DOI":"10.1021\/jm500183r","article-title":"Discovery of a potent and selective \u03b13\u03b24 nicotinic acetylcholine receptor antagonist from an \u03b1-conotoxin synthetic combinatorial library","volume":"57","author":"Chang","year":"2014","journal-title":"J. Med. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"11625","DOI":"10.1074\/jbc.M710288200","article-title":"Amino acid residues that confer high selectivity of the alpha6 nicotinic acetylcholine receptor subunit to alpha-conotoxin MII[S4A,E11A,L15A]","volume":"283","author":"Azam","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"972","DOI":"10.1124\/mol.112.080853","article-title":"\u03b1-Conotoxin PeIA[S9H,V10A,E14N] potently and selectively blocks \u03b16\u03b22\u03b23 versus \u03b16\u03b24 nicotinic acetylcholine receptors","volume":"82","author":"Hone","year":"2012","journal-title":"Mol. Pharmacol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"143","DOI":"10.4161\/chan.2.2.6276","article-title":"Subtype-selective conopeptides targeted to nicotinic receptors: Concerted discovery and biomedical applications","volume":"2","author":"Olivera","year":"2008","journal-title":"Channels (Austin)"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1038\/aps.2009.63","article-title":"Mysterious alpha6-containing nAChRs: Function, pharmacology, and pathophysiology","volume":"30","author":"Yang","year":"2009","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1096\/fj.11-190223","article-title":"Native \u03b16\u03b24* nicotinic receptors control exocytosis in human chromaffin cells of the adrenal gland","volume":"26","author":"McIntosh","year":"2012","journal-title":"FASEB J."},{"key":"ref_57","first-page":"214","article-title":"Effect of alpha-conotoxin MII and its N-terminal derivatives on Ca2+ and Na+ signals induced by nicotine in neuroblastoma cell line SH-SY5Y","volume":"38","author":"Surin","year":"2012","journal-title":"Bioorg. Khim."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1111\/j.1471-4159.2010.06819.x","article-title":"Alexa Fluor 546-ArIB[V11L;V16A] is a potent ligand for selectively labeling alpha 7 nicotinic acetylcholine receptors","volume":"114","author":"Hone","year":"2010","journal-title":"J. Neurochem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1698","DOI":"10.3390\/md9101698","article-title":"Design of new \u03b1-conotoxins: From computer modeling to synthesis of potent cholinergic compounds","volume":"9","author":"Kasheverov","year":"2011","journal-title":"Mar. Drugs"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1021\/ci500158y","article-title":"Deciphering fine molecular details of proteins\u2019 structure and function with a Protein Surface Topography (PST) method","volume":"54","author":"Koromyslova","year":"2014","journal-title":"J. Chem. Inf. Model."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1134\/S1607672915020118","article-title":"Rational design of new ligands for nicotinic receptors on the basis of \u03b1-conotoxin PnIA","volume":"461","author":"Kasheverov","year":"2015","journal-title":"Dokl. Biochem. Biophys."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/0041-0101(91)90107-3","article-title":"Characterization and amino acid sequences of two lethal peptides isolated from venom of Wagler\u2019s pit viper, Trimeresurus wagleri","volume":"29","author":"Weinstein","year":"1991","journal-title":"Toxicon"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"27079","DOI":"10.1074\/jbc.M112.363051","article-title":"Azemiopsin from Azemiops feae viper venom, a novel polypeptide ligand of nicotinic acetylcholine receptor","volume":"287","author":"Utkin","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1074\/mcp.M112.023135","article-title":"Differential evolution and neofunctionalization of snake venom metalloprotease domains","volume":"12","author":"Brust","year":"2013","journal-title":"Mol. Cell. Proteomics"},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1093\/nar\/gks419","article-title":"PEP-FOLD: An updated de novo structure prediction server for both linear and disulfide bonded cyclic peptides","volume":"40","author":"Shen","year":"2012","journal-title":"Nucleic Acids Res."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"6725","DOI":"10.1074\/jbc.M111.322313","article-title":"Dimeric \u03b1-cobratoxin X-ray structure: Localization of intermolecular disulfides and possible mode of binding to nicotinic acetylcholine receptors","volume":"287","author":"Osipov","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"10618","DOI":"10.1074\/jbc.M110.189100","article-title":"NMR structure and action on nicotinic acetylcholine receptors of water-soluble domain of human LYNX1","volume":"286","author":"Lyukmanova","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1002\/elps.200900140","article-title":"Automated comparative protein structure modeling with SWISS-MODEL and Swiss-PdbViewer: A historical perspective","volume":"30","author":"Guex","year":"2009","journal-title":"Electrophoresis"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.tips.2014.11.003","article-title":"Three-finger snake neurotoxins and Ly6 proteins targeting nicotinic acetylcholine receptors: Pharmacological tools and endogenous modulators","volume":"36","author":"Tsetlin","year":"2015","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_70","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_71","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_72","doi-asserted-by":"crossref","first-page":"3758","DOI":"10.1021\/bi5004475","article-title":"Isolation and Structural and Pharmacological Characterization of \u03b1-Elapitoxin-Dpp2d, an Amidated Three Finger Toxin from Black Mamba Venom","volume":"53","author":"Wang","year":"2014","journal-title":"Biochemistry"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1016\/j.bcp.2010.10.004","article-title":"\u03b1-Elapitoxin-Aa2a, a long-chain snake \u03b1-neurotoxin with potent actions on muscle (\u03b11)(2)\u03b2\u03b3\u03b4 nicotinic receptors, lacks the classical high affinity for neuronal \u03b17 nicotinic receptors","volume":"81","author":"Blacklow","year":"2011","journal-title":"Biochem. Pharmacol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/j.bcp.2012.06.024","article-title":"Pharmacological characterization of \u03b1-elapitoxin-Al2a from the venom of the Australian pygmy copperhead (Austrelaps. labialis): An atypical long-chain \u03b1-neurotoxin with only weak affinity for \u03b17 nicotinic receptors","volume":"84","author":"Marcon","year":"2012","journal-title":"Biochem. Pharmacol."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/0006-8993(85)91097-2","article-title":"Acetylcholine receptors of human skeletal muscle: A species difference detected by snake neurotoxins","volume":"346","author":"Ishikawa","year":"1985","journal-title":"Brain Res."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"29030","DOI":"10.1074\/jbc.M605850200","article-title":"Denmotoxin, a three-finger toxin from the colubrid snake Boiga dendrophila (Mangrove Catsnake) with bird-specific activity","volume":"281","author":"Pawlak","year":"2006","journal-title":"J. Biol. Chem."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"1923","DOI":"10.1016\/j.biochi.2013.06.025","article-title":"Identification and characterization of a taxon-specific three-finger toxin from the venom of the Green Vinesnake (Oxybelis fulgidus; Family Colubridae)","volume":"95","author":"Heyborne","year":"2013","journal-title":"Biochimie"},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"14571","DOI":"10.1074\/jbc.M802085200","article-title":"Naturally occurring disulfide-bound dimers of three-fingered toxins: A paradigm for biological activity diversification","volume":"283","author":"Osipov","year":"2008","journal-title":"J. Biol. Chem."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"534","DOI":"10.1096\/fj.08-113555","article-title":"Irditoxin, a novel covalently linked heterodimeric three finger toxin with high taxon-specific neurotoxicity","volume":"23","author":"Pawlak","year":"2009","journal-title":"FASEB J."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"5149","DOI":"10.1073\/pnas.0600847103","article-title":"The cholinergic antagonist alpha-bungarotoxin also binds and blocks a subset of GABA receptors","volume":"103","author":"McCann","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1016\/j.neuropharm.2015.01.001","article-title":"Snake neurotoxin \u03b1-bungarotoxin is an antagonist at native GABAA receptors","volume":"93C","author":"Hannan","year":"2015","journal-title":"Neuropharmacology"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.neuron.2011.03.014","article-title":"Neural systems governed by nicotinic acetylcholine receptors: Emerging hypotheses","volume":"70","author":"Miwa","year":"2011","journal-title":"Neuron"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.conb.2011.11.003","article-title":"Tethering toxins and peptide ligands for modulation of neuronal function","volume":"22","author":"Nitabach","year":"2012","journal-title":"Curr. Opin. Neurobiol."},{"key":"ref_84","first-page":"187","article-title":"Optimizing cholinergic tone through lynx modulators of nicotinic receptors: Implications for plasticity and nicotine addiction","volume":"27","author":"Miwa","year":"2012","journal-title":"Physiology (Bethesda)"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"15888","DOI":"10.1074\/jbc.M112.436576","article-title":"Water-soluble LYNX1 residues important for interaction with muscle-type and\/or neuronal nicotinic receptors","volume":"288","author":"Lyukmanova","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"31423","DOI":"10.1074\/jbc.M114.573667","article-title":"Lynx1 shifts \u03b14\u03b22 nicotinic receptor subunit stoichiometry by affecting assembly in the endoplasmic reticulum","volume":"289","author":"Nichols","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"3420","DOI":"10.1523\/JNEUROSCI.3630-14.2015","article-title":"Ly6h regulates trafficking of alpha7 nicotinic acetylcholine receptors and nicotine-induced potentiation of glutamatergic signaling","volume":"35","author":"Puddifoot","year":"2015","journal-title":"J. Neurosci."},{"key":"ref_88","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_89","doi-asserted-by":"crossref","first-page":"5065","DOI":"10.1111\/j.1742-4658.2009.07203.x","article-title":"Weak toxin WTX from Naja kaouthia cobra venom interacts with both nicotinic and muscarinic acetylcholine receptors","volume":"276","author":"Mordvintsev","year":"2009","journal-title":"FEBS J."},{"key":"ref_90","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_91","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1016\/j.cub.2014.02.026","article-title":"SLEEPLESS is a bifunctional regulator of excitability and cholinergic synaptic transmission","volume":"24","author":"Wu","year":"2014","journal-title":"Curr. Biol."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.toxicon.2011.02.013","article-title":"An unusual phospholipase A2 from puff adder Bitis arietans venom\u2014A novel blocker of nicotinic acetylcholine receptors","volume":"57","author":"Vulfius","year":"2011","journal-title":"Toxicon"},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"e115428","DOI":"10.1371\/journal.pone.0115428","article-title":"Inhibition of nicotinic acetylcholine receptors, a novel facet in the pleiotropic activities of snake venom phospholipases A2","volume":"9","author":"Vulfius","year":"2014","journal-title":"PLoS ONE"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"604","DOI":"10.1134\/S1607672915020143","article-title":"Novel antagonists of nicotinic acethylcholine receptors\u2014Proteins from venoms of viperidae snakes","volume":"461","author":"Vulfius","year":"2015","journal-title":"Dokl. Biochem. Biophys."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"6151","DOI":"10.1074\/jbc.M008467200","article-title":"Location of the polyamine binding site in the vestibule of the nicotinic acetylcholine receptor ion channel","volume":"276","author":"Bixel","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"2425","DOI":"10.1021\/bi300101r","article-title":"Bupropion binds to two sites in the Torpedo nicotinic acetylcholine receptor transmembrane domain: A photoaffinity labeling study with the bupropion analogue [(125)I]-SADU-3\u201372","volume":"51","author":"Pandhare","year":"2012","journal-title":"Biochemistry"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"1306","DOI":"10.1016\/j.neuropharm.2011.07.035","article-title":"Competitive binding at a nicotinic receptor transmembrane site of two \u03b17-selective positive allosteric modulators with differing effects on agonist-evoked","volume":"61","author":"Collins","year":"2011","journal-title":"Neuropharmacology"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"1054","DOI":"10.1016\/j.bcp.2013.05.018","article-title":"Effects of neuronal nicotinic acetylcholine receptor allosteric modulators in animal behavior studies","volume":"86","author":"Pandya","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1016\/j.ejphar.2009.12.028","article-title":"The effect of local anesthetics on the inhibition of adult muscle-type nicotinic acetylcholine receptors by nondepolarizing muscle relaxants","volume":"630","author":"Wang","year":"2010","journal-title":"Eur. J. Pharmacol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.neures.2013.01.005","article-title":"Lidocaine effects on acetylcholine-elicited currents from mouse superior cervical ganglion neurons","volume":"75","author":"Reboreda","year":"2013","journal-title":"Neurosci. Res."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"10622","DOI":"10.1073\/pnas.1301277110","article-title":"Structure and superorganization of acetylcholine receptor-rapsyn complexes","volume":"110","author":"Zuber","year":"2013","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"890","DOI":"10.1111\/j.1460-9568.2010.07569.x","article-title":"MuSK levels differ between adult skeletal muscles and influence postsynaptic plasticity","volume":"33","author":"Punga","year":"2011","journal-title":"Eur. J. Neurosci."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jmb.2009.07.091","article-title":"Crystal structure of the frizzled-like cysteine-rich domain of the receptor tyrosine kinase MuSK","volume":"393","author":"Stiegler","year":"2009","journal-title":"J. Mol. Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"5992","DOI":"10.1016\/j.bmc.2012.06.054","article-title":"Identification of novel \u03b17 nicotinic receptor ligands by in silico screening against the crystal structure of a chimeric \u03b17 receptor ligand binding domain","volume":"20","author":"Akdemir","year":"2012","journal-title":"Bioorg. Med. Chem."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/nature06717","article-title":"X-ray structure of a prokaryotic pentameric ligand-gated ion channel","volume":"452","author":"Hilf","year":"2008","journal-title":"Nature"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1038\/nature07462","article-title":"X-ray structure of a pentameric ligand-gated ion channel in an apparently open conformation","volume":"457","author":"Bocquet","year":"2009","journal-title":"Nature"},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1038\/nature09647","article-title":"X-ray structures of general anaesthetics bound to a pentameric ligand-gated ion channel","volume":"469","author":"Nury","year":"2011","journal-title":"Nature"},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1038\/nature10139","article-title":"Principles of activation and permeation in an anion-selective Cys-loop receptor","volume":"474","author":"Hibbs","year":"2011","journal-title":"Nature"},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1038\/nature13552","article-title":"X-ray structure of the mouse serotonin 5-HT3 receptor","volume":"512","author":"Hassaine","year":"2014","journal-title":"Nature"},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1038\/nature13293","article-title":"Crystal structure of a human GABAA receptor","volume":"512","author":"Miller","year":"2014","journal-title":"Nature"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/7\/5\/1683\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T20:46:19Z","timestamp":1760215579000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/7\/5\/1683"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,5,14]]},"references-count":110,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2015,5]]}},"alternative-id":["toxins7051683"],"URL":"https:\/\/doi.org\/10.3390\/toxins7051683","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,5,14]]}}}