{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T01:52:35Z","timestamp":1792806755303,"version":"4.5.0"},"reference-count":149,"publisher":"MDPI AG","issue":"4","license":[{"start":{"date-parts":[[2023,3,24]],"date-time":"2023-03-24T00:00:00Z","timestamp":1679616000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"National Council for Scientific and Technological Development","award":["DCP (301975\/2019-5)"],"award-info":[{"award-number":["DCP (301975\/2019-5)"]}],"id":[{"id":"https:\/\/ror.org\/03swz6y49","id-type":"ROR","asserted-by":"crossref"}]},{"name":"National Council for Scientific and Technological Development","award":["CAPES \u2013grant #1"],"award-info":[{"award-number":["CAPES \u2013grant #1"]}],"id":[{"id":"https:\/\/ror.org\/03swz6y49","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Instituto Butantan","award":["DCP (301975\/2019-5)"],"award-info":[{"award-number":["DCP (301975\/2019-5)"]}],"id":[{"id":"https:\/\/ror.org\/01whwkf30","id-type":"ROR","asserted-by":"crossref"}]},{"name":"Instituto Butantan","award":["CAPES \u2013grant #1"],"award-info":[{"award-number":["CAPES \u2013grant #1"]}],"id":[{"id":"https:\/\/ror.org\/01whwkf30","id-type":"ROR","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>The Buthidae family of scorpions consists of arthropods with significant medical relevance, as their venom contains a diverse range of biomolecules, including neurotoxins that selectively target ion channels in cell membranes. These ion channels play a crucial role in regulating physiological processes, and any disturbance in their activity can result in channelopathies, which can lead to various diseases such as autoimmune, cardiovascular, immunological, neurological, and neoplastic conditions. Given the importance of ion channels, scorpion peptides represent a valuable resource for developing drugs with targeted specificity for these channels. This review provides a comprehensive overview of the structure and classification of ion channels, the action of scorpion toxins on these channels, and potential avenues for future research. Overall, this review highlights the significance of scorpion venom as a promising source for discovering novel drugs with therapeutic potential for treating channelopathies.<\/jats:p>","DOI":"10.3390\/toxins15040238","type":"journal-article","created":{"date-parts":[[2023,3,24]],"date-time":"2023-03-24T04:31:05Z","timestamp":1679632265000},"page":"238","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":64,"title":["Scorpion Peptides and Ion Channels: An Insightful Review of Mechanisms and Drug Development"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6313-7029","authenticated-orcid":false,"given":"Lais Campelo","family":"Mendes","sequence":"first","affiliation":[{"name":"Programa de P\u00f3s-Gradua\u00e7\u00e3o em Ci\u00eancias\u2014Toxinologia do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"},{"name":"Laborat\u00f3rio de Bioqu\u00edmica do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriela Magn\u00f3lia Melo","family":"Viana","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1162-4201","authenticated-orcid":false,"given":"Ana Leonor Abrah\u00e3o","family":"Nencioni","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Farmacologia do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2406-0860","authenticated-orcid":false,"given":"Daniel Carvalho","family":"Pimenta","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4735-5162","authenticated-orcid":false,"given":"Emidio","family":"Beraldo-Neto","sequence":"additional","affiliation":[{"name":"Laborat\u00f3rio de Bioqu\u00edmica do Instituto Butantan, S\u00e3o Paulo 05503-900, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,3,24]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.toxicon.2018.11.312","article-title":"Arthropod assassins: Crawling biochemists with diverse toxin pharmacopeias","volume":"158","author":"Herzig","year":"2019","journal-title":"Toxicon"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"20210034","DOI":"10.1590\/1678-9199-jvatitd-2021-0034","article-title":"Toxinology in the proteomics era: A review on arachnid venom proteomics","volume":"28","author":"Marchi","year":"2022","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1007\/s00134-020-05924-8","article-title":"Scorpion envenomation: State of the art","volume":"46","author":"Abroug","year":"2020","journal-title":"Intensiv. Care Med."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1016\/j.actatropica.2008.05.021","article-title":"Epidemiology of scorpionism: A global appraisal","volume":"107","author":"Chippaux","year":"2008","journal-title":"Acta Trop."},{"key":"ref_5","first-page":"18","article-title":"Filogenia Molecular Baseada em COI de Alguns Escorpi\u00f5es Buthidae do Egito","volume":"13","author":"Almaaty","year":"2022","journal-title":"J. Biotech"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1016\/bs.mie.2021.01.029","article-title":"Production of recombinant venom peptides as tools for ion channel research","volume":"654","author":"Saikia","year":"2021","journal-title":"Methods Enzymol."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fphar.2022.858348","article-title":"Druggability of Voltage-Gated Sodium Channels\u2014Exploring Old and New Drug Receptor Sites","volume":"13","author":"Wisedchaisri","year":"2022","journal-title":"Front. Pharmacol."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1016\/j.ceca.2019.05.003","article-title":"Anti-tumoral effect of scorpion peptides: Emerging new cellular targets and signaling pathways","volume":"80","author":"Othman","year":"2019","journal-title":"Cell Calcium"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"7093","DOI":"10.1021\/jm501981g","article-title":"Voltage-Gated Sodium Channels: Structure, Function, Pharmacology, and Clinical Indications","volume":"58","author":"Kraus","year":"2015","journal-title":"J. Med. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.neuropharm.2017.10.031","article-title":"Animal Toxins for Channelopathy Treatment","volume":"132","author":"Kozlov","year":"2018","journal-title":"Neuropharmacology"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"170643","DOI":"10.1016\/j.peptides.2021.170643","article-title":"Transcriptomic and proteomic analyses of venom glands from scorpions Liocheles australasiae, Mesobuthus martensii, and Scorpio maurus palmatus","volume":"146","author":"So","year":"2021","journal-title":"Peptides"},{"key":"ref_12","unstructured":"Santib\u00e1\u00f1ez-L\u00f3pez, C. (2022, August 20). 2022 Undefined. Phylogenomics of Scorpions Reveal Contemporaneous Diversification of Scorpion Mammalian Predators and Mammal-Active Sodium Channel Toxins. sharmalabuw.org [Internet]. Available online: http:\/\/www.sharmalabuw.org\/uploads\/1\/3\/6\/1\/13619635\/santib%C3%A1%C3%B1ez-l%C3%B3pez_et_al._2022.pdf."},{"key":"ref_13","first-page":"457","article-title":"Scorpion Envenomation","volume":"371","author":"Isbister","year":"2014","journal-title":"Mass. Med. Soc."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1007\/164_2019_333","article-title":"Exploiting the Diversity of Ion Channels: Modulation of Ion Channels for Therapeutic Indications","volume":"260","author":"Liu","year":"2019","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Demirbilek, H., Galcheva, S., Vuralli, D., Al-Khawaga, S., and Hussain, K. (2019). Ion Transporters, Channelopathies, and Glucose Disorders. Int. J. Mol. Sci., 20, Available online: https:\/\/www.mdpi.com\/1422-0067\/20\/10\/2590\/htm.","DOI":"10.3390\/ijms20102590"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"54","DOI":"10.3389\/fcvm.2019.00054","article-title":"Autoimmune Calcium Channelopathies and Cardiac Electrical Abnormalities","volume":"6","author":"Qu","year":"2019","journal-title":"Front. Cardiovasc. Med."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"699","DOI":"10.1111\/ane.13695","article-title":"Potassium channels and epilepsy","volume":"146","author":"Gao","year":"2022","journal-title":"Acta Neurol. Scand."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1661","DOI":"10.3389\/fphys.2018.01661","article-title":"Emerging Roles of the Membrane Potential: Action Beyond the Action Potential","volume":"9","author":"Kadir","year":"2018","journal-title":"Front. Physiol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1007\/164_2021_513","article-title":"Cardiac K+ Channels and Channelopathies","volume":"267","author":"Schreiber","year":"2021","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.neuropharm.2017.05.029","article-title":"Gene therapy and editing: Novel potential treatments for neuronal channelopathies","volume":"132","author":"Wykes","year":"2018","journal-title":"Neuropharmacology"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Hmed, B., Serria, H., and Mounir, Z.K. (2022, June 04). Scorpion Peptides: Potential Use for New Drug Development. hindawi.com [Internet]. Available online: https:\/\/www.hindawi.com\/journals\/jt\/2013\/958797\/.","DOI":"10.1155\/2013\/958797"},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Peigneur, S., and Tytgat, J. (2018). Toxins in Drug Discovery and Pharmacology. Toxins, 10, Available online: https:\/\/www.mdpi.com\/2072-6651\/10\/3\/126\/htm.","DOI":"10.3390\/toxins10030126"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/bs.apha.2017.01.004","article-title":"Sodium Channels and Venom Peptide Pharmacology","volume":"79","author":"Israel","year":"2017","journal-title":"Adv. Pharmacol."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"2955","DOI":"10.1080\/07391102.2020.1848626","article-title":"Methionine 58 is a key residue in the modulation of BmK scorpion toxin AGP-SYPU2 activity through in silico and in vivo studies","volume":"40","author":"Cui","year":"2020","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1016\/j.toxicon.2006.09.023","article-title":"Voltage-gated sodium channel modulation by scorpion \u03b1-toxins","volume":"49","author":"Bosmans","year":"2007","journal-title":"Toxicon"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/MI\/2006\/54273","article-title":"Balance between Pro- and Anti-Inflammatory Cytokines in Mice Treated with Centruroides noxius Scorpion Venom","volume":"2006","author":"Petricevich","year":"2006","journal-title":"Mediat. Inflamm."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1007\/s11274-018-2484-x","article-title":"Improving the secretory expression of active recombinant AaIT in Pichia pastoris by changing the expression strain and plasmid","volume":"34","author":"Li","year":"2018","journal-title":"World J. Microbiol. Biotechnol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.toxicon.2018.07.024","article-title":"Ts1 from the Brazilian scorpion Tityus serrulatus: A half-century of studies on a multifunctional beta like-toxin","volume":"152","author":"Bougis","year":"2018","journal-title":"Toxicon"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1134\/S1607672919010034","article-title":"Recombinant Production and Structure\u2013Function Study of the Ts1 Toxin from the Brazilian Scorpion Tityus serrulatus","volume":"484","author":"Shenkarev","year":"2019","journal-title":"Dokl. Biochem. Biophys."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"148118","DOI":"10.1590\/1678-9199-jvatitd-1481-18","article-title":"Scorpion toxins targeting Kv1.3 channels: Insights into immunosuppression","volume":"25","author":"Oliveira","year":"2019","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/s42977-021-00071-7","article-title":"The Kv1.3 K + channel in the immune system and its \u201cprecision pharmacology\u201d using peptide toxins","volume":"72","author":"Varga","year":"2021","journal-title":"Biol. Futur."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Qin, C., Yang, X., Zuo, Z., Yang, L., Yang, F., Cao, Z., Chen, Z., and Wu, Y. (2021). BmK86-P1, a New Degradation Peptide with Desirable Thermostability and Kv1.2 Channel-Specific Activity from Traditional Chinese Scorpion Medicinal Material. Toxins, 13.","DOI":"10.3390\/toxins13090610"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1","DOI":"10.7554\/eLife.46170","article-title":"Trans-toxin ion-sensitivity of charybdotoxin-blocked potassium-channels reveals unbinding transitional states","volume":"8","author":"Moldenhauer","year":"2019","journal-title":"eLife"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Beltr\u00e1n-Vidal, J., Carcamo-Noriega, E., Pastor, N., Zamudio-Zu\u00f1iga, F., Guerrero-Vargas, J., Casta\u00f1o, S., Possani, L., and Restano-Cassulini, R. (2021). Colombian Scorpion Centruroides margaritatus: Purification and Characterization of a Gamma Potassium Toxin with Full-Block Activity on the hERG1 Channel. Toxins, 13.","DOI":"10.3390\/toxins13060407"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"1093","DOI":"10.3390\/ph3041093","article-title":"A Cell-Penetrating Peptide from Scorpion Venom, as a Probe of Ca2+-Release Channels\/Ryanodine Receptors","volume":"3","author":"Gurrola","year":"2010","journal-title":"Pharmaceuticals"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0014-5793(00)01239-4","article-title":"Chemical synthesis and characterization of maurocalcine, a scorpion toxin that activates Ca2+ release channel\/ryanodine receptors","volume":"469","author":"Fajloun","year":"2000","journal-title":"FEBS Lett."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1111\/j.1476-5381.2009.00147.x","article-title":"Characterization of hadrucalcin, a peptide from Hadrurus gertschi scorpion venom with pharmacological activity on ryanodine receptors","volume":"157","author":"Schwartz","year":"2009","journal-title":"Br. J. Pharmacol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1042\/BJ20061404","article-title":"Hemicalcin, a new toxin from the Iranian scorpion Hemiscorpius lepturus which is active on ryanodine-sensitive Ca2+ channels","volume":"404","author":"Shahbazzadeh","year":"2007","journal-title":"Biochem. J."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1016\/S0006-291X(02)02859-0","article-title":"Scorpion toxins that block T-type Ca2+ channels in spermatogenic cells inhibit the sperm acrosome reaction","volume":"300","author":"Dyason","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1002\/bip.22748","article-title":"Chlorotoxin: Structure, activity, and potential uses in cancer therapy","volume":"106","author":"Ojeda","year":"2016","journal-title":"Biopolymers"},{"key":"ref_41","doi-asserted-by":"crossref","unstructured":"Aissaoui-Zid, D., Saada, M.-C., Moslah, W., Potier-Cartereau, M., Lemettre, A., Othman, H., Gaysinski, M., Abdelkafi-Koubaa, Z., Souid, S., and Marrakchi, N. (2021). AaTs-1: A Tetrapeptide from Androctonus australis Scorpion Venom, Inhibiting U87 Glioblastoma Cells Proliferation by p53 and FPRL-1 Up-Regulations. Molecules, 26, Available online: https:\/\/www.mdpi.com\/1406366.","DOI":"10.3390\/molecules26247610"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.1016\/j.cell.2019.07.014","article-title":"A Cell-Penetrating Scorpion Toxin Enables Mode-Specific Modulation of TRPA1 and Pain","volume":"178","author":"King","year":"2019","journal-title":"Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"3671","DOI":"10.3390\/toxins7093671","article-title":"Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel","volume":"7","author":"Hakim","year":"2015","journal-title":"Toxins"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1501","DOI":"10.1021\/bi3013017","article-title":"Structural Basis for Activation of Voltage-Gated Cation Channels","volume":"52","author":"Stock","year":"2013","journal-title":"Biochemistry"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1007\/s00424-020-02424-y","article-title":"Ion channelopathies to bridge molecular lesions, channel function, and clinical therapies","volume":"472","author":"Carbone","year":"2020","journal-title":"Pflugers Arch."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1007\/978-1-4939-2845-3_1","article-title":"Introduction: Applying Chemical Biology to Ion Channels","volume":"869","author":"Pless","year":"2015","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Zhao, Y., Chen, Z., Cao, Z., Li, W., and Wu, Y. (2019). Diverse Structural Features of Potassium Channels Characterized by Scorpion Toxins as Molecular Probes. Molecules, 24.","DOI":"10.3390\/molecules24112045"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"581","DOI":"10.2174\/1568026615666150217110710","article-title":"Organic toxins as tools to understand ion channel mechanisms and structure","volume":"15","author":"Rosenbaum","year":"2015","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Van Theemsche, K.M., Van de Sande, D.V., Snyders, D.J., and Labro, A.J. (2020). Hydrophobic Drug\/Toxin Binding Sites in Voltage-Dependent K+ and Na+ Channels. Front. Pharmacol., 11, Available online: https:\/\/www.frontiersin.org\/articles\/10.3389\/fphar.2020.00735\/full.","DOI":"10.3389\/fphar.2020.00735"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"587","DOI":"10.1085\/jgp.201210873","article-title":"An emerging consensus on voltage-dependent gating from computational modeling and molecular dynamics simulations","volume":"140","author":"Vargas","year":"2012","journal-title":"J. Gen. Physiol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1124\/mol.114.097659","article-title":"Structural Basis for Pharmacology of Voltage-Gated Sodium and Calcium Channels","volume":"88","author":"Catterall","year":"2015","journal-title":"Mol. Pharmacol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1007\/s00726-022-03188-8","article-title":"A mutation in the S6 segment of the KvAP channel changes the secondary structure and alters ion channel activity in a lipid bilayer membrane","volume":"54","author":"Malik","year":"2022","journal-title":"Amino Acids"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"323","DOI":"10.1038\/nrm2376","article-title":"How membrane proteins sense voltage","volume":"9","author":"Bezanilla","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"166","DOI":"10.3389\/fphar.2012.00166","article-title":"Mechanism of Electromechanical Coupling in Voltage-Gated Potassium Channels","volume":"3","author":"Blunck","year":"2012","journal-title":"Front. Pharmacol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.1007\/s11064-017-2314-9","article-title":"Forty Years of Sodium Channels: Structure, Function, Pharmacology, and Epilepsy","volume":"42","author":"Catterall","year":"2017","journal-title":"Neurochem. Res."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"3677","DOI":"10.1007\/s00018-015-1948-5","article-title":"Structure of potassium channels","volume":"72","author":"Kuang","year":"2015","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1038\/nrn727","article-title":"Potassium channel structures","volume":"3","author":"Choe","year":"2002","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"10910","DOI":"10.1073\/pnas.89.22.10910","article-title":"A cluster of hydrophobic amino acid residues required for fast Na(+)-channel inactivation","volume":"89","author":"West","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1126\/science.2122519","article-title":"Biophysical and Molecular Mechanisms of Shaker Potassium Channel Inactivation","volume":"250","author":"Hoshi","year":"1990","journal-title":"Science"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pneurobio.2014.12.003","article-title":"Voltage-gated calcium channels: Determinants of channel function and modulation by inorganic cations","volume":"129","author":"Neumaier","year":"2015","journal-title":"Prog. Neurobiol."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1113\/jphysiol.2011.224204","article-title":"Voltage-gated sodium channels at 60: Structure, function and pathophysiology","volume":"590","author":"Catterall","year":"2012","journal-title":"J. Physiol."},{"key":"ref_62","doi-asserted-by":"crossref","unstructured":"Capera, J., Serrano-Novillo, C., Navarro-Perez, M., Cassinelli, S., and Felipe, A. (2019). The Potassium Channel Odyssey: Mechanisms of Traffic and Membrane Arrangement. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20030734"},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1186\/s13073-020-00725-6","article-title":"Gene family information facilitates variant interpretation and identification of disease-associated genes in neurodevelopmental disorders","volume":"12","author":"Lal","year":"2020","journal-title":"Genome Med."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1007\/164_2017_43","article-title":"Cardiac Arrhythmias Related to Sodium Channel Dysfunction","volume":"246","author":"Argenziano","year":"2017","journal-title":"Handb. Exp. Pharmacol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"166967","DOI":"10.1016\/j.jmb.2021.166967","article-title":"Structural Pharmacology of Voltage-Gated Sodium Channels","volume":"433","author":"Noreng","year":"2021","journal-title":"J. Mol. Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1080\/19336950.2019.1649521","article-title":"Role of the voltage sensor module in Nav domain IV on fast inactivation in sodium channelopathies: The implication of closed-state inactivation","volume":"13","author":"Nakajima","year":"2019","journal-title":"Channels"},{"key":"ref_67","doi-asserted-by":"crossref","unstructured":"D\u00edaz-Garc\u00eda, A., and Varela, D. (2020). Voltage-Gated K+\/Na+ Channels and Scorpion Venom Toxins in Cancer. Front. Pharmacol.","DOI":"10.3389\/fphar.2020.00913"},{"key":"ref_68","first-page":"1764","article-title":"Diversity of Potassium Channel Ligands: Focus on Scorpion Toxins","volume":"80","author":"Kuzmenkov","year":"2015","journal-title":"Biochemistry"},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1152\/physrev.00021.2009","article-title":"Inwardly Rectifying Potassium Channels: Their Structure, Function, and Physiological Roles","volume":"90","author":"Hibino","year":"2010","journal-title":"Physiol. Rev."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1124\/pr.57.4.12","article-title":"International Union of Pharmacology. LV. Nomenclature and Molecular Relationships of Two-P Potassium Channels","volume":"57","author":"Goldstein","year":"2005","journal-title":"Pharmacol. Rev."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1124\/pr.57.4.9","article-title":"International Union of Pharmacology. LII. Nomenclature and Molecular Relationships of Calcium-Activated Potassium Channels","volume":"57","author":"Wei","year":"2005","journal-title":"Pharmacol. Rev."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"921","DOI":"10.1038\/nrn1992","article-title":"High-conductance potassium channels of the SLO family","volume":"7","author":"Salkoff","year":"2006","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1016\/j.toxicon.2014.11.233","article-title":"Scorpion venom components as potential candidates for drug development","volume":"93","author":"Ortiz","year":"2015","journal-title":"Toxicon"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"3874","DOI":"10.19102\/icrm.2019.101006","article-title":"Roles and Regulation of Voltage-gated Calcium Channels in Arrhythmias","volume":"10","author":"Kushner","year":"2019","journal-title":"J. Innov. Card. Rhythm Manag."},{"key":"ref_75","unstructured":"Antal, L., and Cancers, M.M.-C. (2022, August 18). 2019 Undefined. T-Type Calcium Channels in Cancer. Available online: https:\/\/www.mdpi.com\/400524."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"466","DOI":"10.1016\/j.neuron.2018.03.017","article-title":"Calcium Channels, Synaptic Plasticity, and Neuropsychiatric Disease","volume":"98","author":"Nanou","year":"2018","journal-title":"Neuron."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1038\/nrd.2015.5","article-title":"Targeting voltage-gated calcium channels in neurological and psychiatric diseases","volume":"15","author":"Zamponi","year":"2015","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.cellbio.16.1.521","article-title":"Structure and Regulation of Voltage-Gated Ca2+ Channels","volume":"16","author":"Catterall","year":"2000","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"213","DOI":"10.3389\/fnmol.2018.00213","article-title":"New Insights Into Interactions of Presynaptic Calcium Channel Subtypes and SNARE Proteins in Neurotransmitter Release","volume":"11","author":"He","year":"2018","journal-title":"Front. Mol. Neurosci."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"811","DOI":"10.1007\/s00424-020-02395-0","article-title":"Cav2.3 R-type calcium channels: From its discovery to pathogenic de novo CACNA1E variants: A historical perspective","volume":"472","author":"Schneider","year":"2020","journal-title":"Pflugers Arch."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1152\/physrev.00047.2017","article-title":"CLC Chloride Channels and Transporters: Structure, Function, Physiology, and Disease","volume":"98","author":"Jentsch","year":"2018","journal-title":"Physiol. Rev."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"96","DOI":"10.3389\/fphys.2020.00096","article-title":"Intracellular Chloride Channels: Novel Biomarkers in Diseases","volume":"11","author":"Patel","year":"2020","journal-title":"Front. Physiol. Front. Media SA"},{"key":"ref_83","unstructured":"(2022, June 27). Polipept\u00eddeos de Toxina de Escorpi\u00e3o Como Agentes Terap\u00eauticos: Uma Vis\u00e3o Geral: Ingenta Connect [Internet]. Available online: https:\/\/www.ingentaconnect.com\/content\/ben\/ppl\/2016\/00000023\/00000009\/art00013."},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1038\/nature20812","article-title":"Structure of a CLC chloride ion channel by cryo-electron microscopy","volume":"541","author":"Park","year":"2016","journal-title":"Nature"},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1126\/science.1195230","article-title":"Structure of a Eukaryotic CLC Transporter Defines an Intermediate State in the Transport Cycle","volume":"330","author":"Feng","year":"2010","journal-title":"Science"},{"key":"ref_86","first-page":"328","article-title":"Lysosomal pathology and osteopetrosis upon loss of H+-driven lysosomal Cl- accumulation","volume":"2010","author":"Weinert","year":"1979","journal-title":"Science"},{"key":"ref_87","doi-asserted-by":"crossref","unstructured":"Van Slegtenhorst, M.A., Tbassl, M., Borsanil, G., Wapenaar, M.C., Ferrero, G.B., de Concillls, L., Rugarli, E.I., Grillo, A., Franco, B., and Zoghbl, H. (1994). A gene from the Xp22.3 region shares homology with voltage-gated chloride channels. Hum Mol Genet., 3.","DOI":"10.1093\/hmg\/3.4.547"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"13854","DOI":"10.1073\/pnas.0606137103","article-title":"Lysosomal storage disease upon disruption of the neuronal chloride transport protein ClC-6","volume":"103","author":"Kornak","year":"2006","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"4056","DOI":"10.1096\/fj.09-130880","article-title":"Lysosomal degradation of endocytosed proteins depends on the chloride transport protein ClC-7","volume":"23","author":"Wartosch","year":"2009","journal-title":"FASEB J."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3389\/fcell.2021.639231","article-title":"Neurodegeneration Upon Dysfunction of Endosomal\/Lysosomal CLC Chloride Transporters","volume":"9","author":"Bose","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"e27739","DOI":"10.1097\/MD.0000000000027739","article-title":"Identification of chloride intracellular channels as prognostic factors correlated with immune infiltration in hepatocellular carcinoma using bioinformatics analysis","volume":"100","author":"Huang","year":"2021","journal-title":"Medicine"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"2093","DOI":"10.1016\/j.febslet.2010.01.027","article-title":"The enigma of the CLIC proteins: Ion channels, redox proteins, enzymes, scaffolding proteins?","volume":"584","author":"Littler","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1038\/s41586-020-2933-1","article-title":"Discoveries in structure and physiology of mechanically activated ion channels","volume":"587","author":"Kefauver","year":"2020","journal-title":"Nature"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Startek, J.B., Boonen, B., Talavera, K., and Meseguer, V. (2019). TRP Channels as Sensors of Chemically-Induced Changes in Cell Membrane Mechanical Properties. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20020371"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"218","DOI":"10.1186\/gb-2011-12-3-218","article-title":"The transient receptor potential family of ion channels","volume":"12","author":"Nilius","year":"2011","journal-title":"Genome Biol."},{"key":"ref_96","unstructured":"(2022, June 24). Physiology, Nociception\u2014StatPearls\u2014NCBI Bookshelf [Internet], Available online: https:\/\/www.ncbi.nlm.nih.gov\/books\/NBK551562\/."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1016\/j.neuron.2019.11.023","article-title":"Structural Insights into Electrophile Irritant Sensing by the Human TRPA1 Channel","volume":"105","author":"Suo","year":"2019","journal-title":"Neuron"},{"key":"ref_98","unstructured":"(2022, June 28). PDF Neurotoxinas escorpi\u00f4nicas) que revisam sobre os canais i\u00f4nicos: Uma bibliografia [Internet]. Available online: https:\/\/www.researchgate.net\/publication\/331043699_Neurotoxinas_escorpionicas_que_atuam_sobre_canais_ionicos_uma_revisao_bibliografica."},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Beraldo Neto, E., de Freitas, L.A., Pimenta, D.C., Lebrun, I., and Nencioni, A.L.A. (2020). Tb1, a Neurotoxin from Tityus bahiensis Scorpion Venom, Induces Epileptic Seizures by Increasing Glutamate Release. Toxins, 12.","DOI":"10.3390\/toxins12020065"},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/S0300-9084(00)01174-3","article-title":"Molecular mechanisms of neurotoxin action on voltage-gated sodium channels","volume":"82","author":"Catterall","year":"2000","journal-title":"Biochimie"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.jmb.2014.07.027","article-title":"From Foe to Friend: Using Animal Toxins to Investigate Ion Channel Function","volume":"427","author":"Kalia","year":"2015","journal-title":"J. Mol. Biol."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/j.toxicon.2006.09.016","article-title":"Novel paradigms on scorpion toxins that affects the activating mechanism of sodium channels","volume":"49","author":"Possani","year":"2007","journal-title":"Toxicon."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"14136","DOI":"10.1074\/jbc.M111.315382","article-title":"Structural Insights into Antibody Sequestering and Neutralizing of Na+ Channel \u03b1-Type Modulator from Old World Scorpion Venom","volume":"287","author":"Fabrichny","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"165","DOI":"10.2147\/DDDT.S24754","article-title":"Emerging options for the management of scorpion stings","volume":"6","author":"Chippaux","year":"2012","journal-title":"Drug Des. Dev. Ther."},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Nencioni, A.L.A., Neto, E.B., de Freitas, L.A., and Dorce, V.A.C. (2018). Effects of Brazilian scorpion venoms on the central nervous system. Centro de Estudos de Venenos e Animais Pe\u00e7onhentos (CEVAP\/UNESP). J. Venom. Anim. Toxins Incl. Trop. Dis., 24, Available online: http:\/\/www.scielo.br\/j\/jvatitd\/a\/j3xFRs78jbh7rQ43NNg4bfK\/?lang=en.","DOI":"10.1186\/s40409-018-0139-x"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"100126","DOI":"10.1016\/j.toxcx.2022.100126","article-title":"Dopaminergic metabolism is affected by intracerebral injection of Tb II-I isolated from Tityus bahiensis scorpion venom","volume":"15","author":"Lebrun","year":"2022","journal-title":"Toxicon X"},{"key":"ref_107","first-page":"67","article-title":"Scorpion venomics: A 2019 overview","volume":"17","author":"Ortiz","year":"2019","journal-title":"Expert Rev. Proteom."},{"key":"ref_108","first-page":"483","article-title":"Disulfide Bonds of Toxin II of the Scorpion Androctonus australis Hector","volume":"47","author":"Kopeyan","year":"1974","journal-title":"JBIC J. Biol. Inorg. Chem."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1111\/j.1399-3011.1982.tb00897.x","article-title":"Covalent structure of the insect toxin of the North African scorpion Androctonus australis Hector","volume":"20","author":"Darbon","year":"2009","journal-title":"Int. J. Pept. Protein Res."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.toxicon.2012.03.022","article-title":"Mapping of scorpion toxin receptor sites at voltage-gated sodium channels","volume":"60","author":"Gurevitz","year":"2012","journal-title":"Toxicon"},{"key":"ref_111","doi-asserted-by":"crossref","unstructured":"Martin-Eauclaire, M.-F., Adi-Bessalem, S., Hammoudi-Triki, D., Laraba-Djebari, F., and Bougis, P.E. (2019). Serotherapy against Voltage-Gated Sodium Channel-Targeting \u03b1-Toxins from Androctonus Scorpion Venom. Toxins, 11.","DOI":"10.3390\/toxins11020063"},{"key":"ref_112","doi-asserted-by":"crossref","unstructured":"Bowman, A., Fitzgerald, C., Pummill, J.F., Rhoads, D.D., and Yamashita, T. (2021). Reduced toxicity of centruroides vittatus (Say, 1821) may result from lowered sodium \u03b2 toxin gene expression and toxin protein production. Toxins, 13.","DOI":"10.3390\/toxins13110828"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"108939","DOI":"10.1016\/j.cbpc.2020.108939","article-title":"Centruroides margaritatus scorpion complete venom exerts cardiovascular effects through alpha-1 adrenergic receptors","volume":"240","author":"Cupitra","year":"2021","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"264","DOI":"10.1016\/j.actatropica.2018.08.002","article-title":"North American scorpion species of public health importance with a reappraisal of historical epidemiology","volume":"187","author":"Possani","year":"2018","journal-title":"Acta Trop."},{"key":"ref_115","doi-asserted-by":"crossref","unstructured":"Rowe, A.H., Xiao, Y., Scales, J., Linse, K.D., Rowe, M.P., Cummins, T.R., and Zakon, H.H. (2011). Isolation and Characterization of CvIV4: A Pain Inducing \u03b1- Scorpion Toxin. PLoS ONE, 6.","DOI":"10.1371\/journal.pone.0023520"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1085\/jgp.200609719","article-title":"\u03b2-Scorpion Toxin Modifies Gating Transitions in All Four Voltage Sensors of the Sodium Channel","volume":"130","author":"Campos","year":"2007","journal-title":"J. Gen. Physiol."},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1007\/BF02257372","article-title":"Classification of scorpion toxins according to amino acid composition and sequence","volume":"20","author":"Dufton","year":"1984","journal-title":"J. Mol. Evol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"920","DOI":"10.2174\/092986609788923329","article-title":"Tityus serrulatus scorpion venom and toxins: An overview","volume":"16","author":"Cologna","year":"2009","journal-title":"Protein Pept. Lett."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1085\/jgp.201110720","article-title":"Scorpion \u03b2-toxin interference with NaV channel voltage sensor gives rise to excitatory and depressant modes","volume":"139","author":"Leipold","year":"2012","journal-title":"J. Gen. Physiol."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/0014-5793(92)80445-M","article-title":"Molecular cloning and nucleotide sequence analysis of a cDNA encoding the main \u03b2-neurotoxin from the venom of the South American scorpion Tityus serrulatus","volume":"302","author":"Ribeiro","year":"1992","journal-title":"FEBS Lett."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.cca.2005.05.012","article-title":"Effects of voltage-gated Na+ channel toxins from Tityus serrulatus venom on rat arterial blood pressure and plasma catecholamines","volume":"141","author":"Vasconcelos","year":"2005","journal-title":"Comp. Biochem. Physiol. Part C Toxicol. Pharmacol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.tips.2004.03.010","article-title":"K+ channels as targets for specific immunomodulation","volume":"25","author":"Chandy","year":"2004","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"5194","DOI":"10.3390\/toxins7124877","article-title":"Computational Studies of Venom Peptides Targeting Potassium Channels","volume":"7","author":"Chen","year":"2015","journal-title":"Toxins"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"107504","DOI":"10.1016\/j.jmgm.2019.107504","article-title":"Elucidation of interaction mechanism of hERG1 potassium channel with scorpion toxins BeKm-1 and BmTx3b","volume":"96","author":"Gunay","year":"2019","journal-title":"J. Mol. Graph. Model."},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"12185","DOI":"10.1073\/pnas.89.24.12185","article-title":"Scorpion toxins targeted against the sarcoplasmic reticulum Ca(2+)-release channel of skeletal and cardiac muscle","volume":"89","author":"Valdivia","year":"1992","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_126","unstructured":"Cooper, D., and Dimri, M. (2022). Biochemistry, Calcium Channels, StatPearls\u2014United States Publisher."},{"key":"ref_127","doi-asserted-by":"crossref","unstructured":"Ahmadi, S., Knerr, J.M., Argemi, L., Bordon, K.C.F., Pucca, M.B., and Cerni, F.A. (2020). Scorpion Venom: Detriments and Benefits. Biomedicines, 8, Available online: https:\/\/www.mdpi.com\/2227-9059\/8\/5\/118\/pdf?version=1590651923.","DOI":"10.3390\/biomedicines8050118"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"14739","DOI":"10.1038\/s41598-018-33133-3","article-title":"CPP-Ts: A new intracellular calcium channel modulator and a promising tool for drug delivery in cancer cells","volume":"8","author":"Horta","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"386384","DOI":"10.1155\/2011\/386384","article-title":"Both basic and acidic amino acid residues of IpTx(a) are involved in triggering substate of RyR1","volume":"2011","author":"Seo","year":"2011","journal-title":"J. Biomed. Biotechnol."},{"key":"ref_130","doi-asserted-by":"crossref","unstructured":"Moslah, W., Aissaoui-Zid, D., Aboudou, S., Abdelkafi-Koubaa, Z., Potier-Cartereau, M., Lemettre, A., Elbini-Dhouib, I., Marrakchi, N., Gigmes, D., and Vandier, C. (2022). Strengthening Anti-Glioblastoma Effect by Multi-Branched Dendrimers Design of a Scorpion Venom Tetrapeptide. Molecules, 27.","DOI":"10.3390\/molecules27030806"},{"key":"ref_131","unstructured":"Striessnig, J. (2022, June 06). NO-C Molecular, 2015 Undefined. Pharmacology of L-Type Calcium Channels: Novel Drugs for Old Targets? ingentaconnect.com [Internet]. Available online: https:\/\/www.ingentaconnect.com\/content\/ben\/cmp\/2015\/00000008\/00000002\/art00003."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.crstbi.2021.07.003","article-title":"Structural basis for the binding of the cancer targeting scorpion toxin, ClTx, to the vascular endothelia growth factor receptor neuropilin-1","volume":"3","author":"Sharma","year":"2021","journal-title":"Curr. Res. Struct. Biol."},{"key":"ref_133","unstructured":"Amalia Due\u00f1as-Cuellar, R., Jos\u00e9 Correia Santana, C., Carolina Martins Magalh\u00e3es, A., Rodrigues Pires, O., Fontes, W., and Castro, M.S. (2022, June 05). Scorpion toxins and ion channels: Potential applications in cancer therapy. Available online: https:\/\/www.mdpi.com\/716776."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"1079","DOI":"10.3390\/toxins7041079","article-title":"Clorotoxina: Um pept\u00eddeo de escorpi\u00e3o natural \u00fatil para diagnosticar glioma e combater a invas\u00e3o de tumores","volume":"7","author":"Dardevet","year":"2015","journal-title":"Toxins"},{"key":"ref_135","first-page":"128","article-title":"Repeated Administration of Vanilloid Receptor TRPV1 Antagonists Attenuates Hyperthermia Elicited by TRPV1 Blockade","volume":"323","author":"Gavva","year":"2007","journal-title":"Experiment"},{"key":"ref_136","doi-asserted-by":"crossref","unstructured":"Jami, S., Erickson, A., and Brierley, S. (2022, June 05). Toxins IV-, 2017 Undefined. Pain-Causing Venom Peptides: Insights into Sensory Neuron Pharmacology. Available online: https:\/\/www.mdpi.com\/249068.","DOI":"10.3390\/toxins10010015"},{"key":"ref_137","doi-asserted-by":"crossref","unstructured":"Geron, M., Hazan, A., and Priel, A. (2017). Animal Toxins Providing Insights into TRPV1 Activation Mechanism. Toxins, 9, Available online: https:\/\/www.mdpi.com\/2072-6651\/9\/10\/326\/htm.","DOI":"10.3390\/toxins9100326"},{"key":"ref_138","doi-asserted-by":"crossref","unstructured":"Hwang, S.-M., Jo, Y.-Y., Cohen, C.F., Kim, Y.-H., Berta, T., and Park, C.-K. (2022). Venom Peptide Toxins Targeting the Outer Pore Region of Transient Receptor Potential Vanilloid 1 in Pain: Implications for Analgesic Drug Development. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23105772"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"848","DOI":"10.2174\/1389201019666181105160744","article-title":"Scorpion Toxins Targeting Voltage-gated Sodium Channels Associated with Pain","volume":"19","author":"Xu","year":"2018","journal-title":"Curr. Pharm. Biotechnol."},{"key":"ref_140","unstructured":"Wang, X., Zhang, S., Zhu, Y., and Zhang, Z. (2022, August 16). MS-M, 2020 undefined. Scorpion Toxins from Buthus martensii Karsch (BmK) as Potential Therapeutic Agents for Neurological Disorders: State of the Art and Beyond. Available online: https:\/\/books.google.com.br\/books?hl=pt-BR&lr=&id=4mwtEAAAQBAJ&oi=fnd&pg=PA133&dq=Scorpion+Toxins+from+Buthus+martensii+Karsch+(BmK)+as+Potential+Therapeutic+Agents+for+Neurological+Disorders:+State+of+the+Art+and+Beyond&ots=zyM9Qn9bM7&sig=ZAQ-c9Wr3wMcoV_hJbazsaNGgBw."},{"key":"ref_141","unstructured":"Dehghan, Z., Ayat, H., and Ahadi, A.M. (2022, August 16). Pharmaceutical AA-IJ of, 2020 undefined. Expression, purification and docking studies on IMe-AGAP, the first antitumor-analgesic like peptide from Iranian Scorpion, Available online: https:\/\/www.ncbi.nlm.nih.gov\/pmc\/articles\/PMC7757975\/."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"110809","DOI":"10.1016\/j.mehy.2022.110809","article-title":"Therapeutic potential of viral vectors that express venom peptides for neurological diseases","volume":"161","author":"Okada","year":"2022","journal-title":"Med. Hypotheses"},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"Deng, S.-Q., Chen, J.-T., Li, W.-W., Chen, M., and Peng, H.-J. (2019). Application of the Scorpion Neurotoxin AaIT against Insect Pests. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20143467"},{"key":"ref_144","doi-asserted-by":"crossref","unstructured":"Zlotkin, E. (2005). Scorpion Venoms. Comprehensive Molecular Insect Science, Elsevier.","DOI":"10.1016\/B0-44-451924-6\/00089-2"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/j.toxicon.2018.11.298","article-title":"Versatile spider venom peptides and their medical and agricultural applications","volume":"158","author":"Saez","year":"2018","journal-title":"Toxicon"},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"3663","DOI":"10.1002\/ps.6396","article-title":"Selective actions of insecticides on desensitizing and non-desensitizing nicotinic acetylcholine receptors in cockroach (Periplaneta americana) neurons","volume":"77","author":"Salgado","year":"2021","journal-title":"Pest Manag. Sci."},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"1237","DOI":"10.1007\/s00726-017-2425-2","article-title":"An insecticidal toxin from Nephila clavata spider venom","volume":"49","author":"Jin","year":"2017","journal-title":"Amino Acids"},{"key":"ref_148","first-page":"692","article-title":"Successful refolding and NMR structure of rMagi3: A disulfide-rich insecticidal spider toxin","volume":"27","author":"Carrillo","year":"2017","journal-title":"Protein Sci."},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"125","DOI":"10.20884\/1.jm.2021.16.2.715","article-title":"Computational Study of Scorpion Venom (Lychas Mucronatus) Activity as Antimicrobial Peptides (AMPs) to the SARS-CoV-2 Main Protease for the Future Coronavirus Disease (COVID-19) Inhibitors","volume":"16","author":"Fakih","year":"2021","journal-title":"Molekul"}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/15\/4\/238\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:02:11Z","timestamp":1760122931000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/15\/4\/238"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,3,24]]},"references-count":149,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2023,4]]}},"alternative-id":["toxins15040238"],"URL":"https:\/\/doi.org\/10.3390\/toxins15040238","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,3,24]]}}}