{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,11]],"date-time":"2026-09-11T04:57:04Z","timestamp":1789102624698,"version":"build-2803163510"},"reference-count":355,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T00:00:00Z","timestamp":1782777600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100009526","name":"Amrita Vishwa Vidyapeetham","doi-asserted-by":"crossref","id":[{"id":"10.13039\/100009526","id-type":"DOI","asserted-by":"crossref"}]},{"id":[{"id":"https:\/\/ror.org\/03am10p12","id-type":"ROR","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Animal venoms are complex biochemical systems composed of proteins, peptides, and small molecules with bioactivity. Traditionally regarded as toxic agents, venom components are increasingly recognized as valuable molecular libraries that can modulate cellular processes in human disease pathophysiology. This review highlights the translational potential of venom-derived molecules, with emphasis on clinically approved venom-derived drugs such as captopril, while also discussing their therapeutic potential for diseases such as cancer, autoimmunity, cardiovascular diseases, chronic pain, neuropsychiatric disorders, and infectious diseases. Special emphasis is given to the mechanisms by which these toxins modulate ion channels, enzymes, and receptor systems. Recent advances in venomics, harnessing proteomics, transcriptomics, and high-throughput screening, are also discussed, which can accelerate the clinical translation of venom-derived therapeutics. Key challenges related to assessing the immunogenicity of the venom-derived compounds, bioavailability, and safety have also been addressed alongside emerging strategies to overcome them. Collectively, these advances can provide a logical framework for developing novel therapeutics, bridging the gap between toxinology and drug discovery.<\/jats:p>","DOI":"10.3390\/toxins18070286","type":"journal-article","created":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T16:56:55Z","timestamp":1782838615000},"page":"286","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["Animal Venoms Targeting Cellular Mechanisms: Advances and Implications for Drug Discovery and Disease Therapy"],"prefix":"10.3390","volume":"18","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-1018-129X","authenticated-orcid":false,"given":"Lucienne","family":"Mathai","sequence":"first","affiliation":[{"name":"School of Biotechnology, Amrita Vishwa Vidyapeetham, Amritapuri, Kollam 690525, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bipin G.","family":"Nair","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Amrita Vishwa Vidyapeetham, Amritapuri, Kollam 690525, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4370-8183","authenticated-orcid":false,"given":"Aswathy","family":"Alangode","sequence":"additional","affiliation":[{"name":"School of Biotechnology, Amrita Vishwa Vidyapeetham, Amritapuri, Kollam 690525, India"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2026,6,30]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Schendel, V., Rash, L.D., Jenner, R.A., and Undheim, E.A.B. (2019). The Diversity of Venom: The Importance of Behavior and Venom System Morphology in Understanding Its Ecology and Evolution. Toxins, 11.","DOI":"10.3390\/toxins11110666"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"2777","DOI":"10.1093\/molbev\/msaa133","article-title":"Venom Systems as Models for Studying the Origin and Regulation of Evolutionary Novelties","volume":"37","author":"Zancolli","year":"2020","journal-title":"Mol. Biol. Evol."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Utkin, Y. (2024). Animal Venoms and Their Components: Molecular Mechanisms of Action V 2.0. Toxins, 16.","DOI":"10.3390\/toxins16110461"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"102227","DOI":"10.1016\/j.toxrep.2026.102227","article-title":"The Venom Revolution in Biomedicine: Unlocking Nature\u2019s Toxin Toolkit for Therapeutic Innovation","volume":"16","author":"Bose","year":"2026","journal-title":"Toxicol. Rep."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"giac048","DOI":"10.1093\/gigascience\/giac048","article-title":"Modern Venomics-Current Insights, Novel Methods, and Future Perspectives in Biological and Applied Animal Venom Research","volume":"11","author":"Anderluh","year":"2022","journal-title":"GigaScience"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Kim, E., Hwang, D.H., Mohan Prakash, R.L., Asirvatham, R.D., Lee, H., Heo, Y., Munawir, A., Seyedian, R., and Kang, C. (2025). Animal Venom in Modern Medicine: A Review of Therapeutic Applications. Toxins, 17.","DOI":"10.3390\/toxins17080371"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"de Souza, J.M., Goncalves, B.D.C., Gomez, M.V., Vieira, L.B., and Ribeiro, F.M. (2018). Animal Toxins as Therapeutic Tools to Treat Neurodegenerative Diseases. Front. Pharmacol., 9.","DOI":"10.3389\/fphar.2018.00145"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"322","DOI":"10.2174\/187152811797200696","article-title":"Therapeutic Potential of Peptide Toxins That Target Ion Channels","volume":"10","author":"Beraud","year":"2011","journal-title":"Inflamm. Allergy Drug Targets"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1038\/nrd1197","article-title":"Therapeutic Potential of Venom Peptides","volume":"2","author":"Lewis","year":"2003","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Rubio, D.C.Z., Arag\u00f3n, D.M., and Alves, I.A. (2025). Innovations in Snake Venom-Derived Therapeutics: A Systematic Review of Global Patents and Their Pharmacological Applications. Toxins, 17.","DOI":"10.3390\/toxins17030136"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Chow, C.Y., and King, G.F. (2024). Shining a Light on Venom-Peptide Receptors: Venom Peptides as Targeted Agents for In Vivo Molecular Imaging. Toxins, 16.","DOI":"10.3390\/toxins16070307"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1111\/j.1745-7254.2006.00293.x","article-title":"A long-form alpha-neurotoxin from cobra venom produces potent opioid-independent analgesia1","volume":"27","author":"Chen","year":"2006","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"124357","DOI":"10.1016\/j.ijbiomac.2023.124357","article-title":"Therapeutic applications of snake venoms: An invaluable potential of new drug candidates","volume":"238","author":"Caldeira","year":"2023","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Zambelli, V.O., Picolo, G., Fernandes, C.A.H., Fontes, M.R.M., and Cury, Y. (2017). Secreted Phospholipases A2 from Animal Venoms in Pain and Analgesia. Toxins, 9.","DOI":"10.3390\/toxins9120406"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.toxicon.2012.09.008","article-title":"Non-enzymatic proteins from snake venoms: A gold mine of pharmacological tools and drug leads","volume":"62","author":"McCleary","year":"2013","journal-title":"Toxicon"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"2602","DOI":"10.1038\/ncomms3602","article-title":"The genome of Mesobuthus martensii reveals a unique adaptation model of arthropods","volume":"4","author":"Cao","year":"2013","journal-title":"Nat. Commun."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.toxicon.2020.05.020","article-title":"Scorpion venom phospholipases A2: A minireview","volume":"184","author":"Krayem","year":"2020","journal-title":"Toxicon"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Wille, A.C.M., Machado, M.I., Souza, S.H., da Justa, H.C., de Fraga-Ferreira, M.E., Mello, E.d.S., Gremski, L.H., and Veiga, S.S. (2025). Brown Spider Venom Phospholipases D: From Potent Molecules Involved in Pathogenesis of Brown Spider Bites to Molecular Tools for Studying Ectosomes, Ectocytosis, and Its Applications. Toxins, 17.","DOI":"10.3390\/toxins17020070"},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Suranse, V., Srikanthan, A., and Sunagar, K. (2018). Animal Venoms: Origin, Diversity and Evolution. Encyclopedia of Life Sciences, Wiley.","DOI":"10.1002\/9780470015902.a0000939.pub2"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"2253","DOI":"10.1111\/brv.13120","article-title":"Prey specificity of predatory venoms","volume":"99","author":"King","year":"2024","journal-title":"Biol. Rev."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"5364","DOI":"10.1021\/acs.jmedchem.3c00097","article-title":"Catalytically Active Snake Venom PLA2 Enzymes: An Overview of Its Elusive Mechanisms of Reaction","volume":"66","author":"Soares","year":"2023","journal-title":"J. Med. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","unstructured":"Ranawaka, U.K., Lalloo, D.G., and De Silva, H.J. (2013). Neurotoxicity in Snakebite\u2014The Limits of Our Knowledge. PLoS Negl. Trop. Dis., 7.","DOI":"10.1371\/journal.pntd.0002302"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"101000","DOI":"10.1016\/j.jbior.2023.101000","article-title":"The wide world of non-mammalian phospholipase D enzymes","volume":"91","author":"Wang","year":"2023","journal-title":"Adv. Biol. Regul."},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Lajoie, D.M., Zobel-Thropp, P.A., Kumirov, V.K., Bandarian, V., Binford, G.J., and Cordes, M.H.J. (2013). Phospholipase D Toxins of Brown Spider Venom Convert Lysophosphatidylcholine and Sphingomyelin to Cyclic Phosphates. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0072372"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1186\/1678-9199-20-23","article-title":"Snake venom L-amino acid oxidases: An overview on their antitumor effects","volume":"20","author":"Costa","year":"2014","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/s41598-018-37435-4","article-title":"L-amino acid oxidase from Bothrops atrox snake venom triggers autophagy, apoptosis and necrosis in normal human keratinocytes","volume":"9","author":"Stransky","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"9323","DOI":"10.1007\/s00253-013-5230-1","article-title":"l-Amino acid oxidase as biocatalyst: A dream too far?","volume":"97","author":"Pollegioni","year":"2013","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1007\/s44371-025-00275-z","article-title":"Reactive oxygen species (ROS): Sources, generation, disease pathophysiology, and antioxidants","volume":"2","author":"Ansari","year":"2025","journal-title":"Discov. Chem."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.toxicon.2013.12.013","article-title":"Effect of l-amino acid oxidase from Calloselasma rhodosthoma snake venom on human neutrophils","volume":"80","author":"Pontes","year":"2014","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1002\/yea.1592","article-title":"Induction of apoptosis in yeast by L-amino acid oxidase from the Malayan pit viper Calloselasma rhodostoma","volume":"25","author":"Ande","year":"2008","journal-title":"Yeast"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Kini, R.M., and Koh, C.Y. (2016). Metalloproteases Affecting Blood Coagulation, Fibrinolysis and Platelet Aggregation from Snake Venoms: Definition and Nomenclature of Interaction Sites. Toxins, 8.","DOI":"10.3390\/toxins8100284"},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","article-title":"Snake Venom Metalloproteinases","volume":"62","author":"Markland","year":"2013","journal-title":"Toxicon"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"12912","DOI":"10.1038\/s41598-020-69396-y","article-title":"Cleavage of Proteoglycans, Plasma Proteins and the Platelet-Derived Growth Factor Receptor in the Hemorrhagic Process Induced by Snake Venom Metalloproteinases","volume":"10","author":"Asega","year":"2020","journal-title":"Sci. Rep."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.biochi.2019.03.022","article-title":"Biochemical and Molecular Characterization of the Hyaluronidase from Bothrops atrox Peruvian Snake Venom","volume":"162","author":"Delgadillo","year":"2019","journal-title":"Biochimie"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"6406","DOI":"10.1016\/j.matpr.2017.12.252","article-title":"A Biological Overview of Hyaluronidase: A Venom Enzyme and Its Inhibition with Plants Materials","volume":"5","author":"Bala","year":"2018","journal-title":"Mater. Today Proc."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"16689","DOI":"10.1074\/jbc.M112.350447","article-title":"Hyaluronidase 1 and \u03b2-Hexosaminidase Have Redundant Functions in Hyaluronan and Chondroitin Sulfate Degradation","volume":"287","author":"Gushulak","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1186\/s40409-015-0042-7","article-title":"Arthropod Venom Hyaluronidases: Biochemical Properties and Potential Applications in Medicine and Biotechnology","volume":"21","author":"Bordon","year":"2015","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"297","DOI":"10.5999\/aps.2020.00752","article-title":"Hyaluronidase: An Overview of Its Properties, Applications, and Side Effects","volume":"47","author":"Jung","year":"2020","journal-title":"Arch. Plast. Surg."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1186\/s43556-025-00299-y","article-title":"Hyaluronidase: Structure, Mechanism of Action, Diseases and Therapeutic Targets","volume":"6","author":"Lu","year":"2025","journal-title":"Mol. Biomed."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1007\/s41048-018-0067-x","article-title":"Animal Protein Toxins: Origins and Therapeutic Applications","volume":"4","author":"Chen","year":"2018","journal-title":"Biophys. Rep."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"126193","DOI":"10.1016\/j.ijpharm.2025.126193","article-title":"Targeting with toxins: An overview of venom peptides in drug delivery","volume":"685","author":"Mazurs","year":"2025","journal-title":"Int. J. Pharm."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Koh, C.Y., and Kini, R.M. (2025). Orphan Three-Finger Toxins from Snake Venoms: Unexplored Library of Novel Biological Ligands with Potential New Structures and Functions. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26188792"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"100090","DOI":"10.1016\/j.pharmr.2025.100090","article-title":"Recent Advances in the Pharmacology of Voltage-Gated Ion Channels","volume":"77","author":"Harris","year":"2025","journal-title":"Pharmacol. Rev."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"114168","DOI":"10.1016\/j.bcp.2020.114168","article-title":"Snake Three-Finger \u03b1-Neurotoxins and Nicotinic Acetylcholine Receptors: Molecules, Mechanisms and Medicine","volume":"181","author":"Nirthanan","year":"2020","journal-title":"Biochem. Pharmacol."},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Choudhury, M., and Das, M. (2025). Snake Venom Three-Finger Neurotoxins and Neurotoxin-Like Proteins: Insights Into Their Structural and Functional Aspects Along with Their Pharmacological Potential. Basic & Clinical Pharmacology & Toxicology, Wiley Online Library.","DOI":"10.1111\/bcpt.70144"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.3390\/toxins4111236","article-title":"Conotoxins Targeting Neuronal Voltage-Gated Sodium Channel Subtypes: Potential Analgesics?","volume":"4","author":"Knapp","year":"2012","journal-title":"Toxins"},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Li, R., Yu, J., Ye, D., Liu, S., Zhang, H., Lin, H., Feng, J., and Deng, K. (2025). Conotoxins: Classification, Prediction, and Future Directions in Bioinformatics. Toxins, 17.","DOI":"10.3390\/toxins17020078"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"e20230039","DOI":"10.1590\/1678-9199-jvatitd-2023-0039","article-title":"Snake Venom Disintegrins Update: Insights about New Findings","volume":"29","author":"Almeida","year":"2023","journal-title":"J. Venom. Anim. Incl. Toxins Trop. Dis."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"8316","DOI":"10.1038\/s41598-019-44767-2","article-title":"RGD-Independent Binding of Russell\u2019s Viper Venom Kunitz-Type Protease Inhibitors to Platelet GPIIb\/IIIa Receptor","volume":"9","author":"Kalita","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/S0146-0005(00)80046-4","article-title":"Angiotensin Converting Enzyme: History and Relevance","volume":"24","author":"Ferreira","year":"2000","journal-title":"Semin. Perinatol."},{"key":"ref_51","doi-asserted-by":"crossref","unstructured":"P\u00e9terfi, O., Boda, F., Szab\u00f3, Z., Ferencz, E., and B\u00e1ba, L. (2019). Hypotensive Snake Venom Components-A Mini-Review. Molecules, 24.","DOI":"10.3390\/molecules24152778"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"1285","DOI":"10.1056\/NEJM199810293391804","article-title":"Effect of Bradykinin-Receptor Blockade on the Response to Angiotensin-Converting-Enzyme Inhibitor in Normotensive and Hypertensive Subjects","volume":"339","author":"Gainer","year":"1998","journal-title":"N. Engl. J. Med."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"6635","DOI":"10.1021\/jp400974n","article-title":"Catalytic Mechanism of Angiotensin-Converting Enzyme and Effects of the Chloride Ion","volume":"117","author":"Zhang","year":"2013","journal-title":"J. Phys. Chem. B"},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"788","DOI":"10.1096\/fj.03-0093life","article-title":"The Discovery of Captopril","volume":"17","author":"Smith","year":"2003","journal-title":"FASEB J."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"919","DOI":"10.1038\/220919a0","article-title":"Conversion of Angiotensin I to Angiotensin II by Cell-Free Extracts of Dog Lung","volume":"220","author":"Bakhle","year":"1968","journal-title":"Nature"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1161\/01.HYP.17.4.589","article-title":"History of the Design of Captopril and Related Inhibitors of Angiotensin Converting Enzyme","volume":"17","author":"Cushman","year":"1991","journal-title":"Hypertension"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Gomez-Gutierrez, P., and Perez, J.J. (2025). Small Molecule Protease Inhibitors as Model Peptidomimetics. Pharmaceuticals, 18.","DOI":"10.3390\/ph18091377"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/S0021-9258(19)45746-3","article-title":"A Potent Reversible Inhibitor of Carboxypeptidase A","volume":"247","author":"Byers","year":"1972","journal-title":"J. Biol. Chem."},{"key":"ref_59","unstructured":"Lasker Foundation (1999). ACE Inhibitors for Treating Hypertension, Lasker Foundation."},{"key":"ref_60","doi-asserted-by":"crossref","unstructured":"Frangieh, J., Rima, M., Fajloun, Z., Henrion, D., Sabatier, J.-M., Legros, C., and Mattei, C. (2021). Snake Venom Components: Tools and Cures to Target Cardiovascular Diseases. Molecules, 26.","DOI":"10.3390\/molecules26082223"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/0033-0620(78)90024-5","article-title":"Captopril (SQ 14,225) (d-3-Mercapto-2-Methylpropanoyl-l-Proline): A Novel Orally Active Inhibitor of Angiotensin-Converting Enzyme and Antihypertensive Agent","volume":"21","author":"Rubin","year":"1978","journal-title":"Prog. Cardiovasc. Dis."},{"key":"ref_62","unstructured":"Davis, S. (2024). Captopril. xPharm: The Comprehensive Pharmacology Reference, Elsevier."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"2583","DOI":"10.1021\/bi00815a005","article-title":"Isolation of Bradykinin-Potentiating Peptides from Bothrops jararaca Venom","volume":"9","author":"Ferreira","year":"1970","journal-title":"Biochemistry"},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"C8","DOI":"10.1016\/0002-9149(92)90276-5","article-title":"Comparative Pharmacokinetics of Captopril, Enalapril, and Quinapril","volume":"69","author":"Vertes","year":"1992","journal-title":"Am. J. Cardiol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1517\/17425250903282773","article-title":"Quinaprilat: A Review of Its Pharmacokinetics, Pharmacodynamics, Toxicological Data and Clinical Application","volume":"5","author":"Kieback","year":"2009","journal-title":"Expert Opin. Drug Metab. Toxicol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"70","DOI":"10.2165\/00003495-198500301-00010","article-title":"Enalapril Maleate versus Captopril","volume":"30","author":"Ayers","year":"1985","journal-title":"Drugs"},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"339","DOI":"10.2165\/00003495-200262020-00009","article-title":"Quinapril: A Further Update of Its Pharmacology and Therapeutic Use in Cardiovascular Disorders","volume":"62","author":"Culy","year":"2002","journal-title":"Drugs"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1007\/s11864-024-01270-9","article-title":"Targeting the Renin-Angiotensin-Aldosterone System (RAAS) for Cardiovascular Protection and Enhanced Oncological Outcomes: Review","volume":"25","author":"Pawlonka","year":"2024","journal-title":"Curr. Treat. Options Oncol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1016\/j.yexcr.2012.02.023","article-title":"Recent Advances Involving the Renin\u2013Angiotensin System","volume":"318","author":"Crowley","year":"2012","journal-title":"Exp. Cell Res."},{"key":"ref_70","first-page":"47","article-title":"The Regulation of ACE-2 in the Heart and Lungs","volume":"9","author":"Kopel","year":"2021","journal-title":"Southwest Respir. Crit. Care Chron."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"R141","DOI":"10.1152\/ajpregu.1978.234.3.R141","article-title":"Angiotensin-Converting Enzyme in Developing Lung and Kidney","volume":"234","author":"Wallace","year":"1978","journal-title":"Am. J. Physiol. Integr. Comp. Physiol."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1056\/NEJMcibr022472","article-title":"Angiotensin-Converting Enzyme 2\u2014A New Cardiac Regulator","volume":"347","author":"Boehm","year":"2002","journal-title":"N. Engl. J. Med."},{"key":"ref_73","unstructured":"Fountain, J.H., Kaur, J., and Lappin, S.L. (2023). Physiology, Renin Angiotensin System, StatPearls."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1161\/HYPERTENSIONAHA.123.19419","article-title":"Hypertension Insights Into the Role of Angiotensin-II AT 1 Receptor-Dependent \u03b2-Arrestin Signaling in Cardiovascular Disease","volume":"81","author":"Mathieu","year":"2024","journal-title":"Hypertension"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1152\/physrev.00038.2017","article-title":"Angiotensin II Signal Transduction: An Update on Mechanisms of Physiology and Pathophysiology","volume":"98","author":"Forrester","year":"2018","journal-title":"Physiol. Rev."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1111\/nyas.12395","article-title":"New Insights into Insulin Action and Resistance in the Vasculature","volume":"1311","author":"Manrique","year":"2014","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_77","first-page":"47","article-title":"Angiotensin II augments renal vasoconstriction via AT1 receptors in L-NAME-induced hypertensive rats","volume":"52","year":"2009","journal-title":"Proc. West. Pharmacol. Soc."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1046\/j.1365-2249.2000.01323.x","article-title":"Angiotensin-Converting Enzyme Inhibitor Captopril Prevents Activation-Induced Apoptosis by Interfering with T Cell Activation Signals","volume":"121","author":"Odaka","year":"2000","journal-title":"Clin. Exp. Immunol."},{"key":"ref_79","doi-asserted-by":"crossref","unstructured":"Stoiljkovic, M., Jakovljevic, V., Milosavljevic, J., Bolevich, S., Jeremic, N., Canovic, P., Fisenko, V.P., Tikhonov, D.A., Krylova, I.N., and Bolevich, S. (2025). Cardioprotective Role of Captopril: From Basic to Applied Investigations. Int. J. Mol. Sci., 26.","DOI":"10.3390\/ijms26157215"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1411","DOI":"10.1161\/01.CIR.97.14.1411","article-title":"Angiotensin-Converting Enzyme Inhibitors","volume":"97","author":"Brown","year":"1998","journal-title":"Circulation"},{"key":"ref_81","doi-asserted-by":"crossref","unstructured":"Zheng, W., Tian, E., Liu, Z., Zhou, C., Yang, P., Tian, K., Liao, W., Li, J., and Ren, C. (2022). Small Molecule Angiotensin Converting Enzyme Inhibitors: A Medicinal Chemistry Perspective. Front. Pharmacol., 13.","DOI":"10.3389\/fphar.2022.968104"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1159\/000048057","article-title":"Alfimeprase: Pharmacology of a Novel Fibrinolytic Metalloproteinase for Thrombolysis","volume":"31","author":"Toombs","year":"2001","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1007\/978-1-62703-339-8_20","article-title":"Reptilase Time (RT)","volume":"Volume 992","author":"Karapetian","year":"2013","journal-title":"Haemostasis; Methods in Molecular"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"16862","DOI":"10.1074\/jbc.M113.464750","article-title":"Batroxobin Binds Fibrin with Higher Affinity and Promotes Clot Expansion to a Greater Extent than Thrombin","volume":"288","author":"Vu","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.jprot.2016.07.006","article-title":"Venomics of Calloselasma rhodostoma, the Malayan Pit Viper: A Complex Toxin Arsenal Unraveled","volume":"148","author":"Tang","year":"2016","journal-title":"J. Proteom."},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Chen, J.R., Xie, X.F., Zhang, H.Q., Li, G.M., Yin, Y.P., Cao, X.Y., Gao, Y.Q., Li, Y.N., Zhang, Y., and Peng, F. (2021). Pharmacological activities and mechanisms of hirudin and its derivatives\u2014A review. Front. Pharmacol., 12.","DOI":"10.3389\/fphar.2021.660757"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"2495","DOI":"10.22207\/JPAM.19.4.01","article-title":"Harnessing Snake Venom for Therapeutics: A Path from Toxins to Treatments","volume":"19","author":"Singh","year":"2025","journal-title":"J. Pure Appl. Microbiol."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"1361","DOI":"10.1517\/14712598.6.12.1361","article-title":"Alfimeprase: A Novel Recombinant Direct-Acting Fibrinolytic","volume":"6","author":"Deitcher","year":"2006","journal-title":"Expert Opin. Biol. Ther."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"3005","DOI":"10.1016\/j.jtha.2023.08.014","article-title":"Fibrinogen and Fibrin: Synthesis, Structure, and Function in Health and Disease","volume":"21","author":"Wolberg","year":"2023","journal-title":"J. Thromb. Haemost. JTH"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1177\/0003319717739720","article-title":"Raised Fibrinogen Levels and Outcome in Outpatients with Peripheral Artery Disease","volume":"69","author":"Altes","year":"2018","journal-title":"Angiology"},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"286","DOI":"10.1164\/rccm.201207-1232OC","article-title":"Elevated Fibrinogen Levels Are Associated with Risk of Pulmonary Embolism, but Not with Deep Venous Thrombosis","volume":"187","author":"Klovaite","year":"2013","journal-title":"Am. J. Respir. Crit. Care Med."},{"key":"ref_92","first-page":"317","article-title":"Plasma Fibrinogen Level May Predict Critical Coronary Artery Stenosis in Young Adults with Myocardial Infarction","volume":"16","author":"Tatli","year":"2009","journal-title":"Cardiol. J."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"870","DOI":"10.1002\/bjs.6632","article-title":"Haemostatic and Fibrinolytic Factors in Men with a Small Abdominal Aortic Aneurysm","volume":"96","author":"Parry","year":"2009","journal-title":"Br. J. Surg."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"3056","DOI":"10.1200\/JCO.2006.05.8438","article-title":"Phase II Trial of Alfimeprase, a Novel-Acting Fibrin Degradation Agent, for Occluded Central Venous Access Devices","volume":"24","author":"Moll","year":"2006","journal-title":"J. Clin. Oncol."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1517\/14712598.8.5.683","article-title":"Alfimeprase for the treatment of acute peripheral arterial occlusion","volume":"8","author":"Moise","year":"2008","journal-title":"Expert Opin. Biol. Ther."},{"key":"ref_96","doi-asserted-by":"crossref","unstructured":"(2008). Alfimeprase. Drugs RD, 9, 185\u2013190.","DOI":"10.2165\/00126839-200809030-00006"},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.jvs.2009.08.053","article-title":"Efficacy and Safety of Alfimeprase in Patients with Acute Peripheral Arterial Occlusion (PAO)","volume":"51","author":"Han","year":"2010","journal-title":"J. Vasc. Surg."},{"key":"ref_98","unstructured":"U.S. Food and Drug Administration (1983). Search Orphan Drug Designations and Approvals."},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/S0076-6879(76)45021-8","article-title":"[18] The Coagulant Enzyme from Bothrops atrox Venom (Batroxobin)","volume":"45","author":"Stocker","year":"1976","journal-title":"Methods Enzymol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"18","DOI":"10.2165\/00003495-199700543-00005","article-title":"Defibrinogenating Enzymes","volume":"54","author":"Bell","year":"1997","journal-title":"Drugs"},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1016\/j.febslet.2004.06.060","article-title":"Functional Characterization of Recombinant Batroxobin, a Snake Venom Thrombin-like Enzyme, Expressed from Pichia Pastoris","volume":"571","author":"You","year":"2004","journal-title":"FEBS Lett."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.thromres.2019.04.019","article-title":"Modulation of the mammalian coagulation system by venoms and other proteins from snakes, arthropods, nematodes and insects","volume":"178","author":"Sachetto","year":"2019","journal-title":"Thromb. Res."},{"key":"ref_103","doi-asserted-by":"crossref","unstructured":"Lan, D., Song, S., Liu, Y., Jiao, B., and Meng, R. (2021). Use of Batroxobin in Central and Peripheral Ischemic Vascular Diseases: A Systematic Review. Front. Neurol., 12.","DOI":"10.3389\/fneur.2021.716778"},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/B978-0-12-813726-0.00164-1","article-title":"Diagnostic Use of Venoms","volume":"167","author":"Francischetti","year":"2019","journal-title":"Transfus. Med. Hemost."},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"499","DOI":"10.5858\/2002-126-0499-LDOD","article-title":"Laboratory Diagnosis of Dysfibrinogenemia","volume":"126","author":"Cunningham","year":"2002","journal-title":"Arch. Pathol. Lab. Med."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"928","DOI":"10.1002\/ajh.21293","article-title":"Laboratory Testing for Fibrinogen Abnormalities","volume":"83","author":"Verhovsek","year":"2008","journal-title":"Am. J. Hematol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"829","DOI":"10.1007\/s40261-018-0673-x","article-title":"Coagulant Effect and Tolerability of Yeast-Produced Recombinant Batroxobin in Healthy Adult Subjects","volume":"38","author":"Choi","year":"2018","journal-title":"Clin. Drug Investig."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1037","DOI":"10.1007\/s12010-011-9192-4","article-title":"Co-Overexpression of PpPDI Enhances Secretion of Ancrod in Pichia Pastoris","volume":"164","author":"Zhang","year":"2011","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"1360","DOI":"10.1111\/j.1538-7836.2008.03057.x","article-title":"The Cut of the Clot(h): Snake Venom Fibrinogenases as Therapeutic Agents","volume":"6","author":"Gardiner","year":"2008","journal-title":"J. Thromb. Haemost."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/0049-3848(73)90024-8","article-title":"Fibrinogen and Its Derivatives in Relationship to Ancrod and Reptilase","volume":"2","author":"Kwaan","year":"1973","journal-title":"Thromb. Res."},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1111\/j.1365-2141.1993.tb08283.x","article-title":"The Fibrinolytic Response to Ancrod Therapy: Characterization of Fibrinogen and Fibrin Degradation Products","volume":"83","author":"Prentice","year":"1993","journal-title":"Br. J. Haematol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1871","DOI":"10.1016\/S0140-6736(06)69776-6","article-title":"Intravenous Ancrod for Acute Ischaemic Stroke in the European Stroke Treatment with Ancrod Trial: A Randomised Controlled Trial","volume":"368","author":"Hennerici","year":"2006","journal-title":"Lancet"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"3277","DOI":"10.1161\/STROKEAHA.111.622753","article-title":"Ancrod and Fibrin Formation: Perspectives on Mechanisms of Action","volume":"42","author":"Liu","year":"2011","journal-title":"Stroke"},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"112878","DOI":"10.1016\/j.biopha.2022.112878","article-title":"From Ancient Leech to Direct Thrombin Inhibitors and beyond: New from Old","volume":"149","author":"Montinari","year":"2022","journal-title":"Biomed. Pharmacother."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1055\/s-0037-1619549","article-title":"Bivalirudin, a Bivalent, Thrombin Specific Anticoagulant as an Alternative to Heparin in Interventional Procedures","volume":"22","author":"Chew","year":"2002","journal-title":"Hamostaseologie"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1517\/13543784.9.5.1119","article-title":"Bivalirudin: A New Generation Antithrombotic Drug","volume":"9","author":"Scatena","year":"2000","journal-title":"Expert Opin. Investig. Drugs"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.beha.2004.02.002","article-title":"Bivalent Direct Thrombin Inhibitors: Hirudin and Bivalirudin","volume":"17","author":"Warkentin","year":"2004","journal-title":"Best Pract. Res. Clin. Haematol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"296","DOI":"10.1051\/ject\/200537296","article-title":"Use of Bivalirudin as an Anticoagulant During Cardiopulmonary Bypass","volume":"37","author":"Veale","year":"2005","journal-title":"J. Extra Corpor. Technol."},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1586\/erc.11.131","article-title":"Desirudin: A Review of the Pharmacology and Clinical Application for the Prevention of Deep Vein Thrombosis","volume":"9","author":"Graetz","year":"2011","journal-title":"Expert Rev. Cardiovasc. Ther."},{"key":"ref_120","doi-asserted-by":"crossref","unstructured":"Chen, Y.C., Chang, Y.T., Chen, C.Y., Shiu, J.H., Cheng, C.H., Huang, C.H., Chen, J.F., and Chuang, W.J. (2020). Structural Insight into Integrin Recognition and Anticancer Activity of Echistatin. Toxins, 12.","DOI":"10.3390\/toxins12110709"},{"key":"ref_121","doi-asserted-by":"crossref","unstructured":"Lazarovici, P., Marcinkiewicz, C., and Lelkes, P.I. (2019). From Snake Venom\u2019s Disintegrins and C-Type Lectins to Anti-Platelet Drugs. Toxins, 11.","DOI":"10.3390\/toxins11050303"},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"136","DOI":"10.1111\/jebm.12253","article-title":"Efficacy and Safety of Eptifibatide versus Tirofiban in Acute Coronary Syndrome Patients: A Systematic Review and Meta-Analysis","volume":"10","author":"Zhou","year":"2017","journal-title":"J. Evid.-Based Med."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.toxicon.2014.10.020","article-title":"Toxins and Drug Discovery","volume":"92","author":"Harvey","year":"2014","journal-title":"Toxicon"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"s43","DOI":"10.1016\/S0002-8703(98)70297-2","article-title":"An Overview of the Results of Clinical Trials with Glycoprotein IIb\/IIIa Inhibitors","volume":"135","author":"Adgey","year":"1998","journal-title":"Am. Heart J."},{"key":"ref_125","unstructured":"Shah, I., Khan, S.O., Malhotra, S., and Fischell, T. (2009). Core Evidence Eptifibatide: The Evidence for Its Role in the Management of Acute Coronary Syndromes, Dove Medical Press Ltd."},{"key":"ref_126","doi-asserted-by":"crossref","unstructured":"Tonin, G., and Klen, J. (2023). Eptifibatide, an Older Therapeutic Peptide with New Indications: From Clinical Pharmacology to Everyday Clinical Practice. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24065446"},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"1199","DOI":"10.1517\/14656566.3.8.1199","article-title":"Eptifibatide: A potent inhibitor of the platelet receptor integrin glycoprotein IIb\/IIIa","volume":"3","author":"Tcheng","year":"2002","journal-title":"Expert Opin. Pharmacother."},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"S332","DOI":"10.1097\/00003246-200205001-00025","article-title":"Platelet Glycoprotein IIb\/IIIa Antagonists: Lessons Learned from Clinical Trials and Future Directions","volume":"30","author":"Leclerc","year":"2002","journal-title":"Crit. Care Med."},{"key":"ref_129","doi-asserted-by":"crossref","first-page":"11795514211006071","DOI":"10.1177\/11795514211006071","article-title":"Therapeutic Potential of Peptides Derived from Animal Venoms: Current Views and Emerging Drugs for Diabetes","volume":"14","author":"McClean","year":"2021","journal-title":"Clin. Med. Insights Endocrinol. Diabetes"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1111\/bcpt.13169","article-title":"Exendin-4 from Heloderma Suspectum Venom: From Discovery to Its Latest Application as Type II Diabetes Combatant","volume":"124","author":"Yap","year":"2019","journal-title":"Basic Clin. Pharmacol. Toxicol."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"320","DOI":"10.3803\/EnM.2014.29.3.320","article-title":"A Novel Long-Acting Glucagon-like Peptide-1 Agonist with Improved Efficacy in Insulin Secretion and \u03b2-Cell Growth","volume":"29","author":"Kim","year":"2014","journal-title":"Endocrinol. Metab."},{"key":"ref_132","doi-asserted-by":"crossref","unstructured":"Raufman, J.-P. (1996). PEPTIDES Bioactive Peptides from Lizard Venoms, Elsevier.","DOI":"10.1016\/0167-0115(96)00135-8"},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1080\/08998280.2006.11928181","article-title":"Exenatide (Byetta) as a Novel Treatment Option for Type 2 Diabetes Mellitus","volume":"19","author":"Bond","year":"2006","journal-title":"Proc. Bayl. Univ. Med. Cent."},{"key":"ref_134","doi-asserted-by":"crossref","first-page":"2069","DOI":"10.1210\/en.2004-1349","article-title":"Exenatide (Exendin-4) Improves Insulin Sensitivity and \u03b2-Cell Mass in Insulin-Resistant Obese fa\/fa Zucker Rats Independent of Glycemia and Body Weight","volume":"146","author":"Gedulin","year":"2005","journal-title":"Endocrinology"},{"key":"ref_135","doi-asserted-by":"crossref","unstructured":"Liu, Q.K. (2024). Mechanisms of Action and Therapeutic Applications of GLP-1 and Dual GIP\/GLP-1 Receptor Agonists. Front. Endocrinol., 15.","DOI":"10.3389\/fendo.2024.1431292"},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1080\/14656566.2017.1282463","article-title":"Exenatide: Pharmacokinetics, Clinical Use, and Future Directions","volume":"18","author":"Knop","year":"2017","journal-title":"Expert Opin. Pharmacother."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.1210\/endo.141.6.7490","article-title":"Exendin-4 Decelerates Food Intake, Weight Gain, and Fat Deposition in Zucker Rats","volume":"141","author":"Szayna","year":"2000","journal-title":"Endocrinology"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"155332","DOI":"10.1016\/j.metabol.2022.155332","article-title":"Pharmacotherapy of Type 2 Diabetes: An Update and Future Directions","volume":"137","author":"DeMarsilis","year":"2022","journal-title":"Metabolism"},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1007\/s44446-025-00038-y","article-title":"GLP-1 Receptor Agonism: A Transformative Approach for Managing Type-2 Diabetes and Obesity","volume":"33","author":"Alharbi","year":"2025","journal-title":"Saudi Pharm. J. SPJ"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"621","DOI":"10.2147\/VHRM.S37969","article-title":"Treatment with exenatide once weekly or twice daily for 30 weeks is associated with changes in several cardiovascular risk markers","volume":"8","author":"Brunell","year":"2012","journal-title":"Vasc. Heal. Risk Manag."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"2028","DOI":"10.1002\/hep.28827","article-title":"Exenatide Improves Both Hepatic and Adipose Tissue Insulin Resistance: A Dynamic Positron Emission Tomography Study","volume":"64","author":"Gastaldelli","year":"2016","journal-title":"Hepatology"},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1007\/s11883-008-0009-z","article-title":"Exenatide as a Treatment for Diabetes and Obesity: Implications for Cardiovascular Risk Reduction","volume":"10","author":"Mafong","year":"2008","journal-title":"Curr. Atheroscler. Rep."},{"key":"ref_143","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1016\/j.toxicon.2010.12.016","article-title":"The Development of Byetta (Exenatide) from the Venom of the Gila Monster as an Anti-Diabetic Agent","volume":"59","author":"Furman","year":"2012","journal-title":"Toxicon"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"108045","DOI":"10.1016\/j.phrs.2025.108045","article-title":"History of Glucagon-like Peptide-1 Receptor Agonists","volume":"222","author":"Darwish","year":"2025","journal-title":"Pharmacol. Res."},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1038\/s41401-020-00501-7","article-title":"Cobrotoxin Could Be an Effective Therapeutic for COVID-19","volume":"41","author":"Lin","year":"2020","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_146","doi-asserted-by":"crossref","unstructured":"Rubiu, E., Restelli, F., Nazzi, V., Mazzapicchi, E., Bonomo, G., Veiceschi, P., Alfiero, T., Agresta, G., Locatelli, D., and Dario, A. (2024). A Benefit\/Risk Assessment of Intrathecal Ziconotide in Chronic Pain: A Narrative Review. J. Clin. Med., 13.","DOI":"10.3390\/jcm13061644"},{"key":"ref_147","doi-asserted-by":"crossref","unstructured":"Bordon, K.d.C.F., Cologna, C.T., Fornari-Baldo, E.C., Pinheiro-J\u00fanior, E.L., Cerni, F.A., Amorim, F.G., Anjolette, F.A.P., Cordeiro, F.A., Wiezel, G.A., and Cardoso, I.A. (2020). From Animal Poisons and Venoms to Medicines: Achievements, Challenges and Perspectives in Drug Discovery. Front. Pharmacol., 11.","DOI":"10.3389\/fphar.2020.01132"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"3845","DOI":"10.1039\/D1AY00717C","article-title":"Separation, Identification and Quantification of Associated Impurities in Cobratide Using Sheathless CE-MS and CE-UV","volume":"13","author":"Liu","year":"2021","journal-title":"Anal. Methods"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1093\/jb\/117.2.438","article-title":"The Structural Loop II of Cobrotoxin Is the Main Binding Region for nAChR and Epitope in the Region Is Conformation-Dependent","volume":"117","author":"Kuo","year":"1995","journal-title":"J. Biochem."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1254\/jphs.94.1","article-title":"Three-Finger \u03b1-Neurotoxins and the Nicotinic Acetylcholine Receptor, Forty Years On","volume":"94","author":"Nirthanan","year":"2004","journal-title":"J. Pharmacol. Sci."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"1087","DOI":"10.1016\/j.jep.2016.11.009","article-title":"Cobrotoxin Extracted from Naja atra Venom Relieves Arthritis Symptoms through Anti-Inflammation and Immunosuppression Effects in Rat Arthritis Model","volume":"194","author":"Zhu","year":"2016","journal-title":"J. Ethnopharmacol."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"69","DOI":"10.2147\/nedt.2007.3.1.69","article-title":"Ziconotide: A Review of Its Pharmacology and Use in the Treatment of Pain","volume":"3","author":"McGivern","year":"2007","journal-title":"Neuropsychiatr. Dis. Treat."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"D454","DOI":"10.1093\/nar\/gkx1084","article-title":"KNOTTIN: The Database of Inhibitor Cystine Knot Scaffold after 10 Years, toward a Systematic Structure Modeling","volume":"46","author":"Postic","year":"2018","journal-title":"Nucleic Acids Res."},{"key":"ref_154","doi-asserted-by":"crossref","unstructured":"Fu, Y., Li, C., Dong, S., Wu, Y., Zhangsun, D., and Luo, S. (2018). Discovery Methodology of Novel Conotoxins from Conus Species. Mar. Drugs, 16.","DOI":"10.3390\/md16110417"},{"key":"ref_155","doi-asserted-by":"crossref","unstructured":"Di Maio, G., Villano, I., Ilardi, C.R., Messina, A., Monda, V., Iodice, A.C., Porro, C., Panaro, M.A., Chieffi, S., and Messina, G. (2023). Mechanisms of Transmission and Processing of Pain: A Narrative Review. Int. J. Environ. Res. Public Health, 20.","DOI":"10.3390\/ijerph20043064"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"3726","DOI":"10.7150\/ijbs.110504","article-title":"Regulatory Action of Calcium and Calcium Channels in Pain Pathways","volume":"21","author":"Zhang","year":"2025","journal-title":"Int. J. Biol. Sci."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"S11","DOI":"10.1097\/01.rhu.0000158686.43637.af","article-title":"The Nature of Pain: Pathophysiology","volume":"11","author":"Katz","year":"2005","journal-title":"J. Clin. Rheumatol."},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1016\/S0885-3924(99)00120-7","article-title":"Update on the Neurophysiology of Pain Transmission and Modulation: Focus on the NMDA-Receptor","volume":"19","author":"Bennett","year":"2000","journal-title":"J. Pain Symptom Manag."},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1002\/cne.901860203","article-title":"Spinal Termination of Functionally Identified Primary Afferent Neurons with Slowly Conducting Myelinated Fibers","volume":"186","author":"Light","year":"1979","journal-title":"J. Comp. Neurol."},{"key":"ref_160","doi-asserted-by":"crossref","unstructured":"Fajloun, Z., Roufayel, R., and Rima, M. (2026). Animal Venoms for Drug Discovery: A Constantly Evolving Research Field. Toxins, 18.","DOI":"10.3390\/toxins18010030"},{"key":"ref_161","first-page":"20","article-title":"asghar Evaluation of Anti-Cancer Effects of Caspian Cobra (Naja naja oxiana) Snake Venom in Comparison with Doxorubicin in HeLa Cancer Cell Line and Normal HFF Fibroblast","volume":"29","author":"Zafari","year":"2021","journal-title":"J. Ilam Univ. Med. Sci."},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"943","DOI":"10.1016\/S0006-3495(03)74533-0","article-title":"A-Bungarotoxin Binding to Acetylcholine Receptor Membranes Studied by Low Angle X-Ray Diffraction","volume":"85","author":"Young","year":"2003","journal-title":"Biophys. J."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"8302","DOI":"10.1074\/jbc.M109.074161","article-title":"Structural and Functional Characterization of a Novel Homodimeric Three-Finger Neurotoxin from the Venom of Ophiophagus hannah (King Cobra)","volume":"285","author":"Roy","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"8543","DOI":"10.1021\/bi00447a041","article-title":"Kappa-Neurotoxins: Heterodimer Formation between Different Neuronal Nicotinic Receptor Antagonists","volume":"28","author":"Chiappinelli","year":"1989","journal-title":"Biochemistry"},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/0006-8993(88)90494-5","article-title":"\u03ba-Bungarotoxin Blocks an \u03b1-Bungarotoxin-Sensitive Nicotinic Receptor in the Insect Central Nervous System","volume":"458","author":"Pinnock","year":"1988","journal-title":"Brain Res."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1016\/0006-8993(88)91481-3","article-title":"\u03ba-Bungarotoxin: Binding of a Neuronal Nicotinic Receptor Antagonist to Chick Optic Lobe and Skeletal Muscle","volume":"439","author":"Wolf","year":"1988","journal-title":"Brain Res."},{"key":"ref_167","doi-asserted-by":"crossref","unstructured":"Kini, R.M., and Koh, C.Y. (2025). Variations in \u201cFunctional Site\u201d Residues and Classification of Three-Finger Neurotoxins in Snake Venoms. Toxins, 17.","DOI":"10.3390\/toxins17080364"},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"552","DOI":"10.1097\/j.pain.0000000000000397","article-title":"Analgesic Effects of Mambalgin Peptide Inhibitors of Acid-Sensing Ion Channels in Inflammatory and Neuropathic Pain","volume":"157","author":"Diochot","year":"2016","journal-title":"Pain"},{"key":"ref_169","doi-asserted-by":"crossref","unstructured":"Kowalczyk, T., Muska\u0142a, M., Piekarski, J., Kowalski, M., Staszewski, M., Konuklugil, B., Rijo, P., and Sitarek, P. (2025). Therapeutic Promise and Biotechnological Prospects of Dendroaspis polylepis Venom Proteins: Mambalgins, Fasciculins, and Dendrotoxins. Int. J. Mol. Sci., 2025.","DOI":"10.3390\/ijms26209895"},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2616","DOI":"10.1074\/jbc.M115.702373","article-title":"Mambalgin-1 Pain-Relieving Peptide, Stepwise Solid-Phase Synthesis, Crystal Structure, and Functional Domain for Acid-Sensing Ion Channel 1a Inhibition","volume":"291","author":"Mourier","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"2437","DOI":"10.1073\/pnas.88.6.2437","article-title":"Calciseptine, a Peptide Isolated from Black Mamba Venom, Is a Specific Blocker of the L-Type Calcium Channel","volume":"88","author":"Schweitz","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_172","doi-asserted-by":"crossref","unstructured":"Yang, D.C., Deuis, J.R., Dashevsky, D., Dobson, J., Jackson, T.N.W., Brust, A., Xie, B., Koludarov, I., Debono, J., and Hendrikx, I. (2016). The Snake with the Scorpion\u2019s Sting: Novel Three-Finger Toxin Sodium Channel Activators from the Venom of the Long-Glanded Blue Coral Snake (Calliophis bivirgatus). Toxins, 8.","DOI":"10.3390\/toxins8100303"},{"key":"ref_173","doi-asserted-by":"crossref","unstructured":"Zhang, Y., Yang, Q., Zhang, Q., Peng, D., Chen, M., Liang, S., Zhou, X., and Liu, Z. (2018). Engineering Gain-of-Function Analogues of the Spider Venom Peptide HNTX-I, A Potent Blocker of the hNaV1.7 Sodium Channel. Toxins, 10.","DOI":"10.3390\/toxins10090358"},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1159\/000092421","article-title":"Comparison of Textilinin-1 with Aprotinin as Serine Protease Inhibitors and as Antifibrinolytic Agents","volume":"34","author":"Flight","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1097\/00001721-200006000-00011","article-title":"Textilinins from Pseudonaja Textilis Textilis. Characterization of Two Plasmin Inhibitors That Reduce Bleeding in an Animal Model","volume":"11","author":"Masci","year":"2000","journal-title":"Blood Coagul. Fibrinolysis Int. J. Haemost. Thromb."},{"key":"ref_176","doi-asserted-by":"crossref","unstructured":"Messadi, E. (2023). Snake Venom Components as Therapeutic Drugs in Ischemic Heart Disease. Biomolecules, 13.","DOI":"10.3390\/biom13101539"},{"key":"ref_177","doi-asserted-by":"crossref","unstructured":"Tourki, B., Mat\u00e9o, P., Morand, J., Elayeb, M., Godin-Ribuot, D., Marrakchi, N., Belaidi, E., and Messadi, E. (2016). Lebetin 2, a Snake Venom-Derived Natriuretic Peptide, Attenuates Acute Myocardial Ischemic Injury through the Modulation of Mitochondrial Permeability Transition Pore at the Time of Reperfusion. PLoS ONE, 11.","DOI":"10.1371\/journal.pone.0162632"},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"802","DOI":"10.1038\/nsb1194-802","article-title":"Three-Dimensional Structure of the RGD-Containing Neurotoxin Homologue Dendroaspin","volume":"1","author":"Sutcliffe","year":"1994","journal-title":"Nat. Struct. Biol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"73S","DOI":"10.1042\/bst021073s","article-title":"Dendroaspin: A Potent Integrin Receptor Inhibitor from the Venoms of Dendroaspis viridis and D. jamesonii","volume":"21","author":"Williams","year":"1993","journal-title":"Biochem. Soc. Trans."},{"key":"ref_180","doi-asserted-by":"crossref","unstructured":"Guo, R., Guo, G., Wang, A., Xu, G., Lai, R., and Jin, H. (2024). Spider-Venom Peptides: Structure, Bioactivity, Strategy, and Research Applications. Molecules, 29.","DOI":"10.3390\/molecules29010035"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"153","DOI":"10.2174\/09298665113206660119","article-title":"Analgesic Effects of Huwentoxin-IV on Animal Models of Inflammatory and Neuropathic Pain","volume":"21","author":"Liu","year":"2014","journal-title":"Protein Pept. Lett."},{"key":"ref_182","doi-asserted-by":"crossref","unstructured":"Land, J., Lintermans, L.L., Stegeman, C.A., Mu\u00f1oz-El\u00edas, E.J., Tarcha, E.J., Iadonato, S.P., Heeringa, P., Rutgers, A., and Abdulahad, W.H. (2017). Kv1.3 Channel Blockade Modulates the Effector Function of B Cells in Granulomatosis with Polyangiitis. Front. Immunol., 8.","DOI":"10.3389\/fimmu.2017.01205"},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"100529","DOI":"10.1016\/j.prmcm.2024.100529","article-title":"Anticoagulant Peptides Derived from Animal-Sourced Traditional Chinese Medicine and Their Pharmacological Effects","volume":"13","author":"Liu","year":"2024","journal-title":"Pharmacol. Res.-Mod. Chin. Med."},{"key":"ref_184","doi-asserted-by":"crossref","unstructured":"Tang, X., Chen, M., Duan, Z., Mwangi, J., Li, P., and Lai, R. (2018). Isolation and Characterization of Poecistasin, an Anti-Thrombotic Antistasin-Type Serine Protease Inhibitor from Leech Poecilobdella manillensis. Toxins, 10.","DOI":"10.3390\/toxins10110429"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"10162","DOI":"10.1016\/S0021-9258(19)81491-6","article-title":"The Amino Acid Sequence of Antistasin. A Potent Inhibitor of Factor Xa Reveals a Repeated Internal Structure","volume":"263","author":"Nutt","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"212","DOI":"10.1046\/j.1432-1327.1998.2530212.x","article-title":"Bdellastasin, a Serine Protease Inhibitor of the Antistasin Family from the Medical Leech (Hirudo medicinalis). Primary Structure, Expression in Yeast, and Characterisation of Native and Recombinant Inhibitor","volume":"253","author":"Moser","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"937","DOI":"10.1111\/j.1432-1033.1994.tb18575.x","article-title":"Isolation and Characterization of Hirustasin, an Antistasin-Type Serine-Proteinase Inhibitor from the Medical Leech Hirudo medicinalis","volume":"219","author":"Mentele","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"2046","DOI":"10.1073\/pnas.88.6.2046","article-title":"Design, Synthesis, and Functional Expression of a Gene for Charybdotoxin, a Peptide Blocker of K+ Channels","volume":"88","author":"Park","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1016\/S0006-3495(92)81630-2","article-title":"Mode of Action of Iberiotoxin, a Potent Blocker of the Large Conductance Ca2+-Activated K+ Channel","volume":"63","author":"Candia","year":"1992","journal-title":"Biophys. J."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"100146","DOI":"10.1016\/j.jtauto.2022.100146","article-title":"Pharmacological Blockade of KV1.3 Channel as a Promising Treatment in Autoimmune Diseases","volume":"5","year":"2022","journal-title":"J. Transl. Autoimmun."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"115023","DOI":"10.1016\/j.bcp.2022.115023","article-title":"sVmKTx, a Transcriptome Analysis-Based Synthetic Peptide Analogue of Vm24, Inhibits Kv1.3 Channels of Human T Cells with Improved Selectivity","volume":"199","author":"Csoti","year":"2022","journal-title":"Biochem. Pharmacol."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"372","DOI":"10.1124\/mol.112.078006","article-title":"Vm24, a Natural Immunosuppressive Peptide, Potently and Selectively Blocks Kv1.3 Potassium Channels of Human T Cells","volume":"82","author":"Varga","year":"2012","journal-title":"Mol. Pharmacol."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"314","DOI":"10.4048\/jbc.2014.17.4.314","article-title":"Anticancer Activity of Cobra Venom Polypeptide, Cytotoxin-II, against Human Breast Adenocarcinoma Cell Line (MCF-7) via the Induction of Apoptosis","volume":"17","author":"Ebrahim","year":"2014","journal-title":"J. Breast Cancer"},{"key":"ref_194","doi-asserted-by":"crossref","unstructured":"Tosti, E., Boni, R., and Gallo, A. (2017). \u039c-Conotoxins Modulating Sodium Currents in Pain Perception and Transmission: A Therapeutic Potential. Mar. Drugs, 15.","DOI":"10.20944\/preprints201709.0026.v1"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"119","DOI":"10.3390\/md403119","article-title":"Conotoxins: Therapeutic Potential and Application","volume":"4","author":"Layer","year":"2006","journal-title":"Mar. Drugs"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1152\/physrev.00020.2003","article-title":"Conus Venoms: A Rich Source of Novel Ion Channel-Targeted Peptides","volume":"84","author":"Terlau","year":"2004","journal-title":"Physiol. Rev."},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"184","DOI":"10.1016\/j.nurt.2007.01.013","article-title":"Ion Channel Pharmacology","volume":"4","author":"Camerino","year":"2007","journal-title":"Neurotherapeutics"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.2174\/0929867311320100005","article-title":"Ion Channels as Drug Targets in Central Nervous System Disorders","volume":"20","author":"Waszkielewicz","year":"2013","journal-title":"Curr. Med. Chem."},{"key":"ref_199","doi-asserted-by":"crossref","first-page":"3911","DOI":"10.1111\/bph.14461","article-title":"GpTx-1 and [Ala5, Phe6, Leu26, Arg28]GpTx-1, Two Peptide NaV1.7 Inhibitors: Analgesic and Tolerance Properties at the Spinal Level","volume":"175","author":"Chen","year":"2018","journal-title":"Br. J. Pharmacol."},{"key":"ref_200","doi-asserted-by":"crossref","unstructured":"Stevens, M., Peigneur, S., Tytgat, J., and Chahine, M. (2011). Neurotoxins and Their Binding Areas on Voltage-Gated Sodium Channels. Front. Pharmacol., 2.","DOI":"10.3389\/fphar.2011.00071"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1038\/s41570-022-00393-7","article-title":"The Chemistry of Snake Venom and Its Medicinal Potential","volume":"67","author":"Oliveira","year":"2022","journal-title":"Nat. Rev. Chem."},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1134\/S1607672919040094","article-title":"Cardiotoxins from Cobra Naja oxiana Change the Force of Contraction and the Character of Rhythmoinotropic Phenomena in the Rat Myocardium","volume":"487","author":"Averin","year":"2019","journal-title":"Dokl. Biochem. Biophys."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"4","DOI":"10.32607\/actanaturae.11375","article-title":"Cardiovascular Effects of Snake Toxins: Cardiotoxicity and Cardioprotection","volume":"13","author":"Averin","year":"2021","journal-title":"Acta Naturae"},{"key":"ref_204","doi-asserted-by":"crossref","unstructured":"AlShammari, A.K., Abd El-Aziz, T.M., and Al-Sabi, A. (2024). Snake Venom: A Promising Source of Neurotoxins Targeting Voltage-Gated Potassium Channels. Toxins, 16.","DOI":"10.3390\/toxins16010012"},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0378-4274(98)00307-5","article-title":"How Do Snake Curaremimetic Toxins Discriminate between Nicotinic Acetylcholine Receptor Subtypes","volume":"102","author":"Servent","year":"1998","journal-title":"Toxicol. Lett."},{"key":"ref_206","doi-asserted-by":"crossref","unstructured":"Munawar, A., Ali, S.A., Akrem, A., and Betzel, C. (2018). Snake Venom Peptides: Tools of Biodiscovery. Toxins, 10.","DOI":"10.3390\/toxins10110474"},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"4543","DOI":"10.1038\/s41467-022-32174-7","article-title":"The Molecular Mechanism of Snake Short-Chain \u03b1-Neurotoxin Binding to Muscle-Type Nicotinic Acetylcholine Receptors","volume":"13","author":"Nys","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.neuropharm.2016.04.027","article-title":"The Muscarinic Antagonists Scopolamine and Atropine Are Competitive Antagonists at 5-HT3 Receptors","volume":"108","author":"Lochner","year":"2016","journal-title":"Neuropharmacology"},{"key":"ref_209","doi-asserted-by":"crossref","unstructured":"Bekbossynova, A., Zharylgap, A., and Filchakova, O. (2021). Venom-Derived Neurotoxins Targeting Nicotinic Acetylcholine Receptors. Molecules, 26.","DOI":"10.3390\/molecules26113373"},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"295","DOI":"10.5483\/BMBRep.2013.46.6.121","article-title":"Acid-Sensing Ion Channels (ASICs): Therapeutic Targets for Neurological Diseases and Their Regulation","volume":"46","author":"Kweon","year":"2013","journal-title":"BMB Rep."},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.coph.2007.09.001","article-title":"Acid-Sensing Ion Channels (ASICs) as Pharmacological Targets for Neurodegenerative Diseases","volume":"8","author":"Xiong","year":"2007","journal-title":"Curr. Opin. Pharmacol."},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"e2021581118","DOI":"10.1073\/pnas.2021581118","article-title":"Mambalgin-3 Potentiates Human Acid-Sensing Ion Channel 1b under Mild to Moderate Acidosis: Implications as an Analgesic Lead","volume":"118","author":"Budusan","year":"2021","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"1744806919858801","DOI":"10.1177\/1744806919858801","article-title":"Nav 1.7 and Nav 1.8: Role in the Pathophysiology of Pain","volume":"15","author":"Hameed","year":"2019","journal-title":"Mol. Pain"},{"key":"ref_214","doi-asserted-by":"crossref","unstructured":"Meng, P., Huang, H., Wang, G., Yang, S., Lu, Q., Liu, J., Lai, R., and Rong, M. (2016). A Novel Toxin from Haplopelma lividum Selectively Inhibits the NaV1.8 Channel and Possesses Potent Analgesic Efficacy. Toxins, 9.","DOI":"10.3390\/toxins9010007"},{"key":"ref_215","doi-asserted-by":"crossref","unstructured":"Tosti, E., Boni, R., and Gallo, A. (2022). Pathophysiological Responses to Conotoxin Modulation of Voltage-Gated Ion Currents. Mar. Drugs, 20.","DOI":"10.3390\/md20050282"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"828","DOI":"10.1124\/pharmrev.123.000923","article-title":"Conotoxins Targeting Voltage-Gated Sodium Ion Channels","volume":"76","author":"Pei","year":"2024","journal-title":"Pharmacol. Rev."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1016\/j.neuropharm.2017.07.002","article-title":"Venom-Derived Peptide Inhibitors of Voltage-Gated Potassium Channels","volume":"127","author":"Norton","year":"2017","journal-title":"Neuropharmacology"},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1016\/j.toxicon.2018.07.008","article-title":"Phoneutria nigriventer Venom: A Pharmacological Treasure","volume":"151","author":"Peigneur","year":"2018","journal-title":"Toxicon"},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/j.bcp.2011.10.019","article-title":"A-1048400 Is a Novel, Orally Active, State-Dependent Neuronal Calcium Channel Blocker That Produces Dose-Dependent Antinociception without Altering Hemodynamic Function in Rats","volume":"83","author":"Scott","year":"2012","journal-title":"Biochem. Pharmacol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"387.e1","DOI":"10.1016\/j.jpain.2013.12.002","article-title":"Mechanistic Insights Into the Analgesic Efficacy of A-1264087, a Novel Neuronal Ca2+ Channel Blocker That Reduces Nociception in Rat Preclinical Pain Models","volume":"15","author":"Zhu","year":"2014","journal-title":"J. Pain"},{"key":"ref_221","doi-asserted-by":"crossref","unstructured":"Dallegrave, E., Taschetto, E., Leal, M.B., Antunes, F.T.T., Gomez, M.V., and de Souza, A.H. (2018). Acute Toxicity of the Recombinant and Native Ph\u03b11\u03b2 Toxin: New Analgesic from Phoneutria nigriventer Spider Venom. Toxins, 10.","DOI":"10.3390\/toxins10120531"},{"key":"ref_222","doi-asserted-by":"crossref","unstructured":"Gerdol, M., Cervelli, M., Mariottini, P., Oliverio, M., Dutertre, S., Modica, M.V., Gerdol, M., Cervelli, M., Mariottini, P., and Oliverio, M. (2019). A Recurrent Motif: Diversity and Evolution of ShKT Domain Containing Proteins in the Vampire Snail Cumia reticulata. Toxins, 11.","DOI":"10.3390\/toxins11020106"},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"573","DOI":"10.1002\/ddr.20467","article-title":"The Lymphocyte Potassium Channels Kv1.3 and KCa3.1 as Targets for Immunosuppression","volume":"72","author":"Lam","year":"2011","journal-title":"Drug Dev. Res."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.toxicon.2013.07.012","article-title":"Scorpion Venom Components That Affect Ion-Channels Function","volume":"76","author":"Gurrola","year":"2013","journal-title":"Toxicon"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"100038","DOI":"10.1016\/j.toxcx.2020.100038","article-title":"Synthetic Peptides to Produce Antivenoms against the Cys-Rich Toxins of Arachnids","volume":"6","author":"Camperi","year":"2020","journal-title":"Toxicon X"},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"2921","DOI":"10.7150\/ijbs.109713","article-title":"Deciphering Scorpion Toxin-Induced Pain: Molecular Mechanisms and Ion Channel Dynamics","volume":"21","author":"He","year":"2025","journal-title":"Int. J. Biol. Sci."},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"116651","DOI":"10.1016\/j.biopha.2024.116651","article-title":"Voltage-Gated Potassium Channel 1.3: A Promising Molecular Target in Multiple Disease Therapy","volume":"175","author":"Cheng","year":"2024","journal-title":"Biomed. Pharmacother."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.3390\/toxins7051749","article-title":"Toxins Targeting the Kv1.3 Channel: Potential Immunomodulators for Autoimmune Diseases","volume":"7","author":"Zhao","year":"2015","journal-title":"Toxins"},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1007\/s10741-019-09825-x","article-title":"\u03b2-Adrenergic Receptor, an Essential Target in Cardiovascular Diseases","volume":"25","author":"Ali","year":"2020","journal-title":"Heart Fail. Rev."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1186\/ar289","article-title":"T-Cell-Mediated Control of Autoimmunity","volume":"3","author":"Mason","year":"2001","journal-title":"Arthritis Res."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"298","DOI":"10.2174\/1570159X11311030005","article-title":"Nicotinic Receptors in Neurodegeneration","volume":"11","author":"Posadas","year":"2013","journal-title":"Curr. Neuropharmacol."},{"key":"ref_232","doi-asserted-by":"crossref","unstructured":"El-Aziz, T.M.A., Soares, A.G., and Stockand, J.D. (2019). Snake Venoms in Drug Discovery: Valuable Therapeutic Tools for Life Saving. Toxins, 11.","DOI":"10.3390\/toxins11100564"},{"key":"ref_233","doi-asserted-by":"crossref","unstructured":"Kalita, B., Utkin, Y.N., and Mukherjee, A.K. (2022). Current Insights in the Mechanisms of Cobra Venom Cytotoxins and Their Complexes in Inducing Toxicity: Implications in Antivenom Therapy. Toxins, 14.","DOI":"10.3390\/toxins14120839"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"3685","DOI":"10.1096\/fj.07-8658com","article-title":"\u03b2-Cardiotoxin: A New Three-finger Toxin from Ophiophagus hannah (King Cobra) Venom with Beta-blocker Activity","volume":"21","author":"Rajagopalan","year":"2007","journal-title":"FASEB J."},{"key":"ref_235","first-page":"e20210110","article-title":"S- And P-Type Cobra Venom Cardiotoxins Differ in Their Action on Isolated Rat Heart","volume":"28","author":"Averin","year":"2022","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_236","doi-asserted-by":"crossref","unstructured":"Allaoui, H., Rached, N., Marrakchi, N., Cherif, A., Mosbah, A., and Messadi, E. (2022). In Silico Study of the Mechanisms Underlying the Action of the Snake Natriuretic-Like Peptide Lebetin 2 during Cardiac Ischemia. Toxins, 14.","DOI":"10.3390\/toxins14110787"},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.cophys.2018.04.008","article-title":"The Nicotinic Acetylcholine Receptor as a Molecular Machine for Neuromuscular Transmission","volume":"4","author":"Bouzat","year":"2018","journal-title":"Curr. Opin. Physiol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1046\/j.1432-1327.1999.00623.x","article-title":"Snake Venom A-neurotoxins and Other \u2018Three-finger\u2019 Proteins","volume":"264","author":"Tsetlin","year":"1999","journal-title":"Eur. J. Biochem."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"281","DOI":"10.6026\/97320630010281","article-title":"Hypothesis A Comparative in Silico Characterization of Functional and Physicochemical Properties of 3FTx (Three Finger Toxin) Proteins from Four Venomous Snakes","volume":"10","author":"Roly","year":"2014","journal-title":"Bioinformation"},{"key":"ref_240","doi-asserted-by":"crossref","unstructured":"Son, L., Kryukova, E., Ziganshin, R., Andreeva, T., Kudryavtsev, D., Kasheverov, I., Tsetlin, V., and Utkin, Y. (2021). Novel Three-Finger Neurotoxins from Naja Melanoleuca Cobra Venom Interact with GABAA and Nicotinic Acetylcholine Receptors. Toxins, 13.","DOI":"10.3390\/toxins13020164"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1038\/nrd4295","article-title":"Muscarinic Acetylcholine Receptors: Novel Opportunities for Drug Development","volume":"13","author":"Kruse","year":"2014","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_242","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1016\/S0041-0101(99)00196-8","article-title":"Muscarinic Toxins: Novel Pharmacological Tools for the Muscarinic Cholinergic System","volume":"38","author":"Jerusalinsky","year":"2000","journal-title":"Toxicon"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"23616","DOI":"10.1074\/jbc.M115.656595","article-title":"Structural Insight into Specificity of Interactions between Nonconventional Three-Finger Weak Toxin from Naja kaouthia (WTX) and Muscarinic Acetylcholine Receptors","volume":"290","author":"Lyukmanova","year":"2015","journal-title":"J. Biol. Chem."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1097\/MBC.0000000000001130","article-title":"The Role of Thrombin in Haemostasis","volume":"33","year":"2022","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/j.blre.2011.03.002","article-title":"Platelets at Work in Primary Hemostasis","volume":"25","author":"Broos","year":"2011","journal-title":"Blood Rev."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/j.blre.2014.09.003","article-title":"Fibrinolysis and the Control of Blood Coagulation","volume":"29","author":"Chapin","year":"2014","journal-title":"Blood Rev."},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"414","DOI":"10.1016\/j.bcmd.2006.03.001","article-title":"Blood Cells as Targets of Snake Toxins","volume":"36","author":"Du","year":"2006","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/0268-960X(93)90004-N","article-title":"Action of Snake Venom Components on the Haemostatic System","volume":"7","author":"Hutton","year":"1993","journal-title":"Blood Rev."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1042\/BJ20060302","article-title":"Anticoagulant Proteins from Snake Venoms: Structure, Function and Mechanism","volume":"397","author":"Kini","year":"2006","journal-title":"Biochem. J."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"171","DOI":"10.3109\/10408449109089878","article-title":"Effects of Snake Venoms on Hemostasis","volume":"21","author":"Meier","year":"1991","journal-title":"Crit. Rev. Toxicol."},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/S0014-5793(01)02212-8","article-title":"Anticoagulants and Inhibitors of Platelet Aggregation Derived from Leeches","volume":"492","author":"Salzet","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_252","doi-asserted-by":"crossref","first-page":"1734","DOI":"10.3324\/haematol.2022.282136","article-title":"The Relative Importance of Platelet Integrins in Hemostasis, Thrombosis and Beyond","volume":"108","author":"Mangin","year":"2023","journal-title":"Haematologica"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1080\/15419060600726183","article-title":"The Effect of the Single Substitution of Arginine within the RGD Tripeptide Motif of a Modified Neurotoxin Dendroaspin on Its Activity of Platelet Aggregation and Cell Adhesion","volume":"13","author":"Lu","year":"2006","journal-title":"Cell Commun. Adhes."},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"2391","DOI":"10.1093\/molbev\/msn179","article-title":"Evolution of Snake Venom Disintegrins by Positive Darwinian Selection","volume":"25","author":"Comas","year":"2008","journal-title":"Mol. Biol. Evol."},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"46-e17","DOI":"10.1111\/anae.12907","article-title":"The Current Place of Aprotinin in the Management of Bleeding","volume":"70","author":"Royston","year":"2015","journal-title":"Anaesthesia"},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1002\/med.21315","article-title":"Recent Advances on Plasmin Inhibitors for the Treatment of Fibrinolysis-Related Disorders","volume":"34","author":"Desai","year":"2014","journal-title":"Med. Res. Rev."},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"117","DOI":"10.4103\/0971-9784.109749","article-title":"Antifibrinolytics in Cardiac Surgery","volume":"16","author":"Dhir","year":"2013","journal-title":"Ann. Card. Anaesth."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"31S","DOI":"10.1111\/j.1537-2995.2007.01574.x","article-title":"Pharmacologic Methods to Reduce Perioperative Bleeding","volume":"48","author":"Levy","year":"2008","journal-title":"Transfusion"},{"key":"ref_259","doi-asserted-by":"crossref","first-page":"e693","DOI":"10.1002\/mco2.693","article-title":"Cell Death Pathways: Molecular Mechanisms and Therapeutic Targets for Cancer","volume":"5","author":"Wang","year":"2024","journal-title":"MedComm"},{"key":"ref_260","doi-asserted-by":"crossref","unstructured":"Freuville, L., Matthys, C., Gilliaux, Q., D\u2019Hondt, L., and Gillet, J.P. (2026). Could Venom-Derived Therapeutics Resolve Treatment Resistance in Refractory EAC?. Trends Mol. Med., in press.","DOI":"10.1016\/j.molmed.2026.03.007"},{"key":"ref_261","doi-asserted-by":"crossref","unstructured":"Arcos, S.S.S., Aguiar, M.R.d.C., de Oliveira, J., da Silva, M.R., Pimentel, I.d.O.C., dos Anjos, N.G., Machado, G.H.R.S., Evangelista, K.B., Portaro, F.C.V., and Iwai, L.K. (2025). Scorpion Venom as a Source of Cancer Drugs: A Comprehensive Proteomic Analysis and Therapeutic Potential. Int. J. Mol. Sci., 26.","DOI":"10.20944\/preprints202508.2046.v1"},{"key":"ref_262","doi-asserted-by":"crossref","unstructured":"Malachias-Pires, G.M., Filardi, E.T.M., Romanazzi, M., Lopes-de-Oliveira, J., dos Santos, I.C., Melo-dos-Santos, G., Rossi, A.B., Proc\u00f3pio Machado, M., da Silva, T.A., and Pucca, M.B. (2025). Animal Venoms as Potential Antitumor Agents Against Leukemia and Lymphoma. Cancers, 17.","DOI":"10.3390\/cancers17142331"},{"key":"ref_263","doi-asserted-by":"crossref","unstructured":"Derakhshani, A., Silvestris, N., Hemmat, N., Asadzadeh, Z., Shadbad, M.A., Nourbakhsh, N.S., Mobasheri, L., Vahedi, P., Shahmirzaie, M., and Brunetti, O. (2020). Targeting TGF-\u03b2-Mediated SMAD Signaling Pathway via Novel Recombinant Cytotoxin II: A Potent Protein from Naja naja oxiana Venom in Melanoma. Molecules, 25.","DOI":"10.3390\/molecules25215148"},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1016\/j.toxicon.2015.09.017","article-title":"Cobra Venom Cytotoxins; Apoptotic or Necrotic Agents?","volume":"108","author":"Ebrahim","year":"2015","journal-title":"Toxicon"},{"key":"ref_265","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1007\/s10989-022-10479-x","article-title":"The Cytotoxic Effects of Partially Purified Cytotoxic Peptides of Naja naja Oxiana Venom on Human Glioblastoma Multiforme: An in Vitro Study","volume":"29","author":"Sinaei","year":"2023","journal-title":"Int. J. Pept. Res. Ther."},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"724","DOI":"10.1016\/j.bbamem.2012.10.014","article-title":"Cysteine-Rich Toxins from Lachesana tarabaevi Spider Venom with Amphiphilic C-Terminal Segments","volume":"1828","author":"Kuzmenkov","year":"2013","journal-title":"Biochim. Biophys. Acta-Biomembr."},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1039\/c8tx00022k","article-title":"Anticancer, Antimicrobial, and Analgesic Activities of Spider Venoms","volume":"7","author":"Akef","year":"2018","journal-title":"Toxicol. Res."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.canlet.2017.05.010","article-title":"Melittin, a Major Peptide Component of Bee Venom, and Its Conjugates in Cancer Therapy","volume":"402","author":"Rady","year":"2017","journal-title":"Cancer Lett."},{"key":"ref_269","doi-asserted-by":"crossref","unstructured":"Rizkallah, J., Charbel, N., Yassine, A., El Masri, A., Raffoul, C., El Sardouk, O., Ghezzawi, M., Abou Nasr, T., and Kreidieh, F. (2025). Melittin-Based Nanoparticles for Cancer Therapy: Mechanisms, Applications, and Future Perspectives. Pharmaceutics, 17.","DOI":"10.3390\/pharmaceutics17081019"},{"key":"ref_270","doi-asserted-by":"crossref","unstructured":"de Santana, C.J.C., Pires J\u00fanior, O.R., Fontes, W., Palma, M.S., and Castro, M.S. (2022). Mastoparans: A Group of Multifunctional \u03b1-Helical Peptides with Promising Therapeutic Properties. Front. Mol. Biosci., 9.","DOI":"10.3389\/fmolb.2022.824989"},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"3195","DOI":"10.1016\/j.bbamem.2016.09.021","article-title":"Mastoparan Is a Membranolytic Anti-Cancer Peptide That Works Synergistically with Gemcitabine in a Mouse Model of Mammary Carcinoma","volume":"1858","author":"Hilchie","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_272","doi-asserted-by":"crossref","unstructured":"Alhakamy, N.A., Ahmed, O.A.A., Md, S., and Fahmy, U.A. (2021). Mastoparan, a Peptide Toxin from Wasp Venom Conjugated Fluvastatin Nanocomplex for Suppression of Lung Cancer Cell Growth. Polymers, 13.","DOI":"10.3390\/polym13234225"},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.peptides.2014.09.024","article-title":"Mastoparan Induces Apoptosis in B16F10-Nex2 Melanoma Cells via the Intrinsic Mitochondrial Pathway and Displays Antitumor Activity in Vivo","volume":"68","author":"Figueiredo","year":"2015","journal-title":"Peptides"},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"3098","DOI":"10.1021\/acsinfecdis.4c00314","article-title":"Venom: A Promising Avenue for Antimicrobial Therapeutics","volume":"10","author":"Samat","year":"2024","journal-title":"ACS Infect. Dis."},{"key":"ref_275","doi-asserted-by":"crossref","unstructured":"Muttiah, B., and Hanafiah, A. (2025). Snake Venom Compounds: A New Frontier in the Battle Against Antibiotic-Resistant Infections. Toxins, 17.","DOI":"10.3390\/toxins17050221"},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"4645","DOI":"10.1007\/s00018-013-1345-x","article-title":"Snake Venoms: Attractive Antimicrobial Proteinaceous Compounds for Therapeutic Purposes","volume":"70","author":"Franco","year":"2013","journal-title":"Cell. Mol. Life Sci. CMLS"},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"1331","DOI":"10.1016\/j.biochi.2006.05.003","article-title":"Purification, Characterization and Cytokine Release Function of a Novel Arg-49 Phospholipase A2 from the Venom of Protobothrops mucrosquamatus","volume":"88","author":"Wei","year":"2006","journal-title":"Biochimie"},{"key":"ref_278","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.peptides.2007.02.008","article-title":"A Bactericidal Homodimeric Phospholipases A2 from Bungarus fasciatus Venom","volume":"28","author":"Xu","year":"2007","journal-title":"Peptides"},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"S237","DOI":"10.1194\/jlr.R800033-JLR200","article-title":"Phospholipase A2 Structure\/Function, Mechanism, and Signaling","volume":"50","author":"Burke","year":"2009","journal-title":"J. Lipid Res."},{"key":"ref_280","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1007\/s11696-019-00939-y","article-title":"Antibacterial Properties of Snake Venom Components","volume":"74","author":"Bocian","year":"2020","journal-title":"Chem. Pap."},{"key":"ref_281","doi-asserted-by":"crossref","unstructured":"Okubo, B.M., Silva, O.N., Migliolo, L., Gomes, D.G., Porto, W.F., Batista, C.L., Ramos, C.S., Holanda, H.H.S., Dias, S.C., and Franco, O.L. (2012). Evaluation of an Antimicrobial L-Amino Acid Oxidase and Peptide Derivatives from Bothropoides mattogrosensis Pitviper Venom. PLoS ONE, 7.","DOI":"10.1371\/journal.pone.0033639"},{"key":"ref_282","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.toxicon.2018.08.009","article-title":"Detection and Identification of Antibacterial Proteins in Snake Venoms Using At-Line Nanofractionation Coupled to LC-MS","volume":"155","author":"Mladic","year":"2018","journal-title":"Toxicon"},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15761\/FDCCR.1000136","article-title":"Therapeutic Potential of Snake Venoms as Antimicrobial Agents","volume":"2","author":"Alam","year":"2019","journal-title":"Front. Drug Chem. Clin. Res."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/j.ejmech.2018.02.055","article-title":"A Novel Synthetic Peptide Inspired on Lys49 Phospholipase A2 from Crotalus oreganus abyssus Snake Venom Active against Multidrug-Resistant Clinical Isolates","volume":"149","author":"Almeida","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"ref_285","doi-asserted-by":"crossref","first-page":"1387","DOI":"10.1016\/j.toxicon.2010.02.016","article-title":"Interaction of Naja naja atra Cardiotoxin 3 with H-Trisaccharide Modulates Its Hemolytic Activity and Membrane-Damaging Activity","volume":"55","author":"Kao","year":"2010","journal-title":"Toxicon"},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.toxicon.2012.04.345","article-title":"Naja naja atra and Naja nigricollis Cardiotoxins Induce Fusion of Escherichia coli and Staphylococcus aureus Membrane-Mimicking Liposomes","volume":"60","author":"Kao","year":"2012","journal-title":"Toxicon"},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"1755","DOI":"10.1016\/j.peptides.2011.06.026","article-title":"Bactericidal Effect of Naja nigricollis Toxin \u03b3 Is Related to Its Membrane-Damaging Activity","volume":"32","author":"Chen","year":"2011","journal-title":"Peptides"},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"126890","DOI":"10.1016\/j.bmcl.2019.126890","article-title":"Antibacterial Activity of Cardiotoxin-like Basic Polypeptide from Cobra Venom","volume":"30","author":"Dubovskii","year":"2020","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/S0924-8579(03)00110-9","article-title":"In Vitro Activities of Small Peptides from Snake Venom against Clinical Isolates of Drug-Resistant Mycobacterium Tuberculosis","volume":"22","author":"Xie","year":"2003","journal-title":"Int. J. Antimicrob. Agents"},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.ijbiomac.2016.02.061","article-title":"Venom Peptides Cathelicidin and Lycotoxin Cause Strong Inhibition of Escherichia coli ATP Synthase","volume":"87","author":"Azim","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_291","doi-asserted-by":"crossref","unstructured":"Park, J., Kim, H., Kang, H.-K., Choi, M.-C., and Park, Y. (2022). Lycosin-II Exhibits Antifungal Activity and Inhibits Dual-Species Biofilm by Candida albicans and Staphylococcus aureus. J. Fungi, 8.","DOI":"10.3390\/jof8090901"},{"key":"ref_292","doi-asserted-by":"crossref","unstructured":"Clare, R.H., Dawson, C.A., Westhorpe, A., Albulescu, L.O., Woodley, C.M., Mosallam, N., Chong, D.J.W., Kool, J., Berry, N.G., and O\u2019Neill, P.M. (2023). Snakebite Drug Discovery: High-Throughput Screening to Identify Novel Snake Venom Metalloproteinase Toxin Inhibitors. Front. Pharmacol., 14.","DOI":"10.3389\/fphar.2023.1328950"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"3530","DOI":"10.1039\/C6MB00516K","article-title":"Advances in Venomics","volume":"12","author":"Oldrati","year":"2016","journal-title":"Mol. Biosyst."},{"key":"ref_294","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1002\/mas.21850","article-title":"Quantification of Snake Venom Proteomes by Mass Spectrometry-Considerations and Perspectives","volume":"43","author":"Calvete","year":"2024","journal-title":"Mass Spectrom. Rev."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1080\/15287394.2023.2188896","article-title":"Lipidomic Profiling of the Brazilian Yellow Scorpion Venom: New Insights into Inflammatory Responses Following Tityus serrulatus Envenomation","volume":"86","author":"Acunha","year":"2023","journal-title":"J. Toxicol. Environ. Health-Part Curr. Issues"},{"key":"ref_296","first-page":"355","article-title":"Lipidomics of Bothrops atrox and Crotalus durissus ruruima Venoms, the Two Major Viperids Involved in Human Envenomings in the Brazilian Amazon","volume":"1001","author":"Maciel","year":"2025","journal-title":"Arch. Toxicol."},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1074\/mcp.RA118.000748","article-title":"Structures of N-Glycans of Bothrops Venoms Revealed as Molecular Signatures That Contribute to Venom Phenotype in Viperid Snakes","volume":"17","author":"Ashline","year":"2018","journal-title":"Mol. Cell. Proteom."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1016\/j.jprot.2015.07.015","article-title":"Cobra Venom Proteome and Glycome Determined from Individual Snakes of Naja atra Reveal Medically Important Dynamic Range and Systematic Geographic Variation","volume":"128","author":"Huang","year":"2015","journal-title":"J. Proteom."},{"key":"ref_299","doi-asserted-by":"crossref","unstructured":"Roman-Ramos, H., and Ho, P.L. (2024). Current Technologies in Snake Venom Analysis and Applications. Toxins, 16.","DOI":"10.3390\/toxins16110458"},{"key":"ref_300","doi-asserted-by":"crossref","unstructured":"Mouchbahani-Constance, S., and Sharif-Naeini, R. (2021). Proteomic and Transcriptomic Techniques to Decipher the Molecular Evolution of Venoms. Toxins, 13.","DOI":"10.3390\/toxins13020154"},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1146\/annurev-animal-021419-083626","article-title":"Omics Technologies for Profiling Toxin Diversity and Evolution in Snake Venom: Impacts on the Discovery of Therapeutic and Diagnostic Agents","volume":"8","author":"Modahl","year":"2020","journal-title":"Annu. Rev. Anim. Biosci."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1016\/j.tips.2020.05.006","article-title":"Causes and Consequences of Snake Venom Variation","volume":"41","author":"Casewell","year":"2020","journal-title":"Trends Pharmacol. Sci."},{"key":"ref_303","doi-asserted-by":"crossref","unstructured":"Slagboom, J., Mladi\u0107, M., Xie, C., Kazandjian, T.D., Vonk, F., Somsen, G.W., Casewell, N.R., and Kool, J. (2020). High Throughput Screening and Identification of Coagulopathic Snake Venom Proteins and Peptides Using Nanofractionation and Proteomics Approaches. PLoS Negl. Trop. Dis., 14.","DOI":"10.1371\/journal.pntd.0007802"},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"117","DOI":"10.3390\/futurepharmacol2020009","article-title":"Snake Venom and 3D Microenvironment Cell Culture: From Production to Drug Development","volume":"2","author":"Kato","year":"2022","journal-title":"Future Pharmacol."},{"key":"ref_305","doi-asserted-by":"crossref","unstructured":"Bittenbinder, M.A., Capinha, L., Da Costa Pereira, D., Slagboom, J., van de Velde, B., Casewell, N.R., Jennings, P., Kool, J., and Vonk, F.J. (2023). Development of a High-Throughput in Vitro Screening Method for the Assessment of Cell-Damaging Activities of Snake Venoms. PLoS Negl. Trop. Dis., 17.","DOI":"10.1371\/journal.pntd.0011564"},{"key":"ref_306","doi-asserted-by":"crossref","unstructured":"Kadasah, S.F., Alrefaei, A.F., Abd Al Galil, F.M., and Alqahtani, A.M.S. (2025). Synergistic Antiproliferative and Pro-Apoptotic Effects of Prunus armeniaca and Bee Venom on Breast Cancer Cells. Front. Oncol., 15.","DOI":"10.3389\/fonc.2025.1647710"},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"189479","DOI":"10.1016\/j.bbcan.2025.189479","article-title":"Snake Venom-Derived Peptides as Anticancer Candidates: Pioneering next-Generation Therapies","volume":"1880","author":"Almeida","year":"2025","journal-title":"Biochim. Biophys. Acta-Rev. Cancer"},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"100118","DOI":"10.1016\/j.toxcx.2022.100118","article-title":"In Vitro and in Vivo Preclinical Venom Inhibition Assays Identify Metalloproteinase Inhibiting Drugs as Potential Future Treatments for Snakebite Envenoming by Dispholidus typus","volume":"14","author":"Menzies","year":"2022","journal-title":"Toxicon X"},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"108421","DOI":"10.1016\/j.toxicon.2025.108421","article-title":"Potential Inhibitors of Metalloproteinases (MMPs) and Phospholipases from Nemopilema nomurai Jellyfish Peptides: An in-Silico Pharmacokinetics and Molecular Docking Studies","volume":"263","author":"Danso","year":"2025","journal-title":"Toxicon"},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"44075","DOI":"10.1038\/s41598-025-27737-9","article-title":"Virtual Screening and Molecular Dynamics Studies of Antivenom Using Flavonoid Compounds Derived from Andrographis echioides","volume":"15","author":"Jeevitha","year":"2025","journal-title":"Sci. Rep."},{"key":"ref_311","first-page":"774","article-title":"In Silico Evaluation of Snake Venom Proteins against Multidrug-Resistant Mycobacterium tuberculosis: A Molecular Dynamics Study and Simulation Dynamic","volume":"15","author":"Fouda","year":"2025","journal-title":"Open Vet. J."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"100880","DOI":"10.1016\/j.imu.2022.100880","article-title":"Molecular Modeling in Drug Discovery","volume":"29","author":"Adelusi","year":"2022","journal-title":"Inform. Med. Unlocked"},{"key":"ref_313","doi-asserted-by":"crossref","unstructured":"Rivera-De-Torre, E., Rimbault, C., Jenkins, T.P., S\u00f8rensen, C.V., Damsbo, A., Saez, N.J., Duhoo, Y., Hackney, C.M., Ellgaard, L., and Laustsen, A.H. (2022). Strategies for Heterologous Expression, Synthesis, and Purification of Animal Venom Toxins. Front. Bioeng. Biotechnol., 9.","DOI":"10.3389\/fbioe.2021.811905"},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/S0041-0101(03)00047-3","article-title":"Functional Expression and Characterization of a Recombinant Phospholipase A2 from Sea Snake Lapemis hardwickii as a Soluble Protein in E. coli","volume":"41","author":"Yang","year":"2003","journal-title":"Toxicon"},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/j.cbpa.2009.03.003","article-title":"Recombinant Expression and Affinity Purification of Snake Venom Gland Parvalbumin in Escherichia coli","volume":"153","author":"Jia","year":"2009","journal-title":"Comp. Biochem. Physiol. A Mol. Integr. Physiol."},{"key":"ref_316","doi-asserted-by":"crossref","unstructured":"Abdel-Rahman, M.A., Cao, Z., El-Aziz, T.M.A., Strong, P.N., and Sabatier, J.-M. (2024). Editorial: Structural and functional venomics as a powerful approach for drug discovery and development. Front. Pharmacol., 15.","DOI":"10.3389\/fphar.2024.1405681"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"1329","DOI":"10.1021\/acs.jproteome.4c00923","article-title":"Categorization and Characterization of Snake Venom Variability through Intact Toxin Analysis by Mass Spectrometry","volume":"24","author":"Alonso","year":"2025","journal-title":"J. Proteome Res."},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/j.toxicon.2019.09.019","article-title":"Enzymatic Labelling of Snake Venom Phospholipase A2 Toxins","volume":"170","author":"Spolaore","year":"2019","journal-title":"Toxicon"},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"3904","DOI":"10.1021\/acs.jproteome.8b00568","article-title":"Combined Proteome and Toxicology Approach Reveals the Lethality of Venom Toxins from Jellyfish Cyanea nozakii","volume":"17","author":"Li","year":"2018","journal-title":"J. Proteome Res."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1111\/brv.12852","article-title":"Global genetic diversity status and trends: Towards a suite of Essential Biodiversity Variables (EBVs) for genetic composition","volume":"97","author":"Hoban","year":"2022","journal-title":"Biol. Rev."},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"e2313440121","DOI":"10.1073\/pnas.2313440121","article-title":"The Genetic Regulatory Architecture and Epigenomic Basis for Age-Related Changes in Rattlesnake Venom","volume":"121","author":"Hogan","year":"2024","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1159\/000092419","article-title":"Development of a Novel Recombinant Disintegrin, Contortrostatin, as an Effective Anti-Tumor and Anti-Angiogenic Agent","volume":"34","author":"Minea","year":"2006","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"596","DOI":"10.2174\/1570159X18666200114160844","article-title":"Pre-Clinical to Clinical Translational Failures and Current Status of Clinical Trials in Stroke Therapy: A Brief Review","volume":"18","author":"Dhir","year":"2020","journal-title":"Curr. Neuropharmacol."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"478","DOI":"10.5414\/CPP44478","article-title":"Ziconotide\u2014A Novel Neuron-Specific Calcium Channel Blocker for the Intrathecal Treatment of Severe Chronic Pain\u2014A Short Review","volume":"44","author":"Klotz","year":"2006","journal-title":"Int. J. Clin. Pharmacol. Ther."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"1084","DOI":"10.1592\/phco.2005.25.8.1084","article-title":"Ziconotide, an Intrathecally Administered N-Type Calcium Channel Antagonist for the Treatment of Chronic Pain","volume":"25","author":"Wermeling","year":"2005","journal-title":"Pharmacotherapy"},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"241","DOI":"10.2165\/00003088-198814040-00002","article-title":"Pharmacokinetics of Captopril in Healthy Subjects and in Patients with Cardiovascular Diseases","volume":"14","author":"Duchin","year":"1988","journal-title":"Clin. Pharmacokinet."},{"key":"ref_327","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1208\/s12248-014-9681-9","article-title":"Early Engineering Approaches to Improve Peptide Developability and Manufacturability","volume":"17","author":"Furman","year":"2014","journal-title":"AAPS J."},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/s41573-020-00114-z","article-title":"Natural Products in Drug Discovery: Advances and Opportunities","volume":"203","author":"Atanasov","year":"2021","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.sajb.2022.05.028","article-title":"Natural Bioactive Products as Promising Therapeutics: A Review of Natural Product-Based Drug Development","volume":"151","author":"Aware","year":"2022","journal-title":"S. Afr. J. Bot."},{"key":"ref_330","doi-asserted-by":"crossref","unstructured":"Ryan, R.Y.M., Seymour, J., Loukas, A., Lopez, J.A., Ikonomopoulou, M.P., and Miles, J.J. (2021). Immunological Responses to Envenomation. Front. Immunol., 12.","DOI":"10.3389\/fimmu.2021.661082"},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"6446","DOI":"10.1038\/s41467-025-60051-6","article-title":"Computational Exploration of Global Venoms for Antimicrobial Discovery with Venomics Artificial Intelligence","volume":"161","author":"Guan","year":"2025","journal-title":"Nat. Commun."},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"114784","DOI":"10.1016\/j.biopha.2023.114784","article-title":"Integrative Toxicogenomics: Advancing Precision Medicine and Toxicology through Artificial Intelligence and OMICs Technology","volume":"163","author":"Singh","year":"2023","journal-title":"Biomed. Pharmacother."},{"key":"ref_333","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1002\/pro.468","article-title":"Determination of the X-Ray Structure of the Snake Venom Protein Omwaprin by Total Chemical Synthesis and Racemic Protein Crystallography","volume":"19","author":"Banigan","year":"2010","journal-title":"Protein Sci. Publ. Protein Soc."},{"key":"ref_334","doi-asserted-by":"crossref","unstructured":"Alves, \u00c1.E.F., Barros, A.B.C., Silva, L.C.F., Carvalho, L.M.M., Pereira, G.M.A., Uch\u00f4a, A.F.C., Barbosa-Filho, J.M., Silva, M.S., Luna, K.P.O., and Soares, K.S.R. (2025). Emerging Trends in Snake Venom-Loaded Nanobiosystems for Advanced Medical Applications: A Comprehensive Overview. Pharmaceutics, 17.","DOI":"10.3390\/pharmaceutics17020204"},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"5551","DOI":"10.1016\/j.egyr.2025.05.021","article-title":"A Systematic Review of Artificial Intelligence and Machine Learning in Energy Sustainability: Research Topics and Trends","volume":"13","author":"Shahverdi","year":"2025","journal-title":"Energy Rep."},{"key":"ref_336","doi-asserted-by":"crossref","unstructured":"Xu, M., Kim, H., Yang, J., Fuentes, A., Meng, Y., Yoon, S., Kim, T., and Park, D.S. (2023). Embracing Limited and Imperfect Training Datasets: Opportunities and Challenges in Plant Disease Recognition Using Deep Learning. Front. Plant Sci., 14.","DOI":"10.3389\/fpls.2023.1225409"},{"key":"ref_337","doi-asserted-by":"crossref","unstructured":"Rossino, G., Marchese, E., Galli, G., Verde, F., Finizio, M., Serra, M., Linciano, P., Collina, S., Rossino, G., and Marchese, E. (2023). Peptides as Therapeutic Agents: Challenges and Opportunities in the Green Transition Era. Molecules, 28.","DOI":"10.3390\/molecules28207165"},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1007\/s00253-026-13850-w","article-title":"Molecular Engineering of Komagataella phaffii for Venom Toxin Production","volume":"110","author":"Cordeiro","year":"2026","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"11399","DOI":"10.1073\/pnas.1914536117","article-title":"Structural venomics reveals evolution of a complex venom by duplication and diversification of an ancient peptide-encoding gene","volume":"117","author":"Pineda","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_340","doi-asserted-by":"crossref","unstructured":"McCarthy, S., Robinson, J., Thalassinos, K., and Tabor, A.B. (2020). A Chemical Biology Approach to Probing the Folding Pathways of the Inhibitory Cystine Knot (ICK) Peptide ProTx-II. Front. Chem., 8.","DOI":"10.3389\/fchem.2020.00228"},{"key":"ref_341","doi-asserted-by":"crossref","unstructured":"Bhatwa, A., Wang, W., Hassan, Y.I., Abraham, N., Li, X.-Z., and Zhou, T. (2021). Challenges Associated with the Formation of Recombinant Protein Inclusion Bodies in Escherichia Coli and Strategies to Address Them for Industrial Applications. Front. Bioeng. Biotechnol., 9.","DOI":"10.3389\/fbioe.2021.630551"},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"2018","DOI":"10.1111\/j.1432-1033.2004.04115.x","article-title":"The First Representative of Glycosylated Three-Fingered Toxins. Cytotoxin from the Naja kaouthia Cobra Venom","volume":"271","author":"Osipov","year":"2004","journal-title":"Eur. J. Biochem."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"27106","DOI":"10.1074\/jbc.M112.366351","article-title":"Multiple Post-Translational Modifications Affect Heterologous Protein Synthesis","volume":"287","author":"Tokmakov","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"110778","DOI":"10.1016\/j.enzmictec.2025.110778","article-title":"Revolutionizing Recombinant Protein Production in Prokaryotic Platforms\u2014Methodologies and Advances","volume":"193","author":"Bhat","year":"2026","journal-title":"Enzym. Microb. Technol."},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"10061","DOI":"10.1021\/acs.iecr.8b00985","article-title":"The Coming Age of Insect Cells for Manufacturing and Development of Protein Therapeutics","volume":"57","author":"Yee","year":"2018","journal-title":"Ind. Eng. Chem. Res."},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"bbaf519","DOI":"10.1093\/bib\/bbaf519","article-title":"Computational Immunology in Venom Research: A Systematic Review of Epitope Prediction and Validation Approaches","volume":"26","author":"Zegrari","year":"2025","journal-title":"Brief. Bioinform."},{"key":"ref_347","doi-asserted-by":"crossref","first-page":"837","DOI":"10.13005\/bbra\/3408","article-title":"Exploring the Future of Medicine: A Comprehensive Review of Emerging Drug Technologies","volume":"22","author":"Vasantha","year":"2025","journal-title":"Biosci. Biotechnol. Res. Asia"},{"key":"ref_348","first-page":"167","article-title":"Machine Learning & Deep Learning Tools in Pharmaceutical Sciences: A Comprehensive Review","volume":"3","author":"Javid","year":"2025","journal-title":"Intell. Pharm."},{"key":"ref_349","doi-asserted-by":"crossref","first-page":"100015","DOI":"10.1016\/j.curpro.2025.100015","article-title":"Advances in Machine Learning for Optimizing Pharmaceutical Drug Discovery","volume":"22","author":"Ogbonna","year":"2025","journal-title":"Curr. Proteom."},{"key":"ref_350","doi-asserted-by":"crossref","unstructured":"Serrano, D.R., Luciano, F.C., Anaya, B.J., Ongoren, B., Kara, A., Molina, G., Ramirez, B.I., S\u00e1nchez-Guirales, S.A., Simon, J.A., and Tomietto, G. (2024). Artificial Intelligence (AI) Applications in Drug Discovery and Drug Delivery: Revolutionizing Personalized Medicine. Pharmaceutics, 16.","DOI":"10.3390\/pharmaceutics16101328"},{"key":"ref_351","doi-asserted-by":"crossref","unstructured":"Han, R., Yoon, H., Kim, G., Lee, H., Lee, Y., Han, R., Yoon, H., Kim, G., Lee, H., and Lee, Y. (2023). Revolutionizing Medicinal Chemistry: The Application of Artificial Intelligence (AI) in Early Drug Discovery. Pharmaceuticals, 16.","DOI":"10.3390\/ph16091259"},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1080\/17460441.2025.2465364","article-title":"The application of snake venom in anticancer drug discovery: An overview of the latest developments","volume":"20","author":"Mukherjee","year":"2025","journal-title":"Expert Opin. Drug Discov."},{"key":"ref_353","doi-asserted-by":"crossref","unstructured":"Romano, J.D., Li, H., Napolitano, T., Realubit, R., Karan, C., Holford, M., and Tatonetti, N.P. (2023). Discovering Venom-Derived Drug Candidates Using Differential Gene Expression. Toxins, 15.","DOI":"10.3390\/toxins15070451"},{"key":"ref_354","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/j.cpt.2025.03.005","article-title":"Arthropod Venom Peptides: Pioneering Nanotechnology in Cancer Treatment and Drug Delivery","volume":"4","author":"Ghodeif","year":"2025","journal-title":"Cancer Pathog. Ther."},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"106652","DOI":"10.1016\/j.jddst.2025.106652","article-title":"Beyond the Peril of Envenomation: A Nanotechnology Approach for Therapeutic Venom Delivery","volume":"105","author":"Soares","year":"2025","journal-title":"J. Drug Deliv. Sci. Technol."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/7\/286\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T04:18:23Z","timestamp":1783570703000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/18\/7\/286"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,30]]},"references-count":355,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2026,7]]}},"alternative-id":["toxins18070286"],"URL":"https:\/\/doi.org\/10.3390\/toxins18070286","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,30]]}}}