{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T12:16:43Z","timestamp":1793362603485,"version":"4.5.0"},"reference-count":194,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2022,11,27]],"date-time":"2022-11-27T00:00:00Z","timestamp":1669507200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2022,11,27]],"date-time":"2022-11-27T00:00:00Z","timestamp":1669507200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"crossref","award":["1154503"],"award-info":[{"award-number":["1154503"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100000925","name":"National Health and Medical Research Council","doi-asserted-by":"crossref","award":["1110343"],"award-info":[{"award-number":["1110343"]}],"id":[{"id":"10.13039\/501100000925","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Arch Toxicol"],"published-print":{"date-parts":[[2023,1]]},"DOI":"10.1007\/s00204-022-03420-0","type":"journal-article","created":{"date-parts":[[2022,11,27]],"date-time":"2022-11-27T16:31:58Z","timestamp":1669566718000},"page":"133-153","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":106,"title":["A current perspective on snake venom composition and constituent protein families"],"prefix":"10.1007","volume":"97","author":[{"given":"Theo","family":"Tasoulis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1519-7419","authenticated-orcid":false,"given":"Geoffrey K.","family":"Isbister","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2022,11,27]]},"reference":[{"issue":"1","key":"3420_CR1","doi-asserted-by":"publisher","first-page":"34","DOI":"10.1038\/s42003-018-0039-1","volume":"1","author":"S Ainsworth","year":"2018","unstructured":"Ainsworth S, Slagboom J, Alomran N et al (2018) The paraspecific neutralisation of snake venom induced coagulopathy by antivenoms. Commun Biol 1(1):34. https:\/\/doi.org\/10.1038\/s42003-018-0039-1","journal-title":"Commun Biol"},{"key":"3420_CR2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ejphar.2021.174022","volume":"899","author":"B Akhtar","year":"2021","unstructured":"Akhtar B, Muhammad F, Sharif A, Anwar MI (2021) Mechanistic insights of snake venom disintegrins in cancer treatment. Eur J Pharmacol 899:174022. https:\/\/doi.org\/10.1016\/j.ejphar.2021.174022","journal-title":"Eur J Pharmacol"},{"issue":"1","key":"3420_CR3","doi-asserted-by":"publisher","first-page":"217","DOI":"10.1007\/s00268-010-0686-y","volume":"35","author":"SA Antoniou","year":"2011","unstructured":"Antoniou SA, Antoniou GA, Learney R, Granderath FA, Antoniou AI (2011) The rod and the serpent: history\u2019s ultimate healing symbol. World J Surg 35(1):217\u2013221. https:\/\/doi.org\/10.1007\/s00268-010-0686-y","journal-title":"World J Surg"},{"issue":"6","key":"3420_CR4","doi-asserted-by":"publisher","first-page":"532","DOI":"10.2174\/1389203716666150515125002","volume":"16","author":"JK Arruda Mac\u00eado","year":"2015","unstructured":"Arruda Mac\u00eado JK, Fox JW, de Souza CM (2015) Disintegrins from snake venoms and their applications in cancer research and therapy. Curr Protein Pept Sci 16(6):532\u2013548. https:\/\/doi.org\/10.2174\/1389203716666150515125002","journal-title":"Curr Protein Pept Sci"},{"issue":"4","key":"3420_CR5","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1038\/hdy.2014.65","volume":"115","author":"F Aubret","year":"2015","unstructured":"Aubret F (2015) Island colonisation and the evolutionary rates of body size in insular neonate snakes. Heredity 115(4):349\u2013356. https:\/\/doi.org\/10.1038\/hdy.2014.65","journal-title":"Heredity"},{"issue":"2","key":"3420_CR6","doi-asserted-by":"publisher","first-page":"6406","DOI":"10.1016\/j.matpr.2017.12.252","volume":"5","author":"E Bala","year":"2018","unstructured":"Bala E, Hazarika R, Singh P, Yasir M, Shrivastava R (2018) A biological overview of hyaluronidase: a venom enzyme and its inhibition with plants materials. Mater Today 5(2):6406\u20136412. https:\/\/doi.org\/10.1016\/j.matpr.2017.12.252","journal-title":"Mater Today"},{"issue":"9","key":"3420_CR7","doi-asserted-by":"publisher","first-page":"1964","DOI":"10.1093\/molbev\/msz125","volume":"36","author":"A Barua","year":"2019","unstructured":"Barua A, Mikheyev AS (2019) Many options, few solutions: over 60 my snakes converged on a few optimal venom formulations. Mol Biol Evol 36(9):1964\u20131974. https:\/\/doi.org\/10.1093\/molbev\/msz125","journal-title":"Mol Biol Evol"},{"issue":"5","key":"3420_CR8","doi-asserted-by":"publisher","first-page":"547","DOI":"10.1016\/0041-0101(87)90290-x","volume":"25","author":"AW Bernheimer","year":"1987","unstructured":"Bernheimer AW, Linder R, Weinstein SA, Kim KS (1987) Isolation and characterization of a phospholipase B from venom of collett\u2019s snake. Pseudechis Colletti Toxicon 25(5):547\u2013554. https:\/\/doi.org\/10.1016\/0041-0101(87)90290-x","journal-title":"Pseudechis Colletti Toxicon"},{"key":"3420_CR9","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbagen.2016.12.022","author":"J Boldrini-Fran\u00e7a","year":"2017","unstructured":"Boldrini-Fran\u00e7a J, Cologna CT, Pucca MB et al (2017) Minor snake venom proteins Structure function and potential applications. General Subjects. https:\/\/doi.org\/10.1016\/j.bbagen.2016.12.022","journal-title":"General Subjects"},{"issue":"6","key":"3420_CR10","doi-asserted-by":"publisher","first-page":"1865","DOI":"10.1007\/s00204-021-03066-4","volume":"95","author":"HM Bolt","year":"2021","unstructured":"Bolt HM (2021) New aspects in snake venom toxicology. Arch Toxicol 95(6):1865\u20131866. https:\/\/doi.org\/10.1007\/s00204-021-03066-4","journal-title":"Arch Toxicol"},{"issue":"12","key":"3420_CR11","doi-asserted-by":"publisher","first-page":"2740","DOI":"10.1016\/j.biochi.2012.08.014","volume":"94","author":"KCF Bordon","year":"2012","unstructured":"Bordon KCF, Perino MG, Giglio JR, Arantes EC (2012) Isolation, enzymatic characterization and antiedematogenic activity of the first reported rattlesnake hyaluronidase from crotalus durissus terrificus venom. Biochimie 94(12):2740\u20132748. https:\/\/doi.org\/10.1016\/j.biochi.2012.08.014","journal-title":"Biochimie"},{"key":"3420_CR12","first-page":"455","volume":"282","author":"J Bryan","year":"2009","unstructured":"Bryan J (2009) From snake venom to ACE inhibitor the discovery and rise of captopril. Pharm J 282:455\u2013456","journal-title":"Pharm J"},{"issue":"Pt 3","key":"3420_CR13","doi-asserted-by":"publisher","first-page":"725","DOI":"10.1042\/BJ20021739","volume":"372","author":"JJ Calvete","year":"2003","unstructured":"Calvete JJ, Moreno-Murciano MP, Theakston RD, Kisiel DG, Marcinkiewicz C (2003) Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering. Biochem J 372(Pt 3):725\u2013734. https:\/\/doi.org\/10.1042\/BJ20021739","journal-title":"Biochem J"},{"issue":"8","key":"3420_CR14","doi-asserted-by":"publisher","first-page":"1063","DOI":"10.1016\/j.toxicon.2005.02.024","volume":"45","author":"JJ Calvete","year":"2005","unstructured":"Calvete JJ, Marcinkiewicz C, Monle\u00f3n D et al (2005) Snake venom disintegrins: evolution of structure and function. Toxicon 45(8):1063\u20131074. https:\/\/doi.org\/10.1016\/j.toxicon.2005.02.024","journal-title":"Toxicon"},{"issue":"8","key":"3420_CR15","doi-asserted-by":"publisher","first-page":"570","DOI":"10.1016\/j.tips.2020.05.006","volume":"41","author":"NR Casewell","year":"2020","unstructured":"Casewell NR, Jackson TNW, Laustsen AH, Sunagar K (2020) Causes and consequences of snake venom variation. Trend Pharmacol Sci 41(8):570\u2013581. https:\/\/doi.org\/10.1016\/j.tips.2020.05.006","journal-title":"Trend Pharmacol Sci"},{"issue":"1","key":"3420_CR16","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1016\/j.cbpb.2004.11.012","volume":"140","author":"AL Cecchini","year":"2005","unstructured":"Cecchini AL, Marcussi S, Silveira LB et al (2005) Biological and enzymatic activities of Micrurus sp (Coral) snake venoms. Comp Biochem Physiol A Mol Integr Physiol 140(1):125\u2013134. https:\/\/doi.org\/10.1016\/j.cbpb.2004.11.012","journal-title":"Comp Biochem Physiol A Mol Integr Physiol"},{"issue":"17","key":"3420_CR17","doi-asserted-by":"publisher","first-page":"3121","DOI":"10.1111\/j.1742-4658.2012.08691.x","volume":"279","author":"L Cendron","year":"2012","unstructured":"Cendron L, Mi\u010deti\u0107 I, Polverino de Laureto P, Paoli M (2012) Structural analysis of trimeric phospholipase A2 neurotoxin from the Australian taipan snake venom. FEBS J 279(17):3121\u20133135. https:\/\/doi.org\/10.1111\/j.1742-4658.2012.08691.x","journal-title":"FEBS J"},{"key":"3420_CR18","doi-asserted-by":"publisher","first-page":"224","DOI":"10.1016\/j.ijbiomac.2020.05.106","volume":"160","author":"A Chanda","year":"2020","unstructured":"Chanda A, Mukherjee AK (2020) Quantitative proteomics to reveal the composition of Southern India spectacled cobra (Naja naja) venom and its immunological cross-reactivity towards commercial antivenom. Int J Biol Macromol 160:224\u2013232. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.05.106","journal-title":"Int J Biol Macromol"},{"issue":"3","key":"3420_CR19","doi-asserted-by":"publisher","first-page":"551","DOI":"10.1111\/j.1476-5381.1978.tb07811.x","volume":"63","author":"CC Chang","year":"1978","unstructured":"Chang CC, Tseng KH (1978) Effect of crotamine, a toxin of South American rattlesnake venom, on the sodium channel of murine skeletal muscle. Br J Pharmacol 63(3):551\u2013559. https:\/\/doi.org\/10.1111\/j.1476-5381.1978.tb07811.x","journal-title":"Br J Pharmacol"},{"issue":"1","key":"3420_CR20","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/0006-8993(83)90902-2","volume":"277","author":"VA Chiappinelli","year":"1983","unstructured":"Chiappinelli VA (1983) Kappa-Bungarotoxin: a probe for the neuronal nicotinic receptor in the avian ciliary ganglion. Brain Res 277(1):9\u201322. https:\/\/doi.org\/10.1016\/0006-8993(83)90902-2","journal-title":"Brain Res"},{"key":"3420_CR21","doi-asserted-by":"publisher","first-page":"33","DOI":"10.1016\/j.toxicon.2017.06.005","volume":"135","author":"M Choudhury","year":"2017","unstructured":"Choudhury M, McCleary RJR, Kesherwani M, Kini RM, Velmurugan D (2017) Comparison of proteomic profiles of the venoms of two of the \u2018Big Four\u2019 snakes of India, the Indian cobra (Naja naja) and the common krait (Bungarus caeruleus), and analyses of their toxins. Toxicon 135:33\u201342. https:\/\/doi.org\/10.1016\/j.toxicon.2017.06.005","journal-title":"Toxicon"},{"issue":"11\u201312","key":"3420_CR22","doi-asserted-by":"publisher","first-page":"696","DOI":"10.5694\/j.1326-5377.2010.tb04108.x","volume":"193","author":"A Churchman","year":"2010","unstructured":"Churchman A, O\u2019Leary MA, Buckley NA et al (2010) Clinical effects of red-bellied black snake (Pseudechis porphyriacus) envenoming and correlation with venom concentrations: Australian Snakebite Project (ASP-11). Med J Aust 193(11\u201312):696\u2013700. https:\/\/doi.org\/10.5694\/j.1326-5377.2010.tb04108.x","journal-title":"Med J Aust"},{"issue":"3","key":"3420_CR23","doi-asserted-by":"publisher","first-page":"330","DOI":"10.1016\/j.toxicon.2008.12.004","volume":"53","author":"P Ciscotto","year":"2009","unstructured":"Ciscotto P, Machado de Avila RA, Coelho EAF et al (2009) Antigenic, microbicidal and antiparasitic properties of an l-amino acid oxidase isolated from Bothrops jararaca snake venom. Toxicon 53(3):330\u2013341. https:\/\/doi.org\/10.1016\/j.toxicon.2008.12.004","journal-title":"Toxicon"},{"issue":"11","key":"3420_CR24","doi-asserted-by":"publisher","first-page":"2655","DOI":"10.1016\/j.peptides.2006.06.003","volume":"27","author":"C Clarke","year":"2006","unstructured":"Clarke C, Kuruppu S, Reeve S, Ian Smith A, Hodgson WC (2006) Oxylepitoxin-1, a reversible neurotoxin from the venom of the inland taipan (Oxyuranus microlepidotus). Peptides 27(11):2655\u20132660. https:\/\/doi.org\/10.1016\/j.peptides.2006.06.003","journal-title":"Peptides"},{"issue":"7","key":"3420_CR25","doi-asserted-by":"publisher","first-page":"1236","DOI":"10.1016\/j.toxicon.2010.03.011","volume":"56","author":"KJ Clemetson","year":"2010","unstructured":"Clemetson KJ (2010) Snaclecs (snake C-type lectins) that inhibit or activate platelets by binding to receptors. Toxicon 56(7):1236\u20131246. https:\/\/doi.org\/10.1016\/j.toxicon.2010.03.011","journal-title":"Toxicon"},{"issue":"2","key":"3420_CR26","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1111\/j.1538-7836.2008.03233.x","volume":"7","author":"KJ Clemetson","year":"2009","unstructured":"Clemetson KJ, Morita T, Manjunatha Kini R (2009) Scientific and standardization committee communications: classification and nomenclature of snake venom C-type lectins and related proteins. J Thromb Haemost 7(2):360. https:\/\/doi.org\/10.1111\/j.1538-7836.2008.03233.x","journal-title":"J Thromb Haemost"},{"key":"3420_CR27","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1186\/1678-9199-20-23","volume":"20","author":"T Costa","year":"2014","unstructured":"Costa T, Burin S, Menaldo D, de Atti\u00e9 F, Sampaio S (2014) Snake venom L-amino acid oxidases: An overview on their antitumor effects. Journal Venom Animal Tox Includ Trop Diseases 20:23. https:\/\/doi.org\/10.1186\/1678-9199-20-23","journal-title":"Journal Venom Animal Tox Includ Trop Diseases"},{"key":"3420_CR28","doi-asserted-by":"crossref","unstructured":"Daltry JC, Wuster W, Thorpe RS (1997) The role of ecology in determining venom variation in the Malayan pitviper, Calloselasma rhodostoma. Venomous Snakes: Ecology, Evolution and Snakebite: Symposia of the Zoological Society of London No.70, Pp. 155-171. Clarendon Press, Oxford","DOI":"10.2307\/1447318"},{"issue":"3","key":"3420_CR29","doi-asserted-by":"publisher","first-page":"446","DOI":"10.1111\/bcp.12739","volume":"81","author":"HA de Silva","year":"2016","unstructured":"de Silva HA, Ryan NM, de Silva HJ (2016a) Adverse reactions to snake antivenom, and their prevention and treatment. Br J Clin Pharmacol 81(3):446\u2013452. https:\/\/doi.org\/10.1111\/bcp.12739","journal-title":"Br J Clin Pharmacol"},{"issue":"18","key":"3420_CR30","doi-asserted-by":"publisher","first-page":"2434","DOI":"10.1016\/j.cub.2016.07.038","volume":"26","author":"NL Dowell","year":"2016","unstructured":"Dowell NL, Giorgianni MW, Kassner VA, Selegue JE, Sanchez EE, Carroll SB (2016) The Deep origin and recent loss of venom toxin genes in rattlesnakes. Curr Biol 26(18):2434\u20132445. https:\/\/doi.org\/10.1016\/j.cub.2016.07.038","journal-title":"Curr Biol"},{"issue":"18","key":"3420_CR31","doi-asserted-by":"publisher","first-page":"13315","DOI":"10.1074\/jbc.R109.076596","volume":"285","author":"S Dutertre","year":"2010","unstructured":"Dutertre S, Lewis RJ (2010) Use of venom peptides to probe ion channel structure and function. J Biol Chem 285(18):13315\u201313320. https:\/\/doi.org\/10.1074\/jbc.R109.076596","journal-title":"J Biol Chem"},{"key":"3420_CR32","doi-asserted-by":"publisher","DOI":"10.3390\/tropicalmed3030104","author":"VE Erulu","year":"2018","unstructured":"Erulu VE, Okumu MO, Ochola FO, Gikunju JK (2018) Revered but poorly understood: a case report of dendroaspis polylepis (black mamba) envenomation in watamu, malindi kenya, and a review of the literature. Trop Med Infect Dis. https:\/\/doi.org\/10.3390\/tropicalmed3030104","journal-title":"Trop Med Infect Dis"},{"issue":"1","key":"3420_CR33","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1016\/S1046-5928(03)00053-6","volume":"30","author":"LF Felicori","year":"2003","unstructured":"Felicori LF, Souza CT, Velarde DT et al (2003) Kallikrein-like proteinase from bushmaster snake venom. Protein Expr Purif 30(1):32\u201342. https:\/\/doi.org\/10.1016\/S1046-5928(03)00053-6","journal-title":"Protein Expr Purif"},{"issue":"1","key":"3420_CR34","doi-asserted-by":"publisher","first-page":"163","DOI":"10.1111\/j.1476-5381.1965.tb02091.x","volume":"24","author":"SH Ferreira","year":"1965","unstructured":"Ferreira SH (1965) A bradykinin-potentiating factor (bpf) present in the venom of bothrops jararca. Br J Pharmacol Chemother 24(1):163\u2013169. https:\/\/doi.org\/10.1111\/j.1476-5381.1965.tb02091.x","journal-title":"Br J Pharmacol Chemother"},{"key":"3420_CR35","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/j.cytogfr.2021.05.003","volume":"60","author":"IG Ferreira","year":"2021","unstructured":"Ferreira IG, Pucca MB, Oliveira ISd, Cerni FA, Jacob BdCdS, Arantes EC (2021) Snake venom vascular endothelial growth factors (svVEGFs): Unravelling their molecular structure, functions, and research potential. Cytokine Growth Factor Rev 60:133\u2013143. https:\/\/doi.org\/10.1016\/j.cytogfr.2021.05.003","journal-title":"Cytokine Growth Factor Rev"},{"key":"3420_CR36","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1016\/j.toxicon.2012.09.009","volume":"62","author":"JW Fox","year":"2013","unstructured":"Fox JW (2013) A brief review of the scientific history of several lesser-known snake venom proteins: l-amino acid oxidases, hyaluronidases and phosphodiesterases. Toxicon 62:75\u201382. https:\/\/doi.org\/10.1016\/j.toxicon.2012.09.009","journal-title":"Toxicon"},{"key":"3420_CR37","volume-title":"Venomous reptiles and their toxins","author":"BG Fry","year":"2015","unstructured":"Fry BG (2015) Venomous reptiles and their toxins. Oxford University Press, New York"},{"issue":"1","key":"3420_CR38","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1081\/TXR-120019018","volume":"22","author":"BG Fry","year":"2003","unstructured":"Fry BG, Winkel KD, Wickramaratna JC, Hodgson WC, W\u00fcster W (2003) Effectiveness of snake antivenom: species and regional venom variation and its clinical impact. J Toxicol Toxin Review 22(1):23\u201334. https:\/\/doi.org\/10.1081\/TXR-120019018","journal-title":"J Toxicol Toxin Review"},{"issue":"3\u20136","key":"3420_CR39","doi-asserted-by":"publisher","first-page":"266","DOI":"10.1159\/000048072","volume":"31","author":"PM Gempeler-Messina","year":"2001","unstructured":"Gempeler-Messina PM, Volz K, B\u00fchler B, M\u00fcller C (2001) Protein c activators from snake venoms and their diagnostic use. Pathophysiol Haemost Thromb 31(3\u20136):266\u2013272. https:\/\/doi.org\/10.1159\/000048072","journal-title":"Pathophysiol Haemost Thromb"},{"issue":"1","key":"3420_CR40","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1021\/acs.jproteome.0c00687","volume":"20","author":"P Ghezellou","year":"2021","unstructured":"Ghezellou P, Albuquerque W, Garikapati V et al (2021) Integrating top-down and bottom-up mass spectrometric strategies for proteomic profiling of iranian saw-scaled viper, echis carinatus sochureki. Venom J Prot Res 20(1):895\u2013908. https:\/\/doi.org\/10.1021\/acs.jproteome.0c00687","journal-title":"Venom J Prot Res"},{"issue":"20","key":"3420_CR41","doi-asserted-by":"publisher","first-page":"10911","DOI":"10.1073\/pnas.1920011117","volume":"117","author":"MW Giorgianni","year":"2020","unstructured":"Giorgianni MW, Dowell NL, Griffin S, Kassner VA, Selegue JE, Carroll SB (2020) The origin and diversification of a novel protein family in venomous snakes. Proc Natl Acad Sci 117(20):10911\u201310920. https:\/\/doi.org\/10.1073\/pnas.1920011117","journal-title":"Proc Natl Acad Sci"},{"key":"3420_CR42","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2020.103707","volume":"218","author":"J Giribaldi","year":"2020","unstructured":"Giribaldi J, Kazandjian T, Amorim FG et al (2020) Venomics of the asp viper vipera aspis aspis from France. J Proteomics 218:103707. https:\/\/doi.org\/10.1016\/j.jprot.2020.103707","journal-title":"J Proteomics"},{"key":"3420_CR43","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/j.jprot.2015.04.029","volume":"135","author":"L Goncalves-Machado","year":"2016","unstructured":"Goncalves-Machado L, Pla D, Sanz L et al (2016) Combined venomics, venom gland transcriptomics, bioactivities, and antivenomics of two bothrops jararaca populations from geographic isolated regions within the brazilian Atlantic rainforest. J Proteomics 135:73\u201389. https:\/\/doi.org\/10.1016\/j.jprot.2015.04.029","journal-title":"J Proteomics"},{"issue":"4","key":"3420_CR44","doi-asserted-by":"publisher","first-page":"796","DOI":"10.1093\/biolinnean\/blz003","volume":"126","author":"DJ Gower","year":"2019","unstructured":"Gower DJ, Sampaio FL, Peichl L et al (2019) Evolution of the eyes of vipers with and without infrared-sensing pit organs. Biol J Lin Soc 126(4):796\u2013823. https:\/\/doi.org\/10.1093\/biolinnean\/blz003","journal-title":"Biol J Lin Soc"},{"issue":"2","key":"3420_CR45","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1016\/j.jprot.2009.01.008","volume":"72","author":"JM Guti\u00e9rrez","year":"2009","unstructured":"Guti\u00e9rrez JM, Lomonte B, Le\u00f3n G et al (2009) Snake venomics and antivenomics: proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming. J Proteomics 72(2):165\u2013182. https:\/\/doi.org\/10.1016\/j.jprot.2009.01.008","journal-title":"J Proteomics"},{"issue":"3","key":"3420_CR46","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/j.biologicals.2011.02.005","volume":"39","author":"JM Guti\u00e9rrez","year":"2011","unstructured":"Guti\u00e9rrez JM, Le\u00f3n G, Burnouf T (2011) Antivenoms for the treatment of snakebite envenomings: The road ahead. Biologicals 39(3):129\u2013142. https:\/\/doi.org\/10.1016\/j.biologicals.2011.02.005","journal-title":"Biologicals"},{"issue":"1","key":"3420_CR47","doi-asserted-by":"publisher","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","volume":"3","author":"JM Guti\u00e9rrez","year":"2017","unstructured":"Guti\u00e9rrez JM, Calvete JJ, Habib AG, Harrison RA, Williams DJ, Warrell DA (2017) Snakebite Envenoming. Nat Rev Dis Primers 3(1):17063. https:\/\/doi.org\/10.1038\/nrdp.2017.63","journal-title":"Nat Rev Dis Primers"},{"issue":"8","key":"3420_CR48","doi-asserted-by":"publisher","first-page":"2088","DOI":"10.1093\/gbe\/evu166","volume":"6","author":"AD Hargreaves","year":"2014","unstructured":"Hargreaves AD, Swain MT, Hegarty MJ, Logan DW, Mulley JF (2014) Restriction and recruitment\u2014gene duplication and the origin and evolution of snake venom toxins. Genome Biol Evol 6(8):2088\u20132095","journal-title":"Genome Biol Evol"},{"issue":"9","key":"3420_CR49","doi-asserted-by":"publisher","first-page":"1768","DOI":"10.1016\/j.jprot.2011.06.019","volume":"74","author":"RA Harrison","year":"2011","unstructured":"Harrison RA, Cook DA, Renjifo C, Casewell NR, Currier RB, Wagstaff SC (2011) Research strategies to improve snakebite treatment: Challenges and progress. J Proteomics 74(9):1768\u20131780. https:\/\/doi.org\/10.1016\/j.jprot.2011.06.019","journal-title":"J Proteomics"},{"issue":"6","key":"3420_CR50","doi-asserted-by":"publisher","first-page":"604","DOI":"10.3109\/15563650.2014.914526","volume":"52","author":"AJ Hart","year":"2014","unstructured":"Hart AJ, Hodgson WC, O\u2019Leary M, Isbister GK (2014) Pharmacokinetics and pharmacodynamics of the myotoxic venom of Pseudechis australis (mulga snake) in the anesthetised rat. Clin Toxicol (phila) 52(6):604\u2013610. https:\/\/doi.org\/10.3109\/15563650.2014.914526","journal-title":"Clin Toxicol (phila)"},{"issue":"1","key":"3420_CR51","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/S0306-3623(96)00173-5","volume":"28","author":"AL Harvey","year":"1997","unstructured":"Harvey AL (1997) Recent studies on dendrotoxins and potassium ion channels. General Pharmacol 28(1):7\u201312. https:\/\/doi.org\/10.1016\/S0306-3623(96)00173-5","journal-title":"General Pharmacol"},{"issue":"1","key":"3420_CR52","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1016\/S0041-0101(00)00162-8","volume":"39","author":"AL Harvey","year":"2001","unstructured":"Harvey AL (2001) Twenty years of dendrotoxins. Toxicon 39(1):15\u201326. https:\/\/doi.org\/10.1016\/S0041-0101(00)00162-8","journal-title":"Toxicon"},{"key":"3420_CR53","doi-asserted-by":"publisher","first-page":"3065","DOI":"10.2174\/0929867043363820","volume":"11","author":"A Harvey","year":"2005","unstructured":"Harvey A, Robertson B (2005) Dendrotoxins: structure-activity relationships and effects on potassium ion channels. Curr Med Chem 11:3065\u20133072. https:\/\/doi.org\/10.2174\/0929867043363820","journal-title":"Curr Med Chem"},{"issue":"9550","key":"3420_CR54","doi-asserted-by":"publisher","first-page":"1871","DOI":"10.1016\/s0140-6736(06)69776-6","volume":"368","author":"MG Hennerici","year":"2006","unstructured":"Hennerici MG, Kay R, Bogousslavsky J, Lenzi GL, Verstraete M, Orgogozo JM (2006) Intravenous ancrod for acute ischaemic stroke in the European stroke treatment with ancrod trial: a randomised controlled trial. Lancet 368(9550):1871\u20131878. https:\/\/doi.org\/10.1016\/s0140-6736(06)69776-6","journal-title":"Lancet"},{"key":"3420_CR55","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxcx.2022.100123","volume":"14","author":"JJ Hiu","year":"2022","unstructured":"Hiu JJ, Yap MKK (2022) The myth of cobra venom cytotoxin: More than just direct cytolytic actions. Toxicon X 14:100123. https:\/\/doi.org\/10.1016\/j.toxcx.2022.100123","journal-title":"Toxicon X"},{"issue":"37","key":"3420_CR56","doi-asserted-by":"publisher","first-page":"13117","DOI":"10.1073\/pnas.0504184102","volume":"102","author":"K-F Huang","year":"2005","unstructured":"Huang K-F, Liu Y-L, Cheng W-J, Ko T-P, Wang AH-J (2005) Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation. Proc Natl Acad Sci 102(37):13117\u201313122. https:\/\/doi.org\/10.1073\/pnas.0504184102","journal-title":"Proc Natl Acad Sci"},{"key":"3420_CR57","doi-asserted-by":"publisher","DOI":"10.3390\/toxins14040277","author":"TM Huynh","year":"2022","unstructured":"Huynh TM, Hodgson WC, Isbister GK, Silva A (2022) The Effect of Australian and Asian Commercial Antivenoms in Reversing the Post-Synaptic Neurotoxicity of O hannah N naja and N kaouthia Venoms In Vitro. Toxins. https:\/\/doi.org\/10.3390\/toxins14040277","journal-title":"Toxins"},{"issue":"4","key":"3420_CR58","doi-asserted-by":"publisher","first-page":"444","DOI":"10.1055\/s-0030-1254053","volume":"36","author":"GK Isbister","year":"2010","unstructured":"Isbister GK (2010) Snakebite doesn\u2019t cause disseminated intravascular coagulation: coagulopathy and thrombotic microangiopathy in snake envenoming. Semin Thromb Hemost 36(4):444\u2013451. https:\/\/doi.org\/10.1055\/s-0030-1254053","journal-title":"Semin Thromb Hemost"},{"issue":"3","key":"3420_CR59","doi-asserted-by":"publisher","first-page":"798","DOI":"10.1016\/j.vaccine.2009.10.055","volume":"28","author":"GK Isbister","year":"2010","unstructured":"Isbister GK, O\u2019Leary MA, Hagan J et al (2010a) Cross-neutralisation of Australian brown snake, taipan and death adder venoms by monovalent antibodies. Vaccine 28(3):798\u2013802. https:\/\/doi.org\/10.1016\/j.vaccine.2009.10.055","journal-title":"Vaccine"},{"issue":"11","key":"3420_CR60","doi-asserted-by":"publisher","first-page":"2504","DOI":"10.1111\/j.1538-7836.2010.04050.x","volume":"8","author":"GK Isbister","year":"2010","unstructured":"Isbister GK, Scorgie FE, O\u2019Leary MA, Seldon M, Brown SG, Lincz LF (2010b) Factor deficiencies in venom-induced consumption coagulopathy resulting from Australian elapid envenomation: Australian Snakebite Project (ASP-10). J Thromb Haemost 8(11):2504\u20132513. https:\/\/doi.org\/10.1111\/j.1538-7836.2010.04050.x","journal-title":"J Thromb Haemost"},{"key":"3420_CR61","doi-asserted-by":"publisher","first-page":"286","DOI":"10.1016\/j.toxicon.2014.08.071","volume":"90","author":"GK Isbister","year":"2014","unstructured":"Isbister GK, Maduwage K, Page CB (2014) Antivenom cross neutralisation in a suspected Asian pit viper envenoming causing severe coagulopathy. Toxicon 90:286\u2013290. https:\/\/doi.org\/10.1016\/j.toxicon.2014.08.071","journal-title":"Toxicon"},{"issue":"11","key":"3420_CR62","doi-asserted-by":"publisher","first-page":"459","DOI":"10.3390\/biomedicines8110459","volume":"8","author":"GK Isbister","year":"2020","unstructured":"Isbister GK, Mirajkar N, Fakes K, Brown SGA, Veerati PC (2020) Phospholipase A2 (PLA2) as an early indicator of envenomation in australian elapid snakebites (ASP-27). Biomedicines 8(11):459","journal-title":"Biomedicines"},{"issue":"1","key":"3420_CR63","doi-asserted-by":"publisher","first-page":"82","DOI":"10.1016\/0006-8993(85)91097-2","volume":"346","author":"Y Ishikawa","year":"1985","unstructured":"Ishikawa Y, Kano M, Tamiya N, Shimada Y (1985) Acetylcholine receptors of human skeletal muscle: a species difference detected by snake neurotoxins. Brain Res 346(1):82\u201388. https:\/\/doi.org\/10.1016\/0006-8993(85)91097-2","journal-title":"Brain Res"},{"issue":"6","key":"3420_CR64","doi-asserted-by":"publisher","first-page":"463","DOI":"10.1080\/14789450.2021.1941892","volume":"18","author":"T Islam","year":"2021","unstructured":"Islam T, Madhubala D, Mukhopadhyay R, Mukherjee AK (2021) Transcriptomic and functional proteomics analyses to unveil the common and unique pathway(s) of neuritogenesis induced by Russell\u2019s viper venom nerve growth factor in rat pheochromocytoma neuronal cells. Expert Rev Proteomics 18(6):463\u2013481. https:\/\/doi.org\/10.1080\/14789450.2021.1941892","journal-title":"Expert Rev Proteomics"},{"issue":"5","key":"3420_CR65","doi-asserted-by":"publisher","first-page":"300","DOI":"10.3390\/toxins14050300","volume":"14","author":"A Isomoto","year":"2022","unstructured":"Isomoto A, Shoguchi E, Hisata K et al (2022) Active expression of genes for protein modification enzymes in habu venom glands. Toxins 14(5):300","journal-title":"Toxins"},{"key":"3420_CR66","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/196754","volume":"2014","author":"LF Izidoro","year":"2014","unstructured":"Izidoro LF, Sobrinho JC, Mendes MM et al (2014) Snake venom L-amino acid oxidases: trends in pharmacology and biochemistry. Biomed Res Int 2014:196754. https:\/\/doi.org\/10.1155\/2014\/196754","journal-title":"Biomed Res Int"},{"issue":"1","key":"3420_CR67","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1007\/s00435-016-0332-9","volume":"136","author":"TNW Jackson","year":"2017","unstructured":"Jackson TNW, Young B, Underwood G et al (2017) Endless forms most beautiful: the evolution of ophidian oral glands, including the venom system, and the use of appropriate terminology for homologous structures. Zoomorphology 136(1):107\u2013130. https:\/\/doi.org\/10.1007\/s00435-016-0332-9","journal-title":"Zoomorphology"},{"key":"3420_CR68","doi-asserted-by":"publisher","first-page":"285","DOI":"10.1016\/j.jprot.2014.01.004","volume":"105","author":"C Jesupret","year":"2014","unstructured":"Jesupret C, Baumann K, Jackson TNW et al (2014) Vintage venoms: Proteomic and pharmacological stability of snake venoms stored for up to eight decades. J Proteomics 105:285\u2013294. https:\/\/doi.org\/10.1016\/j.jprot.2014.01.004","journal-title":"J Proteomics"},{"issue":"7","key":"3420_CR69","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1080\/15563650.2020.1836377","volume":"59","author":"CI Johnston","year":"2021","unstructured":"Johnston CI, Isbister GK (2021) Australian snakebite myotoxicity (ASP-23). Clin Toxicol 59(7):611\u2013618. https:\/\/doi.org\/10.1080\/15563650.2020.1836377","journal-title":"Clin Toxicol"},{"issue":"5","key":"3420_CR70","doi-asserted-by":"publisher","first-page":"417","DOI":"10.3109\/15563650.2013.787535","volume":"51","author":"CI Johnston","year":"2013","unstructured":"Johnston CI, Brown SGA, O\u2019Leary MA et al (2013) Mulga snake (Pseudechis australis) envenoming: a spectrum of myotoxicity, anticoagulant coagulopathy, haemolysis and the role of early antivenom therapy \u2013 Australian Snakebite Project (ASP-19). Clin Toxicol 51(5):417\u2013424. https:\/\/doi.org\/10.3109\/15563650.2013.787535","journal-title":"Clin Toxicol"},{"issue":"3","key":"3420_CR71","doi-asserted-by":"publisher","first-page":"119","DOI":"10.5694\/mja17.00094","volume":"207","author":"CI Johnston","year":"2017","unstructured":"Johnston CI, Ryan NM, Page CB et al (2017b) The australian snakebite project, 2005\u20132015 (ASP-20). Med J Aust 207(3):119\u2013125. https:\/\/doi.org\/10.5694\/mja17.00094","journal-title":"Med J Aust"},{"key":"3420_CR72","doi-asserted-by":"publisher","DOI":"10.1080\/15563650.2016.1250903","author":"CI Johnston","year":"2017","unstructured":"Johnston CI, Ryan NM, O\u2019Leary MA, Brown SG, Isbister GK (2017a) Australian taipan (Oxyuranus spp) envenoming clinical effects and potential benefits of early antivenom therapy-Australian snakebite project. Clin Toxicol. https:\/\/doi.org\/10.1080\/15563650.2016.1250903","journal-title":"Clin Toxicol"},{"issue":"5","key":"3420_CR73","doi-asserted-by":"publisher","first-page":"2206","DOI":"10.1021\/acs.jproteome.9b00077","volume":"18","author":"BK Jones","year":"2019","unstructured":"Jones BK, Saviola AJ, Reilly SB et al (2019) Venom composition in a phenotypically variable pit viper (trimeresurus insularis) across the lesser sunda archipelago. J Proteome Res 18(5):2206\u20132220. https:\/\/doi.org\/10.1021\/acs.jproteome.9b00077","journal-title":"J Proteome Res"},{"issue":"4","key":"3420_CR74","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1016\/j.drudis.2020.12.021","volume":"26","author":"B Kalita","year":"2021","unstructured":"Kalita B, Saviola AJ, Mukherjee AK (2021) From venom to drugs: a review and critical analysis of Indian snake venom toxins envisaged as anticancer drug prototypes. Drug Discovery Today 26(4):993\u20131005. https:\/\/doi.org\/10.1016\/j.drudis.2020.12.021","journal-title":"Drug Discovery Today"},{"issue":"23","key":"3420_CR75","doi-asserted-by":"publisher","first-page":"4544","DOI":"10.1111\/j.1742-4658.2011.08115.x","volume":"278","author":"TS Kang","year":"2011","unstructured":"Kang TS, Georgieva D, Genov N et al (2011) Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis. FEBS J 278(23):4544\u20134576. https:\/\/doi.org\/10.1111\/j.1742-4658.2011.08115.x","journal-title":"FEBS J"},{"issue":"1\u20132","key":"3420_CR76","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1081\/TXR-120004739","volume":"21","author":"KV Kardong","year":"2002","unstructured":"Kardong KV (2002) COLUBRID SNAKES AND DUVERNOY\u2019S \u201cVENOM\u201d GLANDS. J Toxicol 21(1\u20132):1\u201319. https:\/\/doi.org\/10.1081\/TXR-120004739","journal-title":"J Toxicol"},{"issue":"1","key":"3420_CR77","doi-asserted-by":"publisher","first-page":"226","DOI":"10.1111\/j.0014-3820.2005.tb00909.x","volume":"59","author":"JS Keogh","year":"2005","unstructured":"Keogh JS, Scott IA, Hayes C (2005) Rapid and repeated origin of insular gigantism and dwarfism in Australian tiger snakes. Evolution 59(1):226\u2013233. https:\/\/doi.org\/10.1111\/j.0014-3820.2005.tb00909.x","journal-title":"Evolution"},{"key":"3420_CR78","doi-asserted-by":"publisher","DOI":"10.1155\/2014\/675985","volume":"2014","author":"I Kerkis","year":"2014","unstructured":"Kerkis I, Hayashi MAF, Prieto da Silva ARB et al (2014) State of the Art in the Studies on Crotamine, a cell penetrating peptide from south american rattlesnake. Biomed Res Int 2014:675985. https:\/\/doi.org\/10.1155\/2014\/675985","journal-title":"Biomed Res Int"},{"issue":"1","key":"3420_CR79","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1006\/abbi.1999.1345","volume":"369","author":"RT Kerns","year":"1999","unstructured":"Kerns RT, Kini RM, Stefansson S, Evans HJ (1999) Targeting of venom phospholipases: the strongly anticoagulant phospholipase a2 from naja nigricollis venom binds to coagulation factor xa to inhibit the prothrombinase complex. Arch Biochem Biophys 369(1):107\u2013113. https:\/\/doi.org\/10.1006\/abbi.1999.1345","journal-title":"Arch Biochem Biophys"},{"issue":"9","key":"3420_CR80","doi-asserted-by":"publisher","first-page":"815","DOI":"10.1046\/j.1440-1681.2002.03725.x","volume":"29","author":"RM Kini","year":"2002","unstructured":"Kini RM (2002) Molecular moulds with multiple missions: functional sites in three-finger toxins. Clin Exp Pharmacol Physiol 29(9):815\u2013822. https:\/\/doi.org\/10.1046\/j.1440-1681.2002.03725.x","journal-title":"Clin Exp Pharmacol Physiol"},{"issue":"4\u20135","key":"3420_CR81","doi-asserted-by":"publisher","first-page":"200","DOI":"10.1159\/000092424","volume":"34","author":"RM Kini","year":"2005","unstructured":"Kini RM (2005) Serine Proteases Affecting Blood Coagulation and Fibrinolysis from Snake Venoms. Pathophysiol Haemost Thromb 34(4\u20135):200\u2013204. https:\/\/doi.org\/10.1159\/000092424","journal-title":"Pathophysiol Haemost Thromb"},{"issue":"6","key":"3420_CR82","doi-asserted-by":"publisher","first-page":"855","DOI":"10.1016\/j.toxicon.2010.07.010","volume":"56","author":"RM Kini","year":"2010","unstructured":"Kini RM, Doley R (2010) Structure, function and evolution of three-finger toxins: mini proteins with multiple targets. Toxicon 56(6):855\u2013867. https:\/\/doi.org\/10.1016\/j.toxicon.2010.07.010","journal-title":"Toxicon"},{"issue":"5","key":"3420_CR83","doi-asserted-by":"publisher","first-page":"328","DOI":"10.3390\/toxins13050328","volume":"13","author":"JM Kleiz-Ferreira","year":"2021","unstructured":"Kleiz-Ferreira JM, Cirauqui N, Trajano EA, Almeida MdS, Zingali RB (2021) Three-finger toxins from brazilian coral snakes: from molecular framework to insights in biological function. Toxins 13(5):328","journal-title":"Toxins"},{"issue":"2","key":"3420_CR84","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1111\/j.1742-7843.2012.00925.x","volume":"112","author":"R Kornhauser","year":"2013","unstructured":"Kornhauser R, Isbister GK, O\u2019Leary MA, Mirtschin P, Dunstan N, Hodgson WC (2013) Cross-neutralisation of the neurotoxic effects of Egyptian cobra venom with commercial tiger snake antivenom. Basic Clin Pharmacol Toxicol 112(2):138\u2013143. https:\/\/doi.org\/10.1111\/j.1742-7843.2012.00925.x","journal-title":"Basic Clin Pharmacol Toxicol"},{"issue":"3","key":"3420_CR85","doi-asserted-by":"publisher","first-page":"1196","DOI":"10.1124\/jpet.105.093641","volume":"315","author":"S Kuruppu","year":"2005","unstructured":"Kuruppu S, Reeve S, Banerjee Y, Kini RM, Smith AI, Hodgson WC (2005) Isolation and pharmacological characterization of cannitoxin, a presynaptic neurotoxin from the venom of the papuan taipan (Oxyuranus scutellatus canni). J Pharmacol Exp Ther 315(3):1196\u20131202. https:\/\/doi.org\/10.1124\/jpet.105.093641","journal-title":"J Pharmacol Exp Ther"},{"issue":"9316","key":"3420_CR86","doi-asserted-by":"publisher","first-page":"1527","DOI":"10.1016\/s0140-6736(02)08456-8","volume":"359","author":"DG Lalloo","year":"2002","unstructured":"Lalloo DG, Theakston RD, Warrell DA (2002) The African challenge. Lancet 359(9316):1527. https:\/\/doi.org\/10.1016\/s0140-6736(02)08456-8","journal-title":"Lancet"},{"issue":"3","key":"3420_CR87","doi-asserted-by":"publisher","first-page":"239","DOI":"10.1016\/j.toxicon.2011.05.020","volume":"58","author":"J Lane","year":"2011","unstructured":"Lane J, O\u2019Leary MA, Isbister GK (2011) Coagulant effects of black snake (Pseudechis spp) venoms and in vitro efficacy of commercial antivenom. Toxicon 58(3):239\u2013246. https:\/\/doi.org\/10.1016\/j.toxicon.2011.05.020","journal-title":"Toxicon"},{"key":"3420_CR88","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1016\/j.nbt.2017.05.005","volume":"45","author":"AH Laustsen","year":"2018","unstructured":"Laustsen AH (2018) Guiding recombinant antivenom development by omics technologies. N Biotechnol 45:19\u201327. https:\/\/doi.org\/10.1016\/j.nbt.2017.05.005","journal-title":"N Biotechnol"},{"key":"3420_CR89","doi-asserted-by":"publisher","first-page":"23","DOI":"10.1016\/j.toxicon.2015.03.001","volume":"99","author":"AH Laustsen","year":"2015","unstructured":"Laustsen AH, Gutierrez JM, Lohse B et al (2015) Snake venomics of monocled cobra (Naja kaouthia) and investigation of human IgG response against venom toxins. Toxicon 99:23\u201335. https:\/\/doi.org\/10.1016\/j.toxicon.2015.03.001","journal-title":"Toxicon"},{"issue":"12","key":"3420_CR90","doi-asserted-by":"publisher","first-page":"3796","DOI":"10.1161\/strokeaha.109.565119","volume":"40","author":"DE Levy","year":"2009","unstructured":"Levy DE, del Zoppo GJ, Demaerschalk BM et al (2009) Ancrod in acute ischemic stroke: results of 500 subjects beginning treatment within 6 hours of stroke onset in the ancrod stroke program. Stroke 40(12):3796\u20133803. https:\/\/doi.org\/10.1161\/strokeaha.109.565119","journal-title":"Stroke"},{"issue":"9","key":"3420_CR91","first-page":"346","volume":"10","author":"L Li","year":"2018","unstructured":"Li L, Huang J, Lin Y (2018) Snake venoms in cancer therapy: past. Pres Future Toxins 10(9):346","journal-title":"Pres Future Toxins"},{"issue":"1","key":"3420_CR92","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/0041-0101(94)00134-t","volume":"33","author":"WW Lin","year":"1995","unstructured":"Lin WW, Smith LA, Lee CY (1995) A study on the cause of death due to waglerin-I, a toxin from trimeresurus wagleri. Toxicon 33(1):111\u2013114. https:\/\/doi.org\/10.1016\/0041-0101(94)00134-t","journal-title":"Toxicon"},{"issue":"2","key":"3420_CR93","doi-asserted-by":"publisher","first-page":"122","DOI":"10.3390\/toxins14020122","volume":"14","author":"J-H Lin","year":"2022","unstructured":"Lin J-H, Sung W-C, Mu H-W, Hung D-Z (2022) Local cytotoxic effects in cobra envenoming: a pilot study. Toxins 14(2):122","journal-title":"Toxins"},{"key":"3420_CR94","doi-asserted-by":"publisher","first-page":"177","DOI":"10.1016\/j.jprot.2019.01.007","volume":"198","author":"E Lippa","year":"2019","unstructured":"Lippa E, T\u00f6r\u00f6k F, G\u00f3mez A et al (2019) First look into the venom of Roatan Island\u2019s critically endangered coral snake Micrurus ruatanus: Proteomic characterization, toxicity, immunorecognition and neutralization by an antivenom. J Proteomics 198:177\u2013185. https:\/\/doi.org\/10.1016\/j.jprot.2019.01.007","journal-title":"J Proteomics"},{"issue":"1","key":"3420_CR95","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1002\/jmor.20483","volume":"277","author":"Y Liu","year":"2016","unstructured":"Liu Y, Chen Q, Papenfuss TJ, Lu F, Tang Y (2016) Eye and pit size are inversely correlated in crotalinae: implications for selection pressure relaxation. J Morphol 277(1):107\u2013117. https:\/\/doi.org\/10.1002\/jmor.20483","journal-title":"J Morphol"},{"key":"3420_CR96","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.jprot.2018.06.003","volume":"187","author":"CC Liu","year":"2018","unstructured":"Liu CC, Lin CC, Hsiao YC, Wang PJ, Yu JS (2018) Proteomic characterization of six taiwanese snake venoms: identification of species-specific proteins and development of a siscapa-mrm assay for cobra venom factors. J Proteomics 187:59\u201368. https:\/\/doi.org\/10.1016\/j.jprot.2018.06.003","journal-title":"J Proteomics"},{"key":"3420_CR97","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/j.toxicon.2012.10.013","volume":"61","author":"K Maduwage","year":"2013","unstructured":"Maduwage K, Isbister GK, Silva A, Bowatta S, Mendis S, Gawarammana I (2013) Epidemiology and clinical effects of hump-nosed pit viper (Genus: Hypnale) envenoming in Sri Lanka. Toxicon 61:11\u201315. https:\/\/doi.org\/10.1016\/j.toxicon.2012.10.013","journal-title":"Toxicon"},{"key":"3420_CR98","doi-asserted-by":"publisher","first-page":"4827","DOI":"10.1038\/srep04827","volume":"4","author":"K Maduwage","year":"2014","unstructured":"Maduwage K, O\u2019Leary MA, Isbister GK (2014) Diagnosis of snake envenomation using a simple phospholipase A2 assay. Sci Rep 4:4827. https:\/\/doi.org\/10.1038\/srep04827","journal-title":"Sci Rep"},{"key":"3420_CR99","doi-asserted-by":"publisher","first-page":"174","DOI":"10.1016\/j.thromres.2015.12.002","volume":"137","author":"KP Maduwage","year":"2016","unstructured":"Maduwage KP, Scorgie FE, Lincz LF, O\u2019Leary MA, Isbister GK (2016) Procoagulant snake venoms have differential effects in animal plasmas: Implications for antivenom testing in animal models. Thromb Res 137:174\u2013177. https:\/\/doi.org\/10.1016\/j.thromres.2015.12.002","journal-title":"Thromb Res"},{"key":"3420_CR100","doi-asserted-by":"publisher","DOI":"10.1002\/14651858.CD011428.pub2","author":"K Maduwage","year":"2015","unstructured":"Maduwage K, Buckley NA, de Silva HJ, Lalloo DG, Isbister GK (2015) Snake antivenom for snake venom induced consumption coagulopathy. Cochrane Database Syst Rev. https:\/\/doi.org\/10.1002\/14651858.CD011428.pub2","journal-title":"Cochrane Database Syst Rev"},{"key":"3420_CR101","doi-asserted-by":"publisher","first-page":"10","DOI":"10.1016\/j.toxicon.2020.08.016","volume":"187","author":"CCN Mamede","year":"2020","unstructured":"Mamede CCN, de Sousa Simamoto BB, da Cunha Pereira DF, de Oliveira CJ, Ribeiro MSM, de Oliveira F (2020) Edema, hyperalgesia and myonecrosis induced by brazilian bothropic venoms: overview of the last decade. Toxicon 187:10\u201318. https:\/\/doi.org\/10.1016\/j.toxicon.2020.08.016","journal-title":"Toxicon"},{"issue":"12","key":"3420_CR102","doi-asserted-by":"publisher","first-page":"1927","DOI":"10.1016\/S0041-0101(98)00117-2","volume":"36","author":"AC Mancin","year":"1998","unstructured":"Mancin AC, Soares AM, Andri\u00e3o-Escarso SH et al (1998) The analgesic activity of crotamine, a neurotoxin from crotalus durissus terrificus (south american rattlesnake) venom: a biochemical and pharmacological study. Toxicon 36(12):1927\u20131937. https:\/\/doi.org\/10.1016\/S0041-0101(98)00117-2","journal-title":"Toxicon"},{"issue":"1","key":"3420_CR103","doi-asserted-by":"publisher","first-page":"165","DOI":"10.1534\/genetics.114.172437","volume":"199","author":"MJ Margres","year":"2015","unstructured":"Margres MJ, McGivern JJ, Seavy M, Wray KP, Facente J, Rokyta DR (2015) Contrasting modes and tempos of venom expression evolution in two snake species. Genetics 199(1):165\u2013176. https:\/\/doi.org\/10.1534\/genetics.114.172437","journal-title":"Genetics"},{"key":"3420_CR104","doi-asserted-by":"publisher","DOI":"10.3390\/toxins13110782","author":"MJ Margres","year":"2021","unstructured":"Margres MJ, Wray KP, Sanader D et al (2021) Varying Intensities of Introgression Obscure Incipient Venom-Associated Speciation in the Timber Rattlesnake (Crotalus horridus). Toxins. https:\/\/doi.org\/10.3390\/toxins13110782","journal-title":"Toxins"},{"key":"3420_CR105","doi-asserted-by":"publisher","first-page":"103","DOI":"10.1016\/j.toxicon.2013.09.003","volume":"76","author":"G Mion","year":"2013","unstructured":"Mion G, Larr\u00e9ch\u00e9 S, Benois A, Petitjeans F, Puidupin M (2013) Hemostasis dynamics during coagulopathy resulting from echis envenomation. Toxicon 76:103\u2013109. https:\/\/doi.org\/10.1016\/j.toxicon.2013.09.003","journal-title":"Toxicon"},{"issue":"25","key":"3420_CR106","doi-asserted-by":"publisher","first-page":"7895","DOI":"10.1021\/bi025732d","volume":"41","author":"BE Molles","year":"2002","unstructured":"Molles BE, Tsigelny I, Nguyen PD, Gao SX, Sine SM, Taylor P (2002) Residues in the epsilon subunit of the nicotinic acetylcholine receptor interact to confer selectivity of waglerin-1 for the alpha-epsilon subunit interface site. Biochemistry 41(25):7895\u20137906. https:\/\/doi.org\/10.1021\/bi025732d","journal-title":"Biochemistry"},{"issue":"8","key":"3420_CR107","doi-asserted-by":"publisher","first-page":"1560","DOI":"10.1016\/j.toxicon.2008.03.020","volume":"51","author":"C Montecucco","year":"2008","unstructured":"Montecucco C, Rossetto O (2008) On the quaternary structure of taipoxin and textilotoxin: The advantage of being multiple. Toxicon 51(8):1560\u20131562. https:\/\/doi.org\/10.1016\/j.toxicon.2008.03.020","journal-title":"Toxicon"},{"key":"3420_CR108","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2020.103945","volume":"229","author":"D Mora-Obando","year":"2020","unstructured":"Mora-Obando D, Salazar-Valenzuela D, Pla D et al (2020) Venom variation in Bothrops asper lineages from North-Western South America. J Proteomics 229:103945. https:\/\/doi.org\/10.1016\/j.jprot.2020.103945","journal-title":"J Proteomics"},{"key":"3420_CR109","doi-asserted-by":"publisher","first-page":"138","DOI":"10.1016\/j.biochi.2016.08.005","volume":"128\u2013129","author":"AK Mukherjee","year":"2016","unstructured":"Mukherjee AK, Dutta S, Kalita B, Jha DK, Deb P, Mackessy SP (2016) Structural and functional characterization of complex formation between two Kunitz-type serine protease inhibitors from Russell\u2019s Viper venom. Biochimie 128\u2013129:138\u2013147. https:\/\/doi.org\/10.1016\/j.biochi.2016.08.005","journal-title":"Biochimie"},{"key":"3420_CR110","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/j.toxicon.2014.05.003","volume":"86","author":"H Nakamura","year":"2014","unstructured":"Nakamura H, Murakami T, Imamura T et al (2014) Discovery of a novel vascular endothelial growth factor (VEGF) with no affinity to heparin in Gloydius tsushimaensis venom. Toxicon 86:107\u2013115. https:\/\/doi.org\/10.1016\/j.toxicon.2014.05.003","journal-title":"Toxicon"},{"issue":"12","key":"3420_CR111","doi-asserted-by":"publisher","first-page":"2695","DOI":"10.3390\/ijms18122695","volume":"18","author":"V Neale","year":"2017","unstructured":"Neale V, Sotillo J, Seymour JE, Wilson D (2017) The Venom of the Spine-Bellied Sea Snake (Hydrophis curtus): proteome, toxin diversity and intraspecific variation. Int J Mol Sci 18(12):2695. https:\/\/doi.org\/10.3390\/ijms18122695","journal-title":"Int J Mol Sci"},{"key":"3420_CR112","doi-asserted-by":"publisher","DOI":"10.1016\/j.jprot.2020.103865","volume":"225","author":"E Neri-Castro","year":"2020","unstructured":"Neri-Castro E, Sanz L, Olvera-Rodr\u00edguez A, B\u00e9nard-Valle M, Alag\u00f3n A, Calvete JJ (2020) Venomics and biochemical analysis of the black-tailed horned pitviper, Mixcoatlus melanurus, and characterization of melanurutoxin, a novel crotoxin homolog. J Proteomics 225:103865. https:\/\/doi.org\/10.1016\/j.jprot.2020.103865","journal-title":"J Proteomics"},{"issue":"1","key":"3420_CR113","doi-asserted-by":"publisher","first-page":"4543","DOI":"10.1038\/s41467-022-32174-7","volume":"13","author":"M Nys","year":"2022","unstructured":"Nys M, Zarkadas E, Brams M et al (2022) The molecular mechanism of snake short-chain \u03b1-neurotoxin binding to muscle-type nicotinic acetylcholine receptors. Nat Commun 13(1):4543. https:\/\/doi.org\/10.1038\/s41467-022-32174-7","journal-title":"Nat Commun"},{"issue":"1","key":"3420_CR114","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.toxicon.2004.07.028","volume":"45","author":"T Ogawa","year":"2005","unstructured":"Ogawa T, Chijiwa T, Oda-Ueda N, Ohno M (2005) Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon 45(1):1\u201314. https:\/\/doi.org\/10.1016\/j.toxicon.2004.07.028","journal-title":"Toxicon"},{"issue":"8","key":"3420_CR115","doi-asserted-by":"publisher","first-page":"1172","DOI":"10.1016\/j.toxicon.2007.02.012","volume":"49","author":"Y Ogawa","year":"2007","unstructured":"Ogawa Y, Murayama N, Fujita Y, Yanoshita R (2007) Characterization and cDNA cloning of aminopeptidase A from the venom of Gloydius blomhoffi brevicaudus. Toxicon 49(8):1172\u20131181. https:\/\/doi.org\/10.1016\/j.toxicon.2007.02.012","journal-title":"Toxicon"},{"key":"3420_CR116","doi-asserted-by":"publisher","DOI":"10.3390\/toxins11100581","author":"T Ogawa","year":"2019","unstructured":"Ogawa T, Oda-Ueda N, Hisata K et al (2019) Alternative mRNA Splicing in Three Venom Families Underlying a Possible Production of Divergent Venom Proteins of the Habu Snake Protobothrops flavoviridis. Toxins (basel). https:\/\/doi.org\/10.3390\/toxins11100581","journal-title":"Toxins (basel)"},{"key":"3420_CR117","doi-asserted-by":"publisher","DOI":"10.1016\/j.toxcx.2020.100052","author":"OT Olaoba","year":"2020","unstructured":"Olaoba OT, Santos PKd, Selistre-de-Araujo HS, Souza DHFd (2020) Snake venom metalloproteinases (SVMPs) A structure-function update. Toxicon X. https:\/\/doi.org\/10.1016\/j.toxcx.2020.100052","journal-title":"Toxicon X"},{"issue":"7","key":"3420_CR118","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1038\/s41570-022-00393-7","volume":"6","author":"AL Oliveira","year":"2022","unstructured":"Oliveira AL, Viegas MF, da Silva SL, Soares AM, Ramos MJ, Fernandes PA (2022a) The chemistry of snake venom and its medicinal potential. Nat Rev Chem 6(7):451\u2013469. https:\/\/doi.org\/10.1038\/s41570-022-00393-7","journal-title":"Nat Rev Chem"},{"key":"3420_CR119","doi-asserted-by":"publisher","first-page":"121","DOI":"10.1016\/j.toxicon.2022.08.004","volume":"217","author":"ISd Oliveira","year":"2022","unstructured":"Oliveira ISd, Pucca MB, Ferreira IG et al (2022b) State-of-the-art review of snake venom phosphodiesterases (svPDEs). Toxicon 217:121\u2013130. https:\/\/doi.org\/10.1016\/j.toxicon.2022.08.004","journal-title":"Toxicon"},{"key":"3420_CR120","doi-asserted-by":"publisher","DOI":"10.2174\/2666121701666211124151529","author":"S Omidi","year":"2021","unstructured":"Omidi S, Mehrpouya M, Oladnabi M, Azadmehr A, Kazemi-Lomedasht F, Yardehnavi N (2021) Evaluation of venom as a promising tool for drug discovery [focusing on Neurological disorders]. Venom Toxins. https:\/\/doi.org\/10.2174\/2666121701666211124151529","journal-title":"Venom Toxins"},{"issue":"7","key":"3420_CR121","doi-asserted-by":"publisher","first-page":"998","DOI":"10.1016\/j.toxicon.2009.07.001","volume":"54","author":"R Otero-Pati\u00f1o","year":"2009","unstructured":"Otero-Pati\u00f1o R (2009) Epidemiological, clinical and therapeutic aspects of bothrops asper bites. Toxicon 54(7):998\u20131011. https:\/\/doi.org\/10.1016\/j.toxicon.2009.07.001","journal-title":"Toxicon"},{"issue":"4","key":"3420_CR122","doi-asserted-by":"publisher","first-page":"491","DOI":"10.1016\/0041-0101(83)90127-7","volume":"21","author":"C Ouyang","year":"1983","unstructured":"Ouyang C, Huang T-F (1983) Inhibition of platelet aggregation by 5\u2032-nucleotidase purified from Trimeresurus gramineus snake venom. Toxicon 21(4):491\u2013501. https:\/\/doi.org\/10.1016\/0041-0101(83)90127-7","journal-title":"Toxicon"},{"issue":"6","key":"3420_CR123","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.1038\/sj.bjp.0701004","volume":"120","author":"DG Owen","year":"1997","unstructured":"Owen DG, Hall A, Stephens G, Stow J, Robertson B (1997) The relative potencies of dendrotoxins as blockers of the cloned voltage-gated K channel when stably expressed in Chinese hamster ovary cells. Br J Pharmacol 120(6):1029\u20131034","journal-title":"Br J Pharmacol"},{"issue":"16","key":"3420_CR124","doi-asserted-by":"publisher","first-page":"4204","DOI":"10.1093\/emboj\/19.16.4204","volume":"19","author":"PD Pawelek","year":"2000","unstructured":"Pawelek PD, Cheah J, Coulombe R, Macheroux P, Ghisla S, Vrielink A (2000) The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site. EMBO J 19(16):4204\u20134215. https:\/\/doi.org\/10.1093\/emboj\/19.16.4204","journal-title":"EMBO J"},{"issue":"3","key":"3420_CR125","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1016\/j.toxicon.2006.05.013","volume":"48","author":"J Pawlak","year":"2006","unstructured":"Pawlak J, Manjunatha Kini R (2006) Snake venom glutaminyl cyclase. Toxicon 48(3):278\u2013286. https:\/\/doi.org\/10.1016\/j.toxicon.2006.05.013","journal-title":"Toxicon"},{"issue":"1","key":"3420_CR126","doi-asserted-by":"publisher","first-page":"90","DOI":"10.1124\/mol.112.078188","volume":"82","author":"S Peigneur","year":"2012","unstructured":"Peigneur S, Orts DJB, Prieto da Silva AR et al (2012) Crotamine pharmacology revisited: novel insights based on the inhibition of k<sub>v<\/sub> channels. Mol Pharmacol 82(1):90\u201396. https:\/\/doi.org\/10.1124\/mol.112.078188","journal-title":"Mol Pharmacol"},{"issue":"6","key":"3420_CR127","doi-asserted-by":"publisher","first-page":"1058","DOI":"10.1101\/gr.276251.121","volume":"32","author":"BW Perry","year":"2022","unstructured":"Perry BW, Gopalan SS, Pasquesi GIM et al (2022) Snake venom gene expression is coordinated by novel regulatory architecture and the integration of multiple co-opted vertebrate pathways. Genome Res 32(6):1058\u20131073","journal-title":"Genome Res"},{"issue":"15","key":"3420_CR128","doi-asserted-by":"publisher","first-page":"2778","DOI":"10.3390\/molecules24152778","volume":"24","author":"O P\u00e9terfi","year":"2019","unstructured":"P\u00e9terfi O, Boda F, Szab\u00f3 Z, Ferencz E, B\u00e1ba L (2019) Hypotensive snake venom components\u2014a mini-review. Molecules 24(15):2778","journal-title":"Molecules"},{"key":"3420_CR129","doi-asserted-by":"publisher","first-page":"201","DOI":"10.1016\/j.jprot.2016.09.007","volume":"150","author":"D Pla","year":"2017","unstructured":"Pla D, Bande BW, Welton RE et al (2017) Proteomics and antivenomics of papuan black snake (pseudechis papuanus) venom with analysis of its toxicological profile and the preclinical efficacy of australian antivenoms. J Proteomics 150:201\u2013215. https:\/\/doi.org\/10.1016\/j.jprot.2016.09.007","journal-title":"J Proteomics"},{"key":"3420_CR130","doi-asserted-by":"publisher","first-page":"5021924","DOI":"10.1155\/2017\/5021924","volume":"2017","author":"V Quarch","year":"2017","unstructured":"Quarch V, Brander L, Cioccari L (2017) An Unexpected case of black mamba (dendroaspis polylepis) bite in switzerland. Case Rep Crit Care 2017:5021924. https:\/\/doi.org\/10.1155\/2017\/5021924","journal-title":"Case Rep Crit Care"},{"issue":"4","key":"3420_CR131","doi-asserted-by":"publisher","first-page":"611","DOI":"10.1055\/s-0037-1613264","volume":"88","author":"VS Rao","year":"2002","unstructured":"Rao VS, Kini RM (2002) Pseutarin C, a prothrombin activator from pseudonaja textilis venom: its structural and functional similarity to mammalian coagulation factor xa-va complex. J Thromb Haemost 88(4):611\u2013619","journal-title":"J Thromb Haemost"},{"issue":"1906","key":"3420_CR132","doi-asserted-by":"publisher","first-page":"20190810","DOI":"10.1098\/rspb.2019.0810","volume":"286","author":"RM Rautsaw","year":"2019","unstructured":"Rautsaw RM, Hofmann EP, Margres MJ et al (2019) Intraspecific sequence and gene expression variation contribute little to venom diversity in sidewinder rattlesnakes ( Crotalus cerastes). Proc Biol Sci 286(1906):20190810\u201320190810. https:\/\/doi.org\/10.1098\/rspb.2019.0810","journal-title":"Proc Biol Sci"},{"issue":"4","key":"3420_CR133","doi-asserted-by":"publisher","first-page":"659","DOI":"10.1016\/j.biochi.2010.12.008","volume":"93","author":"R Richards","year":"2011","unstructured":"Richards R, St Pierre L, Trabi M et al (2011) Cloning and characterisation of novel cystatins from elapid snake venom glands. Biochimie 93(4):659\u2013668. https:\/\/doi.org\/10.1016\/j.biochi.2010.12.008","journal-title":"Biochimie"},{"issue":"1","key":"3420_CR134","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1016\/s0041-0101(00)00159-8","volume":"39","author":"EG Rowan","year":"2001","unstructured":"Rowan EG (2001) What does \u03b2-bungarotoxin do at the neuromuscular junction? Toxicon 39(1):107\u2013118. https:\/\/doi.org\/10.1016\/s0041-0101(00)00159-8","journal-title":"Toxicon"},{"issue":"3","key":"3420_CR135","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/0041-0101(63)90070-9","volume":"1","author":"FE Russell","year":"1963","unstructured":"Russell FE, Buess FW, Woo MY (1963) Zootoxicological properties of venom phosphodiesterase. Toxicon 1(3):99\u2013108. https:\/\/doi.org\/10.1016\/0041-0101(63)90070-9","journal-title":"Toxicon"},{"issue":"7","key":"3420_CR136","doi-asserted-by":"publisher","first-page":"1380","DOI":"10.3390\/pr10071380","volume":"10","author":"C Sahyoun","year":"2022","unstructured":"Sahyoun C, Rima M, Mattei C, Sabatier J-M, Fajloun Z, Legros C (2022) Separation and Analytical Techniques Used in Snake Venomics: A Review Article. Processes 10(7):1380","journal-title":"Processes"},{"key":"3420_CR137","doi-asserted-by":"publisher","first-page":"28","DOI":"10.1016\/j.jprot.2015.03.015","volume":"121","author":"AJ Saviola","year":"2015","unstructured":"Saviola AJ, Pla D, Sanz L, Castoe TA, Calvete JJ, Mackessy SP (2015) Comparative venomics of the Prairie Rattlesnake (Crotalus viridis viridis) from Colorado: Identification of a novel pattern of ontogenetic changes in venom composition and assessment of the immunoreactivity of the commercial antivenom CroFab(R). J Proteomics 121:28\u201343. https:\/\/doi.org\/10.1016\/j.jprot.2015.03.015","journal-title":"J Proteomics"},{"key":"3420_CR138","doi-asserted-by":"publisher","first-page":"119","DOI":"10.1016\/j.toxicon.2017.08.016","volume":"138","author":"AJ Saviola","year":"2017","unstructured":"Saviola AJ, Gandara AJ, Bryson RW Jr, Mackessy SP (2017) Venom phenotypes of the Rock Rattlesnake (Crotalus lepidus) and the Ridge-nosed Rattlesnake (Crotalus willardi) from Mexico and the United States. Toxicon 138:119\u2013129. https:\/\/doi.org\/10.1016\/j.toxicon.2017.08.016","journal-title":"Toxicon"},{"issue":"4","key":"3420_CR139","doi-asserted-by":"publisher","first-page":"185","DOI":"10.3109\/15569543.2014.942040","volume":"33","author":"AJ Saviola","year":"2014","unstructured":"Saviola AJ, Peichoto ME, Mackessy SP (2014) Rear-fanged snake venoms: an untapped source of novel compounds and potential drug leads. Toxin Rev 33(4):185\u2013201","journal-title":"Toxin Rev"},{"issue":"1","key":"3420_CR140","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1038\/s41598-018-28749-4","volume":"8","author":"H Shibata","year":"2018","unstructured":"Shibata H, Chijiwa T, Oda-Ueda N et al (2018) The habu genome reveals accelerated evolution of venom protein genes. Sci Rep 8(1):1\u20131. https:\/\/doi.org\/10.1038\/s41598-018-28749-4","journal-title":"Sci Rep"},{"issue":"2","key":"3420_CR141","doi-asserted-by":"publisher","first-page":"537","DOI":"10.1042\/bst20190739","volume":"48","author":"A Silva","year":"2020","unstructured":"Silva A, Isbister GK (2020) Current research into snake antivenoms, their mechanisms of action and applications. Biochem Soc Trans 48(2):537\u2013546. https:\/\/doi.org\/10.1042\/bst20190739","journal-title":"Biochem Soc Trans"},{"issue":"10","key":"3420_CR142","doi-asserted-by":"publisher","first-page":"302","DOI":"10.3390\/toxins8100302","volume":"8","author":"A Silva","year":"2016","unstructured":"Silva A, Hodgson WC, Isbister GK (2016b) Cross-neutralisation of in vitro neurotoxicity of asian and australian snake neurotoxins and venoms by different antivenoms. Toxins 8(10):302","journal-title":"Toxins"},{"issue":"5","key":"3420_CR143","doi-asserted-by":"publisher","first-page":"411","DOI":"10.3109\/15563650.2016.1143556","volume":"54","author":"A Silva","year":"2016","unstructured":"Silva A, Maduwage K, Sedgwick M et al (2016c) Neurotoxicity in Russell\u2019s viper (Daboia russelii) envenoming in Sri Lanka: a clinical and neurophysiological study. Clin Toxicol (phila) 54(5):411\u2013419. https:\/\/doi.org\/10.3109\/15563650.2016.1143556","journal-title":"Clin Toxicol (phila)"},{"issue":"23","key":"3420_CR144","doi-asserted-by":"publisher","first-page":"4465","DOI":"10.1007\/s00018-018-2893-x","volume":"75","author":"A Silva","year":"2018","unstructured":"Silva A, Cristofori-Armstrong B, Rash LD, Hodgson WC, Isbister GK (2018) Defining the role of post-synaptic \u03b1-neurotoxins in paralysis due to snake envenoming in humans. Cell Mol Life Sci 75(23):4465\u20134478. https:\/\/doi.org\/10.1007\/s00018-018-2893-x","journal-title":"Cell Mol Life Sci"},{"key":"3420_CR145","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pntd.0004368","author":"A Silva","year":"2016","unstructured":"Silva A, Maduwage KP, Sedgwick MEE et al (2016d) Neuromuscular Effects of Common Krait (Bungarus caeruleus) Envenoming in Sri Lanka. PLoS Negl Trop Dis. https:\/\/doi.org\/10.1371\/journal.pntd.0004368","journal-title":"PLoS Negl Trop Dis"},{"key":"3420_CR146","doi-asserted-by":"publisher","DOI":"10.3390\/toxins9040143","author":"A Silva","year":"2017","unstructured":"Silva A, Hodgson WC, Isbister GK (2017) Antivenom for Neuromuscular Paralysis Resulting From Snake Envenoming. Toxins (basel). https:\/\/doi.org\/10.3390\/toxins9040143","journal-title":"Toxins (basel)"},{"key":"3420_CR147","doi-asserted-by":"publisher","DOI":"10.1016\/j.microc.2022.107187","volume":"175","author":"J Slagboom","year":"2022","unstructured":"Slagboom J, Kaal C, Arrahman A et al (2022) Analytical strategies in venomics. Microchem J 175:107187. https:\/\/doi.org\/10.1016\/j.microc.2022.107187","journal-title":"Microchem J"},{"issue":"3","key":"3420_CR148","doi-asserted-by":"publisher","first-page":"186","DOI":"10.1038\/nmeth.2369","volume":"10","author":"LM Smith","year":"2013","unstructured":"Smith LM, Kelleher NL (2013) Proteoform: a single term describing protein complexity. Nat Methods 10(3):186\u2013187. https:\/\/doi.org\/10.1038\/nmeth.2369","journal-title":"Nat Methods"},{"issue":"16","key":"3420_CR149","doi-asserted-by":"publisher","first-page":"2058","DOI":"10.3390\/ani12162058","volume":"12","author":"F Sofyantoro","year":"2022","unstructured":"Sofyantoro F, Yudha DS, Lischer K et al (2022) Bibliometric analysis of literature in snake venom-related research worldwide (1933&ndash;2022). Animals 12(16):2058","journal-title":"Animals"},{"issue":"7","key":"3420_CR150","first-page":"105","volume":"42","author":"R Souza","year":"2007","unstructured":"Souza R, Lima T, Luiz J, Cardoso CN (2007) The Enigma of the North Margin of the Amazon River: Proven Lachesis Bites in Brazil, Report of Two Cases, General Considerations about the Genus and Bibliographic Review. In 42(7):105\u2013115","journal-title":"In"},{"issue":"9","key":"3420_CR151","doi-asserted-by":"publisher","first-page":"1853","DOI":"10.1093\/molbev\/msi181","volume":"22","author":"L St Pierre","year":"2005","unstructured":"St Pierre L, Masci PP, Filippovich I et al (2005) Comparative analysis of prothrombin activators from the venom of Australian elapids. Mol Biol Evol 22(9):1853\u20131864. https:\/\/doi.org\/10.1093\/molbev\/msi181","journal-title":"Mol Biol Evol"},{"issue":"12","key":"3420_CR152","doi-asserted-by":"publisher","first-page":"1923","DOI":"10.1016\/j.biochi.2006.06.014","volume":"88","author":"L St Pierre","year":"2006","unstructured":"St Pierre L, Flight S, Masci PP et al (2006) Cloning and characterisation of natriuretic peptides from the venom glands of Australian elapids. Biochimie 88(12):1923\u20131931. https:\/\/doi.org\/10.1016\/j.biochi.2006.06.014","journal-title":"Biochimie"},{"issue":"11","key":"3420_CR153","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pone.0081827","volume":"8","author":"K Sunagar","year":"2013","unstructured":"Sunagar K, Fry BG, Jackson TN et al (2013) Molecular evolution of vertebrate neurotrophins: co-option of the highly conserved nerve growth factor gene into the advanced snake venom arsenalf. PLoS ONE 8(11):e81827. https:\/\/doi.org\/10.1371\/journal.pone.0081827","journal-title":"PLoS ONE"},{"key":"3420_CR154","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/j.toxicon.2019.04.006","volume":"165","author":"M Suntravat","year":"2019","unstructured":"Suntravat M, Cromer WE, Marquez J et al (2019) The isolation and characterization of a new snake venom cysteine-rich secretory protein (svCRiSP) from the venom of the Southern Pacific rattlesnake and its effect on vascular permeability. Toxicon 165:22\u201330. https:\/\/doi.org\/10.1016\/j.toxicon.2019.04.006","journal-title":"Toxicon"},{"issue":"6","key":"3420_CR155","doi-asserted-by":"publisher","first-page":"420","DOI":"10.3390\/toxins14060420","volume":"14","author":"V Suranse","year":"2022","unstructured":"Suranse V, Jackson TNW, Sunagar K (2022) Contextual Constraints: Dynamic Evolution of Snake Venom Phospholipase A2. Toxins 14(6):420","journal-title":"Toxins"},{"issue":"1","key":"3420_CR156","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1038\/s41588-019-0559-8","volume":"52","author":"K Suryamohan","year":"2020","unstructured":"Suryamohan K, Krishnankutty SP, Guillory J et al (2020) The Indian cobra reference genome and transcriptome enables comprehensive identification of venom toxins. Nat Genet 52(1):106\u2013117. https:\/\/doi.org\/10.1038\/s41588-019-0559-8","journal-title":"Nat Genet"},{"issue":"Pt 10","key":"3420_CR157","doi-asserted-by":"publisher","first-page":"1034","DOI":"10.1107\/s0907444908023512","volume":"64","author":"N Suzuki","year":"2008","unstructured":"Suzuki N, Yamazaki Y, Brown RL, Fujimoto Z, Morita T, Mizuno H (2008) Structures of pseudechetoxin and pseudecin, two snake-venom cysteine-rich secretory proteins that target cyclic nucleotide-gated ion channels: implications for movement of the C-terminal cysteine-rich domain. Acta Crystallogr D Biol Crystallogr 64(Pt 10):1034\u20131042. https:\/\/doi.org\/10.1107\/s0907444908023512","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"issue":"3","key":"3420_CR158","doi-asserted-by":"publisher","first-page":"175","DOI":"10.3390\/toxins12030175","volume":"12","author":"T Tadokoro","year":"2020","unstructured":"Tadokoro T, M. Modahl C, Maenaka K, Aoki-Shioi N, (2020) Cysteine-Rich Secretory Proteins (CRISPs) from Venomous Snakes: An Overview of the Functional Diversity in a Large and Underappreciated Superfamily. Toxins 12(3):175","journal-title":"Toxins"},{"issue":"5","key":"3420_CR160","doi-asserted-by":"publisher","first-page":"505","DOI":"10.1016\/0041-0101(88)90190-0","volume":"26","author":"N-H Tan","year":"1988","unstructured":"Tan N-H, Tan C-S (1988) Partial purification of acetylcholinesterase from the venom of the shore pit viper (Trimeresurus purpureomaculatus). Toxicon 26(5):505\u2013508. https:\/\/doi.org\/10.1016\/0041-0101(88)90190-0","journal-title":"Toxicon"},{"issue":"1","key":"3420_CR161","doi-asserted-by":"publisher","first-page":"687","DOI":"10.1186\/s12864-015-1828-2","volume":"16","author":"CH Tan","year":"2015","unstructured":"Tan CH, Tan KY, Fung SY, Tan NH (2015) Venom-gland transcriptome and venom proteome of the Malaysian king cobra (Ophiophagus hannah). BMC Genomics 16(1):687. https:\/\/doi.org\/10.1186\/s12864-015-1828-2","journal-title":"BMC Genomics"},{"key":"3420_CR162","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.jprot.2015.11.014","volume":"132","author":"CH Tan","year":"2016","unstructured":"Tan CH, Fung SY, Yap MK, Leong PK, Liew JL, Tan NH (2016) Unveiling the elusive and exotic: Venomics of the Malayan blue coral snake (Calliophis bivirgata flaviceps). J Proteomics 132:1\u201312. https:\/\/doi.org\/10.1016\/j.jprot.2015.11.014","journal-title":"J Proteomics"},{"key":"3420_CR163","doi-asserted-by":"publisher","first-page":"43237","DOI":"10.1038\/srep43237","volume":"7","author":"CH Tan","year":"2017","unstructured":"Tan CH, Tan KY, Yap MK, Tan NH (2017) Venomics of Tropidolaemus wagleri, the sexually dimorphic temple pit viper: Unveiling a deeply conserved atypical toxin arsenal. Sci Rep 7:43237. https:\/\/doi.org\/10.1038\/srep43237","journal-title":"Sci Rep"},{"key":"3420_CR164","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.toxicon.2018.01.015","volume":"144","author":"KK Tan","year":"2018","unstructured":"Tan KK, Bay BH, Gopalakrishnakone P (2018) L-amino acid oxidase from snake venom and its anticancer potential. Toxicon 144:7\u201313. https:\/\/doi.org\/10.1016\/j.toxicon.2018.01.015","journal-title":"Toxicon"},{"issue":"1","key":"3420_CR165","doi-asserted-by":"publisher","first-page":"3","DOI":"10.3390\/toxins11010003","volume":"11","author":"CH Tan","year":"2019","unstructured":"Tan CH, Tan KY, Ng TS, Sim SM, Tan NH (2019) Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom. Toxins 11(1):3","journal-title":"Toxins"},{"key":"3420_CR166","doi-asserted-by":"publisher","DOI":"10.3390\/toxins14040247","author":"CH Tan","year":"2022","unstructured":"Tan CH (2022) Snake Venomics: Fundamentals, Recent Updates, and a Look to the Next Decade. Toxins (basel). https:\/\/doi.org\/10.3390\/toxins14040247","journal-title":"Toxins (basel)"},{"issue":"9","key":"3420_CR167","doi-asserted-by":"publisher","first-page":"290","DOI":"10.3390\/toxins9090290","volume":"9","author":"T Tasoulis","year":"2017","unstructured":"Tasoulis T, Isbister GK (2017) A Review and Database of Snake Venom Proteomes. Toxins (basel) 9(9):290. https:\/\/doi.org\/10.3390\/toxins9090290","journal-title":"Toxins (basel)"},{"issue":"1","key":"3420_CR168","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1186\/s12862-020-1578-x","volume":"20","author":"T Tasoulis","year":"2020","unstructured":"Tasoulis T, Lee MSY, Ziajko M, Dunstan N, Sumner J, Isbister GK (2020a) Activity of two key toxin groups in Australian elapid venoms show a strong correlation to phylogeny but not to diet. BMC Evol Biol 20(1):9. https:\/\/doi.org\/10.1186\/s12862-020-1578-x","journal-title":"BMC Evol Biol"},{"issue":"8","key":"3420_CR169","doi-asserted-by":"publisher","first-page":"485","DOI":"10.3390\/toxins12080485","volume":"12","author":"T Tasoulis","year":"2020","unstructured":"Tasoulis T, Silva A, Veerati PC et al (2020b) Intra-Specific Venom Variation in the Australian Coastal Taipan Oxyuranus scutellatus. Toxins 12(8):485","journal-title":"Toxins"},{"key":"3420_CR170","doi-asserted-by":"publisher","DOI":"10.3389\/fphar.2021.768015","author":"T Tasoulis","year":"2022","unstructured":"Tasoulis T, Pukala TL, Isbister GK (2022a) Investigating Toxin Diversity and Abundance in Snake Venom Proteomes. Front Pharmacol. https:\/\/doi.org\/10.3389\/fphar.2021.768015","journal-title":"Front Pharmacol"},{"issue":"5","key":"3420_CR171","doi-asserted-by":"publisher","first-page":"314","DOI":"10.3390\/toxins14050314","volume":"14","author":"T Tasoulis","year":"2022","unstructured":"Tasoulis T, Wang CR, Sumner J, Dunstan N, Pukala TL, Isbister GK (2022b) The Unusual Metalloprotease-Rich Venom Proteome of the Australian Elapid Snake Hoplocephalus stephensii. Toxins 14(5):314","journal-title":"Toxins"},{"issue":"1","key":"3420_CR172","doi-asserted-by":"publisher","first-page":"46","DOI":"10.1016\/j.toxicon.2005.03.008","volume":"46","author":"K Trummal","year":"2005","unstructured":"Trummal K, Tonismagi K, Siigur E et al (2005) A novel metalloprotease from Vipera lebetina venom induces human endothelial cell apoptosis. Toxicon 46(1):46\u201361. https:\/\/doi.org\/10.1016\/j.toxicon.2005.03.008","journal-title":"Toxicon"},{"key":"3420_CR173","doi-asserted-by":"publisher","first-page":"175","DOI":"10.3389\/fmolb.2020.00175","volume":"7","author":"A Ullah","year":"2020","unstructured":"Ullah A, Masood R (2020) The Sequence and Three-Dimensional Structure Characterization of Snake Venom Phospholipases B. Front Mol Biosci 7:175. https:\/\/doi.org\/10.3389\/fmolb.2020.00175","journal-title":"Front Mol Biosci"},{"key":"3420_CR174","doi-asserted-by":"publisher","first-page":"195","DOI":"10.1016\/j.semcancer.2020.05.006","volume":"80","author":"FA Urra","year":"2022","unstructured":"Urra FA, Araya-Maturana R (2022) Putting the brakes on tumorigenesis with snake venom toxins: New molecular insights for cancer drug discovery. Semin Cancer Biol 80:195\u2013204. https:\/\/doi.org\/10.1016\/j.semcancer.2020.05.006","journal-title":"Semin Cancer Biol"},{"issue":"8","key":"3420_CR175","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pntd.0000796","volume":"4","author":"S Vaiyapuri","year":"2010","unstructured":"Vaiyapuri S, Wagstaff SC, Watson KA, Harrison RA, Gibbins JM, Hutchinson EG (2010) Purification and Functional Characterisation of Rhiminopeptidase A, a Novel Aminopeptidase from the Venom of Bitis gabonica rhinoceros. PLoS Negl Trop Dis 4(8):e796. https:\/\/doi.org\/10.1371\/journal.pntd.0000796","journal-title":"PLoS Negl Trop Dis"},{"issue":"2","key":"3420_CR176","doi-asserted-by":"publisher","first-page":"287","DOI":"10.1016\/0022-1759(91)90015-8","volume":"136","author":"CW Van den Berg","year":"1991","unstructured":"Van den Berg CW, Aerts PC, Van Dijk H (1991) In vivo anti-complementary activities of the cobra venom factors from Naja naja and Naja haje. J Immunol Methods 136(2):287\u2013294. https:\/\/doi.org\/10.1016\/0022-1759(91)90015-8","journal-title":"J Immunol Methods"},{"issue":"1\u20132","key":"3420_CR177","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1081\/Txr-120004740","volume":"21","author":"N Vidal","year":"2002","unstructured":"Vidal N (2002) Colubroid systematics: Evidence for an early appearance of the venom apparatus followed by extensive evolutionary tinkering. Journal of Toxicology-Toxin Reviews 21(1\u20132):21\u201341. https:\/\/doi.org\/10.1081\/Txr-120004740","journal-title":"Journal of Toxicology-Toxin Reviews"},{"issue":"5","key":"3420_CR178","doi-asserted-by":"publisher","first-page":"445","DOI":"10.1016\/j.trstmh.2007.11.006","volume":"102","author":"LE Visser","year":"2008","unstructured":"Visser LE, Kyei-Faried S, Belcher DW, Geelhoed DW, van Leeuwen JS, van Roosmalen J (2008) Failure of a new antivenom to treat Echis ocellatus snake bite in rural Ghana: the importance of quality surveillance. Trans R Soc Trop Med Hyg 102(5):445\u2013450. https:\/\/doi.org\/10.1016\/j.trstmh.2007.11.006","journal-title":"Trans R Soc Trop Med Hyg"},{"issue":"7","key":"3420_CR179","doi-asserted-by":"publisher","first-page":"1198","DOI":"10.1016\/j.toxicon.2010.04.007","volume":"56","author":"C-W Vogel","year":"2010","unstructured":"Vogel C-W, Fritzinger DC (2010) Cobra venom factor: Structure, function, and humanization for therapeutic complement depletion. Toxicon 56(7):1198\u20131222. https:\/\/doi.org\/10.1016\/j.toxicon.2010.04.007","journal-title":"Toxicon"},{"issue":"7204","key":"3420_CR180","doi-asserted-by":"publisher","first-page":"630","DOI":"10.1038\/nature07178","volume":"454","author":"FJ Vonk","year":"2008","unstructured":"Vonk FJ, Admiraal JF, Jackson K et al (2008) Evolutionary origin and development of snake fangs. Nature 454(7204):630\u2013633. https:\/\/doi.org\/10.1038\/nature07178","journal-title":"Nature"},{"issue":"4","key":"3420_CR181","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1002\/bies.201000117","volume":"33","author":"FJ Vonk","year":"2011","unstructured":"Vonk FJ, Jackson K, Doley R, Madaras F, Mirtschin PJ, Vidal N (2011) Snake venom: From fieldwork to the clinic: Recent insights into snake biology, together with new technology allowing high-throughput screening of venom, bring new hope for drug discovery. BioEssays 33(4):269\u2013279. https:\/\/doi.org\/10.1002\/bies.201000117","journal-title":"BioEssays"},{"issue":"51","key":"3420_CR182","doi-asserted-by":"publisher","first-page":"20651","DOI":"10.1073\/pnas.1314702110","volume":"110","author":"FJ Vonk","year":"2013","unstructured":"Vonk FJ, Casewell NR, Henkel CV et al (2013) The king cobra genome reveals dynamic gene evolution and adaptation in the snake venom system. Proc Natl Acad Sci U S A 110(51):20651\u201320656. https:\/\/doi.org\/10.1073\/pnas.1314702110","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"6","key":"3420_CR183","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pmed.0030184","volume":"3","author":"SC Wagstaff","year":"2006","unstructured":"Wagstaff SC, Laing GD, Theakston RD, Papaspyridis C, Harrison RA (2006) Bioinformatics and multiepitope DNA immunization to design rational snake antivenom. PLoS Med 3(6):e184. https:\/\/doi.org\/10.1371\/journal.pmed.0030184","journal-title":"PLoS Med"},{"key":"3420_CR184","doi-asserted-by":"publisher","first-page":"40","DOI":"10.1016\/j.toxicon.2014.04.012","volume":"86","author":"Y-M Wang","year":"2014","unstructured":"Wang Y-M, Huang K-F, Tsai I-H (2014) Snake venom glutaminyl cyclases: Purification, cloning, kinetic study, recombinant expression, and comparison with the human enzyme. Toxicon 86:40\u201350. https:\/\/doi.org\/10.1016\/j.toxicon.2014.04.012","journal-title":"Toxicon"},{"key":"3420_CR185","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.toxicon.2020.08.012","volume":"187","author":"B Wang","year":"2020","unstructured":"Wang B, Wang Q, Wang C et al (2020) A comparative analysis of the proteomes and biological activities of the venoms from two sea snakes, Hydrophis curtus and Hydrophis cyanocinctus, from Hainan, China. Toxicon 187:35\u201346. https:\/\/doi.org\/10.1016\/j.toxicon.2020.08.012","journal-title":"Toxicon"},{"issue":"9708","key":"3420_CR186","doi-asserted-by":"publisher","first-page":"77","DOI":"10.1016\/s0140-6736(09)61754-2","volume":"375","author":"DA Warrell","year":"2010","unstructured":"Warrell DA (2010) Snake bite. Lancet 375(9708):77\u201388. https:\/\/doi.org\/10.1016\/s0140-6736(09)61754-2","journal-title":"Lancet"},{"issue":"2","key":"3420_CR187","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1016\/0041-0101(91)90107-3","volume":"29","author":"SA Weinstein","year":"1991","unstructured":"Weinstein SA, Schmidt JJ, Bernheimer AW, Smith LA (1991) Characterization and amino acid sequences of two lethal peptides isolated from venom of Wagler\u2019s pit viper. Trimeresurus Wagleri Toxicon 29(2):227\u2013236. https:\/\/doi.org\/10.1016\/0041-0101(91)90107-3","journal-title":"Trimeresurus Wagleri Toxicon"},{"issue":"1","key":"3420_CR188","doi-asserted-by":"publisher","first-page":"80","DOI":"10.1186\/s12862-020-01645-0","volume":"20","author":"EP Westeen","year":"2020","unstructured":"Westeen EP, Durso AM, Grundler MC, Rabosky DL, Davis Rabosky AR (2020) What makes a fang? Phylogenetic and ecological controls on tooth evolution in rear-fanged snakes. BMC Evol Biol 20(1):80. https:\/\/doi.org\/10.1186\/s12862-020-01645-0","journal-title":"BMC Evol Biol"},{"key":"3420_CR189","doi-asserted-by":"publisher","first-page":"75","DOI":"10.1584\/jpestics.30.75","volume":"30","author":"C Wheelock","year":"2005","unstructured":"Wheelock C, Shan GM, Ottea J (2005) Overview of Carboxylesterases and Their Role in the Metabolism of Insecticides. J Pesticide Sci 30:75\u201383. https:\/\/doi.org\/10.1584\/jpestics.30.75","journal-title":"J Pesticide Sci"},{"issue":"4","key":"3420_CR190","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1093\/molbev\/msx334","volume":"35","author":"AC Whittington","year":"2018","unstructured":"Whittington AC, Mason AJ, Rokyta DR (2018) A Single Mutation Unlocks Cascading Exaptations in the Origin of a Potent Pitviper Neurotoxin. Mol Biol Evol 35(4):887\u2013898. https:\/\/doi.org\/10.1093\/molbev\/msx334","journal-title":"Mol Biol Evol"},{"issue":"8","key":"3420_CR191","doi-asserted-by":"publisher","first-page":"1051","DOI":"10.1016\/j.toxicon.2005.02.025","volume":"45","author":"LC Wijeyewickrema","year":"2005","unstructured":"Wijeyewickrema LC, Berndt MC, Andrews RK (2005) Snake venom probes of platelet adhesion receptors and their ligands. Toxicon 45(8):1051\u20131061. https:\/\/doi.org\/10.1016\/j.toxicon.2005.02.025","journal-title":"Toxicon"},{"issue":"4","key":"3420_CR192","doi-asserted-by":"publisher","first-page":"342","DOI":"10.7205\/milmed.170.4.342","volume":"170","author":"N Wongtongkam","year":"2005","unstructured":"Wongtongkam N, Wilde H, Sitthi-Amorn C, Ratanabanangkoon K (2005) A Study of 225 Malayan Pit Viper Bites in Thailand. Mil Med 170(4):342\u2013348. https:\/\/doi.org\/10.7205\/milmed.170.4.342","journal-title":"Mil Med"},{"issue":"4","key":"3420_CR193","doi-asserted-by":"publisher","first-page":"663","DOI":"10.2174\/1871520611313040015","volume":"13","author":"Q Xie","year":"2013","unstructured":"Xie Q, Tang N, Wan R, Qi Y, Lin X, Lin J (2013) Recombinant snake venom cystatin inhibits tumor angiogenesis in vitro and in vivo associated with downregulation of VEGF-A165, Flt-1 and bFGF. Anti Agent Med Chem 13(4):663\u2013671. https:\/\/doi.org\/10.2174\/1871520611313040015","journal-title":"Anti Agent Med Chem"},{"issue":"10","key":"3420_CR194","doi-asserted-by":"publisher","first-page":"303","DOI":"10.3390\/toxins8100303","volume":"8","author":"DC Yang","year":"2016","unstructured":"Yang DC, Deuis JR, Dashevsky D et al (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(10):303","journal-title":"Toxins"},{"issue":"1898","key":"3420_CR195","doi-asserted-by":"publisher","first-page":"20182735","DOI":"10.1098\/rspb.2018.2735","volume":"286","author":"G Zancolli","year":"2019","unstructured":"Zancolli G, Calvete JJ, Cardwell MD et al (2019) When one phenotype is not enough: divergent evolutionary trajectories govern venom variation in a widespread rattlesnake species. Proc Biol Sci 286(1898):20182735. https:\/\/doi.org\/10.1098\/rspb.2018.2735","journal-title":"Proc Biol Sci"}],"container-title":["Archives of Toxicology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00204-022-03420-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00204-022-03420-0\/fulltext.html","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00204-022-03420-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,5]],"date-time":"2023-01-05T11:07:03Z","timestamp":1672916823000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00204-022-03420-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11,27]]},"references-count":194,"journal-issue":{"issue":"1","published-print":{"date-parts":[[2023,1]]}},"alternative-id":["3420"],"URL":"https:\/\/doi.org\/10.1007\/s00204-022-03420-0","relation":{},"ISSN":["0340-5761","1432-0738"],"issn-type":[{"value":"0340-5761","type":"print"},{"value":"1432-0738","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,11,27]]},"assertion":[{"value":"11 October 2022","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 November 2022","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"27 November 2022","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}}]}}