{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,24]],"date-time":"2026-04-24T00:55:08Z","timestamp":1776992108722,"version":"3.51.4"},"reference-count":60,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,4,12]],"date-time":"2025-04-12T00:00:00Z","timestamp":1744416000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,4,12]],"date-time":"2025-04-12T00:00:00Z","timestamp":1744416000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100014150","name":"Center of Excellence on Biodiversity","doi-asserted-by":"crossref","award":["BDC PG4-161009"],"award-info":[{"award-number":["BDC PG4-161009"]}],"id":[{"id":"10.13039\/501100014150","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-025-97032-0","type":"journal-article","created":{"date-parts":[[2025,4,12]],"date-time":"2025-04-12T20:42:54Z","timestamp":1744490574000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Comparative in vitro immunoreactivity and protein analysis of Trimeresurus albolabris and Tropidolaemus wagleri venoms"],"prefix":"10.1038","volume":"15","author":[{"given":"Onrapak","family":"Reamtong","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Phorutai","family":"Pearngam","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Panithi","family":"Laoungbua","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Siravit","family":"Sitprija","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tipparat","family":"Thiangtrongjit","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Godchakorn","family":"Srisuk","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Taksa","family":"Vasaruchapong","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Orawan","family":"Khow","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jureeporn","family":"Noiphrom","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Narongsak","family":"Chaiyabutr","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Lawan","family":"Chanhome","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Supeecha","family":"Kumkate","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2025,4,12]]},"reference":[{"key":"97032_CR1","doi-asserted-by":"publisher","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","volume":"3","author":"JM Gutierrez","year":"2017","unstructured":"Gutierrez, J. M. et al. Snakebite envenoming. Nat. Rev. Dis. Primers 3, 17063. https:\/\/doi.org\/10.1038\/nrdp.2017.63 (2017).","journal-title":"Nat. Rev. Dis. Primers"},{"key":"97032_CR2","doi-asserted-by":"publisher","first-page":"1029","DOI":"10.1016\/j.ijbiomac.2020.01.226","volume":"148","author":"M Vanuopadath","year":"2020","unstructured":"Vanuopadath, M., Shaji, S. K., Raveendran, D., Nair, B. G. & Nair, S. S. Delineating the venom toxin arsenal of Malabar pit Viper (Trimeresurus malabaricus) from the Western Ghats of India and evaluating its immunological cross-reactivity and in vitro cytotoxicity. Int. J. Biol. Macromol. 148, 1029\u20131045. https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.01.226 (2020).","journal-title":"Int. J. Biol. Macromol."},{"key":"97032_CR3","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.toxicon.2017.07.017","volume":"137","author":"R Namal Rathnayaka","year":"2017","unstructured":"Namal Rathnayaka, R., Ranathunga, P. & Kularatne, S. A. M. Epidemiology and clinical features of green pit Viper (Trimeresurus trigonocephalus) envenoming in Sri Lanka. Toxicon 137, 99\u2013105. https:\/\/doi.org\/10.1016\/j.toxicon.2017.07.017 (2017).","journal-title":"Toxicon"},{"key":"97032_CR4","doi-asserted-by":"publisher","first-page":"66","DOI":"10.1016\/j.toxicon.2021.09.008","volume":"203","author":"MM Thein","year":"2021","unstructured":"Thein, M. M. et al. Characteristics and significance of green snake bites in Myanmar, especially by the pit Vipers trimeresurus Albolabris and trimeresurus erythrurus. Toxicon 203, 66\u201373. https:\/\/doi.org\/10.1016\/j.toxicon.2021.09.008 (2021).","journal-title":"Toxicon"},{"key":"97032_CR5","doi-asserted-by":"publisher","first-page":"61","DOI":"10.1016\/j.toxicon.2018.11.009","volume":"156","author":"J Blessmann","year":"2018","unstructured":"Blessmann, J. et al. Incidence of snakebites in 3 different geographic regions in Thua Thien Hue Province, central Vietnam: Green pit Vipers and cobras cause the majority of bites. Toxicon 156, 61\u201365. https:\/\/doi.org\/10.1016\/j.toxicon.2018.11.009 (2018).","journal-title":"Toxicon"},{"key":"97032_CR6","first-page":"173","volume":"7","author":"N Pakmanee","year":"1998","unstructured":"Pakmanee, N., Khow, O., Wongtongkam, N., Omori-Satoh, T. & Sitprija, V. Efficacy and cross reactivity of Thai green pit Viper antivenom among venoms of trimeresurus species in Thailand and Japan. J. Nat. Toxins. 7, 173\u2013183 (1998).","journal-title":"J. Nat. Toxins"},{"key":"97032_CR7","doi-asserted-by":"publisher","first-page":"866","DOI":"10.1016\/0035-9203(90)90111-q","volume":"84","author":"RA Hutton","year":"1990","unstructured":"Hutton, R. A. et al. Arboreal green pit Vipers (genus Trimeresurus) of South-East Asia: Bites by T. albolabris and T. macrops in Thailand and a review of the literature. Trans. R Soc. Trop. Med. Hyg. 84, 866\u2013874. https:\/\/doi.org\/10.1016\/0035-9203(90)90111-q (1990).","journal-title":"Trans. R Soc. Trop. Med. Hyg."},{"key":"97032_CR8","doi-asserted-by":"publisher","first-page":"695","DOI":"10.2147\/TCRM.S261303","volume":"16","author":"S Thumtecho","year":"2020","unstructured":"Thumtecho, S. et al. Hematotoxic manifestations and management of green pit Viper bites in Thailand. Ther. Clin. Risk Manag. 16, 695\u2013704. https:\/\/doi.org\/10.2147\/TCRM.S261303 (2020).","journal-title":"Ther. Clin. Risk Manag."},{"key":"97032_CR9","doi-asserted-by":"publisher","unstructured":"Kumkate, S. et al. Venomics and cellular toxicity of Thai pit Vipers (Trimeresurus macrops and T. hageni). Toxins (Basel) 12. https:\/\/doi.org\/10.3390\/toxins12010054 (2020).","DOI":"10.3390\/toxins12010054"},{"key":"97032_CR10","doi-asserted-by":"publisher","first-page":"105528","DOI":"10.1016\/j.actatropica.2020.105528","volume":"209","author":"JL Liew","year":"2020","unstructured":"Liew, J. L., Tan, N. H. & Tan, C. H. Proteomics and preclinical antivenom neutralization of the Mangrove pit Viper (Trimeresurus purpureomaculatus, Malaysia) and white-lipped pit Viper (Trimeresurus albolabris, Thailand) venoms. Acta Trop. 209, 105528. https:\/\/doi.org\/10.1016\/j.actatropica.2020.105528 (2020).","journal-title":"Acta Trop."},{"key":"97032_CR11","doi-asserted-by":"publisher","first-page":"e20210103","DOI":"10.1590\/1678-9199-jvatitd-2021-0103","volume":"28","author":"S Anita","year":"2022","unstructured":"Anita, S. et al. Venom composition of trimeresurus Albolabris, T. insularis, T. puniceus and T. purpureomaculatus from Indonesia. J. Venom. Anim. Toxins Incl. Trop. Dis. 28, e20210103. https:\/\/doi.org\/10.1590\/1678-9199-jvatitd-2021-0103 (2022).","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"issue":"1-40","key":"97032_CR12","first-page":"41","volume":"1644","author":"G Vogel","year":"2007","unstructured":"Vogel, G., David, P., Lutz, M., Van Rooijen, J. & Vidal, N. Revision of the tropidolaemus wagleri-complex (Serpentes: Viperidae: Crotalinae). I. Definition of included taxa and redescription of tropidolaemus wagleri (Boie, 1827). Zootaxa 1644(1\u201340), 41\u201340 (2007).","journal-title":"Zootaxa"},{"key":"97032_CR13","doi-asserted-by":"publisher","first-page":"349","DOI":"10.1016\/0041-0101(89)90182-7","volume":"27","author":"NH Tan","year":"1989","unstructured":"Tan, N. H. & Tan, C. S. The enzymatic activities and lethal toxins of trimeresurus wagleri (speckled pit viper) venom. Toxicon 27, 349\u2013357. https:\/\/doi.org\/10.1016\/0041-0101(89)90182-7 (1989).","journal-title":"Toxicon"},{"key":"97032_CR14","doi-asserted-by":"publisher","first-page":"43237","DOI":"10.1038\/srep43237","volume":"7","author":"CH Tan","year":"2017","unstructured":"Tan, C. H., Tan, K. Y., Yap, M. K. & Tan, N. H. 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 (2017).","journal-title":"Sci. Rep."},{"key":"97032_CR15","doi-asserted-by":"publisher","unstructured":"Zainal Abidin, S. A. et al. Proteomic characterization and comparison of Malaysian tropidolaemus wagleri and cryptelytrops purpureomaculatus venom using Shotgun-Proteomics. Toxins (Basel) 8. https:\/\/doi.org\/10.3390\/toxins8100299 (2016).","DOI":"10.3390\/toxins8100299"},{"key":"97032_CR16","doi-asserted-by":"publisher","first-page":"111","DOI":"10.1016\/0041-0101(94)00134-t","volume":"33","author":"WW Lin","year":"1995","unstructured":"Lin, W. W., Smith, L. A. & Lee, C. Y. A study on the cause of death due to waglerin-I, a toxin from trimeresurus wagleri. Toxicon 33, 111\u2013114. https:\/\/doi.org\/10.1016\/0041-0101(94)00134-t (1995).","journal-title":"Toxicon"},{"key":"97032_CR17","doi-asserted-by":"publisher","first-page":"543","DOI":"10.1016\/S0022-3565(24)38167-4","volume":"289","author":"JJ McArdle","year":"1999","unstructured":"McArdle, J. J. et al. Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor. J. Pharmacol. Exp. Ther. 289, 543\u2013550 (1999).","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"97032_CR18","doi-asserted-by":"publisher","first-page":"8","DOI":"10.1007\/s00239-016-9764-6","volume":"84","author":"J Debono","year":"2017","unstructured":"Debono, J. et al. Viper venom Botox: The molecular origin and evolution of the Waglerin peptides used in Anti-Wrinkle skin cream. J. Mol. Evol. 84, 8\u201311. https:\/\/doi.org\/10.1007\/s00239-016-9764-6 (2017).","journal-title":"J. Mol. Evol."},{"key":"97032_CR19","doi-asserted-by":"publisher","first-page":"32","DOI":"10.1016\/j.toxicon.2017.10.014","volume":"140","author":"CH Tan","year":"2017","unstructured":"Tan, C. H. et al. Cross reactivity and lethality neutralization of venoms of Indonesian trimeresurus complex species by Thai green pit Viper antivenom. Toxicon 140, 32\u201337. https:\/\/doi.org\/10.1016\/j.toxicon.2017.10.014 (2017).","journal-title":"Toxicon"},{"key":"97032_CR20","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1580\/1080-6032(2001)012[0017:vshit]2.0.co;2","volume":"12","author":"L Chanhome","year":"2001","unstructured":"Chanhome, L., Jintakune, P., Wilde, H. & Cox, M. J. Venomous snake husbandry in Thailand. Wilderness Environ. Med. 12, 17\u201323. https:\/\/doi.org\/10.1580\/1080-6032(2001)012[0017:vshit]2.0.co;2 (2001).","journal-title":"Wilderness Environ. Med."},{"key":"97032_CR21","doi-asserted-by":"publisher","first-page":"e0260496","DOI":"10.1371\/journal.pone.0260496","volume":"16","author":"S Sitprija","year":"2021","unstructured":"Sitprija, S. et al. Proteomics and immunocharacterization of Asian mountain pit Viper (Ovophis monticola) venom. PLoS One. 16, e0260496. https:\/\/doi.org\/10.1371\/journal.pone.0260496 (2021).","journal-title":"PLoS One"},{"key":"97032_CR22","doi-asserted-by":"publisher","first-page":"1526","DOI":"10.3390\/toxins6051526","volume":"6","author":"W Danpaiboon","year":"2014","unstructured":"Danpaiboon, W. et al. Ophiophagus Hannah Venom: proteome, components bound by Naja kaouthia antivenin and neutralization by Naja kaouthia neurotoxin-specific human ScFv. Toxins (Basel) 6, 1526\u20131558. https:\/\/doi.org\/10.3390\/toxins6051526 (2014).","journal-title":"Toxins (Basel)"},{"key":"97032_CR23","doi-asserted-by":"publisher","first-page":"e4497","DOI":"10.1002\/pro.4497","volume":"31","author":"JN Clifford","year":"2022","unstructured":"Clifford, J. N. et al. BepiPred-3.0: Improved B-cell epitope prediction using protein Language models. Protein Sci. 31, e4497. https:\/\/doi.org\/10.1002\/pro.4497 (2022).","journal-title":"Protein Sci."},{"key":"97032_CR24","doi-asserted-by":"publisher","first-page":"5425","DOI":"10.1021\/bi00367a013","volume":"25","author":"JM Parker","year":"1986","unstructured":"Parker, J. M., Guo, D. & Hodges, R. S. New hydrophilicity scale derived from high-performance liquid chromatography peptide retention data: Correlation of predicted surface residues with antigenicity and X-ray-derived accessible sites. Biochemistry 25, 5425\u20135432. https:\/\/doi.org\/10.1021\/bi00367a013 (1986).","journal-title":"Biochemistry"},{"key":"97032_CR25","doi-asserted-by":"publisher","first-page":"836","DOI":"10.1128\/JVI.55.3.836-839.1985","volume":"55","author":"EA Emini","year":"1985","unstructured":"Emini, E. A., Hughes, J. V., Perlow, D. S. & Boger, J. Induction of hepatitis A virus-neutralizing antibody by a virus-specific synthetic peptide. J. Virol. 55, 836\u2013839. https:\/\/doi.org\/10.1128\/JVI.55.3.836-839.1985 (1985).","journal-title":"J. Virol."},{"key":"97032_CR26","doi-asserted-by":"publisher","first-page":"172","DOI":"10.1016\/0014-5793(90)80535-q","volume":"276","author":"AS Kolaskar","year":"1990","unstructured":"Kolaskar, A. S. & Tongaonkar, P. C. A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett. 276, 172\u2013174. https:\/\/doi.org\/10.1016\/0014-5793(90)80535-q (1990).","journal-title":"FEBS Lett."},{"key":"97032_CR27","doi-asserted-by":"publisher","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","volume":"596","author":"J Jumper","year":"2021","unstructured":"Jumper, J. et al. Highly accurate protein structure prediction with alphafold. Nature 596, 583\u2013589. https:\/\/doi.org\/10.1038\/s41586-021-03819-2 (2021).","journal-title":"Nature"},{"key":"97032_CR28","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1093\/nar\/28.1.235","volume":"28","author":"HM Berman","year":"2000","unstructured":"Berman, H. M. et al. The protein data bank. Nucleic Acids Res. 28, 235\u2013242. https:\/\/doi.org\/10.1093\/nar\/28.1.235 (2000).","journal-title":"Nucleic Acids Res."},{"key":"97032_CR29","doi-asserted-by":"publisher","first-page":"50","DOI":"10.1016\/j.ympev.2016.07.029","volume":"105","author":"LRV Alencar","year":"2016","unstructured":"Alencar, L. R. V. et al. Diversification in vipers: Phylogenetic relationships, time of divergence and shifts in speciation rates. Mol. Phylogenet Evol. 105, 50\u201362. https:\/\/doi.org\/10.1016\/j.ympev.2016.07.029 (2016).","journal-title":"Mol. Phylogenet Evol."},{"key":"97032_CR30","doi-asserted-by":"publisher","first-page":"e2814","DOI":"10.1371\/journal.pntd.0002814","volume":"8","author":"KM Yamashita","year":"2014","unstructured":"Yamashita, K. M., Alves, A. F., Barbaro, K. C. & Santoro, M. L. Bothrops jararaca venom metalloproteinases are essential for coagulopathy and increase plasma tissue factor levels during envenomation. PLoS Negl. Trop. Dis. 8, e2814. https:\/\/doi.org\/10.1371\/journal.pntd.0002814 (2014).","journal-title":"PLoS Negl. Trop. Dis."},{"key":"97032_CR31","doi-asserted-by":"publisher","first-page":"100052","DOI":"10.1016\/j.toxcx.2020.100052","volume":"7","author":"OT Olaoba","year":"2020","unstructured":"Olaoba, O. T., Dos Santos, K., Selistre-de-Araujo, P., de Ferreira, D. H. & H. S. & Snake venom metalloproteinases (SVMPs): A structure\u2013function update. Toxicon X 7, 100052. https:\/\/doi.org\/10.1016\/j.toxcx.2020.100052 (2020).","journal-title":"Toxicon X"},{"key":"97032_CR32","doi-asserted-by":"publisher","first-page":"3476","DOI":"10.1016\/j.bbagen.2013.02.007","volume":"1830","author":"AK Mukherjee","year":"2013","unstructured":"Mukherjee, A. K. & Mackessy, S. P. Biochemical and Pharmacological properties of a new thrombin-like Serine protease (Russelobin) from the venom of Russell\u2019s Viper (Daboia russelii russelii) and assessment of its therapeutic potential. Biochim. Biophys. Acta 1830, 3476\u20133488. https:\/\/doi.org\/10.1016\/j.bbagen.2013.02.007 (2013).","journal-title":"Biochim. Biophys. Acta"},{"key":"97032_CR33","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1016\/0041-0101(94)90010-8","volume":"32","author":"NH Tan","year":"1994","unstructured":"Tan, N. H., Choy, S. K., Chin, K. M. & Ponnudurai, G. Cross-reactivity of monovalent and polyvalent trimeresurus antivenoms with venoms from various species of trimeresurus (lance-headed pit viper) snake. Toxicon 32, 849\u2013853. https:\/\/doi.org\/10.1016\/0041-0101(94)90010-8 (1994).","journal-title":"Toxicon"},{"key":"97032_CR34","doi-asserted-by":"publisher","unstructured":"Tan, C. H. et al. Venomics of trimeresurus (Popeia) nebularis, the Cameron highlands pit Viper from Malaysia: Insights into venom proteome, toxicity and neutralization of antivenom. Toxins (Basel) 11. https:\/\/doi.org\/10.3390\/toxins11020095 (2019).","DOI":"10.3390\/toxins11020095"},{"key":"97032_CR35","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1016\/j.toxlet.2019.09.003","volume":"316","author":"J Debono","year":"2019","unstructured":"Debono, J., Bos, M. H. A., Frank, N. & Fry, B. Clinical implications of differential antivenom efficacy in neutralising coagulotoxicity produced by venoms from species within the arboreal Viperid snake genus trimeresurus. Toxicol. Lett. 316, 35\u201348. https:\/\/doi.org\/10.1016\/j.toxlet.2019.09.003 (2019).","journal-title":"Toxicol. Lett."},{"key":"97032_CR36","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1016\/j.actatropica.2013.12.015","volume":"132","author":"PK Leong","year":"2014","unstructured":"Leong, P. K. et al. Cross neutralization of common Southeast Asian Viperid venoms by a Thai polyvalent snake antivenom (Hemato polyvalent snake Antivenom). Acta Trop. 132, 7\u201314. https:\/\/doi.org\/10.1016\/j.actatropica.2013.12.015 (2014).","journal-title":"Acta Trop."},{"key":"97032_CR37","doi-asserted-by":"publisher","first-page":"106495","DOI":"10.1016\/j.actatropica.2022.106495","volume":"232","author":"KY Tan","year":"2022","unstructured":"Tan, K. Y., Shamsuddin, N. N. & Tan, C. H. Sharp-nosed pit Viper (Deinagkistrodon acutus) from Taiwan and China: A comparative study on venom toxicity and neutralization by two specific antivenoms across the Strait. Acta Trop. 232, 106495. https:\/\/doi.org\/10.1016\/j.actatropica.2022.106495 (2022).","journal-title":"Acta Trop."},{"key":"97032_CR38","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1016\/0041-0101(91)90107-3","volume":"29","author":"SA Weinstein","year":"1991","unstructured":"Weinstein, S. A., Schmidt, J. J., Bernheimer, A. W. & Smith, L. A. Characterization and amino acid sequences of two lethal peptides isolated from venom of Wagler\u2019s pit Viper, trimeresurus wagleri. Toxicon 29, 227\u2013236. https:\/\/doi.org\/10.1016\/0041-0101(91)90107-3 (1991).","journal-title":"Toxicon"},{"key":"97032_CR39","doi-asserted-by":"publisher","unstructured":"Damm, M., Hempel, B. F., Nalbantsoy, A. & Sussmuth, R. D. Comprehensive snake venomics of the Okinawa Habu pit Viper, protobothrops flavoviridis, by complementary mass spectrometry-guided approaches. Molecules 23. https:\/\/doi.org\/10.3390\/molecules23081893 (2018).","DOI":"10.3390\/molecules23081893"},{"key":"97032_CR40","doi-asserted-by":"publisher","first-page":"140795","DOI":"10.1016\/j.bbapap.2022.140795","volume":"1870","author":"C Bras-Costa","year":"2022","unstructured":"Bras-Costa, C. et al. Profilings of subproteomes of lectin-binding proteins of nine Bothrops venoms reveal variability driven by different glycan types. Biochim. Biophys. Acta Proteins Proteom. 1870, 140795. https:\/\/doi.org\/10.1016\/j.bbapap.2022.140795 (2022).","journal-title":"Biochim. Biophys. Acta Proteins Proteom."},{"key":"97032_CR41","doi-asserted-by":"publisher","first-page":"108625","DOI":"10.1016\/j.cbpc.2019.108625","volume":"227","author":"J Debono","year":"2020","unstructured":"Debono, J., Dashevsky, D., Nouwens, A. & Fry, B. G. The sweet side of Venom: Glycosylated prothrombin activating metalloproteases from dispholidus typus (boomslang) and Thelotornis mossambicanus (twig snake). Comp. Biochem. Physiol. C Toxicol. Pharmacol. 227, 108625. https:\/\/doi.org\/10.1016\/j.cbpc.2019.108625 (2020).","journal-title":"Comp. Biochem. Physiol. C Toxicol. Pharmacol."},{"key":"97032_CR42","doi-asserted-by":"publisher","first-page":"383","DOI":"10.1021\/pr034052+","volume":"3","author":"J Nawarak","year":"2004","unstructured":"Nawarak, J., Phutrakul, S. & Chen, S. T. Analysis of lectin-bound glycoproteins in snake venom from the Elapidae and Viperidae families. J. Proteome Res. 3, 383\u2013392. https:\/\/doi.org\/10.1021\/pr034052+ (2004).","journal-title":"J. Proteome Res."},{"key":"97032_CR43","doi-asserted-by":"publisher","first-page":"e20210080","DOI":"10.1590\/1678-9199-JVATITD-2021-0080","volume":"28","author":"L Chanhome","year":"2022","unstructured":"Chanhome, L. et al. Biochemical and proteomic analyses of venom from a new pit Viper, protobothrops Kelomohy. J. Venom. Anim. Toxins Incl. Trop. Dis. 28, e20210080. https:\/\/doi.org\/10.1590\/1678-9199-JVATITD-2021-0080 (2022).","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"97032_CR44","doi-asserted-by":"publisher","first-page":"1222","DOI":"10.1016\/j.toxicon.2009.12.018","volume":"55","author":"C Correa-Netto","year":"2010","unstructured":"Correa-Netto, C. et al. Immunome and venome of Bothrops jararacussu: A proteomic approach to study the molecular immunology of snake toxins. Toxicon 55, 1222\u20131235. https:\/\/doi.org\/10.1016\/j.toxicon.2009.12.018 (2010).","journal-title":"Toxicon"},{"key":"97032_CR45","doi-asserted-by":"publisher","first-page":"11328","DOI":"10.1038\/s41598-022-13376-x","volume":"12","author":"SK Menzies","year":"2022","unstructured":"Menzies, S. K. et al. Virus-like particles displaying conserved toxin epitopes stimulate polyspecific, murine antibody responses capable of snake venom recognition. Sci. Rep. 12, 11328. https:\/\/doi.org\/10.1038\/s41598-022-13376-x (2022).","journal-title":"Sci. Rep."},{"key":"97032_CR46","doi-asserted-by":"publisher","first-page":"719","DOI":"10.1042\/bst20200110","volume":"48","author":"JJ Hiu","year":"2020","unstructured":"Hiu, J. J. & Yap, M. K. K. Cytotoxicity of snake venom enzymatic toxins: Phospholipase A2 and l-amino acid oxidase. Biochem. Soc. Trans. 48, 719\u2013731. https:\/\/doi.org\/10.1042\/bst20200110 (2020).","journal-title":"Biochem. Soc. Trans."},{"key":"97032_CR47","doi-asserted-by":"publisher","unstructured":"Zambelli, V. O., Picolo, G., Fernandes, C. A. H., Fontes, M. R. M. & Cury, Y. Secreted phospholipases A2 from animal venoms in pain and analgesia. Toxins (Basel) 9. https:\/\/doi.org\/10.3390\/toxins9120406 (2017).","DOI":"10.3390\/toxins9120406"},{"key":"97032_CR48","doi-asserted-by":"publisher","unstructured":"Teixeira, C. F., Landucci, E. C., Antunes, E., Chacur, M. & Cury, Y. Inflammatory effects of snake venom myotoxic phospholipases A2. Toxicon 42, 947\u2013962 (2003). https:\/\/doi.org\/10.1016\/j.toxicon.2003.11.006","DOI":"10.1016\/j.toxicon.2003.11.006"},{"key":"97032_CR49","doi-asserted-by":"publisher","first-page":"864","DOI":"10.1271\/bbb.100783","volume":"75","author":"T Murakami","year":"2011","unstructured":"Murakami, T. et al. A [Lys49]phospholipase A2 from protobothrops flavoviridis venom induces caspase-independent apoptotic cell death accompanied by rapid plasma-membrane rupture in human leukemia cells. Biosci. Biotechnol. Biochem. 75, 864\u2013870. https:\/\/doi.org\/10.1271\/bbb.100783 (2011).","journal-title":"Biosci. Biotechnol. Biochem."},{"key":"97032_CR50","doi-asserted-by":"publisher","unstructured":"Bickler, P. E. Amplification of snake venom toxicity by endogenous signaling pathways. Toxins (Basel) 12. https:\/\/doi.org\/10.3390\/toxins12020068 (2020).","DOI":"10.3390\/toxins12020068"},{"key":"97032_CR51","doi-asserted-by":"publisher","first-page":"57","DOI":"10.1016\/j.toxicon.2020.06.010","volume":"185","author":"W Ning","year":"2020","unstructured":"Ning, W., Yuanyuan, L., Lipeng, Z., Xiang, L. & Chunhong, H. Targeted identification of C-type lectins in snake venom by 2DE and Western blot. Toxicon 185, 57\u201363. https:\/\/doi.org\/10.1016\/j.toxicon.2020.06.010 (2020).","journal-title":"Toxicon"},{"key":"97032_CR52","doi-asserted-by":"publisher","first-page":"414","DOI":"10.1016\/j.bcmd.2006.03.001","volume":"36","author":"XY Du","year":"2006","unstructured":"Du, X. Y., Sim, D. S., Lee, W. H. & Zhang, Y. Blood cells as targets of snake toxins. Blood Cells Mol. Dis. 36, 414\u2013421. https:\/\/doi.org\/10.1016\/j.bcmd.2006.03.001 (2006).","journal-title":"Blood Cells Mol. Dis."},{"key":"97032_CR53","doi-asserted-by":"publisher","first-page":"59","DOI":"10.1016\/j.toxicon.2016.12.007","volume":"126","author":"MA Sartim","year":"2017","unstructured":"Sartim, M. A., Pinheiro, M. P., de P\u00e1dua, R. A. P., Sampaio, S. V. & Nonato, M. C. Structural and binding studies of a C-type galactose-binding lectin from Bothrops Jararacussu snake venom. Toxicon 126, 59\u201369. https:\/\/doi.org\/10.1016\/j.toxicon.2016.12.007 (2017).","journal-title":"Toxicon"},{"key":"97032_CR54","doi-asserted-by":"publisher","first-page":"790","DOI":"10.1186\/1471-2164-14-790","volume":"14","author":"SD Aird","year":"2013","unstructured":"Aird, S. D. et al. Quantitative high-throughput profiling of snake venom gland transcriptomes and proteomes (Ovophis okinavensis and Protobothrops flavoviridis). BMC Genom. 14, 790. https:\/\/doi.org\/10.1186\/1471-2164-14-790 (2013).","journal-title":"BMC Genom."},{"key":"97032_CR55","doi-asserted-by":"publisher","unstructured":"Larr\u00e9ch\u00e9, S. et al. Bleeding and thrombosis: insights into pathophysiology of Bothrops Venom-related hemostasis disorders. Int. J. Mol. Sci. 22 https:\/\/doi.org\/10.3390\/ijms22179643 (2021).","DOI":"10.3390\/ijms22179643"},{"key":"97032_CR56","doi-asserted-by":"publisher","first-page":"296","DOI":"10.1016\/j.ijbiomac.2019.12.015","volume":"144","author":"GN Cezarette","year":"2020","unstructured":"Cezarette, G. N., Sartim, M. A. & Sampaio, S. V. Inflammation and coagulation crosstalk induced by BJcuL, a galactose-binding lectin isolated from Bothrops Jararacussu snake venom. Int. J. Biol. Macromol. 144, 296\u2013304. https:\/\/doi.org\/10.1016\/j.ijbiomac.2019.12.015 (2020).","journal-title":"Int. J. Biol. Macromol."},{"key":"97032_CR57","doi-asserted-by":"publisher","unstructured":"Hatakeyama, D. M. et al. Venom complexity of Bothrops atrox (common lancehead) siblings. J. Venom Anim. Toxins Incl. Trop. Dis. 26, e20200018 (2020). https:\/\/doi.org\/10.1590\/1678-9199-JVATITD-2020-0018","DOI":"10.1590\/1678-9199-JVATITD-2020-0018"},{"key":"97032_CR58","doi-asserted-by":"publisher","unstructured":"Rokyta, D. R., Margres, M. J. & Calvin, K. Post-transcriptional Mechanisms Contribute Little to Phenotypic Variation in Snake Venoms. G3 (Bethesda) 5, 2375\u20132382 (2015). https:\/\/doi.org\/10.1534\/g3.115.020578","DOI":"10.1534\/g3.115.020578"},{"key":"97032_CR59","doi-asserted-by":"publisher","unstructured":"Costa, C. R. C. et al. Edema induced by a crotalus durissus Terrificus venom Serine protease (Cdtsp 2) involves the PAR pathway and PKC and PLC activation. Int. J. Mol. Sci. 19. https:\/\/doi.org\/10.3390\/ijms19082405 (2018).","DOI":"10.3390\/ijms19082405"},{"key":"97032_CR60","doi-asserted-by":"publisher","first-page":"12271","DOI":"10.1038\/s41598-023-39222-2","volume":"13","author":"JJ Hiu","year":"2023","unstructured":"Hiu, J. J., Fung, J. K. Y., Tan, H. S. & Yap, M. K. K. Unveiling the functional epitopes of Cobra venom cytotoxin by immunoinformatics and epitope-omic analyses. Sci. Rep. 13, 12271. https:\/\/doi.org\/10.1038\/s41598-023-39222-2 (2023).","journal-title":"Sci. Rep."}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-97032-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-97032-0","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-97032-0.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,4,12]],"date-time":"2025-04-12T20:42:56Z","timestamp":1744490576000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-97032-0"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,4,12]]},"references-count":60,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["97032"],"URL":"https:\/\/doi.org\/10.1038\/s41598-025-97032-0","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,4,12]]},"assertion":[{"value":"5 December 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 April 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 April 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"The authors declare no competing interests.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"12693"}}