{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,19]],"date-time":"2026-10-19T05:53:11Z","timestamp":1792389191557,"version":"4.4.0"},"reference-count":106,"publisher":"MDPI AG","issue":"11","license":[{"start":{"date-parts":[[2022,11,18]],"date-time":"2022-11-18T00:00:00Z","timestamp":1668729600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Agence Nationale de la Recherche","award":["ANR-18-CE17-0026-01"],"award-info":[{"award-number":["ANR-18-CE17-0026-01"]}]},{"name":"Agence Nationale de la Recherche","award":["ANR-18-CE17-0026-03"],"award-info":[{"award-number":["ANR-18-CE17-0026-03"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Snakebite envenoming is a pathological condition which may occur in response to the injection of venom. Snake venoms contain a complex mixture of biologically active molecules which are responsible for a broad spectrum of clinical manifestations, ranging from local tissue injuries to fatal complications. Snake venom administration commonly provokes local tissue injury often associated with systemic effects, including neurotoxic and cardiotoxic manifestations, bleeding, acute kidney injury, and rhabdomyolysis. An important spectrum of pathogenesis of snake envenomation is the generation of reactive oxygen species (ROS), which can directly provoke tissue damage and also potentiate the deleterious consequences of inflammation at the bite site. Snake venom components known to induce oxidative stress include phospholipases A2, metalloproteinases, three-finger toxins, and L-amino acid oxidase. Clear evidence is mounting suggesting that inflammation and oxidative stress participate in the destructive effects of envenoming, including acute renal failure, tissue necrosis, and unusual susceptibility to bleed (hemorrhage), mostly due to hypocoagulability, neuro\/cardio toxicity, and myonecrosis. Impaired regulation of oxidative stress may also set the stage for secondary\/long-term complications of snakebite envenomation such as musculoskeletal disabilities. Some aspects of natural antioxidant therapeutic options are discussed in this review.<\/jats:p>","DOI":"10.3390\/toxins14110802","type":"journal-article","created":{"date-parts":[[2022,11,21]],"date-time":"2022-11-21T04:33:32Z","timestamp":1669005212000},"page":"802","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":67,"title":["Inflammation and Oxidative Stress in Snakebite Envenomation: A Brief Descriptive Review and Clinical Implications"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7273-2521","authenticated-orcid":false,"given":"Dabor","family":"Resiere","sequence":"first","affiliation":[{"name":"Cardiovascular Research Team EA7525, University of the French West Indies, 97157 Fort de France, France"},{"name":"Department of Critical Care Medicine, Toxicology and Emergency, CHU Martinique, University Hospital of Martinique, 97200 Fort de France, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hossein","family":"Mehdaoui","sequence":"additional","affiliation":[{"name":"Cardiovascular Research Team EA7525, University of the French West Indies, 97157 Fort de France, France"},{"name":"Department of Critical Care Medicine, Toxicology and Emergency, CHU Martinique, University Hospital of Martinique, 97200 Fort de France, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Remi","family":"Neviere","sequence":"additional","affiliation":[{"name":"Cardiovascular Research Team EA7525, University of the French West Indies, 97157 Fort de France, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,11,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"17063","DOI":"10.1038\/nrdp.2017.63","article-title":"Snakebite envenoming","volume":"3","author":"Gutierrez","year":"2017","journal-title":"Nat. Rev. Dis. Prim."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1056\/NEJMra013477","article-title":"Bites of venomous snakes","volume":"347","author":"Gold","year":"2002","journal-title":"N. Engl. J. Med."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1056\/NEJMra2105228","article-title":"Snake Envenomation","volume":"386","author":"Seifert","year":"2022","journal-title":"N. Engl. J. Med."},{"key":"ref_4","first-page":"9","article-title":"Venomous and poisonous animals. III. Elapidae snake envenomation","volume":"67","author":"Chippaux","year":"2007","journal-title":"Med. Trop."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"e057926","DOI":"10.1136\/bmj-2020-057926","article-title":"Managing snakebite","volume":"376","author":"Ralph","year":"2022","journal-title":"BMJ"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/B978-0-12-394384-2.00007-3","article-title":"Biochemistry of envenomation","volume":"57","author":"Kaur","year":"2012","journal-title":"Adv. Clin. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Larr\u00e9ch\u00e9, S., Chippaux, J.P., Chevillard, L., Math\u00e9, S., R\u00e9si\u00e8re, D., Siguret, V., and M\u00e9garbane, B. (2021). Bleeding and Thrombosis: Insights into Pathophysiology of Bothrops Venom-Related Hemostasis Disorders. Int. J. Mol. Sci., 2.","DOI":"10.3390\/ijms22179643"},{"key":"ref_8","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Albulescu, L.O., Clare, R.H., Casewell, N.R., Abd El-Aziz, T.M., Escalante, T., and Rucavado, A. (2021). The Search for Natural and Synthetic Inhibitors That Would Complement Antivenoms as Therapeutics for Snakebite Envenoming. Toxins, 13.","DOI":"10.3390\/toxins13070451"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1128\/CMR.00046-08","article-title":"Pathogen recognition and inflammatory signaling in innate immune defenses","volume":"22","author":"Mogensen","year":"2009","journal-title":"Clin. Microbiol. Rev."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Cavaillon, J.M., and Singer, M. (2018). Inflammation: From Molecular and Cellular Mechanisms to the Clinic, Wiley-VCH.","DOI":"10.1002\/9783527692156"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"a006049","DOI":"10.1101\/cshperspect.a006049","article-title":"Signaling in innate immunity and inflammation","volume":"4","author":"Newton","year":"2012","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"137","DOI":"10.1038\/s41577-020-0391-5","article-title":"Constitutive immune mechanisms: Mediators of host defence and immune regulation","volume":"21","author":"Paludan","year":"2021","journal-title":"Nat. Rev. Immunol."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"661082","DOI":"10.3389\/fimmu.2021.661082","article-title":"Immunological Responses to Envenomation","volume":"12","author":"Ryan","year":"2021","journal-title":"Front. Immunol."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2421","DOI":"10.1038\/jid.2008.118","article-title":"Skin pathology induced by snake venom metalloproteinase: Acute damage, revascularization, and re-epithelization in a mouse ear model","volume":"128","author":"Escalante","year":"2008","journal-title":"J. Investig. Dermatol."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"958","DOI":"10.1016\/j.toxicon.2009.01.038","article-title":"Experimental pathology of local tissue damage induced by Bothrops asper snake venom","volume":"54","author":"Rucavado","year":"2009","journal-title":"Toxicon"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"781","DOI":"10.1038\/s41598-018-37435-4","article-title":"L-amino acid oxidase from Bothrops atrox snake venom triggers autophagy, apoptosis and necrosis in normal human keratinocytes","volume":"9","author":"Stransky","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"526","DOI":"10.1126\/science.1128877","article-title":"Mast cells can enhance resistance to snake and honeybee venoms","volume":"313","author":"Metz","year":"2006","journal-title":"Science"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1007\/s00281-016-0565-1","article-title":"IgE and mast cells in host defense against parasites and venoms","volume":"38","author":"Mukai","year":"2016","journal-title":"Semin. Immunopathol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.alit.2015.09.002","article-title":"Mast cells and IgE in defense against venoms: Possible \u201cgood side\u201d of allergy?","volume":"65","author":"Galli","year":"2016","journal-title":"Allergol. Int."},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Alsolaiss, J., Evans, C.A., Oluoch, G.O., Casewell, N.R., and Harrison, R.A. (2022). Profiling the Murine Acute Phase and Inflammatory Responses to African Snake Venom: An Approach to Inform Acute Snakebite Pathology. Toxins, 14.","DOI":"10.3390\/toxins14040229"},{"key":"ref_21","doi-asserted-by":"crossref","unstructured":"Bickler, P.E. (2020). Amplification of Snake Venom Toxicity by Endogenous Signaling Pathways. Toxins, 12.","DOI":"10.3390\/toxins12020068"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1016\/j.ijbiomac.2017.12.101","article-title":"An overview of the immune modulating effects of enzymatic toxins from snake venoms","volume":"109","author":"Burin","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Avalo, Z., Barrera, M.C., Agudelo-Delgado, M., Tob\u00f3n, G.J., and Ca\u00f1as, C.A. (2022). Biological Effects of Animal Venoms on the Human Immune System. Toxins, 14.","DOI":"10.3390\/toxins14050344"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Cruz, L., and Luo, S. (2017). Inflammatory Action of Secretory Phospholipases A2 from Snake Venoms. Toxins and Drug Discovery. Toxinology, Springer.","DOI":"10.1007\/978-94-007-6452-1"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1016\/j.toxicon.2003.11.006","article-title":"Inflammatory effects of snake venom myotoxic phospholipases A2","volume":"42","author":"Teixeira","year":"2003","journal-title":"Toxicon"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.toxicon.2012.09.006","article-title":"Phospholipases A2: Unveiling the secrets of a functionally versatile group of snake venom toxins","volume":"62","author":"Lomonte","year":"2013","journal-title":"Toxicon"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2082","DOI":"10.3389\/fimmu.2019.02082","article-title":"Inflammation Induced by Platelet-Activating Viperid Snake Venoms: Perspectives on Thromboinflammation","volume":"10","author":"Teixeira","year":"2019","journal-title":"Front. Immunol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Almeida, M.T., Freitas-de-Sousa, L.A., Colombini, M., Gimenes, S.N.C., Kitano, E.S., Faquim-Mauro, E.L., Serrano, S.M.T., and Moura-da-Silva, A.M. (2020). Inflammatory Reaction Induced by Two Metalloproteinases Isolated from Bothrops atrox Venom and by Fragments Generated from the Hydrolysis of Basement Membrane Components. Toxins, 12.","DOI":"10.3390\/toxins12020096"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.toxicon.2012.03.026","article-title":"Jararhagin, a hemorrhagic snake venom metalloproteinase from Bothrops jararaca","volume":"60","author":"Baldo","year":"2012","journal-title":"Toxicon"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"5120","DOI":"10.1021\/pr900489m","article-title":"Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins","volume":"8","author":"Escalante","year":"2009","journal-title":"J. Proteome Res."},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Mac\u00eado, J.K.A., Joseph, J.K., Menon, J., Escalante, T., Rucavado, A., Guti\u00e9rrez, J.M., and Fox, J.W. (2019). Proteomic Analysis of Human Blister Fluids Following Envenomation by Three Snake Species in India: Differential Markers for Venom Mechanisms of Action. Toxins, 11.","DOI":"10.3390\/toxins11050246"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Gimenes, S.N.C., Sachett, J.A.G., Colombini, M., Freitas-de-Sousa, L.A., Ibiapina, H.N.S., Costa, A.G., Santana, M.F., Park, J.J., Sherman, N.E., and Ferreira, L.C.L. (2021). Observation of Bothrops atrox Snake Envenoming Blister Formation from Five Patients: Pathophysiological Insights. Toxins, 13.","DOI":"10.3390\/toxins13110800"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1038\/nature10759","article-title":"Inflammasomes in health and disease","volume":"481","author":"Strowig","year":"2012","journal-title":"Nature"},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Rucavado, A., Nicolau, C.A., Escalante, T., Kim, J., Herrera, C., Guti\u00e9rrez, J.M., and Fox, J.W. (2016). Viperid Envenomation Wound Exudate Contributes to Increased Vascular Permeability via a DAMPs\/TLR-4 Mediated Pathway. Toxins, 8.","DOI":"10.3390\/toxins8120349"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Zornetta, I., Caccin, P., Fernandez, J., Lomonte, B., Gutierrez, J.M., and Montecucco, C. (2012). Envenomations by Bothrops and Crotalus snakes induce the release of mitochondrial alarmins. PLoS Negl. Trop. Dis., 6.","DOI":"10.1371\/journal.pntd.0001526"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Cano-Sanchez, M., Ben-Hassen, K., Louis, O.P., Dantin, F., Gueye, P., Roques, F., Mehdaoui, H., Resiere, D., and Neviere, R. (2022). Bothrops lanceolatus snake venom impairs mitochondrial respiration and induces DNA release in human heart preparation. PLoS Negl. Trop. Dis., 16.","DOI":"10.1371\/journal.pntd.0010523"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"11175","DOI":"10.1038\/s41598-019-47557-y","article-title":"Inhibition of snake venom induced sterile inflammation and PLA2 activity by Titanium dioxide Nanoparticles in experimental animals","volume":"9","author":"Chakrabartty","year":"2019","journal-title":"Sci. Rep."},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Leiguez, E., Giannotti, K.C., Moreira, V., Matsubara, M.H., Guti\u00e9rrez, J.M., Lomonte, B., Rodr\u00edguez, J.P., Balsinde, J., and Teixeira, C. (2014). Critical role of TLR2 and MyD88 for functional response of macrophages to a group IIA-secreted phospholipase A2 from snake venom. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0093741"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.toxicon.2016.04.042","article-title":"The role of TLR2 in the acute inflammatory response induced by Bothrops atrox snake venom","volume":"118","author":"Moreira","year":"2016","journal-title":"Toxicon"},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.toxicon.2013.02.010","article-title":"The crucial role of the MyD88 adaptor protein in the inflammatory response induced by Bothrops atrox venom","volume":"67","author":"Moreira","year":"2013","journal-title":"Toxicon"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.toxicon.2022.05.043","article-title":"Role of Toll-like receptors in local effects in a model of experimental envenoming induced by Bothrops jararacussu snake venom and by two phospholipases A2","volume":"214","author":"Fontana","year":"2022","journal-title":"Toxicon"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.toxicon.2020.09.006","article-title":"Polymorphonuclear neutrophil leukocytes in snakebite envenoming","volume":"187","author":"Zuliani","year":"2020","journal-title":"Toxicon"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1055\/s-0037-1613434","article-title":"Molecular mechanisms of leukocyte recruitment: Organ-specific mechanisms of action","volume":"89","author":"Liu","year":"2003","journal-title":"Thromb. Haemost."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1002\/eji.201142231","article-title":"Neutrophil-active chemokines in in vivo imaging of neutrophil trafficking","volume":"42","author":"Sanz","year":"2012","journal-title":"Eur. J. Immunol."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1080\/0962935021000051548","article-title":"Cell adhesion molecules involved in the leukocyte recruitment induced by venom of the snake Bothrops jararaca","volume":"11","author":"Zamuner","year":"2002","journal-title":"Mediat. Inflamm."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.toxicon.2015.02.014","article-title":"Inflammation and oxidative stress in viper bite: An insight within and beyond","volume":"98","author":"Sunitha","year":"2015","journal-title":"Toxicon"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"e20200053","DOI":"10.1590\/1678-9199-jvatitd-2020-0053","article-title":"Oxidative stress and antioxidant defense in detoxification systems of snake venom-induced toxicity","volume":"26","author":"Dong","year":"2020","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"903","DOI":"10.1016\/0041-0101(81)90089-1","article-title":"Effect of Russell\u2019s venom on lipid peroxidation in organs of the mouse","volume":"19","author":"Ali","year":"1981","journal-title":"Toxicon"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1172\/JCI112001","article-title":"Systemic complement activation, lung injury, and products of lipid peroxidation","volume":"76","author":"Ward","year":"1985","journal-title":"J. Clin. Investig."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/jbt.20121","article-title":"Time-course of lipid peroxidation in different organs of mice treated with Echis pyramidum snake venom","volume":"20","author":"Manthari","year":"2006","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.toxicon.2008.06.015","article-title":"Aminopeptidase activities, oxidative stress and renal function in Crotalus durissus terrificus envenomation in mice","volume":"52","author":"Yamasaki","year":"2008","journal-title":"Toxicon"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1002\/jbt.20376","article-title":"Effects of the Crotalus durissus terrificus snake venom on hepatic metabolism and oxidative stress","volume":"25","author":"Gris","year":"2011","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1186\/1678-9199-20-42","article-title":"Hepatotoxicity and oxidative stress induced by Naja haje crude venom","volume":"20","author":"Dkhil","year":"2014","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.semcancer.2020.05.006","article-title":"Putting the brakes on tumorigenesis with snake venom toxins: New molecular insights for cancer drug discovery","volume":"80","author":"Urra","year":"2022","journal-title":"Semin. Cancer Biol."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2555","DOI":"10.2174\/1568026619666181221120817","article-title":"Animal Venoms have Potential to Treat Cancer","volume":"18","author":"Chatterjee","year":"2018","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/S2221-1691(13)60042-8","article-title":"Therapeutic potential of snake venom in cancer therapy: Current perspectives","volume":"3","author":"Vyas","year":"2013","journal-title":"Asian Pac. J. Trop. Biomed."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"203639","DOI":"10.1155\/2014\/203639","article-title":"Antitumoral activity of snake venom proteins: New trends in cancer therapy","volume":"2014","author":"Calderon","year":"2014","journal-title":"Biomed Res. Int."},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"6485","DOI":"10.2147\/OTT.S115055","article-title":"Snake venom causes apoptosis by increasing the reactive oxygen species in colorectal and breast cancer cell lines","volume":"9","author":"Riyasdeen","year":"2016","journal-title":"Onco. Targets Ther."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"1505","DOI":"10.1016\/S0041-0101(01)00123-4","article-title":"Bothrops asper and Bothrops jararaca snake venoms trigger microbicidal functions of peritoneal leukocytes in vivo","volume":"39","author":"Zamuner","year":"2001","journal-title":"Toxicon"},{"key":"ref_60","first-page":"28","article-title":"Local and systemic biochemical alterations induced by Bothrops atrox snake venom in mice","volume":"3","author":"Kayano","year":"2012","journal-title":"J. Venom Res."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.toxicon.2013.09.019","article-title":"Effect of Bothrops bilineata snake venom on neutrophil function","volume":"76","author":"Pontes","year":"2013","journal-title":"Toxicon"},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"129561","DOI":"10.1016\/j.bbagen.2020.129561","article-title":"The action of Echis carinatus and Naja naja venoms on human neutrophils; an emphasis on NETosis","volume":"1864","author":"Swethakumar","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1007\/s00011-013-0627-y","article-title":"Viper venom-induced oxidative stress and activation of inflammatory cytokines: A therapeutic approach for overlooked issues of snakebite management","volume":"62","author":"Santhosh","year":"2013","journal-title":"Inflamm. Res."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.jab.2014.11.002","article-title":"Systemic oxidative stress in victims of Bothrops snakebites","volume":"13","author":"Strapazzon","year":"2015","journal-title":"J. Appl. Biomed."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"860","DOI":"10.2174\/092986609788923356","article-title":"The phospholipase A2 homologues of snake venoms: Biological activities and their possible adaptive roles","volume":"16","author":"Lomonte","year":"2009","journal-title":"Protein Pept. Lett."},{"key":"ref_66","first-page":"e14662","article-title":"The phospholipase A2 family\u2019s role in metabolic diseases: Focus on skeletal muscle","volume":"9","author":"Gabriel","year":"2021","journal-title":"Physiol. Rep."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1152\/jappl.2000.89.1.72","article-title":"PLA(2) dependence of diaphragm mitochondrial formation of reactive oxygen species","volume":"89","author":"Nethery","year":"2000","journal-title":"J. Appl. Physiol."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1111\/j.1748-1716.2006.01557.x","article-title":"Activation of PLA2 isoforms by cell swelling and ischaemia\/hypoxia","volume":"187","author":"Lambert","year":"2006","journal-title":"Acta Physiol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.toxicon.2003.11.005","article-title":"Skeletal muscle degeneration induced by venom phospholipases A2: Insights into the mechanisms of local and systemic myotoxicity","volume":"42","author":"Ownby","year":"2003","journal-title":"Toxicon"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"719","DOI":"10.1042\/BST20200110","article-title":"Cytotoxicity of snake venom enzymatic toxins: Phospholipase A2 and l-amino acid oxidase","volume":"48","author":"Hiu","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Ranawaka, U.K., Lalloo, D.G., and de Silva, H.J. (2013). Neurotoxicity in snakebite--the limits of our knowledge. PLoS Negl. Trop. Dis., 7.","DOI":"10.1371\/journal.pntd.0002302"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1016\/j.redox.2018.03.012","article-title":"Mitochondrial ROS cause motor deficits induced by synaptic inactivity: Implications for synapse pruning","volume":"16","author":"Sidlauskaite","year":"2018","journal-title":"Redox Biol."},{"key":"ref_73","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Escalante, T., Rucavado, A., and Herrera, C. (2016). Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding. Toxins, 8.","DOI":"10.3390\/toxins8040093"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.bbapap.2006.01.021","article-title":"Isolation and characterization of an apoptotic and platelet aggregation inhibiting L-amino acid oxidase from Vipera berus berus (common viper) venom","volume":"1764","author":"Samel","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.ijbiomac.2016.07.022","article-title":"Mechanism of the cytotoxic effect of l-amino acid oxidase isolated from Bothrops alternatus snake venom","volume":"92","author":"Ribeiro","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1016\/j.toxicon.2007.04.013","article-title":"Molecular characterization of L-amino acid oxidase from king cobra venom","volume":"50","author":"Jin","year":"2007","journal-title":"Toxicon"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"7034","DOI":"10.1016\/j.bmc.2006.06.025","article-title":"Biochemical and functional characterization of an L-amino acid oxidase isolated from Bothrops pirajai snake venom","volume":"14","author":"Izidoro","year":"2006","journal-title":"Bioorg. Med. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"683","DOI":"10.1016\/j.bbagen.2011.04.003","article-title":"Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom","volume":"1810","author":"Naumann","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"270","DOI":"10.2174\/09298673113206660315","article-title":"Cobra cardiotoxins: Membrane interactions and pharmacological potential","volume":"21","author":"Dubovskii","year":"2014","journal-title":"Curr. Med. Chem."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"3169","DOI":"10.1016\/j.febslet.2005.05.006","article-title":"Amphiphilic beta-sheet cobra cardiotoxin targets mitochondria and disrupts its network","volume":"579","author":"Wang","year":"2005","journal-title":"FEBS Lett."},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/j.toxicon.2008.06.013","article-title":"Involvement of mitochondrial alteration and reactive oxygen species generation in Taiwan cobra cardiotoxin-induced apoptotic death of human neuroblastoma SK-N-SH cells","volume":"52","author":"Chen","year":"2008","journal-title":"Toxicon"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1074\/jbc.M113.493270","article-title":"Mitochondrial alterations and oxidative stress in an acute transient mouse model of muscle degeneration: Implications for muscular dystrophy and related muscle pathologies","volume":"289","author":"Gayathri","year":"2014","journal-title":"J. Biol. Chem."},{"key":"ref_83","doi-asserted-by":"crossref","unstructured":"Zhang, B., Li, F., Chen, Z., Shrivastava, I.H., Gasanoff, E.S., and Dagda, R.K. (2019). Naja mossambica mossambica Cobra Cardiotoxin Targets Mitochondria to Disrupt Mitochondrial Membrane Structure and Function. Toxins, 11.","DOI":"10.3390\/toxins11030152"},{"key":"ref_84","doi-asserted-by":"crossref","unstructured":"Li, F., Shrivastava, I.H., Hanlon, P., Dagda, R.K., and Gasanoff, E.S. (2020). Molecular Mechanism by which Cobra Venom Cardiotoxins Interact with the Outer Mitochondrial Membrane. Toxins, 12.","DOI":"10.3390\/toxins12070425"},{"key":"ref_85","doi-asserted-by":"crossref","unstructured":"Waiddyanatha, S., Silva, A., Siribaddana, S., and Isbister, G.K. (2019). Long-term Effects of Snake Envenoming. Toxins, 11.","DOI":"10.3390\/toxins11040193"},{"key":"ref_86","doi-asserted-by":"crossref","unstructured":"Guti\u00e9rrez, J.M., Escalante, T., Hern\u00e1ndez, R., Gastaldello, S., Saravia-Otten, P., and Rucavado, A. (2018). Why is Skeletal Muscle Regeneration Impaired after Myonecrosis Induced by Viperid Snake Venoms?. Toxins, 10.","DOI":"10.3390\/toxins10050182"},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.aanat.2015.07.002","article-title":"Comparative study of muscle regeneration following cardiotoxin and glycerol injury","volume":"202","author":"Mahdy","year":"2015","journal-title":"Ann. Anat."},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"933","DOI":"10.1016\/j.toxicon.2003.11.011","article-title":"Myotoxic phospholipases A2 and the regeneration of skeletal muscles","volume":"42","author":"Harris","year":"2003","journal-title":"Toxicon"},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1007\/s10974-019-09548-4","article-title":"Biotoxins in muscle regeneration research","volume":"40","author":"Mahdy","year":"2019","journal-title":"J. Muscle Res. Cell Motil."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1016\/j.toxicon.2005.08.013","article-title":"Microvessel damage by B. jararacussu snake venom: Pathogenesis and influence on muscle regeneration","volume":"46","author":"Neto","year":"2005","journal-title":"Toxicon"},{"key":"ref_91","doi-asserted-by":"crossref","unstructured":"Hern\u00e1ndez, R., Cabalceta, C., Saravia-Otten, P., Chaves, A., Guti\u00e9rrez, J.M., and Rucavado, A. (2011). Poor regenerative outcome after skeletal muscle necrosis induced by Bothrops asper venom: Alterations in microvasculature and nerves. PLoS ONE, 6.","DOI":"10.1371\/annotation\/9caa2be8-b5e6-4553-8575-f0b575442172"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1089\/ars.2016.6782","article-title":"Redox Control of Skeletal Muscle Regeneration","volume":"27","author":"Pialoux","year":"2017","journal-title":"Antioxid. Redox Signal."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"3829","DOI":"10.1007\/s00467-020-04911-x","article-title":"Snake bite associated with acute kidney injury","volume":"36","author":"Sarkar","year":"2021","journal-title":"Pediatr. Nephrol."},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.toxicon.2015.09.031","article-title":"Bothropoides pauloensis venom effects on isolated perfused kidney and cultured renal tubular epithelial cells","volume":"108","author":"Marinho","year":"2015","journal-title":"Toxicon"},{"key":"ref_95","doi-asserted-by":"crossref","unstructured":"Morais, I.C., Pereira, G.J., Orz\u00e1ez, M., Jorge, R.J., Bincoletto, C., Toyama, M.H., Monteiro, H.S., Smaili, S.S., P\u00e9rez-Pay\u00e1, E., and Martins, A.M. (2015). L-Aminoacid Oxidase from Bothrops leucurus Venom Induces Nephrotoxicity via Apoptosis and Necrosis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0132569"},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.toxicon.2018.06.074","article-title":"Evaluation of KIM-1 as an early biomarker of snakebite-induced AKI in mice","volume":"151","author":"Dantas","year":"2018","journal-title":"Toxicon"},{"key":"ref_97","doi-asserted-by":"crossref","unstructured":"Gois, P.H., Martines, M.S., Ferreira, D., Volpini, R., Canale, D., Malaque, C., Crajoinas, R., Girardi, A.C.C., Massola Shimizu, M.H., and Seguro, A.C. (2017). Allopurinol attenuates acute kidney injury following Bothrops jararaca envenomation. PLoS Negl. Trop. Dis., 11.","DOI":"10.1371\/journal.pntd.0006024"},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"427","DOI":"10.4103\/0971-4065.175987","article-title":"Snakebite mediated acute kidney injury, prognostic predictors, oxidative and carbonyl stress: A prospective study","volume":"26","author":"Mukhopadhyay","year":"2016","journal-title":"Indian J. Nephrol."},{"key":"ref_99","first-page":"342","article-title":"Plasma level of protein modification and inflammatory markers in snakebite induced acute kidney injury patients undergoing haemodialysis\u2014An observational study","volume":"7","author":"Mukherjee","year":"2018","journal-title":"Indian J. Basic Appl. Med. Res."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.toxicon.2013.12.010","article-title":"Effects of N-acetyl-L-cysteine on redox status and markers of renal function in mice inoculated with Bothrops jararaca and Crotalus durissus terrificus venoms","volume":"79","author":"Barone","year":"2014","journal-title":"Toxicon"},{"key":"ref_101","doi-asserted-by":"crossref","unstructured":"Frezzatti, R., and Silveira, P.F. (2011). Allopurinol reduces the lethality associated with acute renal failure induced by Crotalus durissus terrificus snake venom: Comparison with probenecid. PLoS Negl. Trop. Dis., 5.","DOI":"10.1371\/journal.pntd.0001312"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cbi.2010.10.016","article-title":"Quercetin as an inhibitor of snake venom secretory phospholipase A2","volume":"189","author":"Cotrim","year":"2011","journal-title":"Chem. Biol. Interact."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"341270","DOI":"10.1155\/2014\/341270","article-title":"An evaluation of 3-rhamnosylquercetin, a glycosylated form of quercetin, against the myotoxic and edematogenic effects of sPLA 2 from Crotalus durissus terrificus","volume":"2014","author":"Toyama","year":"2014","journal-title":"BioMed Res. Int."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1528","DOI":"10.1016\/j.bbagen.2016.03.031","article-title":"Quercetin-3-O-rhamnoside from Euphorbia hirta protects against snake Venom induced toxicity","volume":"1860","author":"Gopi","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_105","doi-asserted-by":"crossref","unstructured":"Sachetto, A.T.A., Rosa, J.G., and Santoro, M.L. (2018). Rutin (quercetin-3-rutinoside) modulates the hemostatic disturbances and redox imbalance induced by Bothrops jararaca snake venom in mice. PLoS Negl. Trop. Dis., 12.","DOI":"10.1371\/journal.pntd.0006774"},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"842576","DOI":"10.3389\/fimmu.2022.842576","article-title":"Plant-Derived Toxin Inhibitors as Potential Candidates to Complement Antivenom Treatment in Snakebite Envenomations","volume":"13","author":"Maciel","year":"2022","journal-title":"Front. Immunol."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/14\/11\/802\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T01:21:21Z","timestamp":1760145681000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/14\/11\/802"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,11,18]]},"references-count":106,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2022,11]]}},"alternative-id":["toxins14110802"],"URL":"https:\/\/doi.org\/10.3390\/toxins14110802","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2022,11,18]]}}}