Gutiérrez, J. M. et al. Snakebite envenoming. Nat. Rev. Dis. Prim. 3, 17063 (2017).
Google Scholar
Alirol, E., Sharma, S. Okay., Bawaskar, H. S., Kuch, U. & Chappuis, F. Snake chunk in south asia: A overview. PLoS Negl. Trop. Dis. 4, e603 (2010).
Google Scholar
Warrell, D. A. Guidelines of Management of Snake chunk. Lancet 375, 77–88 (2010).
Google Scholar
Gutiérrez, J. M., Theakston, R. D. G. & Warrell, D. A. Confronting the uncared for drawback of snake chunk envenoming: The want for a worldwide partnership. PLoS Med. 3, 0727–0731 (2006).
Google Scholar
Waiddyanatha, S., Silva, A., Siribaddana, S. & Isbister, G. Okay. Long-term results of snake envenoming. Toxins (Basel). 11, 193 (2019).
Google Scholar
Longbottom, J. et al. Vulnerability to snakebite envenoming: a worldwide mapping of hotspots. Lancet 392, 673–684 (2018).
Google Scholar
Vaiyapuri, S. et al. Snakebite and its socio-economic influence on the agricultural inhabitants of Tamil Nadu, India. PLoS One 8, e80090 (2013).
Google Scholar
Pyron, R. A., Burbrink, F. T. & Wiens, J. J. A phylogeny and revised classification of Squamata, together with 4161 species of lizards and snakes. BMC Evol. Biol. 13, 93 (2013).
Google Scholar
Fry, B. G. et al. Molecular evolution and phylogeny of elapid snake venom three-finger toxins. J. Mol. Evol. 57, 110–129 (2003).
Google Scholar
Harris, J. B. & Scott-Davey, T. Secreted Phospholipases A 2 of Snake Venoms: Effects on the Peripheral Neuromuscular System with Comments on the Role of Phospholipases A 2 in Disorders of the CNS and Their Uses in Industry. Toxins (Basel). 5, 2533–2571 (2013).
Google Scholar
Utkin, Y., Sunagar, Okay., Jackson, T. N. W., Reeks, T. & Fry, B. Three finger toxins (3FTXs). In Venomous Reptiles and Their Toxins: Evolution, Pathophysiology and Biodiscovery (ed. Fry, B.) 215–227 (2015).
Karlsson, E., Mbugua, P. M. & Rodriguez-Ithurralde, D. Fasciculins, anticholinesterase toxins from the venom of the inexperienced mamba Dendroaspis angusticeps. J. Physiol. 79, 232–240 (1984).
Google Scholar
Harvey, A. L. Twenty years of dendrotoxins. Toxicon 39, 15–26 (2001).
Google Scholar
Harvey, A. L. & Robertson, B. Dendrotoxins: structure-activity relationships and results on potassium ion channels. Curr. Med. Chem. 11, 3065–3072 (2004).
Google Scholar
White, J. Snake venoms and coagulopathy. Toxicon 45, 951–967 (2005).
Google Scholar
Berling, I. & Isbister, G. Okay. Hematologic Effects and Complications of Snake Envenoming. Transfus. Med. Rev. 29, 82–89 (2015).
Google Scholar
Gutiérrez, J. M., Rucavado, A., Escalante, T. & Díaz, C. Hemorrhage induced by snake venom metalloproteinases: Biochemical and biophysical mechanisms concerned in microvessel injury. Toxicon 45, 997–1011 (2005).
Google Scholar
Gutiérrez, J. M., Escalante, T., Rucavado, A. & Herrera, C. Hemorrhage attributable to snake venom metalloproteinases: A journey of discovery and understanding. Toxins (Basel). 8, 93 (2016).
Google Scholar
Escalante, T. et al. Role of collagens and perlecan in microvascular stability: Exploring the mechanism of capillary vessel injury by snake venom metalloproteinases. PLoS One 6, e28017 (2011).
Google Scholar
Teixeira, C., Moreira, C. & Gutierrez, J. M. Venoms. In Inflammation: From Molecular and Cellular Mechanisms to the Clinic (ed. Cavaillon, J. M., Singer, M.) 99–128 (Wiley, 2018).
Gutiérrez, J. M. & Ownby, C. L. Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of native and systemic myotoxicity. Toxicon 42, 915–931 (2003).
Google Scholar
Montecucco, C., Gutiérrez, J. M. & Lomonte, B. Cellular pathology induced by snake venom phospholipase A2 myotoxins and neurotoxins: Common points of their mechanisms of motion. Cell. Mol. Life Sci. 65, 2897–2912 (2008).
Google Scholar
Sitprija, V. Animal toxins and the kidney. Nat. Clin. Pract. Nephrol. 4, 616–627 (2008).
Google Scholar
Gasanov, S. E., Dagda, R. Okay. & Rael, E. D. Snake Venom Cytotoxins, Phospholipase A2 s, and Zn2+ -dependent Metalloproteinases: Mechanisms of Action and Pharmacological Relevance. J. Clin. Toxicol. 4, 1000181 (2014).
Google Scholar
Rivel, M. et al. Pathogenesis of dermonecrosis induced by venom of the spitting cobra, Naja nigricollis: An experimental research in mice. Toxicon 119, 171–179 (2016).
Google Scholar
Gutiérrez, J. M. & Rucavado, A. Snake venom metalloproteinases: Their position within the pathogenesis of native tissue injury. Biochimie 82, 841–850 (2000).
Google Scholar
Jiménez, N., Escalante, T., Gutiérrez, J. M. & Rucavado, A. Skin pathology induced by snake venom metalloproteinase: Acute injury, revascularization, and re-epithelization in a mouse ear mannequin. J. Invest. Dermatol. 128, 2421–2428 (2008).
Google Scholar
Dubovskii, P., Konshina, A. & Efremov, R. Cobra Cardiotoxins: Membrane Interactions and Pharmacological Potential. Curr. Med. Chem. 21, 270–287 (2013).
Google Scholar
Sarkar, B., Maitra, S. & Ghosh, B. The Effect of Neurotoxin, Haemolysin and Choline Esterase Isolated from Cobra Venom on Heart, Blood Pressure and Respiration. J. Ind. chem. Soc. 30, 453–460 (1942).
Google Scholar
Sarkar, N. Okay. Isolation of cardiotoxin from cobra venom (Naja tripudians), monocellate selection).J. Ind. Chem. Soc 24, 227–232 (1947).
Google Scholar
Harvey, A. L. Cardiotoxins from cobra venoms: Possible mechanisms of motion. Toxin Rev. 4, 41–69 (1985).
Google Scholar
Dufton, M. J. & Hider, R. C. Structure and pharmacology of elapid cytotoxins. Pharm. Ther. 36, 1–40 (1988).
Google Scholar
Kazandjian, T. D. et al. Convergent evolution of pain-inducing defensive venom parts in spitting cobras. Sci. (80-.). 371, 386–390 (2021).
Google Scholar
Lomonte, B., Tarkowski, A. & Hanson, L. Å. Broad cytolytic specificity of myotoxin II, a lysine-49 phospholipase A2 of Bothrops asper snake venom. Toxicon 32, 1359–1369 (1994).
Google Scholar
Bultrón, E., Thelestam, M. & Gutiérrez, J. Effects on cultured mammalian cells of myotoxin III, a phospholipase A2 remoted from Bothrops asper (terciopelo) venom. Biochim. Biophys. Acta – Mol. Cell Res. 1179, 253–259 (1993).
Google Scholar
Queiroz, L. S., Santo Neto, H., Assakura, M. T., Reichl, A. P. & Mandelbaum, F. R. Pathological adjustments in muscle attributable to haemorrhagic and proteolytic components from Bothrops jararaca snake venom. Toxicon 23, 341–345 (1985).
Google Scholar
Ownby, C. L. Structure, perform and biophysical points of the myotoxins from snake venoms. J. Toxicol. – Toxin Rev. 17, 213–238 (1998).
Google Scholar
Rucavado, A., Lomonte, B., Ovadia, M. & Gutiérrez, J. M. Local tissue injury induced by BaP1, a metalloproteinase remoted from Bothrops asper (Terciopelo) snake venom. Exp. Mol. Pathol. 63, 186–199 (1995).
Google Scholar
Williams, H. F. et al. Mechanisms underpinning the everlasting muscle injury induced by snake venom metalloprotease. PLoS Negl. Trop. Dis. 13, 1–20 (2019).
Google Scholar
Alberts, B. et al. Essential cell biology: Fifth worldwide pupil version. (WW Norton & Company., 2018).
Brahma, R. Okay., Modahl, C. M. & Kini, R. M. Three-Finger Toxins. In Handbook of Venoms and Toxins of Reptiles (ed. Mackessy, S. P.) 177–194 (CRC Press, 2021).
Bilwes, A., Rees, B., Moras, D., Ménez, R. & Ménez, A. X-ray construction at 1.55 Å of toxin γ, a cardiotoxin from Naja nigricollis venom: Crystal packing reveals a mannequin for insertion into membranes. J. Mol. Biol. 239, 122–136 (1994).
Google Scholar
Dufton, M. J. & Hider, R. C. Conformational properties of the neurotoxins and cytotoxins remoted from Elapid snake venoms. CRC Crit. Rev. Biochem. 14, 113–171 (1983).
Google Scholar
Dauplais, M., Neumann, J. M., Pinkasfeld, S., Ménez, A. & Roumestand, C. An NMR Study of the Interaction of Cardiotoxin γ from Naja nigricollis with Perdeuterated Dodecylphosphocholine Micelles. Eur. J. Biochem. 230, 213–220 (1995).
Google Scholar
Forouhar, F. et al. Structural foundation of membrane-induced cardiotoxin A3 oligomerization. J. Biol. Chem. 278, 21980–21988 (2003).
Google Scholar
Feofanov, A. V. et al. Cancer cell harm by cytotoxins from cobra venom is mediated via lysosomal injury. Biochem. J. 390, 11–18 (2005).
Google Scholar
Hiu, J. J. & Yap, M. Okay. Okay. The fable of cobra venom cytotoxin: More than simply direct cytolytic actions. Toxicon X 14, 100123 (2022).
Google Scholar
Condrea, E., De Vries, A. & Mager, J. Hemolysis and splitting of human erythrocyte phospholipids by snake venoms. BBA – Spec. Sect. Lipids Relat. Subj. 84, 60–73 (1964).
Google Scholar
Klibansky, C., London, Y., Frenkel, A. & De Vries, A. Enhancing motion of artificial and pure basic polypeptides on erythrocyte-ghost phospholipid hydrolysis by phospholipase A. Biochim. Biophys. Acta – Biomembr. 150, 15–23 (1968).
Google Scholar
Louw, A. I. & Visser, L. The synergism of cardiotoxin and phospholipase A2 in hemolysis. BBA – Biomembr. 512, 163–171 (1978).
Google Scholar
Pucca, M. B. et al. Unity Makes Strength: Exploring Intraspecies and Interspecies Toxin Synergism between Phospholipases A2 and Cytotoxins. Front. Pharmacol. 11, 1–10 (2020).
Google Scholar
Bougis, P. E., Marchot, P. & Rochat, H. In vivo synergy of cardiotoxin and phospholipase A2 from the elapid snake Naja mossambica mossambica. Toxicon 25, 427–431 (1987).
Google Scholar
Kini, R. M. Excitement forward: Structure, perform and mechanism of snake venom phospholipase A2 enzymes. Toxicon 42, 827–840 (2003).
Google Scholar
Tasoulis, T. & Isbister, G. Okay. A present perspective on snake venom composition and constituent protein households. Arch. Toxicol. 97, 133–153 (2022).
Google Scholar
Lomonte, B. & Krizaj, I. Snake venom phospholipase A2 toxins. In Handbook of Venoms and Toxins of Reptiles (ed. Mackessy, S. P.) 389–411 (CRC Press, 2021).
Lynch, V. J. Inventing an arsenal: adaptive evolution and neofunctionalization of snake venom phospholipase A 2 genes. BMC Evol. Biol. 7, 2 (2007).
Kini, R. M. Structure – perform relationships and mechanism of anticoagulant phospholipase A 2 enzymes from snake venoms. Toxicon 45, 1147–1161 (2005).
Google Scholar
Lomonte, B. Lys49 myotoxins, secreted phospholipase A2-like proteins of viperid venoms: A complete overview. Toxicon 224, 107024 (2023).
Google Scholar
Fernández, J. et al. Muscle phospholipid hydrolysis by Bothrops asper Asp49 and Lys49 phospholipase A2 myotoxins – distinct mechanisms of motion. FEBS J. 280, 3878–3886 (2013).
Google Scholar
Fernandes, C. A. H., Borges, R. J., Lomonte, B. & Fontes, M. R. M. A structure-based proposal for a complete myotoxic mechanism of phospholipase A2-like proteins from viperid snake venoms. Biochim. Biophys. Acta – Proteins Proteom. 1844, 2265–2276 (2014).
Google Scholar
Fernandes, C. A. H. et al. Comparison between apo and complexed buildings of bothropstoxin-I reveals the position of Lys122 and Ca2+-binding loop area for the catalytically inactive Lys49-PLA2s. J. Struct. Biol. 171, 31–43 (2010).
Google Scholar
Mora-Obando, D., Fernández, J., Montecucco, C., Gutiérrez, J. M. & Lomonte, B. Synergism between basic Asp49 and Lys49 phospholipase A2 myotoxins of viperid snake venom in vitro and in vivo. PLoS One 9, e109846 (2014).
Google Scholar
Lomonte, B. et al. Comparative research of the cytolytic exercise of myotoxic phospholipases A2 on mouse endothelial (tEnd) and skeletal muscle (C2C12) cells in vitro. Toxicon 37, 145–158 (1999).
Google Scholar
Villalobos, J. C., Mora, R., Lomonte, B., Gutiérrez, J. M. & Angulo, Y. Cytotoxicity induced in myotubes by a Lys49 phospholipase A2 homologue from the venom of the snake Bothrops asper: Evidence of speedy plasma membrane injury and a twin position for extracellular calcium. Toxicol. Vitr. 21, 1382–1389 (2007).
Google Scholar
Cintra-Francischinelli, M. et al. Calcium imaging of muscle cells handled with snake myotoxins reveals toxin synergism and presence of acceptors. Cell. Mol. Life Sci. 66, 1718–1728 (2009).
Google Scholar
López-Dávila, A. J., Lomonte, B. & Gutiérrez, J. M. Alterations of the skeletal muscle contractile equipment in necrosis induced by myotoxic snake venom phospholipases A2: a mini-review. J. Muscle Res. Cell Motil. https://doi.org/10.1007/s10974-023-09662-4 (2023).
Mora, R., Valverde, B., Díaz, C., Lomonte, B. & Gutiérrez, J. M. A Lys49 phospholipase A2 homologue from Bothrops asper snake venom induces proliferation, apoptosis and necrosis in a lymphoblastoid cell line. Toxicon 45, 651–660 (2005).
Google Scholar
Mora, R., Maldonado, A., Valverde, B. & Gutiérrez, J. M. Calcium performs a key position within the results induced by a snake venom Lys49 phospholipase A 2 homologue on a lymphoblastoid cell line. Toxicon 47, 75–86 (2006).
Google Scholar
Mebs, D. & Ownby, C. L. Myotoxic parts of snake venoms: Their biochemical and organic actions. Pharmacol. Ther. 48, 223–236 (1990).
Google Scholar
Tasoulis, T. & Isbister, G. Okay. A overview and database of snake venom proteomes. Toxins (Basel). 9, 290 (2017).
Google Scholar
Hayashi, M. A. F. et al. Cytotoxic results of crotamine are mediated via lysosomal membrane permeabilization. Toxicon 52, 508–517 (2008).
Google Scholar
Kerkis, I., Silva, F. D. S., Pereira, A., Kerkis, A. & Rádis-Baptista, G. Biological versatility of crotamine a cationic peptide from the venom of a South American rattlesnake. Expert Opin. Investig. Drugs 19, 1515–1525 (2010).
Google Scholar
Chang, C. C. & Tseng, Okay. H. Effect of crotamine, a toxin of south american rattlesnake venom, on the sodium channel of murine skeletal muscle. Br. J. Pharmacol. 63, 551–559 (1978).
Google Scholar
Ownby, C. L., Cameron, D. & Tu, A. T. Isolation of myotoxic element from rattlesnake (Crotalus viridis viridis) venom. Electron microscopic evaluation of muscle injury. Am. J. Pathol. 85, 149 (1976).
Google Scholar
Joshi, R. et al. Evaluation of crotamine primarily based probes as intracellular focused distinction brokers for magnetic resonance imaging. Bioorg. Med. Chem. 69, 116863 (2022).
Google Scholar
Frantz, C., Stewart, Okay. M. & Weaver, V. M. The extracellular matrix at a look. J. Cell Sci. 123, 4195–4200 (2010).
Google Scholar
Jayadev, R. & Sherwood, D. R. Basement membranes. Curr. Biol. 27, R207–R211 (2017).
Google Scholar
Grönloh, M. L. B., Arts, J. J. G. & van Buul, J. D. Neutrophil transendothelial migration hotspots – Mechanisms and implications. J. Cell Sci. 134, jcs255653 (2021).
Google Scholar
Escalante, T., Rucavado, A., Fox, J. W. & Gutiérrez, J. M. Key occasions in microvascular injury induced by snake venom hemorrhagic metalloproteinases. J. Proteom. 74, 1781–1794 (2011).
Google Scholar
Gutiérrez, J. M., Escalante, T., Rucavado, A., Herrera, C. & Fox, J. W. A complete view of the structural and useful alterations of extracellular matrix by snake venom metalloproteinases (SVMPs): Novel views on the pathophysiology of envenoming. Toxins (Basel). 8, 304 (2016).
Google Scholar
Tasoulis, T., Pukala, T. L. & Isbister, G. Okay. Investigating Toxin Diversity and Abundance in Snake Venom Proteomes. Front. Pharmacol. 12, 768015 (2022).
Google Scholar
Fox, J. W. & Serrano, S. M. T. Structural concerns of the snake venom metalloproteinases, key members of the M12 reprolysin household of metalloproteinases. Toxicon 45, 969–985 (2005).
Google Scholar
Anai, Okay., Sugiki, M., Yoshida, E. & Maruyama, M. Neutralization of a snake venom hemorrhagic metalloproteinase prevents coagulopathy after subcutaneous injection of Bothrops jararaca venom in rats. Toxicon 40, 63–68 (2002).
Google Scholar
Herrera, C. et al. Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage. PLoS Negl. Trop. Dis. 9, 1–20 (2015).
Google Scholar
Baldo, C., Jamora, C., Yamanouye, N., Zorn, T. M. & Moura-da-Silva, A. M. Mechanisms of vascular injury by hemorrhagic snake venom metalloproteinases: Tissue distribution and in Situ hydrolysis. PLoS Negl. Trop. Dis. 4, e727 (2010).
Google Scholar
Gutiérrez, J. M. et al. Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase remoted from the venom of the snake Bothrops asper (terciopelo). Exp. Mol. Pathol. 62, 28–41 (1995).
Google Scholar
Boer-Lima, P. A., Rocha Gontijo, J. A. & Da Cruz-Höfling, M. A. Bothrops moojeni snake venom-induced renal glomeruli adjustments in rat. Am. J. Trop. Med. Hyg. 67, 217–222 (2002).
Google Scholar
Herrera, C., Escalante, T., Rucavado, A., Fox, J. W. & Gutiérrez, J. M. Metalloproteinases in illness: identification of biomarkers of tissue injury via proteomics. Expert Rev. Proteom. 15, 967–982 (2018).
Google Scholar
Junqueira-de-Azevedo, I. L. M., Campos, P. F., Ching, A. T. C. & Mackessy, S. P. Colubrid Venom Composition: An -Omics Perspective. Toxins (Basel). 8, 1–24 (2016).
Google Scholar
Kemparaju, Okay. & Girish, Okay. S. Snake venom hyaluronidase: A therapeutic goal. Cell Biochem. Funct. 24, 7–12 (2006).
Google Scholar
Girish, Okay. S. & Kemparaju, Okay. The magic glue hyaluronan and its eraser hyaluronidase: A organic overview. Life Sci. 80, 1921–1943 (2007).
Google Scholar
Tu, A. T. & Hendon, R. R. Characterization of lizard venom hyaluronidase and proof for its motion as a spreading issue. Comp. Biochem. Physiol. Part B Comp. Biochem. 76, 377–383 (1983).
Google Scholar
Girish, Okay., Kemparaju, Okay., Nagaraju, S. & Vishwanath, B. Hyaluronidase Inhibitors: A Biological and Therapeutic Perspective. Curr. Med. Chem. 16, 2261–2288 (2009).
Google Scholar
Yingprasertchai, S., Bunyasrisawat, S. & Ratanabanangkoon, Okay. Hyaluronidase inhibitors (sodium cromoglycate and sodium auro-thiomalate) scale back the native tissue injury and lengthen the survival time of mice injected with Naja kaouthia and Calloselasma rhodostoma venoms. Toxicon 42, 635–646 (2003).
Google Scholar
Sunitha, Okay. et al. Inflammation and oxidative stress in viper chunk: An perception inside and past. Toxicon 98, 89–97 (2015).
Google Scholar
Resiere, D., Mehdaoui, H. & Neviere, R. Inflammation and Oxidative Stress in Snakebite Envenomation: A Brief Descriptive Review and Clinical Implications. Toxins (Basel). 14, 802 (2022).
Google Scholar
Rucavado, A. et al. Viperid Envenomation Wound Exudate Contributes to Increased Vascular Permeability by way of a DAMPs/TLR-4 Mediated Pathway. Toxins 8, 349 (2016).
Google Scholar
Zuliani, J. P. Alarmins and inflammatory points associated to snakebite envenomation. Toxicon 226, 107088 (2023).
Google Scholar
Cintra-Francischinelli, M. et al. Bothrops snake myotoxins induce a big efflux of ATP and potassium with spreading of cell injury and ache. Proc. Natl Acad. Sci. USA 107, 14140–14145 (2010).
Google Scholar
Mora, J., Mora, R., Lomonte, B. & Gutiérrez, J. M. Effects of bothrops asper snake venom on lymphatic vessels: Insights right into a hidden facet of envenomation. PLoS Negl. Trop. Dis. 2, e318 (2008).
Google Scholar
Warrell, D. A., Greenwood, B. M., Davidson, N. M., Ormerod, L. D. & Prentice, C. R. Necrosis, haemorrhage and complement depletion following bites by the spitting cobra (Naja nigricollis). Q. J. Med. 45, 1–22 (1976).
Google Scholar
Warrell, D. A. & Ormerod, L. D. Snake Venom Ophthalmia and Blindness Caused by the Spitting Cobra (Naja Nigricollis) in Nigeria. Am. J. Trop. Med. Hyg. 25, 525–529 (1976).
Google Scholar
Gimenes, S. N. C. et al. Observation of bothrops atrox snake envenoming blister formation from 5 sufferers: Pathophysiological insights. Toxins (Basel). 13, 800 (2021).
Google Scholar
De Souza Queiróz, L., Marques, M. J. & Santo Neto, H. Acute native nerve lesions induced by Bothrops jararacussu snake venom. Toxicon 40, 1483–1486 (2002).
Google Scholar
Hernández, R. et al. Poor regenerative consequence after skeletal muscle necrosis induced by bothrops asper venom: Alterations in microvasculature and nerves. PLoS One 6, e19834 (2011).
Google Scholar
Gutiérrez, J. M. et al. Why is Skeletal Muscle Regeneration Impaired after Myonecrosis Induced by Viperid Snake Venoms? Toxins 10, 182 (2018).
Google Scholar
Azevedo-Marques, M. M. et al. Myonecrosis, myoglobinuria and acute renal failure induced by south american rattlesnake (Crotalus durissus terrificus) envenomation in brazil. Toxicon 23, 631–636 (1985).
Google Scholar
White, J. Clinical toxicology of snakebite in Australia and New Guinea. In Handbook of Clinical Toxicology of Animal Venoms and Poisons (eds. Meier, J. & White, J.) 595–617 (CRC Press, 1995).
Pinho, F. M. O., Zanetta, D. M. T. & Burdmann, E. A. Acute renal failure after Crotalus durissus snakebite: A potential survey on 100 sufferers. Kidney Int. 67, 659–667 (2005).
Google Scholar
Arce-Bejarano, R., Lomonte, B. & Gutiérrez, J. M. Intravascular hemolysis induced by the venom of the Eastern coral snake, Micrurus fulvius, in a mouse mannequin: Identification of instantly hemolytic phospholipases A2. Toxicon 90, 26–35 (2014).
Google Scholar
Xie, C. et al. Erythrocyte haemotoxicity profiling of snake venom toxins after nanofractionation. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 1176, 122586 (2021).
Google Scholar
Sitprija, V. & Sitprija, S. Renal results and harm induced by animal toxins. Toxicon 60, 943–953 (2012).
Google Scholar
de Paola, F. & Rossi, M. A. Myocardial injury induced by tropical rattlesnake (Crotalus durissus terrificus) venom in rats. Cardiovasc. Pathol. 2, 77–81 (1993).
Google Scholar
Hoffman, A., Levi, O., Orgad, U. & Nyska, A. Myocarditis following envenoming with Vipera palaestinae in two horses. Toxicon 31, 1623–1628 (1993).
Google Scholar
Tanjoni, I. et al. Jararhagin, a snake venom metalloproteinase, induces a specialised type of apoptosis (anoikis) selective to endothelial cells. Apoptosis 10, 851–861 (2005).
Google Scholar
Díaz, C., Valverde, L., Brenes, O., Rucavado, A. & Gutiérrez, J. M. Characterization of occasions related to apoptosis/anoikis induced by snake venom metalloproteinase BaP1 on human endothelial cells. J. Cell. Biochem. 94, 520–528 (2005).
Google Scholar
Grossmann, J. Molecular mechanisms of ‘detachment-induced apoptosis – Anoikis’. Apoptosis 7, 247–260 (2002).
Google Scholar
Paoli, P., Giannoni, E. & Chiarugi, P. Anoikis molecular pathways and its position in most cancers development. Biochim. Biophys. Acta – Mol. Cell Res. 1833, 3481–3498 (2013).
Google Scholar
Meredith, J. E., Fazeli, B. & Schwartz, M. A. The extracellular matrix as a cell survival issue. Mol. Biol. Cell 4, 953 (1993).
Google Scholar
Aoudjit, F. & Vuori, Okay. Matrix Attachment Regulates FAS-Induced Apoptosis in Endothelial CellsA Role for C-Flip and Implications for Anoikis. J. Cell Biol. 152, 633–644 (2001).
Google Scholar
Borkow, G., Gutiérrez, J. & Ovadia, M. In vitro exercise of BaH1, the primary hemorrhagic toxin of Bothrops asper snake venom on bovine endothelial cells. Toxicon 33, 1387–1391 (1995).
Google Scholar
Araki, S., Masuda, S., Maeda, H., Ying, M. J. & Hayashi, H. Involvement of particular integrins in apoptosis induced by vascular apoptosis-inducing protein 1. Toxicon 40, 535–542 (2002).
Google Scholar
Brenes, O., Muñóz, E., Roldán-Rodríguez, R. & Díaz, C. Cell loss of life induced by Bothrops asper snake venom metalloproteinase on endothelial and different cell strains. Exp. Mol. Pathol. 88, 424–432 (2010).
Google Scholar
Calvete, J. J. et al. Snake venom disintegrins: Evolution of construction and performance. Toxicon 45, 1063–1074 (2005).
Google Scholar
Cesar, P. H. S., Braga, M. A., Trento, M. V. C., Menaldo, D. L. & Marcussi, S. Snake Venom Disintegrins: An Overview of their Interaction with Integrins. Curr. Drug Targets 20, 465–477 (2018).
Google Scholar
Sartim, M. A. & Sampaio, S. V. Snake venom galactoside-binding lectins: A structural and useful overview. J. Venom. Anim. Toxins Incl. Trop. Dis. 21, 1–11 (2015).
Google Scholar
Nunes, E. S. et al. Cytotoxic impact and apoptosis induction by Bothrops leucurus venom lectin on tumor cell strains. Toxicon 59, 667–671 (2012).
Google Scholar
Pathan, J., Mondal, S., Sarkar, A. & Chakrabarty, D. Daboialectin, a C-type lectin from Russell’s viper venom induces cytoskeletal injury and apoptosis in human lung most cancers cells in vitro. Toxicon 127, 11–21 (2017).
Google Scholar
Zhang, C., Medzihradszky, Okay. F., Sánchez, E. E., Basbaum, A. I. & Julius, D. Lys49 myotoxin from the Brazilian lancehead pit viper elicits ache via regulated ATP launch. Proc. Natl Acad. Sci. Usa. 114, E2524–E2532 (2017).
Google Scholar
Bours, M. J. L., Swennen, E. L. R., Di Virgilio, F., Cronstein, B. N. & Dagnelie, P. C. Adenosine 5′-triphosphate and adenosine as endogenous signaling molecules in immunity and irritation. Pharmacol. Ther. 112, 358–404 (2006).
Google Scholar
Di Virgilio, F. Liaisons dangereuses: P2X7 and the inflammasome. Trends Pharmacol. Sci. 28, 465–472 (2007).
Google Scholar
Tonello, F. et al. A Lys49-PLA2 myotoxin of Bothrops asper triggers a speedy loss of life of macrophages that includes autocrine purinergic receptor signaling. Cell Death Dis. 3, e343–e343 (2012).
Google Scholar
Schieber, M. & Chandel, N. S. ROS perform in redox signaling and oxidative stress. Curr. Biol. 24, R453–R462 (2014).
Google Scholar
Fujii, J., Homma, T. & Osaki, T. Superoxide Radicals within the Execution of Cell Death. Antioxidants 11, 501 (2022).
Google Scholar
Du, X. Y. & Clemetson, Okay. J. Snake venom L-amino acid oxidases. Toxicon 40, 659–665 (2002).
Google Scholar
Guo, C., Liu, S., Yao, Y., Zhang, Q. & Sun, M. Z. Past decade research of snake venom l-amino acid oxidase. Toxicon 60, 302–311 (2012).
Google Scholar
Ande, S. R. et al. Mechanisms of cell loss of life induction by L-amino acid oxidase, a significant element of ophidian venom. Apoptosis 11, 1439–1451 (2006).
Google Scholar
Costal-Oliveira, F. et al. L-amino acid oxidase from Bothrops atrox snake venom triggers autophagy, apoptosis and necrosis in regular human keratinocytes. Sci. Rep. 9, 781 (2019).
Google Scholar
Naumann, G. B. et al. Cytotoxicity and inhibition of platelet aggregation attributable to an l-amino acid oxidase from Bothrops leucurus venom. Biochim. Biophys. Acta – Gen. Subj. 1810, 683–694 (2011).
Google Scholar
Torii, S., Naito, M. & Tsuruo, T. Apoxin I, a Novel Apoptosis-inducing Factor with L-Amino Acid Oxidase Activity Purified from Western Diamondback Rattlesnake Venom. J. Biol. Chem. 272, 9539–9542 (1997).
Google Scholar
Abidin, S. A. Z., Rajadurai, P., Chowdhury, E. H., Othman, I. & Naidu, R. Cytotoxic, Anti-Proliferative and Apoptosis Activity of l-Amino Acid Oxidase from Malaysian Cryptelytrops purpureomaculatus (CP-LAAO) Venom on Human Colon Cancer Cells. Mol 23, 1388 (2018).
Google Scholar
Morais, I. C. O. et al. L-Aminoacid Oxidase from Bothrops leucurus Venom Induces Nephrotoxicity by way of Apoptosis and Necrosis. PLoS One 10, e0132569 (2015).
Google Scholar
Tavares, C. et al. l-Amino acid oxidase remoted from Calloselasma rhodostoma snake venom induces cytotoxicity and apoptosis in JAK2V617F-positive cell strains. Rev. Bras. Hematol. Hemoter. 38, 128–134 (2016).
Google Scholar
Burin, S. M. et al. CR-LAAO antileukemic impact towards Bcr-Abl+ cells is mediated by apoptosis and hydrogen peroxide. Int. J. Biol. Macromol. 86, 309–320 (2016).
Google Scholar
Das, T. et al. Inhibition of leukemic U937 cell progress by induction of apoptosis, cell cycle arrest and suppression of VEGF, MMP-2 and MMP-9 actions by cytotoxin protein NN-32 purified from Indian spectacled cobra (Naja naja) venom. Toxicon 65, 1–4 (2013).
Google Scholar
Yang, S.-H., Chien, C.-M., Chang, L.-S. & Lin, S.-R. Cardiotoxin III-Induced Apoptosis Is Mediated by Ca 2+-Dependent Caspase-12 Activation in K562 Cells. J. Biochem Mol. Toxicol. 22, 209–218 (2008).
Google Scholar
Tsai, C. H. et al. Mechanisms of cardiotoxin III-induced apoptosis in human colorectal most cancers Colo205 cells. Clin. Exp. Pharmacol. Physiol. 33, 177–182 (2006).
Google Scholar
Chiou, J. T. et al. Naja atra Cardiotoxin 3 Elicits Autophagy and Apoptosis in U937 Human Leukemia Cells via the Ca2+/PP2A/AMPK Axis. Toxins 11, 527 (2019).
Google Scholar
Gutiérrez, J. M. et al. Tissue pathology induced by snake venoms: How to know a fancy sample of alterations from a techniques biology perspective? Toxicon 55, 166–170 (2010).
Google Scholar
Pucca, M. B. et al. History of Envenoming Therapy and Current Perspectives. Front. Immunol. 10, 1–13 (2019).
Google Scholar
León, G. et al. Current know-how for the economic manufacture of snake antivenoms. Toxicon 151, 63–73 (2018).
Google Scholar
Gutiérrez, J. M. et al. Neutralization of native tissue injury induced by Bothrops asper (terciopelo) snake venom. Toxicon 36, 1529–1538 (1998).
Google Scholar
Gutiérrez, J. M., León, G., Lomonte, B. & Angulo, Y. Antivenoms for snakebite envenomings. Inflamm. Allergy – Drug Targets 10, 369–380 (2011).
Google Scholar
Harrison, R. A. et al. Research methods to enhance snakebite therapy: Challenges and progress. J. Proteom. 74, 1768–1780 (2011).
Google Scholar
Williams, D. J. et al. Ending the drought: New methods for enhancing the circulate of inexpensive, efficient antivenoms in Asia and Africa. J. Proteom. 74, 1735–1767 (2011).
Google Scholar
Gutiérrez, J. M., Lomonte, B., Sanz, L., Calvete, J. J. & Pla, D. Immunological profile of antivenoms: Preclinical evaluation of the efficacy of a polyspecific antivenom via antivenomics and neutralization assays. J. Proteom. 105, 340–350 (2014).
Google Scholar
Ratanabanangkoon, Okay. A Quest for a Universal Plasma-Derived Antivenom Against All Elapid Neurotoxic Snake Venoms. Front. Immunol. 12, 668328 (2021).
Dennis, E. A., Cao, J., Hsu, Y. H., Magrioti, V. & Kokotos, G. Phospholipase A2 enzymes: Physical construction, organic perform, illness implication, chemical inhibition, and therapeutic intervention. Chem. Rev. 111, 6130–6185 (2011).
Google Scholar
Magrioti, V. & Kokotos, G. Phospholipase A2 inhibitors for the therapy of inflammatory ailments: a patent overview (2010–current). Expert Opin. Ther. Pat. 23, 333–344 (2013).
Google Scholar
Serruys, P. W. & Garcia-Garcia, H. M. Phospholipase A2 inhibitors. Curr. Opin. Lipidol. 20, 327–332 (2009).
Google Scholar
Lewin, M., Samuel, S., Merkel, J. & Bickler, P. Varespladib (LY315920) seems to be a potent, broad-spectrum, inhibitor of snake venom phospholipase A2 and a potential pre-referral therapy for envenomation. Toxins (Basel). 8, 248 (2016).
Google Scholar
Gutiérrez, J. M. et al. The seek for pure and artificial inhibitors that will complement antivenoms as therapeutics for snakebite envenoming. Toxins (Basel). 13, 1–30 (2021).
Google Scholar
Lewin, M. R. et al. Delayed oral LY333013 rescues mice from extremely neurotoxic, deadly doses of papuan taipan (Oxyuranus scutellatus) venom. Toxins (Basel). 10, 1–7 (2018).
Google Scholar
Bryan-Quirós, W., Fernández, J., Gutiérrez, J. M., Lewin, M. R. & Lomonte, B. Neutralizing properties of LY315920 towards snake venom group I and II myotoxic phospholipases A2. Toxicon 157, 1–7 (2019).
Google Scholar
Xiao, H. et al. Inactivation of Venom PLA2 Alleviates Myonecrosis and Facilitates Muscle Regeneration in Envenomed Mice: A Time Course Observation. Mol 23, 1911 (2018).
Google Scholar
Bittenbinder, M. A. et al. Coagulotoxic Cobras: Clinical Implications of Strong Anticoagulant Actions of African Spitting Naja Venoms That Are Not Neutralised by Antivenom however Are by LY315920 (Varespladib). Toxins (Basel). 10, 516 (2018).
Google Scholar
Hall, S. R. et al. Repurposed medicine and their mixtures stop morbidity-inducing dermonecrosis attributable to various cytotoxic snake venoms. Nat. Commun. 14, 7812. https://doi.org/10.1101/2022.05.20.492855 (2023).
Carter, R. W. et al. The BRAVO Clinical Study Protocol: Oral Varespladib for Inhibition of Secretory Phospholipase A2 within the Treatment of Snakebite Envenoming. Toxins (Basel). 15, 22 (2023).
Laustsen, A. et al. From Fangs to Pharmacology: The Future of Snakebite Envenoming Therapy. Curr. Pharm. Des. 22, 5270–5293 (2016).
Google Scholar
Jenkins, T. P. et al. Toxin neutralization utilizing different binding proteins. Toxins (Basel). 11, 1–28 (2019).
Google Scholar
Rucavado, A., Escalante, T. & Gutiérrez, J. M. Effect of the metalloproteinase inhibitor batimastat within the systemic toxicity induced by Bothrops asper snake venom: Understanding the position of metalloproteinases in envenomation. Toxicon 43, 417–424 (2004).
Google Scholar
Rucavado, A. et al. Inhibition of native hemorrhage and dermonecrosis induced by Bothrops asper snake venom: Effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA. Am. J. Trop. Med. Hyg. 63, 313–319 (2000).
Google Scholar
Arias, A. S., Rucavado, A. & Gutiérrez, J. M. Peptidomimetic hydroxamate metalloproteinase inhibitors abrogate native and systemic toxicity induced by Echis ocellatus (saw-scaled) snake venom. Toxicon 132, 40–49 (2017).
Google Scholar
Howes, J. M., Theakston, R. D. G. & Laing, G. D. Neutralization of the haemorrhagic actions of viperine snake venoms and venom metalloproteinases utilizing artificial peptide inhibitors and chelators. Toxicon 49, 734–739 (2007).
Google Scholar
Albulescu, L. O. et al. Preclinical validation of a repurposed metallic chelator as an early-intervention therapeutic for hemotoxic snakebite. Sci. Transl. Med. 12, eaay8314 (2020).
Google Scholar
Albulescu, L. O. et al. A therapeutic mixture of two small molecule toxin inhibitors offers broad preclinical efficacy towards viper snakebite. Nat. Commun. 11, 1–14 (2020).
Google Scholar
Sivaramakrishnan, V. et al. Viper venom hyaluronidase and its potential inhibitor evaluation: a multipronged computational investigation. J. Biomol. Struct. Dyn. 35, 1979–1989 (2017).
Google Scholar
Casewell, N. R., Jackson, T. N. W., Laustsen, A. H. & Sunagar, Okay. Causes and Consequences of Snake Venom Variation. Trends Pharmacol. Sci. 41, 570–581 (2020).
Google Scholar
Roncolato, E. C. et al. Human antibody fragments particular for Bothrops jararacussu venom scale back the toxicity of different Bothrops sp. venoms. J. Immunotoxicol. 10, 160–168 (2013).
Google Scholar
Laustsen, A. H. et al. Pros and cons of various therapeutic antibody codecs for recombinant antivenom improvement. Toxicon 146, 151–175 (2018).
Google Scholar
Lauridsen, L. H., Shamaileh, H. A., Edwards, S. L., Taran, E. & Veedu, R. N. Rapid One-Step Selection Method for Generating Nucleic Acid Aptamers: Development of a DNA Aptamer towards α-Bungarotoxin. PLoS One 7, e41702 (2012).
Google Scholar
Chen, Y. J., Tsai, C. Y., Hu, W. P. & Chang, L. S. DNA Aptamers towards Taiwan Banded Krait α-Bungarotoxin Recognize Taiwan Cobra Cardiotoxins. Toxins (Basel). 8, 66 (2016).
Google Scholar
Lynagh, T. et al. Peptide Inhibitors of the α-Cobratoxin-Nicotinic Acetylcholine Receptor Interaction. J. Med. Chem. 63, 13709–13718 (2020).
Google Scholar
O’Brien, J., Lee, S. H., Gutiérrez, J. M. & Shea, Okay. J. Engineered nanoparticles bind elapid snake venom toxins and inhibit venom-induced dermonecrosis. PLoS Negl. Trop. Dis. 12, 1–20 (2018).
Google Scholar
Albulescu, L. O. et al. A decoy-receptor method utilizing nicotinic acetylcholine receptor mimics reveals their potential as novel therapeutics towards neurotoxic snakebite. Front. Pharmacol. 10, 1–15 (2019).
Google Scholar
Otvos, R. A. et al. Analytical workflow for speedy screening and purification of bioactives from venom proteomes. Toxicon 76, 270–281 (2013).
Google Scholar
Palermo, G. et al. Acetylcholine-Binding Protein Affinity Profiling of Neurotoxins in Snake Venoms with Parallel Toxin Identification. Int. J. Mol. Sci. 24, 16769 (2023).
Google Scholar
Nakamoto, M., Escalante, T., Gutiérrez, J. M. & Shea, Okay. J. A Biomimetic of Endogenous Tissue Inhibitors of Metalloproteinases: Inhibition Mechanism and Contribution of Composition, Polymer Size, and Shape to the Inhibitory Effect. Nano Lett. 21, 5663–5670 (2021).
Google Scholar
Puzari, U., Fernandes, P. A. & Mukherjee, A. Okay. Pharmacological re-assessment of conventional medicinal plants-derived inhibitors as antidotes towards snakebite envenoming: A essential overview. J. Ethnopharmacol. 292, 115208. https://doi.org/10.1016/j.jep.2022.115208 (2022).
Lizano, S., Domont, G. & Perales, J. Natural phospholipase A2 myotoxin inhibitor proteins from snakes, mammals and crops. Toxicon 42, 963–977 (2003).
Google Scholar
Bastos, V. A., Gomes-Neto, F., Perales, J., Neves-Ferreira, A. G. C. & Valente, R. H. Natural inhibitors of snake venom metalloendopeptidases: History and present challenges. Toxins (Basel). 8, 250 (2016).
Google Scholar
van Thiel, J. et al. Convergent evolution of toxin resistance in animals. Biol. Rev. 97, 1823–1843 (2022).
Google Scholar
Campos, P. C., de Melo, L. A., Dias, G. L. F. & Fortes-Dias, C. L. Endogenous phospholipase A2 inhibitors in snakes: A short overview. J. Venom. Anim. Toxins Incl. Trop. Dis. 22, 1–7 (2016).
Google Scholar
Fortes-Dias, C. L. Endogenous inhibitors of snake venom phospholipases A2 within the blood plasma of snakes. Toxicon 40, 481–484 (2002). at.
Google Scholar
Neves-Ferreira, A. G. C., Valente, R. H., Perales, J. & Domont, G. B. Natural inhibitors – Innate immunity to snake venoms. In Handbook of Venoms and Toxins of Reptiles (ed. Mackessy, S. P.) 259–284 (2010).
Mors, W. B., Célia Do Nascimento, M., Ruppelt Pereira, B. M. & Alvares Pereira, N. Plant pure merchandise energetic towards snake chunk — the molecular method. Phytochemistry 55, 627–642 (2000).
Google Scholar
Soares, A. M. et al. Medicinal Plants with Inhibitory Properties Against Snake Venoms. Curr. Med. Chem. 12, 2625–2641 (2005).
Google Scholar
Carvalho, B. M. A. et al. Snake Venom PLA 2 s Inhibitors Isolated from Brazilian Plants: Synthetic and Natural Molecules. Biomed. Res. Int. 2013, 153045 (2013).
Google Scholar
Félix-Silva, J., Silva-Junior, A. A., Zucolotto, S. M. & Fernandes-Pedrosa, M. D. F. Medicinal Plants for the Treatment of Local Tissue Damage Induced by Snake Venoms: An Overview from Traditional Use to Pharmacological Evidence. Evidence-based Complement. Altern. Med. 2017, 5748256 (2017).
Zdenek, C. N. et al. A Taxon-Specific and High-Throughput Method for Measuring Ligand Binding to Nicotinic Acetylcholine Receptors. Toxins (Basel). 11, 600 (2019).
Google Scholar
Harris, R. J. et al. Assessing the binding of venoms from aquatic elapids to the nicotinic acetylcholine receptor orthosteric website of various prey fashions. Int. J. Mol. Sci. 21, 1–13 (2020).
Google Scholar
O’Brien, J., Lee, S. H., Onogi, S. & Shea, Okay. J. Engineering the Protein Corona of a Synthetic Polymer Nanoparticle for Broad-Spectrum Sequestration and Neutralization of Venomous Biomacromolecules. J. Am. Chem. Soc. 138, 16604–16607 (2016).
Google Scholar
De Oliveira, M. et al. Antagonism of myotoxic and paralyzing actions of bothropstoxin-I by suramin. Toxicon 42, 373–379 (2003).
Google Scholar
Murakami, M. T. et al. Inhibition of Myotoxic Activity of Bothrops asper Myotoxin II by the Anti-trypanosomal Drug Suramin. J. Mol. Biol. 350, 416–426 (2005).
Google Scholar
Salvador, G. H. M. et al. Structural and useful characterization of suramin-bound MjTX-I from Bothrops moojeni suggests a specific myotoxic mechanism. Sci. Rep. 8, 1–15 (2018).
Google Scholar
Lomonte, B., Moreno, E., Tarkowski, A., Hanson, L. A. & Maccarana, M. Neutralizing interplay between heparins and myotoxin II, a lysine 49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding and cytolytic toxin area by means of artificial peptides and molecular modeling. J. Biol. Chem. 269, 29867–29873 (1994).
Google Scholar
Diccianni, M. B., Mistry, M. J., Hug, Okay. & Harmony, J. A. Okay. Inhibition of phospholipase A2 by heparin. Biochim. Biophys. Acta (BBA)/Lipids Lipid Metab. 1046, 242–248 (1990).
Google Scholar
Rocha, S. L. G. et al. Functional evaluation of DM64, an antimyotoxic protein with immunoglobulin-like construction from Didelphis marsupialis serum. Eur. J. Biochem. 269, 6052–6062 (2002).
Google Scholar
Fernandes, C. A. H. et al. Structural Basis for the Inhibition of a Phospholipase A2-Like Toxin by Caffeic and Aristolochic Acids. PLoS One 10, e0133370 (2015).
Google Scholar
dos Santos, J. I. et al. Structural and Functional Studies of a Bothropic Myotoxin Complexed to Rosmarinic Acid: New Insights into Lys49-PLA2 Inhibition. PLoS One 6, e28521 (2011).
Google Scholar
Ticli, F. Okay. et al. Rosmarinic acid, a brand new snake venom phospholipase A2 inhibitor from Cordia verbenacea (Boraginaceae): antiserum motion potentiation and molecular interplay. Toxicon 46, 318–327 (2005).
Google Scholar
Aung, H. T. et al. Biological and Pathological Studies of Rosmarinic Acid as an Inhibitor of Hemorrhagic Trimeresurus flavoviridis (habu) Venom. Toxins 2, 2478–2489 (2010).
Google Scholar
Chandra, V. et al. Structural Basis of Phospholipase A2 Inhibition for the Synthesis of Prostaglandins by the Plant Alkaloid Aristolochic Acid from a 1.7 Å Crystal Structure†,‡. Biochemistry 41, 10914–10919 (2002).
Google Scholar
Nakamoto, M., Zhao, D., Benice, O. R., Lee, S. H. & Shea, Okay. J. Abiotic Mimic of Endogenous Tissue Inhibitors of Metalloproteinases: Engineering Synthetic Polymer Nanoparticles for Use as a Broad-Spectrum Metalloproteinase. Inhibitor. J. Am. Chem. Soc. 142, 2338–2345 (2020).
Google Scholar
Valente, R. H., Dragulev, B., Perales, J., Fox, J. W. & Domont, G. B. BJ46a, a snake venom metalloproteinase inhibitor isolation, characterization, cloning and insights into its mechanism of motion. Eur. J. Biochem. 268, 3042–3052 (2001).
Google Scholar
Omori-Satoh, T., Sadahiro, S., Ohsaka, A. & Murata, R. Purification and characterization of an antihemorrhagic issue within the serum of Trimeresurus flavoviridis, a crotalid. Biochim. Biophys. Acta – Protein Struct. 285, 414–426 (1972).
Google Scholar
Srinivasa, V. et al. Novel Apigenin Based Small Molecule that Targets Snake Venom Metalloproteases. PLoS One 9, e106364 (2014).
Google Scholar
Preciado, L. M., Comer, J., Núñez, V., Rey-Súarez, P. & Pereañez, J. A. Inhibition of a Snake Venom Metalloproteinase by the Flavonoid Myricetin. Mol 23, 2662 (2018).
Google Scholar
Bala, E., Hazarika, R., Singh, P., Yasir, M. & Shrivastava, R. A organic overview of Hyaluronidase: A venom enzyme and its inhibition with crops supplies. Mater. Today Proc. 5, 6406–6412 (2018).
Google Scholar
Mio, Okay. & Stern, R. Inhibitors of the hyaluronidases. Matrix Biol. 21, 31–37 (2002).
Google Scholar