{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T01:20:01Z","timestamp":1790817601904,"version":"4.1.0"},"reference-count":108,"publisher":"MDPI AG","issue":"7","license":[{"start":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T00:00:00Z","timestamp":1689724800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxins"],"abstract":"<jats:p>Humans have faced poisonous animals since the most ancient times. It is recognized that certain animals, like specific plants, produce toxic substances that can be lethal, but that can also have therapeutic or psychoactive effects. The use of the term \u201cvenom\u201d, which initially designated a poison, remedy, or magic drug, is now confined to animal poisons delivered by biting. Following Louis Pasteur\u2019s work on pathogenic microorganisms, it was hypothesized that venoms could be related to bacterial toxins and that the process of pathogenicity attenuation could be applied to venoms for the prevention and treatment of envenomation. Cesaire Phisalix and Gabriel Bertrand from the National Museum of Natural History as well as Albert Calmette from the Institut Pasteur in Paris were pioneers in the development of antivenomous serotherapy. Gaston Ramon refined the process of venom attenuation for the immunization of horses using a formalin treatment method that was successful for diphtheria and tetanus toxins. This paved the way for the production of antivenomous sera at the Institut Pasteur, as well as for research on venom constituents and the characterization of their biological activities. The specific activities of certain venom components, such as those involved in blood coagulation or the regulation of chloride ion channels, raises the possibility of developing novel therapeutic drugs that could serve as anticoagulants or as a treatment for cystic fibrosis, for example. Scientists of the Institut Pasteur of Paris have significantly contributed to the study of snake venoms, a topic that is reported in this review.<\/jats:p>","DOI":"10.3390\/toxins15070462","type":"journal-article","created":{"date-parts":[[2023,7,19]],"date-time":"2023-07-19T21:21:46Z","timestamp":1689801706000},"page":"462","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["Animal Toxins: A Historical Outlook at the Institut Pasteur of Paris"],"prefix":"10.3390","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-9305-8989","authenticated-orcid":false,"given":"Michel R.","family":"Popoff","sequence":"first","affiliation":[{"name":"Unit\u00e9 des Toxines Bact\u00e9riennes, Institut Pasteur, Universit\u00e9 Paris Cit\u00e9, CNRS UMR 2001 INSERM U1306, F-75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Grazyna","family":"Faure","sequence":"additional","affiliation":[{"name":"Unit\u00e9 R\u00e9cepteurs-Canaux, Institut Pasteur, Universit\u00e9 Paris Cit\u00e9, CNRS UMR 3571, F-75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandra","family":"Legout","sequence":"additional","affiliation":[{"name":"Centre de Ressources et Information Scientifique, Institut Pasteur, Universit\u00e9 Paris Cit\u00e9, F-75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1955-548X","authenticated-orcid":false,"given":"Daniel","family":"Ladant","sequence":"additional","affiliation":[{"name":"Unit\u00e9 de Biochimie des Interactions Macromol\u00e9culaires, Institut Pasteur, Universit\u00e9 Paris Cit\u00e9, CNRS UMR 3528, F-75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,7,19]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"558","DOI":"10.2174\/1871530320666200904105816","article-title":"Venoms and Poisonings during the Centuries: A Narrative Review","volume":"22","author":"Charitos","year":"2022","journal-title":"Endocr. Metab. Immune Disord. Drug Targets"},{"key":"ref_2","first-page":"88","article-title":"Poisons, poisoning and the drug trade in ancient Rome","volume":"45","author":"Cilliers","year":"2000","journal-title":"Akroterion"},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Cavaillon, J.M. (2022). From bacterial poisons to toxins: The early works of Pasteurians. Toxins, 14.","DOI":"10.3390\/toxins14110759"},{"key":"ref_4","first-page":"32","article-title":"La d\u00e9couverte du s\u00e9rum antivenimeux (10 f\u00e9vrier 1894)","volume":"292","author":"Goyffon","year":"2008","journal-title":"Biofutur"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/s40409-016-0074-7","article-title":"Paths to the discovery of antivenom serotherapy in France","volume":"22","author":"Bochner","year":"2016","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"399","DOI":"10.1136\/bmj.2.1859.399","article-title":"The Treatment of Animals Poisoned with Snake Venom by the Injection of Antivenomous Serum","volume":"2","author":"Calmette","year":"1896","journal-title":"Br. Med. J."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"1241","DOI":"10.1016\/S0041-0101(99)00086-0","article-title":"Doctor Albert Calmette 1863\u20131933: Founder of antivenomous serotherapy and of antituberculous BCG vaccination","volume":"37","author":"Hawgood","year":"1999","journal-title":"Toxicon"},{"key":"ref_8","first-page":"10","article-title":"La d\u00e9couverte de la s\u00e9roth\u00e9rapie antivenimeuse en 1894: Physalix et Bertrand ou Calmette?","volume":"106","author":"Brygoo","year":"1985","journal-title":"Bull. Ass. Anc. El\u00e8ves Inst. Pasteur"},{"key":"ref_9","first-page":"275","article-title":"Contribution \u00e0 l\u2019\u00e9tude du venin des serpents. Immunisation des animaux et traitement de l\u2019envenimation","volume":"8","author":"Calmette","year":"1894","journal-title":"Ann. Inst. Pasteur"},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Popoff, M.R., and Legout, S. (2023). Anaerobes and Toxins, a Tradition of the Institut Pasteur. Toxins, 15.","DOI":"10.3390\/toxins15010043"},{"key":"ref_11","first-page":"53","article-title":"Gaston Ramon (1886\u20131963). Le soixanti\u00e8me anniversaire des anatoxines","volume":"18","author":"Gilbrin","year":"1984","journal-title":"Hist. Des Sci. M\u00e9dicales"},{"key":"ref_12","first-page":"353","article-title":"Sur la production acc\u00e9l\u00e9r\u00e9e des s\u00e9rums antivenimeux de diff\u00e9rentes sortes au moyen des anavenins sp\u00e9cifiques et des substances stimulantes de l\u2019immunit\u00e9","volume":"6","author":"Ramon","year":"1941","journal-title":"Rev. Immunol."},{"key":"ref_13","first-page":"1","article-title":"Proc\u00e9d\u00e9 pour accro\u00eftre la production des antitoxines","volume":"40","author":"Ramon","year":"1926","journal-title":"Ann. Inst. Pasteur"},{"key":"ref_14","first-page":"522","article-title":"Biochemical and immunological studies on snake venom. 3. Study of analogues of the Naja nigricollis venom alpha antigen","volume":"116","author":"Boquet","year":"1969","journal-title":"Ann. Inst. Pasteur"},{"key":"ref_15","first-page":"1363","article-title":"Studies on the spreading factor of snake venoms","volume":"152","author":"Boquet","year":"1958","journal-title":"C. R. Seances Soc. Biol. Fil."},{"key":"ref_16","first-page":"293","article-title":"Comparison of the principal pharmacologic properties of different venoms of Echis carinatus (Viperides)","volume":"205","author":"Cheymol","year":"1973","journal-title":"Arch. Int. Pharmacodyn. Ther."},{"key":"ref_17","first-page":"1107","article-title":"Separation of the constituents of Naja naja venin by electrophoresis","volume":"246","author":"Detrait","year":"1958","journal-title":"C. R. Hebd. Seances Acad. Sci."},{"key":"ref_18","first-page":"1163","article-title":"Antigenic relations between a lethal factor in the venom of Echis carinata and neurotoxins in the venoms of Na ja na ja and Na ja nigricollis","volume":"154","author":"Detrait","year":"1960","journal-title":"C. R. Seances Soc. Biol. Fil."},{"key":"ref_19","first-page":"1785","article-title":"Curarizing action of alpha toxin of Naja nigricollis","volume":"263","author":"Pierre","year":"1966","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1016\/0041-0101(73)90030-5","article-title":"An attempt to classify the toxic proteins of Elapidae and Hydrophiidae venoms","volume":"11","author":"Boquet","year":"1973","journal-title":"Toxicon"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/0041-0101(66)90075-4","article-title":"Snake venoms. 2. The chemical constitution of snake venoms and immunity against venoms","volume":"3","author":"Boquet","year":"1966","journal-title":"Toxicon"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/0041-0101(64)90028-5","article-title":"Snake Venoms. I. Physiopathology of Envenomation and Biological Properties of Venoms","volume":"15","author":"Boquet","year":"1964","journal-title":"Toxicon"},{"key":"ref_23","first-page":"2439","article-title":"The antigenicity of toxic proteins from the venoms of Elapidae and Hydrophiidae","volume":"284","author":"Boquet","year":"1977","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_24","first-page":"719","article-title":"Biochemical and immunological research on snale venom. I. Trial separations of the antigens of Naja nigricollis venom by Sephadex filtration","volume":"111","author":"Boquet","year":"1966","journal-title":"Ann. Inst. Pasteur"},{"key":"ref_25","first-page":"1456","article-title":"Attempt at classification of toxic proteins extracted from snake venoms","volume":"271","author":"Boquet","year":"1970","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_26","first-page":"307","article-title":"An attempt to classify by serological techniques the toxic proteins of low molecular weight extracted from Elapidae and Hydrophiidae venoms","volume":"71","author":"Boquet","year":"1972","journal-title":"Taiwan Yi Xue Hui Za Zhi"},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1021\/bi00757a014","article-title":"Some physical properties of the cholinergic receptor protein from Electrophorus electricus revealed by a tritiated alpha-toxin from Naja nigricollis venom","volume":"11","author":"Meunier","year":"1972","journal-title":"Biochemistry"},{"key":"ref_28","first-page":"240","article-title":"Pharmacologic properties of toxins from scorpion venom (Androctonus australis)","volume":"267","year":"1968","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_29","first-page":"379","article-title":"Calcium cycle at the neuromuscular junction","volume":"268","author":"Czajka","year":"1969","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_30","first-page":"2511","article-title":"Pharmacologic action of pure Naja nigricollis venom fractions and calcium liberation in striated muscles","volume":"268","author":"Czajka","year":"1969","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_31","first-page":"1655","article-title":"Tetrodotoxin, calcium and scorpion venom","volume":"271","year":"1970","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_32","first-page":"3021","article-title":"Scorpion venom, calcium and acetylcholine emission by nerve fibers in the ileum of guinea pigs","volume":"275","year":"1972","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_33","first-page":"2703","article-title":"Desensitization of the guinea pig ileum to scorpion venom by various concentrations of ions in the external medium","volume":"278","author":"Goudou","year":"1974","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_34","first-page":"699","article-title":"Pharmacologic properties of the toxins isolated from the sea anemone (Anemonia sulcata)","volume":"283","author":"Choucavy","year":"1976","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_35","first-page":"1335","article-title":"Effect of scorpion venom (Androctonus australis) on neuromuscular transmission inhibited by botulinum toxin in the frog","volume":"285","year":"1977","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1016\/0041-0101(86)90076-0","article-title":"Enhancement by Anemonia sulcata toxin II of spontaneous quantal transmitter release from mammalian motor nerve terminals","volume":"24","author":"Lemeignan","year":"1986","journal-title":"Toxicon"},{"key":"ref_37","first-page":"873","article-title":"Effects of a neurotoxin isolated from the sea anemone, Anemonia sulcata, at frog neuromuscular junction (author\u2019s transl)","volume":"75","author":"Bourneau","year":"1979","journal-title":"J. Physiol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1016\/0022-2828(75)90141-8","article-title":"Effect of toxin II isolated from scorpion venom on action potential and contraction of mammalian heart","volume":"7","author":"Coraboeuf","year":"1975","journal-title":"J. Mol. Cell. Cardiol."},{"key":"ref_39","first-page":"1181","article-title":"Cardiotoxicity in rats of purified gamma toxin isolated from venom of Naja nigricollis and of toxins extracted from scorpion venom","volume":"280","year":"1975","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_40","first-page":"137","article-title":"Action of calcium chloride in the cardiotoxicity in the rat of purified gamma toxin isolated from Naja nigricollis venom","volume":"280","author":"Trethevie","year":"1975","journal-title":"C. R. Acad. Hebd. Seances Acad. Sci. D"},{"key":"ref_41","first-page":"785","article-title":"Delezenne","volume":"8","author":"Hallion","year":"1932","journal-title":"Annls Physiol. PhysicoChimie Biol."},{"key":"ref_42","first-page":"114","article-title":"Relation entre les valeurs antig\u00e9niques des venims blancs et jaunes de Vipera aspis","volume":"131","author":"Lamy","year":"1947","journal-title":"Bull. Acad. Med."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1016\/j.toxicon.2008.06.008","article-title":"Obituary: Cassian Bon\u2014A scientist fascinated by toxins and their therapeutic potential","volume":"52","author":"Goyffon","year":"2008","journal-title":"Toxicon"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"1560","DOI":"10.1073\/pnas.68.7.1560","article-title":"Biological roles of the two components of crotoxin","volume":"68","author":"Hendon","year":"1971","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1111\/j.1432-1033.1979.tb13278.x","article-title":"Postsynaptic effects of crotoxin and of its isolated subunits","volume":"99","author":"Bon","year":"1979","journal-title":"Eur. J. Biochem."},{"key":"ref_46","first-page":"439","article-title":"Crotoxin, half-century of investigations on a phospholipase A2 neurotoxin","volume":"39","author":"Bon","year":"1989","journal-title":"Acta Physiol. Pharmacol. Latinoam."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1111\/j.1471-4159.1992.tb09312.x","article-title":"Differential effects of presynaptic phospholipase A2 neurotoxins on Torpedo synaptosomes","volume":"58","author":"Bon","year":"1992","journal-title":"J. Neurochem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"10708","DOI":"10.1021\/bi00091a022","article-title":"Model for the interaction of crotoxin, a phospholipase A2 neurotoxin, with presynaptic membranes","volume":"32","author":"Bon","year":"1993","journal-title":"Biochemistry"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0303-7207(91)90007-F","article-title":"Crotoxin, a phospholipase A2 neurotoxin from snake venom, interacts with epithelial mammary cells, is internalized and induces secretion","volume":"82","author":"Radvanyi","year":"1991","journal-title":"Mol. Cell. Endocrinol."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"12616","DOI":"10.1016\/S0021-9258(18)33556-7","article-title":"Catalytic activity and reactivity with p-bromophenacyl bromide of the phospholipase subunit of crotoxin. Influence of dimerization and association with the noncatalytic subunit","volume":"257","author":"Radvanyi","year":"1982","journal-title":"J. Biol. Chem."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0041-0101(87)90246-7","article-title":"Several isoforms of crotoxin are present in individual venoms from the South American rattlesnake Crotalus durissus terrificus","volume":"25","author":"Faure","year":"1987","journal-title":"Toxicon"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1021\/bi00402a036","article-title":"Crotoxin, a phospholipase A2 neurotoxin from the South American rattlesnake Crotalus durissus terrificus: Purification of several isoforms and comparison of their molecular structure and of their biological activities","volume":"27","author":"Faure","year":"1988","journal-title":"Biochemistry"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1111\/j.1432-1033.1993.tb17946.x","article-title":"Comparison of crotoxin isoforms reveals that stability of the complex plays a major role in its pharmacological action","volume":"214","author":"Faure","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/0167-4781(91)90132-6","article-title":"Analysis of cDNAs encoding the two subunits of crotoxin, a phospholipase A2 neurotoxin from rattlesnake venom: The acidic non enzymatic subunit derives from a phospholipase A2-like precursor","volume":"1088","author":"Bouchier","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1111\/j.1432-1033.1994.tb18978.x","article-title":"The origin of the diversity of crotoxin isoforms in the venom of Crotalus durissus terrificus","volume":"223","author":"Faure","year":"1994","journal-title":"Eur. J. Biochem."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"8074","DOI":"10.1021\/bi00246a028","article-title":"Multiplicity of acidic subunit isoforms of crotoxin, the phospholipase A2 neurotoxin from Crotalus durissus terrificus venom, results from posttranslational modifications","volume":"30","author":"Faure","year":"1991","journal-title":"Biochemistry"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/0041-0101(96)00064-5","article-title":"Re-examination of crotoxin-membrane interactions","volume":"34","author":"Krizaj","year":"1996","journal-title":"Toxicon"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"2779","DOI":"10.1021\/bi9612374","article-title":"Neurotoxic phospholipases A2 ammodytoxin and crotoxin bind to distinct high-affinity protein acceptors in Torpedo marmorata electric organ","volume":"36","author":"Krizaj","year":"1997","journal-title":"Biochemistry"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/S0041-0101(02)00394-X","article-title":"Crotoxin acceptor protein isolated from Torpedo electric organ: Binding properties to crotoxin by surface plasmon resonance","volume":"41","author":"Faure","year":"2003","journal-title":"Toxicon"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"833","DOI":"10.1016\/S0300-9084(00)01175-5","article-title":"Natural inhibitors of toxic phospholipases A(2)","volume":"82","author":"Faure","year":"2000","journal-title":"Biochimie"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1046\/j.1432-1327.2000.01532.x","article-title":"Interaction of the neurotoxic and nontoxic secretory phospholipases A2 with the crotoxin inhibitor from Crotalus serum","volume":"267","author":"Faure","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1111\/j.1432-1033.1995.tb20355.x","article-title":"Molecular structure and mechanism of action of the crotoxin inhibitor from Crotalus durissus terrificus serum","volume":"227","author":"Perales","year":"1995","journal-title":"Eur. J. Biochem."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"142","DOI":"10.1111\/j.1749-6632.1994.tb26621.x","article-title":"Different evolution of phospholipase A2 neurotoxins (beta-neurotoxins) from Elapidae and Viperidae snakes","volume":"710","author":"Bon","year":"1994","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1007\/978-1-4613-0361-9_12","article-title":"Structure and function relationship of crotoxin, a heterodimeric neurotoxic phospholipase A2 from the venom of a South-American rattlesnake","volume":"391","author":"Choumet","year":"1996","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1016\/0161-5890(92)90125-H","article-title":"Immunochemical analysis of a snake venom phospholipase A2 neurotoxin, crotoxin, with monoclonal antibodies","volume":"29","author":"Choumet","year":"1992","journal-title":"Mol. Immunol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/0014-5793(89)81185-8","article-title":"Neutralization of lethal potency and inhibition of enzymatic activity of a phospholipase A2 neurotoxin, crotoxin, by non-precipitating antibodies (Fab)","volume":"244","author":"Choumet","year":"1989","journal-title":"FEBS Lett."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1515\/BC.1999.071","article-title":"Molecular mimicry between a monoclonal antibody and one subunit of crotoxin, a heterodimeric phospholipase A2 neurotoxin","volume":"380","author":"Choumet","year":"1999","journal-title":"Biol. Chem."},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1515\/bchm.1998.379.7.899","article-title":"A monoclonal antibody directed against the non-toxic subunit of a dimeric phospholipase A2 neurotoxin, crotoxin, neutralizes its toxicity","volume":"379","author":"Choumet","year":"1998","journal-title":"Biol. Chem."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1111\/j.1432-1033.1993.tb19869.x","article-title":"Snake-venom phospholipase A2 neurotoxins. Potentiation of a single-chain neurotoxin by the chaperon subunit of a two-component neurotoxin","volume":"211","author":"Choumet","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.jmb.2011.07.027","article-title":"Crystal structure of crotoxin reveals key residues involved in the stability and toxicity of this potent heterodimeric \u03b2-neurotoxin","volume":"412","author":"Faure","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"10609","DOI":"10.1021\/bi034790b","article-title":"Molecular cloning and expression of a functional snake venom serine proteinase, with platelet aggregating activity, from the Cerastes cerastes viper","volume":"42","author":"Dekhil","year":"2003","journal-title":"Biochemistry"},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1080\/09537109876708","article-title":"Convulxin-induced platelet adhesion and aggregation: Involvement of glycoproteins VI and IaIIa","volume":"9","author":"Lagrue","year":"1998","journal-title":"Platelets"},{"key":"ref_73","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.toxicon.2004.10.007","article-title":"Pharmacokinetic studies of scorpion venom before and after antivenom immunotherapy","volume":"45","author":"Krifi","year":"2005","journal-title":"Toxicon"},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/S0969-2126(98)00119-1","article-title":"The crystal structure of the novel snake venom plasminogen activator TSV-PA: A prototype structure for snake venom serine proteinases","volume":"6","author":"Parry","year":"1998","journal-title":"Structure"},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/j.taap.2006.11.003","article-title":"Toxicokinetic and toxicodynamic analyses of Androctonus australis hector venom in rats: Optimization of antivenom therapy","volume":"218","author":"Lefort","year":"2007","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"ref_76","first-page":"1512","article-title":"Pharmacokinetics of Vipera aspis venom after experimental envenomation in rabbits","volume":"268","author":"Audebert","year":"1994","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/978-1-4613-0361-9_42","article-title":"New approaches in antivenom therapy","volume":"391","author":"Choumet","year":"1996","journal-title":"Adv. Exp. Med. Biol."},{"key":"ref_78","first-page":"1","article-title":"Effect of antivenom on venom pharmacokinetics in experimentally envenomed rabbits: Toward an optimization of antivenom therapy","volume":"281","author":"Choumet","year":"1997","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_79","first-page":"490","article-title":"Absorption and elimination of viper venom after antivenom administration","volume":"285","author":"Choumet","year":"1998","journal-title":"J. Pharmacol. Exp. Ther."},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1016\/S0041-0101(98)00216-5","article-title":"Pharmacokinetics of the toxic fraction of Centruroides limpidus limpidus venom in experimentally envenomed rabbits and effects of immunotherapy with specific F(ab\u2019)2","volume":"37","author":"Choumet","year":"1999","journal-title":"Toxicon"},{"key":"ref_81","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/j.toxicon.2004.11.010","article-title":"Purification and characterization of a hemorrhagic metalloproteinase from Bothrops lanceolatus (Fer-de-lance) snake venom","volume":"45","author":"Stroka","year":"2005","journal-title":"Toxicon"},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/S0041-0101(00)00139-2","article-title":"Coagulant and anticoagulant activities of Bothrops lanceolatus (Fer de lance) venom","volume":"39","author":"Kamiguti","year":"2001","journal-title":"Toxicon"},{"key":"ref_83","first-page":"133","article-title":"Snake venom proteinases as tools in hemostasis studies: Structure-function relationship of a plasminogen activator purified from Trimeresurus stejnegeri venom","volume":"31","author":"Wisner","year":"2001","journal-title":"Haemostasis"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"851","DOI":"10.1016\/S0300-9084(00)01178-0","article-title":"Snake venom proteins acting on hemostasis","volume":"82","author":"Braud","year":"2000","journal-title":"Biochimie"},{"key":"ref_85","first-page":"279","article-title":"Anticoagulant venom and mammalian secreted phospholipases A(2): Protein-versus phospholipid-dependent mechanism of action","volume":"31","author":"Mounier","year":"2001","journal-title":"Haemostasis"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1111\/j.1432-1033.1996.0778p.x","article-title":"The anticoagulant effect of the human secretory phospholipase A2 on blood plasma and on a cell-free system is due to a phospholipid-independent mechanism of action involving the inhibition of factor Va","volume":"237","author":"Mounier","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"780","DOI":"10.1021\/bi00377a019","article-title":"Blood coagulation induced by the venom of Bothrops atrox. 2. Identification, purification, and properties of two factor X activators","volume":"26","author":"Hofmann","year":"1987","journal-title":"Biochemistry"},{"key":"ref_88","doi-asserted-by":"crossref","first-page":"10246","DOI":"10.1074\/jbc.270.17.10246","article-title":"A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning","volume":"270","author":"Zhang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1016\/S0041-0101(97)00118-9","article-title":"Purification from Bothrops lanceolatus (fer de lance) venom of a fibrino(geno)lytic enzyme with esterolytic activity","volume":"36","author":"Donato","year":"1998","journal-title":"Toxicon"},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.1074\/jbc.275.3.1823","article-title":"The contribution of residues 192 and 193 to the specificity of snake venom serine proteinases","volume":"275","author":"Braud","year":"2000","journal-title":"J. Biol. Chem."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"1277","DOI":"10.1016\/0041-0101(95)00070-3","article-title":"An activator of blood coagulation factor X from the venom of Bungarus fasciatus","volume":"33","author":"Zhang","year":"1995","journal-title":"Toxicon"},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"772","DOI":"10.1021\/bi00377a018","article-title":"Blood coagulation induced by the venom of Bothrops atrox. 1. Identification, purification, and properties of a prothrombin activator","volume":"26","author":"Hofmann","year":"1987","journal-title":"Biochemistry"},{"key":"ref_93","first-page":"9","article-title":"Cassian Bon, 1944\u20132008","volume":"RT16","author":"Goyffon","year":"2008","journal-title":"Rencontres Toxinologie"},{"key":"ref_94","doi-asserted-by":"crossref","unstructured":"Nemecz, D., Ostrowski, M., Ravatin, M., Saul, F., and Faure, G. (2020). Crystal Structure of Isoform CBd of the Basic Phospholipase A(2) Subunit of Crotoxin: Description of the Structural Framework of CB for Interaction with Protein Targets. Molecules, 25.","DOI":"10.2210\/pdb6tmy\/pdb"},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.jsb.2009.10.010","article-title":"Comparative structural studies of two natural isoforms of ammodytoxin, phospholipases A2 from Vipera ammodytes ammodytes which differ in neurotoxicity and anticoagulant activity","volume":"169","author":"Saul","year":"2010","journal-title":"J. Struct. Biol."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1016\/j.toxicon.2012.05.009","article-title":"Crystallographic characterization of functional sites of crotoxin and ammodytoxin, potent \u03b2-neurotoxins from Viperidae venom","volume":"60","author":"Faure","year":"2012","journal-title":"Toxicon."},{"key":"ref_97","unstructured":"Gopalakrishnakone, P., Cruz, L.J., and Luo, S. (2017). Toxins and Drug Discovery, Springer."},{"key":"ref_98","doi-asserted-by":"crossref","unstructured":"Faure, G., Gowda, V.T., and Maroun, R.C. (2007). Characterization of a human coagulation factor Xa-binding site on Viperidae snake venom phospholipases A2 by affinity binding studies and molecular bioinformatics. BMC Struct. Biol., 7.","DOI":"10.1186\/1472-6807-7-82"},{"key":"ref_99","doi-asserted-by":"crossref","unstructured":"Kini, R.M., Clemetson, K.J., Merkland, F.S., McClane, M.A., and Moritta, T. (2010). Toxins and Hemostasis: From Bench to Bedside, Springer.","DOI":"10.1007\/978-90-481-9295-3"},{"key":"ref_100","first-page":"671","article-title":"Structural and Functional Characterization of Anticoagulant, FXa-binding Viperidae Snake Venom Phospholipases A2","volume":"58","author":"Faure","year":"2011","journal-title":"Acta Chim. Slov."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"42","DOI":"10.3109\/15569543.2013.860170","article-title":"Human coagulation factor Xa prevents oligomerization of anti-coagulant phospholipases A2","volume":"33","author":"Ostrovski","year":"2014","journal-title":"Toxin Rev."},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.toxicon.2016.02.002","article-title":"Neurotoxic phospholipase A2 from rattlesnake as a new ligand and new regulator of prokaryotic receptor GLIC (proton-gated ion channel from G. violaceus)","volume":"116","author":"Ostrowski","year":"2016","journal-title":"Toxicon"},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"2898","DOI":"10.1016\/j.jmb.2016.05.016","article-title":"Rattlesnake Phospholipase A2 Increases CFTR-Chloride Channel Current and Corrects \u2206F508CFTR Dysfunction: Impact in Cystic Fibrosis","volume":"428","author":"Faure","year":"2016","journal-title":"J. Mol. Biol."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"167929","DOI":"10.1016\/j.jmb.2022.167929","article-title":"Design of Crotoxin-Based Peptides with Potentiator Activity Targeting the \u0394F508NBD1 Cystic Fibrosis Transmembrane Conductance Regulator","volume":"435","author":"Ravatin","year":"2023","journal-title":"J. Mol. Biol."},{"key":"ref_105","first-page":"329","article-title":"[Structures and functions of animal toxins]","volume":"191","author":"Guenneugues","year":"1997","journal-title":"C. R. Seances Soc. Biol. Fil."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0079-6603(08)61036-3","article-title":"Molecular evolution of snake toxins: Is the functional diversity of snake toxins associated with a mechanism of accelerated evolution?","volume":"59","author":"Ohno","year":"1998","journal-title":"Prog. Nucleic Acid. Res. Mol. Biol."},{"key":"ref_107","first-page":"257","article-title":"A review on conotoxins targeting ion channels and acetylcholine receptors of the vertebrate neuromuscular junction","volume":"49","author":"Favreau","year":"1999","journal-title":"Acta Physiol. Pharmacol. Ther. Latinoam."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1203","DOI":"10.1517\/17460441.2013.822365","article-title":"Physical and virtual screening methods for marine toxins and drug discovery targeting nicotinic acetylcholine receptors","volume":"8","author":"Benoit","year":"2013","journal-title":"Expert. Opin. Drug Discov."}],"container-title":["Toxins"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2072-6651\/15\/7\/462\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T20:14:56Z","timestamp":1760127296000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2072-6651\/15\/7\/462"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,19]]},"references-count":108,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2023,7]]}},"alternative-id":["toxins15070462"],"URL":"https:\/\/doi.org\/10.3390\/toxins15070462","relation":{},"ISSN":["2072-6651"],"issn-type":[{"value":"2072-6651","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,7,19]]}}}