{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,1]],"date-time":"2026-11-01T03:30:35Z","timestamp":1793503835122,"version":"4.5.0"},"reference-count":99,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2005,6,1]],"date-time":"2005-06-01T00:00:00Z","timestamp":1117584000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2005,6]]},"DOI":"10.1016\/j.toxicon.2005.02.018","type":"journal-article","created":{"date-parts":[[2005,4,14]],"date-time":"2005-04-14T15:03:14Z","timestamp":1113490994000},"page":"1147-1161","source":"Crossref","is-referenced-by-count":202,"title":["Structure\u2013function relationships and mechanism of anticoagulant phospholipase A2 enzymes from snake venoms"],"prefix":"10.1016","volume":"45","author":[{"given":"R. Manjunatha","family":"Kini","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.toxicon.2005.02.018_bib1","doi-asserted-by":"crossref","first-page":"6814","DOI":"10.1021\/bi00418a025","article-title":"Solubilization and physical characterization of acceptors for dendrotoxin and \u03b2-bungarotoxin from synaptic membranes of rat brain","volume":"27","author":"Black","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib2","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/0005-2744(76)90330-2","article-title":"A phospholipase A2 with anticoagulant activity. II. Inhibition of the phospholipid activity in coagulation","volume":"429","author":"Boffa","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2005.02.018_bib3","series-title":"Natural Toxins","first-page":"131","article-title":"Correlation of enzymatic activity and anticoagulant properties of phospholipase A2","author":"Boffa","year":"1980"},{"key":"10.1016\/j.toxicon.2005.02.018_bib4","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1038\/2161210a0","article-title":"Multiple forms of cobra venom phospholipase A","volume":"216","author":"Braganca","year":"1967","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2005.02.018_bib5","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0041-0101(97)00051-2","article-title":"The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2","volume":"36","author":"Carredano","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib6","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/0049-3848(93)90106-X","article-title":"Human recombinant non pancreatic secreted platelet phospholipase A2 has anticoagulant activity in vitro on human plasma","volume":"70","author":"Cirino","year":"1993","journal-title":"Thromb. Res."},{"key":"10.1016\/j.toxicon.2005.02.018_bib7","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/0041-0101(81)90118-5","article-title":"Effect of modification of one histidine residue on the enzymatic and pharmacological properties of a toxic phospholipase A2 from Naja nigricollis snake venom and less toxic phospholipases A2 from Hemachatus haemachatus and Naja naja atra venoms","volume":"19","author":"Condrea","year":"1981","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib8","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/0041-0101(81)90108-2","article-title":"Dissociation of enzymatic activity from lethality and pharmacological properties by carbamylation of lysines in Naja nigricollis and Naja naja atra snake venom phospholipases A2","volume":"19","author":"Condrea","year":"1981","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib9","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1055\/s-0038-1650134","article-title":"Lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2","volume":"45","author":"Condrea","year":"1981","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.toxicon.2005.02.018_bib10","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1055\/s-0038-1657193","article-title":"Additional evidence for a lack of correlation between anticoagulant activity and phospholipid hydrolysis by snake venom phospholipases A2","volume":"47","author":"Condrea","year":"1982","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.toxicon.2005.02.018_bib11","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0041-0101(83)90005-3","article-title":"Ethoxyformylation and guanidination of snake venom phospholipases A2: effects on enzymatic activity, lethality and some pharmacological properties","volume":"21","author":"Condrea","year":"1983","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib12","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1016\/0024-3205(83)90911-6","article-title":"Effect of methylation of histidine-48 on some enzymatic and pharmacological activities of snake venom phospholipases A2","volume":"32","author":"Condrea","year":"1983","journal-title":"Life Sci."},{"key":"10.1016\/j.toxicon.2005.02.018_bib13","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1055\/s-0038-1657347","article-title":"Anticoagulant activity and phosphatidylserine hydrolysis by venom phospholipases A2","volume":"49","author":"Condrea","year":"1983","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.toxicon.2005.02.018_bib14","doi-asserted-by":"crossref","first-page":"26315","DOI":"10.1074\/jbc.274.37.26315","article-title":"Identification and purification of a novel receptor for secretory phospholipase A2 in porcine cerebral cortex","volume":"274","author":"\u010copi\u010d","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib15","series-title":"Venom Phospholipase Enzymes: Structure, Function and Mechanism","first-page":"29","article-title":"Molecular biology of snake venom phospholipases A2","author":"Danse","year":"1997"},{"key":"10.1016\/j.toxicon.2005.02.018_bib16","doi-asserted-by":"crossref","first-page":"13057","DOI":"10.1016\/S0021-9258(17)36794-7","article-title":"Diversity of group types, regulation, and function of phospholipase A2","volume":"269","author":"Dennis","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib17","doi-asserted-by":"crossref","first-page":"2339","DOI":"10.1046\/j.1471-4159.1995.64052339.x","article-title":"Novel reticular calcium binding protein is purified on taipoxin columns","volume":"64","author":"Dodds","year":"1995","journal-title":"J. Neurochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib18","doi-asserted-by":"crossref","first-page":"21488","DOI":"10.1074\/jbc.272.34.21488","article-title":"Neuronal pentraxin receptor, a novel putative integral membrane pentraxin that interacts with neuronal pentraxin 1 and 2 and taipoxin-associated calcium-binding protein 49","volume":"272","author":"Dodds","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib19","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1111\/j.1432-1033.1983.tb07859.x","article-title":"Conformational properties of phospholipase A2. Secondary structure prediction, circular dichroism and relative interface hydrophilicity","volume":"137","author":"Dufton","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib20","series-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","first-page":"353","article-title":"Anticoagulant effects of phospholipases","author":"Evans","year":"1997"},{"key":"10.1016\/j.toxicon.2005.02.018_bib21","doi-asserted-by":"crossref","first-page":"3793","DOI":"10.1016\/S0021-9258(19)85774-5","article-title":"Isolation of anticoagulant proteins from cobra venom (Naja nigricollis). Identity with phospholipases A2","volume":"255","author":"Evans","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib22","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":"10.1016\/j.toxicon.2005.02.018_bib23","doi-asserted-by":"crossref","first-page":"4481","DOI":"10.1093\/nar\/12.11.4481","article-title":"Blood coagulation factor X mRNA encodes a single polypeptide chain containing a prepro leader sequence","volume":"12","author":"Fung","year":"1984","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.toxicon.2005.02.018_bib24","doi-asserted-by":"crossref","first-page":"2971","DOI":"10.1016\/S0021-9258(19)50682-2","article-title":"The complete cDNA sequence of bovine coagulation factor V","volume":"267","author":"Guinto","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib25","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/0163-7258(85)90038-5","article-title":"Phospholipases in snake venoms and their effects on nerve and muscle","volume":"31","author":"Harris","year":"1985","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.toxicon.2005.02.018_bib26","doi-asserted-by":"crossref","first-page":"4913","DOI":"10.1016\/S0021-9258(17)40140-2","article-title":"Amino acid sequence of phospholipase A2-\u03b1 from the venom of Crotalus adamanteus. A new classification of phospholipases A2 based upon structural determinants","volume":"262","author":"Heinrikson","year":"1977","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib27","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1093\/jb\/101.3.625","article-title":"Selective release of phospholipase A2 and lysophosphatidylserine-specific lysophospholipase from rat platelets","volume":"101","author":"Horigome","year":"1987","journal-title":"J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib28","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1007\/BF00762844","article-title":"Identification of a crotoxin-binding protein in membranes from guinea pig brain by photoaffinity labeling","volume":"22","author":"Hseu","year":"1990","journal-title":"J. Bioenerg. Biomembr."},{"key":"10.1016\/j.toxicon.2005.02.018_bib29","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1006\/bbrc.1997.7416","article-title":"Purification and partial amino acid sequence of a novel protein of the reticulocalbin family","volume":"239","author":"Hseu","year":"1997","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2005.02.018_bib30","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1016\/S0014-5793(99)00177-5","article-title":"Crocalbin: a new calcium-binding protein that is also a binding protein for crotoxin, a neurotoxic phospholipase A2","volume":"445","author":"Hseu","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.toxicon.2005.02.018_bib31","doi-asserted-by":"crossref","first-page":"26338","DOI":"10.1016\/S0021-9258(18)47198-0","article-title":"Determinants of the inhibitory action of purified 14-kDa phospholipases A2 on cell-free prothrombinase complex","volume":"269","author":"Inada","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib99","doi-asserted-by":"crossref","unstructured":"Karlsson, E., 1979. Chemistry of protein toxins in snake venoms. In: Lee, C.Y. (Ed.), Handbook of Experimental Pharmacology, vol. 52, Snake Venoms. Springer, Berlin, pp. 159\u2013212.","DOI":"10.1007\/978-3-642-66913-2_5"},{"key":"10.1016\/j.toxicon.2005.02.018_bib32","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1006\/abbi.1999.1345","article-title":"Targeting of venom phospholipases: the strongly anticoagulant phospholipase A2 from Naja nigricollis venom binds to coagulation factor Xa to inhibit the prothrombinase complex","volume":"369","author":"Kerns","year":"1999","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2005.02.018_bib33","series-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","first-page":"1","article-title":"Phospholipase A2\u2013A complex multifunctional protein puzzle","author":"Kini","year":"1997"},{"key":"10.1016\/j.toxicon.2005.02.018_bib34","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1046\/j.1440-1681.2002.03725.x","article-title":"Molecular molds with multiple missions: functional sites in three-finger toxins","volume":"29","author":"Kini","year":"2002","journal-title":"Clin. Exp. Pharmacol. Physiol."},{"key":"10.1016\/j.toxicon.2005.02.018_bib35","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/j.toxicon.2003.11.002","article-title":"Excitement ahead: structure, function and mechanism of snake venom phospholipase A2 enzymes","volume":"42","author":"Kini","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib36","doi-asserted-by":"crossref","first-page":"14402","DOI":"10.1016\/S0021-9258(18)47808-8","article-title":"Structure\u2013function relationships of phospholipases: the anticoagulant region of phospholipases A2","volume":"262","author":"Kini","year":"1987","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib37","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1055\/s-0038-1647023","article-title":"Correlation between the enzymatic activity, anticoagulant and antiplatelet effects of phospholipase A2 isoenzymes from Naja nigricollis venom","volume":"60","author":"Kini","year":"1988","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.toxicon.2005.02.018_bib38","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/0041-0101(89)90013-5","article-title":"A model to explain the pharmacological effects of snake venom phospholipases A2","volume":"27","author":"Kini","year":"1989","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib39","doi-asserted-by":"crossref","first-page":"1585","DOI":"10.1016\/0041-0101(95)00103-4","article-title":"The role of enzymatic activity in inhibition of the extrinsic tenase complex by phospholipase A2 isoenzymes from Naja nigricollis venom","volume":"33","author":"Kini","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib40","doi-asserted-by":"crossref","first-page":"17786","DOI":"10.1074\/jbc.M002254200","article-title":"Comparison of Biochemical interactions of the neuronal pentraxins. Neuronal pentraxin (NP) receptor binds to taipoxin and taipoxin-associated calcium-binding protein 49 via NP1 and NP2","volume":"275","author":"Kirkpatrick","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib41","doi-asserted-by":"crossref","first-page":"5768","DOI":"10.1016\/S0021-9258(18)83616-X","article-title":"Structure and properties of a human non-pancreatic phospholipase A2","volume":"264","author":"Kramer","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib42","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/S0300-9084(00)01172-X","article-title":"Neuronal receptors for phospholipases A2 and \u03b2-neurotoxicity","volume":"82","author":"Kri\u017eaj","year":"2000","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2005.02.018_bib43","doi-asserted-by":"crossref","first-page":"13938","DOI":"10.1021\/bi00250a049","article-title":"Identification of the neuronal acceptor in bovine cortex for ammodytoxin C, a presynaptically neurotoxic phospholipase A2","volume":"33","author":"Kri\u017eaj","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib44","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/0041-0101(94)00182-8","article-title":"Ammodytoxin A acceptor in bovine brain synaptic membranes","volume":"33","author":"Kri\u017eaj","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib45","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1016\/0041-0101(96)00064-5","article-title":"Re-examination of crotoxin\u2013membrane interactions","volume":"34","author":"Kri\u017eaj","year":"1996","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib46","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":"Kri\u017eaj","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib47","doi-asserted-by":"crossref","first-page":"11503","DOI":"10.1016\/S0021-9258(18)60492-2","article-title":"Identification and properties of very high affinity brain membrane-binding sites for a neurotoxic phospholipase from the Taipan venom","volume":"264","author":"Lambeau","year":"1989","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib48","doi-asserted-by":"crossref","first-page":"9526","DOI":"10.1016\/S0021-9258(19)38881-7","article-title":"Identification and purification of a very high affinity binding protein for toxic phospholipases A2 in skeletal muscle","volume":"265","author":"Lambeau","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib49","series-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","first-page":"389","article-title":"Membrane receptors for venom phospholipases A2","author":"Lambeau","year":"1997"},{"key":"10.1016\/j.toxicon.2005.02.018_bib50","doi-asserted-by":"crossref","first-page":"1626","DOI":"10.1021\/bi00303a007","article-title":"Characterization of bovine prothrombin mRNA and its translation product","volume":"23","author":"MacGillivray","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib51","doi-asserted-by":"crossref","first-page":"1755","DOI":"10.1021\/bi00430a050","article-title":"Complete sequence of the human tissue factor gene, a highly regulated cellular receptor that initiates the coagulation protease cascade","volume":"28","author":"Mackman","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib52","doi-asserted-by":"crossref","first-page":"171","DOI":"10.3109\/10408449109089878","article-title":"Effects of snake venoms on hemostasis","volume":"21","author":"Meier","year":"1991","journal-title":"Crit. Rev. Toxicol."},{"key":"10.1016\/j.toxicon.2005.02.018_bib53","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1042\/bj2230607","article-title":"The contribution of Ca2+ and phospholipids to the activation of human blood-coagulation Factor X by activated Factor IX","volume":"223","author":"Mertens","year":"1984","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib54","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1111\/j.1432-1033.1993.tb18129.x","article-title":"Secretory phospholipase A2 is not required for arachidonic acid liberation during platelet activation","volume":"216","author":"Mounier","year":"1993","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib55","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0005-2760(94)90013-2","article-title":"Platelet secretory phospholipase A2 fails to induce rabbit platelet activation and to release arachidonic acid in contrast with venom phospholipases A2","volume":"1214","author":"Mounier","year":"1994","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2005.02.018_bib56","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":"10.1016\/j.toxicon.2005.02.018_bib57","doi-asserted-by":"crossref","first-page":"23764","DOI":"10.1074\/jbc.273.37.23764","article-title":"Inhibition of prothrombinase by human secretory phospholipase A2 involves binding to factor Xa","volume":"273","author":"Mounier","year":"1998","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib58","doi-asserted-by":"crossref","first-page":"4960","DOI":"10.1046\/j.1432-1327.2000.01523.x","article-title":"Basic residues of human group IIA phospholipase A2 are important for binding to factor Xa and prothrombinase inhibition comparison with other mammalian secreted phospholipases A2","volume":"267","author":"Mounier","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib59","first-page":"279","article-title":"Anticoagulant venom and mammalian secreted phospholipases A2: protein- versus phospholipid-dependent mechanism of action","volume":"31","author":"Mounier","year":"2001","journal-title":"Haemostasis"},{"key":"10.1016\/j.toxicon.2005.02.018_bib60","doi-asserted-by":"crossref","first-page":"10952","DOI":"10.1016\/S0021-9258(19)86616-4","article-title":"The contribution of bovine Factor V and Factor Va to the activity of prothrombinase","volume":"257","author":"Nesheim","year":"1979","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib61","doi-asserted-by":"crossref","first-page":"1443","DOI":"10.1016\/S0021-9258(19)68213-X","article-title":"Studies of the capacity of factor Xa to protect factor Va from inactivation by activated protein C","volume":"257","author":"Nesheim","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib62","doi-asserted-by":"crossref","first-page":"8557","DOI":"10.1073\/pnas.89.18.8557","article-title":"Unusually high conservation of untranslated sequences of cDNAs for Trimeresurus flavoviridis phospholipase A2 isoenzymes","volume":"89","author":"Ogawa","year":"1992","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"10.1016\/j.toxicon.2005.02.018_bib63","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1111\/j.1432-1033.1982.tb06961.x","article-title":"Preparation of neurotoxic 3H-beta-bungarotoxin: demonstration of saturable binding to brain synapses and its inhibition by toxin I","volume":"128","author":"Othman","year":"1982","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib64","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/0304-4165(78)90198-8","article-title":"Purification and characterization of the anticoagulant principle of Trimeresurus mucrosquamatus venom","volume":"541","author":"Ouyang","year":"1978","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2005.02.018_bib65","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/0041-0101(81)90123-9","article-title":"Mechanism of the anticoagulant action of phospholipase A purified from Trimeresurus mucrosquamatus (Formosan habu) snake venom","volume":"19","author":"Ouyang","year":"1981","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib66","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1016\/0041-0101(92)90040-C","article-title":"Characterization of snake venom components acting on blood coagulation and platelet function","volume":"30","author":"Ouyang","year":"1992","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib67","doi-asserted-by":"crossref","first-page":"899","DOI":"10.1042\/bj2570899","article-title":"Dendrotoxin acceptor from bovine synaptic plasma membranes","volume":"257","author":"Parcej","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2005.02.018_bib68","doi-asserted-by":"crossref","first-page":"7734","DOI":"10.1016\/S0021-9258(19)43892-1","article-title":"Snake venom phospholipases A2. A fluorescent study of their binding to phospholipid vesicles. Correlation with their anticoagulant activities","volume":"266","author":"Prigent-Dachary","year":"1980","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib69","series-title":"Hemorrhagic Diseases and Thrombosis","first-page":"391","article-title":"Prothrombin time (one-stage procedure)","author":"Quick","year":"1966"},{"key":"10.1016\/j.toxicon.2005.02.018_bib70","doi-asserted-by":"crossref","first-page":"10015","DOI":"10.1016\/S0021-9258(18)33978-4","article-title":"Binding of \u03b2-bungarotoxin to synaptic membrane fractions of chick brain","volume":"257","author":"Rehm","year":"1982","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib71","doi-asserted-by":"crossref","first-page":"6865","DOI":"10.1016\/S0021-9258(17)39808-3","article-title":"Solubilization and characterization of the \u03b2-bungarotoxin-binding protein of chick brain membranes","volume":"259","author":"Rehm","year":"1984","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib72","series-title":"Natural Toxins","first-page":"129","article-title":"The relationship between enzymatic activity and pharmacological properties of phospholipases","author":"Rosenberg","year":"1986"},{"key":"10.1016\/j.toxicon.2005.02.018_bib73","series-title":"Handbook of Toxinology","first-page":"667","article-title":"Phospholipases","author":"Rosenberg","year":"1990"},{"key":"10.1016\/j.toxicon.2005.02.018_bib74","doi-asserted-by":"crossref","first-page":"3525","DOI":"10.1016\/0006-2952(83)90298-8","article-title":"Dissociation of pharmacological and enzymatic activities of snake venom phospholipases A2 by modification of carboxylate groups","volume":"32","author":"Rosenberg","year":"1983","journal-title":"Biochem. Pharm."},{"key":"10.1016\/j.toxicon.2005.02.018_bib75","series-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","first-page":"97","article-title":"Phospholipase A2: structure and catalytic properties","author":"Scott","year":"1997"},{"key":"10.1016\/j.toxicon.2005.02.018_bib76","doi-asserted-by":"crossref","first-page":"20094","DOI":"10.1016\/S0021-9258(17)30474-X","article-title":"\u03b1-Dendrotoxin acceptor from bovine brain is a K+ channel protein. Evidence from the N-terminal sequence of its larger subunit","volume":"265","author":"Scott","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib77","doi-asserted-by":"crossref","first-page":"289","DOI":"10.1006\/abbi.1999.1672","article-title":"Phospholipase A2 with platelet aggregation inhibitor activity from Austrelaps superbus venom: protein purification and cDNA cloning","volume":"375","author":"Singh","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2005.02.018_bib78","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1006\/jmbi.2001.4550","article-title":"Sequence and crystal structure determination of a basic phospholipase A2 from common krait (Bungarus caeruleus) at 2.4\u00c5 resolution: identification and characterization of its pharmacological sites","volume":"307","author":"Singh","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.toxicon.2005.02.018_bib79","doi-asserted-by":"crossref","first-page":"12493","DOI":"10.1074\/jbc.C100048200","article-title":"A high affinity acceptor for phospholipase A2 with neurotoxic activity is a calmodulin","volume":"276","author":"\u0160ribar","year":"2001","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib80","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1016\/S0006-291X(03)00228-6","article-title":"The neurotoxic phospholipase A2 associates, through a non-phosphorylated binding motif, with 14-3-3 protein \u03b3 and \u03b5 isoforms","volume":"302","author":"\u0160ribar","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2005.02.018_bib81","unstructured":"Stefansson, S., 1990. The mechanism of the anticoagulant effect of the basic phospholipase A2 from Naja nigricollis venom. PhD Dissertation, Virginia Commonwealth University, Richmond, VA, 134 p."},{"key":"10.1016\/j.toxicon.2005.02.018_bib82","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0049-3848(89)90056-X","article-title":"The inhibition of clotting complexes of the extrinsic coagulation cascade by the phospholipase A2 isoenzymes from Naja nigricollis venom","volume":"55","author":"Stefansson","year":"1989","journal-title":"Thromb. Res."},{"key":"10.1016\/j.toxicon.2005.02.018_bib83","doi-asserted-by":"crossref","first-page":"7742","DOI":"10.1021\/bi00485a024","article-title":"The basic phospholipase A2 from Naja nigricollis venom inhibits the prothrombinase complex by a novel nonenzymatic mechanism","volume":"29","author":"Stefansson","year":"1990","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2005.02.018_bib84","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1016\/S0041-0101(97)00014-7","article-title":"Isolation and purification of superbins I and II from Austrelaps superbus (copperhead) snake venom and their anticoagulant and antiplatelet effects","volume":"35","author":"Subburaju","year":"1997","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib85","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/0041-0101(90)90068-I","article-title":"Amino acid sequences of eight phospholipases A2 from the venom of Australian king brown snake Pseudechis australis","volume":"28","author":"Takasaki","year":"1990","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib86","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1093\/bib\/4.1.53","article-title":"Bioinformatics for venom and toxin sciences","volume":"4","author":"Tan","year":"2003","journal-title":"Brief Bioinform."},{"key":"10.1016\/j.toxicon.2005.02.018_bib87","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1007\/BF01025490","article-title":"Specific binding of three neurotoxins with phospholipase A2 activity to synaptosomal membrane preparations from the guinea pig brain","volume":"5","author":"Tzeng","year":"1986","journal-title":"J. Protein Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib88","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S1388-1981(00)00110-4","article-title":"Increasing molecular diversity of secreted phospholipases A2 and their receptors and binding proteins","volume":"1488","author":"Valentin","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2005.02.018_bib89","doi-asserted-by":"crossref","first-page":"3433","DOI":"10.1016\/S0021-9258(19)69627-4","article-title":"The role of phospholipid and factor VIIIa in the activation of bovine factor X","volume":"256","author":"van Dieijen","year":"1981","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib90","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1006\/bbrc.2001.5940","article-title":"High-molecular-mass receptors for ammodytoxin in pig are tissue-specific isoforms of M-type phospholipase A2 receptor","volume":"289","author":"Vardjan","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2005.02.018_bib91","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1111\/j.1432-1033.1980.tb04982.x","article-title":"Correlation of enzymatic activity and anticoagulant properties of phospholipase A2","volume":"112","author":"Verheij","year":"1980","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib92","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/0041-0101(87)90286-8","article-title":"Characterization of three edema inducing phospholipase A2 enzymes from habu (Trimeresurus flavoviridis) venom and their interaction with an alkaloid, aristalochic acid","volume":"25","author":"Vishwanath","year":"1987","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib93","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/0041-0101(88)90278-4","article-title":"Purification and partial biochemical characterization of an edema inducing phospholipase A2 from Vipera russelli (Russell's viper) snake venom","volume":"26","author":"Vishwanath","year":"1988","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2005.02.018_bib94","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1006\/bbrc.1998.9427","article-title":"Identification of a new high-affinity binding protein for neurotoxic phospholipases A2","volume":"251","author":"Vu\u010demilo","year":"1998","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2005.02.018_bib95","doi-asserted-by":"crossref","first-page":"1484","DOI":"10.1016\/S0021-9258(19)40042-2","article-title":"Identification of the binding site for activated protein C on the light chain of factors V and VIII","volume":"265","author":"Walker","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2005.02.018_bib96","doi-asserted-by":"crossref","first-page":"1560","DOI":"10.1126\/science.2274787","article-title":"Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue","volume":"250","author":"White","year":"1990","journal-title":"Science"},{"key":"10.1016\/j.toxicon.2005.02.018_bib97","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1042\/bj0840052","article-title":"The fractionation of Russell's viper venom with special reference to the coagulant protein","volume":"84","author":"Williams","year":"1962","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2005.02.018_bib98","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1016\/S0041-0101(99)00193-2","article-title":"Structure of basic phospholipase A2 from Agkistrodon halys Pallas: implications for its association, hemolytic and anticoagulant activities","volume":"38","author":"Zhao","year":"2000","journal-title":"Toxicon"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010105000772?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010105000772?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,7,8]],"date-time":"2021-07-08T18:23:59Z","timestamp":1625768639000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010105000772"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,6]]},"references-count":99,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2005,6]]}},"alternative-id":["S0041010105000772"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2005.02.018","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2005,6]]}}}