{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T22:23:33Z","timestamp":1777501413184,"version":"3.51.4"},"reference-count":41,"publisher":"Elsevier BV","issue":"11-12","license":[{"start":{"date-parts":[[2009,11,1]],"date-time":"2009-11-01T00:00:00Z","timestamp":1257033600000},"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":["Biochimie"],"published-print":{"date-parts":[[2009,11]]},"DOI":"10.1016\/j.biochi.2009.08.006","type":"journal-article","created":{"date-parts":[[2009,9,5]],"date-time":"2009-09-05T09:06:58Z","timestamp":1252141618000},"page":"1482-1492","source":"Crossref","is-referenced-by-count":18,"title":["Identification of continuous interaction sites in PLA2-based protein complexes by peptide arrays"],"prefix":"10.1016","volume":"91","author":[{"given":"Consuelo Latorre","family":"Fortes-Dias","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Roberta M\u00e1rcia Marques dos","family":"Santos","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Angelo Jos\u00e9","family":"Magro","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcos Roberto de Mattos","family":"Fontes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlos","family":"Ch\u00e1vez-Ol\u00f3rtegui","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Claude","family":"Granier","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2009.08.006_bib1","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0041-0101(78)90056-9","article-title":"Mini-review \u2013 the crotoxin complex, an example of biochemical and pharmacological protein complementation","volume":"16","author":"Habermann","year":"1978","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib2","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":"10.1016\/j.biochi.2009.08.006_bib3","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":"10.1016\/j.biochi.2009.08.006_bib4","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 activity","volume":"27","author":"Faure","year":"1988","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2009.08.006_bib5","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1073\/pnas.75.2.600","article-title":"Search for relationships among the hemolytic, phospholipolytic, and neurotoxic activities of snake venoms","volume":"75","author":"Jeng","year":"1978","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.biochi.2009.08.006_bib6","doi-asserted-by":"crossref","first-page":"871","DOI":"10.1016\/j.toxicon.2007.07.025","article-title":"Understanding the molecular mechanism underlying the presynaptic toxicity of secreted phospholipase A2","author":"Punger\u010dar","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib7","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1016\/j.bbamcr.2008.01.011","article-title":"A pre-synaptically toxic secreted phospholipase A2 is internalized into motoneuron-like cells were it is rapidly translocated into the cytosol","author":"Pra\u017enikar","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2009.08.006_bib8","series-title":"Pharmacology of Neurotransmitter Release","article-title":"Pre-synaptic neurotoxins with enzymatic activities","volume":"vol. 184","author":"Rossetto","year":"2008"},{"key":"10.1016\/j.biochi.2009.08.006_bib9","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/0041-0101(91)90082-3","article-title":"Purification and properties of an antivenom factor from the plasma of the South American rattlesnake (Crotalus durissus terrificus)","volume":"29","author":"Fortes-Dias","year":"1991","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib10","doi-asserted-by":"crossref","first-page":"15646","DOI":"10.1016\/S0021-9258(17)40730-7","article-title":"A phospholipase A2 inhibitor from the plasma of the South American rattlesnake (Crotalus durissus terrificus), protein structure, genomic structure and mechanism of action","volume":"269","author":"Fortes-Dias","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2009.08.006_bib11","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":"10.1016\/j.biochi.2009.08.006_bib12","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1042\/bj3250527","article-title":"Purification and characterization of three distinct types of phospholipase A2 inhibitors from the blood plasma of the Chinese mamushi, Agkistrodon blomhoffii siniticus","volume":"325","author":"Ohkura","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2009.08.006_bib13","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/j.toxicon.2003.11.007","article-title":"Natural phospholipases A2 inhibitor proteins from snakes, mammals and plants","volume":"42","author":"Lizano","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib14","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.bbamem.2005.06.014","article-title":"Inhibition of crotoxin binding to synaptosomes by a receptor-like protein from Crotalus durissus terrificus (the South American rattlesnake)","volume":"1717","author":"Santos","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.biochi.2009.08.006_bib15","doi-asserted-by":"crossref","first-page":"1747","DOI":"10.1016\/S0041-0101(99)00116-6","article-title":"Studies on the specificity of CNF, a phospholipase A2 inhibitor isolated from the blood plasma of the South American rattlesnake (Crotalus durissus terrificus). I.\u00a0Interaction with PLA2 from Lachesis muta muta snake venom","volume":"37","author":"Fortes-Dias","year":"1999","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib16","doi-asserted-by":"crossref","first-page":"4799","DOI":"10.1046\/j.1432-1327.2000.01532.x","article-title":"Interaction of the neurotoxic and non neurotoxic secretory phospholipases A2 with the crotoxin inhibitor from Crotalus serum","volume":"267","author":"Faure","year":"2000","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2009.08.006_bib17","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1007\/BF00997027","article-title":"Biochemistry and pharmacology of the crotoxin complex","volume":"270","author":"R\u00fcbsamen","year":"1971","journal-title":"Naunyn-Schmiedeberg's Arch. Pharmacol."},{"key":"10.1016\/j.biochi.2009.08.006_bib18","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/S0958-1669(00)00178-6","article-title":"Applications of peptide arrays prepared by the SPOT technology","volume":"12","author":"Reineke","year":"2001","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.biochi.2009.08.006_bib19","doi-asserted-by":"crossref","first-page":"9217","DOI":"10.1016\/S0040-4020(01)85612-X","article-title":"SPOT synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support","volume":"48","author":"Frank","year":"1992","journal-title":"Tetrahedron"},{"key":"10.1016\/j.biochi.2009.08.006_bib20","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0022-1759(02)00140-0","article-title":"Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding","volume":"267","author":"Laune","year":"2002","journal-title":"J. Immunol. Methods"},{"key":"10.1016\/j.biochi.2009.08.006_bib21","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1002\/prot.21980","article-title":"Insights into the role of oligomeric state on the biological activities of Crotoxin: crystal structure of a tetrameric phospholipases A2 formed by two isoforms of Crotoxin B from Crotalus durissus terrificus","volume":"72","author":"Marchi-Salvador","year":"2008","journal-title":"Proteins"},{"key":"10.1016\/j.biochi.2009.08.006_bib22","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1016\/0041-0101(80)90002-1","article-title":"Purification of gyroxin from a South American rattlesnake (Crotalus durissus terrificus) venom","volume":"18","author":"Seki","year":"1980","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib23","series-title":"Antibodies a Laboratory Manual","first-page":"349","article-title":"Labeling antibodies","author":"Harlow","year":"1988"},{"key":"10.1016\/j.biochi.2009.08.006_bib24","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.biochi.2009.08.006_bib25","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1002\/prot.1130","article-title":"Molecular mapping of thrombin\u2013receptor interactions","volume":"45","author":"Ayala","year":"2001","journal-title":"Prot. Struct. Funct. Genet."},{"key":"10.1016\/j.biochi.2009.08.006_bib26","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1016\/0014-5793(95)01482-9","article-title":"Use of immobilized synthetic peptides for the identification of contact sites between human interleukin-6 and its receptor","volume":"379","author":"Weiergraber","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2009.08.006_bib27","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1023\/B:MODI.0000036242.01129.27","article-title":"Cellulose membrane supported peptide arrays for deciphering protein-protein interaction sites: the case of PIN, a protein with multiple natural partners","volume":"8","author":"Lajoix","year":"2004","journal-title":"Mol. Divers."},{"key":"10.1016\/j.biochi.2009.08.006_bib28","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/j.toxicon.2003.11.027","article-title":"Mapping structural determinants of biological activities in snake venoms phospholipases A2 by sequence analysis and site directed mutagenesis","volume":"42","author":"Chioato","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib29","doi-asserted-by":"crossref","first-page":"29867","DOI":"10.1016\/S0021-9258(18)43961-0","article-title":"Neutralizing interaction between heparins and myotoxin II, a lysine 49 phospholipase A2 from Bothrops asper snake venom. Identification of a heparin-binding site and cytolytic toxin region by the use of synthetic peptides and molecular modelling","volume":"269","author":"Lomonte","year":"1994","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2009.08.006_bib30","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":"10.1016\/j.biochi.2009.08.006_bib31","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1016\/0041-0101(94)90406-5","article-title":"Antipeptide antibodies directed to the C-terminal part of ammodytoxin A react with the PLA2 subunit of crotoxin and neutralize its pharmacological activity","volume":"32","author":"Curin-\u0160erbec","year":"1994","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib32","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","volume":"42","author":"Kini","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2009.08.006_bib33","doi-asserted-by":"crossref","first-page":"5759","DOI":"10.1046\/j.1432-1033.2002.03301.x","article-title":"The C-terminal region of ammodytoxins is important but no sufficient for neurotoxicity","volume":"269","author":"Prijatelj","year":"2002","journal-title":"Eur. J.\u00a0Biochem."},{"key":"10.1016\/j.biochi.2009.08.006_bib34","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.biochi.2005.06.015","article-title":"The C-terminal and \u03b2-wing regions of ammodytoxin A, a neurotoxic phospholipase A2 from Vipera ammodytes ammodytes, are critical for binding to factor Xa and for anticoagulant effect","volume":"88","author":"Prijatelj","year":"2006","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2009.08.006_bib35","doi-asserted-by":"crossref","first-page":"5800","DOI":"10.1021\/bi060217r","article-title":"Neurotoxicity and other pharmacological activities of the snake venom phospholipases A2 OS2: the N-terminal region is more important than enzymatic activity","volume":"45","author":"Rouault","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2009.08.006_bib36","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1042\/BJ20040125","article-title":"Molecular evolution and structure-function relationships of crotoxin-like and Asn 6-containing phospholipases A2 in pit vipers venoms","volume":"381","author":"Chen","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.biochi.2009.08.006_bib37","doi-asserted-by":"crossref","first-page":"877","DOI":"10.1016\/S1357-2725(01)00065-6","article-title":"Effects of chemical modifications of crotoxin B, the phospholipase A2 subunit of crotoxin from Crotalus durissus terrificus snake venom, on its enzymatic and pharmacological activities","volume":"33","author":"Soares","year":"2001","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.biochi.2009.08.006_bib38","doi-asserted-by":"crossref","first-page":"333","DOI":"10.1111\/j.1432-1033.1974.tb03838.x","article-title":"Biochemistry and pharmacology of the crotoxin complex. Biochemical analysis of crotapotin and the basic Crotalus phospholipase A","volume":"49","author":"Breithaupt","year":"1974","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.biochi.2009.08.006_bib39","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":"10.1016\/j.biochi.2009.08.006_bib40","doi-asserted-by":"crossref","first-page":"11627","DOI":"10.1016\/S0021-9258(17)39077-4","article-title":"A comparison of the crystal structure of phospholipase A2 from bovine pancreas and Crotalus atrox venom","volume":"260","author":"Renetseder","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.biochi.2009.08.006_bib41","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908409002533?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908409002533?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2021,10,10]],"date-time":"2021-10-10T11:25:36Z","timestamp":1633865136000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908409002533"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2009,11]]},"references-count":41,"journal-issue":{"issue":"11-12","published-print":{"date-parts":[[2009,11]]}},"alternative-id":["S0300908409002533"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2009.08.006","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2009,11]]}}}