{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,12]],"date-time":"2025-11-12T05:48:53Z","timestamp":1762926533152,"version":"build-2065373602"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T00:00:00Z","timestamp":1509494400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,11,1]],"date-time":"2017-11-01T00:00:00Z","timestamp":1509494400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,8,4]],"date-time":"2018-08-04T00:00:00Z","timestamp":1533340800000},"content-version":"vor","delay-in-days":276,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100003593","name":"Conselho Nacional de Desenvolvimento Cient\u00edfico e Tecnol\u00f3gico","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003593","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001807","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de S\u00e3o Paulo","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001807","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002322","name":"Coordena\u00e7\u00e3o de Aperfei\u00e7oamento de Pessoal de N\u00edvel Superior","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002322","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2017,11]]},"DOI":"10.1016\/j.biochi.2017.07.009","type":"journal-article","created":{"date-parts":[[2017,7,25]],"date-time":"2017-07-25T07:46:00Z","timestamp":1500968760000},"page":"11-21","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":13,"special_numbering":"C","title":["Structural studies with BnSP-7 reveal an atypical oligomeric conformation compared to phospholipases A2-like toxins"],"prefix":"10.1016","volume":"142","author":[{"given":"Lino Fernando G.","family":"de Lima","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rafael J.","family":"Borges","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maria Alejandra","family":"Viviescas","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Carlos A.H.","family":"Fernandes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marcos R.M.","family":"Fontes","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2017.07.009_bib1","doi-asserted-by":"crossref","first-page":"1591","DOI":"10.1371\/journal.pmed.0050218","article-title":"The global burden of snakebite: a literature analysis and modelling based on regional estimates of envenoming and deaths","volume":"5","author":"Kasturiratne","year":"2008","journal-title":"PLoS Med."},{"key":"10.1016\/j.biochi.2017.07.009_bib2","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1097\/00007691-200002000-00014","article-title":"Bites and stings from venomous animals: a global overview","volume":"22","author":"White","year":"2000","journal-title":"Ther. Drug Monit."},{"key":"10.1016\/j.biochi.2017.07.009_bib3","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1002\/jms.1242","article-title":"Snake venomics. Strategy and applications","volume":"42","author":"Calvete","year":"2007","journal-title":"J.\u00a0Mass. Spectrom."},{"key":"10.1016\/j.biochi.2017.07.009_bib4","doi-asserted-by":"crossref","first-page":"0727","DOI":"10.1371\/journal.pmed.0030150","article-title":"Confronting the neglected problem of snake bite envenoming: the need for a global partnership","volume":"3","author":"Guti\u00e9rrez","year":"2006","journal-title":"PLoS Med."},{"key":"10.1016\/j.biochi.2017.07.009_bib5","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0000569","article-title":"Snake envenoming: a disease of poverty","volume":"3","author":"Harrison","year":"2009","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.biochi.2017.07.009_bib6","series-title":"Animais Pe\u00e7onhentos No Brasil","first-page":"6","article-title":"Epidemiologia dos acidentes por animais pe\u00e7onhentos","author":"Ara\u00fajo","year":"2003"},{"year":"2001","author":"Sa\u00fade","series-title":"Manual de Diagn\u00f3stico e Tratamento de Acidentes por Animais Pe\u00e7onhentos","key":"10.1016\/j.biochi.2017.07.009_bib7"},{"key":"10.1016\/j.biochi.2017.07.009_bib8","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1016\/0041-0101(95)00085-Z","article-title":"Phospholipase A2myotoxins from Bothrops snake venoms","volume":"33","author":"Guti\u00e9rrez","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2017.07.009_bib9","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0000603","article-title":"Snake bite in south asia: a review","volume":"4","author":"Alirol","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.biochi.2017.07.009_bib10","doi-asserted-by":"crossref","first-page":"147","DOI":"10.1007\/s11010-006-1738-3","article-title":"Strong myotoxic activity of Trimeresurusmalabaricus venom: role of metalloproteases","volume":"282","author":"Raghavendra Gowda","year":"2006","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.biochi.2017.07.009_bib11","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.biochi.2017.07.009_bib12","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1016\/j.bbalip.2006.07.011","article-title":"The phospholipase A2 superfamily and its group numbering system","volume":"1761","author":"Schaloske","year":"2006","journal-title":"Biochim. Biophys. Acta - Mol. Cell Biol. Lipids"},{"key":"10.1016\/j.biochi.2017.07.009_bib13","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1007\/s10557-008-6132-9","article-title":"Phospholipase A2 biochemistry","volume":"23","author":"Burke","year":"2009","journal-title":"Cardiovasc. Drugs Ther."},{"key":"10.1016\/j.biochi.2017.07.009_bib14","first-page":"17649","volume":"vol. 265","author":"Holland","year":"1990"},{"key":"10.1016\/j.biochi.2017.07.009_bib15","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.jsb.2010.03.019","article-title":"Comparison between apo and complexed structures of bothropstoxin-I reveals the role of Lys122 and Ca2+-binding loop region for the catalytically inactive Lys49-PLA2s","volume":"171","author":"Fernandes","year":"2010","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.biochi.2017.07.009_bib16","doi-asserted-by":"crossref","first-page":"1587","DOI":"10.1016\/S0041-0101(01)00141-6","article-title":"Identification of the myotoxic site of the Lys49 phospholipase A2 from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities","volume":"39","author":"N\u00fanez","year":"2001","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2017.07.009_bib17","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1016\/j.bbamem.2007.01.023","article-title":"Mapping of the structural determinants of artificial and biological membrane damaging activities of a Lys49 phospholipase A2 by scanning alanine mutagenesis","volume":"1768","author":"Chioato","year":"2007","journal-title":"Biochim. Biophys. Acta - Biomembr."},{"key":"10.1016\/j.biochi.2017.07.009_bib18","doi-asserted-by":"crossref","first-page":"2772","DOI":"10.1016\/j.bbapap.2013.10.009","article-title":"Structural bases for a complete myotoxic mechanism: crystal structures of two non-catalytic phospholipases A2-like from Bothropsbrazili venom","volume":"1834","author":"Fernandes","year":"2013","journal-title":"Biochim. Biophys. Acta - Proteins Proteom."},{"key":"10.1016\/j.biochi.2017.07.009_bib19","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1016\/j.bbapap.2014.09.015","article-title":"A\u00a0structure-based proposal for a comprehensive myotoxic mechanism of phospholipase A2-like proteins from viperid snake venoms","volume":"1844","author":"Fernandes","year":"2014","journal-title":"Biochim. Biophys. Acta - Proteins Proteom."},{"key":"10.1016\/j.biochi.2017.07.009_bib20","doi-asserted-by":"crossref","first-page":"2625","DOI":"10.2174\/092986705774370655","article-title":"Medicinal plants with inhibitory properties against snake venoms","volume":"12","author":"Soares","year":"2005","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.biochi.2017.07.009_bib21","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/j.toxicon.2005.04.023","article-title":"Rosmarinic acid, a new snake venom phospholipase A2 inhibitor from Cordia verbenacea (Boraginaceae): antiserum action potentiation and molecular interaction","volume":"46","author":"Ticli","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2017.07.009_bib22","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0028521","article-title":"Structural and functional studies of a bothropicmyotoxin complexed to rosmarinic acid: new insights into Lys49-PLA2 inhibition","volume":"6","author":"dos Santos","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2017.07.009_bib23","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1371\/journal.pone.0133370","article-title":"Structural basis for the inhibition of a phospholipase A2-like toxin by caffeic and aristolochic acids","volume":"10","author":"Fernandes","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2017.07.009_bib24","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/S0031-9422(00)00229-6","article-title":"Plant natural products active against snake bite\u2013the molecular approach","volume":"55","author":"Mors","year":"2000","journal-title":"Phytochemistry"},{"key":"10.1016\/j.biochi.2017.07.009_bib25","doi-asserted-by":"crossref","first-page":"2374","DOI":"10.1021\/jf970055t","article-title":"Antioxidant activities of caffeic acid and its related hydroxycinnamic acid compounds","volume":"45","author":"Chen","year":"1997","journal-title":"J.\u00a0Agric. Food Chem."},{"key":"10.1016\/j.biochi.2017.07.009_bib26","first-page":"403","article-title":"Cinnamic acid derivatives: a new chapter of various pharmacological activities","volume":"3","author":"Sharma","year":"2011","journal-title":"J.\u00a0Chem. Pharm. Res."},{"key":"10.1016\/j.biochi.2017.07.009_bib27","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1007\/BF02464209","article-title":"Relationship between biological activity and thermodynamic properties of 5,5-dimethyl-1,3-cyclohexanedione derivatives","volume":"32","author":"Bogdashev","year":"1998","journal-title":"Pharm. Chem. J."},{"key":"10.1016\/j.biochi.2017.07.009_bib28","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/S1360-1385(97)01018-2","article-title":"Antioxidant properties of phenolic compounds","volume":"2","author":"Rice-Evans","year":"1997","journal-title":"Trends Plant Sci."},{"key":"10.1016\/j.biochi.2017.07.009_bib29","doi-asserted-by":"crossref","first-page":"3556","DOI":"10.1016\/j.bmcl.2013.04.033","article-title":"Caffeic acid derivatives: a new type of influenza neuraminidase inhibitors","volume":"23","author":"Xie","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"unstructured":"J.W. Agoro, Crystalline caffeic acid derivatives and compositions and method for treating snakebite., US 4124724 A, 1978.","key":"10.1016\/j.biochi.2017.07.009_bib30"},{"key":"10.1016\/j.biochi.2017.07.009_bib31","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1006\/abbi.2000.1790","article-title":"Structural and functional characterization of BnSP-7, a Lys49 myotoxic phospholipase A2 homologue from Bothropsneuwiedipauloensis venom","volume":"378","author":"Soares","year":"2000","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2017.07.009_bib32","doi-asserted-by":"crossref","first-page":"179","DOI":"10.2174\/0929866013409445","article-title":"Comparative biochemical studies of myotoxic phospholipase A2 from Bothrops venom","volume":"8","author":"Toyama","year":"2001","journal-title":"Protein Peptide Lett. USA."},{"key":"10.1016\/j.biochi.2017.07.009_bib33","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1016\/S0167-4838(99)00120-X","article-title":"Crystallization and preliminary X-ray diffraction analysis of a myotoxic phospholipase A2 homologue from Bothropsneuwiedipauloensis venom","volume":"1432","author":"Fontes","year":"1999","journal-title":"Biochim. Biophys. Acta - Protein Struct. Mol. Enzymol."},{"key":"10.1016\/j.biochi.2017.07.009_bib34","doi-asserted-by":"crossref","first-page":"713","DOI":"10.1016\/j.bbrc.2003.10.047","article-title":"Crystal structures of BnSP-7 and BnSP-6, two Lys49-phospholipases A2: quaternary structure and inhibition mechanism insights","volume":"311","author":"Magro","year":"2003","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.biochi.2017.07.009_bib35","doi-asserted-by":"crossref","first-page":"342","DOI":"10.1089\/adt.2011.0380","article-title":"Molecular interaction studies using microscale thermophoresis","volume":"9","author":"Jerabek-Willemsen","year":"2011","journal-title":"Assay Drug Dev. Technol."},{"key":"10.1016\/j.biochi.2017.07.009_bib36","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","article-title":"Processing of X-ray diffraction data collected in oscillation mode","volume":"276","author":"Otwinowski","year":"1997","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.biochi.2017.07.009_bib37","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J.\u00a0Appl. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib38","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib39","doi-asserted-by":"crossref","first-page":"905","DOI":"10.1107\/S0907444998003254","article-title":"Crystallography & NMR system: a new software suite for macromolecular structure determination","volume":"54","author":"Br\u00fcnger","year":"1998","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib40","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","article-title":"Towards automated crystallographic structure refinement with phenix.refine","volume":"68","author":"Afonine","year":"2012","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib41","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1107\/S0907444913000462","article-title":"Bulk-solvent and overall scaling revisited: faster calculations, improved results","volume":"69","author":"Afonine","year":"2013","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib42","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.jsb.2009.04.003","article-title":"Comparative structural studies on Lys49-phospholipases A2 from Bothrops genus reveal their myotoxic site","volume":"167","author":"dos Santos","year":"2009","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.biochi.2017.07.009_bib43","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.biochi.2004.11.005","article-title":"Structural insights for fatty acid binding in a Lys49-phospholipase A2: crystal structure of myotoxin II from Bothropsmoojeni complexed with stearic acid","volume":"87","author":"Watanabe","year":"2005","journal-title":"Biochimie"},{"key":"10.1016\/j.biochi.2017.07.009_bib44","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.toxicon.2013.06.013","article-title":"Structural and functional studies with mycotoxin II from Bothropsmoojeni reveal remarkable similarities and differences compared to other catalytically inactive phospholipases A2-like","volume":"72","author":"Salvador","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2017.07.009_bib45","doi-asserted-by":"crossref","first-page":"2066","DOI":"10.1107\/S1399004715014443","article-title":"Structural and functional evidence for membrane docking and disruption sites on phospholipase A2-like proteins revealed by complexation with the inhibitor suramin","volume":"71","author":"Salvador","year":"2015","journal-title":"Acta Crystallogr. Sect. D."},{"key":"10.1016\/j.biochi.2017.07.009_bib46","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1186\/1758-2946-5-39","article-title":"MOLE 2.0: advanced approach for analysis of biomacromolecular channels","volume":"5","author":"Sehnal","year":"2013","journal-title":"J.\u00a0Cheminformatics"},{"key":"10.1016\/j.biochi.2017.07.009_bib47","doi-asserted-by":"crossref","first-page":"3199","DOI":"10.1016\/j.bbagen.2016.08.003","article-title":"Functional and structural studies of a Phospholipase A2-like protein complexed to zinc ions: insights on its myotoxicity and inhibition mechanism","volume":"1861","author":"Borges","year":"2017","journal-title":"Biochim. Biophys. Acta - Gen. Subj."},{"key":"10.1016\/j.biochi.2017.07.009_bib48","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.\u00a0Mol. Biol."},{"key":"10.1016\/j.biochi.2017.07.009_bib49","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.toxicon.2006.10.011","article-title":"Interfacial surface charge and free accessibility to the PLA2-active site-like region are essential requirements for the activity of Lys49 PLA2 homologues","volume":"49","author":"Murakami","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.biochi.2017.07.009_bib50","doi-asserted-by":"crossref","first-page":"s226","DOI":"10.1107\/S2053273316096558","article-title":"PLA2s-like membrane perturbation mechanism: extracting the most of crystallography data","volume":"72","author":"Borges","year":"2016","journal-title":"Acta Crystallogr. Sect. A Found. Adv."},{"key":"10.1016\/j.biochi.2017.07.009_bib51","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1021\/bi0010470","article-title":"Structural basis for low catalytic activity in Lys49 phospholipases A2-A hypothesis: the crystal structure of piratoxin II complexed to fatty acid","volume":"40","author":"Lee","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2017.07.009_bib52","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. Sect. D. Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2017.07.009_bib53","series-title":"LigPlot\u00a0+: Multiple Ligand \u00c0 Protein Interaction Diagrams for Drug Discovery","first-page":"2778","author":"Laskowski","year":"2011"},{"key":"10.1016\/j.biochi.2017.07.009_bib54","doi-asserted-by":"crossref","first-page":"10037","DOI":"10.1073\/pnas.181342398","article-title":"Electrostatics of nanosystems: application to microtubules and the ribosome","volume":"98","author":"Baker","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2017.07.009_bib55","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera - a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.biochi.2017.07.009_bib56","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1093\/nar\/gkh381","article-title":"PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations","volume":"32","author":"Dolinsky","year":"2004","journal-title":"Nucleic Acids Res."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908417301803?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908417301803?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:08:13Z","timestamp":1759540093000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908417301803"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,11]]},"references-count":56,"alternative-id":["S0300908417301803"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2017.07.009","relation":{},"ISSN":["0300-9084"],"issn-type":[{"type":"print","value":"0300-9084"}],"subject":[],"published":{"date-parts":[[2017,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural studies with BnSP-7 reveal an atypical oligomeric conformation compared to phospholipases A2-like toxins","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2017.07.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM).","name":"copyright","label":"Copyright"}]}}