{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T07:24:47Z","timestamp":1790061887206,"version":"4.0.1"},"reference-count":128,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2020,12,1]],"date-time":"2020-12-01T00:00:00Z","timestamp":1606780800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100000288","name":"Royal Society","doi-asserted-by":"publisher","award":["NA 150195"],"award-info":[{"award-number":["NA 150195"]}],"id":[{"id":"10.13039\/501100000288","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"}]},{"DOI":"10.13039\/501100003105","name":"Universidade Federal de Uberl\u00e2ndia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003105","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004901","name":"Funda\u00e7\u00e3o de Amparo \u00e0 Pesquisa do Estado de Minas Gerais","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004901","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1016\/j.ijbiomac.2020.07.178","type":"journal-article","created":{"date-parts":[[2020,7,19]],"date-time":"2020-07-19T01:31:13Z","timestamp":1595122273000},"page":"616-625","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":30,"special_numbering":"C","title":["Insights into the antiviral activity of phospholipases A2 (PLA2s) from snake venoms"],"prefix":"10.1016","volume":"164","author":[{"given":"S.C.","family":"Teixeira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B.C.","family":"Borges","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.Q.","family":"Oliveira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L.S.","family":"Carregosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L.A.","family":"Bastos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"I.A.","family":"Santos","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.C.G.","family":"Jardim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"F.F.","family":"Melo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"L.M.","family":"Freitas","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V.M.","family":"Rodrigues","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D.S.","family":"Lopes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0005","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1097\/MOP.0000000000000303","article-title":"Enteroviruses in the early 21st century: new manifestations and challenges","volume":"28","author":"Lugo","year":"2016","journal-title":"Curr. Opin. Pediatr."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0010","first-page":"2","article-title":"Human papillomavirus (HPV), HPV-related disease, and the HPV vaccine","volume":"1","author":"Braaten","year":"2008","journal-title":"Rev. Obstet. Gynecol."},{"issue":"5","key":"10.1016\/j.ijbiomac.2020.07.178_bb0015","doi-asserted-by":"crossref","first-page":"729","DOI":"10.1097\/QAD.0b013e32833433fe","article-title":"Examining the promise of HIV elimination by \u2018test and treat\u2019 in hyperendemic settings","volume":"24","author":"Dodd","year":"2010","journal-title":"AIDS (London, England)"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0020","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1146\/annurev.med.59.061606.095540","article-title":"Herpes simplex: insights on pathogenesis and possible vaccines","volume":"59","author":"Koelle","year":"2008","journal-title":"Annu. Rev. Med."},{"issue":"7563","key":"10.1016\/j.ijbiomac.2020.07.178_bb0025","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1038\/nature14594","article-title":"Temporal and spatial analysis of the 2014\u20132015 Ebola virus outbreak in West Africa","volume":"524","author":"Carroll","year":"2015","journal-title":"Nature"},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0030","doi-asserted-by":"crossref","first-page":"116","DOI":"10.3855\/jidc.8217","article-title":"Zika virus outbreak in Brazil","volume":"10","author":"Heukelbach","year":"2016","journal-title":"Journal of infection in developing countries"},{"issue":"7249","key":"10.1016\/j.ijbiomac.2020.07.178_bb0035","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1038\/nature08157","article-title":"Emergence and pandemic potential of swine-origin H1N1 influenza virus","volume":"459","author":"Neumann","year":"2009","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0040","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1007\/s11908-017-0566-9","article-title":"Live attenuated yellow fever 17D vaccine: a legacy vaccine still controlling outbreaks in modern day","volume":"19","author":"Collins","year":"2017","journal-title":"Curr. Infect. Dis. Rep."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0045","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.ijid.2020.03.004","article-title":"The SARS-CoV-2 outbreak: what we know","volume":"94","author":"Wu","year":"2020","journal-title":"Int. J. Infect. Dis."},{"issue":"101","key":"10.1016\/j.ijbiomac.2020.07.178_bb0050","doi-asserted-by":"crossref","DOI":"10.1098\/rsif.2014.0950","article-title":"Global rise in human infectious disease outbreaks","volume":"11","author":"Smith","year":"2014","journal-title":"J. R. Soc. Interface"},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0055","doi-asserted-by":"crossref","first-page":"80","DOI":"10.1007\/s10393-007-0149-6","article-title":"Viral host jumps: moving toward a predictive framework","volume":"5","author":"Pulliam","year":"2008","journal-title":"EcoHealth"},{"issue":"7700","key":"10.1016\/j.ijbiomac.2020.07.178_bb0060","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1038\/s41586-018-0012-7","article-title":"The evolutionary history of vertebrate RNA viruses","volume":"556","author":"Shi","year":"2018","journal-title":"Nature"},{"issue":"12 Suppl","key":"10.1016\/j.ijbiomac.2020.07.178_bb0065","doi-asserted-by":"crossref","first-page":"S82","DOI":"10.1038\/nm1141","article-title":"Influenza: old and new threats","volume":"10","author":"Palese","year":"2004","journal-title":"Nat. Med."},{"issue":"5","key":"10.1016\/j.ijbiomac.2020.07.178_bb0070","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1002\/biot.201400393","article-title":"Emerging influenza viruses and the prospect of a universal influenza virus vaccine","volume":"10","author":"Krammer","year":"2015","journal-title":"Biotechnol. J."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0075","series-title":"Prediction of Number of Cases of 2019 Novel Coronavirus (COVID-19) Using Social Media Search Index","volume":"vol. 17","author":"Qin","year":"2020"},{"issue":"7446","key":"10.1016\/j.ijbiomac.2020.07.178_bb0080","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1038\/nature12060","article-title":"The global distribution and burden of dengue","volume":"496","author":"Bhatt","year":"2013","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0085","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1053\/rvsc.2001.0462","article-title":"Subversion and piracy: DNA viruses and immune evasion","volume":"70","author":"Haig","year":"2001","journal-title":"Res. Vet. Sci."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0090","first-page":"367","author":"Ryu","year":"2017","journal-title":"Antivir. Ther."},{"issue":"9","key":"10.1016\/j.ijbiomac.2020.07.178_bb0095","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1001121","article-title":"Ebolavirus is internalized into host cells via macropinocytosis in a viral glycoprotein-dependent manner","volume":"6","author":"Nanbo","year":"2010","journal-title":"PLoS Pathog."},{"issue":"1\u20134","key":"10.1016\/j.ijbiomac.2020.07.178_bb0100","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1007\/s00709-010-0152-6","article-title":"Mechanisms of viral entry: sneaking in the front door","volume":"244","author":"Thorley","year":"2010","journal-title":"Protoplasma"},{"issue":"Suppl. 3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0105","doi-asserted-by":"crossref","first-page":"S957","DOI":"10.1093\/infdis\/jir326","article-title":"Ebola virus enters host cells by macropinocytosis and clathrin-mediated endocytosis","volume":"204","author":"Aleksandrowicz","year":"2011","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0110","series-title":"Introduction to Viral Structure, Diversity and Biology","first-page":"1","author":"Marintcheva","year":"2018"},{"issue":"16","key":"10.1016\/j.ijbiomac.2020.07.178_bb0115","doi-asserted-by":"crossref","first-page":"2773","DOI":"10.1007\/s00018-010-0357-z","article-title":"Dengue virus life cycle: viral and host factors modulating infectivity","volume":"67","author":"Rodenhuis-Zybert","year":"2010","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0120","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.coi.2014.01.009","article-title":"Challenges and responses in human vaccine development","volume":"28","author":"Kaufmann","year":"2014","journal-title":"Curr. Opin. Immunol."},{"issue":"12","key":"10.1016\/j.ijbiomac.2020.07.178_bb0125","doi-asserted-by":"crossref","first-page":"e1266","DOI":"10.1016\/S2214-109X(18)30418-2","article-title":"The cost and challenge of vaccine development for emerging and emergent infectious diseases","volume":"6","author":"Maslow","year":"2018","journal-title":"Lancet Glob. Health"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0130","doi-asserted-by":"crossref","first-page":"1207","DOI":"10.3389\/fphar.2019.01207","article-title":"The signaling pathways, and therapeutic targets of antiviral agents: focusing on the antiviral approaches and clinical perspectives of anthocyanins in the management of viral diseases","volume":"10","author":"Mohammadi Pour","year":"2019","journal-title":"Front. Pharmacol."},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0135","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.3000003","article-title":"Why are RNA virus mutation rates so damn high?","volume":"16","author":"Duffy","year":"2018","journal-title":"PLoS Biol."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0140","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-4939-8976-8_1","article-title":"Overview of direct-acting antiviral drugs and drug resistance of hepatitis C virus","volume":"1911","author":"Li","year":"2019","journal-title":"Methods in molecular biology (Clifton, N.J.)"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0145","article-title":"Influenza polymerase inhibitors: mechanisms of action and resistance","author":"Takashita","year":"2020","journal-title":"Cold Spring Harbor perspectives in medicine"},{"issue":"9239","key":"10.1016\/j.ijbiomac.2020.07.178_bb0150","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1016\/S0140-6736(00)02854-3","article-title":"Adverse effects of antiretroviral therapy","volume":"356","author":"Carr","year":"2000","journal-title":"Lancet (London, England)"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0155","doi-asserted-by":"crossref","first-page":"283","DOI":"10.7326\/0003-4819-115-4-283","article-title":"Fulminant hepatic failure associated with 2\u2032,3\u2032-dideoxyinosine (ddI)","volume":"115","author":"Lai","year":"1991","journal-title":"Ann. Intern. Med."},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0160","first-page":"229","article-title":"Adverse effects of antiretroviral therapy for HIV infection","volume":"170","author":"Montessori","year":"2004","journal-title":"Can. Med. Assoc. J."},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0165","doi-asserted-by":"crossref","first-page":"303","DOI":"10.3390\/metabo2020303","article-title":"A historical overview of natural products in drug discovery","volume":"2","author":"Dias","year":"2012","journal-title":"Metabolites"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0170","series-title":"Natural Products in Drug Discovery: Impacts and Opportunities \u2014 An Assessment","first-page":"1","author":"Brahmachari","year":"2011"},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0175","doi-asserted-by":"crossref","DOI":"10.3390\/toxins11100564","article-title":"Snake venoms in drug discovery: valuable therapeutic tools for life saving","volume":"11","author":"Mohamed Abd El-Aziz","year":"2019","journal-title":"Toxins"},{"issue":"4\u20135","key":"10.1016\/j.ijbiomac.2020.07.178_bb0180","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1159\/000092430","article-title":"The use of snake venom-derived compounds for new functional diagnostic test kits in the field of haemostasis","volume":"34","author":"Schoni","year":"2005","journal-title":"Pathophysiol. Haemost. Thromb."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0185","doi-asserted-by":"crossref","first-page":"154","DOI":"10.7150\/thno\/v01p0154","article-title":"Integrin targeted therapeutics","volume":"1","author":"Millard","year":"2011","journal-title":"Theranostics"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0190","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.toxicon.2011.03.017","article-title":"From snake venom toxins to therapeutics\u2014cardiovascular examples","volume":"59","author":"Koh","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0195","series-title":"Antitumoral Activity of Snake Venom Proteins: New Trends in Cancer Therapy","first-page":"203639","volume":"vol. 2014","author":"Calderon","year":"2014"},{"issue":"22","key":"10.1016\/j.ijbiomac.2020.07.178_bb0200","doi-asserted-by":"crossref","first-page":"4033","DOI":"10.1021\/bi00798a004","article-title":"Angiotensin-converting enzyme inhibitors from the venom of Bothrops jararaca. Isolation, elucidation of structure, and synthesis","volume":"10","author":"Ondetti","year":"1971","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0205","doi-asserted-by":"crossref","first-page":"589","DOI":"10.1161\/01.HYP.17.4.589","article-title":"History of the design of captopril and related inhibitors of angiotensin converting enzyme","volume":"17","author":"Cushman","year":"1991","journal-title":"Hypertension (Dallas, Tex.: 1979)"},{"issue":"15","key":"10.1016\/j.ijbiomac.2020.07.178_bb0210","doi-asserted-by":"crossref","first-page":"9359","DOI":"10.1016\/S0021-9258(18)92826-7","article-title":"Barbourin. A GPIIb-IIIa-specific integrin antagonist from the venom of Sistrurus m. barbouri","volume":"266","author":"Scarborough","year":"1991","journal-title":"J. Biol. Chem."},{"issue":"36","key":"10.1016\/j.ijbiomac.2020.07.178_bb0215","doi-asserted-by":"crossref","first-page":"19827","DOI":"10.1016\/S0021-9258(19)77710-2","article-title":"Echistatin. A potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus","volume":"263","author":"Gan","year":"1988","journal-title":"J. Biol. Chem."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0220","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1111\/j.1365-2141.1971.tb03415.x","article-title":"Reptilase-R\u2014a new reagent in blood coagulation","volume":"21","author":"Funk","year":"1971","journal-title":"Br. J. Haematol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0225","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/S0021-9150(00)00628-6","article-title":"Defibrinogenating effect of batroxobin (Defibrase) in rats and inhibition of migration of human vascular smooth muscle cells by the plasma of batroxobin-treated rats in vitro","volume":"156","author":"Wang","year":"2001","journal-title":"Atherosclerosis"},{"issue":"7","key":"10.1016\/j.ijbiomac.2020.07.178_bb0230","doi-asserted-by":"crossref","first-page":"1251","DOI":"10.1016\/j.toxicon.2012.08.017","article-title":"Isolation and characterization of moojenin, an acid-active, anticoagulant metalloproteinase from Bothrops moojeni venom","volume":"60","author":"de Morais","year":"2012","journal-title":"Toxicon"},{"issue":"Suppl. 3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0235","first-page":"S77","article-title":"Aulogous fibrin sealant (Vivostat((R))) in the neurosurgical practice: part II: vertebro-spinal procedures","volume":"7","author":"Graziano","year":"2016","journal-title":"Surg. Neurol. Int."},{"issue":"17","key":"10.1016\/j.ijbiomac.2020.07.178_bb0240","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.2174\/0929867324666170605091546","article-title":"Snake venom: from deadly toxins to life-saving therapeutics","volume":"24","author":"Waheed","year":"2017","journal-title":"Curr. Med. Chem."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0245","doi-asserted-by":"crossref","first-page":"28","DOI":"10.1046\/j.1442-2026.2001.00174.x","article-title":"Venom as a source of useful biologically active molecules","volume":"13","author":"Bailey","year":"2001","journal-title":"Emergency medicine (Fremantle, W.A.)"},{"issue":"21","key":"10.1016\/j.ijbiomac.2020.07.178_bb0250","doi-asserted-by":"crossref","first-page":"1868","DOI":"10.2174\/156802661921191024114842","article-title":"Toxins of animal venoms and inhibitors: molecular and biotechnological tools useful to human and animal health","volume":"19","author":"Soares","year":"2019","journal-title":"Curr. Top. Med. Chem."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0255","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1186\/s40409-016-0089-0","article-title":"Antiviral activity of animal venom peptides and related compounds","volume":"23","author":"da Mata","year":"2017","journal-title":"The journal of venomous animals and toxins including tropical diseases"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0260","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1186\/1742-6405-6-25","article-title":"Hypothesis of snake and insect venoms against human immunodeficiency virus: a review","volume":"6","author":"Meenakshisundaram","year":"2009","journal-title":"AIDS Res. Ther."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0265","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."},{"issue":"Suppl. 1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0270","doi-asserted-by":"crossref","first-page":"S177","DOI":"10.1134\/S0006297920140096","article-title":"Phospholipase superfamily: structure, functions, and biotechnological applications","volume":"85","author":"Filkin","year":"2020","journal-title":"Biochemistry. Biokhimiia"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0275","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1007\/978-1-61779-600-5_4","article-title":"Phospholipases: an overview","volume":"861","author":"Aloulou","year":"2012","journal-title":"Methods in molecular biology (Clifton, N.J.)"},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0280","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1016\/0041-0101(96)00036-0","article-title":"Phospholipase A2\u2014a structural review","volume":"34","author":"Arni","year":"1996","journal-title":"Toxicon"},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0285","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"},{"issue":"5\u20136","key":"10.1016\/j.ijbiomac.2020.07.178_bb0290","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/S0090-6980(99)00041-6","article-title":"Insight into prostaglandin, leukotriene, and other eicosanoid functions using mice with targeted gene disruptions","volume":"58","author":"Austin","year":"1999","journal-title":"Prostaglandins & other lipid mediators"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0295","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.toxicon.2012.09.006","article-title":"Phospholipases A2: unveiling the secrets of a functionally versatile group of snake venom toxins","volume":"62","author":"Gutierrez","year":"2013","journal-title":"Toxicon"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0300","doi-asserted-by":"crossref","first-page":"824","DOI":"10.1016\/j.bbagen.2016.12.022","article-title":"Minor snake venom proteins: structure, function and potential applications","volume":"1861","author":"Boldrini-Franca","year":"2017","journal-title":"Biochim. Biophys. Acta, Gen. Subj."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0305","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.jprot.2016.06.029","article-title":"An in-depth snake venom proteopeptidome characterization: benchmarking Bothrops jararaca","volume":"151","author":"Nicolau","year":"2017","journal-title":"J. Proteome"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0310","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/j.actatropica.2019.02.030","article-title":"Proteomic profiling, functional characterization, and immunoneutralization of the venom of Porthidium porrasi, a pitviper endemic to Costa Rica","volume":"193","author":"Mendez","year":"2019","journal-title":"Acta Trop."},{"issue":"11","key":"10.1016\/j.ijbiomac.2020.07.178_bb0315","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"},{"issue":"1\u20132","key":"10.1016\/j.ijbiomac.2020.07.178_bb0320","first-page":"1","article-title":"The expanding superfamily of phospholipase A(2) enzymes: classification and characterization","volume":"1488","author":"Six","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"issue":"22","key":"10.1016\/j.ijbiomac.2020.07.178_bb0325","doi-asserted-by":"crossref","first-page":"13839","DOI":"10.1016\/S0021-9258(18)89822-2","article-title":"A new class of phospholipases A2 with lysine in place of aspartate 49. Functional consequences for calcium and substrate binding","volume":"259","author":"Maraganore","year":"1984","journal-title":"J. Biol. Chem."},{"issue":"7","key":"10.1016\/j.ijbiomac.2020.07.178_bb0330","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1016\/j.toxicon.2008.12.014","article-title":"Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper","volume":"54","author":"Angulo","year":"2009","journal-title":"Toxicon"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0335","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/j.toxicon.2012.02.007","article-title":"Snake venom Lys49 myotoxins: from phospholipases A(2) to non-enzymatic membrane disruptors","volume":"60","author":"Lomonte","year":"2012","journal-title":"Toxicon"},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0340","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.bbagen.2005.11.022","article-title":"N49 phospholipase A2, a unique subgroup of snake venom group II phospholipase A2","volume":"1760","author":"Wei","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"issue":"Pt 3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0345","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1042\/bj3190961","volume":"319","author":"Polgar","year":"1996","journal-title":"The Biochemical journal"},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0350","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/S0041-0101(98)00188-3","article-title":"Lysine 49 phospholipase A2 proteins","volume":"37","author":"Ownby","year":"1999","journal-title":"Toxicon"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0355","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1111\/j.1399-3011.1989.tb01575.x","article-title":"A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides","volume":"34","author":"Kini","year":"1989","journal-title":"Int. J. Pept. Protein Res."},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0360","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 A(2) from Agkistrodon piscivorus piscivorus snake venom: synthetic C-terminal peptides from Lys49, but not from Asp49 myotoxins, exert membrane-damaging activities","volume":"39","author":"Nunez","year":"2001","journal-title":"Toxicon"},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0365","doi-asserted-by":"crossref","first-page":"7326","DOI":"10.1074\/jbc.M410588200","article-title":"A molecular mechanism for Lys49-phospholipase A2 activity based on ligand-induced conformational change","volume":"280","author":"Ambrosio","year":"2005","journal-title":"J. Biol. Chem."},{"issue":"28","key":"10.1016\/j.ijbiomac.2020.07.178_bb0370","doi-asserted-by":"crossref","first-page":"3224","DOI":"10.2174\/138161210793292456","article-title":"Synthetic peptides derived from the C-terminal region of Lys49 phospholipase A2 homologues from viperidae snake venoms: biomimetic activities and potential applications","volume":"16","author":"Lomonte","year":"2010","journal-title":"Curr. Pharm. Des."},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0375","doi-asserted-by":"crossref","first-page":"5534","DOI":"10.1074\/jbc.270.10.5534","article-title":"Structural elements of secretory phospholipases A2 involved in the binding to M-type receptors","volume":"270","author":"Lambeau","year":"1995","journal-title":"J. Biol. Chem."},{"issue":"12","key":"10.1016\/j.ijbiomac.2020.07.178_bb0380","doi-asserted-by":"crossref","first-page":"1475","DOI":"10.1517\/13543784.14.12.1475","article-title":"Targeting integrins for the control of tumour angiogenesis","volume":"14","author":"Akalu","year":"2005","journal-title":"Expert Opin. Investig. Drugs"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0385","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.ijbiomac.2018.09.053","article-title":"Antitumor potential of Pllans-II, an acidic Asp49-PLA2 from Porthidium lansbergii lansbergii snake venom on human cervical carcinoma HeLa cells","volume":"122","author":"Jimenez-Charris","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0390","doi-asserted-by":"crossref","first-page":"10619","DOI":"10.1038\/s41598-018-28846-4","article-title":"Cell surface nucleolin interacts with and internalizes Bothrops asper Lys49 phospholipase A2 and mediates its toxic activity","volume":"8","author":"Massimino","year":"2018","journal-title":"Sci. Rep."},{"issue":"6","key":"10.1016\/j.ijbiomac.2020.07.178_bb0395","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"},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0400","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1111\/bcpt.12921","article-title":"Identification of the molecular determinants of the antibacterial activity of LmutTX, a Lys49 phospholipase A2 homologue isolated from Lachesis muta muta snake venom (Linnaeus, 1766)","volume":"122","author":"Diniz-Sousa","year":"2018","journal-title":"Basic Clin. Pharmacol. Toxicol."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0405","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1186\/s40409-015-0044-5","article-title":"Antitumor potential of the myotoxin BthTX-I from Bothrops jararacussu snake venom: evaluation of cell cycle alterations and death mechanisms induced in tumor cell lines","volume":"21","author":"Prinholato da Silva","year":"2015","journal-title":"The journal of venomous animals and toxins including tropical diseases"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0410","doi-asserted-by":"crossref","first-page":"671","DOI":"10.1016\/j.ijbiomac.2015.10.080","article-title":"Human breast cancer cell death induced by BnSP-6, a Lys-49 PLA(2) homologue from Bothrops pauloensis venom","volume":"82","author":"Azevedo","year":"2016","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0415","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.ijbiomac.2019.05.164","article-title":"Antitumor and antimetastatic effects of PLA2-BthTX-II from Bothrops jararacussu venom on human breast cancer cells","volume":"135","author":"de Vasconcelos Azevedo","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0420","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.matbio.2009.03.007","article-title":"MVL-PLA2, a phospholipase A2 from Macrovipera lebetina transmediterranea venom, inhibits tumor cells adhesion and migration","volume":"28","author":"Bazaa","year":"2009","journal-title":"Matrix Biol."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0425","doi-asserted-by":"crossref","unstructured":"D.C. Nunes, M.M. Figueira, D.S. Lopes, D.L. De Souza, L.F. Izidoro, E.A. Ferro, M.A. Souza, R.S. Rodrigues, V.M. Rodrigues, K.A. Yoneyama, BnSP-7 toxin, a basic phospholipase A2 from Bothrops pauloensis snake venom, interferes with proliferation, ultrastructure and infectivity of Leishmania (Leishmania) amazonensis, Parasitology 140(7) (2013) 844\u201354.","DOI":"10.1017\/S0031182013000012"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0430","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.toxicon.2016.05.010","article-title":"Anti-parasitic effect on Toxoplasma gondii induced by BnSP-7, a Lys49-phospholipase A2 homologue from Bothrops pauloensis venom","volume":"119","author":"Borges","year":"2016","journal-title":"Toxicon"},{"issue":"22","key":"10.1016\/j.ijbiomac.2020.07.178_bb0435","doi-asserted-by":"crossref","first-page":"2032","DOI":"10.2174\/1568026619666190723152520","article-title":"The anthelmintic effect on Strongyloides venezuelensis induced by BnSP- 6, a Lys49-phospholipase A2 homologue from Bothrops pauloensis venom","volume":"19","author":"Rodrigues","year":"2019","journal-title":"Curr. Top. Med. Chem."},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0440","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.toxicon.2011.05.021","article-title":"Crotoxin and phospholipases A(2) from Crotalus durissus terrificus showed antiviral activity against dengue and yellow fever viruses","volume":"59","author":"Muller","year":"2012","journal-title":"Toxicon"},{"issue":"11","key":"10.1016\/j.ijbiomac.2020.07.178_bb0445","doi-asserted-by":"crossref","first-page":"e112351","DOI":"10.1371\/journal.pone.0112351","article-title":"Phospholipase A2 isolated from the venom of Crotalus durissus terrificus inactivates dengue virus and other enveloped viruses by disrupting the viral envelope","volume":"9","author":"Muller","year":"2014","journal-title":"PLoS One"},{"issue":"11","key":"10.1016\/j.ijbiomac.2020.07.178_bb0450","doi-asserted-by":"crossref","first-page":"e0187857","DOI":"10.1371\/journal.pone.0187857","article-title":"Multiple effects of toxins isolated from Crotalus durissus terrificus on the hepatitis C virus life cycle","volume":"12","author":"Shimizu","year":"2017","journal-title":"PLoS One"},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0455","doi-asserted-by":"crossref","first-page":"1780","DOI":"10.3390\/toxins5101780","article-title":"Molecular characterization of Lys49 and Asp49 phospholipases A\u2082 from snake venom and their antiviral activities against dengue virus","volume":"5","author":"Cecilio","year":"2013","journal-title":"Toxins"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0460","doi-asserted-by":"crossref","first-page":"48","DOI":"10.1016\/j.biologicals.2019.12.002","article-title":"Potent virucidal activity against Flaviviridae of a group IIA phospholipase A(2) isolated from the venom of Bothrops asper","volume":"63","author":"Brenes","year":"2020","journal-title":"Biologicals"},{"issue":"6","key":"10.1016\/j.ijbiomac.2020.07.178_bb0465","doi-asserted-by":"crossref","first-page":"875","DOI":"10.1016\/0041-0101(81)90085-4","article-title":"Convulxin, a new toxin from the venom of the South American rattlesnake Crotalus durissus terrificus","volume":"19","author":"Prado-Franceschi","year":"1981","journal-title":"Toxicon"},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0470","doi-asserted-by":"crossref","first-page":"953","DOI":"10.1016\/0041-0101(88)90260-7","article-title":"Gyroxin, a toxin from the venom of Crotalus durissus terrificus, is a thrombin-like enzyme","volume":"26","author":"Alexander","year":"1988","journal-title":"Toxicon"},{"issue":"7","key":"10.1016\/j.ijbiomac.2020.07.178_bb0475","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. U. S. A."},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0480","doi-asserted-by":"crossref","first-page":"274","DOI":"10.1007\/BF00997027","article-title":"Biochemistry and pharmacology of the crotoxin complex. I. Subfractionation and recombination of the crotoxin complex","volume":"270","author":"Rubsamen","year":"1971","journal-title":"Naunyn-Schmiedebergs Archiv fur Pharmakologie"},{"issue":"19","key":"10.1016\/j.ijbiomac.2020.07.178_bb0485","first-page":"749","article-title":"Fosfolipasas A2 segregadas (sPLA2):\u00bfamigas o enemigas? \u00bfActores de la resistencia antibacteriana y antivirus de la inmunodeficiencia humana?","volume":"123","author":"Villarrubia","year":"2004","journal-title":"Med. Clin."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0490","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1007\/BF01024915","article-title":"Bothropstoxin-I: amino acid sequence and function","volume":"12","author":"Cintra","year":"1993","journal-title":"J. Protein Chem."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0495","series-title":"Expression, Purification and Virucidal Activity of Two Recombinant Isoforms of Phospholipase A2 From Crotalus durissus terrificus Venom","first-page":"1159","volume":"vol. 164","author":"Russo","year":"2019"},{"issue":"7","key":"10.1016\/j.ijbiomac.2020.07.178_bb0500","doi-asserted-by":"crossref","first-page":"482","DOI":"10.1038\/nrmicro3046","article-title":"The molecular and structural basis of advanced antiviral therapy for hepatitis C virus infection","volume":"11","author":"Bartenschlager","year":"2013","journal-title":"Nat. Rev. Microbiol."},{"issue":"16","key":"10.1016\/j.ijbiomac.2020.07.178_bb0505","doi-asserted-by":"crossref","first-page":"7964","DOI":"10.1128\/JVI.00826-08","article-title":"Interaction of hepatitis C virus nonstructural protein 5A with core protein is critical for the production of infectious virus particles","volume":"82","author":"Masaki","year":"2008","journal-title":"J. Virol."},{"issue":"3","key":"10.1016\/j.ijbiomac.2020.07.178_bb0510","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.biochi.2006.10.010","article-title":"Purification and partial characterization of two phospholipases A2 from Bothrops leucurus (white-tailed-jararaca) snake venom","volume":"89","author":"Higuchi","year":"2007","journal-title":"Biochimie"},{"issue":"6","key":"10.1016\/j.ijbiomac.2020.07.178_bb0515","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.toxicon.2006.06.021","article-title":"Discovery of novel [Arg49]phospholipase A2 isozymes from Protobothrops elegans venom and regional evolution of Crotalinae snake venom phospholipase A2 isozymes in the southwestern islands of Japan and Taiwan","volume":"48","author":"Chijiwa","year":"2006","journal-title":"Toxicon"},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0520","doi-asserted-by":"crossref","first-page":"3556","DOI":"10.1021\/pr800332p","article-title":"Snake venomics of the lancehead pitviper Bothrops asper: geographic, individual, and ontogenetic variations","volume":"7","author":"Alape-Giron","year":"2008","journal-title":"J. Proteome Res."},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0525","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1046\/j.1432-1327.1998.2530452.x","article-title":"Bactericidal activity of Lys49 and Asp49 myotoxic phospholipases A2 from Bothrops asper snake venom\u2014synthetic Lys49 myotoxin II-(115-129)-peptide identifies its bactericidal region","volume":"253","author":"Paramo","year":"1998","journal-title":"Eur. J. Biochem."},{"issue":"9","key":"10.1016\/j.ijbiomac.2020.07.178_bb0530","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.1021\/cr990139w","article-title":"Interfacial enzymology: the secreted phospholipase A(2)-paradigm","volume":"101","author":"Berg","year":"2001","journal-title":"Chem. Rev."},{"issue":"5","key":"10.1016\/j.ijbiomac.2020.07.178_bb0535","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1172\/JCI6915","article-title":"Secreted phospholipases A(2), a new class of HIV inhibitors that block virus entry into host cells","volume":"104","author":"Fenard","year":"1999","journal-title":"J. Clin. Invest."},{"issue":"19","key":"10.1016\/j.ijbiomac.2020.07.178_bb0540","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."},{"issue":"11","key":"10.1016\/j.ijbiomac.2020.07.178_bb0545","doi-asserted-by":"crossref","first-page":"7043","DOI":"10.1074\/jbc.274.11.7043","article-title":"Both group IB and group IIA secreted phospholipases A2 are natural ligands of the mouse 180-kDa M-type receptor","volume":"274","author":"Cupillard","year":"1999","journal-title":"J. Biol. Chem."},{"issue":"22","key":"10.1016\/j.ijbiomac.2020.07.178_bb0550","doi-asserted-by":"crossref","first-page":"13289","DOI":"10.1016\/S0021-9258(18)51627-6","article-title":"Nigexine, a phospholipase A2 from cobra venom with cytotoxic properties not related to esterase activity. Purification, amino acid sequence, and biological properties","volume":"264","author":"Chwetzoff","year":"1989","journal-title":"J. Biol. Chem."},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0555","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/S0165-6147(99)01300-0","article-title":"Receptors for a growing family of secreted phospholipases A2","volume":"20","author":"Lambeau","year":"1999","journal-title":"Trends Pharmacol. Sci."},{"issue":"1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0560","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/0005-2795(77)90275-6","article-title":"Naja mossambica mossambica venom. Purification, some properties and the amino acid sequences of three phospholipases A (CM-I, CM-II and CM-III)","volume":"493","author":"Joubert","year":"1977","journal-title":"Biochim. Biophys. Acta"},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0565","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1016\/0041-0101(93)90401-4","article-title":"Purification and activation of phospholipase A2 isoforms from Naja mossambica mossambica (spitting cobra) venom","volume":"31","author":"Ahmad","year":"1993","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0570","series-title":"Broad-spectrum Antiviral Agents: Secreted Phospholipase A(2) Targets Viral Envelope Lipid Bilayers Derived From the Endoplasmic Reticulum Membrane","first-page":"15931","volume":"vol. 7","author":"Chen","year":"2017"},{"issue":"8","key":"10.1016\/j.ijbiomac.2020.07.178_bb0575","doi-asserted-by":"crossref","first-page":"2811","DOI":"10.1021\/bi047727a","article-title":"Phospholipase A2 hydrolysis of supported phospholipid bilayers: a neutron reflectivity and ellipsometry study","volume":"44","author":"Vacklin","year":"2005","journal-title":"Biochemistry"},{"issue":"Pt 1","key":"10.1016\/j.ijbiomac.2020.07.178_bb0580","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1242\/jcs.071233","article-title":"Lipid map of the mammalian cell","volume":"124","author":"van Meer","year":"2011","journal-title":"J. Cell Sci."},{"issue":"45","key":"10.1016\/j.ijbiomac.2020.07.178_bb0585","doi-asserted-by":"crossref","first-page":"6852","DOI":"10.1021\/acs.biochem.5b00718","article-title":"Modeling yeast organelle membranes and how lipid diversity influences bilayer properties","volume":"54","author":"Monje-Galvan","year":"2015","journal-title":"Biochemistry"},{"issue":"48","key":"10.1016\/j.ijbiomac.2020.07.178_bb0590","doi-asserted-by":"crossref","first-page":"40525","DOI":"10.1074\/jbc.M112.384446","article-title":"The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during dengue maturation","volume":"287","author":"Zhang","year":"2012","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0595","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"10.1016\/j.ijbiomac.2020.07.178_bb0600","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1186\/1745-6150-4-16","article-title":"A four-column theory for the origin of the genetic code: tracing the evolutionary pathways that gave rise to an optimized code","volume":"4","author":"Higgs","year":"2009","journal-title":"Biol. Direct"},{"issue":"47","key":"10.1016\/j.ijbiomac.2020.07.178_bb0605","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 and cytolytic toxin region by the use of synthetic peptides and molecular modeling","volume":"269","author":"Lomonte","year":"1994","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2020.07.178_bb0610","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.jsb.2009.04.003","article-title":"Comparative structural studies on Lys49-phospholipases A(2) from Bothrops genus reveal their myotoxic site","volume":"167","author":"dos Santos","year":"2009","journal-title":"J. Struct. Biol."},{"issue":"12","key":"10.1016\/j.ijbiomac.2020.07.178_bb0615","doi-asserted-by":"crossref","first-page":"2265","DOI":"10.1016\/j.bbapap.2014.09.015","article-title":"A structure-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"},{"issue":"10","key":"10.1016\/j.ijbiomac.2020.07.178_bb0620","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0109846","article-title":"Synergism between basic Asp49 and Lys49 phospholipase A2 myotoxins of viperid snake venom in vitro and in vivo","volume":"9","author":"Mora-Obando","year":"2014","journal-title":"PLoS One"},{"issue":"11","key":"10.1016\/j.ijbiomac.2020.07.178_bb0625","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1084\/jem.20150632","article-title":"Critical role of phospholipase A2 group IID in age-related susceptibility to severe acute respiratory syndrome-CoV infection","volume":"212","author":"Vijay","year":"2015","journal-title":"J. Exp. Med."},{"issue":"4","key":"10.1016\/j.ijbiomac.2020.07.178_bb0630","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.01463-17","article-title":"Inhibition of cytosolic phospholipase A(2)\u03b1 impairs an early step of coronavirus replication in cell culture","volume":"92","author":"M\u00fcller","year":"2018","journal-title":"J. Virol."},{"issue":"14","key":"10.1016\/j.ijbiomac.2020.07.178_bb0635","doi-asserted-by":"crossref","first-page":"7717","DOI":"10.1128\/JVI.78.14.7717-7726.2004","article-title":"Human cytomegalovirus carries a cell-derived phospholipase A2 required for infectivity","volume":"78","author":"Allal","year":"2004","journal-title":"J. Virol."},{"issue":"7","key":"10.1016\/j.ijbiomac.2020.07.178_bb0640","doi-asserted-by":"crossref","DOI":"10.1371\/journal.ppat.1002829","article-title":"MAP-kinase regulated cytosolic phospholipase A2 activity is essential for production of infectious hepatitis C virus particles","volume":"8","author":"Menzel","year":"2012","journal-title":"PLoS Pathog."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813020339349?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813020339349?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T20:48:26Z","timestamp":1788295706000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813020339349"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,12]]},"references-count":128,"alternative-id":["S0141813020339349"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.07.178","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2020,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Insights into the antiviral activity of phospholipases A2 (PLA2s) from snake venoms","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2020.07.178","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Published by Elsevier B.V.","name":"copyright","label":"Copyright"}]}}