{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:08:22Z","timestamp":1788869302332,"version":"build-2803163510"},"reference-count":45,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,2,1]],"date-time":"2015-02-01T00:00:00Z","timestamp":1422748800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,2,1]],"date-time":"2015-02-01T00:00:00Z","timestamp":1422748800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100003336","name":"Bulgarian National Science Fund","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003336","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Toxicon"],"published-print":{"date-parts":[[2015,2]]},"DOI":"10.1016\/j.toxicon.2014.12.009","type":"journal-article","created":{"date-parts":[[2014,12,20]],"date-time":"2014-12-20T07:42:55Z","timestamp":1419061375000},"page":"36-44","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":15,"special_numbering":"C","title":["Effects of vipoxin and its components on HepG2 cells"],"prefix":"10.1016","volume":"94","author":[{"given":"Jordan","family":"Doumanov","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kirilka","family":"Mladenova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanya","family":"Topouzova-Hristova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stoyanka","family":"Stoitsova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Svetla","family":"Petrova","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"6","key":"10.1016\/j.toxicon.2014.12.009_bib1","doi-asserted-by":"crossref","first-page":"477","DOI":"10.1016\/0041-0101(76)90065-9","article-title":"Action on phosphatidylcholine of the toxic phospholipase A2 from the venom of Bulgarian viper (Vipera ammodytes ammodytes)","volume":"14","author":"Aleksiev","year":"1976","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.12.009_bib2","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1134\/S0006297909030055","article-title":"Hemolytic and anticoagulant study of the neurotoxin vipoxin and its components \u2013 basic phospholipase A2 and an acidic inhibitor","volume":"74","author":"Atanasov","year":"2009","journal-title":"Biochem. Mosc."},{"key":"10.1016\/j.toxicon.2014.12.009_bib3","doi-asserted-by":"crossref","first-page":"1341","DOI":"10.1080\/00032710902954425","article-title":"HPLC assay of phospholipase A2 activity using low-temperature derivatization of fatty acids","volume":"42","author":"Atanasov","year":"2009","journal-title":"Anal. Lett."},{"issue":"4","key":"10.1016\/j.toxicon.2014.12.009_bib4","doi-asserted-by":"crossref","first-page":"169","DOI":"10.2478\/v10102-012-0028-z","article-title":"Acute toxicity of vipoxin and its components: is the acidic component an \u201cinhibitor\u201d of PLA2 toxicity?","volume":"5","author":"Atanasov","year":"2012","journal-title":"Interdiscip. Toxicol."},{"key":"10.1016\/j.toxicon.2014.12.009_bib5","doi-asserted-by":"crossref","first-page":"1552","DOI":"10.1107\/S0907444901013543","article-title":"Structure of the neurotoxic complex vipoxin at 1.4A resolution","volume":"57","author":"Banumathi","year":"2001","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.toxicon.2014.12.009_bib6","doi-asserted-by":"crossref","first-page":"384","DOI":"10.1007\/s000180050440","article-title":"Modulation of phospholipase A2 activity generated by molecular evolution","volume":"56","author":"Betzel","year":"1999","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.toxicon.2014.12.009_bib7","first-page":"663","article-title":"Neurotoxic action of a protein complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes)","volume":"32","author":"Blinov","year":"1979","journal-title":"C.\u00a0R. Acad. Bulg. Sci."},{"key":"10.1016\/j.toxicon.2014.12.009_bib8","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.bbamcr.2006.02.014","article-title":"Interactions of mitochondria with the actin cytoskeleton","volume":"1763","author":"Boldogh","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2014.12.009_bib9","doi-asserted-by":"crossref","first-page":"2063","DOI":"10.1242\/jcs.01049","article-title":"Polarity and lipid raft association of the components of the ciliary neurotrophic factor receptor complex in MDCK cells","volume":"117","author":"Buk","year":"2004","journal-title":"J.\u00a0Cell. Sci."},{"key":"10.1016\/j.toxicon.2014.12.009_bib10","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/203639","article-title":"Antitumoral activity of snake venom proteins: new trends in cancer therapy","author":"Calderon","year":"2014","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.toxicon.2014.12.009_bib11","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/0076-6879(91)97134-K","article-title":"Chromogenic substrates and assay of phospholipases A2","volume":"197","author":"Cho","year":"1991","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2014.12.009_bib12","doi-asserted-by":"crossref","first-page":"6130","DOI":"10.1021\/cr200085w","article-title":"Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention","volume":"111","author":"Dennis","year":"2011","journal-title":"Chem. Rev."},{"issue":"1","key":"10.1016\/j.toxicon.2014.12.009_bib13","first-page":"1000181","article-title":"Snake venom cytotoxins, phospholipase A2s, and Zn2+-dependent metalloproteinases: mechanisms of action and pharmacological relevance","volume":"4","author":"Gasanov","year":"2014","journal-title":"J.\u00a0Clin. Toxicol."},{"key":"10.1016\/j.toxicon.2014.12.009_bib14","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.bbrc.2004.01.174","article-title":"The X-ray structure of a snake venom Gln48 phospholipase A2 at 1.9 \u00c5 resolution reveals anion-binding sites","volume":"316","author":"Georgieva","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2014.12.009_bib15","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/nrm1682","article-title":"The actin cytoskeleton: a key regulator of apoptosis and ageing?","volume":"6","author":"Gourlay","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"8","key":"10.1016\/j.toxicon.2014.12.009_bib16","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1016\/j.toxicon.2003.11.005","article-title":"Skeletal muscle degeneration induced by venom phospholipases A2: insights into the mechanisms of local and systemic myotoxicity","volume":"42","author":"Guti\u00e9rrez","year":"2003","journal-title":"Toxicon"},{"issue":"1","key":"10.1016\/j.toxicon.2014.12.009_bib17","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":"Guti\u00e9rrez","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.12.009_bib18","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1016\/j.bbamem.2006.09.026","article-title":"Lysophospholipid receptors: signalling, pharmacology and regulation by lysophospholipid metabolism","volume":"1768","author":"Heringdorf","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"issue":"10","key":"10.1016\/j.toxicon.2014.12.009_bib19","doi-asserted-by":"crossref","first-page":"1149","DOI":"10.1016\/0041-0101(96)00057-8","article-title":"An aqueous endpoint assay of snake venom phospholipase A2","volume":"34","author":"Holzer","year":"1996","journal-title":"Toxicon"},{"issue":"16","key":"10.1016\/j.toxicon.2014.12.009_bib20","doi-asserted-by":"crossref","first-page":"9357","DOI":"10.1074\/jbc.273.16.9357","article-title":"Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis","volume":"273","author":"J\u00e4nicke","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"issue":"23","key":"10.1016\/j.toxicon.2014.12.009_bib22","doi-asserted-by":"crossref","first-page":"4544","DOI":"10.1111\/j.1742-4658.2011.08115.x","article-title":"Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis","volume":"278","author":"Kang","year":"2011","journal-title":"FEBS J."},{"key":"10.1016\/j.toxicon.2014.12.009_bib23","series-title":"Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism","year":"1997"},{"key":"10.1016\/j.toxicon.2014.12.009_bib24","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":"6","key":"10.1016\/j.toxicon.2014.12.009_bib25","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1016\/0041-0101(89)90013-5","article-title":"A\u00a0model 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.toxicon.2014.12.009_bib26","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.toxicon.2014.12.009_bib27","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.12.009_bib28","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.\u00a0Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.12.009_bib29","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1515\/bchm3.1987.368.1.343","article-title":"Sequence homology between phospholipase and its inhibitor in snake venom. The primary structure of phospholipase A2 of vipoxin from the venom of the Bulgarian viper (Vipera ammodytes ammodytes, Serpentes)","volume":"368","author":"Mancheva","year":"1987","journal-title":"Biol. Chem. Hoppe Seyler"},{"issue":"18","key":"10.1016\/j.toxicon.2014.12.009_bib30","doi-asserted-by":"crossref","first-page":"2897","DOI":"10.1007\/s00018-008-8113-3","article-title":"Cellular pathology induced by snake venom phospholipase A2 myotoxins and neurotoxins: common aspects of their mechanisms of action","volume":"65","author":"Montecucco","year":"2008","journal-title":"Cell. Mol. Life Sci."},{"issue":"1\u20132","key":"10.1016\/j.toxicon.2014.12.009_bib31","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/0022-1759(83)90303-4","article-title":"Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays","volume":"65","author":"Mosmann","year":"1983","journal-title":"J.\u00a0Immunol. Methods"},{"key":"10.1016\/j.toxicon.2014.12.009_bib32","first-page":"1584","article-title":"Comet assay analysis of single-stranded DNA breaks in circulating leukocytes of glaucoma patients","volume":"14","author":"Mozaffarieh","year":"2008","journal-title":"Mol. Vis."},{"key":"10.1016\/j.toxicon.2014.12.009_bib33","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.plipres.2010.12.001","article-title":"Recent progress in phospholipase A2 research: from cells to animals to humans","volume":"50","author":"Murakami","year":"2011","journal-title":"Prog. Lipid Res."},{"issue":"1","key":"10.1016\/j.toxicon.2014.12.009_bib34","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1006\/excr.2000.4834","article-title":"Apoptotic DNA fragmentation","volume":"256","author":"Nagata","year":"2000","journal-title":"Exp. Cell. Res."},{"key":"10.1016\/j.toxicon.2014.12.009_bib35","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/978-1-59745-201-4_6","article-title":"Hepatocyte apoptosis","volume":"481","author":"Najimi","year":"2009","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.toxicon.2014.12.009_bib36","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1038\/nprot.2006.5","article-title":"The comet assay: a method to measure DNA damage in individual cells","volume":"1","author":"Olive","year":"2006","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.toxicon.2014.12.009_bib37","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1038\/sj.cdd.4400988","article-title":"Apoptosis and keratin intermediate filaments","volume":"9","author":"Oshima","year":"2002","journal-title":"Cell Death Differ."},{"key":"10.1016\/j.toxicon.2014.12.009_bib39","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1023\/A:1015332314389","article-title":"Isolation and preliminary enzymatic characterization of a novel PLA2 from Crotalus durissus collilineatus venom","volume":"21","author":"Ponce-Soto","year":"2002","journal-title":"J.\u00a0Protein Chem."},{"issue":"5754","key":"10.1016\/j.toxicon.2014.12.009_bib40","doi-asserted-by":"crossref","first-page":"1678","DOI":"10.1126\/science.1120640","article-title":"Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures","volume":"310","author":"Rigoni","year":"2005","journal-title":"Science"},{"issue":"15","key":"10.1016\/j.toxicon.2014.12.009_bib41","doi-asserted-by":"crossref","first-page":"11238","DOI":"10.1074\/jbc.M610176200","article-title":"Calcium influx and mitochondrial alterations at synapses exposed to snake neurotoxins or their phospholipid hydrolysis products","volume":"282","author":"Rigoni","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"issue":"8","key":"10.1016\/j.toxicon.2014.12.009_bib42","doi-asserted-by":"crossref","first-page":"909","DOI":"10.1016\/j.toxicon.2006.03.004","article-title":"Crotoxin induces actin reorganization and inhibits tyrosine phosphorylation and activity of small GTPases in rat macrophages","volume":"47","author":"Sampaio","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.12.009_bib43","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1388-1981(00)00105-0","article-title":"The expanding superfamily of phospholipase A2 enzymes: classification and characterization","volume":"1488","author":"Six","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2014.12.009_bib44","doi-asserted-by":"crossref","first-page":"76","DOI":"10.1016\/0003-2697(85)90442-7","article-title":"Measurement of protein using bicinchoninic acid","volume":"150","author":"Smith","year":"1985","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2014.12.009_bib45","first-page":"558","article-title":"A\u00a0simple procedure for the isolation of vipoxin \u2013 a neurotoxin with weak phospholipase activity from the venom of the Bulgarian viper","volume":"3","author":"Tchorbanov","year":"1981","journal-title":"J.\u00a0Appl. Biochem."},{"issue":"2","key":"10.1016\/j.toxicon.2014.12.009_bib46","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/0014-5793(77)80165-8","article-title":"Subfractionation and recombination of a neurotoxic complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes)","volume":"76","author":"Tchorbanov","year":"1977","journal-title":"FEBS Lett."},{"issue":"1","key":"10.1016\/j.toxicon.2014.12.009_bib47","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0041-0101(78)90058-2","article-title":"A\u00a0neurotoxic complex from the venom of the Bulgarian viper (Vipera ammodytes ammodytes) and a partial amino acid sequence of the toxic phospholipase A2","volume":"16","author":"Tchorbanov","year":"1978","journal-title":"Toxicon"}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010114006333?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010114006333?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,22]],"date-time":"2025-09-22T21:09:05Z","timestamp":1758575345000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010114006333"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,2]]},"references-count":45,"alternative-id":["S0041010114006333"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2014.12.009","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2015,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Effects of vipoxin and its components on HepG2 cells","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2014.12.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}