{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T12:45:57Z","timestamp":1789908357292,"version":"4.0.1"},"reference-count":81,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,9,1]],"date-time":"2016-09-01T00:00:00Z","timestamp":1472688000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100004329","name":"Slovenian Research Agency","doi-asserted-by":"publisher","award":["P1-0207"],"award-info":[{"award-number":["P1-0207"]}],"id":[{"id":"10.13039\/501100004329","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004329","name":"Slovenian Research Agency","doi-asserted-by":"publisher","award":["P4-0053"],"award-info":[{"award-number":["P4-0053"]}],"id":[{"id":"10.13039\/501100004329","id-type":"DOI","asserted-by":"publisher"}]},{"name":"bilateral cooperation grant Croatia\u2013Slovenia","award":["BI-HR\/16-17-002"],"award-info":[{"award-number":["BI-HR\/16-17-002"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2016,9]]},"DOI":"10.1016\/j.jprot.2016.06.020","type":"journal-article","created":{"date-parts":[[2016,6,22]],"date-time":"2016-06-22T02:48:25Z","timestamp":1466563705000},"page":"34-47","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":62,"special_numbering":"C","title":["Venomics of Vipera berus berus to explain differences in pathology elicited by Vipera ammodytes ammodytes envenomation: Therapeutic implications"],"prefix":"10.1016","volume":"146","author":[{"given":"Zorica","family":"Latinovi\u0107","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Adrijana","family":"Leonardi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jernej","family":"\u0160ribar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tamara","family":"Sajevic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monika C.","family":"\u017du\u017eek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Robert","family":"Frange\u017e","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Beata","family":"Halassy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alenka","family":"Trampu\u0161-Bakija","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u017ee","family":"Punger\u010dar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Igor","family":"Kri\u017eaj","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2016.06.020_bb0005","doi-asserted-by":"crossref","first-page":"86","DOI":"10.1016\/j.toxicon.2011.10.008","article-title":"Epidemiology of snakebites in Europe: a systematic review of the literature","volume":"59","author":"Chippaux","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0010","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1136\/emj.13.5.346","article-title":"Incidence, pathology, and treatment of adder (Vipera berus L.) bites in man","volume":"13","author":"Reading","year":"1996","journal-title":"J. Accid. Emerg. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0015","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1016\/j.ejim.2005.10.001","article-title":"Snake venom poisoning in Greece. Experiences with 147 cases","volume":"17","author":"Frangides","year":"2006","journal-title":"Eur. J. Intern. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0020","first-page":"191","article-title":"Venomous snakebites in southern Croatia","volume":"30","author":"Luk\u0161i\u0107","year":"2006","journal-title":"Coll. Antropol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0025","doi-asserted-by":"crossref","first-page":"8","DOI":"10.1016\/j.toxicon.2016.01.057","article-title":"Venomous snakebites in children in southern Croatia","volume":"112","author":"Karabuva","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0030","doi-asserted-by":"crossref","first-page":"120","DOI":"10.14712\/23362936.2014.42","article-title":"Common viper bites in the Czech Republic - epidemiological and clinical aspects during 15year period (1999\u20132013)","volume":"115","author":"Valenta","year":"2014","journal-title":"Prague Med. Rep."},{"key":"10.1016\/j.jprot.2016.06.020_bb0035","first-page":"793","article-title":"Vipera berus bites in Eastern Poland\u2014a retrospective analysis of 15 case studies","volume":"19","author":"Garkowski","year":"2012","journal-title":"Ann. Agric. Environ. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0040","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1093\/qjmed\/hcn079","article-title":"Neurotoxicity and hypertension following European adder (Vipera berus berus) bites in Hungary: case report and review","volume":"101","author":"Malina","year":"2008","journal-title":"QJM"},{"key":"10.1016\/j.jprot.2016.06.020_bb0045","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/0041-0101(93)90380-2","article-title":"Biological and biochemical activities of Vipera berus (European viper) venom","volume":"31","author":"Calder\u00f3n","year":"1993","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0050","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1016\/j.wem.2010.01.005","article-title":"Vipera berus bites in the Region of Southwest Poland\u2014a clinical analysis of 26 cases","volume":"21","author":"Magdalan","year":"2010","journal-title":"Wilderness Environ. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0055","doi-asserted-by":"crossref","first-page":"1244","DOI":"10.1136\/bmj.331.7527.1244","article-title":"Treatment of bites by adders and exotic venomous snakes","volume":"331","author":"Warrell","year":"2005","journal-title":"BMJ"},{"key":"10.1016\/j.jprot.2016.06.020_bb0060","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1580\/07-WEME-LE-157.1","article-title":"Vipera berus bite in a child, with severe local symptoms and hypotension","volume":"20","author":"Moser","year":"2009","journal-title":"Wilderness Environ. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0065","first-page":"641","article-title":"Mechanism of Vipera berus venom activity and the principles of antivenom administration in treatment","volume":"67","author":"Czajka","year":"2013","journal-title":"Przegl. Epidemiol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0070","first-page":"1","article-title":"Hospital contacts after bite by the European adder (Vipera berus)","volume":"62","author":"H\u00f8nge","year":"2015","journal-title":"Dan. Med. J."},{"key":"10.1016\/j.jprot.2016.06.020_bb0075","doi-asserted-by":"crossref","first-page":"1627","DOI":"10.1016\/S0041-0101(02)00167-8","article-title":"Persistent paresis of the facialis muscle after European adder (Vipera berus) bite on the forehead","volume":"40","author":"Weinelt","year":"2002","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0080","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.neuro.2010.11.007","article-title":"First clinical experiences about the neurotoxic envenomings inflicted by lowland populations of the Balkan adder, Vipera berus bosniensis","volume":"32","author":"Malina","year":"2011","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.jprot.2016.06.020_bb0085","doi-asserted-by":"crossref","first-page":"378","DOI":"10.1016\/j.wem.2013.06.005","article-title":"Further clinical evidence for the existence of neurotoxicity in a population of the European adder (Vipera berus berus) in eastern Hungary: second authenticated case","volume":"24","author":"Malina","year":"2013","journal-title":"Wilderness Environ. Med."},{"key":"10.1016\/j.jprot.2016.06.020_bb0090","doi-asserted-by":"crossref","first-page":"3388","DOI":"10.3390\/toxins6123388","article-title":"Omics meets biology: application to the design and preclinical assessment of antivenoms","volume":"6","author":"Calvete","year":"2014","journal-title":"Toxins (Basel)"},{"key":"10.1016\/j.jprot.2016.06.020_bb0095","doi-asserted-by":"crossref","first-page":"866","DOI":"10.1021\/pr070376c","article-title":"Comparative analysis of the venom proteomes of Vipera ammodytes ammodytes and Vipera ammodytes meridionalis","volume":"7","author":"Georgieva","year":"2008","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2016.06.020_bb0100","doi-asserted-by":"crossref","first-page":"680","DOI":"10.1038\/227680a0","article-title":"Cleavage of structural proteins during the assembly of the head of bacteriophage T4","volume":"227","author":"Laemmli","year":"1970","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2016.06.020_bb0105","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/0003-2697(81)90783-1","article-title":"Silver stain for proteins in polyacrylamide gels: a modified procedure with enhanced uniform sensitivity","volume":"117","author":"Morrissey","year":"1981","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0110","doi-asserted-by":"crossref","first-page":"5046","DOI":"10.1021\/pr3006155","article-title":"Conus consors snail venom proteomics proposes functions, pathways, and novel families involved in its venomic system","volume":"11","author":"Leonardi","year":"2012","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2016.06.020_bb0115","doi-asserted-by":"crossref","first-page":"5745","DOI":"10.1002\/anie.201600190","article-title":"Nonpeptidic selective inhibitors of the chymotrypsin-like (\u03b25 i) subunit of the immunoproteasome","volume":"55","author":"Sosi\u010d","year":"2016","journal-title":"Angew. Chem. Int. Ed. Engl."},{"key":"10.1016\/j.jprot.2016.06.020_bb0120","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1016\/0005-2795(76)90321-4","article-title":"Fibrinogenolytic enzymes of Trimeresurus mucrosquamatus venom","volume":"420","author":"Ouyang","year":"1976","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2016.06.020_bb0125","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.toxicon.2013.11.009","article-title":"Hemorrhagin VaH4, a covalent heterodimeric P-III metalloproteinase from Vipera ammodytes ammodytes with a potential antitumour activity","volume":"77","author":"Leonardi","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0130","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.toxicon.2008.07.015","article-title":"Two coagulation factor X activators from Vipera a. ammodytes venom with potential to treat patients with dysfunctional factors IXa or VIIa","volume":"52","author":"Leonardi","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0135","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.tox.2012.10.013","article-title":"Toxicity of the synthetic polymeric 3-alkylpyridinium salt (APS3) is due to specific block of nicotinic acetylcholine receptors","volume":"303","author":"Grandi\u010d","year":"2013","journal-title":"Toxicology"},{"key":"10.1016\/j.jprot.2016.06.020_bb0140","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0041-0101(94)90078-7","article-title":"Screening of snake venoms for neurotoxic and myotoxic effects using simple in vitro preparations from rodents and chicks","volume":"32","author":"Harvey","year":"1994","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0145","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/j.gene.2006.03.008","article-title":"Venom gland EST analysis of the saw-scaled viper, Echis ocellatus, reveals novel alpha9beta1 integrin-binding motifs in venom metalloproteinases and a new group of putative toxins, renin-like aspartic proteases","volume":"377","author":"Wagstaff","year":"2006","journal-title":"Gene"},{"key":"10.1016\/j.jprot.2016.06.020_bb0150","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.toxicon.2013.11.007","article-title":"VaSP1, catalytically active serine proteinase from Vipera ammodytes ammodytes venom with unconventional active site triad","volume":"77","author":"Kurtovi\u0107","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0155","doi-asserted-by":"crossref","first-page":"178","DOI":"10.1016\/j.cbpc.2008.05.005","article-title":"The role of antibodies specific for toxic sPLA2s and haemorrhagins in neutralizing potential of antisera raised against Vipera ammodytes ammodytes venom","volume":"148","author":"Halassy","year":"2008","journal-title":"Comp. Biochem. Physiol. C. Toxicol. Pharmacol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0160","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2012.09.003","article-title":"The long road of research on snake venom serine proteinases","volume":"62","author":"Serrano","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0165","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.toxicon.2005.02.020","article-title":"Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved","volume":"45","author":"Serrano","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0170","doi-asserted-by":"crossref","first-page":"12566","DOI":"10.1016\/S0021-9258(17)44214-1","article-title":"Kallikrein-like enzymes from Crotalus atrox venom","volume":"258","author":"Bjarnason","year":"1983","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0175","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0041-0101(93)90144-8","article-title":"Effect of bilineobin, a thrombin-like proteinase from the venom of common cantil (Agkistrodon bilineatus)","volume":"31","author":"Komori","year":"1993","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0180","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0041-0101(97)00150-5","article-title":"Characterization of three fibrinogenolytic enzymes from Chinese green tree viper (Trimeresurus stejnegeri) venom","volume":"36","author":"Gao","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0185","doi-asserted-by":"crossref","first-page":"10294","DOI":"10.1021\/bi000145i","article-title":"A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin","volume":"39","author":"Amiconi","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jprot.2016.06.020_bb0190","doi-asserted-by":"crossref","first-page":"826","DOI":"10.1055\/s-0037-1613468","article-title":"Anticoagulant serine fibrinogenases from Vipera lebetina venom: structure-function relationships","volume":"89","author":"Siigur","year":"2003","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.jprot.2016.06.020_bb0195","first-page":"1","article-title":"An overview of hemostatically active components of Vipera ammodytes ammodytes venom","volume":"9543","author":"Sajevic","year":"2013","journal-title":"Toxin Rev."},{"key":"10.1016\/j.jprot.2016.06.020_bb0200","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","article-title":"Snake venom metalloproteinases","volume":"62","author":"Markland","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0205","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.toxicon.2011.01.006","article-title":"Haemostatically active proteins in snake venoms","volume":"57","author":"Sajevic","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0210","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/0742-8413(90)90129-W","article-title":"Isolation and characterization of hemorrhagic metalloproteinase from Vipera berus berus (common viper) venom","volume":"97","author":"Samel","year":"1990","journal-title":"Comp. Biochem. Physiol. C"},{"issue":"6","key":"10.1016\/j.jprot.2016.06.020_bb0215","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1016\/j.biochi.2013.01.003","article-title":"VaH3, one of the principal hemorrhagins in Vipera ammodytes ammodytes venom, is a homodimeric P-IIIc metalloproteinase","volume":"95","author":"Sajevic","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.jprot.2016.06.020_bb0220","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/S0304-4165(01)00206-9","article-title":"Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity","volume":"1568","author":"Siigur","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2016.06.020_bb0225","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1093\/oxfordjournals.jbchem.a131150","article-title":"The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venon and characterization of the new active intermediates","volume":"79","author":"Morita","year":"1976","journal-title":"J. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0230","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1042\/bj20020449","article-title":"A prothrombin activator from Bothrops erythromelas (jararaca-da-seca) snake venom: characterization and molecular cloning","volume":"369","author":"Silva","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2016.06.020_bb0235","doi-asserted-by":"crossref","first-page":"3016","DOI":"10.1111\/j.1742-4658.2008.06466.x","article-title":"Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity","volume":"275","author":"Fox","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.jprot.2016.06.020_bb0240","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0041-0101(94)00143-V","article-title":"Medium molecular weight factor X activating enzyme from Vipera berus berus venom","volume":"33","author":"Samel","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0245","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.bbrc.2007.11.027","article-title":"Molecular characterisation of endogenous snake venom metalloproteinase inhibitors","volume":"365","author":"Wagstaff","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jprot.2016.06.020_bb0250","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1007\/s10557-005-6900-8","article-title":"Rethinking the renin-angiotensin system and its role in cardiovascular regulation","volume":"19","author":"Pagliaro","year":"2005","journal-title":"Cardiovasc. Drugs Ther."},{"key":"10.1016\/j.jprot.2016.06.020_bb0255","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."},{"key":"10.1016\/j.jprot.2016.06.020_bb0260","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.jprot.2016.06.020_bb0265","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0304-4165(93)90081-I","article-title":"Isolation, partial characterization and complete amino acid sequence of the toxic phospholipase A2 from the venom of the common viper, Vipera berus berus","volume":"1157","author":"Kri\u017eaj","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2016.06.020_bb0270","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.toxicon.2011.06.009","article-title":"Ammodytoxin: a window into understanding presynaptic toxicity of secreted phospholipases A2 and more","volume":"58","author":"Kri\u017eaj","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0275","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1111\/j.1432-1033.1991.tb16485.x","article-title":"The primary structure of ammodytin L, a myotoxic phospholipase A2 homologue from Vipera ammodytes venom","volume":"202","author":"Kri\u017eaj","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0280","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.1046\/j.1432-1033.2003.03629.x","article-title":"Sequences and structural organization of phospholipase A2 genes from Vipera aspis aspis, V. aspis zinnikeri and Vipera berus berus venom. Identification of the origin of a new viper population based on ammodytin I1 heterogeneity","volume":"270","author":"Guillemin","year":"2003","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0285","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"},{"key":"10.1016\/j.jprot.2016.06.020_bb0290","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1107\/S1744309108027036","article-title":"Isolation, crystallization and preliminary X-ray diffraction analysis of l-amino-acid oxidase from Vipera ammodytes ammodytes venom","volume":"64","author":"Georgieva","year":"2008","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"key":"10.1016\/j.jprot.2016.06.020_bb0295","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1186\/1471-2199-8-115","article-title":"The venom gland transcriptome of the desert Massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (superfamily Colubroidea)","volume":"8","author":"Pahari","year":"2007","journal-title":"BMC Mol. Biol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0300","doi-asserted-by":"crossref","first-page":"707","DOI":"10.1016\/j.bbapap.2006.01.021","article-title":"Isolation and characterization of an apoptotic and platelet aggregation inhibiting l-amino acid oxidase from Vipera berus berus (common viper) venom","volume":"1764","author":"Samel","year":"2006","journal-title":"Biochim. Biophys. Acta Proteins Proteomics"},{"key":"10.1016\/j.jprot.2016.06.020_bb0305","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/j.toxicon.2004.05.023","article-title":"Structure and function of snake venom cysteine-rich secretory proteins","volume":"44","author":"Yamazaki","year":"2004","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0310","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1093\/molbev\/mss058","article-title":"Evolution of CRISPs associated with toxicoferan-reptilian venom and mammalian reproduction","volume":"29","author":"Sunagar","year":"2012","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0315","doi-asserted-by":"crossref","first-page":"162","DOI":"10.1016\/j.toxicon.2008.11.001","article-title":"Cysteine-rich venom proteins from the snakes of Viperinae subfamily - Molecular cloning and phylogenetic relationship","volume":"53","author":"Ramazanova","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0320","doi-asserted-by":"crossref","first-page":"5628","DOI":"10.1016\/j.jprot.2012.08.008","article-title":"Snake venomics and antivenomics of Protobothrops mucrosquamatus and Viridovipera stejnegeri from Taiwan: keys to understand the variable immune response in horses","volume":"75","author":"Villalta","year":"2012","journal-title":"J. Proteomics"},{"key":"10.1016\/j.jprot.2016.06.020_bb0325","doi-asserted-by":"crossref","first-page":"2708","DOI":"10.1046\/j.1432-1033.2002.02940.x","article-title":"Cloning and characterization of novel snake venom proteins that block smooth muscle contraction","volume":"269","author":"Yamazaki","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0330","doi-asserted-by":"crossref","first-page":"2851","DOI":"10.1007\/s00018-009-0050-2","article-title":"Protein complexes in snake venom","volume":"66","author":"Doley","year":"2009","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.jprot.2016.06.020_bb0335","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1016\/j.toxicon.2010.03.011","article-title":"Snaclecs (snake C-type lectins) that inhibit or activate platelets by binding to receptors","volume":"56","author":"Clemetson","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0340","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.toxicon.2014.04.010","article-title":"Lebecin, a new C-type lectin like protein from Macrovipera lebetina venom with anti-tumor activity against the breast cancer cell line MDA-MB231","volume":"86","author":"Jebali","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0345","doi-asserted-by":"crossref","first-page":"1089","DOI":"10.1016\/j.toxicon.2005.02.022","article-title":"Snake venom C-type lectins interacting with platelet receptors. Structure-function relationships and effects on haemostasis","volume":"45","author":"Lu","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0350","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/S0014-5793(03)00693-8","article-title":"Adaptive evolution in the snake venom Kunitz\/BPTI protein family","volume":"547","author":"\u017dupunski","year":"2003","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2016.06.020_bb0355","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1111\/j.1432-1033.1983.tb07481.x","article-title":"Serine proteinase inhibitors from Vipera ammodytes venom. Isolation and kinetic studies","volume":"133","author":"Ritonja","year":"1983","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0360","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1007\/s00216-013-7453-5","article-title":"Identification of proteins interacting with ammodytoxins in Vipera ammodytes ammodytes venom by immuno-affinity chromatography","volume":"406","author":"Brgles","year":"2014","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jprot.2016.06.020_bb0365","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1038\/nature10607","article-title":"A heteromeric Texas coral snake toxin targets acid-sensing ion channels to produce pain","volume":"479","author":"Bohlen","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.jprot.2016.06.020_bb0370","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1093\/protein\/10.2.131","article-title":"Foci of amino acid residue conservation in the 3D structures of the Kunitz BPTI proteinase inhibitors: how do variants from snake venom differ?","volume":"10","author":"Cardle","year":"1997","journal-title":"Protein Eng."},{"key":"10.1016\/j.jprot.2016.06.020_bb0375","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.matbio.2012.11.015","article-title":"PIVL, a new serine protease inhibitor from Macrovipera lebetina transmediterranea venom, impairs motility of human glioblastoma cells","volume":"32","author":"Morjen","year":"2013","journal-title":"Matrix Biol."},{"key":"10.1016\/j.jprot.2016.06.020_bb0380","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/j.toxicon.2010.12.001","article-title":"Natriuretic peptide drug leads from snake venom","volume":"59","author":"Vink","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0385","doi-asserted-by":"crossref","first-page":"1063","DOI":"10.1016\/j.toxicon.2005.02.024","article-title":"Snake venom disintegrins: evolution of structure and function","volume":"45","author":"Calvete","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0390","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/j.toxicon.2012.09.005","article-title":"The continuing saga of snake venom disintegrins","volume":"62","author":"Calvete","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2016.06.020_bb0395","doi-asserted-by":"crossref","first-page":"725","DOI":"10.1042\/bj20021739","article-title":"Snake venom disintegrins: novel dimeric disintegrins and structural diversification by disulphide bond engineering","volume":"372","author":"Calvete","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2016.06.020_bb0400","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.biochi.2005.06.015","article-title":"The C-terminal and beta-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.jprot.2016.06.020_bb0405","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.biochi.2014.12.013","article-title":"Structural and biochemical characterisation of VaF1, a P-IIIa fibrinogenolytic metalloproteinase from Vipera ammodytes ammodytes venom","volume":"109","author":"Leonardi","year":"2015","journal-title":"Biochimie"}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391916302597?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391916302597?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,7,2]],"date-time":"2022-07-02T00:54:16Z","timestamp":1656723256000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391916302597"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,9]]},"references-count":81,"alternative-id":["S1874391916302597"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2016.06.020","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2016,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Venomics of Vipera berus berus to explain differences in pathology elicited by Vipera ammodytes ammodytes envenomation: Therapeutic implications","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2016.06.020","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2016 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}