{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T20:09:36Z","timestamp":1790798976735,"version":"4.1.0"},"reference-count":147,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,9,1]],"date-time":"2019-09-01T00:00:00Z","timestamp":1567296000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,9,1]],"date-time":"2019-09-01T00:00:00Z","timestamp":1567296000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/100014440","name":"Ministerio de Ciencia, Innovaci\u00f3n y Universidades","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100014440","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Journal of Proteomics"],"published-print":{"date-parts":[[2019,9]]},"DOI":"10.1016\/j.jprot.2019.103443","type":"journal-article","created":{"date-parts":[[2019,7,17]],"date-time":"2019-07-17T12:04:01Z","timestamp":1563365041000},"page":"103443","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":88,"special_numbering":"C","title":["Phylovenomics of Daboia russelii across the Indian subcontinent. Bioactivities and comparative in vivo neutralization and in vitro third-generation antivenomics of antivenoms against venoms from India, Bangladesh and Sri Lanka"],"prefix":"10.1016","volume":"207","author":[{"given":"Davinia","family":"Pla","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Libia","family":"Sanz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sarai","family":"Quesada-Bernat","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mauren","family":"Villalta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joshua","family":"Baal","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mohammad Abdul Wahed","family":"Chowdhury","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guillermo","family":"Le\u00f3n","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8385-3081","authenticated-orcid":false,"given":"Jos\u00e9 M.","family":"Guti\u00e9rrez","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ulrich","family":"Kuch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5026-3122","authenticated-orcid":false,"given":"Juan J.","family":"Calvete","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2019.103443_bb0005","series-title":"An Account of Indian Serpents, Collected on the Coast of Coromandel: Containing Descriptions and Drawings of Each Species, Together with Experiments and Remarks on their Several Poisons","author":"Russell","year":"1796"},{"key":"10.1016\/j.jprot.2019.103443_bb0010","series-title":"The Eponym Dictionary of Reptiles","first-page":"229","author":"Beolens","year":"2011"},{"key":"10.1016\/j.jprot.2019.103443_bb0015","series-title":"The Naturalist's Miscellany Vol. VIII","first-page":"255","author":"Shaw","year":"1797"},{"key":"10.1016\/j.jprot.2019.103443_bb0020","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pntd.0000603","article-title":"Snakebite in South Asia: a review","volume":"4","author":"Alirol","year":"2010","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jprot.2019.103443_bb0025","first-page":"209","article-title":"Phylogeography of the Russell's viper (Daboia russelii) complex in relation to variation in the colour pattern and symptoms of envenoming","volume":"17","author":"Thorpe","year":"2007","journal-title":"Herpetol. J."},{"key":"10.1016\/j.jprot.2019.103443_bb0030","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1111\/j.1095-8312.1992.tb00658.x","article-title":"Population systematics of Russell's viper: a multivariate study","volume":"47","author":"W\u00fcster","year":"1992","journal-title":"Biol. J. Linn. Soc."},{"key":"10.1016\/j.jprot.2019.103443_bb0035","first-page":"33","article-title":"The genus Daboia (Serpentes: Viperidae): Russell's viper","volume":"23","author":"W\u00fcster","year":"1998","journal-title":"Hamadryad"},{"key":"10.1016\/j.jprot.2019.103443_bb0040","first-page":"103","article-title":"Some new races of the Python, Chrysopelea, Binocellate Cobra and Tith-Polonga inhabiting Ceylon and India","volume":"24","author":"Deraniyagala","year":"1945","journal-title":"Spol. Zeylan., Geol. Zool. Anthrop."},{"key":"10.1016\/j.jprot.2019.103443_bb0045","series-title":"Snakes of the World. A Checklist. I. Venomous Snakes","author":"Welch","year":"1994"},{"key":"10.1016\/j.jprot.2019.103443_bb0050","series-title":"True Vipers: Natural History and Toxinology of Old World Vipers","isbn-type":"print","author":"Mallow","year":"2003","ISBN":"https:\/\/id.crossref.org\/isbn\/0894648772"},{"key":"10.1016\/j.jprot.2019.103443_bb0055","author":"Uetz"},{"key":"10.1016\/j.jprot.2019.103443_bb0060","series-title":"Snakes of India. The Field Guide","author":"Whitaker","year":"2007"},{"key":"10.1016\/j.jprot.2019.103443_bb0065","doi-asserted-by":"crossref","first-page":"300","DOI":"10.4103\/0028-3886.158155","article-title":"Snakebite in India today","volume":"63","author":"Whitaker","year":"2015","journal-title":"Neurol. India"},{"key":"10.1016\/j.jprot.2019.103443_bb0070","first-page":"949","article-title":"Development of simple standard assay procedures for the characterization of snake venom","volume":"61","author":"Theakston","year":"1983","journal-title":"Bull. World Health Organ."},{"key":"10.1016\/j.jprot.2019.103443_bb0075","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0041-0101(88)90216-4","article-title":"Geographical variation in India in the composition and lethal potency of Russell's viper (Vipera russelli) venom","volume":"26","author":"Jayanthi","year":"1988","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0080","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0304-4165(99)00053-7","article-title":"Comparative characterisation of Russell's viper (Daboia\/Vipera russelli) venoms from different regions of the Indian peninsula","volume":"1428","author":"Prasad","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2019.103443_bb0085","series-title":"Seminar on Management of Snakebite and Research","first-page":"65","article-title":"Theingi, Geographical Variation of Biological Properties of Russell's Viper (Daboia russelii siamensis) Venom","author":"Tun-Pe","year":"2002"},{"key":"10.1016\/j.jprot.2019.103443_bb0090","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1016\/S0140-6736(85)91550-8","article-title":"Bites by Russell's viper (Vipera russelli siamensis) in Burma: haemostatic, vascular, and renal disturbances and response to treatment","volume":"2","author":"Myint-Lwin","year":"1985","journal-title":"Lancet"},{"key":"10.1016\/j.jprot.2019.103443_bb0095","first-page":"691","article-title":"Paralysis, rhabdomyolysis and haemolysis caused by bites of Russell's viper (Vipera russelli pulchella) in Sri Lanka: failure of Indian (Haffkine) antivenom","volume":"68","author":"Phillips","year":"1988","journal-title":"Q. J. Med."},{"key":"10.1016\/j.jprot.2019.103443_bb0100","doi-asserted-by":"crossref","first-page":"732","DOI":"10.1016\/0035-9203(89)90311-8","article-title":"Snake venoms in science and clinical medicine. 1. Russell's viper: biology, venom and treatment of bites","volume":"83","author":"Warrell","year":"1989","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.jprot.2019.103443_bb0105","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1016\/0035-9203(91)90464-A","article-title":"Bites by Russell's vipers (Daboia russelii siamensis) in Myanmar: effect of the snake's length and recent feeding on venom antigenaemia and severity of envenoming","volume":"85","author":"Tun-Pe","year":"1991","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.jprot.2019.103443_bb0110","series-title":"Venomous Snakes. Ecology, Evolution and Snakebite","first-page":"207","article-title":"Russell's viper in Indonesia: snakebite and systematics","author":"Belt","year":"1997"},{"key":"10.1016\/j.jprot.2019.103443_bb0115","first-page":"855","article-title":"Epidemiology and clinical picture of the Russell's viper (Daboia russelli russelli) bite in Anuradhapura, Sri Lanka: a prospective study of 336 patients","volume":"34","author":"Kularatne","year":"2000","journal-title":"Souteast Asian J. Trop. Med. Public Health"},{"key":"10.1016\/j.jprot.2019.103443_bb0120","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0090198","article-title":"Revisiting Russell's viper (Daboia russelii) bite in Sri Lanka: is abdominal pain an early feature of systemic envenoming?","volume":"9","author":"Kularatne","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jprot.2019.103443_bb0125","doi-asserted-by":"crossref","first-page":"1291","DOI":"10.1016\/S0041-0101(02)00137-X","article-title":"Russell's viper snakebite in Taiwan: differences from other Asian countries","volume":"40","author":"Hung","year":"2002","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0130","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.trstmh.2005.07.020","article-title":"Antivenom treatment and renal dysfunction in Russell's viper snakebite in Taiwan: a case series","volume":"100","author":"Hung","year":"2006","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.jprot.2019.103443_bb0135","doi-asserted-by":"crossref","first-page":"860","DOI":"10.1016\/j.trstmh.2009.02.020","article-title":"Researching nature's venoms and poisons","volume":"103","author":"Warrell","year":"2009","journal-title":"Trans. R. Soc. Trop. Med. Hyg."},{"key":"10.1016\/j.jprot.2019.103443_bb0140","first-page":"38","article-title":"New approaches & technologies of venomics to meet the challenge of human envenoming by snakebites in India","volume":"138","author":"Warrell","year":"2013","journal-title":"Indian J. Med. Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0145","doi-asserted-by":"crossref","first-page":"97","DOI":"10.1093\/qjmed\/hcq214","article-title":"Hypopituitarism following envenoming by Russell's vipers (Daboia siamensis and D.\u202frusselii) resembling Sheehan's syndrome: first case report from Sri Lanka, a review of the literature and recommendations for endocrine management","volume":"104","author":"Antonypillai","year":"2011","journal-title":"Q. J. Med."},{"key":"10.1016\/j.jprot.2019.103443_bb0150","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.toxicon.2012.11.012","article-title":"Acute pituitary insufficiency and hypokalaemia following envenoming by Russell's viper (Daboia russelii) in Sri Lanka: exploring the pathophysiological mechanisms","volume":"63","author":"Jeevagan","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0155","doi-asserted-by":"crossref","first-page":"411","DOI":"10.3109\/15563650.2016.1143556","article-title":"Neurotoxicity in Russell's viper (Daboia russelii) envenoming in Sri Lanka: a clinical and neurophysiological study","volume":"54","author":"Silva","year":"2016","journal-title":"Clin. Toxicol."},{"key":"10.1016\/j.jprot.2019.103443_bb0160","doi-asserted-by":"crossref","first-page":"11","DOI":"10.1007\/s12640-016-9650-4","article-title":"Neurotoxicity in Sri Lankan Russell's Viper (Daboia russelii) envenoming is primarily due to U1-viperitoxin-Dr1a, a pre-synaptic neurotoxin","volume":"31","author":"Silva","year":"2017","journal-title":"Neurotox. Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0165","first-page":"763","article-title":"Acute and chronic pituitary failure resembling Sheehan's syndrome following bites by Russell's viper in Burma","volume":"2","author":"Pe","year":"1987","journal-title":"Lancet"},{"key":"10.1016\/j.jprot.2019.103443_bb0170","series-title":"Venomous Snakes. Ecology, Evolution and Snakebite","first-page":"189","article-title":"Geographical and intraspecies variation in the clinical manifestations of envenoming by snakes","author":"Warrell","year":"1997"},{"key":"10.1016\/j.jprot.2019.103443_bb0175","doi-asserted-by":"crossref","first-page":"479","DOI":"10.4103\/0028-3886.55594","article-title":"Acute ischemic infarct in the middle cerebral artery territory following a Russell's viper bite","volume":"57","author":"Narang","year":"2009","journal-title":"Neurol. India"},{"key":"10.1016\/j.jprot.2019.103443_bb0180","doi-asserted-by":"crossref","first-page":"301","DOI":"10.4103\/0972-2327.91957","article-title":"Posterior circulation ischemic stroke following Russell's viper envenomation","volume":"14","author":"Gouda","year":"2011","journal-title":"Ann. Indian Acad. Neurol."},{"key":"10.1016\/j.jprot.2019.103443_bb0185","first-page":"343","article-title":"A rare case series of ischemic stroke following Russell's Viper Snake bite in India","volume":"49","author":"Pothukuchi","year":"2017","journal-title":"Acta Med. Indones."},{"key":"10.1016\/j.jprot.2019.103443_bb0190","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/0041-0101(90)90081-H","article-title":"Differences between the venoms of two sub-species of Russell's viper: Vipera russelli pulchella and Vipera russelli siamensis","volume":"28","author":"Woodhams","year":"1990","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0195","doi-asserted-by":"crossref","first-page":"7","DOI":"10.3109\/15569543.2013.855789","article-title":"Geographical variation of Indian Russell's viper venom and neutralization of its coagulopathy by polyvalent antivenom","volume":"33","author":"Sharma","year":"2014","journal-title":"Toxin Rev."},{"key":"10.1016\/j.jprot.2019.103443_bb0200","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.jprot.2009.01.006","article-title":"Snake venomics of the Siamese Russell's viper (Daboia russelli siamensis)- relation to pharmacological activities","volume":"72","author":"Risch","year":"2009","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0205","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/j.jprot.2015.08.017","article-title":"Functional venomics of the Sri Lankan Russell's viper (Daboia russelii) and its toxinological correlations","volume":"128","author":"Tan","year":"2015","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0210","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1016\/j.jprot.2016.06.001","article-title":"A proteomic analysis of Pakistan Daboia russelii russelii venom and assessment of potency of Indian polyvalent and monovalent antivenom","volume":"144","author":"Mukherjee","year":"2016","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0215","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1016\/j.toxicon.2015.06.027","article-title":"Unveiling the complexities of Daboia russelii venom, a medically important snake of India, by tandem mass spectrometry","volume":"107","author":"Sharma","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0220","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1021\/acs.jproteome.6b00693","article-title":"Unraveling the proteome composition and immuno-profiling of western India Russell's viper venom for in-depth understanding of its pharmacological properties, clinical manifestations, and effective antivenom treatment","volume":"16","author":"Kalita","year":"2017","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0225","series-title":"Directorate General of Health and Family Welfare","author":"National Snakebite Management Protocol, India","year":"2009"},{"key":"10.1016\/j.jprot.2019.103443_bb0230","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.toxicon.2016.10.007","article-title":"Development of a new polyspecific antivenom for snakebite envenoming in Sri Lanka: analysis of its preclinical efficacy as compared to a currently available antivenom","volume":"122","author":"Villalta","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0235","series-title":"Probit Analysis; A Statistical Treatment of the Sigmoid Response Curve","author":"Finney","year":"1947"},{"key":"10.1016\/j.jprot.2019.103443_bb0240","doi-asserted-by":"crossref","first-page":"887","DOI":"10.1016\/0041-0101(85)90380-0","article-title":"Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom","volume":"23","author":"Guti\u00e9rrez","year":"1985","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0245","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.vascn.2009.06.004","article-title":"A turbidimetric assay for the measurement of clotting times of procoagulant venoms in plasma","volume":"61","author":"O'Leary","year":"2010","journal-title":"J. Pharmacol. Toxiocol. Methods"},{"key":"10.1016\/j.jprot.2019.103443_bb0250","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/0041-0101(89)90096-2","article-title":"Comparative study on coagulant, defibrinating, fibrinolytic and fibrinogenolytic activities of Costa Rican crotaline snake venoms and their neutralization by a polyvalent antivenom","volume":"27","author":"Gen\u00e9","year":"1989","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0255","first-page":"159","article-title":"Pharmacological activities of a toxic phospholipase A isolated from the venom of the snake Bothrops asper","volume":"84C","author":"Guti\u00e9rrez","year":"1986","journal-title":"Comp. Biochem. Physiol."},{"key":"10.1016\/j.jprot.2019.103443_bb0260","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0022-2836(05)80360-2","article-title":"Basic local alignment search tool","volume":"215","author":"Altschul","year":"1990","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jprot.2019.103443_bb0265","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1586\/epr.11.61","article-title":"Proteomic tools against the neglected pathology of snake bite envenoming","volume":"8","author":"Calvete","year":"2011","journal-title":"Exp. Rev. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0270","doi-asserted-by":"crossref","first-page":"557","DOI":"10.1586\/14789450.2015.1073590","article-title":"Constructing comprehensive venom proteome reference maps for integrative venomics","volume":"12","author":"Eichberg","year":"2015","journal-title":"Exp. Rev. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0275","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1586\/14789450.2014.900447","article-title":"Next-generation snake venomics: protein-locus resolution through venom proteome decomplexation","volume":"11","author":"Calvete","year":"2014","journal-title":"Exp. Rev. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0280","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.jprot.2017.06.001","article-title":"Absolute venomics: absolute quantification of intact venom proteins through elemental mass spectrometry","volume":"164","author":"Calder\u00f3n-Celis","year":"2017","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0285","doi-asserted-by":"crossref","DOI":"10.3390\/toxins9050158","article-title":"Third generation antivenomics: pushing the limits of the in vitro preclinical assessment of antivenoms","volume":"9","author":"Pla","year":"2017","journal-title":"Toxins"},{"key":"10.1016\/j.jprot.2019.103443_bb0290","doi-asserted-by":"crossref","first-page":"1870","DOI":"10.1093\/molbev\/msw054","article-title":"MEGA7: molecular evolutionary genetics analysis version 7.0 for bigger datasets","volume":"33","author":"Kumar","year":"2016","journal-title":"Mol. Biol. Evol."},{"key":"10.1016\/j.jprot.2019.103443_bb0295","first-page":"275","article-title":"The rapid generation of mutation data matrices from protein sequences","volume":"8","author":"Jones","year":"1992","journal-title":"Comput. Appl. Biosci."},{"key":"10.1016\/j.jprot.2019.103443_bb0300","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/j.toxicon.2018.04.015","article-title":"Toxin-resolved antivenomics-guided assessment of the immunorecognition landscape of antivenoms","volume":"148","author":"Calvete","year":"2018","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0305","series-title":"Making and Using Antibodies: A Practical Handbook","author":"Howard","year":"2014"},{"key":"10.1016\/j.jprot.2019.103443_bb0310","series-title":"Analyzing Biomolecular Interactions by Mass Spectrometry","first-page":"227","article-title":"Antivenomics: a proteomics tool for studying the immunoreactivity of antivenoms","author":"Calvete","year":"2015"},{"key":"10.1016\/j.jprot.2019.103443_bb0315","article-title":"Translational venomics: third-generation antivenomics of anti-siamese Russell's viper, Daboia siamensis, antivenom manufactured in Taiwan CDC's Vaccine Center","volume":"3","author":"Sanz","year":"2018","journal-title":"Trop. Med. Infect. Dis."},{"key":"10.1016\/j.jprot.2019.103443_bb0320","doi-asserted-by":"crossref","DOI":"10.3390\/toxins11020090","article-title":"Vipera berus berus venom from Russia: venomics, bioactivities and preclinical assessment of Microgen antivenom","volume":"11","author":"Al-Shekhadat","year":"2019","journal-title":"Toxins"},{"key":"10.1016\/j.jprot.2019.103443_bb0325","series-title":"Progress in the Characterization of Venoms and Standardization of Antivenoms","author":"WHO","year":"1981"},{"key":"10.1016\/j.jprot.2019.103443_bb0330","doi-asserted-by":"crossref","first-page":"502","DOI":"10.1016\/j.toxicon.2007.11.002","article-title":"Potency evaluation of antivenoms in Brazil: the national control laboratory experience between 2000 and 2006","volume":"51","author":"Araujo","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0335","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1590\/S1678-91992010000200002","article-title":"Antivenoms: potency or median effective dose, which to use?","volume":"16","author":"Morais","year":"2010","journal-title":"J. Venom. Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.jprot.2019.103443_bb0340","doi-asserted-by":"crossref","first-page":"837","DOI":"10.1080\/14789450.2018.1528150","article-title":"Proteomic analysis reveals geographic variation in venom composition of Russell's Viper in the Indian subcontinent: implications for clinical manifestations post-envenomation and antivenom treatment","volume":"15","author":"Kalita","year":"2018","journal-title":"Expert Rev. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0345","series-title":"Handbook of Clinical Toxinology of Animal Venoms and Poisons","first-page":"493","article-title":"Clinical toxicology of snakebite in Asia","author":"Warrell","year":"1995"},{"key":"10.1016\/j.jprot.2019.103443_bb0350","first-page":"635","article-title":"Venom, antivenom production and the medically important snakes of India","volume":"103","author":"Whitaker","year":"2012","journal-title":"Curr. Sci."},{"key":"10.1016\/j.jprot.2019.103443_bb0355","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jprot.2018.05.003","article-title":"Proteomics, functional characterization and antivenom neutralization of the venom of Pakistani Russell's viper (Daboia russelii) from the wild","volume":"183","author":"Faisal","year":"2018","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0360","first-page":"1020","article-title":"Venom phospholipases of Russell's vipers from Myanmar and eastern India. Cloning, characterization and phylogeographic analysis","volume":"2007","author":"Tsai","year":"1774","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2019.103443_bb0365","doi-asserted-by":"crossref","first-page":"2819","DOI":"10.1021\/acs.jproteome.8b00291","article-title":"Proteomic analysis and immuno-profiling of eastern India Russell's viper (Daboia russelii) venom: correlation between RVV composition and clinical manifestations post RV bite","volume":"17","author":"Kalita","year":"2018","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0370","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1016\/j.ijbiomac.2018.06.083","volume":"118","author":"Kalita","year":"2018","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.jprot.2019.103443_bb0375","doi-asserted-by":"crossref","first-page":"17471","DOI":"10.1016\/S0021-9258(19)77860-0","article-title":"The factor V-activating enzyme (RVV-V) from Russell's viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences","volume":"263","author":"Tokunaga","year":"1988","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0380","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0378-1119(00)00571-0","article-title":"Sequence diversity of Vipera lebetina snake venom gland serine proteinase homologs result of alternative-splicing or genome alteration","volume":"263","author":"Siigur","year":"2001","journal-title":"Gene"},{"key":"10.1016\/j.jprot.2019.103443_bb0385","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1016\/j.toxicon.2018.11.294","article-title":"Biochemistry and pharmacology of proteins and peptides purified from the venoms of the snakes Macrovipera lebetina subspecies","volume":"158","author":"Siigur","year":"2019","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0390","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.toxicon.2011.05.014","article-title":"Phylogenetic analysis of serine proteases from Russell's viper (Daboia russelli siamensis) and Agkistrodon piscivorus leucostoma venom","volume":"58","author":"Sukkapan","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0395","doi-asserted-by":"crossref","first-page":"3476","DOI":"10.1016\/j.bbagen.2013.02.007","article-title":"Biochemical and pharmacological properties of a new thrombin-like serine protease (Russelobin) from the venom of Russell's viper (Daboia russelii russelii) and assessment of its therapeutic potential","volume":"1830","author":"Mukherjee","year":"2013","journal-title":"Biochem. Biophys. Acta-Gen. Sub."},{"key":"10.1016\/j.jprot.2019.103443_bb0400","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0086823","article-title":"The pro-coagulant fibrinogenolytic serine protease isoenzymes purified from Daboia russelii russelii venom coagulate the blood through factor V activation: role of glycosylation on enzymatic activity","volume":"9","author":"Mukherjee","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jprot.2019.103443_bb0405","doi-asserted-by":"crossref","first-page":"3020","DOI":"10.1016\/j.febslet.2011.08.022","article-title":"Structural basis of coagulation factor V recognition for cleavage by RVV-V","volume":"585","author":"Nakayama","year":"2011","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2019.103443_bb0410","doi-asserted-by":"crossref","first-page":"1486","DOI":"10.1016\/j.biochi.2008.05.012","article-title":"P-III hemorrhagic metalloproteinases from Russell's viper venom: cloning, characterization, phylogenetic and functional site analyses","volume":"90","author":"Chen","year":"2008","journal-title":"Biochimie"},{"key":"10.1016\/j.jprot.2019.103443_bb0415","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.toxicon.2018.03.005","article-title":"Analysis of snake venom metalloproteinases from Myanmar Russell's viper transcriptome","volume":"146","author":"Yee","year":"2018","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0420","series-title":"Enzymes from Snake Venom","first-page":"11","article-title":"Proteases that induce hemorrhage","author":"Takeya","year":"1998"},{"key":"10.1016\/j.jprot.2019.103443_bb0425","doi-asserted-by":"crossref","first-page":"5859","DOI":"10.1016\/j.febslet.2007.11.062","article-title":"Crystal structure of RVV-X: an example of evolutionary gain of specificity by ADAM proteinases","volume":"581","author":"Takeda","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2019.103443_bb0430","doi-asserted-by":"crossref","first-page":"14109","DOI":"10.1016\/S0021-9258(19)49685-3","article-title":"Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin- like domains","volume":"267","author":"Takeya","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0435","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1021\/bi00667a023","article-title":"Factor X activating enzyme from Russell's viper venom: isolation and characterization","volume":"15","author":"Kisiel","year":"1976","journal-title":"Biochemistry"},{"key":"10.1016\/j.jprot.2019.103443_bb0440","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/S0167-4838(99)00268-X","article-title":"Snake venom proteases affecting hemostasis and thrombosis","volume":"1477","author":"Matsui","year":"2000","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2019.103443_bb0445","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.toxicon.2005.02.029","article-title":"Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage","volume":"45","author":"Guti\u00e9rrez","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0450","doi-asserted-by":"crossref","DOI":"10.3390\/toxins8100304","article-title":"A comprehensive view of the structural and functional alterations of extracellular matrix by Snake Venom Metalloproteinases (SVMPs): novel perspectives on the pathophysiology of envenoming","volume":"8","author":"Guti\u00e9rrez","year":"2016","journal-title":"Toxins"},{"key":"10.1016\/j.jprot.2019.103443_bb0455","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.toxicon.2012.03.001","article-title":"C-type lectin-like proteins from snake venoms","volume":"60","author":"Arlinghaus","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0460","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1016\/j.toxicon.2005.10.002","article-title":"Characterization and molecular cloning of dabocetin, a potent antiplatelet C-type lectin-like protein from Daboia russellii siamensis venom","volume":"47","author":"Zhong","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0465","series-title":"Handbook of Venoms and Toxins of Reptiles","first-page":"379","article-title":"Snake venom nerve growth factors","author":"Lavin","year":"2010"},{"key":"10.1016\/j.jprot.2019.103443_bb0470","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/S0041-0101(01)00232-X","article-title":"Ophidian envenomation strategies and the role of purines","volume":"40","author":"Aird","year":"2002","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0475","first-page":"1","article-title":"An overview on nucleases (DNase, RNase, and phosphodiesterase) in snake venoms","volume":"75","author":"Dhananjaya","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.jprot.2019.103443_bb0480","doi-asserted-by":"crossref","first-page":"51985","DOI":"10.1074\/jbc.C300454200","article-title":"Snake venom vascular endothelial growth factors (VEGFs) exhibit potent activity through their specific recognition of KDR (VEGF receptor 2)","volume":"278","author":"Yamazaki","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0485","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1007\/s11030-006-9027-3","article-title":"Molecular and functional diversity of vascular endothelial growth factors","volume":"10","author":"Yamazaki","year":"2006","journal-title":"Mol. Divers."},{"key":"10.1016\/j.jprot.2019.103443_bb0490","doi-asserted-by":"crossref","first-page":"16088","DOI":"10.1038\/s41598-018-34363-1","article-title":"Systemic vascular leakage induced in mice by Russell's viper venom from Pakistan","volume":"8","author":"Rucavado","year":"2008","journal-title":"Sci. Rep."},{"key":"10.1016\/j.jprot.2019.103443_bb0495","doi-asserted-by":"crossref","first-page":"2707","DOI":"10.21474\/IJAR01\/2697","article-title":"Clinical features, prognostic factors & outcome of capillary leak syndrome in snake bite envenomation","volume":"4","author":"Thomas","year":"2016","journal-title":"Int. J. Adv. Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0500","doi-asserted-by":"crossref","first-page":"698","DOI":"10.4103\/ijccm.IJCCM_41_17","article-title":"Capillary leak syndrome following snakebite envenomation","volume":"21","author":"Udayabhaskaran","year":"2017","journal-title":"Indian J. Crit. Care Med."},{"key":"10.1016\/j.jprot.2019.103443_bb0505","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.2019.103443_bb0510","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1016\/j.toxicon.2012.05.001","article-title":"Past decade study of snake venom L-amino acid oxidase","volume":"60","author":"Guo","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0515","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.toxicon.2017.04.013","article-title":"The role of platelets in hemostasis and the effects of snake venom toxins on platelet function","volume":"133","author":"de Queiroz","year":"2017","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0520","doi-asserted-by":"crossref","first-page":"15739","DOI":"10.1074\/jbc.M111.323063","article-title":"A novel heparin-dependent inhibitor of activated protein C that potentiates consumptive coagulopathy in Russell's viper envenomation","volume":"287","author":"Cheng","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0525","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1046\/j.1538-7836.2003.00298.x","article-title":"What is all that thrombin for?","volume":"1","author":"Mann","year":"2003","journal-title":"J. Thromb. Haemost."},{"key":"10.1016\/j.jprot.2019.103443_bb0530","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.toxicon.2013.07.006","article-title":"Synergistically acting PLA2: peptide hemorrhagic complex from Daboia russelii venom","volume":"73","author":"Venkatesh","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0535","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/j.toxicon.2014.06.016","article-title":"Pharmacological properties and pathophysiological significance of a Kunitz-type protease inhibitor (Rusvikunin-II) and its protein complex (Rusvikunin complex) purified from Daboia russelii russelii venom","volume":"89","author":"Mukherjee","year":"2014","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0540","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.biochi.2016.08.005","article-title":"Structural and functional characterization of complex formation between two Kunitz-type serine protease inhibitors from Russell's Viper venom","volume":"128\u2013129","author":"Mukherjee","year":"2016","journal-title":"Biochimie"},{"key":"10.1016\/j.jprot.2019.103443_bb0545","doi-asserted-by":"crossref","first-page":"1279","DOI":"10.1016\/0041-0101(91)90116-9","article-title":"Snake venom variability: methods of study, results and interpretation","volume":"29","author":"Chippaux","year":"1991","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0550","doi-asserted-by":"crossref","first-page":"2576","DOI":"10.1016\/j.jprot.2012.02.035","article-title":"Venom variability and envenoming severity outcomes of the Crotalus scutulatus scutulatus (Mojave rattlesnake) from Southern Arizona","volume":"75","author":"Massey","year":"2012","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0555","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.toxicon.2013.03.020","article-title":"Snake venomics: from the inventory of toxins to biology","volume":"75","author":"Calvete","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0560","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1042\/BCJ20160577","article-title":"Venomics: integrative venom proteomics and beyond","volume":"474","author":"Calvete","year":"2017","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2019.103443_bb0565","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.jprot.2018.03.032","article-title":"Molecular mechanisms underlying intraspecific variation in snake venom","volume":"181","author":"Amazonas","year":"2018","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0570","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.2019.103443_bb0575","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1471-2148-7-2","article-title":"Inventing an arsenal: adaptive evolution and neofunctionalization of snake venom phospholipase A2 genes","volume":"7","author":"Lynch","year":"2007","journal-title":"BMC Evol. Biol."},{"key":"10.1016\/j.jprot.2019.103443_bb0580","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1016\/0041-0101(95)00114-X","article-title":"Two types of Russell's viper revealed by variation in phospholipases A2 from venom of the subspecies","volume":"34","author":"Tsai","year":"1996","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0585","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/S0041-0101(97)00051-2","article-title":"The three-dimensional structures of two toxins from snake venom throw light on the anticoagulant and neurotoxic sites of phospholipase A2","volume":"36","author":"Carredano","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0590","doi-asserted-by":"crossref","first-page":"722","DOI":"10.1107\/S0907444907016204","article-title":"Structural and pharmacological comparison of daboiatoxin from Daboia russelli siamensis with viperotoxin F and vipoxin from other vipers","volume":"63","author":"Gopalan","year":"2007","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jprot.2019.103443_bb0595","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0041-0101(94)00133-S","article-title":"A major lethal factor of the venom of Burmese Russell's viper (Daboia russelli siamensis): isolation, N-terminal sequencing and biological activities of daboiatoxin","volume":"33","author":"Thwin","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0600","doi-asserted-by":"crossref","first-page":"151","DOI":"10.4103\/0974-2700.193350","article-title":"The North-South divide in snake bite envenomation in India","volume":"9","author":"Chauhan","year":"2016","journal-title":"J. Emerg. Trauma Shock"},{"key":"10.1016\/j.jprot.2019.103443_bb0605","doi-asserted-by":"crossref","first-page":"665","DOI":"10.1016\/0041-0101(94)90336-0","article-title":"Primary sequence determination of the most basic myonecrotic phospholipase A2 from the venom of Vipera russelli","volume":"32","author":"Gowda","year":"1994","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0610","doi-asserted-by":"crossref","first-page":"71","DOI":"10.2220\/biomedres.31.71","article-title":"Molecular diversity in venom proteins of the Russell's viper (Daboia russelii russelii) and the Indian cobra (Naja naja) in Sri Lanka","volume":"31","author":"Suzuki","year":"2010","journal-title":"Biomed. Res."},{"key":"10.1016\/j.jprot.2019.103443_bb0615","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1016\/0041-0101(89)90136-0","article-title":"Purification and characterization of a major phospholipase A2 from Russell's viper (Vipera russelii) venom","volume":"27","author":"Kasturi","year":"1989","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0620","first-page":"175","article-title":"Antibodies to a phospholipase A2 from Vipera russelli selectively neutralize venom neurotoxicity","volume":"70","author":"Kasturi","year":"1990","journal-title":"Immunology"},{"key":"10.1016\/j.jprot.2019.103443_bb0625","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1006\/jmbi.2000.3537","article-title":"Three-dimensional structure of a presynaptic neurotoxic phospholipase A2 from Daboia russelli pulchella at 2.4 \u00c5 resolution","volume":"296","author":"Chandra","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jprot.2019.103443_bb0630","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0153770","article-title":"Daboxin P, a major phospholipase A2 enzyme from the Indian Daboia russelii russelii venom targets Factor X and Factor Xa for its anticoagulant activity","volume":"11","author":"Sharma","year":"2016","journal-title":"PLoS One"},{"key":"10.1016\/j.jprot.2019.103443_bb0635","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.jprot.2011.01.003","article-title":"Snake population venomics and antivenomics of Bothrops atrox: paedomorphism along its transamazonian dispersal and implications of geographic venom variability on snakebite management","volume":"74","author":"Calvete","year":"2011","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0640","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1080\/14789450.2018.1500904","article-title":"Snake venomics \u2013 from low-resolution toxin-pattern recognition to toxin-resolved venom proteomes with absolute quantification","volume":"15","author":"Calvete","year":"2018","journal-title":"Expert Rev. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0645","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1016\/j.toxicon.2013.01.022","article-title":"Antivenom for snakebite envenoming in Sri Lanka: the need for geographically specific antivenom and improved efficacy","volume":"69","author":"Keyler","year":"2013","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0650","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.actatropica.2012.01.016","article-title":"Immunological properties of Hypnale hypnale (hump-nosed pit viper) venom: antibody production with diagnostic and therapeutic potentials","volume":"122","author":"Tan","year":"2012","journal-title":"Acta Trop."},{"key":"10.1016\/j.jprot.2019.103443_bb0655","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1016\/j.actatropica.2010.11.001","article-title":"Cross neutralization of Hypnale hypnale (hump-nosed pit viper) venom by polyvalent and monovalent Malayan pit viper antivenoms in vitro and in a rodent model","volume":"117","author":"Tan","year":"2011","journal-title":"Acta Trop."},{"key":"10.1016\/j.jprot.2019.103443_bb0660","first-page":"63","article-title":"Phylogenetic relationships of the Agkistrodon","volume":"70","author":"Parkinson","year":"1997","journal-title":"Symp. Zool. Soc. Lond."},{"key":"10.1016\/j.jprot.2019.103443_bb0665","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1006\/mpev.1998.0509","article-title":"Weighting and congruence: a cse study based on three mitochondrial genes in pitvipers","volume":"9","author":"Vidal","year":"1998","journal-title":"Mol. Phylogenet. Evol."},{"key":"10.1016\/j.jprot.2019.103443_bb0670","doi-asserted-by":"crossref","first-page":"338","DOI":"10.1016\/j.jprot.2013.07.020","article-title":"Proteomic comparison of Hypnale hypnale (hump-nosed pit-viper) and Calloselasma rhodostoma (Malayan pit-viper) venoms","volume":"91","author":"Ali","year":"2013","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2019.103443_bb0675","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.toxicon.2014.11.231","article-title":"Proteomic investigation of Sri Lankan hump-nosed pit viper (Hypnale hypnale) venom","volume":"93","author":"Tan","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0680","doi-asserted-by":"crossref","first-page":"659","DOI":"10.1096\/fj.07-9574LSF","article-title":"Dose translation from animal to human studies revisited","volume":"22","author":"Reagan-Shaw","year":"2008","journal-title":"FASEB J."},{"key":"10.1016\/j.jprot.2019.103443_bb0685","doi-asserted-by":"crossref","first-page":"27","DOI":"10.4103\/0976-0105.177703","article-title":"A simple practice guide for dose conversion between animals and human","volume":"7","author":"Nair","year":"2016","journal-title":"J. Basic Clin. Pharm."},{"key":"10.1016\/j.jprot.2019.103443_bb0690","doi-asserted-by":"crossref","first-page":"730","DOI":"10.1016\/0041-0101(86)90037-1","article-title":"Amount of venom injected by Russell's viper (Vipera russelli)","volume":"24","author":"Pe","year":"1986","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0695","doi-asserted-by":"crossref","first-page":"4193","DOI":"10.1021\/ac0498563","article-title":"A model for random sampling and estimation of relative protein abundance in shotgun proteomics","volume":"76","author":"Liu","year":"2004","journal-title":"Anal. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0700","doi-asserted-by":"crossref","first-page":"1017","DOI":"10.1007\/s00216-007-1486-6","article-title":"Quantitative mass spectrometry in proteomics: a critical review","volume":"389","author":"Bantscheff","year":"2007","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0705","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1007\/s00216-012-6203-4","article-title":"Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present","volume":"404","author":"Bantscheff","year":"2012","journal-title":"Anal. Bioanal. Chem."},{"key":"10.1016\/j.jprot.2019.103443_bb0710","doi-asserted-by":"crossref","first-page":"2373","DOI":"10.1074\/mcp.M800203-MCP200","article-title":"Significance analysis of spectral count data in label-free shotgun proteomics","volume":"7","author":"Choi","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0715","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1002\/pmic.201000553","article-title":"Less label, more free: approaches in label-free quantitative mass spectrometry","volume":"11","author":"Neilson","year":"2011","journal-title":"Proteomics"},{"key":"10.1016\/j.jprot.2019.103443_bb0720","doi-asserted-by":"crossref","first-page":"e481","DOI":"10.1093\/bioinformatics\/btl237","article-title":"A computational approach toward label-free protein quantification using predicted peptide detectability","volume":"22","author":"Tang","year":"2006","journal-title":"Bioinformatics"},{"key":"10.1016\/j.jprot.2019.103443_bb0725","doi-asserted-by":"crossref","first-page":"817","DOI":"10.1016\/0041-0101(95)00032-H","article-title":"Biochemical and biological properties of the venom from Russell's viper (Daboia russelli siamensis) of varying ages","volume":"33","author":"Pe","year":"1995","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2019.103443_bb0730","series-title":"Guidelines for the Management of Snake-Bites","first-page":"1","author":"Warrell","year":"2016"},{"key":"10.1016\/j.jprot.2019.103443_bb0735","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1136\/emj.2003.008458","article-title":"Snake envenomation in a north Indian hospital","volume":"22","author":"Sharma","year":"2005","journal-title":"Emerg. Med. J."}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391919302155?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391919302155?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T12:02:28Z","timestamp":1761739348000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391919302155"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,9]]},"references-count":147,"alternative-id":["S1874391919302155"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2019.103443","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2019,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Phylovenomics of Daboia russelii across the Indian subcontinent. Bioactivities and comparative in vivo neutralization and in vitro third-generation antivenomics of antivenoms against venoms from India, Bangladesh and Sri Lanka","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2019.103443","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"103443"}}