{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:21:33Z","timestamp":1791354093934,"version":"4.3.1"},"update-to":[{"DOI":"10.1371\/journal.pntd.0008596","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,2,12]],"date-time":"2021-02-12T00:00:00Z","timestamp":1613088000000}}],"reference-count":85,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2021,2,2]],"date-time":"2021-02-02T00:00:00Z","timestamp":1612224000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"University Grants Commission of India","award":["MRP-MAJOR-BIOC-2013-12157"],"award-info":[{"award-number":["MRP-MAJOR-BIOC-2013-12157"]}]},{"name":"Science and Engineering Research Board, Department of Science and Technology, Government of India","award":["EEQ\/2017\/000737"],"award-info":[{"award-number":["EEQ\/2017\/000737"]}]}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"abstract":"<jats:p>\n                    <jats:italic>Echis carinatus<\/jats:italic>\n                    (EC) is known as saw-scaled viper and it is endemic to the Indian subcontinent. Envenoming by EC represents a major cause of snakebite mortality and morbidity in the Indian subcontinent. Zinc (Zn\n                    <jats:sup>++<\/jats:sup>\n                    ) dependent snake venom metalloproteases (SVMPs) present in\n                    <jats:italic>Echis carinatus<\/jats:italic>\n                    venom (ECV) is well known to cause systemic hemorrhage and coagulopathy in experimental animals. An earlier report has shown that ECV activates neutrophils and releases neutrophil extracellular traps (NETs) that blocks blood vessels leading to severe tissue necrosis. However, the direct involvement of SVMPs in the release of NETs is not clear. Here, we investigated the direct involvement of EC SVMPs in observed pathological symptoms in a preclinical setup using specific Zn\n                    <jats:sup>++<\/jats:sup>\n                    metal chelator, Tetraethyl thiuram disulfide (TTD)\/disulfiram. TTD potently antagonizes the activity of SVMPs-mediated ECM protein degradation in vitro and skin hemorrhage in mice. In addition, TTD protected mice from ECV-induced footpad tissue necrosis by reduced expression of citrullinated H3 (citH3) and myeloperoxidase (MPO) in footpad tissue. TTD also neutralized ECV-induced systemic hemorrhage and conferred protection against lethality in mice. Moreover, TTD inhibited ECV-induced NETosis in human neutrophils and decreased the expression of peptidyl arginine deiminase (PAD) 4, citH3, MPO, and p-ERK. Further, we demonstrated that ECV-induced NETosis and tissue necrosis are mediated via PAR-1-ERK axis. Overall, our results provide an insight into SVMPs-induced toxicities and the promising protective efficacy of TTD can be extrapolated to treat severe tissue necrosis complementing anti-snake venom (ASV).\n                  <\/jats:p>","DOI":"10.1371\/journal.pntd.0008596","type":"journal-article","created":{"date-parts":[[2021,2,2]],"date-time":"2021-02-02T15:46:30Z","timestamp":1612280790000},"page":"e0008596","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":18,"title":["Echis carinatus snake venom metalloprotease-induced toxicities in mice: Therapeutic intervention by a repurposed drug, Tetraethyl thiuram disulfide (Disulfiram)"],"prefix":"10.1371","volume":"15","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3177-030X","authenticated-orcid":true,"given":"Gotravalli V.","family":"Rudresha","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7818-2460","authenticated-orcid":true,"given":"Amog P.","family":"Urs","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9735-765X","authenticated-orcid":true,"given":"Vaddarahally N.","family":"Manjuprasanna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mallanayakanakatte D.","family":"Milan Gowda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Krishnegowda","family":"Jayachandra","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6506-891X","authenticated-orcid":true,"given":"Rajesh","family":"Rajaiah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3284-4163","authenticated-orcid":true,"given":"Bannikuppe S.","family":"Vishwanath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,2,2]]},"reference":[{"issue":"6","key":"pntd.0008596.ref001","doi-asserted-by":"crossref","first-page":"e150","DOI":"10.1371\/journal.pmed.0030150","article-title":"Confronting the neglected problem of snake bite envenoming: the need for a global partnership","volume":"3","author":"JM Gutierrez","year":"2006","journal-title":"Plos Med"},{"issue":"9708","key":"pntd.0008596.ref002","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/S0140-6736(09)61754-2","article-title":"Snake bite","volume":"375","author":"DA Warrell","year":"2010","journal-title":"Lancet"},{"issue":"1","key":"pntd.0008596.ref003","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1016\/j.toxicon.2009.08.006","article-title":"Tissue pathology induced by snake venoms: how to understand a complex pattern of alterations from a systems biology perspective?","volume":"55","author":"JM Gutierrez","year":"2010","journal-title":"Toxicon"},{"issue":"8","key":"pntd.0008596.ref004","doi-asserted-by":"crossref","first-page":"e0135843","DOI":"10.1371\/journal.pone.0135843","article-title":"Progressive Hemorrhage and Myotoxicity Induced by Echis carinatus Venom in Murine Model: Neutralization by Inhibitor Cocktail of N,N,N\u2019,N\u2019-Tetrakis (2-Pyridylmethyl) Ethane-1,2-Diamine and Silymarin","volume":"10","author":"AN Nanjaraj Urs","year":"2015","journal-title":"PLoS One"},{"issue":"2","key":"pntd.0008596.ref005","doi-asserted-by":"crossref","first-page":"97","DOI":"10.4103\/0974-2700.43190","article-title":"Emergency treatment of a snake bite: Pearls from literature","volume":"1","author":"SM Ahmed","year":"2008","journal-title":"J Emerg Trauma Shock"},{"issue":"4","key":"pntd.0008596.ref006","doi-asserted-by":"crossref","first-page":"660","DOI":"10.1590\/S1678-91992008000400009","article-title":"Anti-snake venom: use and adverse reaction in a snake bite study clinic in Bangladesh","volume":"14","author":"MR Amin","year":"2008","journal-title":"J Venom Anim Toxins incl Trop Dis"},{"issue":"9\u201310","key":"pntd.0008596.ref007","doi-asserted-by":"crossref","first-page":"841","DOI":"10.1016\/S0300-9084(00)01163-9","article-title":"Snake venom metalloproteinases: Their role in the pathogenesis of local tissue damage","volume":"82","author":"JM Gutierrez","year":"2000","journal-title":"Biochimie"},{"issue":"8","key":"pntd.0008596.ref008","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":"JM Gutierrez","year":"2005","journal-title":"Toxicon"},{"issue":"1\u20132","key":"pntd.0008596.ref009","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1023\/A:1020651607164","article-title":"Snake venom hyaluronidase: an evidence for isoforms and extracellular matrix degradation","volume":"240","author":"KS Girish","year":"2002","journal-title":"Mol Cell Biochem"},{"issue":"1","key":"pntd.0008596.ref010","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1002\/cbf.1261","article-title":"Snake venom hyaluronidase: a therapeutic target","volume":"24","author":"K Kemparaju","year":"2006","journal-title":"Cell Biochem Funct"},{"issue":"2","key":"pntd.0008596.ref011","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1580\/06-WEME-OR-078R.1","article-title":"Rediscovery of severe saw-scaled viper (Echis sochureki) envenoming in the Thar desert region of Rajasthan, India","volume":"18","author":"DK Kochar","year":"2007","journal-title":"Wilderness Environ Med"},{"issue":"3\u20134","key":"pntd.0008596.ref012","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1016\/j.cbpc.2005.11.005","article-title":"Snake venom metalloproteases\u2014structure and function of catalytic and disintegrin domains","volume":"142","author":"OH Ramos","year":"2006","journal-title":"Comp Biochem Physiol C Toxicol Pharmacol"},{"key":"pntd.0008596.ref013","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.toxicon.2012.09.004","article-title":"Snake venom metalloproteinases","volume":"62","author":"FS Markland","year":"2013","journal-title":"Toxicon"},{"key":"pntd.0008596.ref014","first-page":"392","article-title":"A case of saw scale viper snakebite presenting as pleuro-pericardial haemorrhage","volume":"3","author":"M Lakhotia","year":"2002"},{"key":"pntd.0008596.ref015","doi-asserted-by":"crossref","first-page":"11361","DOI":"10.1038\/ncomms11361","article-title":"NETosis and lack of DNase activity are key factors in Echis carinatus venom-induced tissue destruction","volume":"7","author":"GD Katkar","year":"2016","journal-title":"Nat Commun"},{"key":"pntd.0008596.ref016","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/j.toxicon.2017.10.019","article-title":"Purification and characterization of an anti-hemorrhagic protein from Naja naja (Indian cobra) venom","volume":"140","author":"KN Suvilesh","year":"2017","journal-title":"Toxicon"},{"issue":"9","key":"pntd.0008596.ref017","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1016\/j.jprot.2011.03.026","article-title":"Key events in microvascular damage induced by snake venom hemorrhagic metalloproteinases","volume":"74","author":"T Escalante","year":"2011","journal-title":"J Proteomics"},{"issue":"4","key":"pntd.0008596.ref018","doi-asserted-by":"crossref","first-page":"93","DOI":"10.3390\/toxins8040093","article-title":"Hemorrhage Caused by Snake Venom Metalloproteinases: A Journey of Discovery and Understanding","volume":"8","author":"JM Gutierrez","year":"2016","journal-title":"Toxins (Basel)"},{"issue":"1","key":"pntd.0008596.ref019","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/0041-0101(94)00138-X","article-title":"Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)","volume":"33","author":"JM Gutierrez","year":"1995","journal-title":"Toxicon"},{"issue":"5","key":"pntd.0008596.ref020","doi-asserted-by":"crossref","DOI":"10.3390\/toxins8050155","article-title":"ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview","volume":"8","author":"S Takeda","year":"2016","journal-title":"Toxins (Basel)"},{"issue":"3","key":"pntd.0008596.ref021","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1182\/blood-2012-09-355958","article-title":"Matrix metalloproteases and PAR1 activation","volume":"121","author":"KM Austin","year":"2013","journal-title":"Blood"},{"key":"pntd.0008596.ref022","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.toxicon.2014.11.224","article-title":"Inhibitory potential of three zinc chelating agents against the proteolytic, hemorrhagic, and myotoxic activities of Echis carinatus venom","volume":"93","author":"AN Nanjaraj Urs","year":"2015","journal-title":"Toxicon"},{"issue":"542","key":"pntd.0008596.ref023","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.aay8314","article-title":"Preclinical validation of a repurposed metal chelator as an early-intervention therapeutic for hemotoxic snakebite","volume":"12","author":"LO Albulescu","year":"2020","journal-title":"Sci Transl Med"},{"issue":"3","key":"pntd.0008596.ref024","first-page":"1298","volume":"6","author":"Y Gong","year":"2014","journal-title":"Roles of matrix metalloproteinases and their natural inhibitors in prostate cancer progression"},{"issue":"20","key":"pntd.0008596.ref025","first-page":"2578","volume":"11","author":"CD Raghavendra Gowda","year":"2011","journal-title":"Characterization of major zinc containing myonecrotic and procoagulant metalloprotease \u2018malabarin\u2019from non lethal trimeresurus malabaricus snake venom with thrombin like activity: Its neutralization by chelating agents"},{"issue":"1","key":"pntd.0008596.ref026","doi-asserted-by":"crossref","first-page":"62","DOI":"10.1016\/j.joen.2011.09.005","article-title":"Inhibition of endogenous dentin matrix metalloproteinases by ethylenediaminetetraacetic acid","volume":"38","author":"JM Thompson","year":"2012","journal-title":"J Endod"},{"key":"pntd.0008596.ref027","first-page":"41","volume":"71","author":"JA Perea\u00f1ez","year":"2013","journal-title":"Glycolic acid inhibits enzymatic, hemorrhagic and edema-inducing activities of BaP1, a P\u2013I metalloproteinase from Bothrops asper snake venom: insights from docking and molecular modeling"},{"issue":"1","key":"pntd.0008596.ref028","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0021-9258(19)52451-6","article-title":"Protein measurement with the Folin phenol reagent","volume":"193","author":"OH Lowry","year":"1951","journal-title":"J Biol Chem"},{"issue":"4","key":"pntd.0008596.ref029","first-page":"593","volume":"260","author":"P Patriarca","year":"1972","journal-title":"Phospholipases and phospholipid turnover in Escherichia coli spheroplasts"},{"issue":"2","key":"pntd.0008596.ref030","first-page":"959","volume":"217","author":"JL Reissig","year":"1955","journal-title":"A modified colorimetric method for the estimation of N-acetylamino sugars"},{"issue":"6","key":"pntd.0008596.ref031","first-page":"431","volume":"53","author":"Y MURATA","year":"1963","journal-title":"Studies on snake venom"},{"issue":"1","key":"pntd.0008596.ref032","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/0003-2697(80)90338-3","article-title":"Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates","volume":"102","author":"C Heussen","year":"1980","journal-title":"Anal Biochem"},{"issue":"1","key":"pntd.0008596.ref033","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0003-9861(89)90350-0","article-title":"Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases","volume":"275","author":"EN Baramova","year":"1989","journal-title":"Arch Biochem Biophys"},{"key":"pntd.0008596.ref034","doi-asserted-by":"crossref","first-page":"43","DOI":"10.7883\/yoken1952.13.43","article-title":"Studies on the quantitative method for determination of hemorrhagic activity of Habu snake venom","volume":"13","author":"H Kondo","year":"1960","journal-title":"Jpn J Med Sci Biol"},{"key":"pntd.0008596.ref035","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.toxicon.2020.05.009","article-title":"Serine protease from Tricosanthus tricuspidata accelerates healing of Echis carinatus venom-induced necrotic wound","volume":"183","author":"GV Rudresha","year":"2020","journal-title":"Toxicon"},{"issue":"14","key":"pntd.0008596.ref036","first-page":"9636","volume":"274","author":"L Svensson","year":"1999","journal-title":"Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon"},{"issue":"4","key":"pntd.0008596.ref037","doi-asserted-by":"crossref","first-page":"395","DOI":"10.1016\/0041-0101(86)90199-6","article-title":"Approximate LD50 determinations of snake venoms using eight to ten experimental animals","volume":"24","author":"J Meier","year":"1986","journal-title":"Toxicon"},{"issue":"1","key":"pntd.0008596.ref038","first-page":"111","volume":"69","author":"AN Urs","year":"2015","journal-title":"Local and systemic toxicity of Echis carinatus venom: neutralization by Cassia auriculata L. leaf methanol extract"},{"issue":"1","key":"pntd.0008596.ref039","doi-asserted-by":"crossref","first-page":"e1004593","DOI":"10.1371\/journal.ppat.1004593","article-title":"DNA is an antimicrobial component of neutrophil extracellular traps","volume":"11","author":"TW Halverson","year":"2015","journal-title":"PLoS Pathog"},{"issue":"27","key":"pntd.0008596.ref040","doi-asserted-by":"crossref","first-page":"8391","DOI":"10.1073\/pnas.1424980112","article-title":"CD14 dependence of TLR4 endocytosis and TRIF signaling displays ligand specificity and is dissociable in endotoxin tolerance","volume":"112","author":"R Rajaiah","year":"2015","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"5","key":"pntd.0008596.ref041","doi-asserted-by":"crossref","first-page":"8319","DOI":"10.1002\/jcb.28115","article-title":"Plant DNases are potent therapeutic agents against Echis carinatus venom-induced tissue necrosis in mice","volume":"120","author":"GV Rudresha","year":"2019","journal-title":"J Cell Biochem"},{"issue":"181","key":"pntd.0008596.ref042","first-page":"33","article-title":"Poisoning by bites of the saw-scaled or carpet viper (Echis carinatus) in Nigeria","volume":"46","author":"DA Warrell","year":"1977","journal-title":"Q J Med"},{"issue":"3","key":"pntd.0008596.ref043","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1038\/nri3399","article-title":"Neutrophil recruitment and function in health and inflammation","volume":"13","author":"E Kolaczkowska","year":"2013","journal-title":"Nat Rev Immunol"},{"issue":"10","key":"pntd.0008596.ref044","doi-asserted-by":"crossref","first-page":"452","DOI":"10.1016\/j.it.2011.06.008","article-title":"Neutrophils cascading their way to inflammation","volume":"32","author":"CD Sadik","year":"2011","journal-title":"Trends Immunol"},{"issue":"5663","key":"pntd.0008596.ref045","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1126\/science.1092385","article-title":"Neutrophil extracellular traps kill bacteria","volume":"303","author":"V Brinkmann","year":"2004","journal-title":"Science"},{"key":"pntd.0008596.ref046","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.toxicon.2013.09.019","article-title":"Effect of Bothrops bilineata snake venom on neutrophil function","volume":"76","author":"SS da Setubal","year":"2013","journal-title":"Toxicon"},{"issue":"13","key":"pntd.0008596.ref047","doi-asserted-by":"crossref","first-page":"7326","DOI":"10.1073\/pnas.1909546117","article-title":"NETosis proceeds by cytoskeleton and endomembrane disassembly and PAD4-mediated chromatin decondensation and nuclear envelope rupture","volume":"117","author":"HR Thiam","year":"2020","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"24","key":"pntd.0008596.ref048","doi-asserted-by":"crossref","first-page":"2993","DOI":"10.1161\/CIRCULATIONAHA.111.066787","article-title":"beta-adrenergic receptor stimulation transactivates protease-activated receptor 1 via matrix metalloproteinase 13 in cardiac cells","volume":"125","author":"F Jaffre","year":"2012","journal-title":"Circulation"},{"issue":"3","key":"pntd.0008596.ref049","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1016\/S0377-1237(02)80140-X","article-title":"Clinical Features And Management Of Snake Bite","volume":"58","author":"SR Mehta","year":"2002","journal-title":"Med J Armed Forces India"},{"issue":"4","key":"pntd.0008596.ref050","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1016\/j.semnephrol.2008.04.005","article-title":"Snakebite nephrotoxicity in Asia","volume":"28","author":"T Kanjanabuch","year":"2008","journal-title":"Semin Nephrol"},{"key":"pntd.0008596.ref051","first-page":"63","article-title":"Acute myocardial infarction complicating snake bite","volume":"52","author":"M Maheshwari","year":"2004","journal-title":"J Assoc Physicians India"},{"key":"pntd.0008596.ref052","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1007\/978-94-007-6386-9_22","volume-title":"Clinical Toxinology in Asia Pacific and Africa","author":"JC Menon","year":"2015"},{"issue":"1","key":"pntd.0008596.ref053","first-page":"3","volume":"12","author":"V Kumar","year":"2006","journal-title":"Toxicity and symptomatic identification of species involved in snakebites in the Indian subcontinent"},{"issue":"2","key":"pntd.0008596.ref054","first-page":"254","article-title":"Saw-scaled viper bites in Sri Lanka: is it a different subspecies? Clinical evidence from an authenticated case series","volume":"86","author":"A Gnanathasan","year":"2012","journal-title":"JTAjotm, hygiene"},{"issue":"6","key":"pntd.0008596.ref055","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1111\/bjh.14591","article-title":"Haemotoxic snake venoms: their functional activity, impact on snakebite victims and pharmaceutical promise","volume":"177","author":"J Slagboom","year":"2017","journal-title":"Br J Haematol"},{"issue":"4","key":"pntd.0008596.ref056","doi-asserted-by":"crossref","first-page":"449","DOI":"10.1016\/j.toxicon.2012.02.006","article-title":"On the ancestral recruitment of metalloproteinases into the venom of snakes","volume":"60","author":"NR Casewell","year":"2012","journal-title":"Toxicon"},{"issue":"1","key":"pntd.0008596.ref057","doi-asserted-by":"crossref","first-page":"164","DOI":"10.1016\/j.bbapap.2011.04.009","article-title":"Snake venom metalloproteinases: structure, function and relevance to the mammalian ADAM\/ADAMTS family proteins","volume":"1824","author":"S Takeda","year":"2012","journal-title":"Biochim Biophys Acta"},{"issue":"8","key":"pntd.0008596.ref058","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1016\/j.toxicon.2005.02.012","article-title":"Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases","volume":"45","author":"JW Fox","year":"2005","journal-title":"Toxicon"},{"issue":"3","key":"pntd.0008596.ref059","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1074\/mcp.M112.023135","article-title":"Differential evolution and neofunctionalization of snake venom metalloprotease domains","volume":"12","author":"A Brust","year":"2013","journal-title":"Mol Cell Proteomics"},{"issue":"6","key":"pntd.0008596.ref060","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1016\/0002-9343(90)90534-K","article-title":"Disulfiram treatment of alcoholism","volume":"88","author":"C Wright","year":"1990","journal-title":"Am J Med"},{"issue":"30","key":"pntd.0008596.ref061","doi-asserted-by":"crossref","first-page":"3248","DOI":"10.2174\/1381612825666190816233755","article-title":"An Updated Review of Disulfiram: Molecular Targets and Strategies for Cancer Treatment","volume":"25","author":"Q Yang","year":"2019","journal-title":"Curr Pharm Des"},{"issue":"11","key":"pntd.0008596.ref062","first-page":"1378","article-title":"Disulfiram\u2019s anticancer activity: Evidence and mechanisms","volume":"16","author":"Y Jiao","year":"2016","journal-title":"JA-CAiMC"},{"issue":"3","key":"pntd.0008596.ref063","doi-asserted-by":"crossref","first-page":"692","DOI":"10.1002\/cpt.1220","article-title":"Population Pharmacokinetics and Pharmacodynamics of Disulfiram on Inducing Latent HIV-1 Transcription in a Phase IIb Trial","volume":"105","author":"SA Lee","year":"2019","journal-title":"Clin Pharmacol Ther"},{"issue":"2","key":"pntd.0008596.ref064","article-title":"Disulfiram (Tetraethylthiuram Disulfide) in the Treatment of Lyme Disease and Babesiosis: Report of Experience in Three Cases","volume":"8","author":"KB Liegner","year":"2019","journal-title":"Antibiotics (Basel)"},{"key":"pntd.0008596.ref065","article-title":"Disulfiram Treatment Normalizes Body Weight in Obese Mice","author":"M Bernier","year":"2020","journal-title":"Cell Metab"},{"issue":"5","key":"pntd.0008596.ref066","doi-asserted-by":"crossref","first-page":"1076","DOI":"10.1124\/mol.64.5.1076","article-title":"Inhibition of invasion and angiogenesis by zinc-chelating agent disulfiram","volume":"64","author":"SG Shian","year":"2003","journal-title":"Mol Pharmacol"},{"issue":"5","key":"pntd.0008596.ref067","first-page":"313","volume":"63","author":"A Rucavado","year":"2000","journal-title":"Inhibition of local hemorrhage and dermonecrosis induced by Bothrops asper snake venom: effectiveness of early in situ administration of the peptidomimetic metalloproteinase inhibitor batimastat and the chelating agent CaNa2EDTA"},{"issue":"4","key":"pntd.0008596.ref068","first-page":"417","article-title":"Effect of the metalloproteinase inhibitor batimastat in the systemic toxicity induced by Bothrops asper snake venom: understanding the role of metalloproteinases in envenomation","volume":"43","author":"A Rucavado","year":"2004"},{"key":"pntd.0008596.ref069","doi-asserted-by":"crossref","unstructured":"Xie C, Albulescu L, Bittenbinder MA, Somsen G, Vonk F, Casewell NR, et al. Neutralizing effects of small molecule inhibitors and metal chelators on coagulopathic Viperinae snake venom toxins. 2020.","DOI":"10.1101\/2020.06.02.129643"},{"issue":"5","key":"pntd.0008596.ref070","first-page":"309","article-title":"Repurposing cancer drugs batimastat and marimastat to inhibit the activity of a group I metalloprotease from the venom of the Western diamondback rattlesnake","volume":"12","author":"HJ Layfield","year":"2020","journal-title":"Crotalus atrox"},{"issue":"1","key":"pntd.0008596.ref071","first-page":"1","volume":"1","author":"S Ainsworth","year":"2018","journal-title":"The paraspecific neutralisation of snake venom induced coagulopathy by antivenoms"},{"issue":"2","key":"pntd.0008596.ref072","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/S0006-2952(00)00302-6","article-title":"Effectiveness of batimastat, a synthetic inhibitor of matrix metalloproteinases, in neutralizing local tissue damage induced by BaP1, a hemorrhagic metalloproteinase from the venom of the snake bothrops asper","volume":"60","author":"T Escalante","year":"2000","journal-title":"Biochem Pharmacol"},{"key":"pntd.0008596.ref073","doi-asserted-by":"crossref","unstructured":"DER ROJJoAN. Disulfiram (Antabuse) Editor\u2014Al Rundio, PhD, DNP, RN, APRN, CARN-AP, NEA-BC, DPNAP. 2010;21:54\u20135.","DOI":"10.3109\/10884601003625977"},{"issue":"4","key":"pntd.0008596.ref074","first-page":"459","article-title":"The safety of disulfiram for the treatment of alcohol and cocaine dependence in randomized clinical trials: guidance for clinical practice","volume":"7","author":"R Malcolm","year":"2008","journal-title":"JEoods"},{"issue":"5","key":"pntd.0008596.ref075","first-page":"427","article-title":"Safety issues concerning the use of disulfiram in treating alcohol dependence","volume":"20","author":"J Chick","year":"1999","journal-title":"JDS"},{"key":"pntd.0008596.ref076","volume-title":"Meyler\u2019s side effects of drugs: the international encyclopedia of adverse drug reactions and interactions","author":"JK Aronson","year":"2015"},{"issue":"4","key":"pntd.0008596.ref077","doi-asserted-by":"crossref","first-page":"e0003731","DOI":"10.1371\/journal.pntd.0003731","article-title":"Tissue localization and extracellular matrix degradation by PI, PII and PIII snake venom metalloproteinases: clues on the mechanisms of venom-induced hemorrhage","volume":"9","author":"C Herrera","year":"2015","journal-title":"PLoS Negl Trop Dis"},{"issue":"4","key":"pntd.0008596.ref078","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/0041-0101(85)90367-8","article-title":"Myonecrosis, myoglobinuria and acute renal failure induced by South American rattlesnake (Crotalus durissus terrificus) envenomation in Brazil","volume":"23","author":"MM Azevedo-Marques","year":"1985","journal-title":"Toxicon"},{"key":"pntd.0008596.ref079","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.toxicon.2015.11.014","article-title":"Differential action of medically important Indian BIG FOUR snake venoms on rodent blood coagulation","volume":"110","author":"V Hiremath","year":"2016","journal-title":"Toxicon"},{"issue":"5","key":"pntd.0008596.ref080","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1083\/jcb.201203170","article-title":"Neutrophil extracellular traps: is immunity the second function of chromatin?","volume":"198","author":"V Brinkmann","year":"2012","journal-title":"J Cell Biol"},{"issue":"2","key":"pntd.0008596.ref081","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/j.toxicon.2007.03.020","article-title":"Biochemical and biological characterization of the venoms of Bothriopsis bilineata and Bothriopsis taeniata (Serpentes: Viperidae)","volume":"50","author":"BN Porto","year":"2007","journal-title":"Toxicon"},{"issue":"7","key":"pntd.0008596.ref082","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1038\/nm.3887","article-title":"Diabetes primes neutrophils to undergo NETosis, which impairs wound healing","volume":"21","author":"SL Wong","year":"2015","journal-title":"Nat Med"},{"issue":"29","key":"pntd.0008596.ref083","doi-asserted-by":"crossref","first-page":"24330","DOI":"10.1074\/jbc.M112.356303","article-title":"Matrix metalloprotease-1a promotes tumorigenesis and metastasis","volume":"287","author":"CJ Foley","year":"2012","journal-title":"J Biol Chem"},{"issue":"2","key":"pntd.0008596.ref084","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.cell.2009.02.018","article-title":"Platelet matrix metalloprotease-1 mediates thrombogenesis by activating PAR1 at a cryptic ligand site","volume":"137","author":"V Trivedi","year":"2009","journal-title":"Cell"},{"issue":"1","key":"pntd.0008596.ref085","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1023\/A:1014465611487","article-title":"Importance of metalloproteinases and macrophages in viper snake envenomation-induced local inflammation","volume":"26","author":"EP Costa","year":"2002","journal-title":"Inflammation"}],"updated-by":[{"DOI":"10.1371\/journal.pntd.0008596","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2021,2,12]],"date-time":"2021-02-12T00:00:00Z","timestamp":1613088000000}}],"container-title":["PLOS Neglected Tropical Diseases"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0008596","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,2,12]],"date-time":"2021-02-12T17:02:51Z","timestamp":1613149371000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0008596"}},"subtitle":[],"editor":[{"given":"Stuart Robert","family":"Ainsworth","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2021,2,2]]},"references-count":85,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2021,2,2]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pntd.0008596","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2020.07.17.208348","asserted-by":"object"}]},"ISSN":["1935-2735"],"issn-type":[{"value":"1935-2735","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,2,2]]}}}