{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T21:58:33Z","timestamp":1793051913371,"version":"4.5.0"},"reference-count":92,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2014,2,13]],"date-time":"2014-02-13T00:00:00Z","timestamp":1392249600000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosntds.org"],"crossmark-restriction":false},"short-container-title":["PLoS Negl Trop Dis"],"DOI":"10.1371\/journal.pntd.0002693","type":"journal-article","created":{"date-parts":[[2014,2,13]],"date-time":"2014-02-13T16:55:04Z","timestamp":1392310504000},"page":"e2693","update-policy":"https:\/\/doi.org\/10.1371\/journal.pntd.corrections_policy","source":"Crossref","is-referenced-by-count":51,"title":["Molecular, Immunological, and Biological Characterization of Tityus serrulatus Venom Hyaluronidase: New Insights into Its Role in Envenomation"],"prefix":"10.1371","volume":"8","author":[{"given":"Carolina Campolina Rebello","family":"Horta","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B\u00e1rbara de Freitas","family":"Magalh\u00e3es","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"B\u00e1rbara Bruna Ribeiro","family":"Oliveira-Mendes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anderson Oliveira do","family":"Carmo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Clara Guerra","family":"Duarte","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liza Figueiredo","family":"Felicori","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ricardo Andrez","family":"Machado-de-\u00c1vila","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carlos","family":"Ch\u00e1vez-Ol\u00f3rtegui","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Evanguedes","family":"Kalapothakis","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2014,2,13]]},"reference":[{"key":"ref1","unstructured":"World Health Organization (WHO) (2007) Rabies and envenoming: a neglected public health issue: report of a Consultative Meeting. Geneva: World Health Organization. 36 p."},{"key":"ref2","unstructured":"Academia Brasileira de Ci\u00eancias (ABC) (2010) Doen\u00e7as negligenciadas. Ci\u00eancia e Tecnologia para o Desenvolvimento Nacional: Estudos Estrat\u00e9gicos.\/Souza W, coordinator. Rio de Janeiro: Academia Brasileira de Ci\u00eancias. 56 p."},{"key":"ref3","unstructured":"Brazilian Ministry of Health (2013) Acidentes por escorpi\u00f5es. Available: <ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/portalsaude.saude.gov.br\/portalsaude\/texto\/5818\/783\/acidentes-por-escorpioes.html\" xlink:type=\"simple\">http:\/\/portalsaude.saude.gov.br\/portalsaude\/texto\/5818\/783\/acidentes-por-escorpioes.html<\/ext-link>. Accessed 15 July 2013."},{"key":"ref4","unstructured":"Brazilian Ministry of Health (2013) Acidentes por serpentes. Available: <ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"uri\" xlink:href=\"http:\/\/portalsaude.saude.gov.br\/portalsaude\/texto\/5817\/783\/acidentes-por-serpentes.html\" xlink:type=\"simple\">http:\/\/portalsaude.saude.gov.br\/portalsaude\/texto\/5817\/783\/acidentes-por-serpentes.html<\/ext-link>. Accessed 15 July 2013."},{"key":"ref5","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1590\/S0104-79301995000200002","article-title":"Scorpions, scorpionism, life history strategies and parthenogenesis","volume":"1","author":"WR Louren\u00e7o","year":"1995","journal-title":"J Venom Anim Toxins Incl Trop Dis"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1590\/S1678-91992008000100003","article-title":"Parthenogenesis in scorpions: some history \u2013 new data","volume":"14","author":"WR Louren\u00e7o","year":"2008","journal-title":"J Venom Anim Toxins Incl Trop Dis"},{"key":"ref7","first-page":"10","article-title":"\u00d3bitos por escorpionismo no Brasil (1990\u20131993)","volume":"28","author":"JL Cardoso","year":"1995","journal-title":"Rev Soc Bras Med Trop"},{"key":"ref8","unstructured":"Brazilian Ministry of Health (2001) Manual de diagn\u00f3stico e tratamento de acidentes por animais pe\u00e7onhentos. Funda\u00e7\u00e3o Nacional de Sa\u00fade. 2<sup>a<\/sup> edi\u00e7\u00e3o revisada - Bras\u00edlia: Funda\u00e7\u00e3o Nacional de Sa\u00fade. 120 p."},{"key":"ref9","doi-asserted-by":"crossref","unstructured":"Campos JA, Silva OA, Lopez M, Freire-Maia L (1980) Signs, symptoms and treatment of severe scorpion sting in children. In: Eaker D, Wodstrom T, editors. Natural Toxins. Oxford: Pergamon Press. pp. 61\u201368.","DOI":"10.1016\/B978-0-08-024952-0.50011-9"},{"key":"ref10","unstructured":"Brazilian Ministry of Health (2009) Manual de controle de escorpi\u00f5es. Minist\u00e9rio da Sa\u00fade, Secretaria de Vigil\u00e2ncia em Sa\u00fade, Departamento de Vigil\u00e2ncia Epidemiol\u00f3gica. \u2013 Bras\u00edlia: Minist\u00e9rio da Sa\u00fade. 72 p."},{"key":"ref11","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1016\/S0041-0101(99)00138-5","article-title":"Induction of neutralizing antibodies against <italic>Tityus serrulatus<\/italic> toxins by immunization with a recombinant nontoxic protein","volume":"38","author":"SC Guatimosim","year":"2000","journal-title":"Toxicon"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.toxicon.2004.04.015","article-title":"Molecular characterization of protective antibodies raised in mice by <italic>Tityus serrulatus<\/italic> scorpion venom toxins conjugated to bovine serum albumin","volume":"44","author":"RA Machado de Avila","year":"2004","journal-title":"Toxicon"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"617","DOI":"10.1016\/j.toxicon.2004.07.019","article-title":"Epitope mapping of the antigenic protein TsNTxP from <italic>Tityus serrulatus<\/italic> scorpion venom using mouse, rabbit and sheep antibodies","volume":"44","author":"TM Mendes","year":"2004","journal-title":"Toxicon"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1016\/j.toxicon.2005.07.014","article-title":"Molecular characterization of a neutralizing murine monoclonal antibody against <italic>Tityus serrulatus<\/italic> scorpion venom","volume":"46","author":"LM Alvarenga","year":"2005","journal-title":"Toxicon"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.toxicon.2008.08.005","article-title":"Effective <italic>Tityus serrulatus<\/italic> anti-venom produced using the Ts1 component","volume":"52","author":"TM Mendes","year":"2008","journal-title":"Toxicon"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"1168","DOI":"10.1016\/j.vaccine.2009.11.039","article-title":"<italic>In vivo<\/italic> protection against <italic>Tityus serrulatus<\/italic> scorpion venom by antibodies raised against a discontinuous synthetic epitope","volume":"28","author":"CG Duarte","year":"2010","journal-title":"Vaccine"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"210","DOI":"10.4236\/ojgen.2012.24027","article-title":"Transcriptome analysis of the <italic>Tityus serrulatus<\/italic> scorpion venom gland","volume":"2","author":"ER Alvarenga","year":"2012","journal-title":"Open Journal of Genetics"},{"key":"ref18","unstructured":"Diniz CR (1978) Chemical and pharmacological aspects of <italic>Tityinae<\/italic> venom. In: Bettini S, editor. Arthropod Venoms. Berlin: Springer-Verlag. pp. 379\u2013394."},{"key":"ref19","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1016\/S0006-291X(80)80082-9","article-title":"Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes","volume":"95","author":"E Jover","year":"1980","journal-title":"Biochem Biophys Res Commun"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1007\/BF02906497","article-title":"Purification and chemical characterization of the major toxins from the venom of the Brazilian scorpion <italic>Tityus serrulatus<\/italic> Lutz and Mello","volume":"46","author":"LD Possani","year":"1981","journal-title":"Carlsberg Res Commun"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"831","DOI":"10.1016\/j.toxicon.2005.09.006","article-title":"Overview of scorpion toxins specific for Na+ channels and related peptides: biodiversity, structure\u2013function relationships and evolution","volume":"46","author":"RC Rodr\u00edguez de la Vega","year":"2005","journal-title":"Toxicon"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"920","DOI":"10.2174\/092986609788923329","article-title":"<italic>Tityus serrulatus<\/italic> scorpion venom and toxins: an overview","volume":"16","author":"CT Cologna","year":"2009","journal-title":"Protein Pept Lett"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1111\/j.1742-4658.2012.08545.x","article-title":"Investigation of the relationship between the structure and function of Ts2, a neurotoxin from <italic>Tityus serrulatus<\/italic> venom","volume":"279","author":"CT Cologna","year":"2012","journal-title":"FEBS J"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/0041-0101(82)90240-9","article-title":"Epidemiological and clinical characteristics of the scorpion envenomation in Tunisia","volume":"20","author":"M Goyffon","year":"1982","journal-title":"Toxicon"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"256","DOI":"10.1016\/j.brainres.2008.08.016","article-title":"Carbamazepine is effective in the treatment of 21-day-old Wistar rats injected with <italic>Tityus serrulatus<\/italic> crude venom","volume":"1239","author":"PA Guidine","year":"2008","journal-title":"Brain Res"},{"key":"ref26","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.neulet.2009.08.006","article-title":"Central effects of <italic>Tityus serrulatus<\/italic> and <italic>Tityus bahiensis<\/italic> scorpion venoms after intraperitoneal injection in rats","volume":"463","author":"AL Nencioni","year":"2009","journal-title":"Neurosci Lett"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1016\/j.toxicon.2009.02.002","article-title":"Effects of <italic>Tityus serrulatus<\/italic> scorpion venom on lung mechanics and inflammation in mice","volume":"53","author":"AC Paneque Peres","year":"2009","journal-title":"Toxicon"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/S0165-6147(99)01398-X","article-title":"A unified nomenclature for short-chain peptides isolated from scorpion venoms: alpha-KTx molecular subfamilies","volume":"20","author":"J Tytgat","year":"1999","journal-title":"Trends Pharmacol Sci"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.toxicon.2004.03.022","article-title":"Current views on scorpion toxins specific for K<sup>+<\/sup>-channels","volume":"43","author":"RC Rodr\u00edguez de la Vega","year":"2004","journal-title":"Toxicon"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.toxicon.2011.05.001","article-title":"Purification and characterization of Ts15, the first member of a new \u03b1-KTX subfamily from the venom of the Brazilian scorpion <italic>Tityus serrulatus<\/italic>","volume":"58","author":"CT Cologna","year":"2011","journal-title":"Toxicon"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.toxicon.2008.07.010","article-title":"<italic>Tityus serrulatus<\/italic> venom peptidomics: assessing venom peptide diversity","volume":"52","author":"B Rates","year":"2008","journal-title":"Toxicon"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"585","DOI":"10.2174\/138920309789630589","article-title":"Anionic antimicrobial peptides from eukaryotic organisms","volume":"10","author":"F Harris","year":"2009","journal-title":"Curr Protein Pept Sci"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/j.bbrc.2008.04.104","article-title":"<italic>Tityus serrulatus<\/italic> hypotensins: A new family of peptides from scorpion venom","volume":"371","author":"T Verano-Braga","year":"2008","journal-title":"Biochem Biophys Res Commun"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1016\/j.toxicon.2010.04.006","article-title":"Structure-function studies of <italic>Tityus serrulatus<\/italic> Hypotensin-I (TsHpt-I): A new agonist of B(2) kinin receptor","volume":"56","author":"T Verano-Braga","year":"2010","journal-title":"Toxicon"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"7405","DOI":"10.1074\/jbc.M109.028365","article-title":"Vesicle-associated membrane protein (VAMP) cleavage by a new metalloprotease from the Brazilian scorpion <italic>Tityus serrulatus<\/italic>","volume":"285","author":"PL Fletcher","year":"2010","journal-title":"J Biol Chem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1016\/j.toxicon.2013.02.012","article-title":"Enzymatic properties of venoms from Brazilian scorpions of <italic>Tityus<\/italic> genus and the neutralisation potential of therapeutical antivenoms","volume":"69","author":"EJ Venancio","year":"2013","journal-title":"Toxicon"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/0305-0491(83)90086-X","article-title":"Characterization of lizard venom hyaluronidase and evidence for its action as a spreading factor","volume":"76","author":"AT Tu","year":"1983","journal-title":"Comp Biochem Physiol B Biochem Mol Biol"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1111\/j.1432-1033.1984.tb07997.x","article-title":"The purification and characterization of hyaluronidase from the venom of the honey bee, <italic>Apis mellifera<\/italic>","volume":"139","author":"DM Kemeny","year":"1984","journal-title":"Eur J Biochem"},{"key":"ref39","first-page":"301","article-title":"Isolation and characterisation of hyaluronidase from scorpion (<italic>Heterometrus fulvipus<\/italic>) venom","volume":"20","author":"M Ramanaiah","year":"1990","journal-title":"Biochemistry International"},{"key":"ref40","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"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1223","DOI":"10.1016\/j.toxicon.2012.08.018","article-title":"Identification, cDNA cloning and heterologous expression of a hyaluronidase from the tarantula <italic>Brachypelma vagans<\/italic> venom","volume":"60","author":"H Clement","year":"2012","journal-title":"Toxicon"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"e2206","DOI":"10.1371\/journal.pntd.0002206","article-title":"A novel hyaluronidase from brown spider (<italic>Loxosceles intermedia<\/italic>) venom (Dietrich&apos;s hyaluronidase): from cloning to functional characterization","volume":"7","author":"VP Ferrer","year":"2013","journal-title":"PLoS Negl Trop Dis"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.toxicon.2012.12.019","article-title":"Hyaluronidase from the venom of the social wasp <italic>Polybia paulista<\/italic> (Hymenoptera, Vespidae): Cloning, structural modeling, purification, and immunological analysis","volume":"64","author":"DLJ Jacomini","year":"2013","journal-title":"Toxicon"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.biochi.2004.02.004","article-title":"Isolation and characterization of hyaluronidase a \u201cspreading factor\u201d from Indian cobra (<italic>Naja naja<\/italic>) venom","volume":"86","author":"KS Girish","year":"2004","journal-title":"Biochimie"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1921","DOI":"10.1016\/j.lfs.2007.02.037","article-title":"The magic glue hyaluronan and its eraser hyaluronidase: a biological overview","volume":"80","author":"KS Girish","year":"2007","journal-title":"Life Sci"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0041-0101(87)90170-X","article-title":"What is the treatment for the cardiovascular manifestations of scorpion envenomation?","volume":"25","author":"M Gueron","year":"1987","journal-title":"Toxicon"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"1119","DOI":"10.1016\/0041-0101(96)00074-8","article-title":"Body distribution of <italic>Tityus serrulatus<\/italic> scorpion venom in mice and effects of scorpion antivenom","volume":"34","author":"MP Revelo","year":"1996","journal-title":"Toxicon"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"394","DOI":"10.1016\/0003-9861(77)90053-4","article-title":"Purification and properties of mammalian toxins from the Brazilian scorpion <italic>Tityus serrulatus<\/italic> Lutz and Mello","volume":"180","author":"LD Possani","year":"1977","journal-title":"Arch Biochem Biophys"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"1495","DOI":"10.1016\/S0041-0101(01)00122-2","article-title":"A hyaluronidase from <italic>Tityus serrulatus<\/italic> scorpion venom: isolation, characterization and inhibition by flavonoids","volume":"39","author":"AC Pessini","year":"2001","journal-title":"Toxicon"},{"key":"ref50","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"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1016\/S0041-0101(00)00194-X","article-title":"Screening of expression libraries using ELISA: identification of immunogenic proteins from <italic>Tityus bahiensis<\/italic> and <italic>Tityus serrulatus<\/italic> venom","volume":"39","author":"E Kalapothakis","year":"2001","journal-title":"Toxicon"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"474","DOI":"10.1016\/j.toxicon.2010.04.009","article-title":"Cloning and molecular characterization of BmHYA1, a novel hyaluronidase from the venom of Chinese red scorpion <italic>Buthus martensi<\/italic> Karsch","volume":"56","author":"L Feng","year":"2010","journal-title":"Toxicon"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"3569","DOI":"10.1073\/pnas.90.8.3569","article-title":"Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm","volume":"90","author":"M Gmachl","year":"1993","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"6911","DOI":"10.1021\/bi700382g","article-title":"Structure of human hyaluronidase-1, a hyaluronan hydrolyzing enzyme involved in tumor growth and angiogenesis","volume":"46","author":"KL Chao","year":"2007","journal-title":"Biochemistry"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"2731","DOI":"10.1093\/molbev\/msr121","article-title":"MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods","volume":"28","author":"K Tamura","year":"2011","journal-title":"Molecular Biology and Evolution"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1186\/1471-2105-9-500","article-title":"Prediction of glycosylation sites using random forests","volume":"9","author":"SE Hamby","year":"2008","journal-title":"BMC Bioinformatics"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"629","DOI":"10.1016\/0041-0101(88)90245-0","article-title":"The hyaluronidase activities of some Southeast Asian snake venoms","volume":"26","author":"S Pukrittayakamee","year":"1988","journal-title":"Toxicon"},{"key":"ref58","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":"UK Laemmli","year":"1970","journal-title":"Nature"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1016\/S0041-0101(96)00133-X","article-title":"Neutralizing capacity of antibodies elicited by a non-toxic protein purified from the venom of the scorpion <italic>Tityus serrulatus<\/italic>","volume":"35","author":"C Ch\u00e1vez-Ol\u00f3rtegui","year":"1997","journal-title":"Toxicon"},{"key":"ref60","unstructured":"Karber C (1937) Karber&apos;s method of determining LD<sub>50<\/sub>. In: Burn JH, editor. Biological Standardization. London: Oxford University Press. pp. 37\u201340."},{"key":"ref61","first-page":"948","article-title":"Inhibition of <italic>Naja naja<\/italic> venom hyaluronidase by plant-derived bioactive components and polysaccharides","volume":"70","author":"KS Girish","year":"2005","journal-title":"Biochemistry"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/S0022-1759(02)00140-0","article-title":"Application of the Spot method to the identification of peptides and amino acids from the antibody paratope that contribute to antigen binding","volume":"267","author":"D Laune","year":"2002","journal-title":"J Immunol Methods"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"9217","DOI":"10.1016\/S0040-4020(01)85612-X","article-title":"Spot-synthesis: an easy technique for the positionally addressable, parallel chemical synthesis on a membrane support","volume":"48","author":"R Frank","year":"1992","journal-title":"Tetrahedron"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"4673","DOI":"10.1093\/nar\/22.22.4673","article-title":"ClustalW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice","volume":"22","author":"JD Thompson","year":"1994","journal-title":"Nucleic Acids Res"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"1025","DOI":"10.1016\/S0969-2126(00)00511-6","article-title":"Structure of hyaluronidase, a major allergen of bee venom","volume":"8","author":"Z Markovic-Housley","year":"2000","journal-title":"Structure"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"2577","DOI":"10.1002\/bip.360221211","article-title":"Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features","volume":"22","author":"W Kabsch","year":"1983","journal-title":"Biopolymers"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1006\/jmbi.1993.1626","article-title":"Comparative protein modelling by satisfaction of spatial restraints","volume":"234","author":"A Sali","year":"1993","journal-title":"J Mol Biol"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"W407","DOI":"10.1093\/nar\/gkm290","article-title":"ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins","volume":"35","author":"M Wiederstein","year":"2007","journal-title":"Nucleic Acids Res"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"W555","DOI":"10.1093\/nar\/gkq395","article-title":"3V: cavity, channel and cleft volume calculator and extractor","volume":"38","author":"NR Voss","year":"2010","journal-title":"Nucleic Acids Res"},{"key":"ref70","unstructured":"Delano WL (2002) The PyMOL Molecular Graphics System DeLano Scientific. Palo Alto, California."},{"key":"ref71","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1021\/cr050247k","article-title":"Hyaluronidases: their genomics, structures, and mechanisms of action","volume":"106","author":"R Stern","year":"2006","journal-title":"Chem Rev"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"764","DOI":"10.1093\/glycob\/cwt016","article-title":"Chemoenzymatic synthesis of glycosaminoglycans: Re-creating, re-modeling and re-designing nature&apos;s longest or most complex carbohydrate chains","volume":"23","author":"PL DeAngelis","year":"2013","journal-title":"Glycobiology"},{"key":"ref73","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"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1016\/j.semcancer.2008.03.008","article-title":"Hyalurondiase: both a tumor promoter and suppressor","volume":"18","author":"VB Lokeshwar","year":"2008","journal-title":"Semin Cancer Biol"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1152\/physrev.00052.2009","article-title":"Hyaluronan as an immune regulator in human diseases","volume":"91","author":"D Jiang","year":"2011","journal-title":"Physiol Rev"},{"key":"ref76","unstructured":"Meyer K (1971) Hyaluronidases. In: Boyer PD, editor. The Enzymes, third edition, volume V. New York: Academic Press. pp. 307\u2013320."},{"key":"ref77","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/0305-0491(92)90172-N","article-title":"Purification and partial characterization of hyaluronidase from stonefish (<italic>Synanceja horrida<\/italic>) venom","volume":"101","author":"CH Poh","year":"1992","journal-title":"Comp Biochem Physiol B"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1002\/pro.5560040902","article-title":"Hyaluronidases - a group of neglected enzymes","volume":"4","author":"G Kreil","year":"1995","journal-title":"Protein Sci"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1016\/j.toxicon.2012.09.009","article-title":"A brief review of the scientific history of several lesser-known snake venom proteins: L-amino acid oxidases, hyaluronidases and phosphodiesterases","volume":"62","author":"JW Fox","year":"2013","journal-title":"Toxicon"},{"key":"ref80","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/S0945-053X(01)00172-X","article-title":"The six hyaluronidase-like genes in the human and mouse genomes","volume":"20","author":"AB Csoka","year":"2001","journal-title":"Matrix Biol"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1111\/j.1432-1033.1997.t01-1-00810.x","article-title":"<italic>In vitro<\/italic> mutagenesis of PH-20 hyaluronidase from human sperm","volume":"247","author":"S Arming","year":"1997","journal-title":"Eur J Biochem"},{"key":"ref82","doi-asserted-by":"crossref","first-page":"7954","DOI":"10.1021\/ja970674i","article-title":"Substrate-assisted catalysis unifies two families of chitinolytic enzymes","volume":"119","author":"I Tews","year":"1997","journal-title":"J Am Chem Soc"},{"key":"ref83","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1002\/prot.20592","article-title":"Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis","volume":"61","author":"MJ Jedrzejas","year":"2005","journal-title":"Proteins (Structure Function and Bioinformatics)"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"1433","DOI":"10.1016\/j.lfs.2005.07.015","article-title":"Inhibition of <italic>Naja naja<\/italic> venom hyaluronidase: role in the management of poisonous bite","volume":"78","author":"KS Girish","year":"2006","journal-title":"Life Sci"},{"key":"ref85","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.jep.2009.05.028","article-title":"Local uses of <italic>Aristolochia<\/italic> species and content of nephrotoxic aristolochic acid 1 and 2\u2013a global assessment based on bibliographic sources","volume":"125","author":"M Heinrich","year":"2009","journal-title":"J Ethnopharmacol"},{"key":"ref86","doi-asserted-by":"crossref","first-page":"2261","DOI":"10.2174\/092986709788453078","article-title":"Hyaluronidase inhibitors: a biological and therapeutic perspective","volume":"16","author":"KS Girish","year":"2009","journal-title":"Curr Med Chem"},{"key":"ref87","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/0041-0101(87)90156-5","article-title":"Interaction of phospholipase A2 from <italic>Vipera russelli<\/italic> venom with aristolochic acid: a circular dichroism study","volume":"25","author":"BS Vishwanath","year":"1987","journal-title":"Toxicon"},{"key":"ref88","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1007\/BF00914317","article-title":"Edema-inducing activity of phospholipase A2 purified from human synovial fluid and inhibition by aristolochic acid","volume":"12","author":"BS Vishwanath","year":"1988","journal-title":"Inflammation"},{"key":"ref89","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0162-3109(93)90061-T","article-title":"Effect of aristolochic acid on arachidonic acid cascade and <italic>in vivo<\/italic> models of inflammation","volume":"26","author":"JJ Moreno","year":"1993","journal-title":"Immunopharmacology"},{"key":"ref90","unstructured":"Gowda TV (1997) Interaction of snake venom phospholipases A2 with plant isolates. In: Kini RM, editor. Venom Phospholipase A2 Enzymes: Structure, Function and Mechanism. Chichester, England: John Wiley and Sons. pp. 205\u201321."},{"key":"ref91","doi-asserted-by":"crossref","first-page":"1015","DOI":"10.1016\/0041-0101(85)90397-6","article-title":"Neutralization of hyaluronidase and indirect hemolytic activities of Costa Rican snake venoms by a polyvalent antivenom","volume":"23","author":"JA Gen\u00e9","year":"1985","journal-title":"Toxicon"},{"key":"ref92","doi-asserted-by":"crossref","first-page":"635","DOI":"10.1016\/j.toxicon.2003.09.001","article-title":"Hyaluronidase inhibitors (sodium cromoglycate and sodium auro-thiomalate) reduce the local tissue damage and prolong the survival time of mice injected with <italic>Naja kaouthia<\/italic> and <italic>Calloselasma rhodostoma<\/italic> venoms","volume":"42","author":"S Yingprasertchai","year":"2003","journal-title":"Toxicon"}],"container-title":["PLoS Neglected Tropical Diseases"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pntd.0002693","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,3,26]],"date-time":"2022-03-26T11:16:05Z","timestamp":1648293365000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pntd.0002693"}},"subtitle":[],"editor":[{"given":"Jean-Philippe","family":"Chippaux","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2014,2,13]]},"references-count":92,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2014,2,13]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pntd.0002693","relation":{},"ISSN":["1935-2735"],"issn-type":[{"value":"1935-2735","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,2,13]]}}}