{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T04:14:04Z","timestamp":1777436044975,"version":"3.51.4"},"reference-count":69,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2017,7,1]],"date-time":"2017-07-01T00:00:00Z","timestamp":1498867200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2017,7,1]],"date-time":"2017-07-01T00:00:00Z","timestamp":1498867200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2018,6,16]],"date-time":"2018-06-16T00:00:00Z","timestamp":1529107200000},"content-version":"am","delay-in-days":350,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Science Foundation of China","doi-asserted-by":"publisher","award":["30870303"],"award-info":[{"award-number":["30870303"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100007128","name":"Natural Science Foundation of Shaanxi Province","doi-asserted-by":"publisher","award":["2013JC2-26"],"award-info":[{"award-number":["2013JC2-26"]}],"id":[{"id":"10.13039\/501100007128","id-type":"DOI","asserted-by":"publisher"}]},{"name":"National Innovation and Training Programs","award":["CX16030"],"award-info":[{"award-number":["CX16030"]}]},{"DOI":"10.13039\/501100001869","name":"Academia Sinica","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001869","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001868","name":"National Science Council of Taiwan","doi-asserted-by":"publisher","award":["99-2311-B001-016"],"award-info":[{"award-number":["99-2311-B001-016"]}],"id":[{"id":"10.13039\/501100001868","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":[[2017,7]]},"DOI":"10.1016\/j.jprot.2017.05.024","type":"journal-article","created":{"date-parts":[[2017,5,29]],"date-time":"2017-05-29T12:15:42Z","timestamp":1496060142000},"page":"19-32","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":9,"special_numbering":"C","title":["Serine protease isoforms in Gloydius intermedius venom: Full sequences, molecular phylogeny and evolutionary implications"],"prefix":"10.1016","volume":"164","author":[{"given":"Zhang-Min","family":"Yang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hui","family":"Yu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhen-Zhen","family":"Liu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jian-Zhu","family":"Pei","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yu-E","family":"Yang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Su-Xian","family":"Yan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Cui","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Wen-long","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Zhe-Zhi","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ying-Ming","family":"Wang","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Inn-Ho","family":"Tsai","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jprot.2017.05.024_bb0005","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0014-5793(96)01144-1","article-title":"Accelerated evolution of crotalinae snake venom gland serine proteinases","volume":"397","author":"Deshimaru","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2017.05.024_bb0010","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1186\/1471-2199-8-115","article-title":"The venom gland transcriptome of the desert massasauga rattlesnake (Sistrurus catenatus edwardsii): towards an understanding of venom composition among advanced snakes (superfamily Colubroidea)","volume":"8","author":"Pahari","year":"2007","journal-title":"BMC Mol. Biol."},{"key":"10.1016\/j.jprot.2017.05.024_bb0015","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.toxicon.2015.02.015","article-title":"The transcriptomic and proteomic basis for the evolution of a novel venom phenotype within the timber rattlesnake (Crotalus horridus)","volume":"98","author":"Rokyta","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0020","doi-asserted-by":"crossref","first-page":"790","DOI":"10.1186\/1471-2164-14-790","article-title":"Quantitative high-throughput profiling of snake venom gland transcriptomes and proteomes (Ovophis okinavensis and Protobothrops flavoviridis)","volume":"14","author":"Aird","year":"2013","journal-title":"BMC Genomics"},{"key":"10.1016\/j.jprot.2017.05.024_bb0025","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/j.jprot.2013.11.001","article-title":"Linking the transcriptome and proteome to characterize the venom of the eastern diamondback rattlesnake (Crotalus adamanteus)","volume":"96","author":"Margres","year":"2014","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2017.05.024_bb0030","series-title":"Toxins and Hemostasis: From Bench to Bedside","first-page":"519","article-title":"Thrombin-like enzymes in snake venoms","author":"Mackessy","year":"2010"},{"key":"10.1016\/j.jprot.2017.05.024_bb0035","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1080\/15569540600567321","article-title":"Current status of snake venom thrombin-like enzymes","volume":"25","author":"Castro","year":"2006","journal-title":"Toxin Rev."},{"key":"10.1016\/j.jprot.2017.05.024_bb0040","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj3540161","article-title":"Serine proteinase isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis","volume":"354","author":"Wang","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.jprot.2017.05.024_bb0045","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/j.toxicon.2008.07.014","article-title":"Amino acid sequence of a kinin-releasing enzyme, KR-E-1, from the venom of Agkistrodon caliginosus (Kankoku-mamushi)","volume":"52","author":"Oyama","year":"2008","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0050","doi-asserted-by":"crossref","first-page":"10246","DOI":"10.1074\/jbc.270.17.10246","article-title":"A novel plasminogen activator from snake venom: purification, characterization, and molecular cloning","volume":"270","author":"Zhang","year":"1995","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0055","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1007\/s10930-006-9001-z","article-title":"Characterization of a new platelet aggregating factor from Crotalus durissus cascavella venom","volume":"25","author":"Fonseca","year":"2006","journal-title":"Protein J."},{"key":"10.1016\/j.jprot.2017.05.024_bb0060","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/S0014-5793(00)01803-2","article-title":"Interaction of viper venom serine peptidases with thrombin receptors on human platelets","volume":"477","author":"Santos","year":"2000","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2017.05.024_bb0065","doi-asserted-by":"crossref","first-page":"39309","DOI":"10.1074\/jbc.M508502200","article-title":"Thrombomodulin-independent activation of protein C and specificity of hemostatically active snake venom serine proteinases: crystal structures of native and inhibited Agkistrodon contortrix contortrix protein C activator","volume":"280","author":"Murakami","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0070","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1046\/j.1365-2567.2002.01490.x","article-title":"Flavoxobin, a serine protease from Trimeresurus flavoviridis (habu snake) venom, independently cleaves Arg726-Ser727 of human C3 and acts as a novel, heterologous C3 convertase","volume":"107","author":"Yamamoto","year":"2002","journal-title":"Immunology"},{"key":"10.1016\/j.jprot.2017.05.024_bb0075","first-page":"241","article-title":"Factor V activation and inactivation by venom proteases","volume":"31","author":"Rosing","year":"2001","journal-title":"Haemostasis"},{"key":"10.1016\/j.jprot.2017.05.024_bb0080","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1097\/00001721-200011020-00005","article-title":"The cleavage and inactivation of plasminogen activator inhibitor type 1 and alpha2-antiplasmin by reptilase, a thrombin-like venom enzyme","volume":"11","author":"Urano","year":"2000","journal-title":"Blood Coagul. Fibrinolysis"},{"key":"10.1016\/j.jprot.2017.05.024_bb0085","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/j.biochi.2013.04.006","article-title":"Cotiarinase is a novel prothrombin activator from the venom of Bothrops cotiara","volume":"95","author":"Kitano","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.jprot.2017.05.024_bb0090","doi-asserted-by":"crossref","first-page":"763","DOI":"10.6026\/97320630008563","article-title":"Sequence and phylogenetic analysis of viper venom serine proteases","volume":"8","author":"Vaiyapuri","year":"2012","journal-title":"Bioinformation"},{"key":"10.1016\/j.jprot.2017.05.024_bb0095","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/j.jprot.2014.09.009","article-title":"Structures and functions of crotoxin-like heterodimers and acidic phospholipases A2 from Gloydius intermedius venom: insights into the origin of neurotoxic-type rattlesnakes","volume":"112","author":"Yang","year":"2015","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2017.05.024_bb0100","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1016\/j.toxicon.2015.08.010","article-title":"Transcriptome and proteome of the highly neurotoxic venom of Gloydius intermedius","volume":"107","author":"Yang","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0105","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.toxicon.2009.03.022","article-title":"Cloning of serine protease cDNAs from Crotalus durissus terrificus venom gland and expression of a functional gyroxin homologue in COS-7 cells","volume":"54","author":"Yonamine","year":"2009","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0110","doi-asserted-by":"crossref","first-page":"e100354","DOI":"10.1371\/journal.pone.0100354","article-title":"Correlation between the glycan variations and defibrinogenating activities of acutobin and its recombinant glycoforms","volume":"9","author":"Wang","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.jprot.2017.05.024_bb0115","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/978-1-4939-2365-6_3","article-title":"Design of primers and probes for quantitative real-time PCR methods","volume":"1275","author":"Rodr\u00edguez","year":"2015","journal-title":"Methods Mol. Biol."},{"key":"10.1016\/j.jprot.2017.05.024_bb0120","doi-asserted-by":"crossref","first-page":"402","DOI":"10.1006\/meth.2001.1262","article-title":"Analysis of relative gene expression data using real-time quantitative PCR and the 2(-delta deltaC(T))","volume":"25","author":"Livak","year":"2001","journal-title":"Methods"},{"key":"10.1016\/j.jprot.2017.05.024_bb0125","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0130","series-title":"PHYLIP: The PHYLogeny Inference Package, Version 3.573","author":"Felsenstein","year":"1992"},{"key":"10.1016\/j.jprot.2017.05.024_bb0135","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1111\/j.1558-5646.1985.tb00420.x","article-title":"Confidence limits on phylogenies: an approach using the bootstrap","volume":"39","author":"Felsenstein","year":"1985","journal-title":"Evolution"},{"key":"10.1016\/j.jprot.2017.05.024_bb0140","doi-asserted-by":"crossref","first-page":"1195","DOI":"10.1016\/S0969-2126(98)00119-1","article-title":"The crystal structure of the novel snake venom plasminogen activator TSV-PA: a prototype structure for snake venom serine proteinases","volume":"6","author":"Parry","year":"1998","journal-title":"Structure"},{"key":"10.1016\/j.jprot.2017.05.024_bb0145","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1093\/glycob\/cwh004","article-title":"Biases and complex patterns in the residues flanking protein N-glycosylation sites","volume":"14","author":"Ben-Dor","year":"2004","journal-title":"Glycobiology"},{"key":"10.1016\/j.jprot.2017.05.024_bb0150","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S0167-4838(01)00177-7","article-title":"Structural features of a snake venom thrombin-like enzyme: thrombin and trypsin on a single catalytic platform?","volume":"1547","author":"Castro","year":"2001","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jprot.2017.05.024_bb0155","doi-asserted-by":"crossref","first-page":"10294","DOI":"10.1021\/bi000145i","article-title":"A novel venombin B from Agkistrodon contortrix contortrix: evidence for recognition properties in the surface around the primary specificity pocket different from thrombin","volume":"39","author":"Amiconi","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.jprot.2017.05.024_bb0160","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.ympev.2008.08.019","article-title":"A nesting of vipers: phylogeny and historical biogeography of the Viperidae (Squamata: Serpentes)","volume":"49","author":"W\u00fcster","year":"2008","journal-title":"Mol. Phylogenet. Evol."},{"key":"10.1016\/j.jprot.2017.05.024_bb0165","doi-asserted-by":"crossref","first-page":"144","DOI":"10.1016\/j.toxicon.2014.11.235","article-title":"First crotoxin-like phospholipase A2 complex from a New World non-rattlesnake species: nigroviriditoxin, from the arboreal neotropical snake Bothriechis nigroviridis","volume":"93","author":"Lomonte","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0170","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1016\/j.jprot.2014.01.019","article-title":"Proteomic and biochemical analyses of short-tailed pit viper (Gloydius brevicaudus) venom: age-related variation and composition-activity correlation","volume":"105","author":"Gao","year":"2014","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2017.05.024_bb0175","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/j.toxicon.2006.06.001","article-title":"Primary structure of a thrombin-like serine protease, kangshuanmei, from the venom of Agkistrodon halys brevicaudus stejneger","volume":"48","author":"Sakai","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0180","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1002\/ar.22670","article-title":"Sequence and bioinformatic characterization of expressed sequence tags originated from Gloydius shedaoensis venom gland","volume":"296","author":"Guo","year":"2013","journal-title":"Anat. Rec."},{"key":"10.1016\/j.jprot.2017.05.024_bb0185","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/j.bbrc.2006.01.006","article-title":"A catalog for transcripts in the venom gland of the Agkistrodon acutus: identification of the toxins potentially involved in coagulopathy","volume":"341","author":"Liu","year":"2006","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jprot.2017.05.024_bb0190","doi-asserted-by":"crossref","first-page":"2098","DOI":"10.1021\/pr0602500","article-title":"Venom proteomes of closely related Sistrurus rattlesnakes with divergent diets","volume":"5","author":"Sanz","year":"2006","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2017.05.024_bb0195","doi-asserted-by":"crossref","first-page":"647","DOI":"10.1186\/s12864-015-1832-6","article-title":"Snake venoms are integrated systems, but abundant venom proteins evolve more rapidly","volume":"16","author":"Aird","year":"2015","journal-title":"BMC Genomics"},{"key":"10.1016\/j.jprot.2017.05.024_bb0200","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1016\/S0041-0101(97)00150-5","article-title":"Characterization of three fibrinogenolytic enzymes from Chinese green tree viper (Trimeresurus stejnegeri) venom","volume":"36","author":"Gao","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0205","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.toxicon.2011.05.014","article-title":"Phylogenetic analysis of serine proteinases 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.2017.05.024_bb0210","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/j.jprot.2013.10.036","article-title":"Venomics of New World pit vipers: genus-wide comparisons of venom proteomes across Agkistrodon","volume":"96","author":"Lomonte","year":"2014","journal-title":"J. Proteome"},{"key":"10.1016\/j.jprot.2017.05.024_bb0215","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1007\/s00204-012-0957-5","article-title":"Crystal structure and activating effect on RyRs of AhV_TL-I, a glycosylated thrombin-like enzyme from Agkistrodon halys snake venom","volume":"87","author":"Zeng","year":"2013","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.jprot.2017.05.024_bb0220","doi-asserted-by":"crossref","first-page":"835","DOI":"10.1093\/oxfordjournals.jbchem.a021319","article-title":"Purification and molecular cloning of calobin, a thrombin-like enzyme from Agkistrodon caliginosus (Korean viper)","volume":"119","author":"Hahn","year":"1996","journal-title":"J. Biochem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0225","doi-asserted-by":"crossref","first-page":"569","DOI":"10.1046\/j.1432-1327.1998.2520569.x","article-title":"Purification and amino acid sequence of halystase from snake venom of Agkistrodon halys blomhoffii, a serine protease that cleaves specifically fibrinogen and kininogen","volume":"252","author":"Matsui","year":"1998","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0230","doi-asserted-by":"crossref","first-page":"2965","DOI":"10.1016\/j.febslet.2007.05.047","article-title":"Identification and characterization of Harobin, a novel fibrinogenolytic serine protease from a sea snake (Lapemis hardwickii)","volume":"581","author":"He","year":"2007","journal-title":"FEBS Lett."},{"key":"10.1016\/j.jprot.2017.05.024_bb0235","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.2017.05.024_bb0240","doi-asserted-by":"crossref","first-page":"1200","DOI":"10.1016\/j.toxicon.2007.02.013","article-title":"Molecular cloning of serine proteases from elapid snake venoms","volume":"49","author":"Jin","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0245","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1074\/mcp.M700094-MCP200","article-title":"Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia)","volume":"7","author":"Fry","year":"2008","journal-title":"Mol. Cell. Proteomics"},{"key":"10.1016\/j.jprot.2017.05.024_bb0250","doi-asserted-by":"crossref","first-page":"527","DOI":"10.1007\/s000180050181","article-title":"What have snakes taught us about integrins?","volume":"54","author":"Huang","year":"1998","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.jprot.2017.05.024_bb0255","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1002\/pro.2189","article-title":"Crystal structure of Jararacussin-I: the highly negatively charged catalytic interface contributes to macromolecular selectivity in snake venom thrombin-like enzymes","volume":"22","author":"Ullah","year":"2013","journal-title":"Protein Sci."},{"key":"10.1016\/j.jprot.2017.05.024_bb0260","doi-asserted-by":"crossref","first-page":"1823","DOI":"10.1074\/jbc.275.3.1823","article-title":"The contribution of residues 192 and 193 to the specificity of snake venom serine proteinases","volume":"275","author":"Braud","year":"2000","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0265","doi-asserted-by":"crossref","first-page":"28063","DOI":"10.1074\/jbc.274.40.28063","article-title":"The C-terminal sequence encodes function in serine proteases","volume":"274","author":"Krem","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0270","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.toxicon.2005.02.020","article-title":"Snake venom serine proteinases: sequence homology vs. substrate specificity, a paradox to be solved","volume":"45","author":"Serrano","year":"2005","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0275","doi-asserted-by":"crossref","first-page":"10524","DOI":"10.1074\/jbc.M412900200","article-title":"Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases","volume":"280","author":"Zhu","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0280","doi-asserted-by":"crossref","first-page":"1365","DOI":"10.1016\/j.toxicon.2010.02.014","article-title":"Bhalternin: functional and structural characterization of a new thrombin-like enzyme from Bothrops alternatus snake venom","volume":"55","author":"Costa Jde","year":"2010","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0285","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1107\/S1744309111022548","article-title":"Structure of saxthrombin, a thrombin-like enzyme from Gloydius saxatilis","volume":"67","author":"Huang","year":"2011","journal-title":"Acta Crystallogr. Sect. F: Struct. Biol. Cryst. Commun."},{"key":"10.1016\/j.jprot.2017.05.024_bb0290","doi-asserted-by":"crossref","first-page":"e86823","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.2017.05.024_bb0295","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1006\/bbrc.2001.4452","article-title":"Fibrinogenolytic proteases isolated from the snake venom of Taiwan habu: serine proteases with kallikrein-like and angiotensin-degrading activities","volume":"281","author":"Hung","year":"2001","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.jprot.2017.05.024_bb0300","first-page":"689","article-title":"Jerdonase, a novel serine protease with kinin-releasing and fibrinogenolytic activity from Trimeresurus jerdonii venom","volume":"35","author":"Jia","year":"2003","journal-title":"Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao"},{"key":"10.1016\/j.jprot.2017.05.024_bb0305","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1021\/pr901042p","article-title":"Snake venomic of Crotalus durissus terrificus\u2013correlation with pharmacological activities","volume":"9","author":"Georgieva","year":"2010","journal-title":"J. Proteome Res."},{"key":"10.1016\/j.jprot.2017.05.024_bb0310","doi-asserted-by":"crossref","first-page":"e0004587","DOI":"10.1371\/journal.pntd.0004587","article-title":"Full-length venom protein cDNA sequences from venom-derived mRNA: exploring compositional variation and adaptive multigene evolution","volume":"10","author":"Modahl","year":"2016","journal-title":"PLoS Negl. Trop. Dis."},{"key":"10.1016\/j.jprot.2017.05.024_bb0315","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.toxicon.2015.09.023","article-title":"Proteomic analysis of the rare Uracoan rattlesnake Crotalus vegrandis venom: evidence of a broad arsenal of toxins","volume":"107","author":"Viala","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0320","doi-asserted-by":"crossref","first-page":"2434","DOI":"10.1016\/j.cub.2016.07.038","article-title":"The deep origin and recent loss of venom toxin genes in rattlesnakes","volume":"26","author":"Dowell","year":"2016","journal-title":"Curr. Biol."},{"key":"10.1016\/j.jprot.2017.05.024_bb0325","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1016\/S1097-2765(02)00821-3","article-title":"N-linked glycans direct the cotranslational folding pathway of influenza hemagglutinin","volume":"11","author":"Daniels","year":"2003","journal-title":"Mol. Cell"},{"key":"10.1016\/j.jprot.2017.05.024_bb0330","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.toxicon.2014.12.008","article-title":"Effects of single N-glycosylation site knockout on folding and defibrinogenating activities of acutobin recombinants from HEK293T","volume":"94","author":"Tsai","year":"2015","journal-title":"Toxicon"},{"key":"10.1016\/j.jprot.2017.05.024_bb0335","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1093\/glycob\/cwq195","article-title":"Terminal disialylated multiantennary complex type N-glycans carried on acutobin define the glycosylation characteristics of the Deinagkistrodon acutus venom","volume":"21","author":"Lin","year":"2011","journal-title":"Glycobiology"},{"key":"10.1016\/j.jprot.2017.05.024_bb0340","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1074\/jbc.M115.691097","article-title":"A single glycan at the 99-loop of human kallikrein related peptidase-2 regulates activation and enzymatic activity","volume":"291","author":"Guo","year":"2016","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jprot.2017.05.024_bb0345","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.toxicon.2005.02.016","article-title":"Practical applications of snake venom toxins in haemostasis","volume":"45","author":"Marsh","year":"2005","journal-title":"Toxicon"}],"container-title":["Journal of Proteomics"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391917301914?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1874391917301914?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,29]],"date-time":"2025-10-29T11:58:07Z","timestamp":1761739087000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1874391917301914"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,7]]},"references-count":69,"alternative-id":["S1874391917301914"],"URL":"https:\/\/doi.org\/10.1016\/j.jprot.2017.05.024","relation":{},"ISSN":["1874-3919"],"issn-type":[{"value":"1874-3919","type":"print"}],"subject":[],"published":{"date-parts":[[2017,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Serine protease isoforms in Gloydius intermedius venom: Full sequences, molecular phylogeny and evolutionary implications","name":"articletitle","label":"Article Title"},{"value":"Journal of Proteomics","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.jprot.2017.05.024","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2017 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}