{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T23:57:10Z","timestamp":1778803030447,"version":"3.51.4"},"reference-count":135,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2018,7,1]],"date-time":"2018-07-01T00:00:00Z","timestamp":1530403200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["International Journal of Biological Macromolecules"],"published-print":{"date-parts":[[2018,7]]},"DOI":"10.1016\/j.ijbiomac.2018.03.164","type":"journal-article","created":{"date-parts":[[2018,3,28]],"date-time":"2018-03-28T06:12:46Z","timestamp":1522217566000},"page":"788-811","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":66,"special_numbering":"C","title":["Thrombin-like enzymes from snake venom: Structural characterization and mechanism of action"],"prefix":"10.1016","volume":"114","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3793-7393","authenticated-orcid":false,"given":"Anwar","family":"Ullah","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rehana","family":"Masood","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ijaz","family":"Ali","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kifayat","family":"Ullah","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hamid","family":"Ali","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Haji","family":"Akbar","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Christian","family":"Betzel","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"issue":"9","key":"10.1016\/j.ijbiomac.2018.03.164_bb0005","first-page":"21","article-title":"Enzyme catalysis: the serine proteases","volume":"3","author":"Neitzel","year":"2010","journal-title":"Nat. Educ."},{"issue":"23","key":"10.1016\/j.ijbiomac.2018.03.164_bb0010","doi-asserted-by":"crossref","first-page":"4544","DOI":"10.1111\/j.1742-4658.2011.08115.x","article-title":"Enzymatic toxins from snake venom: structural characterization and mechanism of catalysis","volume":"278","author":"Kang","year":"2011","journal-title":"FEBS J."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0015","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"},{"issue":"6","key":"10.1016\/j.ijbiomac.2018.03.164_bb0020","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0021532","article-title":"Evolutionary analysis of novel serine proteases in the venom gland transcriptome of Bitis gabonica rhinoceros","volume":"6","author":"Vaiyapuri","year":"2011","journal-title":"PLoS One"},{"issue":"7\u20138","key":"10.1016\/j.ijbiomac.2018.03.164_bb0025","doi-asserted-by":"crossref","first-page":"843","DOI":"10.1007\/s00018-003-3325-z","article-title":"Snake venom thrombin-like enzymes: from reptilase to now","volume":"61","author":"Castro","year":"2004","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0030","doi-asserted-by":"crossref","first-page":"528","DOI":"10.1038\/334528a0","article-title":"The molecular evolution of genes and proteins: a tale of two serines","volume":"334","author":"Brenner","year":"1988","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0035","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1016\/j.toxicon.2013.10.016","article-title":"Rapid purification of serine proteinases from Bothrops alternatus and Bothrops moojeni venoms","volume":"76","author":"Fernandes de Oliveira","year":"2013","journal-title":"Toxicon"},{"issue":"3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0040","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1101\/gr.3228405","article-title":"From genome to \u201cvenome\u201d: molecular origin and evolution of the snake venom proteome inferred from phylogenetic analysis of toxin sequences and related body proteins","volume":"15","author":"Fry","year":"2005","journal-title":"Genome Res."},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0045","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0022-2836(72)90210-0","article-title":"Structure of crystalline-chymotrypsin. V. The atomic structure of tosyl-chymotrypsin at 2 \u00c5 resolution","volume":"68","author":"Birktoft","year":"1972","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0050","series-title":"Toxinology","first-page":"1","article-title":"Evolution of resistance to toxins in prey","author":"McCabe","year":"2016"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0055","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1186\/1741-7007-11-20","article-title":"Molecular basis for prey relocation in viperid snakes","volume":"11","author":"Saviola","year":"2013","journal-title":"BMC Biol."},{"issue":"1\u20132","key":"10.1016\/j.ijbiomac.2018.03.164_bb0060","doi-asserted-by":"crossref","first-page":"16","DOI":"10.3109\/15569543.2013.852109","article-title":"Snake venom thrombin-like enzymes","volume":"33","author":"Pradniwat","year":"2014","journal-title":"Toxin Rev."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0065","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1007\/978-90-481-9295-3_30","article-title":"Thrombin-like enzymes in snake venoms toxins and","author":"Mackessy","year":"2010","journal-title":"Hemostasis"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0070","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.pep.2017.05.009","article-title":"Expression, purification and characterization of a novel recombinant SVTLE, r-agkihpin-2, from Gloydius halys Pallas venom gland in Escherichia coli","volume":"136","author":"Sun","year":"2017","journal-title":"Protein Expr. Purif."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0075","doi-asserted-by":"crossref","first-page":"2422","DOI":"10.1021\/pr901128x","article-title":"The venomics of Bothrops alternatus is a pool of acidic proteins with predominant hemorrhagic and coagulopathic activities","volume":"9","author":"Ohler","year":"2010","journal-title":"J. Proteome Res."},{"issue":"12","key":"10.1016\/j.ijbiomac.2018.03.164_bb0080","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0145516","article-title":"Ontogenetic variation in biological activities of venoms from hybrids between Bothrops erythromelas and Bothrops neuwiedi snakes","volume":"10","author":"Santoro","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0085","doi-asserted-by":"crossref","first-page":"825","DOI":"10.1016\/S0041-0101(99)00197-X","article-title":"Identification of high molecular weight serine-proteases in Loxosceles intermedia (brown spider) venom","volume":"38","author":"Veiga","year":"2000","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0090","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1002\/pmic.200401096","article-title":"Proteome analysis of brown spider venom: identification of loxnecrogin isoforms in Loxosceles gaucho venom","volume":"5","author":"Machado","year":"2005","journal-title":"Proteomics"},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0095","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0010393","article-title":"Dual function of a bee venom serine protease: prophenoloxidase-activating factor in arthropods and fibrin(ogen)olytic enzyme in mammals","volume":"5","author":"Choo","year":"2010","journal-title":"PLoS One"},{"issue":"12","key":"10.1016\/j.ijbiomac.2018.03.164_bb0100","doi-asserted-by":"crossref","first-page":"1760","DOI":"10.1016\/j.biochi.2010.09.002","article-title":"Structural and functional comparison of proteolytic enzymes from plant latex and snake venoms","volume":"92","author":"Costa Jde","year":"2010","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0105","first-page":"294","article-title":"Effect of batroxobin on expression of neural cell adhesion molecule in temporal infarction rats and spatial learning and memory disorder","volume":"21","author":"Wu","year":"2001","journal-title":"J. Tradit. Chin. Med."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0110","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.ijbiomac.2018.03.164_bb0115","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1016\/j.toxicon.2016.09.017","article-title":"Agkihpin, a novel SVTLE from Gloydius halys Pallas, promotes platelet aggregation in vitro and inhibits thrombus formation in vivo in murine models of thrombosis","volume":"122","author":"Xie","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0120","first-page":"304","article-title":"A comparison of the platelet aggregation induced by three thrombin-like enzymes of snake venoms and thrombin","volume":"59","author":"Teng","year":"1998","journal-title":"Thromb. Haemost."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0125","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.toxicon.2016.11.001","article-title":"Serine proteinases from Bothrops snake venom activates PI3K\/Akt mediated angiogenesis","volume":"124","author":"Bhat","year":"2016","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0130","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1016\/j.toxicon.2017.06.009","article-title":"Ac2-26 peptide and serine protease of Bothrops atrox similarly induces angiogenesis without triggering local and systemic inflammation in a murine model of dorsal skinfold chamber","volume":"137","author":"Mol\u00e1s","year":"2017","journal-title":"Toxicon"},{"issue":"7","key":"10.1016\/j.ijbiomac.2018.03.164_bb0135","doi-asserted-by":"crossref","first-page":"1476","DOI":"10.1016\/j.biochi.2013.03.015","article-title":"Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: molecular sequence analysis of its cDNA and biochemical properties","volume":"95","author":"Vivas-Ruiz","year":"2013","journal-title":"Biochimie"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0140","doi-asserted-by":"crossref","first-page":"903292","DOI":"10.1155\/2013\/903292","article-title":"Rapid purification and procoagulant and platelet aggregating activities of Rhombeobin: a thrombin-like\/gyroxin-like enzyme from Lachesis muta rhombeata snake venom","volume":"2013","author":"Torres-Huaco","year":"2013","journal-title":"Biomed. Res. Int."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0145","doi-asserted-by":"crossref","first-page":"3030","DOI":"10.1007\/s00018-006-6315-0","article-title":"Snake venom components and their applications in biomedicine","volume":"63","author":"Koh","year":"2006","journal-title":"Cell. Mol. Life Sci."},{"issue":"3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0150","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1159\/000353096","article-title":"In vitro dissolution of calcium oxalate stones with ethylenediaminetetraacetic acid and snake venom thrombin-like enzyme","volume":"92","author":"Zhou","year":"2014","journal-title":"Urol. Int."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0155","article-title":"Multiple uses of fibrin sealant for nervous system treatment following injury and disease","volume":"2017","author":"Biscola","year":"2017","journal-title":"J. Venomous Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0160","doi-asserted-by":"crossref","first-page":"947","DOI":"10.1055\/s-0038-1657657","article-title":"Application of thrombin based fibrin glue and non-thrombin based batroxobin glue on intact human blood vessels: evidence for transmural thrombin activity","volume":"78","author":"Dascombe","year":"1997","journal-title":"Thromb. Haemost."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0165","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1080\/10937400903442514","article-title":"A new fibrin sealant from Crotalus durissus terrificus venom: applications in medicine","volume":"12","author":"Barros","year":"2009","journal-title":"J. Toxicol. Environ. Health B Crit. Rev."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0170","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1186\/s40409-017-0109-8","article-title":"Heterologous fibrin sealant derived from snake venom: from bench to bedside \u2014 an overview","volume":"23","author":"Ferreira Jr","year":"2017","journal-title":"J. Venomous Anim. Toxins Incl. Trop. Dis."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0175","doi-asserted-by":"crossref","first-page":"1171","DOI":"10.1016\/j.toxicon.2005.02.016","article-title":"Pratical applications of snake venom toxins in haemostasis","volume":"45","author":"Marsh","year":"2005","journal-title":"Toxicon"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0180","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1007\/s11239-016-1442-4","article-title":"Carbon monoxide releasing molecule-2 inhibition of snake venom thrombin-like activity: novel biochemical \u201cbrake\u201d?","volume":"43","author":"Nielsen","year":"2017","journal-title":"J. Thromb. Thrombolysis"},{"issue":"7","key":"10.1016\/j.ijbiomac.2018.03.164_bb0185","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.toxicon.2007.01.002","article-title":"Suramin counteracts the haemostatic disturbances produced by Bothrops jararaca snake venom","volume":"49","author":"Fernandes","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0190","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.toxicon.2018.01.005","article-title":"Citrus bioflavonoid, hesperetin, as inhibitor of two thrombin-like snake venom serine proteases isolated from Crotalus simus","volume":"143","author":"Vander Dos Santos","year":"2018","journal-title":"Toxicon"},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0195","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0104952","article-title":"Aqueous leaf extract of Jatropha gossypiifolia L. (Euphorbiaceae) inhibits enzymatic and biological actions of Bothrops jararaca snake venom","volume":"9","author":"F\u00e9lix-Silva","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0200","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.toxicon.2007.02.018","article-title":"BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: role of N-glycosylation in thermostability and active site accessibility","volume":"50","author":"Silva-Junior","year":"2017","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0205","doi-asserted-by":"crossref","first-page":"1059","DOI":"10.1016\/S0041-0101(98)80008-1","article-title":"Purification and partial characterization of a thrombinlike enzyme, balterobin, from the venom of Bothrops alternatus","volume":"36","author":"Smolka","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0210","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1016\/S0041-0101(99)00222-6","article-title":"Characterization of a thrombin-like enzyme from the venom of Trimeresurus jerdonii","volume":"38","author":"Lu","year":"2000","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0215","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1016\/0041-0101(92)90515-7","article-title":"A fibrinogen-clotting serine proteinase from Cerastes cerastes (horned viper) venom with arginine-esterase and amidase activities. Purification, characterization and kinetic parameter determination","volume":"30","author":"Laraba-Djebari","year":"1992","journal-title":"Toxicon"},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0220","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1007\/s10529-017-2441-z","article-title":"Cloning, expression, purification and bioactivity evaluation of a thrombin-like enzyme from Deinagkistrodon acutus venom gland library","volume":"40","author":"Li","year":"2018","journal-title":"Biotechnol. Lett."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0225","doi-asserted-by":"crossref","first-page":"913","DOI":"10.2174\/092986609788923293","article-title":"Venom-sweet-venom: N-linked glycosylation in snake venom toxins","volume":"16","author":"Soares","year":"2009","journal-title":"Protein Pept. Lett."},{"issue":"7","key":"10.1016\/j.ijbiomac.2018.03.164_bb0230","doi-asserted-by":"crossref","first-page":"1476","DOI":"10.1016\/j.biochi.2013.03.015","article-title":"Coagulant thrombin-like enzyme (barnettobin) from Bothrops barnetti venom: molecular sequence analysis of its cDNA and biochemical properties","volume":"95","author":"Vivas-Ruiz","year":"2013","journal-title":"Biochimie"},{"issue":"19","key":"10.1016\/j.ijbiomac.2018.03.164_bb0235","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."},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0240","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."},{"issue":"Pt 8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0245","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."},{"issue":"3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0250","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."},{"issue":"11","key":"10.1016\/j.ijbiomac.2018.03.164_bb0255","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."},{"issue":"16","key":"10.1016\/j.ijbiomac.2018.03.164_bb0260","doi-asserted-by":"crossref","first-page":"7628","DOI":"10.1016\/S0021-9258(18)68544-8","article-title":"Organization of the gene for batroxobin, a thrombin-like snake venom enzyme. Homology with the trypsin\/kallikrein gene family","volume":"263","author":"Itoh","year":"1988","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0265","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1016\/j.toxicon.2011.01.008","article-title":"A high-throughput venom-gland transcriptome for the Eastern Diamondback Rattlesnake (Crotalus adamanteus) and evidence for pervasive positive selection across toxin classes","volume":"57","author":"Rokyta","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0270","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1007\/978-1-4939-7015-5_6","article-title":"Predicting secretory proteins with SignalP","volume":"1611","author":"Nielsen","year":"2017","journal-title":"Methods Mol. Biol."},{"issue":"9","key":"10.1016\/j.ijbiomac.2018.03.164_bb0275","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"},{"issue":"47","key":"10.1016\/j.ijbiomac.2018.03.164_bb0280","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."},{"issue":"24","key":"10.1016\/j.ijbiomac.2018.03.164_bb0285","doi-asserted-by":"crossref","first-page":"21962","DOI":"10.1074\/jbc.M200676200","article-title":"X-ray structure of a serine protease acyl-enzyme complex at 0.95\u00c5 resolution","volume":"277","author":"Katona","year":"2002","journal-title":"J. Biol. Chem."},{"issue":"3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0290","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1006\/jmbi.2001.4872","article-title":"Inhibition of human alpha-thrombin by a phosphonate tripeptide proceeds via a metastable pentacoordinated phosphorus intermediate","volume":"311","author":"Skordalakes","year":"2001","journal-title":"J. Mol. Biol."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0295","doi-asserted-by":"crossref","first-page":"946","DOI":"10.1038\/ng.2343","article-title":"The yak genome and adaptation to life at high altitude","volume":"44","author":"Qiu","year":"2012","journal-title":"Nat. Genet."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0300","doi-asserted-by":"crossref","first-page":"D364","DOI":"10.1093\/nar\/gku1028","article-title":"A series of PDB related databases for everyday needs","volume":"43","author":"Touw","year":"2015","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0305","series-title":"The PyMOL Molecular Graphics System","author":"DeLano","year":"2002"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0310","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0006-291X(67)80055-X","article-title":"On the size of the active site in proteases. I. Papain","volume":"27","author":"Schechter","year":"1967","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0315","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/0022-5193(71)90130-5","article-title":"On the mechanism of proton transfer in the catalysis by serine proteases","volume":"31","author":"Polg\u00e1r","year":"1971","journal-title":"J. Theor. Biol."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0320","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/0141-8130(91)90054-X","article-title":"Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH","volume":"2","author":"Dixon","year":"1991","journal-title":"Int. J. Biol. Macromol."},{"issue":"6777","key":"10.1016\/j.ijbiomac.2018.03.164_bb0325","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1038\/35006683","article-title":"Structural basis for the anticoagulant activity of the thrombin-thrombomodulin complex","volume":"404","author":"Fuentes-Prior","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0330","series-title":"The Proteomics Protocols Handbook","first-page":"571","article-title":"Protein identification and analysis tools on the ExPASy server","author":"Gasteiger","year":"2005"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0335","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1016\/S0041-0101(02)00140-X","article-title":"Purification, characterization and crystallization of Jararacussin-I, a fibrinogen-clotting enzyme isolated from the venom of Bothrops jararacussu","volume":"40","author":"Bortoleto","year":"2002","journal-title":"Toxicon"},{"issue":"Pt 8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0340","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1107\/S1744309107031429","article-title":"Purification, crystallization and preliminary X-ray diffraction analysis of saxthrombin, a thrombin-like enzyme from Gloydius saxatilis venom","volume":"63","author":"Wei","year":"2007","journal-title":"Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun."},{"issue":"Pt 3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0345","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1107\/S2059798317001061","article-title":"CheckMyMetal: a macromolecular metal-binding validation tool","volume":"73","author":"Zheng","year":"2017","journal-title":"Acta Crystallogr. D Struct. Biol."},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0350","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1038\/nprot.2013.172","article-title":"Validation of metal-binding sites in macromolecular structures with the CheckMyMetal web server","volume":"9","author":"Zheng","year":"2014","journal-title":"Nat. Protoc."},{"issue":"6","key":"10.1016\/j.ijbiomac.2018.03.164_bb0355","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1016\/0049-3848(73)90004-2","article-title":"The factor V activating enzyme of Russell's viper venom","volume":"2","author":"Esmon","year":"1973","journal-title":"Thromb. Res."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0360","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1107\/S0907444902023375","article-title":"Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom","volume":"59","author":"Zhu","year":"2003","journal-title":"Acta Crystallogr., Sect. D: Biol. Crystallogr."},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0365","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.toxicon.2007.02.018","article-title":"BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: role of N-glycosylation in thermostability and active site accessibility","volume":"50","author":"Silva-Junior","year":"2007","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0370","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1186\/1471-2105-8-438","article-title":"Glycosylation site prediction using ensembles of support vector machine classifiers","volume":"8","author":"Caragea","year":"2007","journal-title":"BMC Bioinf."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0375","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj3540161","article-title":"Serine protease isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis","volume":"354","author":"Wang","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0380","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1016\/S0041-0101(02)00363-X","article-title":"Purification and characterization of a thrombin like enzyme, elegaxobin II, with Lys bradykinin releasing activity from the venom of Trimeresurus elegans (Sakishima-Habu)","volume":"41","author":"Oyama","year":"2003","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0385","author":"Gupta"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0390","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.ejps.2007.10.008","article-title":"pH dependent effect of glycosylation on protein stability","volume":"33","author":"Wang","year":"2007","journal-title":"Eur. J. Pharm. Sci."},{"issue":"6","key":"10.1016\/j.ijbiomac.2018.03.164_bb0395","first-page":"878","article-title":"Purification, characteristics, molecular cloning and sequence analysis of the thrombin-like enzyme from Gloydius saxatilis","volume":"49","author":"De-Jun","year":"2003","journal-title":"Curr. Zool. (formerly Acta Zool. Sin.)"},{"issue":"33","key":"10.1016\/j.ijbiomac.2018.03.164_bb0400","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.ijbiomac.2018.03.164_bb0405","doi-asserted-by":"crossref","first-page":"261","DOI":"10.3109\/15569549809040394","article-title":"Chemistry and biochemistry of kallikrein-like enzyme from snake venoms","volume":"17","author":"Komori","year":"1998","journal-title":"J. Toxicol., Toxin Rev."},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0410","doi-asserted-by":"crossref","first-page":"18","DOI":"10.1016\/j.toxicon.2007.02.018","article-title":"BJ-48, a novel thrombin-like enzyme from the Bothrops jararacussu venom with high selectivity for Arg over Lys in P1: role of N-glycosylation in thermostability and active site accessibility","volume":"50","author":"Silva-Junior","year":"2007","journal-title":"Toxicon"},{"issue":"1","key":"10.1016\/j.ijbiomac.2018.03.164_bb0415","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1006\/abbi.1995.1208","article-title":"Primary structure of a coagulant enzyme, bilineobin, from Agkistrodon bilineatus venom","volume":"318","author":"Nikai","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0420","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.1006\/jmbi.2001.5305","article-title":"Crystal structure reveals basis for the inhibitor resistance of human brain trypsin","volume":"315","author":"Katona","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0425","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1042\/BJ20051645","article-title":"Functional role of catalytic triad and oxyanion hole-forming residues on enzyme activity of Escherichia coli thioesterase I\/protease I\/phospholipase L1","volume":"397","author":"Li-Chiun","year":"2006","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0430","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1146\/annurev.bb.11.060182.002223","article-title":"Crystallographic and NMR studies of the serine proteases","volume":"11","author":"Steitz","year":"1982","journal-title":"Annu. Rev. Biophys. Bioeng."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0435","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1016\/S1359-0278(96)00052-1","article-title":"Conserved features in the active site of nonhomologous serine proteases","volume":"1","author":"Bagley","year":"1996","journal-title":"Fold. Des."},{"issue":"27","key":"10.1016\/j.ijbiomac.2018.03.164_bb0440","doi-asserted-by":"crossref","first-page":"25644","DOI":"10.1074\/jbc.M503499200","article-title":"Energetic and structural consequences of perturbing Gly-193 in the oxyanion hole of serine proteases","volume":"280","author":"Bobofchak","year":"2005","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0445","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1016\/S0021-9258(18)64384-4","article-title":"Reactivity and catalysis in reactions of the serine hydroxyl group and of O-acyl serines","volume":"236","author":"Anderson","year":"1961","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0450","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1042\/bj0560288","article-title":"The reaction of p-nitrophenyl esters with chymotrypsin and insulin","volume":"56","author":"Hartley","year":"1954","journal-title":"Biochem. J."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0455","doi-asserted-by":"crossref","first-page":"1335","DOI":"10.1073\/pnas.64.4.1335","article-title":"The nature of general base-general acid catalysis in serine proteases","volume":"64","author":"Polg\u00e1r","year":"1969","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"20","key":"10.1016\/j.ijbiomac.2018.03.164_bb0460","doi-asserted-by":"crossref","first-page":"4481","DOI":"10.1021\/bi00665a023","article-title":"A detailed structural comparison between the charge relay system in chymotrypsinogen and in alpha-chymotrypsin","volume":"15","author":"Birktoft","year":"1976","journal-title":"Biochemistry"},{"issue":"28","key":"10.1016\/j.ijbiomac.2018.03.164_bb0465","doi-asserted-by":"crossref","first-page":"29485","DOI":"10.1074\/jbc.M402971200","article-title":"Structural role of Gly (193) in serine proteases: investigations of a G555E (GLY193 in chymotrypsin) mutant of blood coagulation factor XI","volume":"279","author":"Schmidt","year":"2004","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0470","doi-asserted-by":"crossref","first-page":"2956","DOI":"10.1016\/S0021-9258(19)39894-1","article-title":"Experimental and theoretical evidence supporting the role of Gly363 in blood coagulation factor IXa (Gly193 in chymotrypsin) for proper activation of the proenzyme","volume":"265","author":"Bajaj","year":"1990","journal-title":"J. Biol. Chem."},{"issue":"18","key":"10.1016\/j.ijbiomac.2018.03.164_bb0475","doi-asserted-by":"crossref","first-page":"6835","DOI":"10.1073\/pnas.0601910103","article-title":"Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates","volume":"103","author":"Radisky","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0480","doi-asserted-by":"crossref","first-page":"26932","DOI":"10.1039\/C5RA03063C","article-title":"Insights into the C-H\u2026F-C hydrogen bond by Cambridge structural database analyses and computational studies","volume":"5","author":"Dev","year":"2015","journal-title":"RSC Adv."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0485","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1111\/j.1742-4658.2005.04604.x","article-title":"Short hydrogen bonds in proteins","volume":"272","author":"Rajagopal","year":"2005","journal-title":"FEBS J."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0490","series-title":"An Introduction to Hydrogen Bonding","author":"Jeffrey","year":"1997"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0495","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1111\/j.1432-1033.1973.tb03069.x","article-title":"The interaction between alpha-chymotrypsin and pancreatic trypsin inhibitor (Kunitz inhibitor). Kinetic and thermodynamic properties","volume":"38","author":"Vincent","year":"1973","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0500","doi-asserted-by":"crossref","first-page":"3036","DOI":"10.1093\/emboj\/20.12.3036","article-title":"Molecular markers of serine protease evolution","volume":"20","author":"Krem","year":"2001","journal-title":"EMBO J."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0505","doi-asserted-by":"crossref","first-page":"29987","DOI":"10.1074\/jbc.272.48.29987","article-title":"Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold","volume":"272","author":"Perona","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0510","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.ijbiomac.2018.03.164_bb0515","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj3540161","article-title":"Serine protease isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis","volume":"354","author":"Wang","year":"2001","journal-title":"Biochem. J."},{"issue":"8","key":"10.1016\/j.ijbiomac.2018.03.164_bb0520","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.toxicon.2005.02.030","article-title":"Snake venoms and coagulopathy","volume":"45","author":"White","year":"2005","journal-title":"Toxicon"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0525","first-page":"217","article-title":"Cloning, sequence analysis and expression in E. Coli of the cDNA of the thrombin-like enzyme (Pallabin) from the venom of Agkistrodon Halys Pallas","volume":"47","author":"Fan","year":"1999","journal-title":"Biochem. Mol. Biol. Int."},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0530","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"},{"issue":"15","key":"10.1016\/j.ijbiomac.2018.03.164_bb0535","doi-asserted-by":"crossref","first-page":"9488","DOI":"10.1016\/S0021-9258(17)44693-X","article-title":"Hen oviduct signal peptidase is an integral membrane protein","volume":"258","author":"Lively","year":"1983","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0540","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1111\/j.1432-1033.1981.tb05351.x","article-title":"On the hydrophobic nature of signal sequences","volume":"116","author":"von Heijne","year":"1981","journal-title":"Eur. J. Biochem."},{"issue":"4","key":"10.1016\/j.ijbiomac.2018.03.164_bb0545","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1016\/j.jmb.2004.05.028","article-title":"Improved prediction of signal peptides: SignalP 3.0","volume":"340","author":"Bendtsen","year":"2004","journal-title":"J. Mol. Biol."},{"issue":"4","key":"10.1016\/j.ijbiomac.2018.03.164_bb0550","doi-asserted-by":"crossref","first-page":"815","DOI":"10.1002\/pro.5560070401","article-title":"Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes","volume":"7","author":"Khan","year":"1998","journal-title":"Protein Sci."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0555","doi-asserted-by":"crossref","first-page":"1749","DOI":"10.1016\/S0041-0101(98)00126-3","article-title":"Snake venoms and the hemostatic system","volume":"36","author":"Markland","year":"1998","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0560","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/0041-0101(82)90225-2","article-title":"Thrombin-like snake venom proteinases","volume":"20","author":"Stocker","year":"1982","journal-title":"Toxicon"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0565","doi-asserted-by":"crossref","first-page":"701","DOI":"10.1007\/s000180050091","article-title":"Molecular mechanisms of thrombin function","volume":"53","author":"Di Cera","year":"1997","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0570","series-title":"Robbins and Cotran Pathological Basis of Disease: With Student Consult Access","author":"Kumar","year":"2004"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0575","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1111\/j.1749-6632.2001.tb03502.x","article-title":"Determinants of thrombin specifcity","volume":"936","author":"Di Cera","year":"2001","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0580","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.ijbiomac.2018.03.164_bb0585","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1042\/bj3540161","article-title":"Serine protease isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis","volume":"354","author":"Wang","year":"2001","journal-title":"Biochem. J."},{"issue":"27","key":"10.1016\/j.ijbiomac.2018.03.164_bb0590","doi-asserted-by":"crossref","first-page":"19341","DOI":"10.1016\/S0021-9258(18)41780-2","article-title":"Interaction of thrombin des-ETW with antithrombin III, the Kunitz inhibitors, thrombomodulin and protein C. Structural link between the autolysis loop and the Tyr-Pro-Pro-Trp insertion of thrombin","volume":"267","author":"Le Bonniec","year":"1992","journal-title":"J. Biol. Chem."},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0595","doi-asserted-by":"crossref","first-page":"1852","DOI":"10.1073\/pnas.96.5.1852","article-title":"Unexpected crucial role of residue 225 in serine proteases","volume":"96","author":"Guinto","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"47","key":"10.1016\/j.ijbiomac.2018.03.164_bb0600","doi-asserted-by":"crossref","first-page":"11721","DOI":"10.1021\/bi00162a008","article-title":"Thrombin is a Na(+)-activated enzyme","volume":"31","author":"Wells","year":"1992","journal-title":"Biochemistry"},{"issue":"5","key":"10.1016\/j.ijbiomac.2018.03.164_bb0605","doi-asserted-by":"crossref","first-page":"1359","DOI":"10.1016\/S0022-5347(17)39098-5","article-title":"Urothelial injury from ethylenediaminetetraacetic acid used as an irrigant in the urinary tract","volume":"142","author":"Kane","year":"1989","journal-title":"J. Urol."},{"issue":"4","key":"10.1016\/j.ijbiomac.2018.03.164_bb0610","doi-asserted-by":"crossref","first-page":"654","DOI":"10.1111\/j.1464-410X.2005.05701.x","article-title":"Intracrystalline proteins and urolithiasis: a comparison of the protein content and ultrastructure of urinary calcium oxalate monohydrate and dihydrate crystals","volume":"96","author":"Ryall","year":"2005","journal-title":"BJU Int."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0615","series-title":"Kidney Stone Prevention: \u2018Fact Versus Fiction\u2019 Renal and Urology News","author":"Finger","year":"2011"},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0620","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1007\/978-1-4471-4387-1_66","article-title":"Dissolution of stones by oral and irrigative therapy","author":"Korets","year":"2012","journal-title":"Urolithiasis"},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0625","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/0022-2836(91)90025-2","article-title":"Structure of bovine prothrombin fragment 1 refined at 2.25\u00c5 resolution","volume":"220","author":"Seshadri","year":"1991","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0630","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1038\/ki.1978.53","article-title":"Physicochemical aspects of urolithiasis","volume":"13","author":"Finlayson","year":"1978","journal-title":"Kidney Int."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0635","doi-asserted-by":"crossref","first-page":"4017","DOI":"10.1016\/S0021-9258(18)61305-5","article-title":"Mg (II) binding by bovine prothrombin fragment 1 via equilibrium dialysis and the relative roles of Mg (II) and Ca (II) in blood coagulation","volume":"262","author":"Deerfield","year":"1987","journal-title":"J. Biol. Chem."},{"issue":"2","key":"10.1016\/j.ijbiomac.2018.03.164_bb0640","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1016\/S0031-6997(25)00445-4","article-title":"Recent research on the biological activity of suramin","volume":"45","author":"Voogd","year":"1993","journal-title":"Pharmacol. Rev."},{"issue":"3","key":"10.1016\/j.ijbiomac.2018.03.164_bb0645","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.jmb.2005.04.072","article-title":"Inhibition of myotoxic activity of Bothrops asper myotoxin II by the anti-trypanosomal drug suramin","volume":"350","author":"Murakami","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0650","doi-asserted-by":"crossref","first-page":"2077","DOI":"10.1016\/j.biocel.2004.03.007","article-title":"Suramin interaction with human alpha-thrombin: inhibitory effects and binding studies","volume":"36","author":"Monteiro","year":"2004","journal-title":"Int. J. Biochem. Cell Biol."},{"issue":"6","key":"10.1016\/j.ijbiomac.2018.03.164_bb0655","doi-asserted-by":"crossref","first-page":"873","DOI":"10.1016\/j.bbapap.2009.03.011","article-title":"Structural and thermodynamic analysis of thrombin: suramin interaction in solution and crystal phases","volume":"1794","author":"Lima","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"issue":"Web Server issue","key":"10.1016\/j.ijbiomac.2018.03.164_bb0660","doi-asserted-by":"crossref","first-page":"W270","DOI":"10.1093\/nar\/gkr366","article-title":"SwissDock, a protein-small molecule docking web service based on EADock DSS, Nucl","volume":"39","author":"Grosdidier","year":"2011","journal-title":"Acids Res."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0665","first-page":"15","article-title":"Application of the PM6 semi-empirical method to modeling proteins enhances docking accuracy of AutoDock","volume":"1","author":"Bikadi","year":"2009","journal-title":"J. Chem. Inf."},{"key":"10.1016\/j.ijbiomac.2018.03.164_bb0670","doi-asserted-by":"crossref","first-page":"W363","DOI":"10.1093\/nar\/gki481","article-title":"PatchDock and SymmDock: servers for rigid and symmetric docking","volume":"33","author":"Schneidman-Duhovny","year":"2005","journal-title":"Nucleic Acids Res."},{"issue":"Web Server issue","key":"10.1016\/j.ijbiomac.2018.03.164_bb0675","doi-asserted-by":"crossref","first-page":"W229","DOI":"10.1093\/nar\/gkn186","article-title":"FireDock: a web server for fast interaction refinement in molecular docking","volume":"36","author":"Mashiach","year":"2008","journal-title":"Nucleic Acids Res."}],"container-title":["International Journal of Biological Macromolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018302551?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0141813018302551?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,7,3]],"date-time":"2025-07-03T00:56:31Z","timestamp":1751504191000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0141813018302551"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,7]]},"references-count":135,"alternative-id":["S0141813018302551"],"URL":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.03.164","relation":{},"ISSN":["0141-8130"],"issn-type":[{"value":"0141-8130","type":"print"}],"subject":[],"published":{"date-parts":[[2018,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Thrombin-like enzymes from snake venom: Structural characterization and mechanism of action","name":"articletitle","label":"Article Title"},{"value":"International Journal of Biological Macromolecules","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ijbiomac.2018.03.164","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2018 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}]}}