{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,15]],"date-time":"2026-05-15T17:19:55Z","timestamp":1778865595185,"version":"3.51.4"},"reference-count":43,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2014,8,1]],"date-time":"2014-08-01T00:00:00Z","timestamp":1406851200000},"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":["Toxicon"],"published-print":{"date-parts":[[2014,8]]},"DOI":"10.1016\/j.toxicon.2014.04.012","type":"journal-article","created":{"date-parts":[[2014,5,9]],"date-time":"2014-05-09T08:50:31Z","timestamp":1399625431000},"page":"40-50","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":19,"special_numbering":"C","title":["Snake venom glutaminyl cyclases: Purification, cloning, kinetic study, recombinant expression, and comparison with the human enzyme"],"prefix":"10.1016","volume":"86","author":[{"given":"Ying-Ming","family":"Wang","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kai-Fa","family":"Huang","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.toxicon.2014.04.012_bib1","doi-asserted-by":"crossref","first-page":"7069","DOI":"10.1021\/jm900969p","article-title":"Inhibitors for human glutaminyl cyclase by structure based design and bio-isosteric replacement","volume":"52","author":"Buchholz","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib2","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1042\/BJ20040125","article-title":"Molecular evolution and structure-function relationships of crotoxin-like and asparagine-6-containing phospholipases A2 in pitviper venoms","volume":"381","author":"Chen","year":"2004","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2014.04.012_bib3","doi-asserted-by":"crossref","first-page":"883","DOI":"10.1016\/1357-2725(96)00034-9","article-title":"Bovine brain pyroglutamyl aminopeptidase (type-1): purification and characterisation of a neuropeptide-inactivating peptidase","volume":"28","author":"Cummins","year":"1996","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"10.1016\/j.toxicon.2014.04.012_bib4","doi-asserted-by":"crossref","first-page":"176","DOI":"10.1016\/j.jmb.2011.07.027","article-title":"Crystal structure of crotoxin reveals key residues involved in the stability and toxicity of this potent heterodimeric \u03b2-neurotoxin","volume":"412","author":"Faure","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.toxicon.2014.04.012_bib5","series-title":"PHYLIP: the PHYLogeny Inference Package, Version 3.573","author":"Felsenstein","year":"1992"},{"key":"10.1016\/j.toxicon.2014.04.012_bib6","doi-asserted-by":"crossref","first-page":"783","DOI":"10.2307\/2408678","article-title":"Confidence limits on phylogenies: an approach using the bootstrap","volume":"39","author":"Felsenstein","year":"1985","journal-title":"Evolution"},{"key":"10.1016\/j.toxicon.2014.04.012_bib7","first-page":"163","article-title":"A bradykinin-potentiating factor (BPF) present in the venom of Bothrops jararaca","volume":"24","author":"Ferreira","year":"1965","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.toxicon.2014.04.012_bib8","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","volume":"7","author":"Fry","year":"2008","journal-title":"Mol. Cell Proteomics"},{"key":"10.1016\/j.toxicon.2014.04.012_bib9","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.jprot.2013.04.003","article-title":"Neonate-to-adult transition of snake venomics in the short-tailed pitviper, Gloydius brevicaudus","volume":"84","author":"Gao","year":"2013","journal-title":"J. Proteomics"},{"key":"10.1016\/j.toxicon.2014.04.012_bib10","doi-asserted-by":"crossref","first-page":"3065","DOI":"10.2174\/0929867043363820","article-title":"Dendrotoxins: structure-activity relationships and effects on potassium ion channels","volume":"23","author":"Harvey","year":"2004","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib11","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1093\/infdis\/jis729","article-title":"Glutaminyl cyclases as novel targets for the treatment of septic arthritis","volume":"207","author":"Hellvard","year":"2013","journal-title":"J. Infect. Dis."},{"key":"10.1016\/j.toxicon.2014.04.012_bib12","doi-asserted-by":"crossref","first-page":"3047","DOI":"10.1046\/j.1432-1033.2002.02982.x","article-title":"Determinants of the inhibition of a Taiwan habu venom metalloproteinase by its endogenous inhibitors revealed by X-ray","volume":"269","author":"Huang","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib13","doi-asserted-by":"crossref","first-page":"13117","DOI":"10.1073\/pnas.0504184102","article-title":"Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation","volume":"102","author":"Huang","year":"2005","journal-title":"Proc. Nat. Acad. Sci. (U. S. A.)"},{"key":"10.1016\/j.toxicon.2014.04.012_bib14","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.pep.2005.02.020","article-title":"Cloning, expression, characterization, and crystallization of a glutaminyl cyclase from human bone marrow: a single zinc metalloenzyme","volume":"43","author":"Huang","year":"2005","journal-title":"Protein Expr. Purif."},{"key":"10.1016\/j.toxicon.2014.04.012_bib15","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1042\/BJ20071073","article-title":"A conserved hydrogen bond network in the catalytic center of animal glutaminyl cyclases is critical for catalysis","volume":"411","author":"Huang","year":"2008","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2014.04.012_bib16","doi-asserted-by":"crossref","first-page":"12439","DOI":"10.1074\/jbc.M110.208595","article-title":"Structures of human Golgi resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding","volume":"286","author":"Huang","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib17","doi-asserted-by":"crossref","first-page":"38825","DOI":"10.1074\/jbc.R111.288308","article-title":"Pyroglutamate Amyloid-\u03b2 (A\u03b2): a hatchet man in Alzheimer disease","volume":"286","author":"Jawhar","year":"2011","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib18","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1016\/S0300-9084(02)01429-3","article-title":"cDNA sequence and molecular modeling of a nerve growth factor from Bothrops jararacussu venomous gland","volume":"84","author":"Kashima","year":"2002","journal-title":"Biochimie"},{"key":"10.1016\/j.toxicon.2014.04.012_bib19","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/0014-5793(96)00327-4","article-title":"Prediction of potential protein-protein interaction sites from amino acid sequence, identification of a fibrin polymerization site","volume":"385","author":"Kini","year":"1996","journal-title":"FEBS Lett."},{"key":"10.1016\/j.toxicon.2014.04.012_bib20","doi-asserted-by":"crossref","first-page":"1293","DOI":"10.1016\/j.peptides.2008.04.003","article-title":"Crotalphine, a novel potent analgesic peptide from the venom of the South American rattlesnake Crotalus durissus terrificus","volume":"29","author":"Konno","year":"2008","journal-title":"Peptides"},{"key":"10.1016\/j.toxicon.2014.04.012_bib21","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1006\/jmbi.1993.1351","article-title":"Main-chain bond lengths and bond angles in protein structures","volume":"231","author":"Laskowski","year":"1993","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.toxicon.2014.04.012_bib22","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1038\/356083a0","article-title":"Assessment of protein models with three-dimensional profiles","volume":"356","author":"L\u00fcthy","year":"1992","journal-title":"Nature"},{"key":"10.1016\/j.toxicon.2014.04.012_bib23","series-title":"Molecular Cloning: a Laboratory Manual","author":"Maniatis","year":"1989"},{"key":"10.1016\/j.toxicon.2014.04.012_bib24","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/0076-6879(87)55023-6","article-title":"Specific synthesis of DNA in\u00a0vitro via a polymerase catalyzed chain reaction","volume":"155","author":"Mullis","year":"1987","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.toxicon.2014.04.012_bib25","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.1073\/pnas.94.4.1189","article-title":"Cloning and sequence analysis of a Bothrops jararaca cDNA encoding a precursor of seven bradykinin-potentiating peptides and a C-type natriuretic peptide","volume":"94","author":"Murayama","year":"1997","journal-title":"Proc. Nat. Acad. Sci. (U. S. A.)"},{"key":"10.1016\/j.toxicon.2014.04.012_bib26","doi-asserted-by":"crossref","first-page":"278","DOI":"10.1016\/j.toxicon.2006.05.013","article-title":"Snake venom glutaminyl cyclase","volume":"48","author":"Pawlak","year":"2006","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.04.012_bib27","doi-asserted-by":"crossref","first-page":"6280","DOI":"10.1021\/bi200249h","article-title":"Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center","volume":"50","author":"Ruiz-Carrillo","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2014.04.012_bib28","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1006\/abio.2001.5560","article-title":"Continuous spectrometric assays for glutaminyl cyclase activity","volume":"303","author":"Schilling","year":"2002","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib29","doi-asserted-by":"crossref","first-page":"49773","DOI":"10.1074\/jbc.M309077200","article-title":"Identification of human glutaminyl cyclase as a metalloenzyme. Potent inhibition by imidazole derivatives and heterocyclic chelators","volume":"278","author":"Schilling","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib30","doi-asserted-by":"crossref","first-page":"1583","DOI":"10.1515\/BC.2003.175","article-title":"Substrate specificity of glutaminyl cyclases from plants and animals","volume":"384","author":"Schilling","year":"2003","journal-title":"Biol. Chem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib31","doi-asserted-by":"crossref","first-page":"10921","DOI":"10.1021\/bi701043x","article-title":"Isolation and characterization of glutaminyl cyclases from Drosophila: evidence for enzyme forms with different subcellular localization","volume":"46","author":"Schilling","year":"2007","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2014.04.012_bib32","series-title":"Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-state Enzyme System","first-page":"100","author":"Segel","year":"1993"},{"key":"10.1016\/j.toxicon.2014.04.012_bib33","doi-asserted-by":"crossref","first-page":"11831","DOI":"10.1021\/bi9018835","article-title":"Glutaminyl cyclases display significant catalytic proficiency for glutamyl substrates","volume":"48","author":"Seifert","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.toxicon.2014.04.012_bib34","doi-asserted-by":"crossref","first-page":"6522","DOI":"10.1111\/j.1742-4658.2009.07337.x","article-title":"Mammalian glutaminyl cyclases and their isoenzymes have identical enzymatic characteristics","volume":"276","author":"Stephan","year":"2009","journal-title":"FEBS J."},{"key":"10.1016\/j.toxicon.2014.04.012_bib35","doi-asserted-by":"crossref","first-page":"895","DOI":"10.1042\/bj3110895","article-title":"Molecular cloning and characterization of a neurotoxic phospholipase A2 from the venom of Taiwan habu (Trimeresurus mucrosquamatus)","volume":"311","author":"Tsai","year":"1995","journal-title":"Biochem. J."},{"key":"10.1016\/j.toxicon.2014.04.012_bib36","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1006\/abbi.2001.2524","article-title":"Purification, sequencing and phylogenetic analyses of novel Lys-49 phospholipases A2 from venoms of rattlesnakes and other Pitvipers","volume":"394","author":"Tsai","year":"2001","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.toxicon.2014.04.012_bib37","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1016\/j.bbapap.2007.04.012","article-title":"Venom phospholipases of Russell's vipers from Myanmar and eastern India: cloning, characterization and phylogeographic analysis","volume":"1774","author":"Tsai","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.toxicon.2014.04.012_bib38","doi-asserted-by":"crossref","first-page":"332","DOI":"10.1016\/j.toxicon.2010.12.012","article-title":"cDNA cloning, structural, and functional analyses of venom phospholipases A2 and a Kunitz-type protease inhibitor from steppe viper Vipera ursinii renardi","volume":"57","author":"Tsai","year":"2011","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.04.012_bib39","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1016\/j.toxicon.2011.10.016","article-title":"Cloning and characterization of Trimeresurus gracilis venom phospholipases A2: comparison with Ovophis okinavensis venom and the systematic implications","volume":"59","author":"Tsai","year":"2012","journal-title":"Toxicon"},{"key":"10.1016\/j.toxicon.2014.04.012_bib40","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1093\/oxfordjournals.jbchem.a132148","article-title":"Purification and characterization of L-pyrrolidonecarboxylate peptidase from Bacillus amyloliquefacien","volume":"84","author":"Tsuru","year":"1978","journal-title":"J. Biochem."},{"key":"10.1016\/j.toxicon.2014.04.012_bib41","doi-asserted-by":"crossref","first-page":"650","DOI":"10.1016\/j.bbrc.2007.11.027","article-title":"Molecular characterization of endogenous snake venom metalloproteinase inhibitors","volume":"365","author":"Wagstaff","year":"2008","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.toxicon.2014.04.012_bib42","doi-asserted-by":"crossref","first-page":"2273","DOI":"10.1110\/ps.03102403","article-title":"Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities","volume":"12","author":"Watanabe","year":"2003","journal-title":"Protein Sci."},{"key":"10.1016\/j.toxicon.2014.04.012_bib43","doi-asserted-by":"crossref","first-page":"1703","DOI":"10.1002\/rcm.1973","article-title":"Fast analysis of low molecular mass compounds present in snake venom: identification of ten new pyroglutamate-containing peptides","volume":"19","author":"Wermelinger","year":"2005","journal-title":"Rapid Commun. Mass Spectrom."}],"container-title":["Toxicon"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010114001214?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0041010114001214?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2019,8,10]],"date-time":"2019-08-10T05:45:10Z","timestamp":1565415910000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0041010114001214"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,8]]},"references-count":43,"alternative-id":["S0041010114001214"],"URL":"https:\/\/doi.org\/10.1016\/j.toxicon.2014.04.012","relation":{},"ISSN":["0041-0101"],"issn-type":[{"value":"0041-0101","type":"print"}],"subject":[],"published":{"date-parts":[[2014,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Snake venom glutaminyl cyclases: Purification, cloning, kinetic study, recombinant expression, and comparison with the human enzyme","name":"articletitle","label":"Article Title"},{"value":"Toxicon","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.toxicon.2014.04.012","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}