{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T04:27:51Z","timestamp":1791606471246,"version":"4.3.4"},"reference-count":50,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2016,9,1]],"date-time":"2016-09-01T00:00:00Z","timestamp":1472688000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["2013BQ028"],"award-info":[{"award-number":["2013BQ028"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100012226","name":"Fundamental Research Funds for the Central Universities","doi-asserted-by":"crossref","award":["2014QC023"],"award-info":[{"award-number":["2014QC023"]}],"id":[{"id":"10.13039\/501100012226","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["31272069"],"award-info":[{"award-number":["31272069"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"name":"State Administration of Foreign Experts Affairs of China","award":["GDW20154200223"],"award-info":[{"award-number":["GDW20154200223"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Pesticide Biochemistry and Physiology"],"published-print":{"date-parts":[[2016,9]]},"DOI":"10.1016\/j.pestbp.2015.09.009","type":"journal-article","created":{"date-parts":[[2015,9,26]],"date-time":"2015-09-26T02:27:33Z","timestamp":1443234453000},"page":"81-88","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":27,"special_numbering":"C","title":["Identification and functional characterization of an epsilon glutathione S-transferase from the beet armyworm (Spodoptera exigua)"],"prefix":"10.1016","volume":"132","author":[{"given":"Hu","family":"Wan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sha","family":"Zhan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiangdong","family":"Xia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pengfei","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"You","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byung Rae","family":"Jin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianhong","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.pestbp.2015.09.009_bb0005","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1186\/1471-2164-4-35","article-title":"The Anopheles gambiae glutathione transferase supergene family: annotation, phylogeny and expression profiles","volume":"4","author":"Ding","year":"2003","journal-title":"BMC Genomics"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0010","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1016\/S0076-6879(05)01013-X","article-title":"Drosophila glutathione S-transferases","volume":"401","author":"Tu","year":"2005","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0015","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1146\/annurev.ento.51.110104.151104","article-title":"Molecular mechanisms of metabolic resistance to synthetic and natural xenobiotics","volume":"52","author":"Li","year":"2007","journal-title":"Annu. Rev. Entomol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0020","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1021\/tx960072x","article-title":"Structure, catalytic mechanism, and evolution of the glutathione transferases","volume":"10","author":"Armstrong","year":"1997","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0025","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1111\/j.1365-2583.2004.00529.x","article-title":"Insect glutathione transferases and insecticide resistance","volume":"14","author":"Enayati","year":"2005","journal-title":"Insect Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0030","doi-asserted-by":"crossref","first-page":"2123","DOI":"10.1016\/S0031-9422(00)85377-7","article-title":"Biosynthesis of S-(4-ethylamino-6-isopropylamino-2-s-triazine) glutathione: partial purification and properties of glutathione-S-transferase from corn","volume":"9","author":"Frear","year":"1970","journal-title":"Phytochemistry"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0035","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1007\/s10126-007-9034-0","article-title":"Marine glutathione S-transferases","volume":"9","author":"Blanchette","year":"2007","journal-title":"Mar. Biotechnol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0040","first-page":"2","article-title":"Ontogeny of Human Conjugating Enzymes","author":"Coughtrie","year":"2015","journal-title":"Drug Metab. Lett."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0045","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1002\/ps.3558","article-title":"Multiple glutathione S-transferase genes: identification and expression in oriental fruit fly, Bactrocera dorsalis","volume":"70","author":"Hu","year":"2014","journal-title":"Pest Manag. Sci."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0050","doi-asserted-by":"crossref","first-page":"8733","DOI":"10.1074\/jbc.M211776200","article-title":"Identification of residues in glutathione transferase capable of driving functional diversification in evolution. A novel approach to protein redesign","volume":"278","author":"Ivarsson","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0055","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0076-6879(05)01001-3","article-title":"Nomenclature for mammalian soluble glutathione transferases","volume":"401","author":"Mannervik","year":"2005","journal-title":"Methods Enzymol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0060","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1126\/science.1076781","article-title":"Evolution of supergene families associated with insecticide resistance","volume":"298","author":"Ranson","year":"2002","journal-title":"Science"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0065","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1016\/j.ibmb.2007.05.018","article-title":"The Aedes aegypti glutathione transferase family","volume":"37","author":"Lumjuan","year":"2007","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0070","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.ygeno.2012.07.010","article-title":"Glutathione S-transferase (GST) genes in the red flour beetle, Tribolium castaneum, and comparative analysis with five additional insects","volume":"100","author":"Shi","year":"2012","journal-title":"Genomics"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0075","doi-asserted-by":"crossref","first-page":"1158","DOI":"10.1016\/j.ibmb.2008.08.002","article-title":"Identification, genomic organization and expression pattern of glutathione S-transferase in the silkworm, Bombyx mori","volume":"38","author":"Yu","year":"2008","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0080","doi-asserted-by":"crossref","first-page":"592","DOI":"10.1002\/ps.3884","article-title":"Identification and characterisation of multiple glutathione S-transferase genes from the diamondback moth, Plutella xylostella","volume":"71","author":"Chen","year":"2015","journal-title":"Pest Manag. Sci."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0085","article-title":"Genomic insights into the glutathione S-transferase gene family of two rice planthoppers, Nilaparvata lugens (St\u00e5l) and Sogatella furcifera (Horv\u00e1th) (Hemiptera: Delphacidae)","volume":"8","author":"Zhou","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0090","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/j.ibmb.2010.12.005","article-title":"The role of the Aedes aegypti Epsilon glutathione transferases in conferring resistance to DDT and pyrethroid insecticides","volume":"41","author":"Lumjuan","year":"2011","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0095","doi-asserted-by":"crossref","first-page":"358","DOI":"10.1016\/j.jmb.2010.04.020","article-title":"Recognition and detoxification of the insecticide DDT by Drosophila melanogaster glutathione S-transferase D1","volume":"399","author":"Low","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0100","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1016\/S0965-1748(00)00123-5","article-title":"Glutathione S-transferase in the defence against pyrethroids in insects","volume":"31","author":"Kostaropoulos","year":"2001","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0105","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1042\/bj3570065","article-title":"Glutathione S-transferases as antioxidant defence agents confer pyrethroid resistance in Nilaparvata lugens","volume":"357","author":"Vontas","year":"2001","journal-title":"Biochem. J."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0110","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.pestbp.2010.05.005","article-title":"Adult Drosophila melanogaster glutathione S-transferases: effects of acute treatment with methyl parathion","volume":"98","author":"Alias","year":"2010","journal-title":"Pestic. Biochem. Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0115","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1016\/S0965-1748(98)00049-6","article-title":"Molecular cloning and heterologous expression of a glutathione S-transferase involved in insecticide resistance from the diamondback moth, Plutella xylostella","volume":"28","author":"Huang","year":"1998","journal-title":"Insect Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0120","doi-asserted-by":"crossref","first-page":"94","DOI":"10.1016\/j.pestbp.2005.01.003","article-title":"Studies on glutathione S-transferase gene involved in chlorfluazuron resistance of the diamondback moth Plutella xylostella L. (Lepidoptera: Yplutellisae)","volume":"82","author":"Sonoda","year":"2005","journal-title":"Pestic. Biochem. Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0125","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1016\/j.jinsphys.2009.08.017","article-title":"Two epsilon glutathione S-transferase cDNAs from the common cutworm, Spodoptera litura: characterization and developmental and induced expression by insecticides","volume":"55","author":"Deng","year":"2009","journal-title":"J. Insect Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0130","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1016\/j.pestbp.2011.09.006","article-title":"Monitoring of beet armyworm Spodoptera exigua (Lepidoptera: Noctuidae) resistance to chlorantraniliprole in China","volume":"101","author":"Lai","year":"2011","journal-title":"Pestic. Biochem. Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0135","author":"APRD, Arthropod Pesticide Resistance Database"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0140","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1016\/S1226-8615(08)60315-5","article-title":"Relationship between feeding damage by beet armyworm, Spodoptera exigua (Lepidoptera: Noctuidae) and leaf trichome density of potato","volume":"9","author":"Kwon","year":"2006","journal-title":"J. Asia Pac. Entomol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0145","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1016\/j.aspen.2012.02.009","article-title":"Molecular cloning and characterization of a diapause-specific peptide in the beet armyworm, Spodoptera exigua","volume":"15","author":"Wan","year":"2012","journal-title":"J. Asia Pac. Entomol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0150","series-title":"PAUP\u204e. Phylogenetic Analysis Using Parsimony (\u204eand Other Methods), Version 4","author":"Swofford","year":"2000"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0155","doi-asserted-by":"crossref","first-page":"575","DOI":"10.1023\/A:1010301404445","article-title":"A defective viral genome maintained in Escherichia coli for the generation of baculovirus expression vectors","volume":"23","author":"Je","year":"2001","journal-title":"Biotechnol. Lett."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0160","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.dci.2013.05.016","article-title":"Developmental regulation and antifungal activity of a growth-blocking peptide from the beet armyworm Spodoptera exigua","volume":"41","author":"Wan","year":"2013","journal-title":"Dev. Comp. Immunol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0165","doi-asserted-by":"crossref","first-page":"272","DOI":"10.1016\/j.cbpb.2009.11.011","article-title":"Molecular cloning and characterization of 1-Cys and 2-Cys peroxiredoxins from the bumblebee Bombus ignitus","volume":"155","author":"Hu","year":"2010","journal-title":"Comp. Biochem. Physiol. B"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0170","doi-asserted-by":"crossref","first-page":"7130","DOI":"10.1016\/S0021-9258(19)42083-8","article-title":"Glutathione S-transferases. The first enzymatic step in mercapturic acid formation","volume":"249","author":"Habig","year":"1974","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0175","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1016\/j.pestbp.2015.01.009","article-title":"Functional characterization of glutathione S-transferases associated with insecticide resistance in Tetranychus urticae","volume":"121","author":"Pavlidi","year":"2015","journal-title":"Pestic. Biochem. Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0180","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1111\/j.1365-2583.2008.00808.x","article-title":"Transcriptomic profiles of Drosophila melanogaster third instar larval midgut and responses to oxidative stress","volume":"2","author":"Li","year":"2008","journal-title":"Insect Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0185","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3109\/10409238809088226","article-title":"Glutathione transferases structure and catalytic activity","volume":"23","author":"Mannervik","year":"1988","journal-title":"Crit. Rev. Biochem. Mol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0190","doi-asserted-by":"crossref","first-page":"2912","DOI":"10.1046\/j.1432-1327.2001.02179.x","article-title":"Catalytic function of Drosophila melanogaster glutathione S-transferase DmGSTS1-1 (GST-2) in conjugation of lipid peroxidation end products","volume":"268","author":"Singh","year":"2001","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0195","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1007\/s12192-012-0394-7","article-title":"Identification, genomic organization, and oxidative stress response of a sigma class glutathione S-transferase gene (AccGSTS1) in the honey bee, Apis cerana cerana","volume":"18","author":"Yan","year":"2013","journal-title":"Cell Stress Chaperones"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0200","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.ecoenv.2015.05.027","article-title":"Characterization of an epsilon-class glutathione S-transferase involved in tolerance in the silkworm larvae after long term exposure to insecticides","volume":"120","author":"Zhou","year":"2015","journal-title":"Ecotoxicol. Environ. Saf."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0205","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/0305-0491(89)90114-4","article-title":"The comparative enzymology of the glutathione S-transferases from non-vertebrate organisms","volume":"92","author":"Clark","year":"1989","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0210","article-title":"Characterization and functional analysis of four glutathione S-transferases from the migratory locust, Locusta migratoria","volume":"8","author":"Qin","year":"2013","journal-title":"PLoS ONE"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0215","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1016\/j.cbpb.2012.02.004","article-title":"First molluscan theta-class Glutathione S-Transferase: identification, cloning, characterization and transcriptional analysis post immune challenges","volume":"162","author":"Saranya Revathy","year":"2012","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0220","doi-asserted-by":"crossref","first-page":"2094","DOI":"10.1128\/JB.181.7.2094-2101.1999","article-title":"Purfication of a glutathione S-transferase and a glutathione conjugate-specific dehydrogenase involved in isoprene metabolism in Rhodococcus sp. strain AD45","volume":"181","author":"van Hylckama","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0225","first-page":"497","article-title":"Cu(II) and Cd(II) inhibition of rat liver glutathione S-transferase. A steady-state kinetic study","volume":"24","author":"Serafini","year":"1991","journal-title":"Biochem. Int."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0230","article-title":"Short communication direct effect of Cd on glutathione S-transferase and glutathione reductase from Calystegia sepium","volume":"465-473","author":"Lyubenova","year":"2007","journal-title":"Int. J. Phytoremediation"},{"key":"10.1016\/j.pestbp.2015.09.009_bb0235","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1016\/j.jinsphys.2011.10.011","article-title":"Heterologous expression and characterization of a sigma glutathione S-transferase involved in carbaryl detoxification from oriental migratory locust, Locusta migratoria manilensis (Meyen)","volume":"58","author":"Qin","year":"2012","journal-title":"J. Insect Physiol."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0240","doi-asserted-by":"crossref","first-page":"1840","DOI":"10.1016\/S0021-9258(18)46023-1","article-title":"Insect glutathione S-transferases. Biochemical characteristics of the major forms from houseflies susceptible and resistant to insecticides","volume":"267","author":"Fournier","year":"1992","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0245","doi-asserted-by":"crossref","first-page":"957","DOI":"10.1042\/bj20030169","article-title":"Heterologous expression of four glutathione transferase genes genetically linked to a major insecticide-resistance locus from the malaria vector Anopheles gambiae","volume":"373","author":"Ortelli","year":"2003","journal-title":"Biochem. J."},{"key":"10.1016\/j.pestbp.2015.09.009_bb0250","doi-asserted-by":"crossref","first-page":"228","DOI":"10.1016\/j.jsb.2008.08.003","article-title":"Structure of an insect epsilon class glutathione S-transferase from the malaria vector Anopheles gambiae provides an explanation for the high DDT-detoxifying activity","volume":"164","author":"Wang","year":"2008","journal-title":"J. Struct. Biol."}],"container-title":["Pesticide Biochemistry and Physiology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0048357515300341?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0048357515300341?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,5,22]],"date-time":"2022-05-22T09:09:40Z","timestamp":1653210580000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0048357515300341"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,9]]},"references-count":50,"alternative-id":["S0048357515300341"],"URL":"https:\/\/doi.org\/10.1016\/j.pestbp.2015.09.009","relation":{},"ISSN":["0048-3575"],"issn-type":[{"value":"0048-3575","type":"print"}],"subject":[],"published":{"date-parts":[[2016,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Identification and functional characterization of an epsilon glutathione S-transferase from the beet armyworm (Spodoptera exigua)","name":"articletitle","label":"Article Title"},{"value":"Pesticide Biochemistry and Physiology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.pestbp.2015.09.009","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2015 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}]}}