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dc.contributor.authorJeerang Wongtrakulen_US
dc.contributor.authorJantana Wongsantichonen_US
dc.contributor.authorArdcharaporn Vararattanavechen_US
dc.contributor.authorPosri Leelapaten_US
dc.contributor.authorLa Aied Prapanthadaraen_US
dc.contributor.authorAlbert J. Kettermanen_US
dc.contributor.otherChiang Mai Universityen_US
dc.contributor.otherMahidol Universityen_US
dc.date.accessioned2018-09-13T06:27:40Z-
dc.date.available2018-09-13T06:27:40Z-
dc.date.issued2009-01-01en_US
dc.identifier.citationProtein and Peptide Letters. Vol.16, No.1 (2009), 75-81en_US
dc.identifier.issn09298665en_US
dc.identifier.other2-s2.0-61549105346en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=61549105346&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/27309-
dc.description.abstractGlutathione transferases, GSTs, are detoxification proteins that are found in most organisms. The acGSTE3-3 had the ability to conjugate 4-hydroxynonenal, a cytotoxic lipid peroxidation product. Although other Epsilon GSTs showed roles in insecticide metabolism, the acGSTE3-3 appeared to have a major role in detoxifying lipid peroxidation products conferring protection against oxidative damage. © 2009 Bentham Science Publishers Ltd.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=61549105346&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleMolecular cloning and expression of several new anopheles cracens epsilon class glutathione transferasesen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.2174/092986609787049367en_US
Appears in Collections:Scopus 2006-2010

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