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DC Field | Value | Language |
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dc.contributor.author | Jeerang Wongtrakul | en_US |
dc.contributor.author | Jantana Wongsantichon | en_US |
dc.contributor.author | Ardcharaporn Vararattanavech | en_US |
dc.contributor.author | Posri Leelapat | en_US |
dc.contributor.author | La Aied Prapanthadara | en_US |
dc.contributor.author | Albert J. Ketterman | en_US |
dc.date.accessioned | 2018-09-10T03:14:49Z | - |
dc.date.available | 2018-09-10T03:14:49Z | - |
dc.date.issued | 2009-01-01 | en_US |
dc.identifier.issn | 09298665 | en_US |
dc.identifier.other | 2-s2.0-61549105346 | en_US |
dc.identifier.other | 10.2174/092986609787049367 | en_US |
dc.identifier.uri | https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=61549105346&origin=inward | en_US |
dc.identifier.uri | http://cmuir.cmu.ac.th/jspui/handle/6653943832/59409 | - |
dc.description.abstract | Glutathione 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.subject | Biochemistry, Genetics and Molecular Biology | en_US |
dc.title | Molecular cloning and expression of several new anopheles cracens epsilon class glutathione transferases | en_US |
dc.type | Journal | en_US |
article.title.sourcetitle | Protein and Peptide Letters | en_US |
article.volume | 16 | en_US |
article.stream.affiliations | Chiang Mai University | en_US |
article.stream.affiliations | Mahidol University | en_US |
Appears in Collections: | CMUL: Journal Articles |
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