Structure and function of an insect -carboxylesterase ( Esterase7) associated with insecticide resistance-Reference-Cited by-同舟云学术

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Structure and function of an insect -carboxylesterase ( Esterase7) associated with insecticide resistance

Published:2013-06-03 Issue:25 Volume:110 Page:10177-10182
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Jackson C. J.,Liu J.-W.,Carr P. D.,Younus F.,Coppin C.,Meirelles T.,Lethier M.,Pandey G.,Ollis D. L.,Russell R. J.,Weik M.,Oakeshott J. G.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference47 articles.

1. A single amino acid substitution converts a carboxylesterase to an organophosphorus hydrolase and confers insecticide resistance on a blowfly

2. Organophosphate poisoning

3. Functional fat body proteomics and gene targeting reveal in vivo functions of Drosophila melanogaster α-Esterase-7

4. Two different amino acid substitutions in the ali-esterase, E3, confer alternative types of organophosphorus insecticide resistance in the sheep blowfly, Lucilia cuprina

5. Developmental expression and gene/enzyme identifications in the alpha esterase gene cluster of Drosophila melanogaster

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