@article{clements_wiegmann_sorenson_smith_neese_roe_2000, title={Genetic variation in the Myzus persicae complex (Homoptera : Aphididae): Evidence for a single species}, volume={93}, ISSN={["1938-2901"]}, DOI={10.1603/0013-8746(2000)093[0031:GVITMP]2.0.CO;2}, abstractNote={Abstract Genetic variation was assessed for the closely related aphids Myzus nicotianae Blackman and Myzus persicae (Sulzer), previously classified as a single species. Populations of both red and green color morphs, collected from tobacco and nontobacco hosts from 3 continents, were analyzed via random amplified polymorphic DNA (RAPD)-polymerase chain reaction (PCR) and mitochondrial cytochrome oxidase II (COII) and elongation factor- 1 alpha (EF-1α) gene sequencing. Three other Myzus species—M. cerasi (F.), M. hemerocallis Takahashi, and M. varians Davidson)—were used as outgroups in our analyses. RAPD-PCR analysis revealed many, easily detectable genetic polymorphisms between the Myzus persicae complex and the outgroup species. The small number of polymorphisms detected within the complex were not correlated with host plant or the geographic origin of populations. The sequences of both COII and EF-1α for all populations within the M. persicae complex were identical, although significant variation was evident between the M. persicae complex and outgroup taxa. These results strongly suggest the synonymy of M. persicae and M. nicotianae.}, number={1}, journal={ANNALS OF THE ENTOMOLOGICAL SOCIETY OF AMERICA}, author={Clements, KM and Wiegmann, BM and Sorenson, CE and Smith, CF and Neese, PA and Roe, RM}, year={2000}, month={Jan}, pages={31–46} }
 @article{clements_sorenson_wiegmann_neese_roe_2000, title={Genetic, biochemical, and behavioral uniformity among populations of Myzus nicotianae and Myzus persicae}, volume={95}, ISSN={["1570-7458"]}, DOI={10.1046/j.1570-7458.2000.00666.x}, abstractNote={Abstract}, number={3}, journal={ENTOMOLOGIA EXPERIMENTALIS ET APPLICATA}, author={Clements, KM and Sorenson, CE and Wiegmann, BM and Neese, PA and Roe, RM}, year={2000}, month={Jun}, pages={269–281} }
 @article{clements_sorenson_wiegmann_roe_1999, title={Insecticide resistance in the Myzus persicae complex (Homoptera: Aphididae) with emphasis on tobacco pest management}, volume={3}, number={1}, journal={Reviews in Toxicology}, author={Clements, K. M. and Sorenson, C. E. and Wiegmann, B. M. and Roe, R. M.}, year={1999}, pages={1} }
 @article{cherrington_falls_rose_clements_philpot_levi_hodgson_1998, title={Molecular cloning, sequence, and expression of mouse flavin-containing monooxygenases 1 and 5 (FMO1 and FMO5)}, volume={12}, DOI={10.1002/(sici)1099-0461(1998)12:4<205::aid-jbt2>3.3.co;2-4}, abstractNote={Full-length cDNA clones encoding FMO1 and FMO5 have been isolated from a library constructed with mRNA from the liver of a female CD-1 mouse. The derived sequence of FMO1 contains 2310 bases: 1596 in the coding region, 301 in the 5′-flanking region, and 413 in the 3′-flanking region. The sequence for FMO5 consists of 3168 bases; 1599 in the coding region, 812 in the 5′-flanking region, and 757 in the 3′-flanking region. The sequence of FMO1 encodes a protein of 532 amino acids with a predicted molecular weight of 59.9 kDa and shows 83.3% identity to human FMO1 and 83–94% identity to other FMO1 homologs. FMO5 encodes a protein of 533 amino acids with a predicted molecular weight of 60.0 kDa and 84.1% identity to human FMO5 and 83–84% identity to other FMO5 orthologs. Two GxGxxG putative pyrophosphate binding domains exist beginning at positions 9 and 191 for FMO1, and 10 and 192 for FMO5. Mouse FMO1 and FMO5 were expressed in E. coli and show similar mobility to the native proteins as determined by SDS-PAGE. The expressed FMO1 protein showed activity toward methimazole, and FMO5 was active toward n -octylamine. In addition, FMO1 was shown to metabolize radiolabeled phorate, whereas FMO5 showed no activity toward phorate. © 1998 John Wiley & Sons, Inc. J Biochem Toxicol 12: 205–212, 1998}, number={1998}, journal={Journal of Biochemical and Molecular Toxicology}, author={Cherrington, N. J. and Falls, J. G. and Rose, R. L. and Clements, K. M. and Philpot, R. M. and Levi, P. E. and Hodgson, E.}, year={1998}, pages={205–212} }
 @article{falls_cherrington_clements_philpot_levi_rose_hodgson_1997, title={Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): Comparison with the human isoform}, volume={347}, ISSN={["0003-9861"]}, DOI={10.1006/abbi.1997.0322}, abstractNote={The sequence of mouse flavin-containing monooxygenase 3 (FMO3) was obtained from several clones isolated from a mouse liver cDNA library. The nucleotide sequence of mouse FMO3 was 2020 bases in length containing 37 bases in the 5' flanking region, 1602 in the coding region, and 381 in the 3' flanking region. The derived protein sequence consisted of 534 amino acids including the putative flavin adenine dinucleotide and NADP+ pyrophosphate binding sites (characteristic of mammalian FMOs) starting at positions 9 and 191, respectively. The mouse FMO3 protein sequence was 79 and 82% identical to the human and rabbit FMO3 sequences, respectively. Mouse FMO3 was expressed in Escherichia coli and compared to E. coli expressed human FMO3. The FMO3 proteins migrated with the same mobility ( approximately 58 kDa) as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting. The expressed FMO3 enzymes (mouse and human forms) were sensitive to heat and reacted in a similar manner toward metal ions and detergent. Catalytic activities of mouse and human FMO3 were high toward the substrate methimazole; however, in the presence of trimethylamine and thioacetamide, FMO-dependent methimazole oxidation by both enzymes was reduced by greater than 85%. Other substrates which inhibited methimazole oxidation were thiourea and thiobenzamide and to a lesser degree N,N-dimethylaniline. When probed with mouse FMO3 cDNA, FMO3 transcripts were detected in hepatic mRNA samples from female mice, but not in samples from males. FMO3 was detected in mRNA samples from male and female mouse lung, but FMO3 message was not detected in mouse kidney sample from either gender. Results of immunoblotting confirmed the tissue- and gender-dependent expression of mouse FMO3.}, number={1}, journal={ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS}, author={Falls, JG and Cherrington, NJ and Clements, KM and Philpot, RM and Levi, PE and Rose, RL and Hodgson, E}, year={1997}, month={Nov}, pages={9–18} }