@article{khalil_donohue_thompson_jeffers_ananthapadmanaban_sonenshine_mitchell_roe_2011, title={Full-length sequence, regulation and developmental studies of a second vitellogenin gene from the American dog tick, Dermacentor variabilis}, volume={57}, ISSN={["1879-1611"]}, DOI={10.1016/j.jinsphys.2010.12.008}, abstractNote={Vitellogenin (Vg) is the precursor of vitellin (Vn) which is the major yolk protein in eggs. In a previous report, we isolated and characterized the first Vg message from the American dog tick Dermacentor variabilis. In the current study, we describe a second Vg gene from the same tick. The Vg2 cDNA is 5956 nucleotides with a 5775 nt open reading frame coding for 1925 amino acids. The conceptual amino acid translation contains a 16-residues putative signal peptide, N-terminal lipid binding domain and C-terminal von Willebrand factor type D domain present in all known Vgs. Moreover, the amino acid sequence shows a typical GLCG domain and several RXXR cleavage sites present in most isolated Vgs. Tryptic digest-mass fingerprinting of Vg and Vn recognized 11 fragments that exist in the amino acid translation of DvVg2 cDNA. Injection of virgin females with 20 hydroxyecdysone induced DvVg2 expression, vitellogenesis and oviposition. Using RT-PCR, DvVg2 expression was detected only in tick females after mating and feeding to repletion. Northern blot analysis showed that DvVg2 is expressed in fat body and gut cells of vitellogenic females but not in the ovary. DvVg2 expression was not detected in adult fed or unfed males. The characteristics that distinguish Vg from other similar tick storage proteins like the carrier protein, CP (another hemelipoglycoprotein) are discussed.}, number={3}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Khalil, Sayed M. S. and Donohue, Kevin V. and Thompson, Deborah M. and Jeffers, Laura A. and Ananthapadmanaban, Usha and Sonenshine, Daniel E. and Mitchell, Robert D. and Roe, R. Michael}, year={2011}, month={Mar}, pages={400–408} }
 @misc{henkens_o'daly_wojciechowski_zhang_r._n._r._t._d._r._et al._2007, title={Electrochemical detection of nucleic acid sequences}, volume={7,169,358}, number={2007 Jan. 30}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Henkens, R. and O'Daly, J. and Wojciechowski, M. and Zhang, H. and R., Naser and N., Roe and R., Stewart and T., Thompson and D., Sundseth and R. and et al.}, year={2007} }
 @article{mitchell_ross_osgood_sonenshine_donohue_khalil_thompson_roe_2007, title={Molecular characterization, tissue-specific expression and RNAi knockdown of the first vitellogenin receptor from a tick}, volume={37}, ISSN={["1879-0240"]}, DOI={10.1016/j.ibmb.2007.01.005}, abstractNote={This is the first full-length message for a vitellogenin receptor (VgR) sequenced from ticks. VgRs, members of the low-density lipoprotein receptor (LDLR) superfamily, mediate the uptake of the yolk protein, vitellogenin (Vg), from the hemolymph. The VgR message from the American dog tick, Dermacentor variabilis (GenBank accession No. DQ103506.4) comprised 5673 bp which coded for a 1798 aa deduced protein with a predicted 196.6 kDa molecular mass. After removing the 20 aa signal peptide, the 1778 aa deduced mature protein had a predicted 196.6 kDa molecular mass. BLAST comparisons showed the highest similarity to the VgR of the cockroach, Periplaneta americana. VgR message was expressed in mated female ovary but absent in female midgut and salivary glands or whole body mRNA from blood fed males, indicating that it is both sex and tissue specific. VgR transcript was absent in virgin (previtellogenic) females but present in ovaries of mated females following drop off. RNAi showed that unfed adult ticks injected with a VgR-dsRNA probe failed to lay eggs, develop brown eggs or fully express VgR transcript (Northern blots). In contrast, controls oviposited numerous normal brown eggs and showed strong expression of VgR transcripts. These results show that the expression of the VgR message is essential for Vg uptake and egg development in the American dog tick.}, number={4}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Mitchell, Robert D., III and Ross, Elizabeth and Osgood, Christopher and Sonenshine, Daniel E. and Donohue, Kevin V. and Khalil, Sayed M. and Thompson, Deborah M. and Roe, R. Michael}, year={2007}, month={Apr}, pages={375–388} }
 @article{deborah_khalil_jeffers_sonenshine_mitchell_osgood_roe_2007, title={Sequence and the developmental and tissue-specific regulation of the first complete vitellogenin messenger RNA from ticks responsible for heme sequestration}, volume={37}, ISSN={["0965-1748"]}, DOI={10.1016/j.ibmb.2007.01.004}, abstractNote={The first full-length mRNA for vitellogenin (Vg) from ticks was sequenced. This also represents the first complete sequence of Vg from the Chelicerata and of a heme binding Vg. The Vg cDNA from the American dog tick, Dermacentor variabilis was 5744nt in length (GenBank Accession number AY885250), which coded for a protein of 1843 aa with a calculated molecular weight of 208 kD. This protein had an 18 aa signal sequence, a single RXXR cleavage signal that would generate two subunits (49.5 and 157K in molecular weight) and lipoprotein N-terminal and carboxy von Willebrand factor type D domains. Tryptic digest MS analysis of vitellin protein confirmed the function of the cDNA as the tick yolk protein. Apparently, vitellin in D. variabilis is oligomeric (possibly dimeric) and is comprised of a mixture of the uncleaved monomer and subunits that were predicted from the single RXXR cleavage signal. The highly conserved GL/ICG motif close to the C-terminus in insect Vg genes was different in the tick Vg message, i.e., GLCS. This variant was also present in a partial sequence of Vg from Boophilus microplus. Phylogenic analysis showed that the full length Vg cDNA from D. variabilis and the partial cDNA from B. microplus were distinct from insects and Crustacea. The Vg message was not found in whole body RNA from unfed or fed males or in unfed and partially fed (virgin) females as determined by Northern blotting. The message was found in replete (mated) pre-ovipositional females, increased to higher levels in ovipositing females and was absent after egg laying was complete. The endocrine regulation of the Vg mRNA is discussed. The tissue sources of the Vg message are both the gut and fat body. Tryptic digest MS fingerprinting suggests that a second Vg mRNA might be present in the American dog tick, which needs further study.}, number={4}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Deborah, M. Thompson and Khalil, Sayed M. S. and Jeffers, Laura A. and Sonenshine, Daniel E. and Mitchell, Robert D. and Osgood, Christopher J. and Roe, R. Michael}, year={2007}, month={Apr}, pages={363–374} }
 @article{thompson_khalil_jeffers_ananthapadmanaban_sonenshine_mitchell_osgood_apperson_roe_2005, title={In vivo role of 20-hydroxyecdysone in the regulation of the vitellogenin mRNA and egg development in the American dog tick, Dermacentor variabilis (Say)}, volume={51}, ISSN={["1879-1611"]}, DOI={10.1016/j.jinsphys.2005.05.011}, abstractNote={Injection of the hormone 20-hydroxyecdysone (20-E) into partially fed (virgin) female adults of the American dog tick, Dermacentor variabilis, while they are attached and feeding on the rabbit host, initiated the expression of the vitellogenin (Vg) gene, and Vg protein secretion and uptake by the ovary. The induction of egg production by 20-E in this bioassay was dose dependent in the range of 1–50 times the concentration normally found in a replete, vitellogenic female. Ticks examined 4 d after the 50× treatment were still attached to the host, had numerous enlarged vitellin-filled (brown) oocytes in their ovaries, but had not engorged to repletion. The ovaries reached weights similar to those found in untreated, replete (mated) females (pre-oviposition) while solvent-injected controls demonstrated no increase in oocyte size or increase in ovary weight. An increase in the levels of a putative Vg protein was observed in hemolymph samples collected 1, 2 and 3 d post-20-E injection but was not observed in the corresponding solvent controls as determined by native PAGE. Analysis of the ecdysteroid-induced protein by tryptic digestion-mass fingerprinting and BLASTP found that the putative Vg had the strongest match to GP80 (U49934), the partial sequence for the vitellogenin protein from Boophilus microplus. A partial Vg cDNA was cloned and sequenced from replete females of D. variabilis with a high similarity to GP80. Using this message as a probe, Northern blots conducted with RNA collected from partially fed, virgin females 1, 2 and 3 d post-20-E injection showed upregulation of the Vg mRNA on all 3 days. Controls injected with solvent only showed no Vg mRNA. Injections with juvenile hormone III did not stimulate Vg expression, oocyte growth or full engorgement. These studies indicate that ecdysteroids and not JH can initiate expression of the Vg gene, Vg protein synthesis and release into hemolymph, and Vg uptake into developing oocytes under bioassay conditions mimicking normal feeding on the host.}, number={10}, journal={JOURNAL OF INSECT PHYSIOLOGY}, author={Thompson, DM and Khalil, SMS and Jeffers, LA and Ananthapadmanaban, U and Sonenshine, DE and Mitchell, RD and Osgood, CJ and Apperson, CS and Roe, RM}, year={2005}, month={Oct}, pages={1105–1116} }
 @article{jeffers_thompson_ben-yakir_roe_2005, title={Movement of proteins across the digestive system of the tobacco budworm, Heliothis virescens}, volume={117}, ISSN={["1570-7458"]}, DOI={10.1111/j.1570-7458.2005.00342.x}, abstractNote={Abstract}, number={2}, journal={ENTOMOLOGIA EXPERIMENTALIS ET APPLICATA}, author={Jeffers, LA and Thompson, DM and Ben-Yakir, D and Roe, RM}, year={2005}, month={Nov}, pages={135–146} }
 @article{vanderherchen_isherwood_thompson_linderman_roe_2005, title={Toxicity of novel aromatic and aliphatic organic acid and ester analogs of trypsin modulating oostatic factor to larvae of the northern house mosquito, Culex pipiens complex, and the tobacco hornworm, Manduca sexta}, volume={81}, ISSN={["1095-9939"]}, DOI={10.1016/j.pestbp.2004.09.006}, abstractNote={Eight non-peptidic chemical analogs of trypsin modulating oostatic factor (TMOF, NH2-YDPAP6), an insect hormone inhibiting trypsin biosynthesis in mosquitoes, were synthesized based on the structure of the native peptide. The median lethal concentration (LC50) for the chemical analogs, TMOF and FDPAP (a peptidic analog of TMOF) was estimated for larvae of the northern house mosquito, the Culex pipiens complex, using a static 5-day bioassay. Four of these compounds demonstrated the same larvicidal activity as TMOF, while three of these compounds were 1.2–2.5-fold more active than TMOF. The compounds introduced by injection were toxic to fourth instars of the tobacco hornworm, Manduca sexta, except for TMOF, FDPAP, and PPHEN. Injection of TMOF and FDPAP into fourth stadium and TMOF into second stadium M. sexta had no effect on trypsin activity, growth, or mortality. Apparently the mosquito hormone is inactive in the tobacco hornworm at the developmental stages examined. Three TMOF analogs (CHEA, PHEA, and PHA) demonstrating the highest activity by injection in M. sexta were also found to be toxic by injection in fourth instars of the tobacco budworm, Heliothis virescens, and the cotton bollworm, Helicoverpa zea, as well as adult male German cockroaches, Blattela germanica. A two-choice feeding bioassay with H. virescens indicated that at least one of the TMOF analogs, PHEA, has anti-feeding properties.}, number={2}, journal={PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY}, author={Vanderherchen, MB and Isherwood, M and Thompson, DM and Linderman, RJ and Roe, RM}, year={2005}, month={Feb}, pages={71–84} }
 @article{thompson_young_edens_olmstead_leblanc_hodgson_roe_2004, title={Non-target toxicology of a new mosquito larvicide, trypsin modulating oostatic factor}, volume={80}, ISSN={["1095-9939"]}, DOI={10.1016/j.pestbp.2004.06.009}, abstractNote={Trypsin modulating oostatic factor (TMOF), a peptide hormone originally isolated from the ovaries of adult Aedes aegypti, is currently under commercial development as a new pesticide chemistry with a novel mode of action for the control of larval mosquitoes. The objective of the current research is to evaluate potential risks of the use of TMOF as an insecticide on non-target organisms. TMOF (YDPAP6) was degraded in vitro (as determined by HPLC and LC/MS) to DPAP6, PAP6, and then AP6 by leucine aminopeptidase, a pancreatic enzyme found in the digestive system of vertebrates. The rate of degradation of TMOF and PAP6 was significantly greater than that of DPAP6, while no metabolism of AP6 was found. TMOF technical insecticide was produced on a commercial scale by recombinant yeast (heat-killed before application). The technical TMOF when administered in a single dose by gavage to male and female mice at 2000 mg dry weight/kg body weight produced no negative effects as compared to controls up to 12 days after treatment. When male and female mallard ducks were treated by gavage with 1250 mg dry weight of technical TMOF/kg body weight each day for 5 days, again no toxic effects were noted through 35 days after the last treatment. TMOF technical insecticide was also applied to the shaved skin of male and female rabbits at the rate of 2000 mg/kg for 1–2 days, with no effect. The end point observations in these in vivo experiments were mortality; changes in growth rate, behavior, body structure, and color; and possible lesions observed during necropsy. Finally, Daphnia incubated with technical TMOF in rearing water at the level of 1.0 × 106 yeast cells/ml (10 mg/ml) also demonstrated no negative effects on mortality, growth, molting, time to first brood, and production of viable neonates. It appears from these studies that TMOF can be degraded by vertebrate digestive proteases and technical TMOF is not toxic to the non-target organisms examined.}, number={3}, journal={PESTICIDE BIOCHEMISTRY AND PHYSIOLOGY}, author={Thompson, DM and Young, HP and Edens, FW and Olmstead, AW and LeBlanc, GA and Hodgson, E and Roe, RM}, year={2004}, month={Nov}, pages={131–142} }
 @misc{linderman_roe_thompson_vanderherehen_2003, title={Pesticidal activity of functionalized alkenes}, volume={6,660,770}, number={2003 Dec. 9}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Linderman, R. J. and Roe, R. M. and Thompson, D. M. and Vanderherehen, M.}, year={2003} }
 @misc{henkens_o'daly_wojciechowski_zhang_r._n._r._t._d._r._et al._2002, title={Electrochemical detection of nucleic acid sequences}, volume={6,391,558}, number={2002 May 21}, publisher={Washington, DC: U.S. Patent and Trademark Office}, author={Henkens, R. and O'Daly, J. and Wojciechowski, M. and Zhang, H. and R., Naser and N., Roe and R., Stewart and T., Thompson and D., Sundseth and R. and et al.}, year={2002} }
 @article{linderman_roe_harris_thompson_2000, title={Inhibition of insect juvenile hormone epoxide hydrolase: asymmetric synthesis and assay of glycidol-ester and epoxy-ester inhibitors of Trichoplusia ni epoxide hydrolase}, volume={30}, ISSN={["0965-1748"]}, DOI={10.1016/S0965-1748(00)00048-5}, abstractNote={Juvenile hormone (JH) undergoes metabolic degradation by two major pathways involving JH esterase and JH epoxide hydrolase (EH). While considerable effort has been focussed on the study of JH esterase and the development of inhibitors for this enzyme, much less has been reported on the study of JH-EH. In this work, the asymmetric synthesis of two classes of inhibitors of recombinant JH-EH from Trichoplusia ni, a glycidol-ester series and an epoxy-ester series is reported. The most effective glycidol-ester inhibitor, compound 1, exhibited an I(50) of 1.2x10(-8) M, and the most effective epoxy-ester inhibitor, compound 11, exhibited an I(50) of 9.4x10(-8) M. The potency of the inhibitors was found to be dependent on the absolute configuration of the epoxide. In both series of inhibitors, the C-10 R-configuration was found to be significantly more potent that the corresponding C-10 S-configuration. A mechanism for epoxide hydration catalyzed by insect EH is also presented.}, number={8-9}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Linderman, RJ and Roe, RM and Harris, SV and Thompson, DM}, year={2000}, pages={767–774} }
 @article{harris_thompson_linderman_tomalski_roe_1999, title={Cloning and expression of a novel juvenile hormone-metabolizing epoxide hydrolase during larval-pupal metamorphosis of the cabbage looper, Trichoplusia ni}, volume={8}, ISSN={["1365-2583"]}, DOI={10.1046/j.1365-2583.1999.810085.x}, abstractNote={Abstract}, number={1}, journal={INSECT MOLECULAR BIOLOGY}, author={Harris, SV and Thompson, DM and Linderman, RJ and Tomalski, MD and Roe, RM}, year={1999}, month={Feb}, pages={85–96} }
 @article{roe_hodgson_rose_thompson_devorshak_anspaugh_linderman_harris_tomalski_1998, title={Basic principles and rationale for the use of insect genes in bioremediation: esterases, phosphotriesterase, cytochrome P450 and epoxide hydrolase}, volume={2}, number={1998}, journal={Reviews in Toxicology}, author={Roe, R. M. and Hodgson, E. and Rose, R. L. and Thompson, D. M. and Devorshak, C. and Anspaugh, D. D. and Linderman, R. J. and Harris, S. V. and Tomalski, M. D.}, year={1998}, pages={169–178} }
 @article{rose_goh_thompson_verma_heckel_gahan_roe_hodgson_1997, title={Cytochrome P450 (CYP)9A1 in Heliothis virescens: The first member of a new CYP family}, volume={27}, ISSN={["1879-0240"]}, DOI={10.1016/S0965-1748(97)00036-2}, abstractNote={A novel cytochrome P450 cDNA with its complete coding sequence and part or all of the 3' (77 nucleotides) and 5' (87 nucleotides) non-coding sequence was isolated from the tobacco budworm, Heliothis virescens (F). The 1763 nucleotide sequence encodes a protein of 532 amino acids which includes a hydrophobic N-terminal region and the highly conserved heme binding regions typical of P450s. Low sequence similarity to other P450 sequences and the presence of a thromboxane synthase-like insertion upstream from the I helix resulted in its assignment as the first member of family 9, i.e. CYP9A1. CYP9A1 is most similar to CYP3A1 from the rat (34.7% identity), but is also similar to the insect P450s from family 6, including CYP6B1v1 from Papilio polyxenes (33.3%), CYP6A2A from Drosophila melanogaster (32.4%), CYP6A3 from Musca domestica (31.7%) and CYP6B2 from Helicoverpa armigera (30.1%). Comparative Western and Northern blot studies indicate that expression of CYP9A1 in thiodicarb selected populations of tobacco budworm is associated with insecticide resistance. The pattern of restriction fragment length polymorphism (RELP) variation in offspring of single-pair matings demonstrated autosomal inheritance of CYP9A1 and enabled its assignment to linkage group 7. The coding region of CYP9A1 occupies no more than 10 kb in the tobacco budworm genome.}, number={6}, journal={INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY}, author={Rose, RL and Goh, D and Thompson, DM and Verma, KD and Heckel, DG and Gahan, LJ and Roe, RM and Hodgson, E}, year={1997}, month={Jun}, pages={605–615} }
 @article{thompson_anspaugh_gahan_heckel_roe_1996, title={Cloning of a putative juvenile hormone-responsive storage protein gene from the tobacco budworm, Heliothis virescens}, volume={32}, number={3}, journal={Archives of Insect Biochemistry and Physiology}, author={Thompson, D. M. and Anspaugh, D. D. and Gahan, L. J. and Heckel, D. G. and Roe, R. M.}, year={1996}, pages={439} }