메뉴 건너뛰기




Volumn 172, Issue 1-2, 2010, Pages 114-121

Baculovirus expression, biochemical characterization and organophosphate sensitivity of rBmAChE1, rBmAChE2, and rBmAChE3 of Rhipicephalus (Boophilus) microplus

Author keywords

Acari; Acaricide resistance; Acetylcholinesterase; AChE; Cattle fever tick; Ixodidae

Indexed keywords

1,5 BIS(4 ALLYLDIMETHYLAMMONIUMPHENYL)PENTAN 3 ONE DIBROMIDE; ACETYLCHOLINESTERASE; ACETYLCHOLINESTERASE 1; ACETYLCHOLINESTERASE 2; ACETYLCHOLINESTERASE 3; ACETYLTHIOCHOLINE; COMPLEMENTARY DNA; ISO OMPA; MALAOXON; ORGANOPHOSPHATE; PARAOXON; PHYSOSTIGMINE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 77955336022     PISSN: 03044017     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.vetpar.2010.04.016     Document Type: Article
Times cited : (50)

References (66)
  • 1
    • 77955248113 scopus 로고    scopus 로고
    • Developmental aspects of the cholinergic system
    • in press, doi: 10.1016/j.bbr.2009.12.049
    • Abreu-Villaça, Y., Filgueiras, C.C., Manhães, A.C., in press. Developmental aspects of the cholinergic system, Behav. Brain Res, doi: 10.1016/j.bbr.2009.12.049.
    • Behav. Brain Res
    • Abreu-Villaça, Y.1    Filgueiras, C.C.2    Manhães, A.C.3
  • 2
    • 0032143668 scopus 로고    scopus 로고
    • Acetylcholinesterase cDNA of the cattle tick, Boophilus microplus: characterisation and role in organophosphate resistance
    • Baxter G.D., Barker S.C. Acetylcholinesterase cDNA of the cattle tick, Boophilus microplus: characterisation and role in organophosphate resistance. Insect Biochem. Mol. Biol. 1998, 28:581-589.
    • (1998) Insect Biochem. Mol. Biol. , vol.28 , pp. 581-589
    • Baxter, G.D.1    Barker, S.C.2
  • 3
    • 0032752206 scopus 로고    scopus 로고
    • Comparison of acetylcholinesterase genes from cattle ticks
    • Baxter G.D., Barker S.C. Comparison of acetylcholinesterase genes from cattle ticks. Int. J. Parasitol. 1999, 29:1765-1774.
    • (1999) Int. J. Parasitol. , vol.29 , pp. 1765-1774
    • Baxter, G.D.1    Barker, S.C.2
  • 4
    • 0036015626 scopus 로고    scopus 로고
    • Analysis of the sequence and expression of a second putative acetylcholinesterase cDNA from organophosphate-susceptible and organophosphate-resistant cattle ticks
    • Baxter G.D., Barker S.C. Analysis of the sequence and expression of a second putative acetylcholinesterase cDNA from organophosphate-susceptible and organophosphate-resistant cattle ticks. Insect Biochem. Mol. Biol. 2002, 32:815-820.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 815-820
    • Baxter, G.D.1    Barker, S.C.2
  • 5
    • 0031011594 scopus 로고    scopus 로고
    • Analysis of molecular forms and pharmacological properties of acetylcholinesterase in several mosquito species
    • Bourguet D., Roig A., Toutant J.-P., Arpagaus M. Analysis of molecular forms and pharmacological properties of acetylcholinesterase in several mosquito species. Neurochem. Int. 1997, 31:65-72.
    • (1997) Neurochem. Int. , vol.31 , pp. 65-72
    • Bourguet, D.1    Roig, A.2    Toutant, J.-P.3    Arpagaus, M.4
  • 6
    • 0023972530 scopus 로고
    • Metabolism of coumaphos in susceptible and resistant strains of Boophilus microplus (Acari: Ixodidae)
    • Bull D.L., Ahrens E.H. Metabolism of coumaphos in susceptible and resistant strains of Boophilus microplus (Acari: Ixodidae). J. Med. Entomol. 1988, 25:94-98.
    • (1988) J. Med. Entomol. , vol.25 , pp. 94-98
    • Bull, D.L.1    Ahrens, E.H.2
  • 9
    • 0034697999 scopus 로고    scopus 로고
    • Four genes encode acetylcholinesterase in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression
    • Combes D., Fedon Y., Grauso M., Toutant J.-P., Arpagaus M. Four genes encode acetylcholinesterase in the nematodes Caenorhabditis elegans and Caenorhabditis briggsae. cDNA sequences, genomic structures, mutations and in vivo expression. J. Mol. Biol. 2000, 300:727-742.
    • (2000) J. Mol. Biol. , vol.300 , pp. 727-742
    • Combes, D.1    Fedon, Y.2    Grauso, M.3    Toutant, J.-P.4    Arpagaus, M.5
  • 11
    • 0027535179 scopus 로고
    • Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins
    • Cygler M., Schrag J.D., Sussman J.L., Harel M., Silman I., Gentry M.K., Doctor B.P. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci. 1993, 2:366-382.
    • (1993) Protein Sci. , vol.2 , pp. 366-382
    • Cygler, M.1    Schrag, J.D.2    Sussman, J.L.3    Harel, M.4    Silman, I.5    Gentry, M.K.6    Doctor, B.P.7
  • 13
    • 0038515076 scopus 로고    scopus 로고
    • Efficacy of various concentrations of coumaphos to control adult, nymphal, and larval stages of an organophosphate-resistant strain of Boophilus microplus on infested cattle
    • Davey R.B., George J.E., Miller R.J. Efficacy of various concentrations of coumaphos to control adult, nymphal, and larval stages of an organophosphate-resistant strain of Boophilus microplus on infested cattle. Am. J. Vet. Res. 2003, 64:684-689.
    • (2003) Am. J. Vet. Res. , vol.64 , pp. 684-689
    • Davey, R.B.1    George, J.E.2    Miller, R.J.3
  • 14
    • 0026503135 scopus 로고
    • Drosophila acetylcholinesterase - expression of a functional precursor in Xenopus oocytes
    • Fournier D., Mutero A., Rungger D. Drosophila acetylcholinesterase - expression of a functional precursor in Xenopus oocytes. Eur. J. Biochem. 1992, 203:513-519.
    • (1992) Eur. J. Biochem. , vol.203 , pp. 513-519
    • Fournier, D.1    Mutero, A.2    Rungger, D.3
  • 16
    • 0034808451 scopus 로고    scopus 로고
    • An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics
    • Gao J.-R., Zhu K.Y. An acetylcholinesterase purified from the greenbug (Schizaphis graminum) with some unique enzymological and pharmacological characteristics. Insect Biochem. Mol. Biol. 2001, 31:1095-1104.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 1095-1104
    • Gao, J.-R.1    Zhu, K.Y.2
  • 17
    • 0043129820 scopus 로고    scopus 로고
    • The campaign to keep Boophilus ticks out of the United States: technical problems and solutions
    • G.G. Wagner, W.W. Buisch (Eds.)
    • George J.E. The campaign to keep Boophilus ticks out of the United States: technical problems and solutions. Proceedings of the 100th Annual Meeting of the U.S. Animal Health Assoc. 1996, 196-206. G.G. Wagner, W.W. Buisch (Eds.).
    • (1996) Proceedings of the 100th Annual Meeting of the U.S. Animal Health Assoc. , pp. 196-206
    • George, J.E.1
  • 18
    • 0030808310 scopus 로고    scopus 로고
    • Interactions underlying subunit associations in cholinesterases
    • Giles K. Interactions underlying subunit associations in cholinesterases. Protein Eng. 1997, 10:677-685.
    • (1997) Protein Eng. , vol.10 , pp. 677-685
    • Giles, K.1
  • 19
    • 0017779755 scopus 로고
    • Eradication programs for the arthropod parasites of livestock
    • Graham O.H., Hourrigan J.L. Eradication programs for the arthropod parasites of livestock. J. Med. Entomol. 1977, 13:629-658.
    • (1977) J. Med. Entomol. , vol.13 , pp. 629-658
    • Graham, O.H.1    Hourrigan, J.L.2
  • 20
    • 38549159882 scopus 로고    scopus 로고
    • Non-hydrolytic functions of acetylcholinesterase. The significance of C-terminal peptides
    • Greenfield S.A., Zimmermann M., Bond C.E. Non-hydrolytic functions of acetylcholinesterase. The significance of C-terminal peptides. FEBS J. 2008, 275:604-611.
    • (2008) FEBS J. , vol.275 , pp. 604-611
    • Greenfield, S.A.1    Zimmermann, M.2    Bond, C.E.3
  • 22
    • 0033220206 scopus 로고    scopus 로고
    • Cloning and sequencing of a putative acetylcholinesterase from Boophilus microplus (Acari: Ixodidae)
    • Hernandez R.H., He H., Chen A.C., Ivy G.W., George J.E., Wagner G.G. Cloning and sequencing of a putative acetylcholinesterase from Boophilus microplus (Acari: Ixodidae). J. Med. Entomol. 1999, 36:764-770.
    • (1999) J. Med. Entomol. , vol.36 , pp. 764-770
    • Hernandez, R.H.1    He, H.2    Chen, A.C.3    Ivy, G.W.4    George, J.E.5    Wagner, G.G.6
  • 24
    • 77149168461 scopus 로고    scopus 로고
    • Acetylcholinesterase of the cat flea Ctenocephalides felis: identification of two distinct genes and biochemical characterization of recombinant and in vivo enzyme activities
    • Ilg T., Schmalz S., Werr M., Cramer J. Acetylcholinesterase of the cat flea Ctenocephalides felis: identification of two distinct genes and biochemical characterization of recombinant and in vivo enzyme activities. Insect Biochem. Mol. Biol. 2010, 40:153-164.
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 153-164
    • Ilg, T.1    Schmalz, S.2    Werr, M.3    Cramer, J.4
  • 25
    • 38549098085 scopus 로고    scopus 로고
    • Amyloid-cholinesterase interactions. Implications for Alzheimer's disease
    • Inestrosa N.C., Dinamarca M.C., Alvarez A. Amyloid-cholinesterase interactions. Implications for Alzheimer's disease. FEBS J. 2008, 275:625-632.
    • (2008) FEBS J. , vol.275 , pp. 625-632
    • Inestrosa, N.C.1    Dinamarca, M.C.2    Alvarez, A.3
  • 26
    • 68749089501 scopus 로고    scopus 로고
    • Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae
    • Jiang H., Liu S., Zhao P., Pope C. Recombinant expression and biochemical characterization of the catalytic domain of acetylcholinesterase-1 from the African malaria mosquito, Anopheles gambiae. Insect Biochem. Mol. Biol. 2009, 39:646-653.
    • (2009) Insect Biochem. Mol. Biol. , vol.39 , pp. 646-653
    • Jiang, H.1    Liu, S.2    Zhao, P.3    Pope, C.4
  • 27
    • 38549144587 scopus 로고    scopus 로고
    • Acetylcholinesterase and apoptosis. A novel perspective for an old enzyme
    • Jiang H., Zhang X.-J. Acetylcholinesterase and apoptosis. A novel perspective for an old enzyme. FEBS J. 2008, 275:612-617.
    • (2008) FEBS J. , vol.275 , pp. 612-617
    • Jiang, H.1    Zhang, X.-J.2
  • 28
    • 52449122884 scopus 로고    scopus 로고
    • Non-enzymatic developmental functions of acetylcholinesterase - the question of redundancy
    • Johnson G., Swart C., Moore S.W. Non-enzymatic developmental functions of acetylcholinesterase - the question of redundancy. FEBS J. 2008, 275:5129-5138.
    • (2008) FEBS J. , vol.275 , pp. 5129-5138
    • Johnson, G.1    Swart, C.2    Moore, S.W.3
  • 29
    • 52049090209 scopus 로고    scopus 로고
    • Comparison of two acetylcholinesterase gene cDNAs of the lesser mealworm, Alphitobius diaperinus, in insecticide susceptible and resistant strains
    • Kozaki T., Kimmelblatt B.A., Hamm R.L., Scott J.G. Comparison of two acetylcholinesterase gene cDNAs of the lesser mealworm, Alphitobius diaperinus, in insecticide susceptible and resistant strains. Arch. Insect Biochem. Physiol. 2008, 67:130-138.
    • (2008) Arch. Insect Biochem. Physiol. , vol.67 , pp. 130-138
    • Kozaki, T.1    Kimmelblatt, B.A.2    Hamm, R.L.3    Scott, J.G.4
  • 30
    • 0002532582 scopus 로고
    • The activity and organophosphate inhibition of cholinesterase from susceptible and resistant ticks (Acari)
    • Lee R.M., Batham P. The activity and organophosphate inhibition of cholinesterase from susceptible and resistant ticks (Acari). Entomol. Exp. Appl. 1966, 9:13-24.
    • (1966) Entomol. Exp. Appl. , vol.9 , pp. 13-24
    • Lee, R.M.1    Batham, P.2
  • 31
    • 1642331278 scopus 로고    scopus 로고
    • Resistance to coumaphos and diazinon in Boophilus microplus (Acari: Ixodidae) and evidence for the involvement of an oxidative detoxification mechanism
    • Li A.Y., Davey R.B., Miller R.J., George J.E. Resistance to coumaphos and diazinon in Boophilus microplus (Acari: Ixodidae) and evidence for the involvement of an oxidative detoxification mechanism. J. Med. Entomol. 2003, 40:482-490.
    • (2003) J. Med. Entomol. , vol.40 , pp. 482-490
    • Li, A.Y.1    Davey, R.B.2    Miller, R.J.3    George, J.E.4
  • 33
    • 2942560860 scopus 로고    scopus 로고
    • Mutations of acetylcholinesterase which confer insecticide resistance in Drosophila melanogaster populations
    • Menozzi P., Shi M.A., Lougarre A., Tang Z.H., Fournier D. Mutations of acetylcholinesterase which confer insecticide resistance in Drosophila melanogaster populations. BMC Evol. Biol. 2004, 4:4.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 4
    • Menozzi, P.1    Shi, M.A.2    Lougarre, A.3    Tang, Z.H.4    Fournier, D.5
  • 34
    • 25444463285 scopus 로고    scopus 로고
    • First report of organophosphate-resistant Boophilus microplus (Acari: Ixodidae) within the United States
    • Miller R., Davey R.B., George J.E. First report of organophosphate-resistant Boophilus microplus (Acari: Ixodidae) within the United States. J. Med. Entomol. 2005, 45:912-917.
    • (2005) J. Med. Entomol. , vol.45 , pp. 912-917
    • Miller, R.1    Davey, R.B.2    George, J.E.3
  • 35
    • 52449084495 scopus 로고    scopus 로고
    • Identification and correction of abnormal, incomplete and mispredicted proteins in public databases
    • Nagy A., Hegyi H., Farkas K., Tordai H., Kozma E., Banyai L., Patthy L. Identification and correction of abnormal, incomplete and mispredicted proteins in public databases. BMC Bioinform. 2008, 9:353.
    • (2008) BMC Bioinform. , vol.9 , pp. 353
    • Nagy, A.1    Hegyi, H.2    Farkas, K.3    Tordai, H.4    Kozma, E.5    Banyai, L.6    Patthy, L.7
  • 37
    • 9144265895 scopus 로고    scopus 로고
    • Retrieving sequences of enzymes experimentally characterized but erroneously annotated: the case of putrescine carbamoyltransferase
    • Naumoff D.G., Xu Y., Glansdorf N., Labedan B. Retrieving sequences of enzymes experimentally characterized but erroneously annotated: the case of putrescine carbamoyltransferase. BMC Genomics 2004, 5:52.
    • (2004) BMC Genomics , vol.5 , pp. 52
    • Naumoff, D.G.1    Xu, Y.2    Glansdorf, N.3    Labedan, B.4
  • 39
    • 50649113765 scopus 로고    scopus 로고
    • Novel acetylcholinesterase target site for malaria mosquito control
    • Pang Y.P. Novel acetylcholinesterase target site for malaria mosquito control. PLoS One 2006, 1:e58.
    • (2006) PLoS One , vol.1
    • Pang, Y.P.1
  • 40
    • 33845671661 scopus 로고    scopus 로고
    • Species marker for developing novel and safe pesticides
    • Pang Y.P. Species marker for developing novel and safe pesticides. Bioorg. Med. Chem. Lett. 2007, 17:197-199.
    • (2007) Bioorg. Med. Chem. Lett. , vol.17 , pp. 197-199
    • Pang, Y.P.1
  • 41
    • 84992083651 scopus 로고    scopus 로고
    • Selective and irreversible inhibitors of aphid acetylcholinesterases: steps toward human-safe insecticides
    • Pang Y.P., Singh S.K., Gao Y., Lassiter T.L., Mishra R.K., Zhu K.Y., Brimijoin S. Selective and irreversible inhibitors of aphid acetylcholinesterases: steps toward human-safe insecticides. PLoS One 2009, 4:e4349.
    • (2009) PLoS One , vol.4
    • Pang, Y.P.1    Singh, S.K.2    Gao, Y.3    Lassiter, T.L.4    Mishra, R.K.5    Zhu, K.Y.6    Brimijoin, S.7
  • 42
    • 38549176068 scopus 로고    scopus 로고
    • Acetylcholinesterase in cell adhesion, neurite growth and network formation
    • Paraoanu L.E., Layer P.G. Acetylcholinesterase in cell adhesion, neurite growth and network formation. FEBS J. 2008, 275:618-624.
    • (2008) FEBS J. , vol.275 , pp. 618-624
    • Paraoanu, L.E.1    Layer, P.G.2
  • 43
    • 34249329852 scopus 로고    scopus 로고
    • Expression and possible functions of the cholinergic system in a murine embryonic stem cell line
    • Paraoanu L.E., Steinert G., Koehler A., Wessler I., Layer P.G. Expression and possible functions of the cholinergic system in a murine embryonic stem cell line. Life Sci. 2007, 80:2375-2379.
    • (2007) Life Sci. , vol.80 , pp. 2375-2379
    • Paraoanu, L.E.1    Steinert, G.2    Koehler, A.3    Wessler, I.4    Layer, P.G.5
  • 44
    • 30944444336 scopus 로고    scopus 로고
    • Biochemical diagnosis of organophosphate-insensitivity with neural acetylcholinesterase extracted by sonication from the adult tick synganglion
    • Pruett J.H., Pound J.M. Biochemical diagnosis of organophosphate-insensitivity with neural acetylcholinesterase extracted by sonication from the adult tick synganglion. Vet. Parasitol. 2006, 135:355-363.
    • (2006) Vet. Parasitol. , vol.135 , pp. 355-363
    • Pruett, J.H.1    Pound, J.M.2
  • 46
    • 0039610311 scopus 로고
    • Resistencia en garrapatas Boophilus microplus, a los ixodicides en Mexico
    • J.M. Perez Trujillo, E. Gonzales Padila (Eds.)
    • Santamaría E.M., Fragoso S.H. Resistencia en garrapatas Boophilus microplus, a los ixodicides en Mexico. Proceedings, 14th Pan American Congress on Veterinary Sciences 1994, 473-474. J.M. Perez Trujillo, E. Gonzales Padila (Eds.).
    • (1994) Proceedings, 14th Pan American Congress on Veterinary Sciences , pp. 473-474
    • Santamaría, E.M.1    Fragoso, S.H.2
  • 47
    • 0024263346 scopus 로고
    • Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase
    • Schumacher M., Maulet Y., Camp S., Taylor P. Multiple messenger RNA species give rise to the structural diversity in acetylcholinesterase. J. Biol. Chem. 1988, 263:18979-18987.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18979-18987
    • Schumacher, M.1    Maulet, Y.2    Camp, S.3    Taylor, P.4
  • 48
    • 0014247745 scopus 로고
    • A mechanism of resistance to organophosphorous acaricides in a strain of the cattle tick Boophilus microplus
    • Schuntner C.A., Roulston W.J., Schnitzerling H.J. A mechanism of resistance to organophosphorous acaricides in a strain of the cattle tick Boophilus microplus. Aust. J. Biol. Sci. 1968, 21:97-109.
    • (1968) Aust. J. Biol. Sci. , vol.21 , pp. 97-109
    • Schuntner, C.A.1    Roulston, W.J.2    Schnitzerling, H.J.3
  • 49
    • 2942557198 scopus 로고    scopus 로고
    • Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance
    • Shi M.A., Lougarre A., Alies C., Fremaux I., Tang Z.H., Stojan J., Fournier D. Acetylcholinesterase alterations reveal the fitness cost of mutations conferring insecticide resistance. BMC Evol. Biol. 2004, 4:5.
    • (2004) BMC Evol. Biol. , vol.4 , pp. 5
    • Shi, M.A.1    Lougarre, A.2    Alies, C.3    Fremaux, I.4    Tang, Z.H.5    Stojan, J.6    Fournier, D.7
  • 50
    • 18744414554 scopus 로고    scopus 로고
    • Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology
    • Silman I., Sussman J.L. Acetylcholinesterase: 'classical' and 'non-classical' functions and pharmacology. Curr. Opin. Pharmacol. 2005, 5:293-302.
    • (2005) Curr. Opin. Pharmacol. , vol.5 , pp. 293-302
    • Silman, I.1    Sussman, J.L.2
  • 51
    • 50649087289 scopus 로고    scopus 로고
    • Acetylcholinesterase: how is structure related to function?
    • Silman I., Sussman J.L. Acetylcholinesterase: how is structure related to function?. Chem. Biol. Interact. 2008, 175:3-10.
    • (2008) Chem. Biol. Interact. , vol.175 , pp. 3-10
    • Silman, I.1    Sussman, J.L.2
  • 52
    • 38549105907 scopus 로고    scopus 로고
    • Cholinesterases, from molecular complexity to non-hydrolytic functions
    • Soreq H. Cholinesterases, from molecular complexity to non-hydrolytic functions. FEBS J. 2008, 275:603.
    • (2008) FEBS J. , vol.275 , pp. 603
    • Soreq, H.1
  • 53
    • 1942520265 scopus 로고    scopus 로고
    • Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate
    • Stojan J., Brochler L., Alies C., Cooetier J.P., Fournier D. Inhibition of Drosophila melanogaster acetylcholinesterase by high concentrations of substrate. Eur. J. Biochem. 2004, 271:1364-1371.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1364-1371
    • Stojan, J.1    Brochler, L.2    Alies, C.3    Cooetier, J.P.4    Fournier, D.5
  • 54
    • 2542534682 scopus 로고    scopus 로고
    • Identification of a third Boophilus microplus (Acari: Ixodidae) cDNA presumptively encoding an acetylcholinesterase
    • Temeyer K.B., Davey R.B., Chen A.C. Identification of a third Boophilus microplus (Acari: Ixodidae) cDNA presumptively encoding an acetylcholinesterase. J. Med. Entomol. 2004, 41:259-268.
    • (2004) J. Med. Entomol. , vol.41 , pp. 259-268
    • Temeyer, K.B.1    Davey, R.B.2    Chen, A.C.3
  • 55
    • 75549087738 scopus 로고    scopus 로고
    • Genotyping mutations in BmAChE3: a survey of organophosphate-resistant and -susceptible strains of Rhipicephalus (Boophilus) microplus
    • Temeyer K.B., Olafson P.U., Miller R.J. Genotyping mutations in BmAChE3: a survey of organophosphate-resistant and -susceptible strains of Rhipicephalus (Boophilus) microplus. J. Med. Entomol. 2009, 46:1355-1360.
    • (2009) J. Med. Entomol. , vol.46 , pp. 1355-1360
    • Temeyer, K.B.1    Olafson, P.U.2    Miller, R.J.3
  • 57
    • 36749029015 scopus 로고    scopus 로고
    • R86Q, a mutation in BmAChE3 yielding a Rhipicephalus microplus organophosphate-insensitive acetylcholinesterase
    • Temeyer K.B., Pruett J.H., Olafson P.U., Chen A.C. R86Q, a mutation in BmAChE3 yielding a Rhipicephalus microplus organophosphate-insensitive acetylcholinesterase. J. Med. Entomol. 2007, 44:1013-1018.
    • (2007) J. Med. Entomol. , vol.44 , pp. 1013-1018
    • Temeyer, K.B.1    Pruett, J.H.2    Olafson, P.U.3    Chen, A.C.4
  • 58
    • 33748343800 scopus 로고    scopus 로고
    • Baculovirus expression of BmAChE3, a cDNA encoding an acetylcholinesterase of Boophilus microplus (Acari: Ixodidae)
    • Temeyer K.B., Pruett J.H., Untalan P.M., Chen A.C. Baculovirus expression of BmAChE3, a cDNA encoding an acetylcholinesterase of Boophilus microplus (Acari: Ixodidae). J. Med. Entomol. 2006, 43:707-712.
    • (2006) J. Med. Entomol. , vol.43 , pp. 707-712
    • Temeyer, K.B.1    Pruett, J.H.2    Untalan, P.M.3    Chen, A.C.4
  • 59
    • 0024489712 scopus 로고
    • Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms
    • Toutant J.-P. Insect acetylcholinesterase: catalytic properties, tissue distribution and molecular forms. Progr. Neurobiol. 1989, 32:423-446.
    • (1989) Progr. Neurobiol. , vol.32 , pp. 423-446
    • Toutant, J.-P.1
  • 60
    • 0036383033 scopus 로고    scopus 로고
    • How many genes encode cholinesterase in arthropods?
    • Villatte F., Bachman T.T. How many genes encode cholinesterase in arthropods?. Pest. Biochem. Physiol. 2002, 73:122-129.
    • (2002) Pest. Biochem. Physiol. , vol.73 , pp. 122-129
    • Villatte, F.1    Bachman, T.T.2
  • 61
    • 0033924767 scopus 로고    scopus 로고
    • A high number of mutations in insect acetylcholinesterase may provide insecticide resistance
    • Villatte F., Ziliani P., Marcel V., Menozzi P., Fournier D. A high number of mutations in insect acetylcholinesterase may provide insecticide resistance. Pest. Biochem. Physiol. 2000, 67:95-102.
    • (2000) Pest. Biochem. Physiol. , vol.67 , pp. 95-102
    • Villatte, F.1    Ziliani, P.2    Marcel, V.3    Menozzi, P.4    Fournier, D.5
  • 63
    • 0031964633 scopus 로고    scopus 로고
    • Non-neuronal acetylcholine, a locally acting molecule, widely distributed in biological systems: expression and function in humans
    • Wessler I., Kirkpatrick C.J., Rake K. Non-neuronal acetylcholine, a locally acting molecule, widely distributed in biological systems: expression and function in humans. Pharmacol. Ther. 1998, 77:59-79.
    • (1998) Pharmacol. Ther. , vol.77 , pp. 59-79
    • Wessler, I.1    Kirkpatrick, C.J.2    Rake, K.3
  • 64
    • 1442315097 scopus 로고    scopus 로고
    • Cloning and sequencing of putative acetylcholinesterase cDNAs from the American dog tick, Dermacentor variabilis, and the brown dog tick, Rhipicephalus sanguineus (Acari: Ixodidae)
    • Xu G., Fang Q., Keirans J., Durden L. Cloning and sequencing of putative acetylcholinesterase cDNAs from the American dog tick, Dermacentor variabilis, and the brown dog tick, Rhipicephalus sanguineus (Acari: Ixodidae). J. Med. Entomol. 2003, 40:890-896.
    • (2003) J. Med. Entomol. , vol.40 , pp. 890-896
    • Xu, G.1    Fang, Q.2    Keirans, J.3    Durden, L.4
  • 65
    • 33748932546 scopus 로고    scopus 로고
    • Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission
    • Zimmerman G., Soreq H. Termination and beyond: acetylcholinesterase as a modulator of synaptic transmission. Cell Tissue Res. 2006, 326:665-669.
    • (2006) Cell Tissue Res. , vol.326 , pp. 665-669
    • Zimmerman, G.1    Soreq, H.2
  • 66
    • 0027966740 scopus 로고
    • Purification and characterization of acetylcholinesterase from the Colorado potato beetle, Leptinotarsa decemlineata (Say)
    • Zhu K.Y., Clark J.M. Purification and characterization of acetylcholinesterase from the Colorado potato beetle, Leptinotarsa decemlineata (Say). Insect Biochem. Mol. Biol. 1994, 24:453-461.
    • (1994) Insect Biochem. Mol. Biol. , vol.24 , pp. 453-461
    • Zhu, K.Y.1    Clark, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.