메뉴 건너뛰기




Volumn 4, Issue DEC, 2013, Pages

Phylogenetic investigation of peptide hormone and growth factor receptors in five dipteran genomes

Author keywords

GPCR; Guanylyl cyclase; Neuropeptide; Protein hormone; Receptor tyrosine kinase; Serine threonine kinase

Indexed keywords

ALLATOSTATIN RECEPTOR; BURISCON RECEPTOR; CALCITONIN LIKE DIURETIC HORMONE RECEPTOR; CORAZONIN RECEPTOR; CORTICOTROPIN RELEASING FACTOR LIKE DIURETIC HORMONE RECEPTOR; ECDYSONE RECEPTOR; G PROTEIN COUPLED RECEPTOR; GPA2 RECEPTOR; GPB5 RECEPTOR; GROWTH FACTOR RECEPTOR; HORMONE RECEPTOR; LATROPHILIN RECEPTOR; METHUSELAH LIKE RECEPTOR; MYOSUPPRESSIN RECEPTOR; NEUROPEPTIDE F RECEPTOR; NEUROPEPTIDE Y RECEPTOR; ORPHAN NUCLEAR RECEPTOR; PEPTIDE HORMONE; PIGMENT DISPERSING FACTOR RECEPTOR; PROCTOLIN RECEPTOR; PROTHORACICOTROPIC HORMONE RECEPTOR; RECEPTOR; RECEPTOR GUANYLYL CYCLASE; RHODOPSIN RECEPTOR; SECRETIN RECEPTOR; TACHYKININ RECEPTOR; TRANSFORMING GROWTH FACTOR BETA RECEPTOR; TRISSIN RECEPTOR; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84892164439     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2013.00193     Document Type: Article
Times cited : (39)

References (195)
  • 1
    • 79954539025 scopus 로고    scopus 로고
    • Receptor tyrosine kinase signaling-a proteomic perspective
    • doi: 10.1016/j.advenzreg.2010.10.005
    • Biarc J, Chalkley RJ, Burlingame AL, Bradshaw RA. Receptor tyrosine kinase signaling-a proteomic perspective. Adv Enzyme Regul (2011) 51:293-305. doi: 10.1016/j.advenzreg.2010.10.005.
    • (2011) Adv Enzyme Regul , vol.51 , pp. 293-305
    • Biarc, J.1    Chalkley, R.J.2    Burlingame, A.L.3    Bradshaw, R.A.4
  • 2
    • 79951852079 scopus 로고    scopus 로고
    • Regulation and therapeutic targeting of peptide-activated receptor guanylyl cyclases
    • doi:10.1016/j.pharmthera.2010.12.005
    • Potter LR. Regulation and therapeutic targeting of peptide-activated receptor guanylyl cyclases. Pharmacol Ther (2011) 130:71-82. doi:10.1016/j.pharmthera.2010.12.005.
    • (2011) Pharmacol Ther , vol.130 , pp. 71-82
    • Potter, L.R.1
  • 3
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • doi:10.1016/j.cell.2010.06.011
    • Lemmon MA, Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell (2010) 141:1117-34. doi:10.1016/j.cell.2010.06.011.
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 4
    • 71549152525 scopus 로고    scopus 로고
    • Mass spectrometric profiling of (neuro)-peptides in the worker honeybee, Apis mellifera
    • doi:10.1016/j.neuropharm.2009.06.026
    • Boerjan B, Cardoen D, Bogaerts A, Landuyt B, Schoofs L, Verleyen P. Mass spectrometric profiling of (neuro)-peptides in the worker honeybee, Apis mellifera. Neuropharmacology (2010) 58:248-58. doi:10.1016/j.neuropharm.2009.06.026.
    • (2010) Neuropharmacology , vol.58 , pp. 248-258
    • Boerjan, B.1    Cardoen, D.2    Bogaerts, A.3    Landuyt, B.4    Schoofs, L.5    Verleyen, P.6
  • 5
    • 0033850610 scopus 로고    scopus 로고
    • Exploring the Caenorhabditis elegans and Drosophila melanogaster genomes to understand neuropeptide and peptidase function
    • doi:10.1042/0300-5127:0280464
    • Coates D, Siviter R, Isaac RE. Exploring the Caenorhabditis elegans and Drosophila melanogaster genomes to understand neuropeptide and peptidase function. Biochem Soc Trans (2000) 28:464-9. doi:10.1042/0300-5127:0280464.
    • (2000) Biochem Soc Trans , vol.28 , pp. 464-469
    • Coates, D.1    Siviter, R.2    Isaac, R.E.3
  • 6
    • 77957359170 scopus 로고    scopus 로고
    • Genomics and peptidomics of neuropeptides and protein hormones present in the parasitic wasp Nasonia vitripennis
    • doi:10.1021/pr100570j
    • Hauser F, Neupert S, Williamson M, Predel R, Tanaka Y, Grimmelikhuijzen CJ. Genomics and peptidomics of neuropeptides and protein hormones present in the parasitic wasp Nasonia vitripennis. J Proteome Res (2010) 9:5296-310. doi:10.1021/pr100570j.
    • (2010) J Proteome Res , vol.9 , pp. 5296-5310
    • Hauser, F.1    Neupert, S.2    Williamson, M.3    Predel, R.4    Tanaka, Y.5    Grimmelikhuijzen, C.J.6
  • 7
    • 0034824368 scopus 로고    scopus 로고
    • Neuropeptides and neuropeptide receptors in the Drosophila melanogaster genome
    • doi:10.1101/gr.169901
    • Hewes RS, Taghert PH. Neuropeptides and neuropeptide receptors in the Drosophila melanogaster genome. Genome Res (2001) 11:1126-42. doi:10.1101/gr.169901.
    • (2001) Genome Res , vol.11 , pp. 1126-1142
    • Hewes, R.S.1    Taghert, P.H.2
  • 8
    • 33749554743 scopus 로고    scopus 로고
    • From the genome to the proteome: uncovering peptides in the Apis brain
    • doi:10.1126/science.1124128
    • Hummon AB, Richmond TA, Verleyen P, Baggerman G, Huybrechts J, Ewing MA, et al. From the genome to the proteome: uncovering peptides in the Apis brain. Science (2006) 314:647-9. doi:10.1126/science.1124128.
    • (2006) Science , vol.314 , pp. 647-649
    • Hummon, A.B.1    Richmond, T.A.2    Verleyen, P.3    Baggerman, G.4    Huybrechts, J.5    Ewing, M.A.6
  • 10
    • 0037020020 scopus 로고    scopus 로고
    • Neuropeptides and peptide hormones in Anopheles gambiae
    • doi:10.1126/science.1076827
    • Riehle MA, Garczynski SF, Crim JW, Hill CA, Brown MR. Neuropeptides and peptide hormones in Anopheles gambiae. Science (2002) 298:172-5. doi:10.1126/science.1076827.
    • (2002) Science , vol.298 , pp. 172-175
    • Riehle, M.A.1    Garczynski, S.F.2    Crim, J.W.3    Hill, C.A.4    Brown, M.R.5
  • 11
    • 59649109131 scopus 로고    scopus 로고
    • The unique evolution of neuropeptide genes in the silkworm Bombyx mori
    • doi:10.1016/j.ibmb.2008.04.009
    • Roller L, Yamanaka N, Watanabe K, Daubnerová I, Žitnan D, Kataoka H, et al. The unique evolution of neuropeptide genes in the silkworm Bombyx mori. Insect Biochem Mol Biol (2008) 38:1147-57. doi:10.1016/j.ibmb.2008.04.009.
    • (2008) Insect Biochem Mol Biol , vol.38 , pp. 1147-1157
    • Roller, L.1    Yamanaka, N.2    Watanabe, K.3    Daubnerová, I.4    Žitnan, D.5    Kataoka, H.6
  • 12
    • 40749124939 scopus 로고    scopus 로고
    • Prediction of neuropeptide cleavage sites in insects
    • doi:10.1093/bioinformatics/btn044
    • Southey BR, Sweedler JV, Rodriguez-Zas SL. Prediction of neuropeptide cleavage sites in insects. Bioinformatics (2008) 24:815-25. doi:10.1093/bioinformatics/btn044.
    • (2008) Bioinformatics , vol.24 , pp. 815-825
    • Southey, B.R.1    Sweedler, J.V.2    Rodriguez-Zas, S.L.3
  • 13
    • 84857138383 scopus 로고    scopus 로고
    • In silico cloning of genes encoding neuropeptides, neurohormones and their putative G-protein coupled receptors in a spider mite
    • doi:10.1016/j.ibmb.2011.12.009
    • Veenstra JA, Rombauts S, Grbic M. In silico cloning of genes encoding neuropeptides, neurohormones and their putative G-protein coupled receptors in a spider mite. Insect Biochem Mol Biol (2012) 42:277-95. doi:10.1016/j.ibmb.2011.12.009.
    • (2012) Insect Biochem Mol Biol , vol.42 , pp. 277-295
    • Veenstra, J.A.1    Rombauts, S.2    Grbic, M.3
  • 14
    • 38049066995 scopus 로고    scopus 로고
    • Genomics, transcriptomics, and peptidomics of neuropeptides and protein hormones in the red flour beetle Tribolium castaneum
    • doi:10.1101/gr.6714008
    • Li B, Predel R, Neupert S, Hauser F, Tanaka Y, Cazzamali G, et al. Genomics, transcriptomics, and peptidomics of neuropeptides and protein hormones in the red flour beetle Tribolium castaneum. Genome Res (2008) 18:113-22. doi:10.1101/gr.6714008.
    • (2008) Genome Res , vol.18 , pp. 113-122
    • Li, B.1    Predel, R.2    Neupert, S.3    Hauser, F.4    Tanaka, Y.5    Cazzamali, G.6
  • 15
    • 84864129174 scopus 로고    scopus 로고
    • Structure-activity and immunochemical data provide evidence of developmental-and tissue-specific myosuppressin signaling
    • doi:10.1016/j.peptides.2012.05.002
    • Dickerson M, McCormick J, Mispelon M, Paisley K, Nichols R. Structure-activity and immunochemical data provide evidence of developmental-and tissue-specific myosuppressin signaling. Peptides (2012) 36:272-9. doi:10.1016/j.peptides.2012.05.002.
    • (2012) Peptides , vol.36 , pp. 272-279
    • Dickerson, M.1    McCormick, J.2    Mispelon, M.3    Paisley, K.4    Nichols, R.5
  • 16
    • 29644448174 scopus 로고    scopus 로고
    • Identifying neuropeptide and protein hormone receptors in Drosophila melanogaster by exploiting genomic data
    • doi:10.1093/bfgp/eli003
    • Hauser F, Williamson M, Cazzamali G, Grimmelikhuijzen CJ. Identifying neuropeptide and protein hormone receptors in Drosophila melanogaster by exploiting genomic data. Brief Funct Genomic Proteomic (2006) 4:321-30. doi:10.1093/bfgp/eli003.
    • (2006) Brief Funct Genomic Proteomic , vol.4 , pp. 321-330
    • Hauser, F.1    Williamson, M.2    Cazzamali, G.3    Grimmelikhuijzen, C.J.4
  • 17
    • 33750477657 scopus 로고    scopus 로고
    • A review of neurohormone GPCRs present in the fruitfly Drosophila melanogaster and the honey bee Apis mellifera
    • doi:10.1016/j.pneurobio.2006.07.005
    • Hauser F, Cazzamali G, Williamson M, Blenau W, Grimmelikhuijzen CJ. A review of neurohormone GPCRs present in the fruitfly Drosophila melanogaster and the honey bee Apis mellifera. Prog Neurobiol (2006) 80:1-19. doi:10.1016/j.pneurobio.2006.07.005.
    • (2006) Prog Neurobiol , vol.80 , pp. 1-19
    • Hauser, F.1    Cazzamali, G.2    Williamson, M.3    Blenau, W.4    Grimmelikhuijzen, C.J.5
  • 18
    • 37549060383 scopus 로고    scopus 로고
    • A genome-wide inventory of neurohormone GPCRs in the red flour beetle Tribolium castaneum
    • doi:10.1016/j.yfrne.2007.10.003
    • Hauser F, Cazzamali G, Williamson M, Park Y, Li B, Tanaka Y, et al. A genome-wide inventory of neurohormone GPCRs in the red flour beetle Tribolium castaneum. Front Neuroendocrinol (2008) 29:142-65. doi:10.1016/j.yfrne.2007.10.003.
    • (2008) Front Neuroendocrinol , vol.29 , pp. 142-165
    • Hauser, F.1    Cazzamali, G.2    Williamson, M.3    Park, Y.4    Li, B.5    Tanaka, Y.6
  • 19
    • 82755176150 scopus 로고    scopus 로고
    • Identification and functional characterization of two orphan G-protein-coupled receptors for adipokinetic hormones from silkworm Bombyx mori
    • doi:10.1074/jbc.M111.275602
    • Shi Y, Huang H, Deng X, He X, Yang J, Yang H, et al. Identification and functional characterization of two orphan G-protein-coupled receptors for adipokinetic hormones from silkworm Bombyx mori. J Biol Chem (2011) 286:42390-402. doi:10.1074/jbc.M111.275602.
    • (2011) J Biol Chem , vol.286 , pp. 42390-42402
    • Shi, Y.1    Huang, H.2    Deng, X.3    He, X.4    Yang, J.5    Yang, H.6
  • 20
    • 52449133985 scopus 로고    scopus 로고
    • Neuropeptide receptor transcriptome reveals unidentified neuroendocrine pathways
    • doi:10.1371/journal.pone.0003048
    • Yamanaka N, Yamamoto S, Žitnan D, Watanabe K, Kawada T, Satake H, et al. Neuropeptide receptor transcriptome reveals unidentified neuroendocrine pathways. PLoS One (2008) 3:e3048. doi:10.1371/journal.pone.0003048.
    • (2008) PLoS One , vol.3
    • Yamanaka, N.1    Yamamoto, S.2    Žitnan, D.3    Watanabe, K.4    Kawada, T.5    Satake, H.6
  • 21
    • 77954660568 scopus 로고    scopus 로고
    • The G protein-coupled receptors in the silkworm, Bombyx mori
    • doi:10.1016/j.ibmb.2010.05.005
    • Fan Y, Sun P, Wang Y, He X, Deng X, Chen X, et al. The G protein-coupled receptors in the silkworm, Bombyx mori. Insect Biochem Mol Biol (2010) 40:581-91. doi:10.1016/j.ibmb.2010.05.005.
    • (2010) Insect Biochem Mol Biol , vol.40 , pp. 581-591
    • Fan, Y.1    Sun, P.2    Wang, Y.3    He, X.4    Deng, X.5    Chen, X.6
  • 22
    • 0041342066 scopus 로고    scopus 로고
    • Drosophila neuropeptide signaling
    • doi:10.1016/S0065-2660(03)01001-0
    • Taghert PH, Veenstra JA. Drosophila neuropeptide signaling. Adv Genet (2003) 49:1-65. doi:10.1016/S0065-2660(03)01001-0.
    • (2003) Adv Genet , vol.49 , pp. 1-65
    • Taghert, P.H.1    Veenstra, J.A.2
  • 24
    • 0037020037 scopus 로고    scopus 로고
    • G protein coupled receptors in Anopheles gambiae
    • doi:10.1126/Science.1076196
    • Hill CA, Fox AN, Pitts RJ, Kent LB, Tan PL, Chrystal MA, et al. G protein coupled receptors in Anopheles gambiae. Science (2002) 298:176-8. doi:10.1126/Science.1076196.
    • (2002) Science , vol.298 , pp. 176-178
    • Hill, C.A.1    Fox, A.N.2    Pitts, R.J.3    Kent, L.B.4    Tan, P.L.5    Chrystal, M.A.6
  • 25
    • 25444440081 scopus 로고    scopus 로고
    • Cross genome phylogenetic analysis of human and Drosophila G protein-coupled receptors: application to functional annotation of orphan receptors
    • doi:10.1186/1471-2164-6-106
    • Metpally RP, Sowdhamini R. Cross genome phylogenetic analysis of human and Drosophila G protein-coupled receptors: application to functional annotation of orphan receptors. BMC Genomics (2005) 6:106. doi:10.1186/1471-2164-6-106.
    • (2005) BMC Genomics , vol.6 , pp. 106
    • Metpally, R.P.1    Sowdhamini, R.2
  • 26
    • 0037020114 scopus 로고    scopus 로고
    • The genome sequence of the malaria mosquito Anopheles gambiae
    • doi:10.1126/Science.1076181
    • Holt RA, Subramanian GM, Halpern A, Sutton GG, Charlab R, Nusskern DR, et al. The genome sequence of the malaria mosquito Anopheles gambiae. Science (2002) 298:129-49. doi:10.1126/Science.1076181.
    • (2002) Science , vol.298 , pp. 129-149
    • Holt, R.A.1    Subramanian, G.M.2    Halpern, A.3    Sutton, G.G.4    Charlab, R.5    Nusskern, D.R.6
  • 27
    • 34250902354 scopus 로고    scopus 로고
    • Genome sequence of Aedes aegypti, a major arbovirus vector
    • doi:10.1126/Science.1138878
    • Nene V, Wortman JR, Lawson D, Haas B, Kodira C, Tu ZJ, et al. Genome sequence of Aedes aegypti, a major arbovirus vector. Science (2007) 316:1718-23. doi:10.1126/Science.1138878.
    • (2007) Science , vol.316 , pp. 1718-1723
    • Nene, V.1    Wortman, J.R.2    Lawson, D.3    Haas, B.4    Kodira, C.5    Tu, Z.J.6
  • 28
    • 77957370433 scopus 로고    scopus 로고
    • Sequencing of Culex quinquefasciatus establishes a platform for mosquito comparative genomics
    • doi:10.1126/Science.1191864
    • Arensburger P, Megy K, Waterhouse RM, Abrudan J, Amedeo P, Antelo B, et al. Sequencing of Culex quinquefasciatus establishes a platform for mosquito comparative genomics. Science (2010) 330:86-8. doi:10.1126/Science.1191864.
    • (2010) Science , vol.330 , pp. 86-88
    • Arensburger, P.1    Megy, K.2    Waterhouse, R.M.3    Abrudan, J.4    Amedeo, P.5    Antelo, B.6
  • 29
    • 84874419329 scopus 로고    scopus 로고
    • Feeding and the rhodopsin family g-protein coupled receptors in nematodes and arthropods
    • doi:10.3389/fendo.2012.00157
    • Cardoso JC, Felix RC, Fonseca VG, Power DM. Feeding and the rhodopsin family g-protein coupled receptors in nematodes and arthropods. Front Endocrinol (Lausanne) (2012) 3:157. doi:10.3389/fendo.2012.00157.
    • (2012) Front Endocrinol (Lausanne) , vol.3 , pp. 157
    • Cardoso, J.C.1    Felix, R.C.2    Fonseca, V.G.3    Power, D.M.4
  • 30
    • 0037126208 scopus 로고    scopus 로고
    • Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands
    • RESEARCH006. doi:10.1186/gb-2002-3-11-research0063
    • Joost P, Methner A. Phylogenetic analysis of 277 human G-protein-coupled receptors as a tool for the prediction of orphan receptor ligands. Genome Biol (2002) 3(11):RESEARCH006. doi:10.1186/gb-2002-3-11-research0063.
    • (2002) Genome Biol , vol.3 , Issue.11
    • Joost, P.1    Methner, A.2
  • 31
    • 80055082271 scopus 로고    scopus 로고
    • Accelerated profile HMM searches
    • doi:10.1371/Journal.Pcbi.1002195
    • Eddy SR. Accelerated profile HMM searches. PLoS Comput Biol (2011) 7:e1002195. doi:10.1371/Journal.Pcbi.1002195.
    • (2011) PLoS Comput Biol , vol.7
    • Eddy, S.R.1
  • 33
    • 0028174033 scopus 로고
    • Fingerprinting G-protein-coupled receptors
    • doi:10.1093/protein/7.2.195
    • Attwood TK, Findlay JB. Fingerprinting G-protein-coupled receptors. Protein Eng (1994) 7:195-203. doi:10.1093/protein/7.2.195.
    • (1994) Protein Eng , vol.7 , pp. 195-203
    • Attwood, T.K.1    Findlay, J.B.2
  • 34
    • 0034710148 scopus 로고    scopus 로고
    • Drosophila melanogaster G protein-coupled receptors
    • doi:10.1083/Jcb.150.2.F83
    • Brody T, Cravchik A. Drosophila melanogaster G protein-coupled receptors. J Cell Biol (2000) 150:F83-8. doi:10.1083/Jcb.150.2.F83.
    • (2000) J Cell Biol , vol.150
    • Brody, T.1    Cravchik, A.2
  • 35
    • 10044222704 scopus 로고    scopus 로고
    • CLANS: a Java application for visualizing protein families based on pairwise similarity
    • doi:10.1093/Bioinformatics/Bth444
    • Frickey T, Lupas A. CLANS: a Java application for visualizing protein families based on pairwise similarity. Bioinformatics (2004) 20:3702-4. doi:10.1093/Bioinformatics/Bth444.
    • (2004) Bioinformatics , vol.20 , pp. 3702-3704
    • Frickey, T.1    Lupas, A.2
  • 36
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • doi:10.1093/Nar/Gki198
    • Katoh K, Kuma K, Toh H, Miyata T. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res (2005) 33:511-8. doi:10.1093/Nar/Gki198.
    • (2005) Nucleic Acids Res , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 37
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • doi:10.1093/Nar/Gkh340
    • Edgar RC. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res (2004) 32:1792-7. doi:10.1093/Nar/Gkh340.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 38
    • 65449188232 scopus 로고    scopus 로고
    • Jalview version 2-a multiple sequence alignment editor and analysis workbench
    • doi:10.1093/bioinformatics/btp033
    • Waterhouse AM, Procter JB, Martin DM, Clamp M, Barton GJ. Jalview version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics (2009) 25:1189-91. doi:10.1093/bioinformatics/btp033.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 39
    • 77950806408 scopus 로고    scopus 로고
    • New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0
    • doi:10.1093/Sysbio/Syq010
    • Guindon S, Dufayard JF, Lefort V, Anisimova M, Hordijk W, Gascuel O. New algorithms and methods to estimate maximum-likelihood phylogenies: assessing the performance of PhyML 3.0. Syst Biol (2010) 59:307-21. doi:10.1093/Sysbio/Syq010.
    • (2010) Syst Biol , vol.59 , pp. 307-321
    • Guindon, S.1    Dufayard, J.F.2    Lefort, V.3    Anisimova, M.4    Hordijk, W.5    Gascuel, O.6
  • 41
    • 77953916959 scopus 로고    scopus 로고
    • Mutagenesis of human neuropeptide Y/peptide YY receptor Y2 reveals additional differences to Y1 in interactions with highly conserved ligand positions
    • doi:10.1016/j.regpep.2010.04.011
    • Åkerberg H, Fällmar H, Sjödin P, Boukharta L, Gutiérrez-de-Terán H, Lundell I, et al. Mutagenesis of human neuropeptide Y/peptide YY receptor Y2 reveals additional differences to Y1 in interactions with highly conserved ligand positions. Regul Pept (2010) 163:120-9. doi:10.1016/j.regpep.2010.04.011.
    • (2010) Regul Pept , vol.163 , pp. 120-129
    • Åkerberg, H.1    Fällmar, H.2    Sjödin, P.3    Boukharta, L.4    Gutiérrez-de-Terán, H.5    Lundell, I.6
  • 42
    • 0037042210 scopus 로고    scopus 로고
    • Reciprocal mutations of neuropeptide Y receptor Y2 in human and chicken identify amino acids important for antagonist binding
    • doi:10.1016/S0014-5793(02)02534-6
    • Berglund MM, Fredriksson R, Salaneck E, Larhammar D. Reciprocal mutations of neuropeptide Y receptor Y2 in human and chicken identify amino acids important for antagonist binding. FEBS Lett (2002) 518:5-9. doi:10.1016/S0014-5793(02)02534-6.
    • (2002) FEBS Lett , vol.518 , pp. 5-9
    • Berglund, M.M.1    Fredriksson, R.2    Salaneck, E.3    Larhammar, D.4
  • 43
    • 79960838045 scopus 로고    scopus 로고
    • Identification of positions in the human neuropeptide Y/peptide YY receptor Y2 that contribute to pharmacological differences between receptor subtypes
    • doi:10.1016/j.npep.2011.05.006
    • Fällmar H, Åkerberg H, Gutiérrez-de-Terán H, Lundell I, Mohell N, Larhammar D. Identification of positions in the human neuropeptide Y/peptide YY receptor Y2 that contribute to pharmacological differences between receptor subtypes. Neuropeptides (2011) 45:293-300. doi:10.1016/j.npep.2011.05.006.
    • (2011) Neuropeptides , vol.45 , pp. 293-300
    • Fällmar, H.1    Åkerberg, H.2    Gutiérrez-de-Terán, H.3    Lundell, I.4    Mohell, N.5    Larhammar, D.6
  • 44
    • 1542332885 scopus 로고    scopus 로고
    • Time flies, a new molecular time-scale for brachyceran fly evolution without a clock
    • doi:10.1080/10635150390250965
    • Wiegmann BM, Yeates DK, Thorne JL, Kishino H. Time flies, a new molecular time-scale for brachyceran fly evolution without a clock. Syst Biol (2003) 52:745-56. doi:10.1080/10635150390250965.
    • (2003) Syst Biol , vol.52 , pp. 745-756
    • Wiegmann, B.M.1    Yeates, D.K.2    Thorne, J.L.3    Kishino, H.4
  • 45
    • 33646067726 scopus 로고    scopus 로고
    • Analysis of the complete mitochondrial DNA from Anopheles funestus: an improved dipteran mitochondrial genome annotation and a temporal dimension of mosquito evolution
    • doi:10.1016/J.Ympev.2006.01.006
    • Krzywinski J, Grushko OG, Besansky NJ. Analysis of the complete mitochondrial DNA from Anopheles funestus: an improved dipteran mitochondrial genome annotation and a temporal dimension of mosquito evolution. Mol Phylogenet Evol (2006) 39:417-23. doi:10.1016/J.Ympev.2006.01.006.
    • (2006) Mol Phylogenet Evol , vol.39 , pp. 417-423
    • Krzywinski, J.1    Grushko, O.G.2    Besansky, N.J.3
  • 46
    • 74049139522 scopus 로고    scopus 로고
    • Phylogenetic analysis and temporal diversification of mosquitoes (Diptera: Culicidae) based on nuclear genes and morphology
    • doi:10.1186/1471-2148-9-298
    • Reidenbach KR, Cook S, Bertone MA, Harbach RE, Wiegmann BM, Besansky NJ. Phylogenetic analysis and temporal diversification of mosquitoes (Diptera: Culicidae) based on nuclear genes and morphology. BMC Evol Biol (2009) 9:298. doi:10.1186/1471-2148-9-298.
    • (2009) BMC Evol Biol , vol.9 , pp. 298
    • Reidenbach, K.R.1    Cook, S.2    Bertone, M.A.3    Harbach, R.E.4    Wiegmann, B.M.5    Besansky, N.J.6
  • 48
    • 84858332552 scopus 로고    scopus 로고
    • An evolutionary comparison of leucine-rich repeat containing G protein-coupled receptors reveals a novel LGR subtype
    • doi:10.1016/J.Peptides.2011.11.004
    • Van Hiel MB, Vandersmissen HP, Van Loy T, Broeck JV. An evolutionary comparison of leucine-rich repeat containing G protein-coupled receptors reveals a novel LGR subtype. Peptides (2012) 34:193-200. doi:10.1016/J.Peptides.2011.11.004.
    • (2012) Peptides , vol.34 , pp. 193-200
    • Van Hiel, M.B.1    Vandersmissen, H.P.2    Van Loy, T.3    Broeck, J.V.4
  • 49
    • 23044484252 scopus 로고    scopus 로고
    • Heterodimeric fly glycoprotein hormone-a2 (GPA2) and glycoprotein hormone-β5 (GPB5) activate fly leucine-rich repeat-containing G protein-coupled receptor-1 (DLGR1) and stimulation of human thyrotropin receptors by chimeric fly GPA2 and human GPB5
    • doi:10.1210/En.2005-0317
    • Sudo S, Kuwabara Y, Park JI, Hsu SY, Hsueh AJ. Heterodimeric fly glycoprotein hormone-a2 (GPA2) and glycoprotein hormone-β5 (GPB5) activate fly leucine-rich repeat-containing G protein-coupled receptor-1 (DLGR1) and stimulation of human thyrotropin receptors by chimeric fly GPA2 and human GPB5. Endocrinology (2005) 146:3596-604. doi:10.1210/En.2005-0317.
    • (2005) Endocrinology , vol.146 , pp. 3596-3604
    • Sudo, S.1    Kuwabara, Y.2    Park, J.I.3    Hsu, S.Y.4    Hsueh, A.J.5
  • 50
    • 14544303674 scopus 로고    scopus 로고
    • Bursicon, the insect cuticle-hardening hormone, is a heterodimeric cystine knot protein that activates G protein-coupled receptor LGR2
    • doi:10.1073/Pnas.0409916102
    • Luo CW, Dewey EM, Sudo S, Ewer J, Hsu SY, Honegger HW, et al. Bursicon, the insect cuticle-hardening hormone, is a heterodimeric cystine knot protein that activates G protein-coupled receptor LGR2. Proc Natl Acad Sci U S A (2005) 102:2820-5. doi:10.1073/Pnas.0409916102.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2820-2825
    • Luo, C.W.1    Dewey, E.M.2    Sudo, S.3    Ewer, J.4    Hsu, S.Y.5    Honegger, H.W.6
  • 51
    • 16444370116 scopus 로고    scopus 로고
    • Drosophila molting neurohormone bursicon is a heterodimer and the natural agonist of the orphan receptor DLGR2
    • doi:10.1016/J.FEBSlet.2005.03.006
    • Mendive FM, Van Loy T, Claeysen S, Poels J, Williamson M, Hauser F, et al. Drosophila molting neurohormone bursicon is a heterodimer and the natural agonist of the orphan receptor DLGR2. FEBS Lett (2005) 579:2171-6. doi:10.1016/J.FEBSlet.2005.03.006.
    • (2005) FEBS Lett , vol.579 , pp. 2171-2176
    • Mendive, F.M.1    Van Loy, T.2    Claeysen, S.3    Poels, J.4    Williamson, M.5    Hauser, F.6
  • 52
    • 0344885581 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes
    • doi:10.1073/pnas.0336132100
    • Zhu Y, Rice CD, Pang Y, Pace M, Thomas P. Cloning, expression, and characterization of a membrane progestin receptor and evidence it is an intermediary in meiotic maturation of fish oocytes. Proc Natl Acad Sci U S A (2003) 100:2231-6. doi:10.1073/pnas.0336132100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2231-2236
    • Zhu, Y.1    Rice, C.D.2    Pang, Y.3    Pace, M.4    Thomas, P.5
  • 53
    • 21544445248 scopus 로고    scopus 로고
    • Rapid, nongenomic responses to ecdysteroids and catecholamines mediated by a novel Drosophila G-protein-coupled receptor
    • doi:10.1523/JNEUROSCI.1005-05.2005
    • Srivastava DP, Yu EJ, Kennedy K, Chatwin H, Reale V, Hamon M, et al. Rapid, nongenomic responses to ecdysteroids and catecholamines mediated by a novel Drosophila G-protein-coupled receptor. J Neurosci (2005) 25:6145-55. doi:10.1523/JNEUROSCI.1005-05.2005.
    • (2005) J Neurosci , vol.25 , pp. 6145-6155
    • Srivastava, D.P.1    Yu, E.J.2    Kennedy, K.3    Chatwin, H.4    Reale, V.5    Hamon, M.6
  • 54
    • 26244436194 scopus 로고    scopus 로고
    • moody Encodes two GPCRs that regulate cocaine behaviors and blood-brain barrier permeability in Drosophila
    • doi:10.1016/J.Cell.2005.07.029
    • Bainton RJ, Tsai LT, Schwabe T, DeSalvo M, Gaul U, Heberlein U. moody Encodes two GPCRs that regulate cocaine behaviors and blood-brain barrier permeability in Drosophila. Cell (2005) 123:145-56. doi:10.1016/J.Cell.2005.07.029.
    • (2005) Cell , vol.123 , pp. 145-156
    • Bainton, R.J.1    Tsai, L.T.2    Schwabe, T.3    DeSalvo, M.4    Gaul, U.5    Heberlein, U.6
  • 55
    • 84861101400 scopus 로고    scopus 로고
    • Anopheles gambiae corazonin: gene structure, expression and effect on mosquito heart physiology
    • doi:10.1111/J.1365-2583.2012.01140.X
    • Hillyer JF, Estévez-Lao TY, Funkhouser LJ, Aluoch VA. Anopheles gambiae corazonin: gene structure, expression and effect on mosquito heart physiology. Insect Mol Biol (2012) 21:343-55. doi:10.1111/J.1365-2583.2012.01140.X.
    • (2012) Insect Mol Biol , vol.21 , pp. 343-355
    • Hillyer, J.F.1    Estévez-Lao, T.Y.2    Funkhouser, L.J.3    Aluoch, V.A.4
  • 56
    • 84873436861 scopus 로고    scopus 로고
    • Cardioacceleratory function of the neurohormone CCAP in the mosquito Anopheles gambiae
    • doi:10.1242/Jeb.077164
    • Estévez-Lao TY, Boyce DS, Honegger HW, Hillyer JF. Cardioacceleratory function of the neurohormone CCAP in the mosquito Anopheles gambiae. J Exp Biol (2013) 216:601-13. doi:10.1242/Jeb.077164.
    • (2013) J Exp Biol , vol.216 , pp. 601-613
    • Estévez-Lao, T.Y.1    Boyce, D.S.2    Honegger, H.W.3    Hillyer, J.F.4
  • 57
    • 84869097636 scopus 로고    scopus 로고
    • Identified peptidergic neurons in the Drosophila brain regulate insulin-producing cells, stress responses and metabolism by coexpressed short neuropeptide F and corazonin
    • doi:10.1007/S00018-012-1097-Z
    • Kapan N, Lushchak OV, Luo JN, Nässel DR. Identified peptidergic neurons in the Drosophila brain regulate insulin-producing cells, stress responses and metabolism by coexpressed short neuropeptide F and corazonin. Cell Mol Life Sci (2012) 69:4051-66. doi:10.1007/S00018-012-1097-Z.
    • (2012) Cell Mol Life Sci , vol.69 , pp. 4051-4066
    • Kapan, N.1    Lushchak, O.V.2    Luo, J.N.3    Nässel, D.R.4
  • 58
    • 77953931115 scopus 로고    scopus 로고
    • Drosophila neuropeptides in regulation of physiology and behavior
    • doi:10.1016/J.Pneurobio.2010.04.010
    • Nässel DR, Winther AM. Drosophila neuropeptides in regulation of physiology and behavior. Prog Neurobiol (2010) 92:42-104. doi:10.1016/J.Pneurobio.2010.04.010.
    • (2010) Prog Neurobiol , vol.92 , pp. 42-104
    • Nässel, D.R.1    Winther, A.M.2
  • 59
    • 77951280408 scopus 로고    scopus 로고
    • Discovery of a novel insect neuropeptide signaling system closely related to the insect adipokinetic hormone and corazonin hormonal systems
    • doi:10.1074/Jbc.M109.045369
    • Hansen KK, Stafflinger E, Schneider M, Hauser F, Cazzamali G, Williamson M, et al. Discovery of a novel insect neuropeptide signaling system closely related to the insect adipokinetic hormone and corazonin hormonal systems. J Biol Chem (2010) 285:10736-47. doi:10.1074/Jbc.M109.045369.
    • (2010) J Biol Chem , vol.285 , pp. 10736-10747
    • Hansen, K.K.1    Stafflinger, E.2    Schneider, M.3    Hauser, F.4    Cazzamali, G.5    Williamson, M.6
  • 60
    • 0036333274 scopus 로고    scopus 로고
    • Deletion of the ecdysis-triggering hormone gene leads to lethal ecdysis deficiency
    • Park Y, Filippov V, Gill SS, Adams ME. Deletion of the ecdysis-triggering hormone gene leads to lethal ecdysis deficiency. Development (2002) 129:493-503.
    • (2002) Development , vol.129 , pp. 493-503
    • Park, Y.1    Filippov, V.2    Gill, S.S.3    Adams, M.E.4
  • 61
    • 70449622749 scopus 로고    scopus 로고
    • The adipokinetic hormone system in Culicinae (Diptera: Culicidae): molecular identification and characterization of two adipokinetic hormone (AKH) precursors from Aedes aegypti and Culex pipiens and two putative AKH receptor variants from Ae
    • doi:10.1016/J.Ibmb.2009.09.002
    • Kaufmann C, Merzendorfer H, Gäde G. The adipokinetic hormone system in Culicinae (Diptera: Culicidae): molecular identification and characterization of two adipokinetic hormone (AKH) precursors from Aedes aegypti and Culex pipiens and two putative AKH receptor variants from Ae. aegypti. Insect Biochem Mol Biol (2009) 39:770-81. doi:10.1016/J.Ibmb.2009.09.002.
    • (2009) aegypti. Insect Biochem Mol Biol , vol.39 , pp. 770-781
    • Kaufmann, C.1    Merzendorfer, H.2    Gäde, G.3
  • 62
    • 38749096300 scopus 로고    scopus 로고
    • Regulation of carbohydrate metabolism and flight performance by a hypertrehalosaemic hormone in the mosquito Anopheles gambiae
    • doi:10.1016/J.Jinsphys.2007.10.007
    • Kaufmann C, Brown MR. Regulation of carbohydrate metabolism and flight performance by a hypertrehalosaemic hormone in the mosquito Anopheles gambiae. J Insect Physiol (2008) 54:367-77. doi:10.1016/J.Jinsphys.2007.10.007.
    • (2008) J Insect Physiol , vol.54 , pp. 367-377
    • Kaufmann, C.1    Brown, M.R.2
  • 63
    • 84862500571 scopus 로고    scopus 로고
    • Structure-activity studies of Drosophila adipokinetic hormone (AKH) by a cellular expression system of dipteran AKH receptors
    • doi:10.1016/J.Ygcen.2012.04.025
    • Caers J, Peeters L, Janssen T, De Haes W, Gäde G, Schoofs L. Structure-activity studies of Drosophila adipokinetic hormone (AKH) by a cellular expression system of dipteran AKH receptors. Gen Comp Endocrinol (2012) 177:332-7. doi:10.1016/J.Ygcen.2012.04.025.
    • (2012) Gen Comp Endocrinol , vol.177 , pp. 332-337
    • Caers, J.1    Peeters, L.2    Janssen, T.3    De Haes, W.4    Gäde, G.5    Schoofs, L.6
  • 64
    • 79951510097 scopus 로고    scopus 로고
    • Open conformation of adipokinetic hormone receptor from the malaria mosquito facilitates hormone binding
    • doi:10.1016/J.Peptides.2010.08.017
    • Mugumbate G, Jackson GE, van der Spoel D. Open conformation of adipokinetic hormone receptor from the malaria mosquito facilitates hormone binding. Peptides (2011) 32:553-9. doi:10.1016/J.Peptides.2010.08.017.
    • (2011) Peptides , vol.32 , pp. 553-559
    • Mugumbate, G.1    Jackson, G.E.2    van der Spoel, D.3
  • 65
    • 84857141366 scopus 로고    scopus 로고
    • Functional characterization of an allatotropin receptor expressed in the corpora allata of mosquitoes
    • doi:10.1016/J.Peptides.2011.07.025
    • Nouzova M, Brockhoff A, Mayoral JG, Goodwin M, Meyerhof W, Noriega FG. Functional characterization of an allatotropin receptor expressed in the corpora allata of mosquitoes. Peptides (2012) 34:201-8. doi:10.1016/J.Peptides.2011.07.025.
    • (2012) Peptides , vol.34 , pp. 201-208
    • Nouzova, M.1    Brockhoff, A.2    Mayoral, J.G.3    Goodwin, M.4    Meyerhof, W.5    Noriega, F.G.6
  • 66
    • 79955891894 scopus 로고    scopus 로고
    • Insulin production and signaling in renal tubules of Drosophila is under control of tachykinin-related peptide and regulates stress resistance
    • doi:10.1371/journal.pone.0019866
    • Söderberg JA, Birse RT, Nassel DR. Insulin production and signaling in renal tubules of Drosophila is under control of tachykinin-related peptide and regulates stress resistance. PLoS One (2011) 6:e19866. doi:10.1371/journal.pone.0019866.
    • (2011) PLoS One , vol.6
    • Söderberg, J.A.1    Birse, R.T.2    Nassel, D.R.3
  • 67
    • 0036298729 scopus 로고    scopus 로고
    • Cloning and functional expression of the first Drosophila melanogaster sulfakinin receptor DSK-R1
    • doi:10.1006/Bbrc.2002.6459
    • Kubiak TM, Larsen MJ, Burton KJ, Bannow CA, Martin RA, Zantello MR, et al. Cloning and functional expression of the first Drosophila melanogaster sulfakinin receptor DSK-R1. Biochem Biophys Res Commun (2002) 291:313-20. doi:10.1006/Bbrc.2002.6459.
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 313-320
    • Kubiak, T.M.1    Larsen, M.J.2    Burton, K.J.3    Bannow, C.A.4    Martin, R.A.5    Zantello, M.R.6
  • 68
    • 80052634142 scopus 로고    scopus 로고
    • Identification of the Drosophila and Tribolium receptors for the recently discovered insect RYamide neuropeptides
    • doi:10.1016/J.Bbrc.2011.07.131
    • Collin C, Hauser F, Krogh-Meyer P, Hansen KK, de Valdivia EG, Williamson M, et al. Identification of the Drosophila and Tribolium receptors for the recently discovered insect RYamide neuropeptides. Biochem Biophys Res Commun (2011) 412:578-83. doi:10.1016/J.Bbrc.2011.07.131.
    • (2011) Biochem Biophys Res Commun , vol.412 , pp. 578-583
    • Collin, C.1    Hauser, F.2    Krogh-Meyer, P.3    Hansen, K.K.4    de Valdivia, E.G.5    Williamson, M.6
  • 69
    • 80054077505 scopus 로고    scopus 로고
    • Identification of the endogenous cysteine-rich peptide trissin, a ligand for an orphan G protein-coupled receptor in Drosophila
    • doi:10.1016/J.Bbrc.2011.09.018
    • Ida T, Takahashi T, Tominaga H, Sato T, Kume K, Yoshizawa-Kumagaye K, et al. Identification of the endogenous cysteine-rich peptide trissin, a ligand for an orphan G protein-coupled receptor in Drosophila. Biochem Biophys Res Commun (2011) 414:44-8. doi:10.1016/J.Bbrc.2011.09.018.
    • (2011) Biochem Biophys Res Commun , vol.414 , pp. 44-48
    • Ida, T.1    Takahashi, T.2    Tominaga, H.3    Sato, T.4    Kume, K.5    Yoshizawa-Kumagaye, K.6
  • 70
    • 0034725575 scopus 로고    scopus 로고
    • Expression and functional characterization of a Drosophila neuropeptide precursor with homology to mammalian preprotachykinin A
    • doi:10.1074/Jbc.M002875200
    • Siviter RJ, Coast GM, Winther AM, Nachman RJ, Taylor CA, Shirras AD, et al. Expression and functional characterization of a Drosophila neuropeptide precursor with homology to mammalian preprotachykinin A. J Biol Chem (2000) 275:23273-80. doi:10.1074/Jbc.M002875200.
    • (2000) J Biol Chem , vol.275 , pp. 23273-23280
    • Siviter, R.J.1    Coast, G.M.2    Winther, A.M.3    Nachman, R.J.4    Taylor, C.A.5    Shirras, A.D.6
  • 71
    • 83155172619 scopus 로고    scopus 로고
    • Regulation of insulin-producing cells in the adult Drosophila brain via the tachykinin peptide receptor DTKR
    • doi:10.1242/Jeb.062091
    • Birse RT, Söderberg JA, Luo JL, Winther AM, Nässel DR. Regulation of insulin-producing cells in the adult Drosophila brain via the tachykinin peptide receptor DTKR. J Exp Biol (2011) 214:4201-8. doi:10.1242/Jeb.062091.
    • (2011) J Exp Biol , vol.214 , pp. 4201-4208
    • Birse, R.T.1    Söderberg, J.A.2    Luo, J.L.3    Winther, A.M.4    Nässel, D.R.5
  • 72
    • 84892163833 scopus 로고    scopus 로고
    • Role of tachykinin-related peptide signaling in response to metabolic stress
    • Birse R, Winther AM, Nässel DR. Role of tachykinin-related peptide signaling in response to metabolic stress. J Neurogenet (2006) 20(3-4):89.
    • (2006) J Neurogenet , vol.20 , Issue.3-4 , pp. 89
    • Birse, R.1    Winther, A.M.2    Nässel, D.R.3
  • 73
    • 0025991955 scopus 로고
    • Cloning, heterologous expression and developmental regulation of a Drosophila receptor for tachykinin-like peptides
    • Li XJ, Wolfgang W, Wu YN, North RA, Forte M. Cloning, heterologous expression and developmental regulation of a Drosophila receptor for tachykinin-like peptides. EMBO J (1991) 10:3221-9.
    • (1991) EMBO J , vol.10 , pp. 3221-3229
    • Li, X.J.1    Wolfgang, W.2    Wu, Y.N.3    North, R.A.4    Forte, M.5
  • 74
    • 60749133751 scopus 로고    scopus 로고
    • Characterization and distribution of NKD, a receptor for Drosophila tachykinin-related peptide 6
    • doi:10.1016/J.Peptides.2008.10.012
    • Poels J, Birse RT, Nachman RJ, Fichna J, Janecka A, Broeck JV, et al. Characterization and distribution of NKD, a receptor for Drosophila tachykinin-related peptide 6. Peptides (2009) 30:545-56. doi:10.1016/J.Peptides.2008.10.012.
    • (2009) Peptides , vol.30 , pp. 545-556
    • Poels, J.1    Birse, R.T.2    Nachman, R.J.3    Fichna, J.4    Janecka, A.5    Broeck, J.V.6
  • 75
    • 33845654333 scopus 로고    scopus 로고
    • Functional comparison of two evolutionary conserved insect neurokinin-like receptors
    • doi:10.1016/J.Peptides.2006.06.014
    • Poels J, Verlinden H, Fichna J, Van Loy T, Franssens V, Studzian K, et al. Functional comparison of two evolutionary conserved insect neurokinin-like receptors. Peptides (2007) 28:103-8. doi:10.1016/J.Peptides.2006.06.014.
    • (2007) Peptides , vol.28 , pp. 103-108
    • Poels, J.1    Verlinden, H.2    Fichna, J.3    Van Loy, T.4    Franssens, V.5    Studzian, K.6
  • 76
    • 77049103571 scopus 로고    scopus 로고
    • Tachykinin-related peptides and their receptors in invertebrates: a current view
    • doi:10.1016/J.Peptides.2009.09.023
    • Van Loy T, Vandersmissen HP, Poels J, Van Hiel MB, Verlinden H, Vanden Broeck J. Tachykinin-related peptides and their receptors in invertebrates: a current view. Peptides (2010) 31:520-4. doi:10.1016/J.Peptides.2009.09.023.
    • (2010) Peptides , vol.31 , pp. 520-524
    • Van Loy, T.1    Vandersmissen, H.P.2    Poels, J.3    Van Hiel, M.B.4    Verlinden, H.5    Vanden Broeck, J.6
  • 77
    • 84883814632 scopus 로고    scopus 로고
    • Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects
    • doi:10.1073/pnas.1310676110
    • Jiang H, Lkhagva A, Daubnerová I, Chae HS, Simo L, Jung SH, et al. Natalisin, a tachykinin-like signaling system, regulates sexual activity and fecundity in insects. Proc Natl Acad Sci U S A (2013) 110:3526-34. doi:10.1073/pnas.1310676110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 3526-3534
    • Jiang, H.1    Lkhagva, A.2    Daubnerová, I.3    Chae, H.S.4    Simo, L.5    Jung, S.H.6
  • 78
    • 80053328839 scopus 로고    scopus 로고
    • Transcellular and paracellular pathways of transepithelial fluid secretion in Malpighian (renal) tubules of the yellow fever mosquito Aedes aegypti
    • doi:10.1111/J.1748-1716.2010.02195.X
    • Beyenbach KW, Piermarini PM. Transcellular and paracellular pathways of transepithelial fluid secretion in Malpighian (renal) tubules of the yellow fever mosquito Aedes aegypti. Acta Physiol (2011) 202:387-407. doi:10.1111/J.1748-1716.2010.02195.X.
    • (2011) Acta Physiol , vol.202 , pp. 387-407
    • Beyenbach, K.W.1    Piermarini, P.M.2
  • 79
    • 84878460780 scopus 로고    scopus 로고
    • A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells
    • doi:10.1098/Rspb.2012.2943
    • Cabrero P, Richmond L, Nitabach M, Davies SA, Dow JA. A biogenic amine and a neuropeptide act identically: tyramine signals through calcium in Drosophila tubule stellate cells. Proc Biol Sci (2013) 280:20122943. doi:10.1098/Rspb.2012.2943.
    • (2013) Proc Biol Sci , vol.280 , pp. 20122943
    • Cabrero, P.1    Richmond, L.2    Nitabach, M.3    Davies, S.A.4    Dow, J.A.5
  • 80
    • 80855144153 scopus 로고    scopus 로고
    • Mosquito Aedes aegypti (L.) leucokinin receptor is critical for in vivo fluid excretion post blood feeding
    • doi:10.1016/J.FEBSlet.2011.10.001
    • Kersch CN, Pietrantonio PV. Mosquito Aedes aegypti (L.) leucokinin receptor is critical for in vivo fluid excretion post blood feeding. FEBS Lett (2011) 585:3507-12. doi:10.1016/J.FEBSlet.2011.10.001.
    • (2011) FEBS Lett , vol.585 , pp. 3507-3512
    • Kersch, C.N.1    Pietrantonio, P.V.2
  • 81
    • 78751575970 scopus 로고    scopus 로고
    • The kinin receptor is expressed in the Malpighian tubule stellate cells in the mosquito Aedes aegypti (L.): a new model needed to explain ion transport?
    • doi:10.1016/J.Ibmb.2010.10.033
    • Lu HL, Kersch C, Pietrantonio PV. The kinin receptor is expressed in the Malpighian tubule stellate cells in the mosquito Aedes aegypti (L.): a new model needed to explain ion transport? Insect Biochem Mol Biol (2011) 41:135-40. doi:10.1016/J.Ibmb.2010.10.033.
    • (2011) Insect Biochem Mol Biol , vol.41 , pp. 135-140
    • Lu, H.L.1    Kersch, C.2    Pietrantonio, P.V.3
  • 82
    • 0037064075 scopus 로고    scopus 로고
    • Systematic G-protein-coupled receptor analysis in Drosophila melanogaster identifies a leucokinin receptor with novel roles
    • doi:10.1074/Jbc.M203694200
    • Radford JC, Davies SA, Dow JA. Systematic G-protein-coupled receptor analysis in Drosophila melanogaster identifies a leucokinin receptor with novel roles. J Biol Chem (2002) 277(41):38810-7. doi:10.1074/Jbc.M203694200.
    • (2002) J Biol Chem , vol.277 , Issue.41 , pp. 38810-38817
    • Radford, J.C.1    Davies, S.A.2    Dow, J.A.3
  • 83
    • 42149131477 scopus 로고    scopus 로고
    • Cloning and identification of the first oxytocin/vasopressin-like receptor and its ligand from insects
    • doi:10.1073/Pnas.0710897105
    • Stafflinger E, Hansen KK, Hauser F, Schneider M, Cazzamali G, Williamson M, et al. Cloning and identification of the first oxytocin/vasopressin-like receptor and its ligand from insects. Proc Natl Acad Sci U S A (2008) 105:3262-7. doi:10.1073/Pnas.0710897105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3262-3267
    • Stafflinger, E.1    Hansen, K.K.2    Hauser, F.3    Schneider, M.4    Cazzamali, G.5    Williamson, M.6
  • 84
    • 79958016332 scopus 로고    scopus 로고
    • A comparative review of short and long neuropeptide F signaling in invertebrates: any similarities to vertebrate neuropeptide Y signaling?
    • doi:10.1016/J.Peptides.2011.03.013
    • Nässel DR, Wegener C. A comparative review of short and long neuropeptide F signaling in invertebrates: any similarities to vertebrate neuropeptide Y signaling? Peptides (2011) 32:1335-55. doi:10.1016/J.Peptides.2011.03.013.
    • (2011) Peptides , vol.32 , pp. 1335-1355
    • Nässel, D.R.1    Wegener, C.2
  • 85
    • 11144249786 scopus 로고    scopus 로고
    • Characterization of neuropeptide F and its receptor from the African malaria mosquito, Anopheles gambiae
    • doi:10.1016/J.Peptides.2004.07.014
    • Garczynski SF, Crim JW, Brown MR. Characterization of neuropeptide F and its receptor from the African malaria mosquito, Anopheles gambiae. Peptides (2005) 26:99-107. doi:10.1016/J.Peptides.2004.07.014.
    • (2005) Peptides , vol.26 , pp. 99-107
    • Garczynski, S.F.1    Crim, J.W.2    Brown, M.R.3
  • 86
    • 8444250340 scopus 로고    scopus 로고
    • The anterior stomach of larval mosquitoes (Aedes aegypti): effects of neuropeptides on transepithelial ion transport and muscular motility
    • doi:10.1242/Jeb.01208
    • Onken H, Moffett SB, Moffett DE. The anterior stomach of larval mosquitoes (Aedes aegypti): effects of neuropeptides on transepithelial ion transport and muscular motility. J Exp Biol (2004) 207:3731-9. doi:10.1242/Jeb.01208.
    • (2004) J Exp Biol , vol.207 , pp. 3731-3739
    • Onken, H.1    Moffett, S.B.2    Moffett, D.E.3
  • 87
    • 0036701095 scopus 로고    scopus 로고
    • Neuropeptide F and its expression in the yellow fever mosquito, Aedes aegypti
    • doi:10.1016/S0196-9781(02)00074-8
    • Stanek DM, Pohl J, Crim JW, Brown MR. Neuropeptide F and its expression in the yellow fever mosquito, Aedes aegypti. Peptides (2002) 23:1367-78. doi:10.1016/S0196-9781(02)00074-8.
    • (2002) Peptides , vol.23 , pp. 1367-1378
    • Stanek, D.M.1    Pohl, J.2    Crim, J.W.3    Brown, M.R.4
  • 88
    • 45149145966 scopus 로고
    • Isolation and characterization of ovarian ecdysteroidogenic hormones from the mosquito, Aedes aegypti
    • doi:10.1016/0020-1790(89)90100-5
    • Matsumoto S, Brown MR, Suzuki A, Lea AO. Isolation and characterization of ovarian ecdysteroidogenic hormones from the mosquito, Aedes aegypti. Insect Biochem (1989) 19:651-6. doi:10.1016/0020-1790(89)90100-5.
    • (1989) Insect Biochem , vol.19 , pp. 651-656
    • Matsumoto, S.1    Brown, M.R.2    Suzuki, A.3    Lea, A.O.4
  • 89
    • 0036517531 scopus 로고    scopus 로고
    • Characterization of the AeaHP gene and its expression in the mosquito Aedes aegypti (Diptera: Culicidae)
    • doi:10.1603/0022-2585-39.2.331
    • Stracker TH, Thompson S, Grossman GL, Riehle MA, Brown MR. Characterization of the AeaHP gene and its expression in the mosquito Aedes aegypti (Diptera: Culicidae). J Med Entomol (2002) 39:331-42. doi:10.1603/0022-2585-39.2.331.
    • (2002) J Med Entomol , vol.39 , pp. 331-342
    • Stracker, T.H.1    Thompson, S.2    Grossman, G.L.3    Riehle, M.A.4    Brown, M.R.5
  • 90
    • 0027954180 scopus 로고
    • Endogenous regulation of mosquito host-seeking behavior by a neuropeptide
    • doi:10.1016/0022-1910(94)90158-9
    • Brown MR, Klowden MJ, Crim JW, Young L, Shrouder LA, Lea AO. Endogenous regulation of mosquito host-seeking behavior by a neuropeptide. J Insect Physiol (1994) 40:399-406. doi:10.1016/0022-1910(94)90158-9.
    • (1994) J Insect Physiol , vol.40 , pp. 399-406
    • Brown, M.R.1    Klowden, M.J.2    Crim, J.W.3    Young, L.4    Shrouder, L.A.5    Lea, A.O.6
  • 91
    • 84858332808 scopus 로고    scopus 로고
    • The host-seeking inhibitory peptide, Aea-HP-1, is made in the male accessory gland and transferred to the female during copulation
    • doi:10.1016/J.Peptides.2011.10.027
    • Naccarati C, Audsley N, Keen JN, Kim JH, Howell GJ, Kim YJ, et al. The host-seeking inhibitory peptide, Aea-HP-1, is made in the male accessory gland and transferred to the female during copulation. Peptides (2012) 34:150-7. doi:10.1016/J.Peptides.2011.10.027.
    • (2012) Peptides , vol.34 , pp. 150-157
    • Naccarati, C.1    Audsley, N.2    Keen, J.N.3    Kim, J.H.4    Howell, G.J.5    Kim, Y.J.6
  • 92
    • 0036129531 scopus 로고    scopus 로고
    • Characterization of a functional neuropeptide F receptor from Drosophila melanogaster
    • doi:10.1016/S0196-9781(01)00647-7
    • Garczynski SF, Brown MR, Shen P, Murray TF, Crim JW. Characterization of a functional neuropeptide F receptor from Drosophila melanogaster. Peptides (2002) 23:773-80. doi:10.1016/S0196-9781(01)00647-7.
    • (2002) Peptides , vol.23 , pp. 773-780
    • Garczynski, S.F.1    Brown, M.R.2    Shen, P.3    Murray, T.F.4    Crim, J.W.5
  • 93
    • 0036406632 scopus 로고    scopus 로고
    • Characterization of the short neuropeptide F receptor from Drosophila melanogaster
    • doi:10.1016/S0006-291X(02)02351-3
    • Mertens I, Meeusen T, Huybrechts R, De Loof A, Schoofs L. Characterization of the short neuropeptide F receptor from Drosophila melanogaster. Biochem Biophys Res Commun (2002) 297:1140-8. doi:10.1016/S0006-291X(02)02351-3.
    • (2002) Biochem Biophys Res Commun , vol.297 , pp. 1140-1148
    • Mertens, I.1    Meeusen, T.2    Huybrechts, R.3    De Loof, A.4    Schoofs, L.5
  • 94
    • 84887303297 scopus 로고    scopus 로고
    • Functional and genetic characterization of neuropeptide Y-like receptors in Aedes aegypti
    • doi:10.1371/journal.pntd.0002486
    • Liesch J, Bellani LL, Vosshall LB. Functional and genetic characterization of neuropeptide Y-like receptors in Aedes aegypti. PLoS Negl Trop Dis (2013) 7:e2486. doi:10.1371/journal.pntd.0002486.
    • (2013) PLoS Negl Trop Dis , vol.7
    • Liesch, J.1    Bellani, L.L.2    Vosshall, L.B.3
  • 96
    • 78650854702 scopus 로고    scopus 로고
    • The Drosophila genes CG14593 and CG30106 code for G-protein-coupled receptors specifically activated by the neuropeptides CCHamide-1 and CCHamide-2
    • doi:10.1016/J.Bbrc.2010.11.089
    • Hansen KK, Hauser F, Williamson M, Weber SB, Grimmelikhuijzen CJ. The Drosophila genes CG14593 and CG30106 code for G-protein-coupled receptors specifically activated by the neuropeptides CCHamide-1 and CCHamide-2. Biochem Biophys Res Commun (2011) 404:184-9. doi:10.1016/J.Bbrc.2010.11.089.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 184-189
    • Hansen, K.K.1    Hauser, F.2    Williamson, M.3    Weber, S.B.4    Grimmelikhuijzen, C.J.5
  • 97
    • 33846345087 scopus 로고    scopus 로고
    • The role of allatostatins in juvenile hormone synthesis in insects and crustaceans
    • doi:10.1146/Annurev.Ento.51.110104.151050
    • Stay B, Tobe SS. The role of allatostatins in juvenile hormone synthesis in insects and crustaceans. Annu Rev Entomol (2007) 52:277-99. doi:10.1146/Annurev.Ento.51.110104.151050.
    • (2007) Annu Rev Entomol , vol.52 , pp. 277-299
    • Stay, B.1    Tobe, S.S.2
  • 98
    • 0033382684 scopus 로고    scopus 로고
    • Allatostatins: a growing family of neuropeptides with structural and functional diversity
    • doi:10.1111/J.1749-6632.1999.Tb07902.X
    • Bendena WG, Donly BC, Tobe SS. Allatostatins: a growing family of neuropeptides with structural and functional diversity. Ann N Y Acad Sci (1999) 897:311-29. doi:10.1111/J.1749-6632.1999.Tb07902.X.
    • (1999) Ann N Y Acad Sci , vol.897 , pp. 311-329
    • Bendena, W.G.1    Donly, B.C.2    Tobe, S.S.3
  • 99
    • 0033876759 scopus 로고    scopus 로고
    • Molecular cloning and genomic organization of a second probable allatostatin receptor from Drosophila melanogaster
    • doi:10.1006/Bbrc.2000.2964
    • Lenz C, Williamson M, Grimmelikhuijzen CJ. Molecular cloning and genomic organization of a second probable allatostatin receptor from Drosophila melanogaster. Biochem Biophys Res Commun (2000) 273:571-7. doi:10.1006/Bbrc.2000.2964.
    • (2000) Biochem Biophys Res Commun , vol.273 , pp. 571-577
    • Lenz, C.1    Williamson, M.2    Grimmelikhuijzen, C.J.3
  • 100
    • 0036757382 scopus 로고    scopus 로고
    • Neuropeptides in the nervous system of Drosophila and other insects: multiple roles as neuromodulators and neurohormones
    • doi:10.1016/S0301-0082(02)00057-6
    • Nässel DR. Neuropeptides in the nervous system of Drosophila and other insects: multiple roles as neuromodulators and neurohormones. Prog Neurobiol (2002) 68:1-84. doi:10.1016/S0301-0082(02)00057-6.
    • (2002) Prog Neurobiol , vol.68 , pp. 1-84
    • Nässel, D.R.1
  • 101
    • 0030887904 scopus 로고    scopus 로고
    • A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid secretion by the Malpighian tubules and hindgut contractions
    • doi:10.1074/jbc.272.16.10402
    • Veenstra JA, Pattillo JM, Petzel DH. A single cDNA encodes all three Aedes leucokinins, which stimulate both fluid secretion by the Malpighian tubules and hindgut contractions. J Biol Chem (1997) 272:10402-7. doi:10.1074/jbc.272.16.10402.
    • (1997) J Biol Chem , vol.272 , pp. 10402-10407
    • Veenstra, J.A.1    Pattillo, J.M.2    Petzel, D.H.3
  • 102
    • 0037131272 scopus 로고    scopus 로고
    • Functional annotation of two orphan G-protein-coupled receptors, Drostar1 and-2, from Drosophila melanogaster and their ligands by reverse pharmacology
    • doi:10.1074/Jbc.M206931200
    • Kreienkamp HJ, Larusson HJ, Witte I, Roeder T, Birgul N, Hönck HH, et al. Functional annotation of two orphan G-protein-coupled receptors, Drostar1 and-2, from Drosophila melanogaster and their ligands by reverse pharmacology. J Biol Chem (2002) 277:39937-43. doi:10.1074/Jbc.M206931200.
    • (2002) J Biol Chem , vol.277 , pp. 39937-39943
    • Kreienkamp, H.J.1    Larusson, H.J.2    Witte, I.3    Roeder, T.4    Birgul, N.5    Hönck, H.H.6
  • 104
    • 1542360636 scopus 로고    scopus 로고
    • Inhibition of juvenile hormone biosynthesis in mosquitoes: effect of allatostatic head factors, PISCF-and YXFGL-amide-allatostatins
    • doi:10.1016/J.Regpep.2003.12.004
    • Li YP, Hernandez-Martinez S, Noriega FG. Inhibition of juvenile hormone biosynthesis in mosquitoes: effect of allatostatic head factors, PISCF-and YXFGL-amide-allatostatins. Regul Pept (2004) 118:175-82. doi:10.1016/J.Regpep.2003.12.004.
    • (2004) Regul Pept , vol.118 , pp. 175-182
    • Li, Y.P.1    Hernandez-Martinez, S.2    Noriega, F.G.3
  • 105
    • 84860428879 scopus 로고    scopus 로고
    • The FGLamide-allatostatins influence foraging behavior in Drosophila melanogaster
    • doi:10.1371/journal.pone.0036059
    • Wang C, Chin-Sang I, Bendena WG. The FGLamide-allatostatins influence foraging behavior in Drosophila melanogaster. PLoS One (2012) 7:e36059. doi:10.1371/journal.pone.0036059.
    • (2012) PLoS One , vol.7
    • Wang, C.1    Chin-Sang, I.2    Bendena, W.G.3
  • 106
    • 0036081577 scopus 로고    scopus 로고
    • Two nitridergic peptides are encoded by the gene capability in Drosophila melanogaster
    • doi:10.1152/ajpregu.00584.2001
    • Kean L, Cazenave W, Costes L, Broderick KE, Graham S, Pollock VP, et al. Two nitridergic peptides are encoded by the gene capability in Drosophila melanogaster. Am J Physiol (2002) 282:R1297-307. doi:10.1152/ajpregu.00584.2001.
    • (2002) Am J Physiol , vol.282
    • Kean, L.1    Cazenave, W.2    Costes, L.3    Broderick, K.E.4    Graham, S.5    Pollock, V.P.6
  • 107
    • 65049090532 scopus 로고    scopus 로고
    • Ecdysis triggering hormone signaling in the yellow fever mosquito Aedes aegypti
    • doi:10.1016/J.Ygcen.2009.03.004
    • Dai L, Adams ME. Ecdysis triggering hormone signaling in the yellow fever mosquito Aedes aegypti. Gen Comp Endocrinol (2009) 162:43-51. doi:10.1016/J.Ygcen.2009.03.004.
    • (2009) Gen Comp Endocrinol , vol.162 , pp. 43-51
    • Dai, L.1    Adams, M.E.2
  • 108
    • 34548226875 scopus 로고    scopus 로고
    • Identification of one capa and two pyrokinin receptors from the malaria mosquito Anopheles gambiae
    • doi:10.1016/J.Bbre.2007.06.190
    • Olsen SS, Cazzamali G, Williamson M, Grimmelikhuijzen CJ, Hauser F. Identification of one capa and two pyrokinin receptors from the malaria mosquito Anopheles gambiae. Biochem Biophys Res Commun (2007) 362:245-51. doi:10.1016/J.Bbre.2007.06.190.
    • (2007) Biochem Biophys Res Commun , vol.362 , pp. 245-251
    • Olsen, S.S.1    Cazzamali, G.2    Williamson, M.3    Grimmelikhuijzen, C.J.4    Hauser, F.5
  • 110
    • 79955734395 scopus 로고    scopus 로고
    • The pyrokinin/pheromone biosynthesis-activating neuropeptide (PBAN) family of peptides and their receptors in Insecta: evolutionary trace indicates potential receptor ligand-binding domains
    • doi:10.1111/J.1365-2583.2010.01065.X
    • Jurenka R, Nusawardani T. The pyrokinin/pheromone biosynthesis-activating neuropeptide (PBAN) family of peptides and their receptors in Insecta: evolutionary trace indicates potential receptor ligand-binding domains. Insect Mol Biol (2011) 20:323-34. doi:10.1111/J.1365-2583.2010.01065.X.
    • (2011) Insect Mol Biol , vol.20 , pp. 323-334
    • Jurenka, R.1    Nusawardani, T.2
  • 111
    • 0036910451 scopus 로고    scopus 로고
    • Molecular identification of the first insect ecdysis triggering hormone receptors
    • doi:10.1016/S0006-291x(02)02798-5
    • Iversen A, Cazzamali G, Williamson M, Hauser F, Grimmelikhuijzen CJ. Molecular identification of the first insect ecdysis triggering hormone receptors. Biochem Biophys Res Commun (2002) 299:924-31. doi:10.1016/S0006-291x(02)02798-5.
    • (2002) Biochem Biophys Res Commun , vol.299 , pp. 924-931
    • Iversen, A.1    Cazzamali, G.2    Williamson, M.3    Hauser, F.4    Grimmelikhuijzen, C.J.5
  • 112
    • 0038381524 scopus 로고    scopus 로고
    • Two subtypes of ecdysis-triggering hormone receptor in Drosophila melanogaster
    • doi:10.1074/Jbc.M301119200
    • Park Y, Kim YJ, Dupriez V, Adams ME. Two subtypes of ecdysis-triggering hormone receptor in Drosophila melanogaster. J Biol Chem (2003) 278:17710-5. doi:10.1074/Jbc.M301119200.
    • (2003) J Biol Chem , vol.278 , pp. 17710-17715
    • Park, Y.1    Kim, Y.J.2    Dupriez, V.3    Adams, M.E.4
  • 113
    • 77049103801 scopus 로고    scopus 로고
    • Ecdysis triggering hormone signaling in arthropods
    • doi:10.1016/J.Peptides.2009.11.022
    • Roller L, Zitnanová I, Dai L, Šimo L, Park Y, Satake H, et al. Ecdysis triggering hormone signaling in arthropods. Peptides (2010) 31:429-41. doi:10.1016/J.Peptides.2009.11.022.
    • (2010) Peptides , vol.31 , pp. 429-441
    • Roller, L.1    Zitnanová, I.2    Dai, L.3    Šimo, L.4    Park, Y.5    Satake, H.6
  • 114
    • 0029394857 scopus 로고
    • Nonlinear dynamics of neurochemical modulation of mosquito oviduct and hindgut contractions
    • Messer AC, Brown MR. Nonlinear dynamics of neurochemical modulation of mosquito oviduct and hindgut contractions. J Exp Biol (1995) 198:2325-36.
    • (1995) J Exp Biol , vol.198 , pp. 2325-2336
    • Messer, A.C.1    Brown, M.R.2
  • 115
    • 0347993100 scopus 로고    scopus 로고
    • Identification of Drosophila neuropeptide receptors by G protein-coupled receptors-beta-arrestin2 interactions
    • doi:10.1074/Jbc.M306756200
    • Johnson EC, Bohn LM, Barak LS, Birse RT, Nässel DR, Caron MG, et al. Identification of Drosophila neuropeptide receptors by G protein-coupled receptors-beta-arrestin2 interactions. J Biol Chem (2003) 278:52172-8. doi:10.1074/Jbc.M306756200.
    • (2003) J Biol Chem , vol.278 , pp. 52172-52178
    • Johnson, E.C.1    Bohn, L.M.2    Barak, L.S.3    Birse, R.T.4    Nässel, D.R.5    Caron, M.G.6
  • 116
    • 0037180521 scopus 로고    scopus 로고
    • Identification in Drosophila melanogaster of the invertebrate G protein-coupled FMRFamide receptor
    • doi:10.1073/Pnas.252339599
    • Meeusen T, Mertens I, Clynen E, Baggerman G, Nichols R, Nachman RJ, et al. Identification in Drosophila melanogaster of the invertebrate G protein-coupled FMRFamide receptor. Proc Natl Acad Sci U S A (2002) 99:15363-8. doi:10.1073/Pnas.252339599.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 15363-15368
    • Meeusen, T.1    Mertens, I.2    Clynen, E.3    Baggerman, G.4    Nichols, R.5    Nachman, R.J.6
  • 117
    • 0038113303 scopus 로고    scopus 로고
    • The structure of the FMRFamide receptor and activity of the cardioexcitatory neuropeptide are conserved in mosquito
    • doi:10.1016/S0143-4179(03)00023-4
    • Duttlinger A, Mispelon M, Nichols R. The structure of the FMRFamide receptor and activity of the cardioexcitatory neuropeptide are conserved in mosquito. Neuropeptides (2003) 37:120-6. doi:10.1016/S0143-4179(03)00023-4.
    • (2003) Neuropeptides , vol.37 , pp. 120-126
    • Duttlinger, A.1    Mispelon, M.2    Nichols, R.3
  • 118
    • 0037208953 scopus 로고    scopus 로고
    • Signaling pathways and physiological functions of Drosophila melanogaster FMRFamide-related peptides
    • doi:10.1146/Annurev.Ento.48.091801.112525
    • Nichols R. Signaling pathways and physiological functions of Drosophila melanogaster FMRFamide-related peptides. Annu Rev Entomol (2003) 48:485-503. doi:10.1146/Annurev.Ento.48.091801.112525.
    • (2003) Annu Rev Entomol , vol.48 , pp. 485-503
    • Nichols, R.1
  • 119
    • 77957331884 scopus 로고    scopus 로고
    • Myoinhibiting peptides are the ancestral ligands of the promiscuous Drosophila sex peptide receptor
    • doi:10.1007/S00018-010-0393-8
    • Poels J, Van Loy T, Vandersmissen HP, Van Hiel B, Van Soest S, Nachman RJ, et al. Myoinhibiting peptides are the ancestral ligands of the promiscuous Drosophila sex peptide receptor. Cell Mol Life Sci (2010) 67:3511-22. doi:10.1007/S00018-010-0393-8.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3511-3522
    • Poels, J.1    Van Loy, T.2    Vandersmissen, H.P.3    Van Hiel, B.4    Van Soest, S.5    Nachman, R.J.6
  • 121
    • 0042140707 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of the first two specific insect myosuppressin receptors
    • doi:10.1073/Pnas.1632197100
    • Egerod K, Reynisson E, Hauser F, Cazzamali G, Williamson M, Grimmelikhuijzen CJ. Molecular cloning and functional expression of the first two specific insect myosuppressin receptors. Proc Natl Acad Sci U S A (2003) 100:9808-13. doi:10.1073/Pnas.1632197100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9808-9813
    • Egerod, K.1    Reynisson, E.2    Hauser, F.3    Cazzamali, G.4    Williamson, M.5    Grimmelikhuijzen, C.J.6
  • 122
    • 0022514574 scopus 로고
    • Black widow spider venom-induced release of neurotransmitters: mammalian synaptosomes are stimulated by a unique venom component (alpha-latrotoxin), insect synaptosomes by multiple components
    • doi:10.1016/0306-4522(86)90005-9
    • Knipper M, Madeddu L, Breer H, Meldolesi J. Black widow spider venom-induced release of neurotransmitters: mammalian synaptosomes are stimulated by a unique venom component (alpha-latrotoxin), insect synaptosomes by multiple components. Neuroscience (1986) 19:55-62. doi:10.1016/0306-4522(86)90005-9.
    • (1986) Neuroscience , vol.19 , pp. 55-62
    • Knipper, M.1    Madeddu, L.2    Breer, H.3    Meldolesi, J.4
  • 123
    • 79960748416 scopus 로고    scopus 로고
    • The latrophilins, "split-personality" receptors
    • Silva JP, Ushkaryov YA. The latrophilins, "split-personality" receptors. Adv Exp Med Biol (2010) 706:59-75.
    • (2010) Adv Exp Med Biol , vol.706 , pp. 59-75
    • Silva, J.P.1    Ushkaryov, Y.A.2
  • 124
    • 33847415775 scopus 로고    scopus 로고
    • Insecticidal toxins from black widow spider venom
    • doi:10.1016/j.toxicon.2006.11.021
    • Rohou A, Nield J, Ushkaryov YA. Insecticidal toxins from black widow spider venom. Toxicon (2007) 49:531-49. doi:10.1016/j.toxicon.2006.11.021.
    • (2007) Toxicon , vol.49 , pp. 531-549
    • Rohou, A.1    Nield, J.2    Ushkaryov, Y.A.3
  • 125
    • 79961071808 scopus 로고    scopus 로고
    • Latrophilin 1 and its endogenous ligand lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities
    • doi:10.1073/pnas.1019434108
    • Silva JP, Lelianova VG, Ermolyuk YS, Vysokov N, Hitchen PG, Berninghausen O, et al. Latrophilin 1 and its endogenous ligand lasso/teneurin-2 form a high-affinity transsynaptic receptor pair with signaling capabilities. Proc Natl Acad Sci U S A (2011) 108:12113-8. doi:10.1073/pnas.1019434108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 12113-12118
    • Silva, J.P.1    Lelianova, V.G.2    Ermolyuk, Y.S.3    Vysokov, N.4    Hitchen, P.G.5    Berninghausen, O.6
  • 126
    • 84875382511 scopus 로고    scopus 로고
    • Comparative genomic analysis and evolution of family-B G protein-coupled receptors from six model insect species
    • doi:10.1016/J.Gene.2013.01.061
    • Li CJ, Chen M, Sang M, Liu X, Wu W, Li B. Comparative genomic analysis and evolution of family-B G protein-coupled receptors from six model insect species. Gene (2013) 519:1-12. doi:10.1016/J.Gene.2013.01.061.
    • (2013) Gene , vol.519 , pp. 1-12
    • Li, C.J.1    Chen, M.2    Sang, M.3    Liu, X.4    Wu, W.5    Li, B.6
  • 127
    • 33846634186 scopus 로고    scopus 로고
    • Evolution of secretin family GPCR members in the metazoa
    • doi:10.1186/1471-2148-6-108
    • Cardoso JC, Pinto VC, Vieira FA, Clark MS, Power DM. Evolution of secretin family GPCR members in the metazoa. BMC Evol Biol (2006) 6:108. doi:10.1186/1471-2148-6-108.
    • (2006) BMC Evol Biol , vol.6 , pp. 108
    • Cardoso, J.C.1    Pinto, V.C.2    Vieira, F.A.3    Clark, M.S.4    Power, D.M.5
  • 128
    • 84892176517 scopus 로고    scopus 로고
    • Molecular analysis of light pulse stimulated blood feeding inhibition in Anopheles gambiae
    • doi:10.1186/1472-6793-8-23
    • Das S, Dimopoulos G. Molecular analysis of light pulse stimulated blood feeding inhibition in Anopheles gambiae. Am J Trop Med Hyg (2008) 79:333. doi:10.1186/1472-6793-8-23.
    • (2008) Am J Trop Med Hyg , vol.79 , pp. 333
    • Das, S.1    Dimopoulos, G.2
  • 129
    • 70349090033 scopus 로고    scopus 로고
    • Functional differences between two CRF-related diuretic hormone receptors in Drosophila
    • doi:10.1242/Jeb.033175
    • Hector CE, Bretz CA, Zhao Y, Johnson EC. Functional differences between two CRF-related diuretic hormone receptors in Drosophila. J Exp Biol (2009) 212:3142-7. doi:10.1242/Jeb.033175.
    • (2009) J Exp Biol , vol.212 , pp. 3142-3147
    • Hector, C.E.1    Bretz, C.A.2    Zhao, Y.3    Johnson, E.C.4
  • 130
    • 0031832021 scopus 로고    scopus 로고
    • Dose-dependent effects of CRF-like diuretic peptide on transcellular and paracellular transport pathways
    • Clark TM, Hayes TK, Beyenbach KW. Dose-dependent effects of CRF-like diuretic peptide on transcellular and paracellular transport pathways. Am J Physiol (1998) 274:F834-40.
    • (1998) Am J Physiol , vol.274
    • Clark, T.M.1    Hayes, T.K.2    Beyenbach, K.W.3
  • 131
    • 54549112035 scopus 로고    scopus 로고
    • Diuretic hormone 44 receptor in Malpighian tubules of the mosquito Aedes aegypti: evidence for transcriptional regulation paralleling urination
    • doi:10.1111/J.1365-2583.2008.00817.X
    • Jagge CL, Pietrantonio PV. Diuretic hormone 44 receptor in Malpighian tubules of the mosquito Aedes aegypti: evidence for transcriptional regulation paralleling urination. Insect Mol Biol (2008) 17:413-26. doi:10.1111/J.1365-2583.2008.00817.X.
    • (2008) Insect Mol Biol , vol.17 , pp. 413-426
    • Jagge, C.L.1    Pietrantonio, P.V.2
  • 132
    • 84865864193 scopus 로고    scopus 로고
    • Calcitonin-like diuretic hormones in insects
    • doi:10.1016/J.Ibmb.2012.06.006
    • Zandawala M. Calcitonin-like diuretic hormones in insects. Insect Biochem Mol Biol (2012) 42:816-25. doi:10.1016/J.Ibmb.2012.06.006.
    • (2012) Insect Biochem Mol Biol , vol.42 , pp. 816-825
    • Zandawala, M.1
  • 133
    • 25844477132 scopus 로고    scopus 로고
    • Mosquito natriuretic peptide identified as a calcitonin-like diuretic hormone in Anopheles gambiae (Giles)
    • doi:10.1242/Jeb.01760
    • Coast GM, Garside CS, Webster SG, Schegg KM, Schooley DA. Mosquito natriuretic peptide identified as a calcitonin-like diuretic hormone in Anopheles gambiae (Giles). J Exp Biol (2005) 208:3281-91. doi:10.1242/Jeb.01760.
    • (2005) J Exp Biol , vol.208 , pp. 3281-3291
    • Coast, G.M.1    Garside, C.S.2    Webster, S.G.3    Schegg, K.M.4    Schooley, D.A.5
  • 134
    • 84870550626 scopus 로고    scopus 로고
    • Role in diuresis of a calcitonin receptor (GPRCAL1) expressed in a distal-proximal gradient in renal organs of the mosquito Aedes aegypti (L.)
    • doi:10.1371/journal.pone.0050374
    • Kwon H, Lu HL, Longnecker MT, Pietrantonio PV. Role in diuresis of a calcitonin receptor (GPRCAL1) expressed in a distal-proximal gradient in renal organs of the mosquito Aedes aegypti (L.). PLoS One (2012) 7:e50374. doi:10.1371/journal.pone.0050374.
    • (2012) PLoS One , vol.7
    • Kwon, H.1    Lu, H.L.2    Longnecker, M.T.3    Pietrantonio, P.V.4
  • 135
    • 0032582489 scopus 로고    scopus 로고
    • Extended life-span and stress resistance in the Drosophila mutant Methuselah
    • doi:10.1126/Science.282.5390.943
    • Lin YJ, Seroude L, Benzer S. Extended life-span and stress resistance in the Drosophila mutant Methuselah. Science (1998) 282:943-6. doi:10.1126/Science.282.5390.943.
    • (1998) Science , vol.282 , pp. 943-946
    • Lin, Y.J.1    Seroude, L.2    Benzer, S.3
  • 136
    • 0035957435 scopus 로고    scopus 로고
    • Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan
    • doi:10.1073/Pnas.051625298
    • West AP, Llamas LL, Snow PM, Benzer S, Bjorkman PJ. Crystal structure of the ectodomain of Methuselah, a Drosophila G protein-coupled receptor associated with extended lifespan. Proc Natl Acad Sci U S A (2001) 98:3744-9. doi:10.1073/Pnas.051625298.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3744-3749
    • West, A.P.1    Llamas, L.L.2    Snow, P.M.3    Benzer, S.4    Bjorkman, P.J.5
  • 137
    • 2942748080 scopus 로고    scopus 로고
    • The endogenous ligand stunted of the GPCR Methuselah extends lifespan in Drosophila
    • doi:10.1038/Ncb1133
    • Cvejic S, Zhu Z, Felice SJ, Berman Y, Huang XY. The endogenous ligand stunted of the GPCR Methuselah extends lifespan in Drosophila. Nat Cell Biol (2004) 6:540-6. doi:10.1038/Ncb1133.
    • (2004) Nat Cell Biol , vol.6 , pp. 540-546
    • Cvejic, S.1    Zhu, Z.2    Felice, S.J.3    Berman, Y.4    Huang, X.Y.5
  • 138
    • 70350509607 scopus 로고    scopus 로고
    • The Drosophila G protein-coupled receptor, Methuselah, exhibits a promiscuous response to peptides
    • doi:10.1002/Pro.221
    • Ja WW, Carvalho GB, Madrigal M, Roberts RW, Benzer S. The Drosophila G protein-coupled receptor, Methuselah, exhibits a promiscuous response to peptides. Protein Sci (2009) 18:2203-8. doi:10.1002/Pro.221.
    • (2009) Protein Sci , vol.18 , pp. 2203-2208
    • Ja, W.W.1    Carvalho, G.B.2    Madrigal, M.3    Roberts, R.W.4    Benzer, S.5
  • 139
    • 0032484023 scopus 로고    scopus 로고
    • a-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors-G-protein coupling not required for triggering exocytosis
    • doi:10.1074/Jbc.273.49.32715
    • Sugita S, Ichtchenko K, Khvotchev M, Südhof TC. a-Latrotoxin receptor CIRL/latrophilin 1 (CL1) defines an unusual family of ubiquitous G-protein-linked receptors-G-protein coupling not required for triggering exocytosis. J Biol Chem (1998) 273:32715-24. doi:10.1074/Jbc.273.49.32715.
    • (1998) J Biol Chem , vol.273 , pp. 32715-32724
    • Sugita, S.1    Ichtchenko, K.2    Khvotchev, M.3    Südhof, T.C.4
  • 140
    • 82355161914 scopus 로고    scopus 로고
    • The hector G-protein coupled receptor is required in a subset of fruitless neurons for male courtship behavior
    • doi:10.1371/journal.pone.0028269
    • Li YL, Hoxha V, Lama C, Dinh BH, Vo CN, Dauwalder B. The hector G-protein coupled receptor is required in a subset of fruitless neurons for male courtship behavior. PLoS One (2011) 6:e28269. doi:10.1371/journal.pone.0028269.
    • (2011) PLoS One , vol.6
    • Li, Y.L.1    Hoxha, V.2    Lama, C.3    Dinh, B.H.4    Vo, C.N.5    Dauwalder, B.6
  • 141
    • 14744269527 scopus 로고    scopus 로고
    • Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two-dimensional capillary liquid chromatography quadrupole time-of-flight mass spectrometry
    • doi:10.1002/Jms.744
    • Baggerman G, Boonen K, Verleyen P, De Loof A, Schoofs L. Peptidomic analysis of the larval Drosophila melanogaster central nervous system by two-dimensional capillary liquid chromatography quadrupole time-of-flight mass spectrometry. J Mass Spectrom (2005) 40:250-60. doi:10.1002/Jms.744.
    • (2005) J Mass Spectrom , vol.40 , pp. 250-260
    • Baggerman, G.1    Boonen, K.2    Verleyen, P.3    De Loof, A.4    Schoofs, L.5
  • 142
    • 84858332292 scopus 로고    scopus 로고
    • The receptor guanylate cyclase Gyc76C and a peptide ligand, NPLP1-VQQ, modulate the innate immune IMD pathway in response to salt stress
    • doi:10.1016/J.Peptides.2011.08.019
    • Overend G, Cabrero P, Guo AX, Sebastian S, Cundall M, Armstrong H, et al. The receptor guanylate cyclase Gyc76C and a peptide ligand, NPLP1-VQQ, modulate the innate immune IMD pathway in response to salt stress. Peptides (2012) 34:209-18. doi:10.1016/J.Peptides.2011.08.019.
    • (2012) Peptides , vol.34 , pp. 209-218
    • Overend, G.1    Cabrero, P.2    Guo, A.X.3    Sebastian, S.4    Cundall, M.5    Armstrong, H.6
  • 143
    • 69449084683 scopus 로고    scopus 로고
    • Receptor guanylyl cyclases in Inka cells targeted by eclosion hormone
    • doi:10.1073/Pnas.0812593106
    • Chang JC, Yang RB, Adams ME, Lu KH. Receptor guanylyl cyclases in Inka cells targeted by eclosion hormone. Proc Natl Acad Sci U S A (2009) 106:13371-6. doi:10.1073/Pnas.0812593106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13371-13376
    • Chang, J.C.1    Yang, R.B.2    Adams, M.E.3    Lu, K.H.4
  • 144
    • 30844437476 scopus 로고    scopus 로고
    • Signaling and function of insulin-like peptides in insects
    • doi:10.1146/annurev.ento.51.110104.151011
    • Wu Q, Brown MR. Signaling and function of insulin-like peptides in insects. Annu Rev Entomol (2006) 51:1-24. doi:10.1146/annurev.ento.51.110104.151011.
    • (2006) Annu Rev Entomol , vol.51 , pp. 1-24
    • Wu, Q.1    Brown, M.R.2
  • 145
    • 0023390967 scopus 로고
    • Structure and ligand specificity of the Drosophila melanogaster insulin receptor
    • Fernandez-Almonacid R, Rosen OM. Structure and ligand specificity of the Drosophila melanogaster insulin receptor. Mol Cell Biol (1987) 7:2718-27.
    • (1987) Mol Cell Biol , vol.7 , pp. 2718-2727
    • Fernandez-Almonacid, R.1    Rosen, O.M.2
  • 146
    • 0022389345 scopus 로고
    • Acquisition of insulin-dependent protein tyrosine kinase-activity during Drosophila embryogenesis
    • Petruzzelli L, Herrera R, Garcia-Arenas R, Rosen OM. Acquisition of insulin-dependent protein tyrosine kinase-activity during Drosophila embryogenesis. J Biol Chem (1985) 260:6072-5.
    • (1985) J Biol Chem , vol.260 , pp. 6072-6075
    • Petruzzelli, L.1    Herrera, R.2    Garcia-Arenas, R.3    Rosen, O.M.4
  • 147
    • 0035916357 scopus 로고    scopus 로고
    • An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control
    • doi:10.1016/S0960-9822(01)00068-9
    • Brogiolo W, Stocker H, Ikeya T, Rintelen F, Fernandez R, Hafen E. An evolutionarily conserved function of the Drosophila insulin receptor and insulin-like peptides in growth control. Curr Biol (2001) 11:213-21. doi:10.1016/S0960-9822(01)00068-9.
    • (2001) Curr Biol , vol.11 , pp. 213-221
    • Brogiolo, W.1    Stocker, H.2    Ikeya, T.3    Rintelen, F.4    Fernandez, R.5    Hafen, E.6
  • 148
    • 84859363786 scopus 로고    scopus 로고
    • Insulin-like peptides: structure, signaling, and function
    • Gilbert LI, editor. New York, NY: Elsevier Academic Press.
    • Antonova Y, Arik AJ, Moore W, Riehle MR, Brown MR. Insulin-like peptides: structure, signaling, and function. In: Gilbert LI, editor. Insect Endocrinology. New York, NY: Elsevier Academic Press (2012). p. 63-92.
    • (2012) Insect Endocrinology , pp. 63-92
    • Antonova, Y.1    Arik, A.J.2    Moore, W.3    Riehle, M.R.4    Brown, M.R.5
  • 149
    • 77956343172 scopus 로고    scopus 로고
    • Two insulin-like peptide family members from the mosquito Aedes aegypti exhibit differential biological and receptor binding activities
    • doi:10.1016/j.mce.2010.07.003
    • Wen Z, Gulia M, Clark KD, Dhara A, Crim JW, Strand MR, et al. Two insulin-like peptide family members from the mosquito Aedes aegypti exhibit differential biological and receptor binding activities. Mol Cell Endocrinol (2010) 328:47-55. doi:10.1016/j.mce.2010.07.003.
    • (2010) Mol Cell Endocrinol , vol.328 , pp. 47-55
    • Wen, Z.1    Gulia, M.2    Clark, K.D.3    Dhara, A.4    Crim, J.W.5    Strand, M.R.6
  • 150
    • 78650954923 scopus 로고    scopus 로고
    • Structural and biological properties of the Drosophila insulin-like peptide 5 show evolutionary conservation
    • doi:10.1074/Jbc.M110.156018
    • Sajid W, Kulahin N, Schluckebier G, Ribel U, Henderson HR, Tatar M, et al. Structural and biological properties of the Drosophila insulin-like peptide 5 show evolutionary conservation. J Biol Chem (2011) 286:661-73. doi:10.1074/Jbc.M110.156018.
    • (2011) J Biol Chem , vol.286 , pp. 661-673
    • Sajid, W.1    Kulahin, N.2    Schluckebier, G.3    Ribel, U.4    Henderson, H.R.5    Tatar, M.6
  • 151
    • 44449157170 scopus 로고    scopus 로고
    • An insulin-like peptide regulates egg maturation and metabolism in the mosquito Aedes aegypti
    • doi:10.1073/Pnas.0800478105
    • Brown MR, Clark KD, Gulia M, Zhao Z, Garczynski SF, Crim JW, et al. An insulin-like peptide regulates egg maturation and metabolism in the mosquito Aedes aegypti. Proc Natl Acad Sci U S A (2008) 105:5716-21. doi:10.1073/Pnas.0800478105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5716-5721
    • Brown, M.R.1    Clark, K.D.2    Gulia, M.3    Zhao, Z.4    Garczynski, S.F.5    Crim, J.W.6
  • 152
    • 84867566062 scopus 로고    scopus 로고
    • Ovary ecdysteroidogenic hormone activates egg maturation in the mosquito Georgecraigius atropalpus after adult eclosion or a blood meal
    • doi:10.1242/Jeb.074617
    • Gulia-Nuss M, Eum JH, Strand MR, Brown MR. Ovary ecdysteroidogenic hormone activates egg maturation in the mosquito Georgecraigius atropalpus after adult eclosion or a blood meal. J Exp Biol (2012) 215:3758-67. doi:10.1242/Jeb.074617.
    • (2012) J Exp Biol , vol.215 , pp. 3758-3767
    • Gulia-Nuss, M.1    Eum, J.H.2    Strand, M.R.3    Brown, M.R.4
  • 153
    • 79957603530 scopus 로고    scopus 로고
    • Insulin-like peptides and the target of rapamycin pathway coordinately regulate blood digestion and egg maturation in the mosquito Aedes aegypti
    • doi:10.1371/journal.pone.0020401
    • Gulia-Nuss M, Robertson AE, Brown MR, Strand MR. Insulin-like peptides and the target of rapamycin pathway coordinately regulate blood digestion and egg maturation in the mosquito Aedes aegypti. PLoS One (2011) 6:e20401. doi:10.1371/journal.pone.0020401.
    • (2011) PLoS One , vol.6
    • Gulia-Nuss, M.1    Robertson, A.E.2    Brown, M.R.3    Strand, M.R.4
  • 154
    • 80055098733 scopus 로고    scopus 로고
    • Blood feeding and insulin-like peptide 3 stimulate proliferation of hemocytes in the mosquito Aedes aegypti
    • doi:10.1371/Journal.Ppat.1002274
    • Castillo J, Brown MR, Strand MR. Blood feeding and insulin-like peptide 3 stimulate proliferation of hemocytes in the mosquito Aedes aegypti. PLoS Pathog (2011) 7:e1002274. doi:10.1371/Journal.Ppat.1002274.
    • (2011) PLoS Pathog , vol.7
    • Castillo, J.1    Brown, M.R.2    Strand, M.R.3
  • 155
    • 80053461384 scopus 로고    scopus 로고
    • The receptor tyrosine kinase Alk controls neurofibromin functions in Drosophila growth and learning
    • doi:10.1371/Journal.Pgen.1002281
    • Gouzi JY, Moressis A, Walker JA, Apostolopoulou AA, Palmer RH, Bernards A, et al. The receptor tyrosine kinase Alk controls neurofibromin functions in Drosophila growth and learning. PLoS Genet (2011) 7:e1002281. doi:10.1371/Journal.Pgen.1002281.
    • (2011) PLoS Genet , vol.7
    • Gouzi, J.Y.1    Moressis, A.2    Walker, J.A.3    Apostolopoulou, A.A.4    Palmer, R.H.5    Bernards, A.6
  • 156
    • 79960673330 scopus 로고    scopus 로고
    • An evolutionary conserved role for anaplastic lymphoma kinase in behavioral responses to ethanol
    • doi:10.1371/journal.pone.0022636
    • Lasek AW, Lim J, Kliethermes CL, Berger KH, Joslyn G, Brush G, et al. An evolutionary conserved role for anaplastic lymphoma kinase in behavioral responses to ethanol. PLoS One (2011) 6:e22636. doi:10.1371/journal.pone.0022636.
    • (2011) PLoS One , vol.6
    • Lasek, A.W.1    Lim, J.2    Kliethermes, C.L.3    Berger, K.H.4    Joslyn, G.5    Brush, G.6
  • 157
    • 0034933673 scopus 로고    scopus 로고
    • Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo
    • doi:10.1046/J.1365-2443.2001.00440.X
    • Lorén CE, Scully A, Grabbe C, Edeen PT, Thomas J, McKeown M, et al. Identification and characterization of DAlk: a novel Drosophila melanogaster RTK which drives ERK activation in vivo. Genes Cells (2001) 6:531-44. doi:10.1046/J.1365-2443.2001.00440.X.
    • (2001) Genes Cells , vol.6 , pp. 531-544
    • Lorén, C.E.1    Scully, A.2    Grabbe, C.3    Edeen, P.T.4    Thomas, J.5    McKeown, M.6
  • 158
    • 66949152073 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase: signalling in development and disease
    • doi:10.1042/Bj20090387
    • Palmer RH, Vernersson E, Grabbe C, Hallberg B. Anaplastic lymphoma kinase: signalling in development and disease. Biochem J (2009) 420:345-61. doi:10.1042/Bj20090387.
    • (2009) Biochem J , vol.420 , pp. 345-361
    • Palmer, R.H.1    Vernersson, E.2    Grabbe, C.3    Hallberg, B.4
  • 159
    • 34249816481 scopus 로고    scopus 로고
    • The ligand jelly belly (Jeb) activates the Drosophila Alk RTK to drive PC12 cell differentiation, but is unable to activate the mouse ALK RTK
    • doi:10.1002/Jez.B.21146
    • Yang HL, Eriksson T, Vernersson E, Vigny M, Hallberg B, Palmer RH. The ligand jelly belly (Jeb) activates the Drosophila Alk RTK to drive PC12 cell differentiation, but is unable to activate the mouse ALK RTK. J Exp Zool B Mol Dev Evol (2007) 308(3):269-82. doi:10.1002/Jez.B.21146.
    • (2007) J Exp Zool B Mol Dev Evol , vol.308 , Issue.3 , pp. 269-282
    • Yang, H.L.1    Eriksson, T.2    Vernersson, E.3    Vigny, M.4    Hallberg, B.5    Palmer, R.H.6
  • 160
    • 66249089158 scopus 로고    scopus 로고
    • A new family of receptor tyrosine kinases with a venus flytrap binding domain in insects and other invertebrates activated by amino acids
    • doi:10.1371/journal.pone.0005651
    • Ahier A, Rondard P, Gouignard N, Khayath N, Huang S, Trolet J, et al. A new family of receptor tyrosine kinases with a venus flytrap binding domain in insects and other invertebrates activated by amino acids. PLoS One (2009) 4:e5651. doi:10.1371/journal.pone.0005651.
    • (2009) PLoS One , vol.4
    • Ahier, A.1    Rondard, P.2    Gouignard, N.3    Khayath, N.4    Huang, S.5    Trolet, J.6
  • 161
    • 12244250728 scopus 로고    scopus 로고
    • An unusual receptor tyrosine kinase of Schistosoma mansoni contains a venus flytrap module
    • doi:10.1016/S0166-6851(02)00249-9
    • Vicogne J, Pin JP, Lardans V, Capron M, Noël C, Dissous C. An unusual receptor tyrosine kinase of Schistosoma mansoni contains a venus flytrap module. Mol Biochem Parasitol (2003) 126:51-62. doi:10.1016/S0166-6851(02)00249-9.
    • (2003) Mol Biochem Parasitol , vol.126 , pp. 51-62
    • Vicogne, J.1    Pin, J.P.2    Lardans, V.3    Capron, M.4    Noël, C.5    Dissous, C.6
  • 162
    • 36549022180 scopus 로고    scopus 로고
    • Prothoracicotropic hormone regulates developmental timing and body size in Drosophila
    • doi:10.1016/J.Devcel.2007.11.003
    • McBrayer Z, Ono H, Shimell M, Parvy JP, Beckstead RB, Warren JT, et al. Prothoracicotropic hormone regulates developmental timing and body size in Drosophila. Dev Cell (2007) 13:857-71. doi:10.1016/J.Devcel.2007.11.003.
    • (2007) Dev Cell , vol.13 , pp. 857-871
    • McBrayer, Z.1    Ono, H.2    Shimell, M.3    Parvy, J.P.4    Beckstead, R.B.5    Warren, J.T.6
  • 163
    • 71549168637 scopus 로고    scopus 로고
    • The insect neuropeptide PTTH activates receptor tyrosine kinase torso to initiate metamorphosis
    • doi:10.1126/Science.1176450
    • Rewitz KF, Yamanaka N, Gilbert LI, O'Connor MB. The insect neuropeptide PTTH activates receptor tyrosine kinase torso to initiate metamorphosis. Science (2009) 326:1403-5. doi:10.1126/Science.1176450.
    • (2009) Science , vol.326 , pp. 1403-1405
    • Rewitz, K.F.1    Yamanaka, N.2    Gilbert, L.I.3    O'Connor, M.B.4
  • 164
    • 84857141188 scopus 로고    scopus 로고
    • Prothoracicotropic hormone
    • Gilbert LI, editor. New York, NY: Elsevier Academic Press.
    • Smith W, Rybczynski R. Prothoracicotropic hormone. In: Gilbert LI, editor. Insect Endocrinology. New York, NY: Elsevier Academic Press (2012). p. 1-62.
    • (2012) Insect Endocrinology , pp. 1-62
    • Smith, W.1    Rybczynski, R.2
  • 165
    • 77958509462 scopus 로고    scopus 로고
    • Analysis of molecular markers for metamorphic competency and their response to starvation or feeding in the mosquito, Aedes aegypti (Diptera: Culicidae)
    • doi:10.1016/j.jinsphys.2010.08.020
    • Telang A, Peterson B, Frame L, Baker E, Brown MR. Analysis of molecular markers for metamorphic competency and their response to starvation or feeding in the mosquito, Aedes aegypti (Diptera: Culicidae). J Insect Physiol (2010) 56:1925-34. doi:10.1016/j.jinsphys.2010.08.020.
    • (2010) J Insect Physiol , vol.56 , pp. 1925-1934
    • Telang, A.1    Peterson, B.2    Frame, L.3    Baker, E.4    Brown, M.R.5
  • 166
    • 0023149149 scopus 로고
    • Multiple forms of cerebral peptides with steroidogenic functions in pupal and adult brains of the yellow fever mosquito, Aedes aegypti
    • doi:10.1016/0303-7207(87)90071-2
    • Whisenton LR, Kelly TJ, Bollenbacher WE. Multiple forms of cerebral peptides with steroidogenic functions in pupal and adult brains of the yellow fever mosquito, Aedes aegypti. Mol Cell Endocrinol (1987) 50:3-14. doi:10.1016/0303-7207(87)90071-2.
    • (1987) Mol Cell Endocrinol , vol.50 , pp. 3-14
    • Whisenton, L.R.1    Kelly, T.J.2    Bollenbacher, W.E.3
  • 167
    • 79952295211 scopus 로고    scopus 로고
    • Molecular structure of the prothoracicotropic hormone gene in the northern house mosquito, Culex pipiens, and its expression analysis in association with diapause and blood feeding
    • doi:10.1111/j.1365-2583.2010.01058.x
    • Zhang Q, Denlinger DL. Molecular structure of the prothoracicotropic hormone gene in the northern house mosquito, Culex pipiens, and its expression analysis in association with diapause and blood feeding. Insect Mol Biol (2011) 20:201-13. doi:10.1111/j.1365-2583.2010.01058.x.
    • (2011) Insect Mol Biol , vol.20 , pp. 201-213
    • Zhang, Q.1    Denlinger, D.L.2
  • 168
    • 0001288280 scopus 로고
    • Inactive prothoracic glands in larvae and pupae of Aedes aegypti: ecdysteroid release by tissues in the thorax and abdomen
    • doi:10.1016/0965-1748(92)90032-A
    • Jenkins SP, Brown MR, Lea AO. Inactive prothoracic glands in larvae and pupae of Aedes aegypti: ecdysteroid release by tissues in the thorax and abdomen. Insect Biochem Mol Biol (1992) 22:553-9. doi:10.1016/0965-1748(92)90032-A.
    • (1992) Insect Biochem Mol Biol , vol.22 , pp. 553-559
    • Jenkins, S.P.1    Brown, M.R.2    Lea, A.O.3
  • 169
    • 79955133184 scopus 로고    scopus 로고
    • EGF signaling regulates the proliferation of intestinal stem cells in Drosophila
    • doi:10.1242/Dev.056671
    • Biteau B, Jasper H. EGF signaling regulates the proliferation of intestinal stem cells in Drosophila. Development (2011) 138:1045-55. doi:10.1242/Dev.056671.
    • (2011) Development , vol.138 , pp. 1045-1055
    • Biteau, B.1    Jasper, H.2
  • 170
    • 26444536535 scopus 로고    scopus 로고
    • Regulating the dynamics of EGF receptor signaling in space and time
    • doi:10.1242/Dev.02006
    • Shilo BZ. Regulating the dynamics of EGF receptor signaling in space and time. Development (2005) 132:4017-27. doi:10.1242/Dev.02006.
    • (2005) Development , vol.132 , pp. 4017-4027
    • Shilo, B.Z.1
  • 171
    • 0035543645 scopus 로고    scopus 로고
    • Developmental variation in epidermal growth factor receptor size and localization in the malaria mosquito, Anopheles gambiae
    • doi:10.1046/J.0962-1075.2001.00302.X
    • Lycett G, Blass C, Louis C. Developmental variation in epidermal growth factor receptor size and localization in the malaria mosquito, Anopheles gambiae. Insect Mol Biol (2001) 10:619-28. doi:10.1046/J.0962-1075.2001.00302.X.
    • (2001) Insect Mol Biol , vol.10 , pp. 619-628
    • Lycett, G.1    Blass, C.2    Louis, C.3
  • 172
    • 84864981200 scopus 로고    scopus 로고
    • Autocrine platelet-derived growth factor-vascular endothelial growth factor receptor-related (Pvr) pathway activity controls intestinal stem cell proliferation in the adult Drosophila midgut
    • doi:10.1074/Jbc.M112.378018
    • Bond D, Foley E. Autocrine platelet-derived growth factor-vascular endothelial growth factor receptor-related (Pvr) pathway activity controls intestinal stem cell proliferation in the adult Drosophila midgut. J Biol Chem (2012) 287:27359-70. doi:10.1074/Jbc.M112.378018.
    • (2012) J Biol Chem , vol.287 , pp. 27359-27370
    • Bond, D.1    Foley, E.2
  • 173
    • 0037155683 scopus 로고    scopus 로고
    • Developmental control of blood cell migration by the Drosophila VEGF pathway
    • doi:10.1016/S0092-8674(02)00676-1
    • Cho NK, Keyes L, Johnson E, Heller J, Ryner L, Karim F, et al. Developmental control of blood cell migration by the Drosophila VEGF pathway. Cell (2002) 108:865-76. doi:10.1016/S0092-8674(02)00676-1.
    • (2002) Cell , vol.108 , pp. 865-876
    • Cho, N.K.1    Keyes, L.2    Johnson, E.3    Heller, J.4    Ryner, L.5    Karim, F.6
  • 174
    • 65549142248 scopus 로고    scopus 로고
    • FGF ligands in Drosophila have distinct activities required to support cell migration and differentiation
    • doi:10.1242/Dev.027904
    • Kadam S, McMahon A, Tzou P, Stathopoulos A. FGF ligands in Drosophila have distinct activities required to support cell migration and differentiation. Development (2009) 136:739-47. doi:10.1242/Dev.027904.
    • (2009) Development , vol.136 , pp. 739-747
    • Kadam, S.1    McMahon, A.2    Tzou, P.3    Stathopoulos, A.4
  • 175
    • 85047677255 scopus 로고    scopus 로고
    • Expression pattern of Drosophila ret suggests a common ancestral origin between the metamorphosis precursors in insect endoderm and the vertebrate enteric neurons
    • doi:10.1073/Pnas.021558598
    • Hahn M, Bishop JM. Expression pattern of Drosophila ret suggests a common ancestral origin between the metamorphosis precursors in insect endoderm and the vertebrate enteric neurons. Proc Natl Acad Sci U S A (2001) 98:1053-8. doi:10.1073/Pnas.021558598.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1053-1058
    • Hahn, M.1    Bishop, J.M.2
  • 176
    • 18144392678 scopus 로고    scopus 로고
    • ZD6474 suppresses oncogenic RET isoforms in a Drosophila model for type 2 multiple endocrine neoplasia syndromes and papillary thyroid carcinoma
    • doi:10.1158/0008-5472.Can-04-4561
    • Vidal M, Wells S, Ryan A, Cagan R. ZD6474 suppresses oncogenic RET isoforms in a Drosophila model for type 2 multiple endocrine neoplasia syndromes and papillary thyroid carcinoma. Cancer Res (2005) 65:3538-41. doi:10.1158/0008-5472.Can-04-4561.
    • (2005) Cancer Res , vol.65 , pp. 3538-3541
    • Vidal, M.1    Wells, S.2    Ryan, A.3    Cagan, R.4
  • 177
    • 0037237125 scopus 로고    scopus 로고
    • Expression and function of the Ror-family receptor tyrosine kinases during development: lessons from genetic analyses of nematodes, mice, and humans
    • doi:10.1081/RRS-120018757
    • Yoda A, Oishi I, Minami Y. Expression and function of the Ror-family receptor tyrosine kinases during development: lessons from genetic analyses of nematodes, mice, and humans. J Recept Signal Transduct Res (2003) 23(1):1-15. doi:10.1081/RRS-120018757.
    • (2003) J Recept Signal Transduct Res , vol.23 , Issue.1 , pp. 1-15
    • Yoda, A.1    Oishi, I.2    Minami, Y.3
  • 178
    • 33744542647 scopus 로고    scopus 로고
    • Drosophila Eph receptor guides specific axon branches of mushroom body neurons
    • doi:10.1242/Dev.02353
    • Boyle M, Nighorn A, Thomas JB. Drosophila Eph receptor guides specific axon branches of mushroom body neurons. Development (2006) 133:1845-54. doi:10.1242/Dev.02353.
    • (2006) Development , vol.133 , pp. 1845-1854
    • Boyle, M.1    Nighorn, A.2    Thomas, J.B.3
  • 179
    • 84862752910 scopus 로고    scopus 로고
    • Structural studies of the TGF-βs and their receptors-insights into evolution of the TGF-β superfamily
    • doi:10.1016/j.febslet.2012.05.028
    • Hinck AP. Structural studies of the TGF-βs and their receptors-insights into evolution of the TGF-β superfamily. FEBS Lett (2012) 586:1860-70. doi:10.1016/j.febslet.2012.05.028.
    • (2012) FEBS Lett , vol.586 , pp. 1860-1870
    • Hinck, A.P.1
  • 180
    • 62649156796 scopus 로고    scopus 로고
    • Emergence, development and diversification of the TGF-β signalling pathway within the animal kingdom
    • doi:10.1186/1471-2148-9-28
    • Huminiecki L, Goldovsky L, Freilich S, Moustakas A, Ouzounis C, Heldin CH. Emergence, development and diversification of the TGF-β signalling pathway within the animal kingdom. BMC Evol Biol (2009) 9:28. doi:10.1186/1471-2148-9-28.
    • (2009) BMC Evol Biol , vol.9 , pp. 28
    • Huminiecki, L.1    Goldovsky, L.2    Freilich, S.3    Moustakas, A.4    Ouzounis, C.5    Heldin, C.H.6
  • 181
    • 84862771592 scopus 로고    scopus 로고
    • TGF-β signaling in development and disease
    • doi:10.1016/j.febslet.2012.05.030
    • Massagué J. TGF-β signaling in development and disease. FEBS Lett (2012) 586:1833. doi:10.1016/j.febslet.2012.05.030.
    • (2012) FEBS Lett , vol.586 , pp. 1833
    • Massagué, J.1
  • 182
    • 37449025150 scopus 로고    scopus 로고
    • Distinct signaling of Drosophila activin/TGF-β family members
    • Gesualdi SC, Haerry TE. Distinct signaling of Drosophila activin/TGF-β family members. Fly (Austin) (2007) 1:212-21.
    • (2007) Fly (Austin) , vol.1 , pp. 212-221
    • Gesualdi, S.C.1    Haerry, T.E.2
  • 183
    • 4043166192 scopus 로고    scopus 로고
    • Transforming growth factor-βs and related gene products in mosquito vectors of human malaria parasites: signaling architecture for immunological crosstalk
    • doi:10.1016/J.Molimm.2004.06.001
    • Lieber MJ, Luckhart S. Transforming growth factor-βs and related gene products in mosquito vectors of human malaria parasites: signaling architecture for immunological crosstalk. Mol Immunol (2004) 41:965-77. doi:10.1016/J.Molimm.2004.06.001.
    • (2004) Mol Immunol , vol.41 , pp. 965-977
    • Lieber, M.J.1    Luckhart, S.2
  • 184
    • 79958109656 scopus 로고    scopus 로고
    • Neuroendocrine regulation of Drosophila metamorphosis requires TGF-β/activin signaling
    • doi:10.1242/Dev.063412
    • Gibbens YY, Warren JT, Gilbert LI, O'Connor MB. Neuroendocrine regulation of Drosophila metamorphosis requires TGF-β/activin signaling. Development (2011) 138:2693-703. doi:10.1242/Dev.063412.
    • (2011) Development , vol.138 , pp. 2693-2703
    • Gibbens, Y.Y.1    Warren, J.T.2    Gilbert, L.I.3    O'Connor, M.B.4
  • 185
    • 4344646412 scopus 로고    scopus 로고
    • Regulation of gonadotropins by inhibin and activin
    • doi:10.1055/S-2004-831901
    • Gregory SJ, Kaiser UB. Regulation of gonadotropins by inhibin and activin. Semin Reprod Med (2004) 22:253-67. doi:10.1055/S-2004-831901.
    • (2004) Semin Reprod Med , vol.22 , pp. 253-267
    • Gregory, S.J.1    Kaiser, U.B.2
  • 186
    • 80455135050 scopus 로고    scopus 로고
    • Differential synthesis and action of TGF-β superfamily ligands in mouse and rat islets
    • doi:10.4161/Isl.3.6.18013
    • Brown ML, Kimura F, Bonomi LM, Ungerleider NA, Schneyer AL. Differential synthesis and action of TGF-β superfamily ligands in mouse and rat islets. Islets (2011) 3:367-75. doi:10.4161/Isl.3.6.18013.
    • (2011) Islets , vol.3 , pp. 367-375
    • Brown, M.L.1    Kimura, F.2    Bonomi, L.M.3    Ungerleider, N.A.4    Schneyer, A.L.5
  • 187
    • 66349113763 scopus 로고    scopus 로고
    • MAPK ERK signaling regulates the TGF-β1-dependent mosquito response to Plasmodium falciparum
    • doi:10.1371/journal.ppat.1000366
    • Surachetpong W, Singh N, Cheung KW, Luckhart S. MAPK ERK signaling regulates the TGF-β1-dependent mosquito response to Plasmodium falciparum. PLoS Pathog (2009) 5:e1000366. doi:10.1371/journal.ppat.1000366.
    • (2009) PLoS Pathog , vol.5
    • Surachetpong, W.1    Singh, N.2    Cheung, K.W.3    Luckhart, S.4
  • 188
    • 5644293442 scopus 로고    scopus 로고
    • Cross-talk between nitric oxide and transforming growth factor-β1 in malaria
    • doi:10.2174/1566524043359999
    • Vodovotz Y, Zamora R, Lieber MJ, Luckhart S. Cross-talk between nitric oxide and transforming growth factor-β1 in malaria. Curr Mol Med (2004) 4:787-97. doi:10.2174/1566524043359999.
    • (2004) Curr Mol Med , vol.4 , pp. 787-797
    • Vodovotz, Y.1    Zamora, R.2    Lieber, M.J.3    Luckhart, S.4
  • 189
    • 77953916959 scopus 로고    scopus 로고
    • Mutagenesis of human neuropeptide Y/peptide YY receptor Y2 reveals additional differences to Y1 in interactions with highly conserved ligand positions
    • doi:10.1016/J.Regpep.2010.04.011
    • Akerberg H, Fallmar H, Sjodin P, Boukharta L, Gutierrez-de-Teran H, Lundell I, et al. Mutagenesis of human neuropeptide Y/peptide YY receptor Y2 reveals additional differences to Y1 in interactions with highly conserved ligand positions. Regul Pept (2010) 163:120-9. doi:10.1016/J.Regpep.2010.04.011.
    • (2010) Regul Pept , vol.163 , pp. 120-129
    • Akerberg, H.1    Fallmar, H.2    Sjodin, P.3    Boukharta, L.4    Gutierrez-de-Teran, H.5    Lundell, I.6
  • 191
    • 0028169253 scopus 로고
    • Acidic residues in extracellular loops of the human Y1 neuropeptide Y receptor are essential for ligand binding
    • Walker P, Munoz M, Martinez R, Peitsch MC. Acidic residues in extracellular loops of the human Y1 neuropeptide Y receptor are essential for ligand binding. J Biol Chem (1994) 269:2863-9.
    • (1994) J Biol Chem , vol.269 , pp. 2863-2869
    • Walker, P.1    Munoz, M.2    Martinez, R.3    Peitsch, M.C.4
  • 192
    • 0029155366 scopus 로고
    • Role of a hydrophobic pocket of the human Y1 neuropeptide Y receptor in ligand binding
    • doi:10.1016/0303-7207(95)03603-5
    • Sautel M, Martinez R, Munoz M, Peitsch MC, Beck-Sickinger AG, Walker P. Role of a hydrophobic pocket of the human Y1 neuropeptide Y receptor in ligand binding. Mol Cell Endocrinol (1995) 112:215-22. doi:10.1016/0303-7207(95)03603-5.
    • (1995) Mol Cell Endocrinol , vol.112 , pp. 215-222
    • Sautel, M.1    Martinez, R.2    Munoz, M.3    Peitsch, M.C.4    Beck-Sickinger, A.G.5    Walker, P.6
  • 193
    • 9444264701 scopus 로고    scopus 로고
    • Neuropeptide Y and the nonpeptide antagonist BIBP 3226 share an overlapping binding site at the human Y1 receptor
    • Sautel M, Rudolf K, Wittneben H, Herzog H, Martinez R, Munoz M, et al. Neuropeptide Y and the nonpeptide antagonist BIBP 3226 share an overlapping binding site at the human Y1 receptor. Mol Pharmacol (1996) 50:285-92.
    • (1996) Mol Pharmacol , vol.50 , pp. 285-292
    • Sautel, M.1    Rudolf, K.2    Wittneben, H.3    Herzog, H.4    Martinez, R.5    Munoz, M.6
  • 194
    • 0042925465 scopus 로고    scopus 로고
    • Molecular cloning, functional expression, and gene silencing of two Drosophila receptors for the Drosophila neuropeptide pyrokinin-2
    • doi:10.1016/J.Bbrc.2003.08.022
    • Rosenkilde C, Cazzamali G, Williamson M, Hauser F, Søndergaard L, DeLotto R, et al. Molecular cloning, functional expression, and gene silencing of two Drosophila receptors for the Drosophila neuropeptide pyrokinin-2. Biochem Biophys Res Commun (2003) 309:485-94. doi:10.1016/J.Bbrc.2003.08.022.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 485-494
    • Rosenkilde, C.1    Cazzamali, G.2    Williamson, M.3    Hauser, F.4    Søndergaard, L.5    DeLotto, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.