메뉴 건너뛰기




Volumn 20, Issue 6, 2011, Pages 801-811

Identification of specific sites in the third intracellular loop and carboxyl terminus of the Bombyx mori pheromone biosynthesis activating neuropeptide receptor crucial for ligand-induced internalization

Author keywords

Bombyx mori; GPCR; PBAN receptor; receptor internalization; site directed mutagenesis

Indexed keywords

INSECT PROTEIN; LIGAND; NEUROPEPTIDE RECEPTOR; PHEROMONE; PHOSPHOLIPASE C;

EID: 80755187816     PISSN: 09621075     EISSN: 13652583     Source Type: Journal    
DOI: 10.1111/j.1365-2583.2011.01110.x     Document Type: Article
Times cited : (13)

References (48)
  • 1
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • DOI 10.1006/jmbi.1999.3310
    • Blom, N., Gammeltoft, S., and, Brunak, S., (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294: 1351-1362. (Pubitemid 30008805)
    • (1999) Journal of Molecular Biology , vol.294 , Issue.5 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 2
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • DOI 10.1146/annurev.biochem.72.121801.161800
    • Bonifacino, J.S., and, Traub, L.M., (2003) Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 72: 395-447. (Pubitemid 36930451)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 3
    • 65549153181 scopus 로고    scopus 로고
    • G protein independent phosphorylation and internalization of the δ-opioid receptor
    • Bradbury, F.A., Zelnik, J.C., and, Traynor, J.R., (2009) G protein independent phosphorylation and internalization of the δ-opioid receptor. J Neurochem 109: 1526-1535.
    • (2009) J Neurochem , vol.109 , pp. 1526-1535
    • Bradbury, F.A.1    Zelnik, J.C.2    Traynor, J.R.3
  • 4
    • 77957916306 scopus 로고    scopus 로고
    • Expression of pheromone biosynthesis activating neuropeptide and its receptor (PBANR) mRNA in adult female Spodoptera exigua (Lepidoptera: Noctuidae)
    • Cheng, Y., Luo, L., Jiang, X., Zhang, L., and, Niu, C., (2010) Expression of pheromone biosynthesis activating neuropeptide and its receptor (PBANR) mRNA in adult female Spodoptera exigua (Lepidoptera: Noctuidae). Arch Insect Biochem Physiol 75: 13-27.
    • (2010) Arch Insect Biochem Physiol , vol.75 , pp. 13-27
    • Cheng, Y.1    Luo, L.2    Jiang, X.3    Zhang, L.4    Niu, C.5
  • 5
    • 0042693027 scopus 로고    scopus 로고
    • Identification of a G protein-coupled receptor for pheromone biosynthesis activating neuropeptide from pheromone glands of the moth Helicoverpa zea
    • DOI 10.1073/pnas.1632485100
    • Choi, M.Y., Fuerst, E.J., Rafaeli, A., and, Jurenka, R., (2003) Identification of a G protein-coupled receptor for pheromone biosynthesis activating neuropeptide from pheromone glands of the moth Helicoverpa zea. Proc Natl Acad Sci USA 100: 9721-9726. (Pubitemid 37087008)
    • (2003) Proceedings of the National Academy of Sciences of the United States of America , vol.100 , Issue.17 , pp. 9721-9726
    • Choi, M.-Y.1    Fuerst, E.-J.2    Rafaeli, A.3    Jurenka, R.4
  • 6
    • 33947180429 scopus 로고    scopus 로고
    • Role of extracellular domains in PBAN/pyrokinin GPCRs from insects using chimera receptors
    • DOI 10.1016/j.ibmb.2006.12.004, PII S0965174806002529
    • Choi, M.Y., Fuerst, E.J., Rafaeli, A., and, Jurenka, R., (2007) Role of extracellular domains in PBAN/pyrokinin GPCRs from insects using chimera receptors. Insect Biochem Mol Biol 37: 296-306. (Pubitemid 46401387)
    • (2007) Insect Biochemistry and Molecular Biology , vol.37 , Issue.4 , pp. 296-306
    • Choi, M.-Y.1    Fuerst, E.-J.2    Rafaeli, A.3    Jurenka, R.4
  • 7
    • 33750488472 scopus 로고    scopus 로고
    • Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor
    • DOI 10.1007/s00109-006-0087-8
    • Claus, M., Neumann, S., Kleinau, G., Krause, G., and, Paschke, R., (2006) Structural determinants for G-protein activation and specificity in the third intracellular loop of the thyroid-stimulating hormone receptor. J Mol Med 84: 943-954. (Pubitemid 44655872)
    • (2006) Journal of Molecular Medicine , vol.84 , Issue.11 , pp. 943-954
    • Claus, M.1    Neumann, S.2    Kleinau, G.3    Krause, G.4    Paschke, R.5
  • 8
    • 33947362949 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor export trafficking
    • DOI 10.1016/j.bbamem.2006.09.008, PII S0005273606003518
    • Dong, C., Filipeanu, C.M., Duvernay, M.T., and, Wu, G., (2007) Regulation of G protein-coupled receptor export trafficking. Biochim Biophys Acta 1768: 853-870. (Pubitemid 46452538)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.4 , pp. 853-870
    • Dong, C.1    Filipeanu, C.M.2    Duvernay, M.T.3    Wu, G.4
  • 9
    • 24344487961 scopus 로고    scopus 로고
    • The regulatory mechanisms of export trafficking of G protein-coupled receptors
    • DOI 10.1016/j.cellsig.2005.05.020, PII S0898656805001269
    • Duvernay, M.T., Filipeanu, C.M., and, Wu, G., (2005) The regulatory mechanisms of export trafficking of G protein-coupled receptors. Cell Signal 17: 1457-1465. (Pubitemid 41253985)
    • (2005) Cellular Signalling , vol.17 , Issue.12 , pp. 1457-1465
    • Duvernay, M.T.1    Filipeanu, C.M.2    Wu, G.3
  • 10
    • 23244460898 scopus 로고    scopus 로고
    • Unconventional homologous internalization of the angiotensin II type-1 receptor induced by G-protein-independent signals
    • DOI 10.1161/01.HYP.0000172621.68061.22
    • Feng, Y., Ding, Y., Ren, S., Zhou, L., Xu, C., and, Karnik, S., (2005) Unconventional homologous internalization of the angiotensin II type-1 receptor induced by G-protein-independent signals. Hypertension 46: 419-425. (Pubitemid 41099179)
    • (2005) Hypertension , vol.46 , Issue.2 , pp. 419-425
    • Feng, Y.-H.1    Ding, Y.2    Ren, S.3    Zhou, L.4    Xu, C.5    Karnik, S.S.6
  • 11
    • 0035101820 scopus 로고    scopus 로고
    • Evolving concepts in G protein-coupled receptor endocytosis: The role in receptor desensitization and signaling
    • Ferguson, S., (2001) Evolving concepts in G protein-coupled receptor endocytosis: the role in receptor desensitization and signaling. Pharmacol Rev 53: 1-24. (Pubitemid 32173106)
    • (2001) Pharmacological Reviews , vol.53 , Issue.1 , pp. 1-24
    • Ferguson, S.S.G.1
  • 12
    • 0034464742 scopus 로고    scopus 로고
    • Uncovering molecular mechanisms involved in activation of G protein-coupled receptors
    • DOI 10.1210/er.21.1.90
    • Gether, U., (2000) Uncovering molecular mechanisms involved in activation of G protein-coupled receptors. Endocr Rev 21: 90-113. (Pubitemid 32260396)
    • (2000) Endocrine Reviews , vol.21 , Issue.1 , pp. 90-113
    • Gether, U.1
  • 13
    • 79958768993 scopus 로고    scopus 로고
    • Identification of distinct c-terminal domains of the Bombyx adipokinetic hromone receptor that are essential for receptor export, phosphorylation and internalization
    • Huang, H., Deng, X., He, X., Yang, W., Li, G., Shi, Y., et al,. (2011) Identification of distinct c-terminal domains of the Bombyx adipokinetic hromone receptor that are essential for receptor export, phosphorylation and internalization. Cell Signal 23: 1455-1465.
    • (2011) Cell Signal , vol.23 , pp. 1455-1465
    • Huang, H.1    Deng, X.2    He, X.3    Yang, W.4    Li, G.5    Shi, Y.6
  • 14
    • 10944238495 scopus 로고    scopus 로고
    • Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor from the silkmoth, Bombyx mori: Significance of the carboxyl terminus in receptor internalization
    • DOI 10.1074/jbc.M408142200
    • Hull, J.J., Ohnishi, A., Moto, K., Kawasaki, Y., Kurata, R., Suzuki, M.G., et al,. (2004) Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor from the silkmoth, Bombyx mori: significance of the carboxyl terminus in receptor internalization. J Biol Chem 279: 51500-51507. (Pubitemid 40017898)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.49 , pp. 51500-51507
    • Hull, J.J.1    Ohnishi, A.2    Moto, K.3    Kawasaki, Y.4    Kurata, R.5    Suzuki, M.G.6    Matsumoto, S.7
  • 15
    • 22144446834 scopus 로고    scopus 로고
    • Regulatory mechanisms underlying pheromone biosynthesis activating neuropeptide (PBAN)-induced internalization of the Bombyx mori PBAN receptor
    • DOI 10.1016/j.bbrc.2005.06.050, PII S0006291X05012751
    • Hull, J.J., Ohnishi, A., and, Matsumoto, S., (2005) Regulatory mechanisms underlying pheromone biosynthesis activating neuropeptide (PBAN)-induced internalization of the Bombyx mori PBAN receptor. Biochem Biophys Res Commun 334: 69-78. (Pubitemid 40978508)
    • (2005) Biochemical and Biophysical Research Communications , vol.334 , Issue.1 , pp. 69-78
    • Hull, J.J.1    Ohnishi, A.2    Matsumoto, S.3
  • 16
    • 71449115743 scopus 로고    scopus 로고
    • Bombyx mori homologs of STIM1 and Orai1 are essential components of the signal transduction cascade that regulates sex pheromone production
    • Hull, J.J., Lee, J.M., Kajigaya, R., and, Matsumoto, S., (2009) Bombyx mori homologs of STIM1 and Orai1 are essential components of the signal transduction cascade that regulates sex pheromone production. J Biol Chem 284: 31200-31213.
    • (2009) J Biol Chem , vol.284 , pp. 31200-31213
    • Hull, J.J.1    Lee, J.M.2    Kajigaya, R.3    Matsumoto, S.4
  • 17
    • 77954329194 scopus 로고    scopus 로고
    • Gqalpha-linked phospholipase Cbeta1 and phospholipase Cgamma are essential components of the pheromone biosynthesis activating neuropeptide (PBAN) signal transduction cascade
    • Hull, J.J., Lee, J.M., and, Matsumoto, S., (2010) Gqalpha-linked phospholipase Cbeta1 and phospholipase Cgamma are essential components of the pheromone biosynthesis activating neuropeptide (PBAN) signal transduction cascade. Insect Mol Biol 19: 553-566.
    • (2010) Insect Mol Biol , vol.19 , pp. 553-566
    • Hull, J.J.1    Lee, J.M.2    Matsumoto, S.3
  • 18
    • 1642487716 scopus 로고    scopus 로고
    • Identification and functional analysis of Hyphantria cunea nucleopolyhedrovirus iap genes
    • DOI 10.1016/j.virol.2004.01.002, PII S0042682204000224
    • Ikeda, M., Yanagimoto, K., and, Kobayashi, M., (2004) Identification and functional analysis of Hyphantria cunea nucleopolyhedrovirus iap genes. Virology 321: 359-371. (Pubitemid 38406049)
    • (2004) Virology , vol.321 , Issue.2 , pp. 359-371
    • Ikeda, M.1    Yanagimoto, K.2    Kobayashi, M.3
  • 19
    • 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
    • Jurenka, R., and, Nusawardani, T., (2011) 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 20: 323-334.
    • (2011) Insect Mol Biol , vol.20 , pp. 323-334
    • Jurenka, R.1    Nusawardani, T.2
  • 20
    • 84990442860 scopus 로고
    • Control of the pheromone biosynthetic pathway in Helicoverpa zea by the pheromone biosynthesis activating neuropeptide (PBAN)
    • Jurenka, R.A., Jacquin, E., and, Roelofs, W.L., (1991a) Control of the pheromone biosynthetic pathway in Helicoverpa zea by the pheromone biosynthesis activating neuropeptide (PBAN). Arch Insect Biochem Physiol 17: 81-91.
    • (1991) Arch Insect Biochem Physiol , vol.17 , pp. 81-91
    • Jurenka, R.A.1    Jacquin, E.2    Roelofs, W.L.3
  • 22
    • 40349114499 scopus 로고    scopus 로고
    • Agonist-selective mechanisms of GPCR desensitization
    • DOI 10.1038/sj.bjp.0707604, PII 0707604
    • Kelly, E., Bailey, C.P., and, Henderson, G., (2008) Agonist-selective mechanisms of GPCR desensitization. Br J Pharmacol 153: S379-S388. (Pubitemid 351340999)
    • (2008) British Journal of Pharmacology , vol.153 , Issue.SUPPL. 1
    • Kelly, E.1    Bailey, C.P.2    Henderson, G.3
  • 23
    • 39149130300 scopus 로고    scopus 로고
    • The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: Identification, functional expression, and structure-activity relationships of ligand analogs
    • Kim, Y.J., Nachman, R.J., Aimanova, K., Gill, S., and, Adams, M.E., (2008) The pheromone biosynthesis activating neuropeptide (PBAN) receptor of Heliothis virescens: identification, functional expression, and structure-activity relationships of ligand analogs. Peptides 29: 268-275.
    • (2008) Peptides , vol.29 , pp. 268-275
    • Kim, Y.J.1    Nachman, R.J.2    Aimanova, K.3    Gill, S.4    Adams, M.E.5
  • 24
    • 79251644004 scopus 로고    scopus 로고
    • Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor
    • Kleinau, G., Jaeschke, H., Worth, C., Mueller, S., Gonzalez, J., Paschke, R., et al,. (2010) Principles and determinants of G-protein coupling by the rhodopsin-like thyrotropin receptor. PLoS ONE 5: e9745.
    • (2010) PLoS ONE , vol.5
    • Kleinau, G.1    Jaeschke, H.2    Worth, C.3    Mueller, S.4    Gonzalez, J.5    Paschke, R.6
  • 25
    • 3042798261 scopus 로고    scopus 로고
    • Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: Molecular modeling and mutagenesis approaches to receptor structure and function
    • DOI 10.1016/j.pharmthera.2004.05.002, PII S0163725804000695
    • Kristiansen, K., (2004) Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol Ther 103: 21-80. (Pubitemid 38891912)
    • (2004) Pharmacology and Therapeutics , vol.103 , Issue.1 , pp. 21-80
    • Kristiansen, K.1
  • 26
    • 79952186617 scopus 로고    scopus 로고
    • RNA interference of pheromone biosynthesis-activating neuropeptide receptor suppresses mating behavior by inhibiting sex pheromone production in Plutella xylostella (L.)
    • Lee, D.W., Shrestha, S., Kim, A.Y., Park, S.J., Yang, C.Y., Kim, Y., and, Koh, Y.H., (2011) RNA interference of pheromone biosynthesis-activating neuropeptide receptor suppresses mating behavior by inhibiting sex pheromone production in Plutella xylostella (L.). Insect Biochem Mol Biol 41: 236-243.
    • (2011) Insect Biochem Mol Biol , vol.41 , pp. 236-243
    • Lee, D.W.1    Shrestha, S.2    Kim, A.Y.3    Park, S.J.4    Yang, C.Y.5    Kim, Y.6    Koh, Y.H.7
  • 27
    • 70350512023 scopus 로고    scopus 로고
    • Alternative splicing of G protein-coupled receptors: Physiology and pathophysiology
    • Markovic, D., and, Challiss, R.A.J., (2009) Alternative splicing of G protein-coupled receptors: physiology and pathophysiology. Cell Mol Life Sci 66: 3337-3352.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3337-3352
    • Markovic, D.1    Challiss, R.A.J.2
  • 28
    • 0029262493 scopus 로고
    • Intracellular transduction in the regulation of pheromone biosynthesis of the silkworm, Bombyx mori: Suggested involvement of calmodulin and phosphoprotein phosphatase
    • Matsumoto, S., Ozawa, R., Nagamine, T., Kim, G.-H., Uchiumi, K., Shono, T., et al,. (1995) Intracellular transduction in the regulation of pheromone biosynthesis of the silkworm, Bombyx mori: suggested involvement of calmodulin and phosphoprotein phosphatase. Biosci Biotechnol Biochem 59: 560-562.
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 560-562
    • Matsumoto, S.1    Ozawa, R.2    Nagamine, T.3    Kim, G.-H.4    Uchiumi, K.5    Shono, T.6
  • 29
    • 0036837103 scopus 로고    scopus 로고
    • Chemical characterization of cytoplasmic lipid droplets in the pheromone-producing cells of the silkmoth, Bombyx mori
    • Matsumoto, S., Fonagy, A., Yamamoto, M., Wang, F., Yokoyama, N., Esumi, Y., et al,. (2002) Chemical characterization of cytoplasmic lipid droplets in the pheromone-producing cells of the silkmoth, Bombyx mori. Insect Biochem Mol Biol 32: 1447-1455.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1447-1455
    • Matsumoto, S.1    Fonagy, A.2    Yamamoto, M.3    Wang, F.4    Yokoyama, N.5    Esumi, Y.6
  • 30
    • 0001229722 scopus 로고    scopus 로고
    • Splice variants of G protein-coupled receptors
    • Minneman, K.P., (2001) Splice variants of G protein-coupled receptors. Mol Interv 1: 108-116.
    • (2001) Mol Interv , vol.1 , pp. 108-116
    • Minneman, K.P.1
  • 31
    • 33645218195 scopus 로고    scopus 로고
    • Targeted disruption of genes in the Bombyx mori sex pheromone biosynthetic pathway
    • Ohnishi, A., Hull, J.J., and, Matsumoto, S., (2006) Targeted disruption of genes in the Bombyx mori sex pheromone biosynthetic pathway. Proc Natl Acad Sci USA 103: 4398-4403.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4398-4403
    • Ohnishi, A.1    Hull, J.J.2    Matsumoto, S.3
  • 32
    • 79959866727 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent protein kinase II (CaMKII)-mediated phosphorylation of the insect PAT family protein Bombyx mori lipid storage droplet protein-1 (BmLsd1)
    • 2+/calmodulin-dependent protein kinase II (CaMKII)-mediated phosphorylation of the insect PAT family protein Bombyx mori lipid storage droplet protein-1 (BmLsd1). J Biol Chem 286: 24101-24112.
    • (2011) J Biol Chem , vol.286 , pp. 24101-24112
    • Ohnishi, A.1    Hull, J.J.2    Kaji, M.3    Hashimoto, K.4    Lee, J.M.5    Tsuneizumi, K.6
  • 33
    • 0034651539 scopus 로고    scopus 로고
    • Multiple pathways control protein kinase C phosphorylation
    • Parekh, D.B., Ziegler, W., and, Parker, P.J., (2000) Multiple pathways control protein kinase C phosphorylation. EMBO J 19: 496-503. (Pubitemid 30093722)
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 496-503
    • Parekh, D.B.1    Ziegler, W.2    Parker, P.J.3
  • 34
    • 65049087685 scopus 로고    scopus 로고
    • Pheromone biosynthesis activating neuropeptide (PBAN): Regulatory role and mode of action
    • Rafaeli, A., (2009) Pheromone biosynthesis activating neuropeptide (PBAN): regulatory role and mode of action. Gen Comp Endocrinol 162: 69-78.
    • (2009) Gen Comp Endocrinol , vol.162 , pp. 69-78
    • Rafaeli, A.1
  • 35
    • 0030240464 scopus 로고    scopus 로고
    • Down regulation of pheromone biosynthesis: Cellular mechanisms of pheromonostatic responses
    • DOI 10.1016/S0965-1748(96)00029-X, PII S096517489600029X
    • Rafaeli, A., and, Gileadi, C., (1996) Down regulation of pheromone biosynthesis: cellular mechanisms of pheromonostatic responses. Insect Biochem Mol Biol 26: 797-807. (Pubitemid 27091744)
    • (1996) Insect Biochemistry and Molecular Biology , vol.26 , Issue.8-9 , pp. 797-807
    • Rafaeli, A.1    Gileadi, C.2
  • 36
    • 34248353417 scopus 로고    scopus 로고
    • Spatial distribution and differential expression of the PBAN receptor in tissues of adult Helicoverpa spp. (Lepidoptera: Noctuidae)
    • DOI 10.1111/j.1365-2583.2007.00725.x
    • Rafaeli, A., Bober, R., Becker, L., Choi, M.Y., Fuerst, E.J., and, Jurenka, R., (2007) Spatial distribution and differential expression of the PBAN receptor in tissues of adult Helicoverpa spp. (Lepidoptera: Noctuidae). Insect Mol Biol 16: 287-293. (Pubitemid 46733763)
    • (2007) Insect Molecular Biology , vol.16 , Issue.3 , pp. 287-293
    • Rafaeli, A.1    Bober, R.2    Becker, L.3    Choi, M.-Y.4    Fuerst, E.-J.5    Jurenka, R.6
  • 38
    • 0029136890 scopus 로고
    • Multi-signal transduction of the pheromonotropic response by pheromone gland incubations of Helicoverpa armigera
    • Soroker, V., and, Rafaeli, A., (1995) Multi-signal transduction of the pheromonotropic response by pheromone gland incubations of Helicoverpa armigera. Insect Biochem Mol Biol 25: 1-9.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 1-9
    • Soroker, V.1    Rafaeli, A.2
  • 39
    • 72849107561 scopus 로고    scopus 로고
    • The role of rhodopsin glycosylation in protein folding, trafficking, and light-sensitive retinal degeneration
    • Tam, B.M., and, Moritz, O.L., (2009) The role of rhodopsin glycosylation in protein folding, trafficking, and light-sensitive retinal degeneration. J Neurosci 29: 15145-15154.
    • (2009) J Neurosci , vol.29 , pp. 15145-15154
    • Tam, B.M.1    Moritz, O.L.2
  • 41
    • 47849101639 scopus 로고    scopus 로고
    • Location, location, location. site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling
    • Tobin, A.B., Butcher, A.J., and, Kong, K.C., (2008) Location, location, location. site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling. Trends Pharmacol Sci 29: 413-420.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 413-420
    • Tobin, A.B.1    Butcher, A.J.2    Kong, K.C.3
  • 43
    • 10744231506 scopus 로고    scopus 로고
    • Characterization and transcriptional profiles of three Spodoptera frugiperda genes encoding cysteine-rich peptides. A new class of defensin-like genes from lepidopteran insects?
    • DOI 10.1016/S0378-1119(03)00789-3
    • Volkoff, A.N., Rocher, J., d'Alençon, E., Bouton, M., Landais, I., Quesada-Moraga, E., et al,. (2003) Characterization and transcriptional profiles of three Spodoptera frugiperda genes encoding cystein-rich peptides. A new class of defensin-like genes from lepidopteran insects? Gene 319: 43-53. (Pubitemid 37346199)
    • (2003) Gene , vol.319 , Issue.1-2 , pp. 43-53
    • Volkoff, A.-N.1    Rocher, J.2    D'Alencon, E.3    Bouton, M.4    Landais, I.5    Quesada-Moraga, E.6    Vey, A.7    Fournier, P.8    Mita, K.9    Devauchelle, G.10
  • 44
    • 2642703472 scopus 로고    scopus 로고
    • Deletions in the third intracellular loop of the thyrotropin receptor
    • Wonerow, P., Schöneberg, T., Schultz, G., Gudermann, T., and, Paschke, R., (1998) Deletions in the third intracellular loop of the thyrotropin receptor. J Biol Chem 273: 7900-7905.
    • (1998) J Biol Chem , vol.273 , pp. 7900-7905
    • Wonerow, P.1    Schöneberg, T.2    Schultz, G.3    Gudermann, T.4    Paschke, R.5
  • 45
    • 0037762755 scopus 로고    scopus 로고
    • G protein selectivity is regulated by multiple intracellular regions of GPCRs
    • DOI 10.1159/000068914
    • Wong, S.K., (2003) G protein selectivity is regulated by multiple intracellular regions of GPCRs. Neurosignals 12: 1-12. (Pubitemid 37490488)
    • (2003) NeuroSignals , vol.12 , Issue.1 , pp. 1-12
    • Wong, S.K.-F.1
  • 46
    • 0031718841 scopus 로고    scopus 로고
    • A modified overlap extension PCR method to create chimeric genes in the absence of restriction enzymes
    • DOI 10.1023/A:1008848517221
    • Wurch, T., Lestienne, F., and, Pauwels, P., (1998) A modified overlap extension PCR method to create chimeric genes in the absence of restriction enzymes. Biotech Tech 12: 653-657. (Pubitemid 28456279)
    • (1998) Biotechnology Techniques , vol.12 , Issue.9 , pp. 653-657
    • Wurch, T.1    Lestienne, F.2    Pauwels, P.J.3
  • 47
    • 0036219208 scopus 로고    scopus 로고
    • q coupling specificity
    • DOI 10.1210/me.16.4.814
    • Yang, M., Wang, W., Zhong, M., Philippi, A., Lichtarge, O., and, Sanborn, B.M., (2002) Lysine 270 in the third intracellular domain of the oxytocin receptor is an important determinant for G alpha(q) coupling specificity. Mol Endocrinol 16: 814-823. (Pubitemid 34297749)
    • (2002) Molecular Endocrinology , vol.16 , Issue.4 , pp. 814-823
    • Yang, M.1    Wang, W.2    Zhong, M.3    Philippi, A.4    Lichtarge, O.5    Sanborn, B.M.6
  • 48
    • 34047265151 scopus 로고    scopus 로고
    • Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae
    • DOI 10.1016/j.gene.2006.12.025, PII S0378111907000121
    • Zheng, L., Lytle, C., Njauw, C.N., Altstein, M., and, Martins-Green, M., (2007) Cloning and characterization of the pheromone biosynthesis activating neuropeptide receptor gene in Spodoptera littoralis larvae. Gene 393: 20-30. (Pubitemid 46551523)
    • (2007) Gene , vol.393 , Issue.1-2 , pp. 20-30
    • Zheng, L.1    Lytle, C.2    Njauw, C.-n.3    Altstein, M.4    Martins-Green, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.