메뉴 건너뛰기




Volumn 6, Issue MAR, 2015, Pages

Structures a nd functions of insect arylalkylamine N acetyltransferase (iaaNAT); a key enzyme for physiological and behavioral switch in arthropods

Author keywords

Arylalkylamine N acetyl transferase (aaNAT); Arylamine N acetyltransferase; Circadian rhythms; Melatonin (MEL); Photoperiodism; Serotonin (5HT); UV adaptation

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); ARALKYLAMINE ACETYLTRANSFERASE; MELATONIN; REACTIVE OXYGEN METABOLITE;

EID: 84926468796     PISSN: None     EISSN: 1664042X     Source Type: Journal    
DOI: 10.3389/fphys.2015.00113     Document Type: Article
Times cited : (38)

References (143)
  • 1
    • 33746519078 scopus 로고    scopus 로고
    • Melatonin in Glycyrrhiza uralensis: response of plant roots to spectral quality of light and UV-B radiation
    • Afreen, F., Zobayed, S.M.A., and Kozai, T. (2006). Melatonin in Glycyrrhiza uralensis: response of plant roots to spectral quality of light and UV-B radiation. J Pineal Res 41, 108-115. doi:10.1111/j.1600-079X.2006.00337.x
    • (2006) J Pineal Res , vol.41 , pp. 108-115
    • Afreen, F.1    Zobayed, S.M.A.2    Kozai, T.3
  • 2
    • 67949085047 scopus 로고    scopus 로고
    • Day-night and depth differences in haemolymph melatonin of the Norway lobster, Nephrops norvegicus (L.)
    • Aguzzi, J., Sanchez-Pardo, J., Garcia, J.A., and Sarda, F. (2009) Day-night and depth differences in haemolymph melatonin of the Norway lobster, Nephrops norvegicus (L.). Deep-Sea Research I 56, 1894-1905. doi: 10.1016/j.dsr.2009.06.001
    • (2009) Deep-Sea Research I , vol.56 , pp. 1894-1905
    • Aguzzi, J.1    Sanchez-Pardo, J.2    Garcia, J.A.3    Sarda, F.4
  • 3
    • 0031492901 scopus 로고    scopus 로고
    • Cholinergic and serotonergic control of prothoracic hormonr release during the pupal stage of the silkworm, Bombyx mori (Lepidoptera: Bombicidae)
    • Aizono, Y., Yamada, T., Hirooka, K., Takeda, M., Shirai, Y., and Matsubara, F. (1997). Cholinergic and serotonergic control of prothoracic hormonr release during the pupal stage of the silkworm, Bombyx mori (Lepidoptera: Bombicidae). App Entomol Zool 32, 508-511.
    • (1997) App Entomol Zool , vol.32 , pp. 508-511
    • Aizono, Y.1    Yamada, T.2    Hirooka, K.3    Takeda, M.4    Shirai, Y.5    Matsubara, F.6
  • 4
    • 34247151073 scopus 로고    scopus 로고
    • Melatonin: therapeutic and clinical utilization
    • Altun, A., and Ugur-Altun, B. (2007). Melatonin: therapeutic and clinical utilization. Int J Clin Pract 61(5), 835-845. doi: 10.1111/j.1742-1241.2006.01191.x
    • (2007) Int J Clin Pract , vol.61 , Issue.5 , pp. 835-845
    • Altun, A.1    Ugur-Altun, B.2
  • 5
    • 0033646107 scopus 로고    scopus 로고
    • Purification, cloning and characterization of a second arylalkylamine N acetyltransferase from Drosophila melanogaster
    • Amherd R., Hintermann, E., Walz D., AVolter, M., and Meyer, U.A. (2000). Purification, cloning and characterization of a second arylalkylamine N acetyltransferase from Drosophila melanogaster. DNA Cell Biol 19, 697-705. doi: 10.1089/10445490050199081.
    • (2000) DNA Cell Biol , vol.19 , pp. 697-705
    • Amherd, R.1    Hintermann, E.2    Walz, D.3    A.Volter, M.4    Meyer, U.A.5
  • 6
    • 0032395612 scopus 로고    scopus 로고
    • Characterization and kinetic analysis of indolamine N-acetyltransferase from the collaterial glands of the American cockroach, Periplaneta americana
    • Asano, H, and Takeda, M. (1998). Characterization and kinetic analysis of indolamine N-acetyltransferase from the collaterial glands of the American cockroach, Periplaneta americana. Appl Entomol Zool 33, 127-132.
    • (1998) Appl Entomol Zool , vol.33 , pp. 127-132
    • Asano, H.1    Takeda, M.2
  • 7
    • 0038278664 scopus 로고    scopus 로고
    • Multiple forms of arylalkylamine N acetyltransferase (NAT) from cockroach female colleterial glands and activity changes during oocyte maturation
    • Asano, H., Bembenek, J., and Takeda, M. (2003). Multiple forms of arylalkylamine N acetyltransferase (NAT) from cockroach female colleterial glands and activity changes during oocyte maturation. Comp Biochem Physiol A 134, 795-803. doi: 10.1016/S1095-6433(03)00013-8
    • (2003) Comp Biochem Physiol A , vol.134 , pp. 795-803
    • Asano, H.1    Bembenek, J.2    Takeda, M.3
  • 8
    • 0016256663 scopus 로고
    • The pineal gland: a neurochemical transducer
    • Axelrod, J. (1974). The pineal gland: a neurochemical transducer. Science 184, 1341- 1348. doi: 10.1126/science.184.4144.1341
    • (1974) Science , vol.184 , pp. 1341-1348
    • Axelrod, J.1
  • 10
    • 0030903999 scopus 로고    scopus 로고
    • The rat arylalkylamine N acetyltransferase gene promoter cAMP activation via a cAMP-responsive element-CCAAT complex
    • Baler, R., Covington, S., and Klein, D.C. (1997). The rat arylalkylamine N acetyltransferase gene promoter cAMP activation via a cAMP-responsive element-CCAAT complex. J Biol Chem 272, 6979-6985. 10.1074/jbc.272.11.6979
    • (1997) J Biol Chem , vol.272 , pp. 6979-6985
    • Baler, R.1    Covington, S.2    Klein, D.C.3
  • 11
    • 84887467996 scopus 로고    scopus 로고
    • Identification, characterization and analysis of expression of genes encoding arylalkylamine N-acetyltransferases in the pea aphid Acyrthosiphon pisum
    • Barberà, M., Mengual, B., Collantes-Alegre, J.M., Cortés, T., González, A., and Martínez-Torres, D. (2013). Identification, characterization and analysis of expression of genes encoding arylalkylamine N-acetyltransferases in the pea aphid Acyrthosiphon pisum. Insect Mol Biol 22(6), 623-634. doi: 10.1111/imb.12050
    • (2013) Insect Mol Biol , vol.22 , Issue.6 , pp. 623-634
    • Barberà, M.1    Mengual, B.2    Collantes-Alegre, J.M.3    Cortés, T.4    González, A.5    Martínez-Torres, D.6
  • 13
    • 84926440225 scopus 로고    scopus 로고
    • Melatonin and N acetyltransferase in the cockroach Periplaneta americana, their relevance to circadian clock
    • eds. T. Oishi, K. Tsutsui, S. Tanaka and S. Kikuyama
    • Bembenek, J., Ichihara, N., Sakamoto, K., and Takeda, M. (2004). Melatonin and N acetyltransferase in the cockroach Periplaneta americana, their relevance to circadian clock, in Trend Comp Endo Crinol, eds. T. Oishi, K. Tsutsui, S. Tanaka and S. Kikuyama. 80-81.
    • (2004) Trend Comp Endo Crinol , pp. 80-81
    • Bembenek, J.1    Ichihara, N.2    Sakamoto, K.3    Takeda, M.4
  • 14
    • 11144340878 scopus 로고    scopus 로고
    • Day/night fluctuation in melatonin content, arylalkylamine N-acetyltransferase activity and nat mRNA expression in the CNS, peripheral tissues and hemolymph of the cockroach, Periplaneta americana
    • Bembenek, J., Sehadova, H., Ichihara, N., and Takeda, M. (2005a). Day/night fluctuation in melatonin content, arylalkylamine N-acetyltransferase activity and nat mRNA expression in the CNS, peripheral tissues and hemolymph of the cockroach, Periplaneta americana. Comp Biochem Physiol B 140, 27-36. 10.1016/j.cbpc.2004.03.017
    • (2005) Comp Biochem Physiol B , vol.140 , pp. 27-36
    • Bembenek, J.1    Sehadova, H.2    Ichihara, N.3    Takeda, M.4
  • 15
    • 24044499680 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA encoding arylalkylamine N-acetyltransferase from the testicular system of Periplaneta american: Primary protein structure and expression analysis
    • Bembenek, J., Sakamoto, K., and Takeda, M. (2005b). Molecular cloning of a cDNA encoding arylalkylamine N-acetyltransferase from the testicular system of Periplaneta american: Primary protein structure and expression analysis. Arch Insect Biochem Physiol 59, 219-229. doi: 10.1002/arch.20070
    • (2005) Arch Insect Biochem Physiol , vol.59 , pp. 219-229
    • Bembenek, J.1    Sakamoto, K.2    Takeda, M.3
  • 16
    • 0031020569 scopus 로고    scopus 로고
    • Avian melatonin synthesis: photic and circadian regulation of serotonin N acetyltransferase mRNA in the chicken pineal gland and retina
    • Bernard, M., Iuvone, P.M., Cassone, V.M., Roseboom, P.H., Coon, S.L., and Klein, D.C. (1997). Avian melatonin synthesis: photic and circadian regulation of serotonin N acetyltransferase mRNA in the chicken pineal gland and retina. J Neurochem 68, 1, 213-224. doi: 10.1046/j.1471-4159.1997.68010213.x
    • (1997) J Neurochem , vol.68 , Issue.1 , pp. 213-224
    • Bernard, M.1    Iuvone, P.M.2    Cassone, V.M.3    Roseboom, P.H.4    Coon, S.L.5    Klein, D.C.6
  • 17
    • 0037039865 scopus 로고    scopus 로고
    • Phototransduction by retinal ganglion cells that set the circadian clock
    • Berson, D.M., Dunn, F.A., and Takao, M. (2002). Phototransduction by retinal ganglion cells that set the circadian clock. Science 295, 1070-1073. doi: 10.1126/science.1067262
    • (2002) Science , vol.295 , pp. 1070-1073
    • Berson, D.M.1    Dunn, F.A.2    Takao, M.3
  • 18
    • 34250346126 scopus 로고    scopus 로고
    • A novel photoreaction mechanism for the circadian blue lightphotoreceptor Drosophila cryptochrome
    • Berndt, A., Kottke, T., Breitkreuz, H., Dvorsky, R., Hennig, S., Alexander, M., and Wolf, E. (2007). A novel photoreaction mechanism for the circadian blue lightphotoreceptor Drosophila cryptochrome. J Biol Chem 282, 13011-13021. doi: 10.1074/jbc.M608872200
    • (2007) J Biol Chem , vol.282 , pp. 13011-13021
    • Berndt, A.1    Kottke, T.2    Breitkreuz, H.3    Dvorsky, R.4    Hennig, S.5    Alexander, M.6    Wolf, E.7
  • 19
    • 0030728953 scopus 로고    scopus 로고
    • Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family
    • Blackshaw, S., and Snyder, S.H. (1997). Parapinopsin, a novel catfish opsin localized to the parapineal organ, defines a new gene family. J Neurosci 17, 8083-8092.
    • (1997) J Neurosci , vol.17 , pp. 8083-8092
    • Blackshaw, S.1    Snyder, S.H.2
  • 20
    • 0037381222 scopus 로고    scopus 로고
    • Melatonin and 5-methoxytryptophol (5-ML) in nervous and/or neurosensory structures of a gastropod mollusk (Helix aspersa maxima): synthesis and diurnal rhythms
    • Blanc, A., Vivien-Roels, B., Pevet, P., Attia, J., and Buisson, B. (2003). Melatonin and 5-methoxytryptophol (5-ML) in nervous and/or neurosensory structures of a gastropod mollusk (Helix aspersa maxima): synthesis and diurnal rhythms. Gen Comp Endocrinol 131, 168-175. doi: 10.1016/S0016-6480(03)00008-X
    • (2003) Gen Comp Endocrinol , vol.131 , pp. 168-175
    • Blanc, A.1    Vivien-Roels, B.2    Pevet, P.3    Attia, J.4    Buisson, B.5
  • 21
    • 0029560035 scopus 로고
    • Diurnal variation in mRNA encoding serotonin N-acetyltransferase in pineal gland
    • Borjigin, J., Wang, M.M., and Snyder, S.H. (1995). Diurnal variation in mRNA encoding serotonin N-acetyltransferase in pineal gland. Nature 378(6559), 783- 785. doi:10.1038/378783a0
    • (1995) Nature , vol.378 , Issue.6559 , pp. 783-785
    • Borjigin, J.1    Wang, M.M.2    Snyder, S.H.3
  • 22
    • 51249118269 scopus 로고    scopus 로고
    • Monoamine oxidase inactivation: from pathophysiology to therapeutics
    • 1527-1533
    • Bortolato, M., Chen, K., and Shih, J.C. (2008). Monoamine oxidase inactivation: from pathophysiology to therapeutics. Adv Drug Deliv Rev 60, 13-14, 1527-1533.
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.13-14
    • Bortolato, M.1    Chen, K.2    Shih, J.C.3
  • 23
    • 0035882385 scopus 로고    scopus 로고
    • Action spectrum for melatonin regulation in humans: evidence for a novel circadian photoreceptor
    • Brainard, G.C., Hanifin, J.P., Greeson, J.M., Byrne, B., Glickman, G., Gerner, E., and Rollag, M.D. (2001). Action spectrum for melatonin regulation in humans: evidence for a novel circadian photoreceptor. J Neurosci 21, 6405-6412.
    • (2001) J Neurosci , vol.21 , pp. 6405-6412
    • Brainard, G.C.1    Hanifin, J.P.2    Greeson, J.M.3    Byrne, B.4    Glickman, G.5    Gerner, E.6    Rollag, M.D.7
  • 24
    • 51449101022 scopus 로고    scopus 로고
    • Thirty four years since discovery of gastrointestinal melatonin
    • Bubenik, G.A. (2008). Thirty four years since discovery of gastrointestinal melatonin. J Physiol Pharmacol Suppl 2, 33-51. doi:10.1016/j.addr.2008.06.002
    • (2008) J Physiol Pharmacol Suppl , vol.2 , pp. 33-51
    • Bubenik, G.A.1
  • 25
    • 84885678865 scopus 로고    scopus 로고
    • Molecular cloning and functional analysis of serotonin N-acetyltransferase from the cyanobacterium Synechocystis s
    • Byeon, Y., Lee, K., Park, Y.I., Park, S., and Back, K. (2013). Molecular cloning and functional analysis of serotonin N-acetyltransferase from the cyanobacterium Synechocystis sp. PCC 6803. J Pineal Res 55, 371-376. doi: 10.1111/jpi.12080
    • (2013) PCC 6803. J Pineal Res , vol.55 , pp. 371-376
    • Byeon, Y.1    Lee, K.2    Park, Y.I.3    Park, S.4    Back, K.5
  • 26
    • 84890117208 scopus 로고    scopus 로고
    • Cellular localization and kinetics of the rice melatonin biosynthetic enzymes SNAT and ASMT
    • Byeon, Y., Lee, H.Y., Lee, K., Park, S., and Back, K. (2014). Cellular localization and kinetics of the rice melatonin biosynthetic enzymes SNAT and ASMT. J Pineal Res 56, 107-114. doi: 10.1111/jpi.12103
    • (2014) J Pineal Res , vol.56 , pp. 107-114
    • Byeon, Y.1    Lee, H.Y.2    Lee, K.3    Park, S.4    Back, K.5
  • 27
    • 84857358236 scopus 로고    scopus 로고
    • Malatonin: Neuritogenesis and neuroprotective effects in crustacean x organ cells
    • Cary, G.A., Cuttler, A.S., Duda, K.A., Kusema, T., Myers, J.A., and Tilden, A.R. (2012), Malatonin: Neuritogenesis and neuroprotective effects in crustacean x organ cells. Comp Biochem Physiol A 161, 355-360. doi: 10.1016/j.cbpa.2011.12.005
    • (2012) Comp Biochem Physiol A , vol.161 , pp. 355-360
    • Cary, G.A.1    Cuttler, A.S.2    Duda, K.A.3    Kusema, T.4    Myers, J.A.5    Tilden, A.R.6
  • 28
    • 0034693265 scopus 로고    scopus 로고
    • Characterization of the chicken serotonin N-acetyltransferase gene. Activation via clock gene heterodimers/E box interaction
    • Chong, N.W., Bernard, M., and Klein, D.C. (2000). Characterization of the chicken serotonin N-acetyltransferase gene. Activation via clock gene heterodimers/E box interaction. J Biol Chem 275, 32991-32998. doi: 10.1074/jbc.M005671200
    • (2000) J Biol Chem , vol.275 , pp. 32991-32998
    • Chong, N.W.1    Bernard, M.2    Klein, D.C.3
  • 29
    • 0029593545 scopus 로고
    • Pineal serotonin N-acetyltransferase; Expression cloning and molecular analysis
    • Coon, S.L., Roseboom, P.H., Baker, R., Weller, J.L., Namboodiri, M.A.A., Koonin, E.V., and Klein D.C. (1995). Pineal serotonin N-acetyltransferase; Expression cloning and molecular analysis. Science 270, 1681-1683. doi: 1126/science.270.5242.1681
    • (1995) Science , vol.270 , pp. 1681-1683
    • Coon, S.L.1    Roseboom, P.H.2    Baker, R.3    Weller, J.L.4    Namboodiri, M.A.A.5    Koonin, E.V.6    Klein, D.C.7
  • 30
    • 33646695203 scopus 로고    scopus 로고
    • Evolution of arylalkylamine N-acetyltransferase: Emergence and divergence
    • Coon, S.L., and Klein, D.C. (2006). Evolution of arylalkylamine N-acetyltransferase: Emergence and divergence. Mol Cell Endocrinol 252, 2-10. doi: 10.1016/j.mce.2006.03.039
    • (2006) Mol Cell Endocrinol , vol.252 , pp. 2-10
    • Coon, S.L.1    Klein, D.C.2
  • 31
    • 77953523384 scopus 로고    scopus 로고
    • Mutations of an arylalkylamine-N-acetyltransferase, Bm-iAANAT, are responsible for silkworm melanism mutant
    • Dai, F.Y., Qiao, L., Tong, X.L., Cao, C., Chen, P., Chen, J., Lu, C., and Xiang, Z.H. (2010). Mutations of an arylalkylamine-N-acetyltransferase, Bm-iAANAT, are responsible for silkworm melanism mutant. J Biol Chem 285(25), 19553-19560. doi: 10.1074/jbc.M109.096743
    • (2010) J Biol Chem , vol.285 , Issue.25 , pp. 19553-19560
    • Dai, F.Y.1    Qiao, L.2    Tong, X.L.3    Cao, C.4    Chen, P.5    Chen, J.6    Lu, C.7    Xiang, Z.H.8
  • 32
    • 0015426630 scopus 로고
    • Sensitive assay for serotonin N-acetyltransferase activity in rat pineal
    • Deguchi, T., and Axelrod, J. (1972). Sensitive assay for serotonin N-acetyltransferase activity in rat pineal. Anal Biochem 50, 174-179. doi: 10.1016/0003- 2697(72)90496-4
    • (1972) Anal Biochem , vol.50 , pp. 174-179
    • Deguchi, T.1    Axelrod, J.2
  • 33
    • 0015397131 scopus 로고
    • Control of circadian change of serotonin N acetyltransferase activity in the pineal organ by the β-adrenergic receptor
    • Deguchi, T., and Axelrod, J. (1972b). Control of circadian change of serotonin N acetyltransferase activity in the pineal organ by the β-adrenergic receptor. Proc Natl Acad Sci U S A. 69, 2547-2550. doi: 10.1038/290706a0
    • (1972) Proc Natl Acad Sci U S A , vol.69 , pp. 2547-2550
    • Deguchi, T.1    Axelrod, J.2
  • 34
    • 0019408647 scopus 로고
    • Rhodopsin-like photosensitivity of isolated chicken pineal gland
    • Deguchi, T. (1981). Rhodopsin-like photosensitivity of isolated chicken pineal gland. Nature 290, 706-707.
    • (1981) Nature , vol.290 , pp. 706-707
    • Deguchi, T.1
  • 35
    • 0026713308 scopus 로고
    • Sequences and expression of alleles of polymorphic arylamine N acetyltransferase of human liver
    • Deguchi, T. (1992). Sequences and expression of alleles of polymorphic arylamine N acetyltransferase of human liver. J Biol Chem 267, 18140-18147.
    • (1992) J Biol Chem , vol.267 , pp. 18140-18147
    • Deguchi, T.1
  • 37
    • 0034781648 scopus 로고    scopus 로고
    • Melatonin synthesis in the rat hardelian gland:age-and time related effect
    • Dieridane, Y., and Touitou, Y. (2001). Melatonin synthesis in the rat hardelian gland:age-and time related effect. Exp Eye Res 72, 487-92. doi: 10.1006/exer.2000.0973
    • (2001) Exp Eye Res , vol.72 , pp. 487-492
    • Dieridane, Y.1    Touitou, Y.2
  • 38
    • 0033877252 scopus 로고    scopus 로고
    • GCN5-related N-acetyltransferases: a structural overview
    • Dyda, F., Klein, D.C., and Hickman, A.B. (2000). GCN5-related N-acetyltransferases: a structural overview. Annu Rev Biophys Biomol Struct 29, 81-103. doi: 10.1146/annurev.biophys.29.1.81
    • (2000) Annu Rev Biophys Biomol Struct , vol.29 , pp. 81-103
    • Dyda, F.1    Klein, D.C.2    Hickman, A.B.3
  • 39
    • 0025880699 scopus 로고
    • Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases
    • Ebisawa, T., and Deguchi, T. (1991) Structure and restriction fragment length polymorphism of genes for human liver arylamine N-acetyltransferases. Biochem Biophys Res Commun 177, 1252-1257. doi: 10.1016/0006-291X(91)90676-X
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 1252-1257
    • Ebisawa, T.1    Deguchi, T.2
  • 40
    • 0032956319 scopus 로고    scopus 로고
    • Cellular circadian clocks in the pineal
    • Falcón, J. (1999). Cellular circadian clocks in the pineal. Prog Neurobiol 58, 121-162. doi: 10.1016/S0301-0082(98)00078-1
    • (1999) Prog Neurobiol , vol.58 , pp. 121-162
    • Falcón, J.1
  • 42
    • 34548280761 scopus 로고    scopus 로고
    • Circadian vision
    • Foster, R.G., and Hankins, M.W. (2007). Circadian vision. Curr Biol 17, R746-R751. doi: 10.1016/j.cub.2007.07.007
    • (2007) Curr Biol , vol.17 , pp. R746-R751
    • Foster, R.G.1    Hankins, M.W.2
  • 43
    • 79960380554 scopus 로고    scopus 로고
    • Melatonin as a natural ally against oxidative stress: a physicochemical examination
    • Galano, A., Tan, D.X., and Reiter, R.J. (2011). Melatonin as a natural ally against oxidative stress: a physicochemical examination. J Pineal Res 51, 1-16. doi: 10.1111/j.1600-079X.2011.00916.x
    • (2011) J Pineal Res , vol.51 , pp. 1-16
    • Galano, A.1    Tan, D.X.2    Reiter, R.J.3
  • 45
    • 0035861575 scopus 로고    scopus 로고
    • Characterization of the Saccharomyces cerevisiae Homolog of the melatonin rhythm enzyme arylalkylamine N-acetyltransferease (EC 2.3.1.87)
    • Ganguly, S., Mummanenit, P., Steinbach, P.J., Klein, D.C., and Coon, S.L. (2001). Characterization of the Saccharomyces cerevisiae Homolog of the melatonin rhythm enzyme arylalkylamine N-acetyltransferease (EC 2.3.1.87). J Biol Chemi 276, 47239-47247. doi: 10.1074/jbc.M107222200
    • (2001) J Biol Chemi , vol.276 , pp. 47239-47247
    • Ganguly, S.1    Mummanenit, P.2    Steinbach, P.J.3    Klein, D.C.4    Coon, S.L.5
  • 46
    • 0035991396 scopus 로고    scopus 로고
    • Control of melatonin synthesis in the mammalian pineal gland: the critical role of serotonin acetylation
    • Ganguly, S., Coon, S.L., and Klein, D.C. (2002). Control of melatonin synthesis in the mammalian pineal gland: the critical role of serotonin acetylation. Cell Tissue Res 309(1), 127-137. doi: 10.1007/s00441-002-0579-y
    • (2002) Cell Tissue Res , vol.309 , Issue.1 , pp. 127-137
    • Ganguly, S.1    Coon, S.L.2    Klein, D.C.3
  • 47
    • 77349116153 scopus 로고    scopus 로고
    • Effect of melatonin in the antioxidant defense system in the locomotor muscles of the estuarine crab Neohelice granulata (Decapoda, Brachyura)
    • Geihs, M.A., Vargas, M.A., Maciel, F.E., Caldas, S.S., Cruz, B.P., Primel, E.G., Monserrat, J.M., and Nery, L.E.M. (2010). Effect of melatonin in the antioxidant defense system in the locomotor muscles of the estuarine crab Neohelice granulata (Decapoda, Brachyura), Gen Comp Endocrinol 166, 72-82 doi: 10.1016/j.ygcen.2009.09.018
    • (2010) Gen Comp Endocrinol , vol.166 , pp. 72-82
    • Geihs, M.A.1    Vargas, M.A.2    Maciel, F.E.3    Caldas, S.S.4    Cruz, B.P.5    Primel, E.G.6    Monserrat, J.M.7    Nery, L.E.M.8
  • 48
    • 0033867715 scopus 로고    scopus 로고
    • Cryptochromes: sensory reception, transduction, and clock functions subserving circadian systems
    • Hall, J.C. (2000). Cryptochromes: sensory reception, transduction, and clock functions subserving circadian systems. Curr Opin Neurobiol 10, 456-466. doi: 10.1016/S0959-4388(00)00117-3
    • (2000) Curr Opin Neurobiol , vol.10 , pp. 456-466
    • Hall, J.C.1
  • 49
    • 84863912392 scopus 로고    scopus 로고
    • Evolution of insect arylalkylamine N-acetyltransferases: Structural evidence from the yellow fever mosquito, Aedes aegypti
    • July, 17, 2012
    • Han, Q., Robinson, H., Ding, H., Christensen, B.M., and Li, J. (2012). Evolution of insect arylalkylamine N-acetyltransferases: Structural evidence from the yellow fever mosquito, Aedes aegypti. Proc Natl Acad Sci U S A July 17, 2012, 109(29), 11669-11674. doi: 10.1073/pnas.1206828109
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.29 , pp. 11669-11674
    • Han, Q.1    Robinson, H.2    Ding, H.3    Christensen, B.M.4    Li, J.5
  • 50
    • 38049042773 scopus 로고    scopus 로고
    • Melanopsin: an exciting photopigment
    • Hankins, M.W., Peirson, S.N., and Foster, R.G. (2008). Melanopsin: an exciting photopigment. Trends Neurosci 31, 27-36. doi: 10.1016/j.tins.2007.11.002
    • (2008) Trends Neurosci , vol.31 , pp. 27-36
    • Hankins, M.W.1    Peirson, S.N.2    Foster, R.G.3
  • 51
    • 0037405555 scopus 로고    scopus 로고
    • Non-vertebrate melatonin
    • Hardeland, R., and Poeggeler, B. (2003). Non-vertebrate melatonin. J Pineal Res 34, 233-241. doi: 10.1034/j.1600-079X.2003.00040.x
    • (2003) J Pineal Res , vol.34 , pp. 233-241
    • Hardeland, R.1    Poeggeler, B.2
  • 52
    • 0037039784 scopus 로고    scopus 로고
    • Melanopsin containing retinal ganglion cells: architecture, projections, and intrinsic photosensitivity
    • Hattar, S., Liao, H.W., Takao, M., Berson, D.M., and Yau, K. W. (2002). Melanopsin containing retinal ganglion cells: architecture, projections, and intrinsic photosensitivity. Science 295, 1065-1070. doi: 10.1126/science.1069609
    • (2002) Science , vol.295 , pp. 1065-1070
    • Hattar, S.1    Liao, H.W.2    Takao, M.3    Berson, D.M.4    Yau, K.W.5
  • 53
    • 0036496285 scopus 로고    scopus 로고
    • UV-B-induced formation of reactive oxygen species and oxidative damage of the cyanobacterium Anabaena sp.: protective effects of ascorbic acid and N-acetyl-L-cysteine
    • He Y.Y., and Häder, D.P. (2002). UV-B-induced formation of reactive oxygen species and oxidative damage of the cyanobacterium Anabaena sp.: protective effects of ascorbic acid and N-acetyl-L-cysteine. J Photochem Photobiol B 66, 115-124. doi: 10.1016/S1011-1344(02)00231-2
    • (2002) J Photochem Photobiol B , vol.66 , pp. 115-124
    • He, Y.Y.1    Häder, D.P.2
  • 54
    • 33751381461 scopus 로고    scopus 로고
    • TimeTree: a public knowledge-base of divergence times among organisms
    • Hedges, S.B., Dudley, J., and Kumar, S. (2006). TimeTree: a public knowledge-base of divergence times among organisms. Bioinformatics 22(23), 2971-2972. doi: 10.1093/bioinformatics/btl505
    • (2006) Bioinformatics , vol.22 , Issue.23 , pp. 2971-2972
    • Hedges, S.B.1    Dudley, J.2    Kumar, S.3
  • 55
    • 0028834807 scopus 로고
    • Isolation and characterization of an arylalkylamine N-acetyltransferase from Drosophila melanogaster
    • Hintermann, E., Jeno, P., and Meyer, U.A. (1995) Isolation and characterization of an arylalkylamine N-acetyltransferase from Drosophila melanogaster. FEBS Lett 375, 148-150. doi: 10.1016/0014-5793(95)01198-N
    • (1995) FEBS Lett , vol.375 , pp. 148-150
    • Hintermann, E.1    Jeno, P.2    Meyer, U.A.3
  • 56
    • 0029910010 scopus 로고    scopus 로고
    • Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and gut
    • Hintermann, E., Grieder, N.C., Amherd, R., Brodbeck, D., and Mayer, U.A. (1996). Cloning of an arylalkylamine N-acetyltransferase (aaNAT1) from Drosophila melanogaster expressed in the nervous system and gut. Proc Natl Acad Sci U S A 93, 12315-12320.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 12315-12320
    • Hintermann, E.1    Grieder, N.C.2    Amherd, R.3    Brodbeck, D.4    Mayer, U.A.5
  • 57
    • 77955773370 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of two putative serotonin receptors in the brain of Antheraea pernyi pupa
    • Hiragaki, S., Kawabe, Y., and Takeda, M. (2008). Molecular cloning and expression analysis of two putative serotonin receptors in the brain of Antheraea pernyi pupa. Int J Wild Silkmoth & Silk 13, 1-14.
    • (2008) Int J Wild Silkmoth & Silk , vol.13 , pp. 1-14
    • Hiragaki, S.1    Kawabe, Y.2    Takeda, M.3
  • 58
    • 67651163926 scopus 로고    scopus 로고
    • Putative regulatory mechanism of prothoracicotropic hormone (PTTH) secretion in the American cockroach, Periplaneta americana as inferred from co-locatization of Rab8, PTTH and protein kinase C in neurosectretory cells
    • Hiragaki, S., Uno, T., and Takeda, M. (2009). Putative regulatory mechanism of prothoracicotropic hormone (PTTH) secretion in the American cockroach, Periplaneta americana as inferred from co-locatization of Rab8, PTTH and protein kinase C in neurosectretory cells. Cell Tiss Res 335, 607-615. doi: 10.1007/s00441-008-0747-9
    • (2009) Cell Tiss Res , vol.335 , pp. 607-615
    • Hiragaki, S.1    Uno, T.2    Takeda, M.3
  • 59
    • 0000895721 scopus 로고
    • Pineal grand: Influence on gonads of male hamsters
    • Hoffman, R.A., and Reiter, R.J, (1965). Pineal grand: Influence on gonads of male hamsters. Science 148(3677), 1609-1611. doi: 10.1126/science.148.3677.1609
    • (1965) Science , vol.148 , Issue.3677 , pp. 1609-1611
    • Hoffman, R.A.1    Reiter, R.J.2
  • 60
    • 11944260694 scopus 로고
    • Insect cuticle sclerotization
    • Hopkins, T.L., and Krames, K.J. (1992). Insect cuticle sclerotization. Annu Rev Entomol 37, 273-302. doi: 10.1146/annurev.en.37.010192.001421
    • (1992) Annu Rev Entomol , vol.37 , pp. 273-302
    • Hopkins, T.L.1    Krames, K.J.2
  • 61
    • 11144339327 scopus 로고    scopus 로고
    • Melatonin-induced neuropeptide release from isolated locust corpora cardiaca
    • Huybrechts, J., De Loof, A., and Schoofs, L. (2005). Melatonin-induced neuropeptide release from isolated locust corpora cardiaca. PEPTIDES 26, 73-80. doi: 10.1016/j.peptides.2004.07.012
    • (2005) PEPTIDES , vol.26 , pp. 73-80
    • Huybrechts, J.1    De Loof, A.2    Schoofs, L.3
  • 62
    • 0031105493 scopus 로고    scopus 로고
    • Purification of erotonin N-acetyltransferase from cockroach testicular glands
    • Ichihara, N., Okada, M., Nakagawa, H., and Takeda, M. (1997). Purification of erotonin N-acetyltransferase from cockroach testicular glands. Insect Biochem Molec Biol 27, 241-246. doi: 10.1016/S0965-1748(96)00091-4
    • (1997) Insect Biochem Molec Biol , vol.27 , pp. 241-246
    • Ichihara, N.1    Okada, M.2    Nakagawa, H.3    Takeda, M.4
  • 63
    • 84926484040 scopus 로고    scopus 로고
    • Purification of arylalkylamine N acetyltransferases from three organs of the American cockroach in Insects
    • eds. D. Konopinska, G. Goldsworthy, J. Nawrot, I. Orchard, and G. Rozinski. (Poland: Univ. Wroclow Press)
    • Ichihara, N., Okada, M., and Takeda M. (1998). Purification of arylalkylamine N acetyltransferases from three organs of the American cockroach in Insects: Chemical physiological and environmental aspects, eds. D. Konopinska, G. Goldsworthy, J. Nawrot, I. Orchard, and G. Rozinski. (Poland: Univ. Wroclow Press), 70-80.
    • (1998) Chemical physiological and environmental aspects , pp. 70-80
    • Ichihara, N.1    Okada, M.2    Takeda, M.3
  • 64
    • 0035189104 scopus 로고    scopus 로고
    • Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana
    • Ichihara, N., Okada, M., and Takeda, M. (2001). Characterization and purification of polymorphic arylalkylamine N-acetyltransferase from the American cockroach, Periplaneta americana. Insect Biochem Mol Biol 32, 15-22. doi: 10.1016/S0965- 1748(01)00075-3
    • (2001) Insect Biochem Mol Biol , vol.32 , pp. 15-22
    • Ichihara, N.1    Okada, M.2    Takeda, M.3
  • 65
    • 0029281730 scopus 로고
    • Day-night changes in melatonin levels in different organs of the cricket (Gryllus bimaculatus)
    • Itoh, M.T., Hattori, A., Sumi, Y., and Suzuki, T. (1995a). Day-night changes in melatonin levels in different organs of the cricket (Gryllus bimaculatus). J Pineal Res 18, 165-169. doi: 10.1111/j.1600-079X.1995.tb00156.x
    • (1995) J Pineal Res , vol.18 , pp. 165-169
    • Itoh, M.T.1    Hattori, A.2    Sumi, Y.3    Suzuki, T.4
  • 66
    • 0028802641 scopus 로고
    • Melatonin and arylalkylamine N-acetyltransferase activity in the silkworm, Bombyx mori
    • Itoh M.T., Hattori, A., Nomura, T., Sumi, Y. and Suzuki, T. (1995b) Melatonin and arylalkylamine N-acetyltransferase activity in the silkworm, Bombyx mori. Moll.Cell. Endocrinol. 115, 59-64. doi: 10.1016/0303-7207(95)03670-3
    • (1995) Moll.Cell. Endocrinol. , vol.115 , pp. 59-64
    • Itoh, M.T.1    Hattori, A.2    Nomura, T.3    Sumi, Y.4    Suzuki, T.5
  • 67
    • 0030869530 scopus 로고    scopus 로고
    • Hydroxyindole-O methyltransferaseactivity in the silkworm (Bombyx mori)
    • Itoh M.T., Hattori, A., Nomura, T., Sumi, Y. and Suzuki, T. (1997) Hydroxyindole-O methyltransferaseactivity in the silkworm (Bombyx mori). Brain Res. 765, 61-66. doi: 10.1016/S0006-8993(97)00482-4
    • (1997) Brain Res. , vol.765 , pp. 61-66
    • Itoh, M.T.1    Hattori, A.2    Nomura, T.3    Sumi, Y.4    Suzuki, T.5
  • 68
    • 0032514278 scopus 로고    scopus 로고
    • Circadian clock controlling arylalkylamine N acetyltransferase like activity in cricket (Gryllus bimaculatus) egg
    • Itoh M.T. and Sumi,Y. (1998a) Circadian clock controlling arylalkylamine N acetyltransferase like activity in cricket (Gryllus bimaculatus) egg. Brain. Res. 799, 172-175. doi: 10.1016/S0006-8993(98)00443-0
    • (1998) Brain. Res. , vol.799 , pp. 172-175
    • Itoh, M.T.1    Sumi, Y.2
  • 69
    • 0032545671 scopus 로고    scopus 로고
    • Melatonin and serotonin N-acetyltransferase activity in developing eggs of the cricket Gryllus bimaculatus
    • Itoh M.T. and Sumi,Y. (1998b) Melatonin and serotonin N-acetyltransferase activity in developing eggs of the cricket Gryllus bimaculatus. Brain Res. 781,91-99. doi: 10.1016/S0006-8993(97)01220-1
    • (1998) Brain Res. , vol.781 , pp. 91-99
    • Itoh, M.T.1    Sumi, Y.2
  • 70
    • 17544369648 scopus 로고    scopus 로고
    • Circadian clocks, clock networks, arylalkylamine N-acetyltransferase, and melatonin in the retina
    • Iuvone, P.M., Tosinis, G., Pozdeyev, N., Haque, R., Klein D.C., and Chaurasia, S.S. (2005). Circadian clocks, clock networks, arylalkylamine N-acetyltransferase, and melatonin in the retina. Progress in RETINAL and EYE RESEARCH 24, 433-456. doi: 10.1016/j.preteyeres.2005.01.003
    • (2005) Progress in RETINAL and EYE RESEARCH , vol.24 , pp. 433-456
    • Iuvone, P.M.1    Tosinis, G.2    Pozdeyev, N.3    Haque, R.4    Klein, D.C.5    Chaurasia, S.S.6
  • 71
    • 2942709486 scopus 로고    scopus 로고
    • Evolution of cell-cell signaling in animals: did late horizontal gene transfer from bacteria have a role?
    • Iyer, L.M., Aravind, L., Coon, S.L., Klein, D.C., and Koonin, E.V. (2004). Evolution of cell-cell signaling in animals: did late horizontal gene transfer from bacteria have a role? Trends Genet 20(7), 292-299. doi: 10.1016/j.tig.2004.05.007
    • (2004) Trends Genet , vol.20 , Issue.7 , pp. 292-299
    • Iyer, L.M.1    Aravind, L.2    Coon, S.L.3    Klein, D.C.4    Koonin, E.V.5
  • 72
    • 60649116239 scopus 로고    scopus 로고
    • Characterization of arylalkylamine N-acetyltransferase (NAT) activities and action spectrum for suppression in the band-legged cricket, Dianemobius nigrofasciatus (Orthoptera: Grillidae)
    • Izawa, N., Suzuki, T., Watanabe, M., and Takeda, M. (2009) Characterization of arylalkylamine N-acetyltransferase (NAT) activities and action spectrum for suppression in the band-legged cricket, Dianemobius nigrofasciatus (Orthoptera: Grillidae). Comp Biochem Physiol B 152, 346-351. doi: 10.1016/j.cbpb.2008.12.016
    • (2009) Comp Biochem Physiol B , vol.152 , pp. 346-351
    • Izawa, N.1    Suzuki, T.2    Watanabe, M.3    Takeda, M.4
  • 73
    • 0028056803 scopus 로고
    • Ultraviolet light-induced free radical formation in skin: an electron paramagnetic resonance study
    • Jurkiewicz, B.A. and Buettner, G.R. (1994). Ultraviolet light-induced free radical formation in skin: an electron paramagnetic resonance study. Photochem Photobiol 59, 1-4. doi: 10.1111/j.1751-1097.1994.tb04993.x
    • (1994) Photochem Photobiol , vol.59 , pp. 1-4
    • Jurkiewicz, B.A.1    Buettner, G.R.2
  • 74
    • 84885178331 scopus 로고    scopus 로고
    • Molecular cloning of rice serotonin N-acetyltransferase, the penultimate gene in plant melatonin biosynthesis
    • Kang, K., Lee, K., Park, S., Byeon, Y., and Back, K. (2013). Molecular cloning of rice serotonin N-acetyltransferase, the penultimate gene in plant melatonin biosynthesis. J Pineal Res 55, 7-13. doi: 10.1111/jpi.12011
    • (2013) J Pineal Res , vol.55 , pp. 7-13
    • Kang, K.1    Lee, K.2    Park, S.3    Byeon, Y.4    Back, K.5
  • 75
    • 0011442195 scopus 로고
    • Identifizierung von N-acetyl 3, 4-dixydroxy-h-phenäthylamin (N acetyldopamine) als Tyrosinmetabolit
    • Karlson, P., Sekeris, C.E., and Sekeri, K.E. (1962). Zum Tyrosinstoffwechsel der Insecten: VI. Identifizierung von N-acetyl 3, 4-dixydroxy-h-phenäthylamin (N acetyldopamine) als Tyrosinmetabolit. Z Phys Chem 327, 86-94.
    • (1962) Z Phys Chem , vol.327 , pp. 86-94
    • Karlson, P.1    Sekeris, C.E.2    Sekeri, K.E.3
  • 76
    • 36749057745 scopus 로고    scopus 로고
    • Immunohistochemical characterization of a parapinopsin containing photoreceptor cell involved in the ultraviolet/green discrimination in the pineal organ of the river lamprey Lethenteron japonicum
    • Kawano-Yamashita, E., Terakita, A., Koyanagi, M., Shichida, Y., Oishi, T., and Tamotsu, S. (2007). Immunohistochemical characterization of a parapinopsin containing photoreceptor cell involved in the ultraviolet/green discrimination in the pineal organ of the river lamprey Lethenteron japonicum. J Exp Biol 210, 3821-3829. doi: 10.1242/jeb.007161
    • (2007) J Exp Biol , vol.210 , pp. 3821-3829
    • Kawano-Yamashita, E.1    Terakita, A.2    Koyanagi, M.3    Shichida, Y.4    Oishi, T.5    Tamotsu, S.6
  • 77
    • 0018582407 scopus 로고
    • Cytochemical investigation of acetyl-serotonin-transferase activity in the pineal gland
    • Kerenyi, N.A., Balogh, I., Somogyi, E., and Sotonyi, P. (1979). Cytochemical investigation of acetyl-serotonin-transferase activity in the pineal gland. Cell Mol Biol Incl Cyto-Enzymol 25, 259-262.
    • (1979) Cell Mol Biol Incl Cyto-Enzymol , vol.25 , pp. 259-262
    • Kerenyi, N.A.1    Balogh, I.2    Somogyi, E.3    Sotonyi, P.4
  • 78
    • 0014941795 scopus 로고
    • Indole metabolism in the pineal gland: a circadian rhythm in N-acetyltransferase
    • Klein, D.C., and Weller, J.L. (1970). Indole metabolism in the pineal gland: a circadian rhythm in N-acetyltransferase. Science 169, 1093-1095. doi: 10.1126/science.169.3950.1093
    • (1970) Science , vol.169 , pp. 1093-1095
    • Klein, D.C.1    Weller, J.L.2
  • 79
    • 33947510169 scopus 로고    scopus 로고
    • Arylalkylamine N-acetyltransferase: "the Timezyme"
    • Klein, D.C. (2007). Arylalkylamine N-acetyltransferase: "the Timezyme". J Biol Chem 282, 4233-4237. doi: 10.1074/jbc.R600036200
    • (2007) J Biol Chem , vol.282 , pp. 4233-4237
    • Klein, D.C.1
  • 80
    • 0028322286 scopus 로고
    • The pineal organ as a component of the biological clock
    • Korf, H.W. (1994). The pineal organ as a component of the biological clock. Ann N Y Acad Sci 719, 13-42. doi: 10.1111/j.1749-6632.1994.tb56818.x
    • (1994) Ann N Y Acad Sci , vol.719 , pp. 13-42
    • Korf, H.W.1
  • 82
    • 20144378876 scopus 로고    scopus 로고
    • Cephalochordate melanopsin: evolutionary linkage between invertebrate visual cells and vertebrate photosensitive retinal ganglion cells
    • Koyanagi, M., Kubokawa, K., Tsukamoto, H., Shichida, Y., and Terakita, A. (2005). Cephalochordate melanopsin: evolutionary linkage between invertebrate visual cells and vertebrate photosensitive retinal ganglion cells. Curr Biol 15, 1065- 1069. doi: 10.1016/j.cub.2005.04.063
    • (2005) Curr Biol , vol.15 , pp. 1065-1069
    • Koyanagi, M.1    Kubokawa, K.2    Tsukamoto, H.3    Shichida, Y.4    Terakita, A.5
  • 83
    • 52149109504 scopus 로고    scopus 로고
    • Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin
    • Koyanagi, M., and Terakita, A. (2008). Gq-coupled rhodopsin subfamily composed of invertebrate visual pigment and melanopsin. Photochem Photobiol 84, 1024- 1030. doi: 10.1111/j.1751-1097.2008.00369.x
    • (2008) Photochem Photobiol , vol.84 , pp. 1024-1030
    • Koyanagi, M.1    Terakita, A.2
  • 84
    • 84885612151 scopus 로고    scopus 로고
    • Identification of genes for melatonin synthetic enzymes in 'Red Fuji' apple (Malus domestica Borkh. cv. Red) and their expression and melatonin production during fruit development
    • Lei, Q., Wang, L., Tan, D.X., Zhao, Y., Zheng, X.D., Chen, H., Li, Q.T., Zuo, B.X., and Kong, J. (2013). Identification of genes for melatonin synthetic enzymes in 'Red Fuji' apple (Malus domestica Borkh. cv. Red) and their expression and melatonin production during fruit development. J Pineal Res 55, 443-451. doi: 10.1111/jpi.12096
    • (2013) J Pineal Res , vol.55 , pp. 443-451
    • Lei, Q.1    Wang, L.2    Tan, D.X.3    Zhao, Y.4    Zheng, X.D.5    Chen, H.6    Li, Q.T.7    Zuo, B.X.8    Kong, J.9
  • 87
    • 0036694407 scopus 로고    scopus 로고
    • Changes in brain monoamine contents in diapause pupae of Antheraea pernyi when activated under long-day and by chilling
    • Matsumoto, M., and Takeda, M. (2002). Changes in brain monoamine contents in diapause pupae of Antheraea pernyi when activated under long-day and by chilling. J Insect Physiol 48, 265-771. doi: 10.1016/S0022-1910(02)00102-6
    • (2002) J Insect Physiol , vol.48 , pp. 265-771
    • Matsumoto, M.1    Takeda, M.2
  • 88
    • 79959799364 scopus 로고    scopus 로고
    • Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti
    • Mehere, P., Han, Q., Christensen, B.M., and Li, J. (2011). Identification and characterization of two arylalkylamine N-acetyltransferases in the yellow fever mosquito, Aedes aegypti. Insect Biochem Molec Biol 41, 707-714. doi: 10.1016/j.ibmb.2011.05.002
    • (2011) Insect Biochem Molec Biol , vol.41 , pp. 707-714
    • Mehere, P.1    Han, Q.2    Christensen, B.M.3    Li, J.4
  • 89
    • 0033578365 scopus 로고    scopus 로고
    • Decoding photoperiodic time through Per1 and ICER gene amplitude
    • Messager, S., Ross. A.W., Barrett, P., and Morgan, P.J. (1999). Decoding photoperiodic time through Per1 and ICER gene amplitude. Proc Natl Acad Sci U S A. 96(17), 9938-9943. doi: 10.1073/pnas.96.17.9938
    • (1999) Proc Natl Acad Sci U S A. , vol.96 , Issue.17 , pp. 9938-9943
    • Messager, S.1    Ross, A.W.2    Barrett, P.3    Morgan, P.J.4
  • 90
    • 84863571935 scopus 로고    scopus 로고
    • Daily variation in melatonin synthesis and arylalkylamine N-acetyltransferase activity in the nematode Caenorhabditis elegans
    • Migliori, M.L., Romanowski, A., Simonetta, S.H., Valdez, D., Guido, M., and Golombek, D.A. (2012). Daily variation in melatonin synthesis and arylalkylamine N-acetyltransferase activity in the nematode Caenorhabditis elegans. J Pineal Res 53, 38-46. doi: 10.1111/j.1600-079X.2011.00969.x
    • (2012) J Pineal Res , vol.53 , pp. 38-46
    • Migliori, M.L.1    Romanowski, A.2    Simonetta, S.H.3    Valdez, D.4    Guido, M.5    Golombek, D.A.6
  • 91
    • 84899821509 scopus 로고    scopus 로고
    • N-acetyltransferase (nat) is a critical conjunct of photoperiodism between the circadian system and endocrine axis in Antheraea pernyi
    • Mohamed, A.A., Wang, Q.-S., Bembenek, J., Ichihara, N., Hiragaki, S., Suzuki, T., and Takeda, M. (2014). N-acetyltransferase (nat) is a critical conjunct of photoperiodism between the circadian system and endocrine axis in Antheraea pernyi PLoS ONE 9(3): e92680 10.1371/journal.pone.0092680. doi: 10.1371/journal.pone.0092680
    • (2014) PLoS ONE , vol.9 , Issue.3
    • Mohamed, A.A.1    Wang, Q.-S.2    Bembenek, J.3    Ichihara, N.4    Hiragaki, S.5    Suzuki, T.6    Takeda, M.7
  • 92
    • 84905050809 scopus 로고    scopus 로고
    • Universality and diversity in the signal transduction pathway that regulates seasonal reproduction in vertebrates
    • Nakane, Y., and Yoshimura, T. (2014). Universality and diversity in the signal transduction pathway that regulates seasonal reproduction in vertebrates. Front Neurosci 8, 115. doi: 10.3389/fnins.2014.00115
    • (2014) Front Neurosci , vol.8 , pp. 115
    • Nakane, Y.1    Yoshimura, T.2
  • 93
    • 0023154078 scopus 로고
    • A simple and rapid method for the purification of ovine pineal arylalkylamine N acetyltransferase
    • Namboodiri, M.A.A., Brownstein, M.J., Voisin, P., Weller, J.L., and Klein, D. (1987). A simple and rapid method for the purification of ovine pineal arylalkylamine N acetyltransferase. J Neurochem 48, 580-585. doi: 10.1111/j.1471- 4159.1987.tb04132.x
    • (1987) J Neurochem , vol.48 , pp. 580-585
    • Namboodiri, M.A.A.1    Brownstein, M.J.2    Voisin, P.3    Weller, J.L.4    Klein, D.5
  • 94
    • 0024452437 scopus 로고
    • Purification of cone visual pigments from chicken retina
    • Okano, T., Fukada, Y., Artamonov, I.D., and Yoshizawa, T. (1989). Purification of cone visual pigments from chicken retina. Biochemistry 28, 8848-8856. doi: 10.1021/bi00448a025
    • (1989) Biochemistry , vol.28 , pp. 8848-8856
    • Okano, T.1    Fukada, Y.2    Artamonov, I.D.3    Yoshizawa, T.4
  • 95
    • 0028143702 scopus 로고
    • Pinopsin is a chicken pineal photoreceptive molecule
    • Okano, T., Yoshizawa, T., and Fukada, Y. (1994). Pinopsin is a chicken pineal photoreceptive molecule. Nature 372, 94-97. doi: 10.1038/372094a0
    • (1994) Nature , vol.372 , pp. 94-97
    • Okano, T.1    Yoshizawa, T.2    Fukada, Y.3
  • 97
    • 84873428434 scopus 로고    scopus 로고
    • Kinetic analysis of purified recombinant rice N-acetylserotonin methyltransferase and peak melatonin production in etiolated rice shoots
    • Park, S., Byeon, Y., Kim, Y. S., and Back, K. (2013a). Kinetic analysis of purified recombinant rice N-acetylserotonin methyltransferase and peak melatonin production in etiolated rice shoots. J Pineal Res 54, 139-144. doi: 10.1111/j.1600- 079X.2012.01019.x
    • (2013) J Pineal Res , vol.54 , pp. 139-144
    • Park, S.1    Byeon, Y.2    Kim, Y.S.3    Back, K.4
  • 98
    • 84874946826 scopus 로고    scopus 로고
    • Melatonin1058 rich transgenic rice plants exhibit resistance to herbicide-induced oxidative stress
    • Park, S., Lee, D. E., Jang, H., Byeon, Y., Kim, Y. S., and Back, K. (2013b). Melatonin1058 rich transgenic rice plants exhibit resistance to herbicide-induced oxidative stress. J Pineal Res 54, 258-263. doi: 10.1111/j.1600-079X.2012.01029.x
    • (2013) J Pineal Res , vol.54 , pp. 258-263
    • Park, S.1    Lee, D.E.2    Jang, H.3    Byeon, Y.4    Kim, Y.S.5    Back, K.6
  • 102
  • 104
    • 0030914428 scopus 로고    scopus 로고
    • Pharmacological actions of melatonin in oxygen radical pathophysiology
    • Reiter, R.J., Tang, L., Garcia, J.J., and Muñoz-Hoyos, A. (1997). Pharmacological actions of melatonin in oxygen radical pathophysiology. Life Sciences 60, 2255- 2271. doi: 10.1016/S0024-3205(97)00030-1
    • (1997) Life Sciences , vol.60 , pp. 2255- 2271
    • Reiter, R.J.1    Tang, L.2    Garcia, J.J.3    Muñoz-Hoyos, A.4
  • 105
    • 0033768749 scopus 로고    scopus 로고
    • Actions of melatonin in the reduction of oxidative stress
    • Reiter, R.J., Tan, D.X., Osuna, C., and Gitto, E. (2000). Actions of melatonin in the reduction of oxidative stress. J Biomed Sci 7, 444-458. doi: 10.1007/BF02253360
    • (2000) J Biomed Sci , vol.7 , pp. 444-458
    • Reiter, R.J.1    Tan, D.X.2    Osuna, C.3    Gitto, E.4
  • 106
    • 33947592217 scopus 로고    scopus 로고
    • Melatonin and its metabolites: new findings regarding their production and their radical scavenging actions
    • Reiter, R.J., Tan, D.X., Terron, M.P., Flores, L.J., and Czarnocki, Z. (2007). Melatonin and its metabolites: new findings regarding their production and their radical scavenging actions. Acta Biochim Pol 54, 1-9.
    • (2007) Acta Biochim Pol , vol.54 , pp. 1-9
    • Reiter, R.J.1    Tan, D.X.2    Terron, M.P.3    Flores, L.J.4    Czarnocki, Z.5
  • 107
    • 70349577367 scopus 로고    scopus 로고
    • Reducing oxidative/nitrosative stress: a newly-discovered genre for melatonin
    • Reiter, R.J., Paredes, S.D., Manchester, L.C., and Tan, D.X. (2009). Reducing oxidative/nitrosative stress: a newly-discovered genre for melatonin. Crit Rev Biochem Mol Biol 44, 175-200. doi: 10.1080/10409230903044914
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , pp. 175-200
    • Reiter, R.J.1    Paredes, S.D.2    Manchester, L.C.3    Tan, D.X.4
  • 108
    • 77955506965 scopus 로고    scopus 로고
    • Melatonin: a multitasking molecule
    • Reiter, R.J., Tan, D.X., and Fuentes-Broto, L. (2010). Melatonin: a multitasking molecule. Prog Brain Res 181, 127-151. doi: 10.1016/S0079-6123(08)81008-4
    • (2010) Prog Brain Res , vol.181 , pp. 127-151
    • Reiter, R.J.1    Tan, D.X.2    Fuentes-Broto, L.3
  • 109
    • 84876850102 scopus 로고    scopus 로고
    • The universal nature, unequal distribution and antioxidant functions of melatonin and its derivatives
    • Reiter, R.J., Tan, D.X., Rosales-Corral, S., and Manchester, L.C. (2013). The universal nature, unequal distribution and antioxidant functions of melatonin and its derivatives. Mini Rev Med Chem 13, 373-384. doi: 10.1016/S0079- 6123(08)81008-4
    • (2013) Mini Rev Med Chem , vol.13 , pp. 373-384
    • Reiter, R.J.1    Tan, D.X.2    Rosales-Corral, S.3    Manchester, L.C.4
  • 110
    • 0034103403 scopus 로고    scopus 로고
    • A neuroendocrine releasing effect of melatonin in the brain of an insect, Periplaneta americana (L.)
    • Richter, K., Peschke, E., and Peschke, D. (2000). A neuroendocrine releasing effect of melatonin in the brain of an insect, Periplaneta americana (L.). J Pineal Res 28, 129-135. doi: 10.1034/j.1600-079X.2001.280301.x
    • (2000) J Pineal Res , vol.28 , pp. 129-135
    • Richter, K.1    Peschke, E.2    Peschke, D.3
  • 111
    • 84874635344 scopus 로고    scopus 로고
    • Rapid birth-and-death evolution of the xenobiotic metabolizing NAT gene family in vertebrates with evidence of adaptive selection
    • Sabbagh, A., Marin, J., Veyssière, C., Lecompte, E., Boukouvala, S., Poloni, E., Darlu, P., and Crouau-Roy, B. (2013). Rapid birth-and-death evolution of the xenobiotic metabolizing NAT gene family in vertebrates with evidence of adaptive selection. BMC Evol Biol 13, 62. doi: 10.1186/1471-2148-13-62
    • (2013) BMC Evol Biol , vol.13 , pp. 62
    • Sabbagh, A.1    Marin, J.2    Veyssière, C.3    Lecompte, E.4    Boukouvala, S.5    Poloni, E.6    Darlu, P.7    Crouau-Roy, B.8
  • 112
    • 0014070709 scopus 로고
    • On the origin of mitosing cells
    • Sagan, L. (1967). On the origin of mitosing cells. J Theor Biol 14, 225-274. doi: 10.1016/0022-5193(67)90079-3
    • (1967) J Theor Biol , vol.14 , pp. 225-274
    • Sagan, L.1
  • 113
    • 77950593667 scopus 로고    scopus 로고
    • Evidence for the involvement of selected biogenic amines (serotonin and melatonin) in the regulation of molting of the edible crab, Oziotelphusa senex senex Fabricius
    • 261-164
    • Sainath, S.B., and Reddy P.S. (2010). Evidence for the involvement of selected biogenic amines (serotonin and melatonin) in the regulation of molting of the edible crab, Oziotelphusa senex senex Fabricius. Aquaculture 302, 261-164. doi: 10.1016/j.aquaculture.2010.02.025
    • (2010) Aquaculture , vol.302
    • Sainath, S.B.1    Reddy, P.S.2
  • 114
    • 22044446394 scopus 로고    scopus 로고
    • Characterization of indolamine N acetyltransferase activity from the head ganglia of the American cockroach, Periplaneta americana
    • Sakamoto, T., Ichihara, N., and Takeda, M. (1998). Characterization of indolamine N acetyltransferase activity from the head ganglia of the American cockroach, Periplaneta americana. Appl Entomol Zool 33, 97-104.
    • (1998) Appl Entomol Zool , vol.33 , pp. 97-104
    • Sakamoto, T.1    Ichihara, N.2    Takeda, M.3
  • 115
    • 8644228625 scopus 로고    scopus 로고
    • Distribution of circadian clock-related proteins in the cephalic nervous system of the silkworm, Bombyx mori
    • Sehadová, H., Markova, E.P., Sehnal, F., and Takeda, M. (2004). Distribution of circadian clock-related proteins in the cephalic nervous system of the silkworm, Bombyx mori. J Biol Rhythms 19, 466-482. doi: 10.1177/0748730404269153
    • (2004) J Biol Rhythms , vol.19 , pp. 466-482
    • Sehadová, H.1    Markova, E.P.2    Sehnal, F.3    Takeda, M.4
  • 116
    • 0011389465 scopus 로고
    • Zum Tyrosinstoffwechsel der Insekten, VII. Der katabolische Abbau des Tyrosins und die Biogenese der Sklerotisierungs substanz, N-acetyl-dopamin
    • Sekeris, C.E., and Karlson, P. (1962). Zum Tyrosinstoffwechsel der Insekten, VII. Der katabolische Abbau des Tyrosins und die Biogenese der Sklerotisierungs substanz, N-acetyl-dopamin. Biochim Biophys Acta 62, 103-113.
    • (1962) Biochim Biophys Acta , vol.62 , pp. 103-113
    • Sekeris, C.E.1    Karlson, P.2
  • 117
    • 0028350366 scopus 로고
    • Dose-response effects of acute ultraviolet irradiation on antioxidants and molecular markers of oxidation in murine epidermis and dermis
    • Shindo, Y., Witt, E., Han, D., and Packer, L. (1994). Dose-response effects of acute ultraviolet irradiation on antioxidants and molecular markers of oxidation in murine epidermis and dermis. J Invest Dermatol 102, 470-475.
    • (1994) J Invest Dermatol , vol.102 , pp. 470-475
    • Shindo, Y.1    Witt, E.2    Han, D.3    Packer, L.4
  • 118
    • 0346154806 scopus 로고    scopus 로고
    • Metabolism of monoamines in invertebrates: the relative importance of monoamine oxidase in different phyla
    • Sloley, B.D. (2004). Metabolism of monoamines in invertebrates: the relative importance of monoamine oxidase in different phyla. Neurotoxicology 25, 175- 183. doi: 10.1016/S0161-813X(03)00096-2
    • (2004) Neurotoxicology , vol.25 , pp. 175-183
    • Sloley, B.D.1
  • 119
  • 121
    • 48549086439 scopus 로고    scopus 로고
    • UV radiation elevates arylalkylamine N-acetyltransferase activity and melatonin content in the two-spotted spider mite, Tetranychus urticae
    • Suzuki, T., Takashima, T., Izawa, N., Watanabe, M., and Takeda, M. (2008) UV radiation elevates arylalkylamine N-acetyltransferase activity and melatonin content in the two-spotted spider mite, Tetranychus urticae. J Insect Physiol 54, 1168-1174. doi: 10.1016/j.jinsphys.2008.06.005
    • (2008) J Insect Physiol , vol.54 , pp. 1168-1174
    • Suzuki, T.1    Takashima, T.2    Izawa, N.3    Watanabe, M.4    Takeda, M.5
  • 122
    • 58349110847 scopus 로고    scopus 로고
    • Action spectrum for the suppression of arylalkylamine N-acetyltransferase activity in the two-spotted spider mite Tetranychus Urticae
    • Suzuki, T., Izawa, N., Takashima, T., Watanabe, M., and Takeda, M. (2009a). Action spectrum for the suppression of arylalkylamine N-acetyltransferase activity in the two-spotted spider mite Tetranychus Urticae. Photochem Photobiol 85,214-219. doi: 10.1111/j.1751-1097.2008.00419.x
    • (2009) Photochem Photobiol , vol.85 , pp. 214-219
    • Suzuki, T.1    Izawa, N.2    Takashima, T.3    Watanabe, M.4    Takeda, M.5
  • 123
    • 65849139378 scopus 로고    scopus 로고
    • UV tolerance in the two-spotted spider mite, Tetranychus urticae (accepted for publication)
    • Suzuki, T., Watanabe, M. and Takeda, M. (2009b). UV tolerance in the two-spotted spider mite, Tetranychus urticae (accepted for publication) J Insect Physiol 55,649-654. doi: 10.1016/j.jinsphys.2009.04.005
    • (2009) J Insect Physiol , vol.55 , pp. 649-654
    • Suzuki, T.1    Watanabe, M.2    Takeda, M.3
  • 124
    • 84875254198 scopus 로고    scopus 로고
    • Photo-orientation may regulate seasonal habitat selection in the two-spotted spider mite Tetranychus urticae
    • Suzuki, T., Kojima, T., Takeda, M., and Sakuma, M. (2013). Photo-orientation may regulate seasonal habitat selection in the two-spotted spider mite Tetranychus urticae. J Exp Biol 216, 977-983. 10.1242/jeb.079582. doi: 10.1242/jeb.079582
    • (2013) J Exp Biol , vol.216 , pp. 977-983
    • Suzuki, T.1    Kojima, T.2    Takeda, M.3    Sakuma, M.4
  • 125
    • 84893464472 scopus 로고    scopus 로고
    • An LED-based UV-B irradiation system for tiny organisms: system description and demonstration experiment to determine the hatchability of eggs from four Tetranychus spider mite species from Okinawa
    • Suzuki, T., Yoshioka, Y., Tsarsitalidou, O., Ntalia, V., Ohno, S., Ohyama, K., Kitashima, Y., Gotoh, T., Takeda, M., and Koveos, D.S. (2014) An LED-based UV-B irradiation system for tiny organisms: system description and demonstration experiment to determine the hatchability of eggs from four Tetranychus spider mite species from Okinawa. J Insect Physiol 62, 1-10. doi: 10.1016/j.jinsphys.2014.01.005
    • (2014) J Insect Physiol , vol.62 , pp. 1-10
    • Suzuki, T.1    Yoshioka, Y.2    Tsarsitalidou, O.3    Ntalia, V.4    Ohno, S.5    Ohyama, K.6    Kitashima, Y.7    Gotoh, T.8    Takeda, M.9    Koveos, D.S.10
  • 126
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • 2725-2029
    • Tamura, K., Stecher, G., Peterson, D., Filipski, A., and Kumar, S. (2013). MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol 30(12), 2725-2029. doi: 10.1093/molbev/mst197
    • (2013) Mol Biol Evol , vol.30 , Issue.12
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 127
    • 0033910011 scopus 로고    scopus 로고
    • Significance of melatonin in antioxidative defense system: reactions and products
    • Tan, D.X., Manchester, L.C., Reiter, R.J., Qi, W.B., Karbownik, M., and Calvo, J.R. (2000). Significance of melatonin in antioxidative defense system: reactions and products. Neurosignals 9, 137-159. doi: 10.1159/000014635
    • (2000) Neurosignals , vol.9 , pp. 137-159
    • Tan, D.X.1    Manchester, L.C.2    Reiter, R.J.3    Qi, W.B.4    Karbownik, M.5    Calvo, J.R.6
  • 128
    • 0036482282 scopus 로고    scopus 로고
    • Chemical and physical properties and potential mechanisms: melatonin as a broad spectrum antioxidant and free radical scavenger
    • Tan, D.X., Reiter, R.J., Manchester, L.C., Yan, M.T., El-Sawi, M., Sainz, R.M., Mayo, J.C., Kohen, R., Allegra, M.C., and Hardeland, R. (2002). Chemical and physical properties and potential mechanisms: melatonin as a broad spectrum antioxidant and free radical scavenger. Curr Top Med Chem 2, 181-197. doi: 10.2174/1568026023394443#sthash.Tu7V9vS6.dpuf
    • (2002) Curr Top Med Chem , vol.2 , pp. 181-197
    • Tan, D.X.1    Reiter, R.J.2    Manchester, L.C.3    Yan, M.T.4    El-Sawi, M.5    Sainz, R.M.6    Mayo, J.C.7    Kohen, R.8    Allegra, M.C.9    Hardeland, R.10
  • 129
    • 33845536018 scopus 로고    scopus 로고
    • One molecule, many derivatives: A never-ending interaction of melatonin with reactive oxygen and nitrogen species?
    • Tan, D.X., Manchester, L.C., Terron, M.P., Flores, L.J., and Reiter, R.J. (2007). One molecule, many derivatives: A never-ending interaction of melatonin with reactive oxygen and nitrogen species?. J Pineal Res 42, 28-42. doi: 10.1111/j.1600-079X.2006.00407.x
    • (2007) J Pineal Res , vol.42 , pp. 28-42
    • Tan, D.X.1    Manchester, L.C.2    Terron, M.P.3    Flores, L.J.4    Reiter, R.J.5
  • 130
    • 84855894824 scopus 로고    scopus 로고
    • Functional roles of melatonin in plants, and perspectives in nutritional and agricultural science
    • Tan, D., Hardeland, R., Manchester, L.C., Korkmaz, A., Ma, S., Rosales-Corral, S., and Reiter, R.J. (2012). Functional roles of melatonin in plants, and perspectives in nutritional and agricultural science. J Exp Bot 63, 2, 577-597. doi: 10.1093/jxb/err256
    • (2012) J Exp Bot , vol.63 , Issue.2 , pp. 577-597
    • Tan, D.1    Hardeland, R.2    Manchester, L.C.3    Korkmaz, A.4    Ma, S.5    Rosales-Corral, S.6    Reiter, R.J.7
  • 131
    • 84873458408 scopus 로고    scopus 로고
    • Mitochondria and chloroplasts as the original sites of melatonin synthesis: a hypothesis related to melatonin's primary function and evolution in eukaryotes
    • Tan, D.X., Manchester, L.C., Liu, X., Rosales-Corral, S.A., Acuna-Castroviejo, D., and Reiter, R.J. (2013). Mitochondria and chloroplasts as the original sites of melatonin synthesis: a hypothesis related to melatonin's primary function and evolution in eukaryotes. J Pineal Res 54, 127-138. doi: 10.1111/jpi.12026
    • (2013) J Pineal Res , vol.54 , pp. 127-138
    • Tan, D.X.1    Manchester, L.C.2    Liu, X.3    Rosales-Corral, S.A.4    Acuna-Castroviejo, D.5    Reiter, R.J.6
  • 132
    • 34547206277 scopus 로고    scopus 로고
    • Melatonin signaling regulates locomotion behavior and homeostatic states through distinct receptor pathways in Caenorhabditis ellegans
    • Tanaka, D., Furusawa, K., Kameyama, K., Okamoto, H., and Doi, M. (2007), Melatonin signaling regulates locomotion behavior and homeostatic states through distinct receptor pathways in Caenorhabditis ellegans. Neuropharmacology 53, 157-168. doi: 10.1016/j.neuropharm.2007.04.017
    • (2007) Neuropharmacology , vol.53 , pp. 157-168
    • Tanaka, D.1    Furusawa, K.2    Kameyama, K.3    Okamoto, H.4    Doi, M.5
  • 133
    • 84926440224 scopus 로고    scopus 로고
    • Molecular, pharmacological and spectroscopic approaches to mechanism of diapause termination in Antheraea pernyi with a special reference to arylalkylamine N-acetyltransferase
    • Doctoral Dissertation, Kobe University
    • Tsugehara, T. (2006). Molecular, pharmacological and spectroscopic approaches to mechanism of diapause termination in Antheraea pernyi with a special reference to arylalkylamine N-acetyltransferase. Doctoral Dissertation, Kobe University, 83.
    • (2006) , pp. 83
    • Tsugehara, T.1
  • 134
    • 34249082778 scopus 로고    scopus 로고
    • Cloning and characterization of insect arylalkylamine N-acetyltransferase for Bombyx mori
    • Tsugehara, T., Iwai, S., Fujiwara, Y., Mita, K., and Takeda, M. (2007) Cloning and characterization of insect arylalkylamine N-acetyltransferase for Bombyx mori. Comp Biochem Physiol B 147, 358-366. doi: 10.1016/j.cbpb.2006.10.112
    • (2007) Comp Biochem Physiol B , vol.147 , pp. 358-366
    • Tsugehara, T.1    Iwai, S.2    Fujiwara, Y.3    Mita, K.4    Takeda, M.5
  • 135
    • 84870278217 scopus 로고    scopus 로고
    • Characterization of arylalkylamine N acetyltransferase from Antheraea pernyi and pesticidal drug design based on the baculovirus-expressed enzyme
    • Tsugehara, T., Imai, T., and Takeda, M. (2013) Characterization of arylalkylamine N acetyltransferase from Antheraea pernyi and pesticidal drug design based on the baculovirus-expressed enzyme. Comp Biochem Physiol C 157, 93-102. doi: 10.1016/j.cbpc.2012.10.003
    • (2013) Comp Biochem Physiol C , vol.157 , pp. 93-102
    • Tsugehara, T.1    Imai, T.2    Takeda, M.3
  • 136
    • 0036546520 scopus 로고    scopus 로고
    • Tales from the crypt (ochromes)
    • Van Gelder, R.N. (2002). Tales from the crypt (ochromes). J Biol Rhythms 17, 110-120. doi: 10.1177/074873002129002401
    • (2002) J Biol Rhythms , vol.17 , pp. 110-120
    • Van Gelder, R.N.1
  • 137
    • 0029867030 scopus 로고    scopus 로고
    • The insect neuropeptide prothoracicptropic hormone is released with a daily rhythm: re-evaluation of its role in development
    • Vafopoulou, X., and Steele, C.G.H. (1996) The insect neuropeptide prothoracicptropic hormone is released with a daily rhythm: re-evaluation of its role in development. Proc Natl Acad Sci U S A. 93, 3368-3372.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 3368-3372
    • Vafopoulou, X.1    Steele, C.G.H.2
  • 138
    • 84892598957 scopus 로고    scopus 로고
    • Serotonin receptor B may lock the gate of PTTH release/synthesis in the Chinese silk moth, Antheraea pernyi; a diapause initiation/maintenance mechanism?
    • Wang, Q.S., Mohamed, A.A., and Takeda, M. (2013) Serotonin receptor B may lock the gate of PTTH release/synthesis in the Chinese silk moth, Antheraea pernyi; a diapause initiation/maintenance mechanism? PLoS ONE 8, e7938110.1371 /journal.pone.0079381. doi: 10.1371/journal.pone.0079381
    • (2013) PLoS ONE , vol.8
    • Wang, Q.S.1    Mohamed, A.A.2    Takeda, M.3
  • 139
    • 0029295356 scopus 로고    scopus 로고
    • N-acetyltransferase, hydroxyindole-O-methyltransferase and melatonin in the optic lobes of the giant tiger shrimp Penaeus monodon
    • Withyachumnarnkul, B., Pongtippatee, P., and Ajpru, S. (2007). N-acetyltransferase, hydroxyindole-O-methyltransferase and melatonin in the optic lobes of the giant tiger shrimp Penaeus monodon. J Pineal Res 18, 217-221. doi: 10.1111/j.1600- 079X.1995.tb00162.x
    • (2007) J Pineal Res , vol.18 , pp. 217-221
    • Withyachumnarnkul, B.1    Pongtippatee, P.2    Ajpru, S.3
  • 140
    • 0035879648 scopus 로고    scopus 로고
    • Melatonin in drinking water synchronizes a circadian rhythm of locomotor activity in the house cricket, Acheta domesticus
    • Yamano, H., Watari, Y., Arai, T., and Takeda, M. (2001). Melatonin in drinking water synchronizes a circadian rhythm of locomotor activity in the house cricket, Acheta domesticus. J Insect Physiol 47, 943-949. doi: 10.1016/S0022- 1910(01)00067-1
    • (2001) J Insect Physiol , vol.47 , pp. 943-949
    • Yamano, H.1    Watari, Y.2    Arai, T.3    Takeda, M.4
  • 141
    • 84881311628 scopus 로고    scopus 로고
    • Thyroid hormone and seasonal regulation of reproduction
    • Yoshimura, T. (2013). Thyroid hormone and seasonal regulation of reproduction. Front Neuroendocrinol 34(3), 157-166. doi: 10.1016/j.yfrne.2013.04.002
    • (2013) Front Neuroendocrinol , vol.34 , Issue.3 , pp. 157-166
    • Yoshimura, T.1
  • 142
    • 78649813006 scopus 로고    scopus 로고
    • Disruption of an N-acetyltransferase gene in the silkworm reveals a novel role in pigmentation
    • Zhan, S., Guo, Q., Li, M., Li. M., Li. J., Miao. X., and Huang, Y. (2010). Disruption of an N-acetyltransferase gene in the silkworm reveals a novel role in pigmentation. Development 137(23), 4083-4090. doi: 10.1242/dev.053678
    • (2010) Development , vol.137 , Issue.23 , pp. 4083-4090
    • Zhan, S.1    Guo, Q.2    Li, M.3    Li, M.4    Li, J.5    Miao, X.6    Huang, Y.7
  • 143
    • 84872675331 scopus 로고    scopus 로고
    • Melatonin promotes water-stress tolerance, lateral root formation, and seed germination in cucumber (Cucumis sativus L.)
    • Zhang, N., Zhao, B., Zhang, H.J., Weeda, S., Yang, C., Yang, Z.C., Ren, S., and Guo, Y.D. (2013). Melatonin promotes water-stress tolerance, lateral root formation, and seed germination in cucumber (Cucumis sativus L.). J Pneal Res 54, 15-23. doi: 10.1111/j.1600-079X.2012.01015.x
    • (2013) J Pneal Res , vol.54 , pp. 15-23
    • Zhang, N.1    Zhao, B.2    Zhang, H.J.3    Weeda, S.4    Yang, C.5    Yang, Z.C.6    Ren, S.7    Guo, Y.D.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.