메뉴 건너뛰기




Volumn 5, Issue JUN, 2014, Pages

The evolution and variety of RFamide-type neuropeptides: Insights from deuterostomian invertebrates

Author keywords

Deuterostome; Echinoderm; Evolution; Hemichordate; Neuropeptide; Receptor; RFamide

Indexed keywords

AGEGLSSPFWSLAAPQRF AMIDE; CHOLECYSTOKININ; FLFQPQRFAMIDE; G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR 10; G PROTEIN COUPLED RECEPTOR 103; G PROTEIN COUPLED RECEPTOR 54; GASTRIN; GONADOTROPIN ANTAGONIST; KISSPEPTIN; LEUCYLPROLYLLEUCYLARGINYLPHENYLALANINAMIDE; LUQIN; NEUROPEPTIDE; NEUROPEPTIDE FF; NEUROPEPTIDE Y; PEPTIDES AND PROTEINS; PHENYLALANYLMETHIONYLARGINYLPHENYLALANINAMIDE; PROLACTIN RELEASING PEPTIDE; PYROGLUTAMYLATED RFAMIDE PEPTIDE; RHODOPSIN; SIFAMIDE; SIKPSAYLPLRF AMIDE; UNCLASSIFIED DRUG;

EID: 84905443771     PISSN: None     EISSN: 16642392     Source Type: Journal    
DOI: 10.3389/fendo.2014.00093     Document Type: Review
Times cited : (65)

References (85)
  • 1
    • 77953931115 scopus 로고    scopus 로고
    • Drosophila neuropeptides in regulation of physiology and behavior
    • doi:10.1016/j.pneurobio.2010.04.010
    • Nassel 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
    • Nassel, D.R.1    Winther, A.M.2
  • 2
    • 84867128022 scopus 로고    scopus 로고
    • Peptide neuromodulation in invertebrate model systems
    • doi:10.1016/j.neuron.2012.08.035
    • Taghert PH, Nitabach MN. Peptide neuromodulation in invertebrate model systems. Neuron (2012) 76:82-97. doi:10.1016/j.neuron.2012.08.035
    • (2012) Neuron , vol.76 , pp. 82-97
    • Taghert, P.H.1    Nitabach, M.N.2
  • 3
    • 84891126528 scopus 로고    scopus 로고
    • Ancient neuromodulation by vasopressin/oxytocin-related peptides
    • doi:10.4161/worm.24246
    • Beets I, Temmerman L, Janssen T, Schoofs L. Ancient neuromodulation by vasopressin/oxytocin-related peptides. Worm (2013) 2:e24246. doi:10.4161/worm.24246
    • (2013) Worm , vol.2
    • Beets, I.1    Temmerman, L.2    Janssen, T.3    Schoofs, L.4
  • 4
    • 77952547163 scopus 로고    scopus 로고
    • Neurohormones and neuropeptides encoded by the genome of Lottia gigantea, with reference to other mollusks and insects
    • doi:10.1016/j.ygcen.2010.02.010
    • Veenstra JA. Neurohormones and neuropeptides encoded by the genome of Lottia gigantea, with reference to other mollusks and insects. Gen Comp Endocrinol (2010) 167:86-103. doi:10.1016/j.ygcen.2010.02.010
    • (2010) Gen Comp Endocrinol , vol.167 , pp. 86-103
    • Veenstra, J.A.1
  • 5
    • 79952489969 scopus 로고    scopus 로고
    • Neuropeptide evolution: neurohormones and neuropeptides predicted from the genomes of Capitella teleta and Helobdella robusta
    • doi:10.1016/j.ygcen.2011.01.005
    • Veenstra JA. Neuropeptide evolution: neurohormones and neuropeptides predicted from the genomes of Capitella teleta and Helobdella robusta. Gen Comp Endocrinol (2011) 171:160-75. doi:10.1016/j.ygcen.2011.01.005
    • (2011) Gen Comp Endocrinol , vol.171 , pp. 160-175
    • Veenstra, J.A.1
  • 6
    • 84867744675 scopus 로고    scopus 로고
    • The neuropeptide transcriptome of a model echinoderm, the sea urchin Strongylocentrotus purpuratus
    • doi:10.1016/j.ygcen.2012.09.009
    • Rowe ML, Elphick MR. The neuropeptide transcriptome of a model echinoderm, the sea urchin Strongylocentrotus purpuratus. Gen Comp Endocrinol (2012) 179:331-44. doi:10.1016/j.ygcen.2012.09.009
    • (2012) Gen Comp Endocrinol , vol.179 , pp. 331-344
    • Rowe, M.L.1    Elphick, M.R.2
  • 7
    • 84878150640 scopus 로고    scopus 로고
    • Global view of the evolution and diversity of metazoan neuropeptide signaling
    • doi:10.1073/pnas.1221833110
    • Jekely G. Global view of the evolution and diversity of metazoan neuropeptide signaling. Proc Natl Acad Sci U S A (2013) 110:8702-7. doi:10.1073/pnas.1221833110
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 8702-8707
    • Jekely, G.1
  • 8
    • 84878435930 scopus 로고    scopus 로고
    • Molecular evolution of peptidergic signaling systems in bilaterians
    • doi:10.1073/pnas.1219956110
    • Mirabeau O, Joly JS. Molecular evolution of peptidergic signaling systems in bilaterians. Proc Natl Acad Sci U S A (2013) 110:E2028-37. doi:10.1073/pnas.1219956110
    • (2013) Proc Natl Acad Sci U S A , vol.110
    • Mirabeau, O.1    Joly, J.S.2
  • 9
    • 2442675424 scopus 로고    scopus 로고
    • The expanding family of -RFamide peptides and their effects on feeding behaviour
    • doi:10.1113/expphysiol.2004.027169
    • Dockray GJ. The expanding family of -RFamide peptides and their effects on feeding behaviour. Exp Physiol (2004) 89:229-35. doi:10.1113/expphysiol.2004.027169
    • (2004) Exp Physiol , vol.89 , pp. 229-235
    • Dockray, G.J.1
  • 10
    • 33947413580 scopus 로고    scopus 로고
    • The role of RFamide peptides in feeding
    • doi:10.1677/JOE-06-0069
    • Bechtold DA, Luckman SM. The role of RFamide peptides in feeding. J Endocrinol (2007) 192:3-15. doi:10.1677/JOE-06-0069
    • (2007) J Endocrinol , vol.192 , pp. 3-15
    • Bechtold, D.A.1    Luckman, S.M.2
  • 12
    • 0014128052 scopus 로고
    • Heart excitatory and inhibitory substances in molluscan ganglia
    • doi:10.1016/0010-406X(67)90775-X
    • Frontali N, Williams L, Welsh JH. Heart excitatory and inhibitory substances in molluscan ganglia. Comp Biochem Physiol (1967) 22:833-41. doi:10.1016/0010-406X(67)90775-X
    • (1967) Comp Biochem Physiol , vol.22 , pp. 833-841
    • Frontali, N.1    Williams, L.2    Welsh, J.H.3
  • 13
    • 0017773076 scopus 로고
    • Structure of a molluscan cardioexcitatory neuropeptide
    • doi:10.1126/science.877582
    • Price DA, Greenberg MJ. Structure of a molluscan cardioexcitatory neuropeptide. Science (1977) 197:670-1. doi:10.1126/science.877582
    • (1977) Science , vol.197 , pp. 670-671
    • Price, D.A.1    Greenberg, M.J.2
  • 14
    • 0019164030 scopus 로고
    • Immunocytochemical identification of neural elements in the central nervous systems of a snail, some insects, a fish, and a mammal with an antiserum to the molluscan cardio-excitatory tetrapeptide FMRF-amide
    • doi:10.1007/BF00236917
    • Boer HH, Schot LP, Veenstra JA, Reichelt D. Immunocytochemical identification of neural elements in the central nervous systems of a snail, some insects, a fish, and a mammal with an antiserum to the molluscan cardio-excitatory tetrapeptide FMRF-amide. Cell Tissue Res (1980) 213:21-7. doi:10.1007/BF00236917
    • (1980) Cell Tissue Res , vol.213 , pp. 21-27
    • Boer, H.H.1    Schot, L.P.2    Veenstra, J.A.3    Reichelt, D.4
  • 15
    • 0001262708 scopus 로고
    • The hunting of the FaRPs: the distribution of FMRFamide-related peptides
    • doi:10.2307/1541933
    • Price D, Greenberg M. The hunting of the FaRPs: the distribution of FMRFamide-related peptides. Biol Bull (1989) 177:198-205. doi:10.2307/1541933
    • (1989) Biol Bull , vol.177 , pp. 198-205
    • Price, D.1    Greenberg, M.2
  • 16
    • 77951937499 scopus 로고    scopus 로고
    • A review of FMRFamide- and RFamide-like peptides in metazoa
    • doi:10.1007/s10158-010-0097-7
    • Walker RJ, Papaioannou S, Holden-Dye L. A review of FMRFamide- and RFamide-like peptides in metazoa. Invert Neurosci (2009) 9:111-53. doi:10.1007/s10158-010-0097-7
    • (2009) Invert Neurosci , vol.9 , pp. 111-153
    • Walker, R.J.1    Papaioannou, S.2    Holden-Dye, L.3
  • 17
    • 0020601865 scopus 로고
    • A novel active pentapeptide from chicken brain identified by antibodies to FMRFamide
    • doi:10.1038/305328a0
    • Dockray GJ, Reeve JR Jr, Shively J, Gayton RJ, Barnard CS. A novel active pentapeptide from chicken brain identified by antibodies to FMRFamide. Nature (1983) 305:328-30. doi:10.1038/305328a0
    • (1983) Nature , vol.305 , pp. 328-330
    • Dockray, G.J.1    Reeve Jr., J.R.2    Shively, J.3    Gayton, R.J.4    Barnard, C.S.5
  • 19
    • 0035281823 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a novel avian hypothalamic neuropeptide exerting an inhibitory effect on gonadotropin release
    • doi:10.1042/0264-6021:3540379
    • Satake H, Hisada M, Kawada T, Minakata H, Ukena K, Tsutsui K. Characterization of a cDNA encoding a novel avian hypothalamic neuropeptide exerting an inhibitory effect on gonadotropin release. Biochem J (2001) 354:379-85. doi:10.1042/0264-6021:3540379
    • (2001) Biochem J , vol.354 , pp. 379-385
    • Satake, H.1    Hisada, M.2    Kawada, T.3    Minakata, H.4    Ukena, K.5    Tsutsui, K.6
  • 20
    • 78649505408 scopus 로고    scopus 로고
    • Recent studies of gonadotropin-inhibitory hormone (GnIH) in the mammalian hypothalamus, pituitary and gonads
    • doi:10.1016/j.brainres.2010.10.001
    • Bentley GE, Tsutsui K, Kriegsfeld LJ. Recent studies of gonadotropin-inhibitory hormone (GnIH) in the mammalian hypothalamus, pituitary and gonads. Brain Res (2010) 1364:62-71. doi:10.1016/j.brainres.2010.10.001
    • (2010) Brain Res , vol.1364 , pp. 62-71
    • Bentley, G.E.1    Tsutsui, K.2    Kriegsfeld, L.J.3
  • 21
    • 84882816807 scopus 로고    scopus 로고
    • Gonadotropin-inhibitory hormone (GnIH), GnIH receptor and cell signaling
    • doi:10.1016/j.ygcen.2013.02.030
    • Ubuka T, Son YL, Bentley GE, Millar RP, Tsutsui K. Gonadotropin-inhibitory hormone (GnIH), GnIH receptor and cell signaling. Gen Comp Endocrinol (2013) 190:10-7. doi:10.1016/j.ygcen.2013.02.030
    • (2013) Gen Comp Endocrinol , vol.190 , pp. 10-17
    • Ubuka, T.1    Son, Y.L.2    Bentley, G.E.3    Millar, R.P.4    Tsutsui, K.5
  • 22
    • 0034671712 scopus 로고    scopus 로고
    • Identification and characterization of two G protein-coupled receptors for neuropeptide FF
    • doi:10.1074/jbc.M004385200
    • Bonini JA, Jones LK, Adham N, Forray C, Artymyshyn R, Durkin MM, et al. Identification and characterization of two G protein-coupled receptors for neuropeptide FF. J Biol Chem (2000) 275:39324-31. doi:10.1074/jbc.M004385200
    • (2000) J Biol Chem , vol.275 , pp. 39324-39331
    • Bonini, J.A.1    Jones, L.K.2    Adham, N.3    Forray, C.4    Artymyshyn, R.5    Durkin, M.M.6
  • 23
    • 0035813104 scopus 로고    scopus 로고
    • Identification and characterization of novel mammalian neuropeptide FF-like peptides that attenuate morphine-induced antinociception
    • doi:10.1074/jbc.M105308200
    • Liu QY, Guan XM, Martin WJ, McDonald TP, Clements MK, Jiang QP, et al. Identification and characterization of novel mammalian neuropeptide FF-like peptides that attenuate morphine-induced antinociception. J Biol Chem (2001) 276:36961-9. doi:10.1074/jbc.M105308200
    • (2001) J Biol Chem , vol.276 , pp. 36961-36969
    • Liu, Q.Y.1    Guan, X.M.2    Martin, W.J.3    McDonald, T.P.4    Clements, M.K.5    Jiang, Q.P.6
  • 24
    • 0037144161 scopus 로고    scopus 로고
    • Pharmacological characterization of human NPFF(1) and NPFF(2) receptors expressed in CHO cells by using NPY Y(1) receptor antagonists
    • doi:10.1016/S0014-2999(02)02224-0
    • Mollereau C, Mazarguil H, Marcus D, Quelven I, Kotani M, Lannoy V, et al. Pharmacological characterization of human NPFF(1) and NPFF(2) receptors expressed in CHO cells by using NPY Y(1) receptor antagonists. Eur J Pharmacol (2002) 451:245-56. doi:10.1016/S0014-2999(02)02224-0
    • (2002) Eur J Pharmacol , vol.451 , pp. 245-256
    • Mollereau, C.1    Mazarguil, H.2    Marcus, D.3    Quelven, I.4    Kotani, M.5    Lannoy, V.6
  • 25
    • 77954616184 scopus 로고    scopus 로고
    • Phylogenetic aspects of gonadotropin-inhibitory hormone and its homologs in vertebrates
    • doi:10.1111/j.1749-6632.2010.05510.x
    • Tsutsui K. Phylogenetic aspects of gonadotropin-inhibitory hormone and its homologs in vertebrates. Ann N Y Acad Sci (2010) 1200:75-84. doi:10.1111/j.1749-6632.2010.05510.x
    • (2010) Ann N Y Acad Sci , vol.1200 , pp. 75-84
    • Tsutsui, K.1
  • 26
    • 84860321220 scopus 로고    scopus 로고
    • Evolutionary origin of the structure and function of gonadotropin-inhibitory hormone: insights from lampreys
    • doi:10.1210/en.2011-2046
    • Osugi T, Daukss D, Gazda K, Ubuka T, Kosugi T, Nozaki M, et al. Evolutionary origin of the structure and function of gonadotropin-inhibitory hormone: insights from lampreys. Endocrinology (2012) 153:2362-74. doi:10.1210/en.2011-2046
    • (2012) Endocrinology , vol.153 , pp. 2362-2374
    • Osugi, T.1    Daukss, D.2    Gazda, K.3    Ubuka, T.4    Kosugi, T.5    Nozaki, M.6
  • 27
    • 0011981114 scopus 로고
    • Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine
    • doi:10.1073/pnas.82.22.7757
    • Yang HY, Fratta W, Majane EA, Costa E. Isolation, sequencing, synthesis, and pharmacological characterization of two brain neuropeptides that modulate the action of morphine. Proc Natl Acad Sci U S A (1985) 82:7757-61. doi:10.1073/pnas.82.22.7757
    • (1985) Proc Natl Acad Sci U S A , vol.82 , pp. 7757-7761
    • Yang, H.Y.1    Fratta, W.2    Majane, E.A.3    Costa, E.4
  • 28
    • 0030789876 scopus 로고    scopus 로고
    • A human gene encoding morphine modulating peptides related to NPFF and FMRFamide
    • doi:10.1016/S0014-5793(97)00557-7
    • Perry SJ, Huang EYK, Cronk D, Bagust J, Sharma R, Walker RJ, et al. A human gene encoding morphine modulating peptides related to NPFF and FMRFamide. FEBS Lett (1997) 409:426-30. doi:10.1016/S0014-5793(97)00557-7
    • (1997) FEBS Lett , vol.409 , pp. 426-430
    • Perry, S.J.1    Huang, E.Y.K.2    Cronk, D.3    Bagust, J.4    Sharma, R.5    Walker, R.J.6
  • 30
    • 0034714345 scopus 로고    scopus 로고
    • Receptor for the pain modulatory neuropeptides FF and AF is an orphan G protein-coupled receptor
    • doi:10.1074/jbc.M004515200
    • Elshourbagy NA, Ames RS, Fitzgerald LR, Foley JJ, Chambers JK, Szekeres PG, et al. Receptor for the pain modulatory neuropeptides FF and AF is an orphan G protein-coupled receptor. J Biol Chem (2000) 275:25965-71. doi:10.1074/jbc.M004515200
    • (2000) J Biol Chem , vol.275 , pp. 25965-25971
    • Elshourbagy, N.A.1    Ames, R.S.2    Fitzgerald, L.R.3    Foley, J.J.4    Chambers, J.K.5    Szekeres, P.G.6
  • 31
    • 18844464025 scopus 로고    scopus 로고
    • Detailed distribution of neuropeptide FF receptors (NPFF1 and NPFF2) in the rat, mouse, octodon, rabbit, guinea pig, and marmoset monkey brains: a comparative autoradiographic study
    • doi:10.1002/syn.10305
    • Gouarderes C, Puget A, Zajac JM. Detailed distribution of neuropeptide FF receptors (NPFF1 and NPFF2) in the rat, mouse, octodon, rabbit, guinea pig, and marmoset monkey brains: a comparative autoradiographic study. Synapse (2004) 51:249-69. doi:10.1002/syn.10305
    • (2004) Synapse , vol.51 , pp. 249-269
    • Gouarderes, C.1    Puget, A.2    Zajac, J.M.3
  • 32
    • 0023248448 scopus 로고
    • Elevation of arterial pressure in rats by two new vertebrate peptides FLFQPQRF-NH2 and AGEGLSSPFWSLAAPQRF-NH2 which are immunoreactive to FMRF-NH2 antiserum
    • doi:10.1016/0143-4179(87)90087-4
    • Roth BL, Disimone J, Majane EA, Yang HY. Elevation of arterial pressure in rats by two new vertebrate peptides FLFQPQRF-NH2 and AGEGLSSPFWSLAAPQRF-NH2 which are immunoreactive to FMRF-NH2 antiserum. Neuropeptides (1987) 10:37-42. doi:10.1016/0143-4179(87)90087-4
    • (1987) Neuropeptides , vol.10 , pp. 37-42
    • Roth, B.L.1    Disimone, J.2    Majane, E.A.3    Yang, H.Y.4
  • 33
    • 0029078498 scopus 로고
    • Mechanisms underlying the cardiovascular responses to peripheral administration of NPFF in the rat
    • Allard M, Labrouche S, Nosjean A, Laguzzi R. Mechanisms underlying the cardiovascular responses to peripheral administration of NPFF in the rat. J Pharmacol Exp Ther (1995) 274:577-83.
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 577-583
    • Allard, M.1    Labrouche, S.2    Nosjean, A.3    Laguzzi, R.4
  • 34
    • 77949273326 scopus 로고    scopus 로고
    • Pressor and tachycardic responses to intrathecal administration of neuropeptide FF in anesthetized rats
    • doi:10.1016/j.peptides.2009.11.003
    • Fang Q, Li N, Jiang TN, Liu Q, Li YL, Wang R. Pressor and tachycardic responses to intrathecal administration of neuropeptide FF in anesthetized rats. Peptides (2010) 31:683-8. doi:10.1016/j.peptides.2009.11.003
    • (2010) Peptides , vol.31 , pp. 683-688
    • Fang, Q.1    Li, N.2    Jiang, T.N.3    Liu, Q.4    Li, Y.L.5    Wang, R.6
  • 35
    • 80054925597 scopus 로고    scopus 로고
    • Characterization of novel RFamide peptides in the central nervous system of the brown hagfish: isolation, localization, and functional analysis
    • doi:10.1210/en.2011-1375
    • Osugi T, Uchida K, Nozaki M, Tsutsui K. Characterization of novel RFamide peptides in the central nervous system of the brown hagfish: isolation, localization, and functional analysis. Endocrinology (2011) 152:4252-64. doi:10.1210/en.2011-1375
    • (2011) Endocrinology , vol.152 , pp. 4252-4264
    • Osugi, T.1    Uchida, K.2    Nozaki, M.3    Tsutsui, K.4
  • 36
    • 33646895928 scopus 로고    scopus 로고
    • Evolutionary origin and divergence of PQRFamide peptides and LPXRFamide peptides in the RFamide peptide family. Insights from novel lamprey RFamide peptides
    • doi:10.1111/j.1742-4658.2006.05187.x
    • Osugi T, Ukena K, Sower SA, Kawauchi H, Tsutsui K. Evolutionary origin and divergence of PQRFamide peptides and LPXRFamide peptides in the RFamide peptide family. Insights from novel lamprey RFamide peptides. FEBS J (2006) 273:1731-43. doi:10.1111/j.1742-4658.2006.05187.x
    • (2006) FEBS J , vol.273 , pp. 1731-1743
    • Osugi, T.1    Ukena, K.2    Sower, S.A.3    Kawauchi, H.4    Tsutsui, K.5
  • 37
    • 84861687315 scopus 로고    scopus 로고
    • Effects of lamprey PQRFamide peptides on brain gonadotropin-releasing hormone concentrations and pituitary gonadotropin-beta mRNA expression
    • doi:10.1016/j.ygcen.2012.04.024
    • Daukss D, Gazda K, Kosugi T, Osugi T, Tsutsui K, Sower SA. Effects of lamprey PQRFamide peptides on brain gonadotropin-releasing hormone concentrations and pituitary gonadotropin-beta mRNA expression. Gen Comp Endocrinol (2012) 177:215-9. doi:10.1016/j.ygcen.2012.04.024
    • (2012) Gen Comp Endocrinol , vol.177 , pp. 215-219
    • Daukss, D.1    Gazda, K.2    Kosugi, T.3    Osugi, T.4    Tsutsui, K.5    Sower, S.A.6
  • 38
    • 0028971215 scopus 로고
    • Orphanin FQ: a neuropeptide that activates an opioidlike G protein-coupled receptor
    • doi:10.1126/science.270.5237.792
    • Reinscheid RK, Nothacker HP, Bourson A, Ardati A, Henningsen RA, Bunzow JR, et al. Orphanin FQ: a neuropeptide that activates an opioidlike G protein-coupled receptor. Science (1995) 270:792-4. doi:10.1126/science.270.5237.792
    • (1995) Science , vol.270 , pp. 792-794
    • Reinscheid, R.K.1    Nothacker, H.P.2    Bourson, A.3    Ardati, A.4    Henningsen, R.A.5    Bunzow, J.R.6
  • 40
    • 10744229822 scopus 로고    scopus 로고
    • Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity
    • doi:10.1073/pnas.2434676100
    • Chartrel N, Dujardin C, Anouar Y, Leprince J, Decker A, Clerens S, et al. Identification of 26RFa, a hypothalamic neuropeptide of the RFamide peptide family with orexigenic activity. Proc Natl Acad Sci U S A (2003) 100:15247-52. doi:10.1073/pnas.2434676100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 15247-15252
    • Chartrel, N.1    Dujardin, C.2    Anouar, Y.3    Leprince, J.4    Decker, A.5    Clerens, S.6
  • 41
    • 0344875603 scopus 로고    scopus 로고
    • A new peptidic ligand and its receptor regulating adrenal function in rats
    • doi:10.1074/jbc.M305270200
    • Fukusumi S, Yoshida H, Fujii R, Maruyama M, Komatsu H, Habata Y, et al. A new peptidic ligand and its receptor regulating adrenal function in rats. J Biol Chem (2003) 278:46387-95. doi:10.1074/jbc.M305270200
    • (2003) J Biol Chem , vol.278 , pp. 46387-46395
    • Fukusumi, S.1    Yoshida, H.2    Fujii, R.3    Maruyama, M.4    Komatsu, H.5    Habata, Y.6
  • 42
    • 0041344654 scopus 로고    scopus 로고
    • Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155
    • doi:10.1074/jbc.M302945200
    • Jiang Y, Luo L, Gustafson EL, Yadav D, Laverty M, Murgolo N, et al. Identification and characterization of a novel RF-amide peptide ligand for orphan G-protein-coupled receptor SP9155. J Biol Chem (2003) 278:27652-7. doi:10.1074/jbc.M302945200
    • (2003) J Biol Chem , vol.278 , pp. 27652-27657
    • Jiang, Y.1    Luo, L.2    Gustafson, E.L.3    Yadav, D.4    Laverty, M.5    Murgolo, N.6
  • 43
    • 54049127256 scopus 로고    scopus 로고
    • Central administration of the RFamide peptides, QRFP-26 and QRFP-43, increases high fat food intake in rats
    • doi:10.1016/j.peptides.2008.07.024
    • Primeaux SD, Blackmon C, Barnes MJ, Braymer HD, Bray GA. Central administration of the RFamide peptides, QRFP-26 and QRFP-43, increases high fat food intake in rats. Peptides (2008) 29:1994-2000. doi:10.1016/j.peptides.2008.07.024
    • (2008) Peptides , vol.29 , pp. 1994-2000
    • Primeaux, S.D.1    Blackmon, C.2    Barnes, M.J.3    Braymer, H.D.4    Bray, G.A.5
  • 44
    • 80053113944 scopus 로고    scopus 로고
    • The RFamide neuropeptide 26RFa and its role in the control of neuroendocrine functions
    • doi:10.1016/j.yfrne.2011.04.001
    • Chartrel N, Alonzeau J, Alexandre D, Jeandel L, Alvear-Perez R, Leprince J, et al. The RFamide neuropeptide 26RFa and its role in the control of neuroendocrine functions. Front Neuroendocrinol (2011) 32:387-97. doi:10.1016/j.yfrne.2011.04.001
    • (2011) Front Neuroendocrinol , vol.32 , pp. 387-397
    • Chartrel, N.1    Alonzeau, J.2    Alexandre, D.3    Jeandel, L.4    Alvear-Perez, R.5    Leprince, J.6
  • 45
    • 79958000159 scopus 로고    scopus 로고
    • QRFP in female rats: effects on high fat food intake and hypothalamic gene expression across the estrous cycle
    • doi:10.1016/j.peptides.2011.03.022
    • Primeaux SD. QRFP in female rats: effects on high fat food intake and hypothalamic gene expression across the estrous cycle. Peptides (2011) 32:1270-5. doi:10.1016/j.peptides.2011.03.022
    • (2011) Peptides , vol.32 , pp. 1270-1275
    • Primeaux, S.D.1
  • 46
    • 84890560157 scopus 로고    scopus 로고
    • Hypothalamic QRFP: regulation of food intake and fat selection
    • doi:10.1055/s-0033-1353181
    • Primeaux SD, Barnes MJ, Braymer HD. Hypothalamic QRFP: regulation of food intake and fat selection. Horm Metab Res (2013) 45:967-74. doi:10.1055/s-0033-1353181
    • (2013) Horm Metab Res , vol.45 , pp. 967-974
    • Primeaux, S.D.1    Barnes, M.J.2    Braymer, H.D.3
  • 47
    • 62949085357 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of the first non-mammalian 26RFa/QRFP orthologue in goldfish, Carassius auratus
    • doi:10.1016/j.mce.2009.01.009
    • Liu Y, Zhang Y, Li S, Huang W, Liu X, Lu D, et al. Molecular cloning and functional characterization of the first non-mammalian 26RFa/QRFP orthologue in goldfish, Carassius auratus. Mol Cell Endocrinol (2009) 303:82-90. doi:10.1016/j.mce.2009.01.009
    • (2009) Mol Cell Endocrinol , vol.303 , pp. 82-90
    • Liu, Y.1    Zhang, Y.2    Li, S.3    Huang, W.4    Liu, X.5    Lu, D.6
  • 48
    • 84901412429 scopus 로고    scopus 로고
    • Molecular evolution and function of 26RFa/QRFP and its cognate receptor
    • doi:10.1530/JME-13-0207
    • Ukena K, Osugi T, Leprince J, Vaudry H, Tsutsui K. Molecular evolution and function of 26RFa/QRFP and its cognate receptor. J Mol Endocrinol (2014) 52(3):T119-31. doi:10.1530/JME-13-0207
    • (2014) J Mol Endocrinol , vol.52 , Issue.3
    • Ukena, K.1    Osugi, T.2    Leprince, J.3    Vaudry, H.4    Tsutsui, K.5
  • 50
    • 0033918243 scopus 로고    scopus 로고
    • Alternative role for prolactin-releasing peptide in the regulation of food intake
    • doi:10.1038/76597
    • Lawrence CB, Celsi F, Brennand J, Luckman SM. Alternative role for prolactin-releasing peptide in the regulation of food intake. Nat Neurosci (2000) 3:645-6. doi:10.1038/76597
    • (2000) Nat Neurosci , vol.3 , pp. 645-646
    • Lawrence, C.B.1    Celsi, F.2    Brennand, J.3    Luckman, S.M.4
  • 51
    • 0037322922 scopus 로고    scopus 로고
    • Prolactin-releasing peptide and its homolog RFRP-1 act in hypothalamus but not in anterior pituitary gland to stimulate stress hormone secretion
    • doi:10.1385/ENDO:20:1-2:59
    • Samson WK, Keown C, Samson CK, Samson HW, Lane B, Baker JR, et al. Prolactin-releasing peptide and its homolog RFRP-1 act in hypothalamus but not in anterior pituitary gland to stimulate stress hormone secretion. Endocrine (2003) 20:59-66. doi:10.1385/ENDO:20:1-2:59
    • (2003) Endocrine , vol.20 , pp. 59-66
    • Samson, W.K.1    Keown, C.2    Samson, C.K.3    Samson, H.W.4    Lane, B.5    Baker, J.R.6
  • 52
    • 34547114008 scopus 로고    scopus 로고
    • RFamide peptides inhibit the expression of melanotropin and growth hormone genes in the pituitary of an Agnathan, the sea lamprey, Petromyzon marinus
    • doi:10.1210/en.2007-0356
    • Moriyama S, Kasahara M, Amiya N, Takahashi A, Amano M, Sower SA, et al. RFamide peptides inhibit the expression of melanotropin and growth hormone genes in the pituitary of an Agnathan, the sea lamprey, Petromyzon marinus. Endocrinology (2007) 148:3740-9. doi:10.1210/en.2007-0356
    • (2007) Endocrinology , vol.148 , pp. 3740-3749
    • Moriyama, S.1    Kasahara, M.2    Amiya, N.3    Takahashi, A.4    Amano, M.5    Sower, S.A.6
  • 53
    • 21044438894 scopus 로고    scopus 로고
    • Origin of the prolactin-releasing hormone (PRLH) receptors: evidence of coevolution between PRLH and a redundant neuropeptide Y receptor during vertebrate evolution
    • doi:10.1016/j.ygeno.2005.02.007
    • Lagerstrom MC, Fredriksson R, Bjarnadottir TK, Fridmanis D, Holmquist T, Andersson J, et al. Origin of the prolactin-releasing hormone (PRLH) receptors: evidence of coevolution between PRLH and a redundant neuropeptide Y receptor during vertebrate evolution. Genomics (2005) 85:688-703. doi:10.1016/j.ygeno.2005.02.007
    • (2005) Genomics , vol.85 , pp. 688-703
    • Lagerstrom, M.C.1    Fredriksson, R.2    Bjarnadottir, T.K.3    Fridmanis, D.4    Holmquist, T.5    Andersson, J.6
  • 54
    • 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
    • Nassel 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
    • Nassel, D.R.1    Wegener, C.2
  • 55
    • 0036093385 scopus 로고    scopus 로고
    • A homolog of mammalian PRL-releasing peptide (fish arginyl-phenylalanyl-amide peptide) is a major hypothalamic peptide of PRL release in teleost fish
    • doi:10.1210/endo.143.6.8744
    • Moriyama S, Ito T, Takahashi A, Amano M, Sower SA, Hirano T, et al. A homolog of mammalian PRL-releasing peptide (fish arginyl-phenylalanyl-amide peptide) is a major hypothalamic peptide of PRL release in teleost fish. Endocrinology (2002) 143:2071-9. doi:10.1210/endo.143.6.8744
    • (2002) Endocrinology , vol.143 , pp. 2071-2079
    • Moriyama, S.1    Ito, T.2    Takahashi, A.3    Amano, M.4    Sower, S.A.5    Hirano, T.6
  • 56
    • 33751161687 scopus 로고    scopus 로고
    • Prolactin-releasing peptide, food intake, and hydromineral balance in goldfish
    • doi:10.1152/ajpregu.00129.2006
    • Kelly SP, Peter RE. Prolactin-releasing peptide, food intake, and hydromineral balance in goldfish. Am J Physiol Regul Integr Comp Physiol (2006) 291:R1474-81. doi:10.1152/ajpregu.00129.2006
    • (2006) Am J Physiol Regul Integr Comp Physiol , vol.291
    • Kelly, S.P.1    Peter, R.E.2
  • 57
    • 0035860778 scopus 로고    scopus 로고
    • The metastasis suppressor gene KiSS-1 encodes kisspeptins, the natural ligands of the orphan G protein-coupled receptor GPR54
    • doi:10.1074/jbc.M104847200
    • Kotani M, Detheux M, Vandenbogaerde A, Communi D, Vanderwinden JM, Le Poul E, et al. The metastasis suppressor gene KiSS-1 encodes kisspeptins, the natural ligands of the orphan G protein-coupled receptor GPR54. J Biol Chem (2001) 276:34631-6. doi:10.1074/jbc.M104847200
    • (2001) J Biol Chem , vol.276 , pp. 34631-34636
    • Kotani, M.1    Detheux, M.2    Vandenbogaerde, A.3    Communi, D.4    Vanderwinden, J.M.5    Le Poul, E.6
  • 58
    • 0141814637 scopus 로고    scopus 로고
    • Hypogonadotropic hypogonadism due to loss of function of the KiSS1-derived peptide receptor GPR54
    • doi:10.1073/pnas.1834399100
    • de Roux N, Genin E, Carel JC, Matsuda F, Chaussain JL, Milgrom E. Hypogonadotropic hypogonadism due to loss of function of the KiSS1-derived peptide receptor GPR54. Proc Natl Acad Sci U S A (2003) 100:10972-6. doi:10.1073/pnas.1834399100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10972-10976
    • de Roux, N.1    Genin, E.2    Carel, J.C.3    Matsuda, F.4    Chaussain, J.L.5    Milgrom, E.6
  • 59
    • 66649090350 scopus 로고    scopus 로고
    • Molecular evolution of multiple forms of kisspeptins and GPR54 receptors in vertebrates
    • doi:10.1210/en.2008-1679
    • Lee YR, Tsunekawa K, Moon MJ, Um HN, Hwang JI, Osugi T, et al. Molecular evolution of multiple forms of kisspeptins and GPR54 receptors in vertebrates. Endocrinology (2009) 150:2837-46. doi:10.1210/en.2008-1679
    • (2009) Endocrinology , vol.150 , pp. 2837-2846
    • Lee, Y.R.1    Tsunekawa, K.2    Moon, M.J.3    Um, H.N.4    Hwang, J.I.5    Osugi, T.6
  • 60
    • 84874382571 scopus 로고    scopus 로고
    • Comparative evolutionary histories of kisspeptins and kisspeptin receptors in vertebrates reveal both parallel and divergent features
    • doi:10.3389/fendo.2012.00173
    • Pasquier J, Lafont AG, Tostivint H, Vaudry H, Rousseau K, Dufour S. Comparative evolutionary histories of kisspeptins and kisspeptin receptors in vertebrates reveal both parallel and divergent features. Front Endocrinol (2012) 3:173. doi:10.3389/fendo.2012.00173
    • (2012) Front Endocrinol , vol.3 , pp. 173
    • Pasquier, J.1    Lafont, A.G.2    Tostivint, H.3    Vaudry, H.4    Rousseau, K.5    Dufour, S.6
  • 61
    • 79953184987 scopus 로고    scopus 로고
    • Organization of two independent kisspeptin systems derived from evolutionary-ancient kiss genes in the brain of zebrafish
    • doi:10.1210/en.2010-0948
    • Servili A, Le Page Y, Leprince J, Caraty A, Escobar S, Parhar IS, et al. Organization of two independent kisspeptin systems derived from evolutionary-ancient kiss genes in the brain of zebrafish. Endocrinology (2011) 152:1527-40. doi:10.1210/en.2010-0948
    • (2011) Endocrinology , vol.152 , pp. 1527-1540
    • Servili, A.1    Le Page, Y.2    Leprince, J.3    Caraty, A.4    Escobar, S.5    Parhar, I.S.6
  • 63
    • 84884186618 scopus 로고    scopus 로고
    • Functional significance of GnRH and kisspeptin, and their cognate receptors in teleost reproduction
    • doi:10.3389/fendo.2013.00024
    • Gopurappilly R, Ogawa S, Parhar IS. Functional significance of GnRH and kisspeptin, and their cognate receptors in teleost reproduction. Front Endocrinol (2013) 4:24. doi:10.3389/fendo.2013.00024
    • (2013) Front Endocrinol , vol.4 , pp. 24
    • Gopurappilly, R.1    Ogawa, S.2    Parhar, I.S.3
  • 65
    • 33751504034 scopus 로고    scopus 로고
    • The neuropeptide SIFamide modulates sexual behavior in Drosophila
    • doi:10.1016/j.bbrc.2006.11.030
    • Terhzaz S, Rosay P, Goodwin SF, Veenstra JA. The neuropeptide SIFamide modulates sexual behavior in Drosophila. Biochem Biophys Res Commun (2007) 352:305-10. doi:10.1016/j.bbrc.2006.11.030
    • (2007) Biochem Biophys Res Commun , vol.352 , pp. 305-310
    • Terhzaz, S.1    Rosay, P.2    Goodwin, S.F.3    Veenstra, J.A.4
  • 66
    • 84883774240 scopus 로고    scopus 로고
    • From gonadotropin-inhibitory hormone to SIFamides: are echinoderm SALMFamides the "missing link" in a bilaterian family of neuropeptides that regulate reproductive processes?
    • doi:10.1016/j.ygcen.2013.08.009
    • Elphick MR. From gonadotropin-inhibitory hormone to SIFamides: are echinoderm SALMFamides the "missing link" in a bilaterian family of neuropeptides that regulate reproductive processes? Gen Comp Endocrinol (2013) 193:229-33. doi:10.1016/j.ygcen.2013.08.009
    • (2013) Gen Comp Endocrinol , vol.193 , pp. 229-233
    • Elphick, M.R.1
  • 67
    • 2242464840 scopus 로고    scopus 로고
    • The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins
    • doi:10.1126/science.1080049
    • Dehal P, Satou Y, Campbell RK, Chapman J, Degnan B, De Tomaso A, et al. The draft genome of Ciona intestinalis: insights into chordate and vertebrate origins. Science (2002) 298:2157-67. doi:10.1126/science.1080049
    • (2002) Science , vol.298 , pp. 2157-2167
    • Dehal, P.1    Satou, Y.2    Campbell, R.K.3    Chapman, J.4    Degnan, B.5    De Tomaso, A.6
  • 68
    • 45749086679 scopus 로고    scopus 로고
    • The amphioxus genome and the evolution of the chordate karyotype
    • doi:10.1038/nature06967
    • Putnam NH, Butts T, Ferrier DE, Furlong RF, Hellsten U, Kawashima T, et al. The amphioxus genome and the evolution of the chordate karyotype. Nature (2008) 453:1064-71. doi:10.1038/nature06967
    • (2008) Nature , vol.453 , pp. 1064-1071
    • Putnam, N.H.1    Butts, T.2    Ferrier, D.E.3    Furlong, R.F.4    Hellsten, U.5    Kawashima, T.6
  • 69
    • 46449117934 scopus 로고    scopus 로고
    • cDNA sequences for transcription factors and signaling proteins of the hemichordate Saccoglossus kowalevskii: efficacy of the expressed sequence tag (EST) approach for evolutionary and developmental studies of a new organism
    • doi:10.2307/25470670
    • Freeman RM Jr, Wu M, Cordonnier-Pratt MM, Pratt LH, Gruber CE, Smith M, et al. cDNA sequences for transcription factors and signaling proteins of the hemichordate Saccoglossus kowalevskii: efficacy of the expressed sequence tag (EST) approach for evolutionary and developmental studies of a new organism. Biol Bull (2008) 214:284-302. doi:10.2307/25470670
    • (2008) Biol Bull , vol.214 , pp. 284-302
    • Freeman Jr., R.M.1    Wu, M.2    Cordonnier-Pratt, M.M.3    Pratt, L.H.4    Gruber, C.E.5    Smith, M.6
  • 71
    • 84908618156 scopus 로고    scopus 로고
    • SALMFamide salmagundi: the biology of a neuropeptide family in echinoderms
    • doi:10.1016/j.ygcen.2014.02.012
    • Elphick MR. SALMFamide salmagundi: the biology of a neuropeptide family in echinoderms. Gen Comp Endocrinol (2014). doi:10.1016/j.ygcen.2014.02.012
    • (2014) Gen Comp Endocrinol
    • Elphick, M.R.1
  • 72
    • 84874918531 scopus 로고    scopus 로고
    • The evolution and diversity of SALMFamide neuropeptides
    • doi:10.1371/journal.pone.0059076
    • Elphick MR, Achhala S, Martynyuk N. The evolution and diversity of SALMFamide neuropeptides. PLoS One (2013) 8:e59076. doi:10.1371/journal.pone.0059076
    • (2013) PLoS One , vol.8
    • Elphick, M.R.1    Achhala, S.2    Martynyuk, N.3
  • 74
    • 0021164983 scopus 로고
    • Isolation and characterization of reptilian insulin, glucagon, and pancreatic polypeptide: complete amino acid sequence of alligator (Alligator mississippiensis) insulin and pancreatic polypeptide
    • doi:10.1016/0016-6480(84)90135-7
    • Lance V, Hamilton JW, Rouse JB, Kimmel JR, Pollock HG. Isolation and characterization of reptilian insulin, glucagon, and pancreatic polypeptide: complete amino acid sequence of alligator (Alligator mississippiensis) insulin and pancreatic polypeptide. Gen Comp Endocrinol (1984) 55:112-24. doi:10.1016/0016-6480(84)90135-7
    • (1984) Gen Comp Endocrinol , vol.55 , pp. 112-124
    • Lance, V.1    Hamilton, J.W.2    Rouse, J.B.3    Kimmel, J.R.4    Pollock, H.G.5
  • 75
    • 84891053642 scopus 로고    scopus 로고
    • Neuropeptides and polypeptide hormones in echinoderms: new insights from analysis of the transcriptome of the sea cucumber Apostichopus japonicus
    • doi:10.1016/j.ygcen.2013.12.002
    • Rowe ML, Achhala S, Elphick MR. Neuropeptides and polypeptide hormones in echinoderms: new insights from analysis of the transcriptome of the sea cucumber Apostichopus japonicus. Gen Comp Endocrinol (2014) 197:43-55. doi:10.1016/j.ygcen.2013.12.002
    • (2014) Gen Comp Endocrinol , vol.197 , pp. 43-55
    • Rowe, M.L.1    Achhala, S.2    Elphick, M.R.3
  • 76
    • 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, Gonzalez de Valdivia E, 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    Gonzalez de Valdivia, E.5    Williamson, M.6
  • 77
    • 0028097620 scopus 로고
    • Evolution of the gastrointestinal endocrine system (with special reference to gastrin and CCK)
    • doi:10.1016/S0950-351X(05)80224-1
    • Dimaline R, Dockray GJ. Evolution of the gastrointestinal endocrine system (with special reference to gastrin and CCK). Baillieres Clin Endocrinol Metab (1994) 8:1-24. doi:10.1016/S0950-351X(05)80224-1
    • (1994) Baillieres Clin Endocrinol Metab , vol.8 , pp. 1-24
    • Dimaline, R.1    Dockray, G.J.2
  • 78
    • 34447275485 scopus 로고    scopus 로고
    • The biology of cholecystokinin and gastrin peptides
    • doi:10.2174/156802607780960483
    • Rehfeld JF, Friis-Hansen L, Goetze JP, Hansen TV. The biology of cholecystokinin and gastrin peptides. Curr Top Med Chem (2007) 7:1154-65. doi:10.2174/156802607780960483
    • (2007) Curr Top Med Chem , vol.7 , pp. 1154-1165
    • Rehfeld, J.F.1    Friis-Hansen, L.2    Goetze, J.P.3    Hansen, T.V.4
  • 79
    • 0025261194 scopus 로고
    • Cionin: a disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis
    • Johnsen AH, Rehfeld JF. Cionin: a disulfotyrosyl hybrid of cholecystokinin and gastrin from the neural ganglion of the protochordate Ciona intestinalis. J Biol Chem (1990) 265:3054-8.
    • (1990) J Biol Chem , vol.265 , pp. 3054-3058
    • Johnsen, A.H.1    Rehfeld, J.F.2
  • 80
    • 0022996473 scopus 로고
    • Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin
    • doi:10.1126/science.3749893
    • Nachman RJ, Holman GM, Haddon WF, Ling N. Leucosulfakinin, a sulfated insect neuropeptide with homology to gastrin and cholecystokinin. Science (1986) 234:71-3. doi:10.1126/science.3749893
    • (1986) Science , vol.234 , pp. 71-73
    • Nachman, R.J.1    Holman, G.M.2    Haddon, W.F.3    Ling, N.4
  • 81
    • 75149164801 scopus 로고    scopus 로고
    • Evolution of gastrointestinal hormones: the cholecystokinin/gastrin family
    • doi:10.1097/MED.0b013e328334e535
    • Baldwin GS, Patel O, Shulkes A. Evolution of gastrointestinal hormones: the cholecystokinin/gastrin family. Curr Opin Endocrinol Diabetes Obes (2010) 17:77-88. doi:10.1097/MED.0b013e328334e535
    • (2010) Curr Opin Endocrinol Diabetes Obes , vol.17 , pp. 77-88
    • Baldwin, G.S.1    Patel, O.2    Shulkes, A.3
  • 82
    • 44249103225 scopus 로고    scopus 로고
    • Discovery of a cholecystokinin-gastrin-like signaling system in nematodes
    • doi:10.1210/en.2007-1772
    • Janssen T, Meelkop E, Lindemans M, Verstraelen K, Husson SJ, Temmerman L, et al. Discovery of a cholecystokinin-gastrin-like signaling system in nematodes. Endocrinology (2008) 149:2826-39. doi:10.1210/en.2007-1772
    • (2008) Endocrinology , vol.149 , pp. 2826-2839
    • Janssen, T.1    Meelkop, E.2    Lindemans, M.3    Verstraelen, K.4    Husson, S.J.5    Temmerman, L.6
  • 83
    • 0028929881 scopus 로고
    • Processing of the L5-67 precursor peptide and characterization of LUQIN in the LUQ neurons of Aplysia californica
    • doi:10.1016/0196-9781(94)00140-5
    • Aloyz RS, DesGroseillers L. Processing of the L5-67 precursor peptide and characterization of LUQIN in the LUQ neurons of Aplysia californica. Peptides (1995) 16:331-8. doi:10.1016/0196-9781(94)00140-5
    • (1995) Peptides , vol.16 , pp. 331-338
    • Aloyz, R.S.1    DesGroseillers, L.2
  • 84
    • 0023020753 scopus 로고
    • Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones
    • doi:10.1073/pnas.83.24.9817
    • Grimmelikhuijzen CJ, Graff D. Isolation of pyroGlu-Gly-Arg-Phe-NH2 (Antho-RFamide), a neuropeptide from sea anemones. Proc Natl Acad Sci U S A (1986) 83:9817-21. doi:10.1073/pnas.83.24.9817
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 9817-9821
    • Grimmelikhuijzen, C.J.1    Graff, D.2
  • 85
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • doi:10.1124/mol.63.6.1256
    • Fredriksson R, Lagerstrom MC, Lundin LG, Schioth HB. The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints. Mol Pharmacol (2003) 63:1256-72. doi:10.1124/mol.63.6.1256
    • (2003) Mol Pharmacol , vol.63 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.G.3    Schioth, H.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.