메뉴 건너뛰기




Volumn 1220, Issue 1, 2011, Pages 34-48

Evolution of POMC: Origin, phylogeny, posttranslational processing, and the melanocortins

Author keywords

ACTH; Evolution; Melanocortins; POMC; MSH; endorphin

Indexed keywords

ALPHA INTERMEDIN; BETA ENDORPHIN; BETA INTERMEDIN; CORTICOTROPIN; GAMMA INTERMEDIN; MELANOCORTIN; NOCICEPTIN RECEPTOR; OPIATE; OPIATE RECEPTOR; PROOPIOMELANOCORTIN;

EID: 79952483291     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2010.05928.x     Document Type: Article
Times cited : (105)

References (116)
  • 1
    • 0019268826 scopus 로고
    • Structure and biosynthesis of pro-adrenocorticotropin/endorphin and related peptides
    • Eipper, B.A. & R.E. Mains 1980. Structure and biosynthesis of pro-adrenocorticotropin/endorphin and related peptides. Endocr. Rev. 1: 1-27.
    • (1980) Endocr. Rev. , vol.1 , pp. 1-27
    • Eipper, B.A.1    Mains, R.E.2
  • 2
    • 0036629570 scopus 로고    scopus 로고
    • Analyzing the evolution of the opioid/orphanin gene family
    • Dores, R.M. et al 2002. Analyzing the evolution of the opioid/orphanin gene family. Mass Spectrometry Rev. 21: 220-243.
    • (2002) Mass Spectrometry Rev. , vol.21 , pp. 220-243
    • Dores, R.M.1
  • 3
    • 77956286755 scopus 로고    scopus 로고
    • Concomitant duplication of the opioid peptide and receptor genes before the origin of jawed vertebrates
    • Sundstrom, G. et al 2010. Concomitant duplication of the opioid peptide and receptor genes before the origin of jawed vertebrates. PLoS One. 5: e10512.
    • (2010) PLoS One , vol.5
    • Sundstrom, G.1
  • 4
    • 0014237181 scopus 로고
    • Evolution from fish to mammals by gene duplication
    • Ohno, S. et al 1968. Evolution from fish to mammals by gene duplication. Hereditas 59: 169-187.
    • (1968) Hereditas , vol.59 , pp. 169-187
    • Ohno, S.1
  • 5
    • 0027284770 scopus 로고
    • Evolution of the vertebrate genome as reflected in paralogous chromosomal regions in man and the house mouse
    • Lundin, L.G. 1993. Evolution of the vertebrate genome as reflected in paralogous chromosomal regions in man and the house mouse. Genomics 16: 1-19.
    • (1993) Genomics , vol.16 , pp. 1-19
    • Lundin, L.G.1
  • 6
    • 0028598861 scopus 로고
    • Gene duplications and the origins of vertebrate development
    • Holland, P.W. et al 1994. Gene duplications and the origins of vertebrate development. Development (Suppl.): 125-133.
    • (1994) Development , Issue.SUPPL. , pp. 125-133
    • Holland, P.W.1
  • 7
    • 77954567591 scopus 로고    scopus 로고
    • Evolution of the opioid/ORL-1 receptor gene family
    • McClendon, J. et al 2010. Evolution of the opioid/ORL-1 receptor gene family. Ann. N.Y. Acad. Sci. 1200: 85-94.
    • (2010) Ann. N.Y. Acad. Sci. , vol.1200 , pp. 85-94
    • Mcclendon, J.1
  • 8
    • 0020048094 scopus 로고
    • Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin
    • Noda, M. et al 1982. Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin. Nature 295: 202-206.
    • (1982) Nature , vol.295 , pp. 202-206
    • Noda, M.1
  • 9
    • 0019977784 scopus 로고
    • Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor
    • Kakidani, H. et al 1982. Cloning and sequence analysis of cDNA for porcine beta-neo-endorphin/dynorphin precursor. Nature 298: 245-249.
    • (1982) Nature , vol.298 , pp. 245-249
    • Kakidani, H.1
  • 10
    • 0036315118 scopus 로고    scopus 로고
    • Identification of a fourth opioid core sequence in a prodynorphin cDNA cloned from the brain of the Amphibian, Bufo marinus: deciphering the evolution of prodynorphin and proenkephalin
    • Danielson, P. et al 2002. Identification of a fourth opioid core sequence in a prodynorphin cDNA cloned from the brain of the Amphibian, Bufo marinus: deciphering the evolution of prodynorphin and proenkephalin. Neuroendocrinology 76: 55-62.
    • (2002) Neuroendocrinology , vol.76 , pp. 55-62
    • Danielson, P.1
  • 11
    • 2542590123 scopus 로고    scopus 로고
    • Reconstructing the evolution of the prodynorphin gene: cloning of prodynorphin cDNAs from the brain of the Australian Lungfish and the African Lungfish
    • Dores, R.M. et al 2004. Reconstructing the evolution of the prodynorphin gene: cloning of prodynorphin cDNAs from the brain of the Australian Lungfish and the African Lungfish. Neuroendocrinology 79: 185-196.
    • (2004) Neuroendocrinology , vol.79 , pp. 185-196
    • Dores, R.M.1
  • 12
    • 0346101740 scopus 로고    scopus 로고
    • Cloning and characterization of Xen-dorphin prohormone from Xenopus laevis: a new opioid-like prohormone distinct from proenkephalin and prodynorphin
    • Pattee, P. et al 2003. Cloning and characterization of Xen-dorphin prohormone from Xenopus laevis: a new opioid-like prohormone distinct from proenkephalin and prodynorphin. J. Biol. Chem. 278: 53098-53104.
    • (2003) J. Biol. Chem. , vol.278 , pp. 53098-53104
    • Pattee, P.1
  • 13
    • 33645412356 scopus 로고    scopus 로고
    • Trends in the evolution of the prodynorphin gene in teleosts: cloning of eel and tilapia prodynorphin cDNAs
    • Alrubaian, J. et al 2006. Trends in the evolution of the prodynorphin gene in teleosts: cloning of eel and tilapia prodynorphin cDNAs. Peptides 27: 797-804.
    • (2006) Peptides , vol.27 , pp. 797-804
    • Alrubaian, J.1
  • 14
    • 58149457376 scopus 로고    scopus 로고
    • Binding studies of novel non-mammalian enkephalins, structures predicted from frog and lungfish brain cDNA sequences
    • Bojnik, E. et al 2009. Binding studies of novel non-mammalian enkephalins, structures predicted from frog and lungfish brain cDNA sequences. Neuropharmacology 158: 867-874.
    • (2009) Neuropharmacology , vol.158 , pp. 867-874
    • Bojnik, E.1
  • 15
    • 0029166509 scopus 로고
    • Isolation and structure of the endogenous agonist of opioid receptor-like ORL1 receptor
    • Meunier, J.C. et al 1995. Isolation and structure of the endogenous agonist of opioid receptor-like ORL1 receptor. Nature 377: 532-535.
    • (1995) Nature , vol.377 , pp. 532-535
    • Meunier, J.C.1
  • 16
    • 0028971215 scopus 로고
    • Orphanin FQ: a neuropeptide that activates an opioidlike G protein-coupled receptor
    • Reinscheid, R.K. et al 1995. Orphanin FQ: a neuropeptide that activates an opioidlike G protein-coupled receptor. Science 270: 792-794.
    • (1995) Science , vol.270 , pp. 792-794
    • Reinscheid, R.K.1
  • 17
    • 0029738628 scopus 로고    scopus 로고
    • Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene
    • Mollereau, C. et al 1996. Structure, tissue distribution, and chromosomal localization of the prepronociceptin gene. Proc. Natl. Acad. Sci. U.S.A. 93: 8666-8670.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8666-8670
    • Mollereau, C.1
  • 18
    • 0035933850 scopus 로고    scopus 로고
    • Sturgeon orphanin, a molecular "fossil" that bridges the gap between the opioids and orphanin FQ/nociceptin
    • Danielson, P.B. et al 2001. Sturgeon orphanin, a molecular "fossil" that bridges the gap between the opioids and orphanin FQ/nociceptin. J. Biol. Chem. 276: 22114-22119.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22114-22119
    • Danielson, P.B.1
  • 19
    • 0018346407 scopus 로고
    • Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor
    • Nakanishi, S. et al 1979. Nucleotide sequence of cloned cDNA for bovine corticotropin-beta-lipotropin precursor. Nature 278: 423-427.
    • (1979) Nature , vol.278 , pp. 423-427
    • Nakanishi, S.1
  • 20
    • 33845572889 scopus 로고    scopus 로고
    • Studies on the physiological studies of the melanocortin system
    • Cone, R.D. 2006. Studies on the physiological studies of the melanocortin system. Endocrine Rev. 27: 736-749.
    • (2006) Endocrine Rev. , vol.27 , pp. 736-749
    • Cone, R.D.1
  • 21
    • 18144389768 scopus 로고    scopus 로고
    • Trends in the evolution of the proopiomelanocortin gene
    • Dores, R.M. & S. Lecaude 2005. Trends in the evolution of the proopiomelanocortin gene. Gen. Comp. Endocrinol. 142: 81-93.
    • (2005) Gen. Comp. Endocrinol. , vol.142 , pp. 81-93
    • Dores, R.M.1    Lecaude, S.2
  • 22
    • 33744968831 scopus 로고    scopus 로고
    • Occurance of two functionally distinct proopiomelanocortin genes in all modern lampreys
    • Takahashi, A. et al 2006. Occurance of two functionally distinct proopiomelanocortin genes in all modern lampreys. Gen. Comp. Endocrinol. 148: 72-78.
    • (2006) Gen. Comp. Endocrinol. , vol.148 , pp. 72-78
    • Takahashi, A.1
  • 23
    • 0029100803 scopus 로고
    • The appearance of proopiomelanocortin early in vertebrate evolution: cloning and sequencing of POMC from a lamprey pituitary cDNA library
    • Henig, J.A. et al 1995. The appearance of proopiomelanocortin early in vertebrate evolution: cloning and sequencing of POMC from a lamprey pituitary cDNA library. Gen. Comp. Endocrinol. 99: 137-144.
    • (1995) Gen. Comp. Endocrinol. , vol.99 , pp. 137-144
    • Henig, J.A.1
  • 24
    • 0029142971 scopus 로고
    • Melanotropin and coritcotropin are encoded on two distinct genes in the lamprey, the earliest evolved extant vertebrate
    • Takahashi, A. et al 1995. Melanotropin and coritcotropin are encoded on two distinct genes in the lamprey, the earliest evolved extant vertebrate. Biochem. Biophys. Res. Commun. 213: 490-496.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 490-496
    • Takahashi, A.1
  • 25
    • 57749184792 scopus 로고    scopus 로고
    • Timing of genomic duplications relative to the origin of the vertebrates: did cyclostomes diverge before or after?
    • Kuraku, S. et al 2009. Timing of genomic duplications relative to the origin of the vertebrates: did cyclostomes diverge before or after? Mol. Biol. Evol. 26: 47-59.
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 47-59
    • Kuraku, S.1
  • 26
    • 77953455738 scopus 로고    scopus 로고
    • End-devonian extinction and a bottleneck in the early evolution of modern jawed vertebrates
    • Sallan, L.C. & M.I. Coates 2010. End-devonian extinction and a bottleneck in the early evolution of modern jawed vertebrates. Proc. Natl. Acad. Sci. U.S.A. 122: 265-281.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.122 , pp. 265-281
    • Sallan, L.C.1    Coates, M.I.2
  • 27
    • 0033040338 scopus 로고    scopus 로고
    • A newly characterized melanotropin in proopiomelanocortin in pituitaries of an Elasmobranch, Squalus acanthias
    • Amemiya, Y. et al 1999. A newly characterized melanotropin in proopiomelanocortin in pituitaries of an Elasmobranch, Squalus acanthias. Gen. Comp. Endocrinol. 114: 387-395.
    • (1999) Gen. Comp. Endocrinol. , vol.114 , pp. 387-395
    • Amemiya, Y.1
  • 28
    • 0041663483 scopus 로고    scopus 로고
    • Presence of the δ-MSH sequence in a proopiomelanocortin cDNA cloned from the pituitary of the galeoid shark, Heterodontus portusjacksoni
    • Dores, R.M. et al 2003. Presence of the δ-MSH sequence in a proopiomelanocortin cDNA cloned from the pituitary of the galeoid shark, Heterodontus portusjacksoni. Gen. Comp. Endocrinol. 133: 71-79.
    • (2003) Gen. Comp. Endocrinol , vol.133 , pp. 71-79
    • Dores, R.M.1
  • 29
    • 0034006668 scopus 로고    scopus 로고
    • Molecular cloning of proopiomelanocortin cDNA from an elasmobranch, Dasyatis akajei
    • Amemiya, Y., A. Takahashi, N. Suzuki, et al 2000. Molecular cloning of proopiomelanocortin cDNA from an elasmobranch, Dasyatis akajei. Gen. Comp. Endocrinol. 118: 105-112.
    • (2000) Gen. Comp. Endocrinol , vol.118 , pp. 105-112
    • Amemiya, Y.1    Takahashi, A.2    Suzuki, N.3
  • 30
    • 0344393088 scopus 로고    scopus 로고
    • Molecular cloning of proopiomelanocortin cDNA in the ratfish a holocephalan
    • Takahashi, A. et al 2004. Molecular cloning of proopiomelanocortin cDNA in the ratfish a holocephalan. Gen. Comp. Endocrinol. 135: 159-165.
    • (2004) Gen. Comp. Endocrinol. , vol.135 , pp. 159-165
    • Takahashi, A.1
  • 31
    • 0003524487 scopus 로고
    • rd Edition
    • John Wiley & Sons. New York
    • rd Edition. John Wiley & Sons. New York
    • (1994)
    • Nelson, J.S.1
  • 32
    • 85040870915 scopus 로고
    • Vertebrate Paleontology and Evolution
    • W.H. Freeman Press. New York
    • Carroll, R.L. 1988. Vertebrate Paleontology and Evolution. W.H. Freeman Press. New York
    • (1988)
    • Carroll, R.L.1
  • 33
    • 0035542539 scopus 로고    scopus 로고
    • The sister-group of the Teleostei: consensus and disagreements
    • Arratia, G. 2001. The sister-group of the Teleostei: consensus and disagreements. J. Vertebrate Paleontology 21: 767-773.
    • (2001) J. Vertebrate Paleontology , vol.21 , pp. 767-773
    • Arratia, G.1
  • 34
    • 0345283045 scopus 로고    scopus 로고
    • Characterizing a proopiomelanocortin cDNA cloned from the brain of the Bichir, Polypterus senegalus: evaluating phylogenetic relationships among ray-finned fish
    • Bagrosky, B. et al 2003. Characterizing a proopiomelanocortin cDNA cloned from the brain of the Bichir, Polypterus senegalus: evaluating phylogenetic relationships among ray-finned fish. Gen. Comp. Endocrinol. 134: 339-346.
    • (2003) Gen. Comp. Endocrinol , vol.134 , pp. 339-346
    • Bagrosky, B.1
  • 35
    • 0031566179 scopus 로고    scopus 로고
    • Sturgeon proopiomelanocortin has a remnant of γ-melanotropin
    • Ameniya, Y. et al 1997. Sturgeon proopiomelanocortin has a remnant of γ-melanotropin. Biochem. Biophys. Res. Commun. 230: 452-456.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 452-456
    • Ameniya, Y.1
  • 36
    • 0032885669 scopus 로고    scopus 로고
    • Cloning of a second proopiomelanocortin cDNA from the pituitary of the sturgeon, Acipenser transmontanus
    • Alrubaian, J. et al. 1999. Cloning of a second proopiomelanocortin cDNA from the pituitary of the sturgeon, Acipenser transmontanus. Peptides 20: 431-436.
    • (1999) Peptides , vol.20 , pp. 431-436
    • Alrubaian, J.1
  • 37
    • 0032731706 scopus 로고    scopus 로고
    • Duplication of the POMC gene in the paddlefish (Polyodon spathula): analysis of γ-MSH, ACTH, and β-endorphin regions of ray-finned fish POMC
    • Danielson, P.B. et al 1999. Duplication of the POMC gene in the paddlefish (Polyodon spathula): analysis of γ-MSH, ACTH, and β-endorphin regions of ray-finned fish POMC. Gen. Comp. Endocrinol. 116: 164-177.
    • (1999) Gen. Comp. Endocrinol , vol.116 , pp. 164-177
    • Danielson, P.B.1
  • 38
    • 0021684777 scopus 로고
    • Biosynthesis, processing and release of pro-opiomelanocortin related peptides in the intermediate lobe of the pituitary gland of the frog (Rana ridibunda)
    • Vaudry, H. et al 1984. Biosynthesis, processing and release of pro-opiomelanocortin related peptides in the intermediate lobe of the pituitary gland of the frog (Rana ridibunda). Peptides 5: 905-912.
    • (1984) Peptides , vol.5 , pp. 905-912
    • Vaudry, H.1
  • 39
    • 0037836013 scopus 로고    scopus 로고
    • Neuropepide-processing carboxypeptidases
    • Wei, S. et al 2003. Neuropepide-processing carboxypeptidases. Life Sci. 73: 655-662.
    • (2003) Life Sci. , vol.73 , pp. 655-662
    • Wei, S.1
  • 41
    • 0038718992 scopus 로고    scopus 로고
    • Evaluating the radiation of the POMC gene in teleost: characterization of American eel POMC
    • Alrubaian, J. et al 2003. Evaluating the radiation of the POMC gene in teleost: characterization of American eel POMC. Gen. Comp. Endocrinol. 132: 384-390.
    • (2003) Gen. Comp. Endocrinol. , vol.132 , pp. 384-390
    • Alrubaian, J.1
  • 42
    • 0032566364 scopus 로고    scopus 로고
    • Cloning and expression of two proopiomelanocortin mRNAs in the common carp (Cyprinus carpio L.)
    • Arends, R.J. et al 1998. Cloning and expression of two proopiomelanocortin mRNAs in the common carp (Cyprinus carpio L.). Mol. Cell. Endocrinol. 143: 23-31.
    • (1998) Mol. Cell. Endocrinol. , vol.143 , pp. 23-31
    • Arends, R.J.1
  • 43
    • 0345599261 scopus 로고    scopus 로고
    • Identification of two proopiomelanocortin genes in zebrafish (Danio rerio)
    • Gonzalez-Nunez, V. et al 2003. Identification of two proopiomelanocortin genes in zebrafish (Danio rerio). Brain Res. Mol. Brain Res. 120: 1-8.
    • (2003) Brain Res. Mol. Brain Res. , vol.120 , pp. 1-8
    • Gonzalez-Nunez, V.1
  • 44
    • 0030174299 scopus 로고    scopus 로고
    • Two types of cDNAs encoding proopiomelanocortin of sockeye salmon, Onchorhynchus nerka
    • Okuta, A. et al 1996. Two types of cDNAs encoding proopiomelanocortin of sockeye salmon, Onchorhynchus nerka. Zool. Sci. 13: 421-427.
    • (1996) Zool. Sci. , vol.13 , pp. 421-427
    • Okuta, A.1
  • 45
    • 0033394037 scopus 로고    scopus 로고
    • Cloning of a neoteleost (Oreochromis mossambicus) POMC cDNA reveals a deletion of the γ-MSH region and most of the joining peptide region: implications for POMC processing
    • Lee, J. et al 1999. Cloning of a neoteleost (Oreochromis mossambicus) POMC cDNA reveals a deletion of the γ-MSH region and most of the joining peptide region: implications for POMC processing. Peptides 20: 1391-1399.
    • (1999) Peptides , vol.20 , pp. 1391-1399
    • Lee, J.1
  • 46
    • 0344672940 scopus 로고    scopus 로고
    • Cloning of a proopiomelanocortin cDNA from the pituitary gland of the sea bass (Dicentrarchus labrax) and assessment of mRNA expression in different tissues by means of real-time PCR
    • Varsamos, S. et al 2003. Cloning of a proopiomelanocortin cDNA from the pituitary gland of the sea bass (Dicentrarchus labrax) and assessment of mRNA expression in different tissues by means of real-time PCR. J. Endocrinol. 176: 405-414.
    • (2003) J. Endocrinol. , vol.176 , pp. 405-414
    • Varsamos, S.1
  • 47
    • 43249121803 scopus 로고    scopus 로고
    • Evaluation of posttranslational processing of proopiomelanocortin in the banded houndshark pituitary by combined cDNA cloning and mass spectrometry
    • Takahashi, A. et al 2008. Evaluation of posttranslational processing of proopiomelanocortin in the banded houndshark pituitary by combined cDNA cloning and mass spectrometry. Gen. Comp. Endocrinol. 157: 41-48.
    • (2008) Gen. Comp. Endocrinol. , vol.157 , pp. 41-48
    • Takahashi, A.1
  • 48
    • 0032796806 scopus 로고    scopus 로고
    • Cloning of proopiomelanocortin from the brain of the African lungfish, Protopterus annectens, and the brain of the western spadefoot toad, Spea multiplicatus
    • Lee, J. et al 1999. Cloning of proopiomelanocortin from the brain of the African lungfish, Protopterus annectens, and the brain of the western spadefoot toad, Spea multiplicatus. Neuroendocrinology 70: 43-54.
    • (1999) Neuroendocrinology , vol.70 , pp. 43-54
    • Lee, J.1
  • 49
    • 0032831246 scopus 로고    scopus 로고
    • Molecular cloning of lungfish proopiomelanocortin cDNA
    • Amemiya, Y. et al 1999. Molecular cloning of lungfish proopiomelanocortin cDNA. Gen. Comp. Endocrinol. 115:415-421.
    • (1999) Gen. Comp. Endocrinol. , vol.115 , pp. 415-421
    • Amemiya, Y.1
  • 50
    • 0033427639 scopus 로고    scopus 로고
    • Cloning of a POMC cDNA from the pituitary of the Australian Lungfish, Neoceratodus forsteri: analyzing trends in the organization of the prohormone precursor, proopiomelanocortin
    • Dores, R.M. et al 1999. Cloning of a POMC cDNA from the pituitary of the Australian Lungfish, Neoceratodus forsteri: analyzing trends in the organization of the prohormone precursor, proopiomelanocortin. Gen. Comp. Endocrinol. 116: 433-444.
    • (1999) Gen. Comp. Endocrinol. , vol.116 , pp. 433-444
    • Dores, R.M.1
  • 51
    • 0037442117 scopus 로고    scopus 로고
    • Identification of proopiomelanocortin-related peptides in the rostral pars distalis of the pituitary in coelacanth: evolutionary implications
    • Takahashi, A. et al 2003. Identification of proopiomelanocortin-related peptides in the rostral pars distalis of the pituitary in coelacanth: evolutionary implications. Gen. Comp. Endocrinol. 130: 340-349.
    • (2003) Gen. Comp. Endocrinol. , vol.130 , pp. 340-349
    • Takahashi, A.1
  • 52
    • 79952470678 scopus 로고
    • Nucleotide sequence of a cloned cDNA for pro-opiomelanocortin in the amphibian Xenopus laevis
    • Martens, G.J.M. et al 1985. Nucleotide sequence of a cloned cDNA for pro-opiomelanocortin in the amphibian Xenopus laevis. J. Biol. Chem. 256: 5683-5688.
    • (1985) J. Biol. Chem. , vol.256 , pp. 5683-5688
    • Martens, G.J.M.1
  • 53
    • 0036170117 scopus 로고    scopus 로고
    • Cladistic analysis of anuran POMC sequences
    • Alrubaian, J. et al 2002. Cladistic analysis of anuran POMC sequences. Peptides 23: 443-452.
    • (2002) Peptides , vol.23 , pp. 443-452
    • Alrubaian, J.1
  • 54
    • 25144452265 scopus 로고    scopus 로고
    • Analyzing the radiation of the melanocortins in amphibians: cloning of POMC cDNAs from the pituitary of the urodele amphibians, Amphiuma means and Necturus maculosus
    • Kozak, K. et al 2005. Analyzing the radiation of the melanocortins in amphibians: cloning of POMC cDNAs from the pituitary of the urodele amphibians, Amphiuma means and Necturus maculosus. Peptides 26: 1920-1928.
    • (2005) Peptides , vol.26 , pp. 1920-1928
    • Kozak, K.1
  • 55
    • 0037382471 scopus 로고    scopus 로고
    • Molecular cloning of proopiomelanocortin (POMC) cDNA from mud turtle, Pelodiscus sinensis
    • Shen, S.-T. et al 2003. Molecular cloning of proopiomelanocortin (POMC) cDNA from mud turtle, Pelodiscus sinensis. Gen. Comp. Endocrinol. 131: 192-201.
    • (2003) Gen. Comp. Endocrinol. , vol.131 , pp. 192-201
    • Shen, S.-T.1
  • 56
    • 3042796951 scopus 로고    scopus 로고
    • Molecular characterization of the leopard gecko POMC gene and expressional change in the testis by acclimation to low temperature and with a short photoperiod
    • Endo, D. & M.K. Park 2004. Molecular characterization of the leopard gecko POMC gene and expressional change in the testis by acclimation to low temperature and with a short photoperiod. Gen. Comp. Endocrinol. 138: 70-77.
    • (2004) Gen. Comp. Endocrinol. , vol.138 , pp. 70-77
    • Endo, D.1    Park, M.K.2
  • 57
    • 33646034016 scopus 로고    scopus 로고
    • Molecular cloning and characterization of preproopiomelanocortin cDNA from the ostrich
    • Naude R. et al 2006. Molecular cloning and characterization of preproopiomelanocortin cDNA from the ostrich. Gen. Comp. Endocrinol. 146: 310-317.
    • (2006) Gen. Comp. Endocrinol. , vol.146 , pp. 310-317
    • Naude, R.1
  • 58
    • 34547124329 scopus 로고    scopus 로고
    • Analyzing the evolution of β-endorphin posttranslational processing events: studies on reptiles
    • Shoureshi, P. et al 2007. Analyzing the evolution of β-endorphin posttranslational processing events: studies on reptiles. Gen. Comp. Endocrinol. 153: 145-158.
    • (2007) Gen. Comp. Endocrinol. , vol.153 , pp. 145-158
    • Shoureshi, P.1
  • 59
    • 0021196999 scopus 로고
    • Polyprotein gene expression: generation of diversity of neuroendocrine peptides
    • Douglass, J. et al 1984. Polyprotein gene expression: generation of diversity of neuroendocrine peptides. Ann. Rev. Biochem. 53: 665-715.
    • (1984) Ann. Rev. Biochem. , vol.53 , pp. 665-715
    • Douglass, J.1
  • 60
    • 0027231892 scopus 로고
    • A view of the N-acetylation of α-melanocyte-stimulating hormone and β-endorphin from a phylogenetic perspective
    • Dores, R.M. et al 1993. A view of the N-acetylation of α-melanocyte-stimulating hormone and β-endorphin from a phylogenetic perspective. Ann. N.Y. Acad. Sci. 680: 161-174.
    • (1993) Ann. N.Y. Acad. Sci. , vol.680 , pp. 161-174
    • Dores, R.M.1
  • 61
    • 0346973368 scopus 로고    scopus 로고
    • Comparative aspects of intracellular proteolytic processing of peptide hormone precursors: studies of proopiomelanocortin processing
    • Tanaka, S. 2003. Comparative aspects of intracellular proteolytic processing of peptide hormone precursors: studies of proopiomelanocortin processing. Zoolog. Sci. 20: 1183-1198.
    • (2003) Zoolog. Sci. , vol.20 , pp. 1183-1198
    • Tanaka, S.1
  • 62
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides
    • Seidah, N. & M. Chretien 1999. Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848: 45-62.
    • (1999) Brain Res , vol.848 , pp. 45-62
    • Seidah, N.1    Chretien, M.2
  • 63
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou, A. et al 1999. Proteolytic processing in the secretory pathway. J. Biol. Chem. 274: 20745-20748.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20745-20748
    • Zhou, A.1
  • 64
    • 0023959725 scopus 로고
    • Proopiomelanocortin processing in the pituitary, central nervous system, and peripheral tissues
    • Smith, A.I. & J.W. Funder 1988. Proopiomelanocortin processing in the pituitary, central nervous system, and peripheral tissues. Endocr. Rev. 9: 159-179.
    • (1988) Endocr. Rev. , vol.9 , pp. 159-179
    • Smith, A.I.1    Funder, J.W.2
  • 65
    • 0036125112 scopus 로고    scopus 로고
    • Review: pro-opiomelanocortin processing in the hypothalamus: impact on melanocortin signaling and obesity
    • Prichard, L.E. et al 2002. Review: pro-opiomelanocortin processing in the hypothalamus: impact on melanocortin signaling and obesity. J. Endocrinol. 172: 411-421.
    • (2002) J. Endocrinol. , vol.172 , pp. 411-421
    • Prichard, L.E.1
  • 66
    • 0024157819 scopus 로고
    • Alpha-melanocyte-stimulating hormone (alpha-MSH) in the brain of the cartilaginous fish. Immunohistochemical localization and biochemical characterization
    • Vallarino, M. et al 1988. Alpha-melanocyte-stimulating hormone (alpha-MSH) in the brain of the cartilaginous fish. Immunohistochemical localization and biochemical characterization. Peptides 9: 899-907.
    • (1988) Peptides , vol.9 , pp. 899-907
    • Vallarino, M.1
  • 67
    • 16244373644 scopus 로고    scopus 로고
    • Immunocytochemical localization and ontogenetic development of alpha-melanocyte-stimulating hormone (alpha-MSH) in the brain of a pleuronectiform fish, barfin founder
    • Amano, M. et al 2005. Immunocytochemical localization and ontogenetic development of alpha-melanocyte-stimulating hormone (alpha-MSH) in the brain of a pleuronectiform fish, barfin founder. Cell Tissue Res. 320: 127-134.
    • (2005) Cell Tissue Res. , vol.320 , pp. 127-134
    • Amano, M.1
  • 68
    • 0026637722 scopus 로고
    • Alpha-melanocyte-stimulating hormone (α-MSH) in the brain of the African lungfish, Protopterus annectens: immunohistochemical localization and biochemical characterization
    • Vallarino, M. et al 1992. Alpha-melanocyte-stimulating hormone (α-MSH) in the brain of the African lungfish, Protopterus annectens: immunohistochemical localization and biochemical characterization. J. Comp. Neurol. 322: 266-274.
    • (1992) J. Comp. Neurol. , vol.322 , pp. 266-274
    • Vallarino, M.1
  • 69
    • 0020807843 scopus 로고
    • Immunological characterization of endorphins, adrenocorticiotrophin and melanotropins in frog hypothalamus
    • Jegou, S. et al 1983. Immunological characterization of endorphins, adrenocorticiotrophin and melanotropins in frog hypothalamus. Gen. Comp. Endocrinol. 51: 246-254.
    • (1983) Gen. Comp. Endocrinol. , vol.51 , pp. 246-254
    • Jegou, S.1
  • 70
    • 0021705699 scopus 로고
    • Localization of neurons containing pro-opiomelancortin-related peptides in the hypothalamus and midbrain of the reptile, Anolis carolinensis: evidence for region specific processing of β-endorphin
    • Dores, R.M. et al 1984. Localization of neurons containing pro-opiomelancortin-related peptides in the hypothalamus and midbrain of the reptile, Anolis carolinensis: evidence for region specific processing of β-endorphin. Brain Res. 324: 384-389.
    • (1984) Brain Res. , vol.324 , pp. 384-389
    • Dores, R.M.1
  • 71
    • 0038727489 scopus 로고    scopus 로고
    • Avian melanocortin system: α-MSH may act as an autocrine/paracrine hormone. A mini-review
    • Takeuchi, S. et al 2003. Avian melanocortin system: α-MSH may act as an autocrine/paracrine hormone. A mini-review. Ann. N.Y. Acad. Sci. 944: 366-372.
    • (2003) Ann. N.Y. Acad. Sci. , vol.944 , pp. 366-372
    • Takeuchi, S.1
  • 73
    • 0027324907 scopus 로고
    • Design, synthesis, and conformation of superpotent and prolonged acting melanotropins
    • Hruby, V.J. et al 1993. Design, synthesis, and conformation of superpotent and prolonged acting melanotropins. Ann. N.Y. Acad. Sci. 680: 51-63.
    • (1993) Ann. N.Y. Acad. Sci. , vol.680 , pp. 51-63
    • Hruby, V.J.1
  • 74
    • 0010434337 scopus 로고
    • Handbook of Psychopharmacology
    • In, L. Overson, S.D. Iverson & S.H. Snyder, Eds. Plenum Publishing Corp. New York
    • Akil, H. & S.J. Watson 1982. β-endorphin and biosynthetically related peptides in the CNS. In Handbook of Psychopharmacology, Vol. 16. L. Overson, S.D. Iverson & S.H. Snyder, Eds.: 2009-2243. Plenum Publishing Corp. New York
    • (1982) β-endorphin and biosynthetically related peptides in the CNS , vol.16 , pp. 2009-2243
    • Akil, H.1    Watson, S.J.2
  • 75
    • 0028173406 scopus 로고
    • The posttranslational modification of ß-endorphin in the intermediate pituitary of the toad, Bufo marinus, includes processing at a monobasic cleavage site
    • Dores, R.M. et al 1994. The posttranslational modification of ß-endorphin in the intermediate pituitary of the toad, Bufo marinus, includes processing at a monobasic cleavage site. Peptides 15: 1497-1504.
    • (1994) Peptides , vol.15 , pp. 1497-1504
    • Dores, R.M.1
  • 76
    • 0026673108 scopus 로고
    • Detection of met-enkephalin in the pars intermedia of the lampreys, Ichthyomyzon marinus and Petromyzon marinus
    • Dores, R.M. & L.K. McDonald 1992. Detection of met-enkephalin in the pars intermedia of the lampreys, Ichthyomyzon marinus and Petromyzon marinus. Gen. Comp. Endocrinol. 88: 292-297.
    • (1992) Gen. Comp. Endocrinol. , vol.88 , pp. 292-297
    • Dores, R.M.1    Mcdonald, L.K.2
  • 77
    • 33744994508 scopus 로고    scopus 로고
    • Posttranslational processing of proopiomelanocortin family molecules in sea lamprey based on mass spectrometric and chemical analysis
    • Takahashi, A. et al 2005. Posttranslational processing of proopiomelanocortin family molecules in sea lamprey based on mass spectrometric and chemical analysis. Gen. Comp. Endocrinol. 148: 79-84.
    • (2005) Gen. Comp. Endocrinol. , vol.148 , pp. 79-84
    • Takahashi, A.1
  • 78
    • 0022476781 scopus 로고
    • Characterization of endorphins from the pituitary of the spiny dogfish, Squalus acanthias
    • Lorenz, R.G. et al 1986. Characterization of endorphins from the pituitary of the spiny dogfish, Squalus acanthias. Peptides 7: 119-126.
    • (1986) Peptides , vol.7 , pp. 119-126
    • Lorenz, R.G.1
  • 79
    • 0026476061 scopus 로고
    • The processing of β-endorphin and α-melanotropin in Xenopus pars intermedia is influenced by background adaptation
    • Maruthainar, K. et al 1992. The processing of β-endorphin and α-melanotropin in Xenopus pars intermedia is influenced by background adaptation. J. Endocrinol. 135: 469-478.
    • (1992) J. Endocrinol. , vol.135 , pp. 469-478
    • Maruthainar, K.1
  • 80
    • 0027270782 scopus 로고
    • A,N-acetyl β-endorphin(1-8) is the terminal product of processing of endorphins in the melanotrope cell of Xenopus laevis, as demonstrated by FAB tandem mass spectrometry
    • van Strien, F.J.C. et al 1993. A, N-acetyl β-endorphin(1-8) is the terminal product of processing of endorphins in the melanotrope cell of Xenopus laevis, as demonstrated by FAB tandem mass spectrometry. Biochem. Biophys. Res. Commun. 191: 262-268.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 262-268
    • van Strien, F.J.C.1
  • 81
    • 0028232568 scopus 로고
    • Detection of N-acetylated forms of α-MSH and β-endorphin in the intermediate pituitary of the holostean fishes, Lepisosteus spatula, Lepisosteus osseus, and Amia calva
    • Dores, R.M. et al 1994. Detection of N-acetylated forms of α-MSH and β-endorphin in the intermediate pituitary of the holostean fishes, Lepisosteus spatula, Lepisosteus osseus, and Amia calva. Peptides 15: 483-487.
    • (1994) Peptides , vol.15 , pp. 483-487
    • Dores, R.M.1
  • 82
    • 0024160212 scopus 로고
    • The isolation of multiple forms of β-endorphin from the pars intermedia of the Australian lungfish, Neoceratodus forsteri
    • Dores, R.M. et al 1988. The isolation of multiple forms of β-endorphin from the pars intermedia of the Australian lungfish, Neoceratodus forsteri. Peptides 9: 801-808.
    • (1988) Peptides , vol.9 , pp. 801-808
    • Dores, R.M.1
  • 83
    • 0021083285 scopus 로고
    • Further characteristics of the major forms of reptile β-endorphin
    • Dores, R.M. 1983. Further characteristics of the major forms of reptile β-endorphin. Peptides 4: 897-905.
    • (1983) Peptides , vol.4 , pp. 897-905
    • Dores, R.M.1
  • 84
    • 0021061977 scopus 로고
    • Biosynthesis of multiple forms of β-endorphin in the reptile intermediate pituitary
    • Dores, R.M. & A.M. Surprentant 1983. Biosynthesis of multiple forms of β-endorphin in the reptile intermediate pituitary. Peptides 4: 889-896.
    • (1983) Peptides , vol.4 , pp. 889-896
    • Dores, R.M.1    Surprentant, A.M.2
  • 85
    • 77953311302 scopus 로고    scopus 로고
    • Analysis of peptides in prohormone convertase 1/3 null mouse brain using quantitative peptidomics
    • Wardman, J.H. et al 2010. Analysis of peptides in prohormone convertase 1/3 null mouse brain using quantitative peptidomics. J. Neurochem. 114: 215-225.
    • (2010) J. Neurochem. , vol.114 , pp. 215-225
    • Wardman, J.H.1
  • 86
    • 0031985151 scopus 로고    scopus 로고
    • Prodynorphin processing by proprotein convertase 2. Cleavage at a single basic residue and enhanced processing in the presence of carboxypeptidase activity
    • Day, R. et al 1998. Prodynorphin processing by proprotein convertase 2. Cleavage at a single basic residue and enhanced processing in the presence of carboxypeptidase activity. J. Biol. Chem. 273: 829-836.
    • (1998) J. Biol. Chem. , vol.273 , pp. 829-836
    • Day, R.1
  • 87
    • 0019818146 scopus 로고
    • Opiate binding properties of naturally occurring N- and C-terminus modified β-endorphin
    • Akil, H. et al 1981. Opiate binding properties of naturally occurring N- and C-terminus modified β-endorphin. Peptides 2: 289-292.
    • (1981) Peptides , vol.2 , pp. 289-292
    • Akil, H.1
  • 88
    • 0018332852 scopus 로고
    • The N-acetylation of corticotropin and fragments of corticotropin by a rat pituitary N-acetyltransferase
    • Woodford, T.A. & J.E. Dixon 1979. The N-acetylation of corticotropin and fragments of corticotropin by a rat pituitary N-acetyltransferase. J. Biol. Chem. 254: 4993-4999.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4993-4999
    • Woodford, T.A.1    Dixon, J.E.2
  • 89
    • 0020429868 scopus 로고
    • Acetylation of α-melanotropin and β-endorphin in the rat intermediate pituitary
    • Glembotski, C.C. 1982. Acetylation of α-melanotropin and β-endorphin in the rat intermediate pituitary. J. Biol. Chem. 257: 10493-10500.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10493-10500
    • Glembotski, C.C.1
  • 90
    • 0020033116 scopus 로고
    • Review article: distribution of β-endorphin related peptides in rat pituitary and brain
    • Zakarian, S. & D. Smyth 1982. Review article: distribution of β-endorphin related peptides in rat pituitary and brain. Biochem J. 202: 561-571.
    • (1982) Biochem J , vol.202 , pp. 561-571
    • Zakarian, S.1    Smyth, D.2
  • 91
    • 0022646943 scopus 로고
    • Coordinate regulation of peptide acetyltransferase activity and proopiomelanocortin gene expression in the intermediate lobes of the rat pituitary
    • Millington, W.R. et al 1986. Coordinate regulation of peptide acetyltransferase activity and proopiomelanocortin gene expression in the intermediate lobes of the rat pituitary. Endocrinology 118: 2024-2033.
    • (1986) Endocrinology , vol.118 , pp. 2024-2033
    • Millington, W.R.1
  • 92
    • 0014835018 scopus 로고
    • Purification and amino acid sequence of melanocyte-stimulating hormone from the dogfish
    • Lowry, P.J. & A. Chadwick 1970. Purification and amino acid sequence of melanocyte-stimulating hormone from the dogfish, Squalus acanthias. Biochem J. 118: 713-718.
    • (1970) Squalus acanthias. Biochem J. , vol.118 , pp. 713-718
    • Lowry, P.J.1    Chadwick, A.2
  • 93
    • 0020045020 scopus 로고
    • Peptides derived from pro-opiocortin in the pituitary gland of the dogfish, Squalus acanthias
    • Denning-Kendall, P.A. et al 1981. Peptides derived from pro-opiocortin in the pituitary gland of the dogfish, Squalus acanthias. J. Endocrinol. 93: 381-390.
    • (1981) J. Endocrinol. , vol.93 , pp. 381-390
    • Denning-Kendall, P.A.1
  • 94
    • 0028264558 scopus 로고
    • The melanotropes of the lizard, Anolis carolinensis lack N-acetylating mechanisms for both α-MSH and ß-endorphin
    • Dores, R.M. et al 1994. The melanotropes of the lizard, Anolis carolinensis lack N-acetylating mechanisms for both α-MSH and ß-endorphin. Neuroendocrinology 59: 603-609.
    • (1994) Neuroendocrinology , vol.59 , pp. 603-609
    • Dores, R.M.1
  • 95
    • 0019867059 scopus 로고
    • N-α-acetylation is linked to α-MSH release from pars intermedia of the amphibian pituitary gland
    • Martens, G.J.M. et al 1981. N-α-acetylation is linked to α-MSH release from pars intermedia of the amphibian pituitary gland. Nature 294: 558-560.
    • (1981) Nature , vol.294 , pp. 558-560
    • Martens, G.J.M.1
  • 96
    • 0027196015 scopus 로고    scopus 로고
    • Multi-hormone regulation of pituitary melanotrophs
    • Tonon, M.C. et al Multi-hormone regulation of pituitary melanotrophs. Ann. N.Y. Acad. Sci. 680: 175-187.
    • Ann. N.Y. Acad. Sci. , vol.680 , pp. 175-187
    • Tonon, M.C.1
  • 97
    • 0025040420 scopus 로고
    • Detection of N-acetylated forms of β-endorphin and non-acetylated α-MSH in the intermediate pituitary of the toad, Bufo marinus
    • Steveson, T.C. et al 1990. Detection of N-acetylated forms of β-endorphin and non-acetylated α-MSH in the intermediate pituitary of the toad, Bufo marinus. Peptides 11:797-803.
    • (1990) Peptides , vol.11 , pp. 797-803
    • Steveson, T.C.1
  • 98
    • 0026085457 scopus 로고
    • Differential mechanisms for the N-acetylation of α-MSH and β-endorphin in the intermediate pituitary of the frog, Xenopus laevis
    • Dores, R.M. et al 1991. Differential mechanisms for the N-acetylation of α-MSH and β-endorphin in the intermediate pituitary of the frog, Xenopus laevis. Neuroendocrinology 53: 54-62.
    • (1991) Neuroendocrinology , vol.53 , pp. 54-62
    • Dores, R.M.1
  • 99
    • 0026755933 scopus 로고
    • Detection and partial characterization of proopiomelanocortin related end-products from the pars intermedia of the toad, Bombina orientalis
    • Dores, R.M. et al 1992. Detection and partial characterization of proopiomelanocortin related end-products from the pars intermedia of the toad, Bombina orientalis. Gen. Comp. Endocrinol. 87: 197-207.
    • (1992) Gen. Comp. Endocrinol. , vol.87 , pp. 197-207
    • Dores, R.M.1
  • 100
    • 0029951496 scopus 로고    scopus 로고
    • POMC-related products in the intermediate pituitary of the amphibian, Bufo marinus: differential subcellular processing in the golgi and secretory granules
    • Steveson, T.C. & R.M. Dores 1996. POMC-related products in the intermediate pituitary of the amphibian, Bufo marinus: differential subcellular processing in the golgi and secretory granules. Peptides 17: 425-434.
    • (1996) Peptides , vol.17 , pp. 425-434
    • Steveson, T.C.1    Dores, R.M.2
  • 101
    • 0022621305 scopus 로고
    • Thyrotropin-releasing hormone precursor: characterization in rat brain
    • Lechan, R.M. et al 1986. Thyrotropin-releasing hormone precursor: characterization in rat brain. Science 231: 159-161.
    • (1986) Science , vol.231 , pp. 159-161
    • Lechan, R.M.1
  • 102
    • 0021112184 scopus 로고
    • Saccharomyces cerevisiae contains two discrete genes coding for the alpha-factor pheromone
    • Singh, A. et al 1983. Saccharomyces cerevisiae contains two discrete genes coding for the alpha-factor pheromone. Nucleic Acids Res. 11: 4049-4063.
    • (1983) Nucleic Acids Res , vol.11 , pp. 4049-4063
    • Singh, A.1
  • 103
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • Schioth, H.B. & R. Fredriksson 2005. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol. Pharmacol. 67: 1414-1425.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1414-1425
    • Schioth, H.B.1    Fredriksson, R.2
  • 104
    • 60449098464 scopus 로고    scopus 로고
    • Modeling the evolution of the MC2R and MC5R genes: studies on the cartilaginous fish, Heterondotus francisci
    • Baron, A. et al 2009. Modeling the evolution of the MC2R and MC5R genes: studies on the cartilaginous fish, Heterondotus francisci. Gen. Comp. Endocrinol. 161: 13-19.
    • (2009) Gen. Comp. Endocrinol. , vol.161 , pp. 13-19
    • Baron, A.1
  • 105
    • 1542510107 scopus 로고    scopus 로고
    • The melanocortin system in Fugu: determination of POMC/AGRP/MCR gene repertoire and synteny, as well as pharmacology and anatomical distribution of the MCRs
    • Klovins, J. et al 2004. The melanocortin system in Fugu: determination of POMC/AGRP/MCR gene repertoire and synteny, as well as pharmacology and anatomical distribution of the MCRs. Mol. Biol. Evol. 21: 563-579.
    • (2004) Mol. Biol. Evol. , vol.21 , pp. 563-579
    • Klovins, J.1
  • 107
    • 23944512136 scopus 로고    scopus 로고
    • Interactions of human melanocortin 4 receptors with nonpeptide and peptide agonists
    • Pogozheva, I.D. et al 2005. Interactions of human melanocortin 4 receptors with nonpeptide and peptide agonists. Biochemistry 44: 11329-11341.
    • (2005) Biochemistry , vol.44 , pp. 11329-11341
    • Pogozheva, I.D.1
  • 108
    • 0016241399 scopus 로고
    • Corticotorpin-like peptides in the rat pituitary
    • Scott, A.P. et al 1974. Corticotorpin-like peptides in the rat pituitary. J. Endocrinol. 61: 355-367.
    • (1974) J. Endocrinol. , vol.61 , pp. 355-367
    • Scott, A.P.1
  • 109
    • 0025289444 scopus 로고
    • Analysis of ACTH-related and CLIP-related peptides partially purified from the pituitary of the Australian lungfish, Neoceratodus fosteri
    • Dores, R.M. et al 1990. Analysis of ACTH-related and CLIP-related peptides partially purified from the pituitary of the Australian lungfish, Neoceratodus fosteri. Gen. Comp. Endocrinol. 79: 64-73.
    • (1990) Gen. Comp. Endocrinol. , vol.79 , pp. 64-73
    • Dores, R.M.1
  • 110
    • 0017620408 scopus 로고
    • ACTH: a short introductory review
    • Schwyzer, R. 1977. ACTH: a short introductory review. Ann N.Y. Acad. Sci. 297: 3-26.
    • (1977) Ann N.Y. Acad. Sci. , vol.297 , pp. 3-26
    • Schwyzer, R.1
  • 111
    • 0026800892 scopus 로고
    • The cloning of a family of genes that encode the melanocortin receptors
    • Mountjoy, K.G. 1992. The cloning of a family of genes that encode the melanocortin receptors. Science 257: 1248-1251.
    • (1992) Science , vol.257 , pp. 1248-1251
    • Mountjoy, K.G.1
  • 112
    • 1042264043 scopus 로고    scopus 로고
    • Mutational analysis of evolutionarily conserved ACTH residues
    • Costa, J.L. et al 2004. Mutational analysis of evolutionarily conserved ACTH residues. Gen. Comp. Endocrinol. 136: 12-16.
    • (2004) Gen. Comp. Endocrinol. , vol.136 , pp. 12-16
    • Costa, J.L.1
  • 113
    • 0028865937 scopus 로고
    • Isolation and characterization of melanotropins from lamprey pituitary glands
    • Takahashi, A. et al. 1995. Isolation and characterization of melanotropins from lamprey pituitary glands. Int. J. Peptide Protein Res. 46: 197-204.
    • (1995) Int. J. Peptide Protein Res. , vol.46 , pp. 197-204
    • Takahashi, A.1
  • 114
    • 0019180771 scopus 로고
    • Most of the coding region of rat ACTH/β-LPH precursor gene lacks intervening sequences
    • Drouin, J. & H.M. Goodman 1980. Most of the coding region of rat ACTH/β-LPH precursor gene lacks intervening sequences. Nature 288: 610-613.
    • (1980) Nature , vol.288 , pp. 610-613
    • Drouin, J.1    Goodman, H.M.2
  • 115
    • 0031239695 scopus 로고    scopus 로고
    • Deciphering posttranslational processing events in the pituitary of a neopterygian fish: cloning of a gar POMC cDNA
    • Dores, R.M. et al 1997. Deciphering posttranslational processing events in the pituitary of a neopterygian fish: cloning of a gar POMC cDNA. Gen. Comp. Endocrinol. 107: 401-413.
    • (1997) Gen. Comp. Endocrinol. , vol.107 , pp. 401-413
    • Dores, R.M.1
  • 116
    • 0025612269 scopus 로고
    • Characterization of the cDNA encoding proopiomelanocortin in the frog Rana ridibunda
    • Hilario, E. et al 1990. Characterization of the cDNA encoding proopiomelanocortin in the frog Rana ridibunda. Biochem. Biophys. Res. Commun. 173: 653-659.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 653-659
    • Hilario, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.