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Volumn 272, Issue 4, 2005, Pages 942-955

Planarian peptidylglycine-hydroxylating monooxygenase, a neuropeptide processing enzyme, colocalizes with cytochrome b561 along the central nervous system

Author keywords

Cytochrome b 561; Neuroendocrine vesicle; Neuropeptide amidation; Peptidylglycine hydroxylating monooxygenase; Planarian

Indexed keywords

COMPLEMENTARY DNA; CYTOCHROME B; CYTOCHROME B561; MESSENGER RNA; NEUROPEPTIDE; PEPTIDYLGLYCINE ALPHA HYDROXYLATING MONOOXYGENASE; UNCLASSIFIED DRUG; UNSPECIFIC MONOOXYGENASE;

EID: 14044279780     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2004.04528.x     Document Type: Article
Times cited : (19)

References (64)
  • 2
    • 0027418132 scopus 로고
    • Peptidylglycine α-amidating monooxgenase: A multifunctional protein with catalytic, processing, and routing domains
    • Eipper BA, Milgram SL, Husten EJ, Yun H & Mains RE (1993) Peptidylglycine α-amidating monooxgenase: a multifunctional protein with catalytic, processing, and routing domains. Protein Sci 2, 489-497.
    • (1993) Protein Sci , vol.2 , pp. 489-497
    • Eipper, B.A.1    Milgram, S.L.2    Husten, E.J.3    Yun, H.4    Mains, R.E.5
  • 3
    • 0034307010 scopus 로고    scopus 로고
    • PHM is required for normal developmental transitions and for biosynthesis of secretory peptides in Drosophila
    • Jiang N, Kolhekar AS, Jacobs PS, Mains RE, Eipper BA & Taghert PH (2000) PHM is required for normal developmental transitions and for biosynthesis of secretory peptides in Drosophila. Dev Biol 226, 118-136.
    • (2000) Dev Biol , vol.226 , pp. 118-136
    • Jiang, N.1    Kolhekar, A.S.2    Jacobs, P.S.3    Mains, R.E.4    Eipper, B.A.5    Taghert, P.H.6
  • 5
    • 0029797222 scopus 로고    scopus 로고
    • Peptides in the nervous systems of cnidarians: Structure, function, and biosynthesis
    • Grimmelikhuijzen CJP, Leviev I & Carstensen K (1996) Peptides in the nervous systems of cnidarians: structure, function, and biosynthesis. Int Rev Cytol 167, 37-89.
    • (1996) Int Rev Cytol , vol.167 , pp. 37-89
    • Grimmelikhuijzen, C.J.P.1    Leviev, I.2    Carstensen, K.3
  • 6
    • 0026514908 scopus 로고
    • The biosynthesis of neuropeptides: Peptide alpha-amidation
    • Eipper BA, Stoffers DA & Mains RE (1992) The biosynthesis of neuropeptides: peptide alpha-amidation. Annu Rev Neurosci 15, 57-85.
    • (1992) Annu Rev Neurosci , vol.15 , pp. 57-85
    • Eipper, B.A.1    Stoffers, D.A.2    Mains, R.E.3
  • 7
    • 0000821179 scopus 로고    scopus 로고
    • New insights into copper monooxygenases and peptide amidation: Structure, mechanism and function
    • Prigge ST, Mains RE, Eipper BA & Amzel LM (2000) New insights into copper monooxygenases and peptide amidation: structure, mechanism and function. Cell Mol Life Sci 57, 1236-1259.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1236-1259
    • Prigge, S.T.1    Mains, R.E.2    Eipper, B.A.3    Amzel, L.M.4
  • 8
    • 0024286951 scopus 로고
    • Cloning of cDNA encoding a new peptide C-terminal α-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin
    • Ohsuye K, Kitano K, Wada Y, Fuchimura K, Tanaka S, Mizuno K & Matsuo H (1988) Cloning of cDNA encoding a new peptide C-terminal α-amidating enzyme having a putative membrane-spanning domain from Xenopus laevis skin. Biochem Biophys Res Commun 150, 1275-1281.
    • (1988) Biochem Biophys Res Commun , vol.150 , pp. 1275-1281
    • Ohsuye, K.1    Kitano, K.2    Wada, Y.3    Fuchimura, K.4    Tanaka, S.5    Mizuno, K.6    Matsuo, H.7
  • 9
    • 0000614022 scopus 로고
    • Alternative mRNA splicing generates multiple forms of peptidyl-glycine α-amidating monooxygenase in rat atrium
    • Stoffers DA, Barthe-Rosa C & Eipper BA (1989) Alternative mRNA splicing generates multiple forms of peptidyl-glycine α-amidating monooxygenase in rat atrium. Proc Natl Acad Sci USA 86, 735-739.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 735-739
    • Stoffers, D.A.1    Barthe-Rosa, C.2    Eipper, B.A.3
  • 10
    • 0034693285 scopus 로고    scopus 로고
    • Neuropeptide amidation: Cloning of a bifunctional alpha-amidating enzyme from Aplysia
    • Fan X, Spijker S, Akalal D-BG & Nagle GT (2000) Neuropeptide amidation: cloning of a bifunctional alpha-amidating enzyme from Aplysia. Mol Brain Res 82, 25-34.
    • (2000) Mol Brain Res , vol.82 , pp. 25-34
    • Fan, X.1    Spijker, S.2    Akalal, D.-B.G.3    Nagle, G.T.4
  • 12
    • 0031577792 scopus 로고    scopus 로고
    • Molecular cloning of a peptidylglycine α-hydroxylating monooxygenase from sea anemones
    • Hauser F, Williamson M & Grimmelikhuijzen CJP (1997) Molecular cloning of a peptidylglycine α-hydroxylating monooxygenase from sea anemones. Biochem Biophys Res Commun 241, 509-512.
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 509-512
    • Hauser, F.1    Williamson, M.2    Grimmelikhuijzen, C.J.P.3
  • 13
    • 0032940523 scopus 로고    scopus 로고
    • A molluscan peptide α-amidating enzyme precursor that generates five distinct enzymes
    • Spijker S, Smit AB, Eipper BA, Malik A, Mains RE & Geraerts WPM (1999) A molluscan peptide α-amidating enzyme precursor that generates five distinct enzymes. FASEB J 13, 735-748.
    • (1999) FASEB J , vol.13 , pp. 735-748
    • Spijker, S.1    Smit, A.B.2    Eipper, B.A.3    Malik, A.4    Mains, R.E.5    Wpm, G.6
  • 14
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signalling domains
    • Schultz J, Milpetz F, Bork P & Ponting CP (1998) SMART, a simple modular architecture research tool: identification of signalling domains. Proc Natl Acad Sci USA 95, 5857-5864.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 15
    • 0032372679 scopus 로고    scopus 로고
    • Structure of the planarian central nervous system (CNS) revealed by neuronal cell markers
    • Agata K, Soejima Y, Kato K, Kobayashi C, Umesono Y & Watanabe K (1998) Structure of the planarian central nervous system (CNS) revealed by neuronal cell markers. Zool Sci 15, 433-440.
    • (1998) Zool Sci , vol.15 , pp. 433-440
    • Agata, K.1    Soejima, Y.2    Kato, K.3    Kobayashi, C.4    Umesono, Y.5    Watanabe, K.6
  • 16
    • 0029068215 scopus 로고
    • Localisation, quantitation, and characterisation of neuropeptide F- And FMRFamide-immunoreactive peptides in turbellarians and a monogenean: A comparative study
    • Johnston RN, Shaw C, Brennan GP, Maule AG & Halton DW (1995) Localisation, quantitation, and characterisation of neuropeptide F- and FMRFamide-immunoreactive peptides in turbellarians and a monogenean: a comparative study. J Comp Neurol 357, 76-84.
    • (1995) J Comp Neurol , vol.357 , pp. 76-84
    • Johnston, R.N.1    Shaw, C.2    Brennan, G.P.3    Maule, A.G.4    Halton, D.W.5
  • 17
    • 0029889492 scopus 로고    scopus 로고
    • Platyhelminth FMRFamide-related peptides
    • Shaw C, Maule AG & Halton DW (1996) Platyhelminth FMRFamide-related peptides. Int J Parasitol 26, 335-345.
    • (1996) Int J Parasitol , vol.26 , pp. 335-345
    • Shaw, C.1    Maule, A.G.2    Halton, D.W.3
  • 18
    • 0029420510 scopus 로고
    • The nervous system of Tricladida. II. Neuroanatomy of Dugesia tigrina (Paludicola, Dugesiidae): An immunocytochemical study
    • Reuter M, Gustafsson MK, Sheiman IM, Terenina N, Halton DW, Maule AG & Shaw C (1995) The nervous system of Tricladida. II. Neuroanatomy of Dugesia tigrina (Paludicola, Dugesiidae): an immunocytochemical study. Invert Neurosci 1, 133-143.
    • (1995) Invert Neurosci , vol.1 , pp. 133-143
    • Reuter, M.1    Gustafsson, M.K.2    Sheiman, I.M.3    Terenina, N.4    Halton, D.W.5    Maule, A.G.6    Shaw, C.7
  • 20
    • 0023952257 scopus 로고
    • Dopamine beta-hydroxylase of adrenal chromaffin granules: Structure and function
    • Stewart LC & Klinman JP (1988) Dopamine beta-hydroxylase of adrenal chromaffin granules: structure and function. Annu Rev Biochem 57, 551-592.
    • (1988) Annu Rev Biochem , vol.57 , pp. 551-592
    • Stewart, L.C.1    Klinman, J.P.2
  • 21
    • 0023009792 scopus 로고
    • Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes
    • Beers MF, Johnson RG & Scarpa A (1986) Evidence for an ascorbate shuttle for the transfer of reducing equivalents across chromaffin granule membranes. J Biol Chem 261, 2529-2535.
    • (1986) J Biol Chem , vol.261 , pp. 2529-2535
    • Beers, M.F.1    Johnson, R.G.2    Scarpa, A.3
  • 22
    • 0020657388 scopus 로고
    • Electron transfer across the chromaffin granule membrane
    • Njus D, Knoth J, Cook C & Kelley PM (1983) Electron transfer across the chromaffin granule membrane. J Biol Chem 258, 27-30.
    • (1983) J Biol Chem , vol.258 , pp. 27-30
    • Njus, D.1    Knoth, J.2    Cook, C.3    Kelley, P.M.4
  • 23
    • 0021993676 scopus 로고
    • Electron transfer across posterior pituitary neurosecretory vesicle membranes
    • Russell JT, Levine M & Njus D (1985) Electron transfer across posterior pituitary neurosecretory vesicle membranes. J Biol Chem 260, 226-231.
    • (1985) J Biol Chem , vol.260 , pp. 226-231
    • Russell, J.T.1    Levine, M.2    Njus, D.3
  • 24
    • 0022350362 scopus 로고
    • Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells
    • Levine M, Morita K & Pollard H (1985) Enhancement of norepinephrine biosynthesis by ascorbic acid in cultured bovine chromaffin cells. J Biol Chem 260, 12942-12947.
    • (1985) J Biol Chem , vol.260 , pp. 12942-12947
    • Levine, M.1    Morita, K.2    Pollard, H.3
  • 25
    • 0023001148 scopus 로고
    • Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intravesicular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase
    • Wakefield LM, Cass AEG & Radda GK (1986) Electron transfer across the chromaffin granule membrane. Use of EPR to demonstrate reduction of intravesicular ascorbate radical by the extravesicular mitochondrial NADH:ascorbate radical oxidoreductase. J Biol Chem 261, 9746-9752.
    • (1986) J Biol Chem , vol.261 , pp. 9746-9752
    • Wakefield, L.M.1    Cass, A.E.G.2    Radda, G.K.3
  • 26
    • 0030817141 scopus 로고    scopus 로고
    • 561 from bovine adrenal chromaffin vesicles, as revealed by a new purification procedure and EPR spectroscopy
    • 561 from bovine adrenal chromaffin vesicles, as revealed by a new purification procedure and EPR spectroscopy. J Biol Chem 272, 23206-23210.
    • (1997) J Biol Chem , vol.272 , pp. 23206-23210
    • Tsubaki, M.1    Nakayama, M.2    Okuyama, E.3    Ichikawa, Y.4    Hori, H.5
  • 27
    • 0032568938 scopus 로고    scopus 로고
    • 561 from bovine adrenal chromaffin vesicles, as revealed by pulse radiolysis
    • 561 from bovine adrenal chromaffin vesicles, as revealed by pulse radiolysis. J Biol Chem 273, 16038-16042.
    • (1998) J Biol Chem , vol.273 , pp. 16038-16042
    • Kobayashi, K.1    Tsubaki, M.2    Tagawa, S.3
  • 28
    • 0000395131 scopus 로고
    • Studies on the respiratory enzymes of the adrenal gland I. The medulla
    • Spiro MJ & Ball EG (1961) Studies on the respiratory enzymes of the adrenal gland I. The medulla. J Biol Chem 236, 225-230.
    • (1961) J Biol Chem , vol.236 , pp. 225-230
    • Spiro, M.J.1    Ball, E.G.2
  • 29
    • 0013854424 scopus 로고
    • Cytochrome 559 in the microsome of the adrenal medulla
    • Ichikawa Y & Yamano T (1965) Cytochrome 559 in the microsome of the adrenal medulla. Biochem Biophys Res Commun 20, 26-30.
    • (1965) Biochem Biophys Res Commun , vol.20 , pp. 26-30
    • Ichikawa, Y.1    Yamano, T.2
  • 30
    • 0021289369 scopus 로고
    • 561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles
    • 561 is present in bovine adrenal chromaffin vesicles and posterior pituitary neurosecretory vesicles. J Biol Chem 259, 4885-4889.
    • (1984) J Biol Chem , vol.259 , pp. 4885-4889
    • Duong, L.T.1    Fleming, P.J.2    Russell, J.T.3
  • 31
    • 0023161655 scopus 로고
    • 561 can be detected in many neuroendocrine tissues using a specific monoclonal antibody
    • 561 can be detected in many neuroendocrine tissues using a specific monoclonal antibody. Neuroscience 22, 149-157.
    • (1987) Neuroscience , vol.22 , pp. 149-157
    • Pruss, R.M.1    Shepard, E.A.2
  • 32
    • 0024835974 scopus 로고
    • Adrenal chromaffin granules and secretory granules from thyroid parafollicular cells have several common antigens
    • Weiler R, Cidon S, Gershon MD, Tamir H, Hogue-Angeletti R & Winkler H (1989) Adrenal chromaffin granules and secretory granules from thyroid parafollicular cells have several common antigens. FEBS Lett 257, 457-459.
    • (1989) FEBS Lett , vol.257 , pp. 457-459
    • Weiler, R.1    Cidon, S.2    Gershon, M.D.3    Tamir, H.4    Hogue-Angeletti, R.5    Winkler, H.6
  • 33
    • 0017834607 scopus 로고
    • Cytochrome b-561 in sympathetic nerve terminal vesicles from rat vas deferens
    • Fried G (1978) Cytochrome b-561 in sympathetic nerve terminal vesicles from rat vas deferens. Biochim Biophys Acta 507, 175-177.
    • (1978) Biochim Biophys Acta , vol.507 , pp. 175-177
    • Fried, G.1
  • 35
    • 0021309347 scopus 로고
    • The asymmetric orientation of cytochrome b561 in bovine chromaffin granule membranes
    • Duong LT & Fleming PJ (1984) The asymmetric orientation of cytochrome b561 in bovine chromaffin granule membranes. Arch Biochem Biophys 228, 332-341.
    • (1984) Arch Biochem Biophys , vol.228 , pp. 332-341
    • Duong, L.T.1    Fleming, P.J.2
  • 36
    • 0015214389 scopus 로고
    • 561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome
    • 561 of the bovine adrenal chromaffin granules. A high potential b-type cytochrome. Biochim Biophys Acta 253, 487-491.
    • (1971) Biochim Biophys Acta , vol.253 , pp. 487-491
    • Flatmark, T.1    Terland, O.2
  • 38
    • 0038503407 scopus 로고    scopus 로고
    • Stopped-flow analyses on the reaction of ascorbate with cytochrome b561 purified from bovine chromaffin vesicle membranes
    • Takigami T, Takeuchi F, Nakagawa M, Hase T & Tsubaki M (2003) Stopped-flow analyses on the reaction of ascorbate with cytochrome b561 purified from bovine chromaffin vesicle membranes. Biochemistry 42, 8110-8118.
    • (2003) Biochemistry , vol.42 , pp. 8110-8118
    • Takigami, T.1    Takeuchi, F.2    Nakagawa, M.3    Hase, T.4    Tsubaki, M.5
  • 39
    • 1642504227 scopus 로고    scopus 로고
    • 561 from bovine chromaffin vesicles studied by EPR, resonance Raman, and ascorbate reduction assay
    • 561 from bovine chromaffin vesicles studied by EPR, resonance Raman, and ascorbate reduction assay. J Biochem 135, 53-64.
    • (2004) J Biochem , vol.135 , pp. 53-64
    • Takeuchi, F.1    Hori, H.2    Obayashi, E.3    Shiro, Y.4    Tsubaki, M.5
  • 40
    • 0036188664 scopus 로고    scopus 로고
    • Planarian cytochrome b561: Conservation of a six-transmembrane structure and localization along the central and peripheral nervous system
    • Asada A, Kusakawa T, Orii H, Agata K, Watanabe K & Tsubaki M (2002) Planarian cytochrome b561: conservation of a six-transmembrane structure and localization along the central and peripheral nervous system. J Biochem 131, 175-182.
    • (2002) J Biochem , vol.131 , pp. 175-182
    • Asada, A.1    Kusakawa, T.2    Orii, H.3    Agata, K.4    Watanabe, K.5    Tsubaki, M.6
  • 41
    • 0032861557 scopus 로고    scopus 로고
    • Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase
    • Prigge ST, Kolhekar AS, Eipper BA, Mains RE & Amzel LM (1999) Substrate-mediated electron transfer in peptidylglycine α-hydroxylating monooxygenase. Nat Struct Biol 6, 976-983.
    • (1999) Nat Struct Biol , vol.6 , pp. 976-983
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 43
    • 0038031970 scopus 로고    scopus 로고
    • Search for the evolutionary origin of a brain: Planarian brain characterized by microarray
    • Nakazawa M, Cebriá F, Mineta K, Ikeo K, Agata K & Gojobori T (2003) Search for the evolutionary origin of a brain: planarian brain characterized by microarray. Mol Biol Evol 20, 784-791.
    • (2003) Mol Biol Evol , vol.20 , pp. 784-791
    • Nakazawa, M.1    Cebriá, F.2    Mineta, K.3    Ikeo, K.4    Agata, K.5    Gojobori, T.6
  • 44
    • 0038610837 scopus 로고    scopus 로고
    • Origin and evolutionary process of the CNS elucidated by comparative genomics analysis of planarian ESTs
    • Mineta K, Nakazawa M, Cebriá F, Ikeo K, Agata K & Gojobori T (2003) Origin and evolutionary process of the CNS elucidated by comparative genomics analysis of planarian ESTs. Proc Natl Acad Sci USA 100, 7666-7671.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7666-7671
    • Mineta, K.1    Nakazawa, M.2    Cebriá, F.3    Ikeo, K.4    Agata, K.5    Gojobori, T.6
  • 45
    • 0034342451 scopus 로고    scopus 로고
    • Organization and regeneration ability of spontaneous supernumerary eyes in planarians - Eye regeneration field and pathway selection by optic nerves
    • Sakai F, Agata K, Orii H & Watanabe K (2000) Organization and regeneration ability of spontaneous supernumerary eyes in planarians - eye regeneration field and pathway selection by optic nerves. Zool Sci 17, 375-381.
    • (2000) Zool Sci , vol.17 , pp. 375-381
    • Sakai, F.1    Agata, K.2    Orii, H.3    Watanabe, K.4
  • 47
    • 0030699146 scopus 로고    scopus 로고
    • Amidation of bioactive peptides: The structure of peptidylglycine ́-hydroxylating monooxygenase
    • Prigge ST, Kolhekar AS, Eipper BA, Mains RE & Amzel LM (1997) Amidation of bioactive peptides: the structure of peptidylglycine ́-hydroxylating monooxygenase. Science 278, 1300-1305.
    • (1997) Science , vol.278 , pp. 1300-1305
    • Prigge, S.T.1    Kolhekar, A.S.2    Eipper, B.A.3    Mains, R.E.4    Amzel, L.M.5
  • 48
    • 0028768981 scopus 로고
    • a. Identification of a sulfur ligand at the dioxygen binding site by EXAFS and FTIR spectroscopy
    • A. Identification of a sulfur ligand at the dioxygen binding site by EXAFS and FTIR spectroscopy. J Am Chem Soc 116, 1924-1931.
    • (1994) J Am Chem Soc , vol.116 , pp. 1924-1931
    • Reedy, B.J.1    Blackburn, N.J.2
  • 49
    • 0025025585 scopus 로고
    • Characterization of a carbon monoxide complex of reduced dopamine β-hydroxylase
    • Blackburn NJ, Pettingill TM, Seagraves KS & Shigeta RT (1990) Characterization of a carbon monoxide complex of reduced dopamine β-hydroxylase. J Biol Chem 265, 15383-15386.
    • (1990) J Biol Chem , vol.265 , pp. 15383-15386
    • Blackburn, N.J.1    Pettingill, T.M.2    Seagraves, K.S.3    Shigeta, R.T.4
  • 50
    • 0033576285 scopus 로고    scopus 로고
    • Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity
    • Jaron S & Blackburn NJ (1999) Does superoxide channel between the copper centers in peptidylglycine monooxygenase? A new mechanism based on carbon monoxide reactivity. Biochemistry 38, 15086-15096.
    • (1999) Biochemistry , vol.38 , pp. 15086-15096
    • Jaron, S.1    Blackburn, N.J.2
  • 51
    • 0029739477 scopus 로고    scopus 로고
    • Structural investigation on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme
    • Boswell JS, Reedy BJ, Kulathila R, Merkler D & Blackburn NJ (1996) Structural investigation on the coordination environment of the active-site copper centers of recombinant bifunctional peptidylglycine α-amidating enzyme. Biochemistry 35, 12241-12250.
    • (1996) Biochemistry , vol.35 , pp. 12241-12250
    • Boswell, J.S.1    Reedy, B.J.2    Kulathila, R.3    Merkler, D.4    Blackburn, N.J.5
  • 52
    • 0028913562 scopus 로고
    • The catalytic core of peptidylglycine α-hydroxylating monooxygenase: Investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance
    • Eipper BA, Quon ASW, Mains RE, Boswell JS & Blackburn NJ (1995) The catalytic core of peptidylglycine α-hydroxylating monooxygenase: investigation by site-directed mutagenesis, Cu X-ray absorption spectroscopy, and electron paramagnetic resonance. Biochemistry 34, 2857-2865.
    • (1995) Biochemistry , vol.34 , pp. 2857-2865
    • Eipper, B.A.1    Quon, A.S.W.2    Mains, R.E.3    Boswell, J.S.4    Blackburn, N.J.5
  • 53
    • 0022156894 scopus 로고
    • The brain of the planarian as the ancestor of the human brain
    • Sarnat HB & Netsky MG (1985) The brain of the planarian as the ancestor of the human brain. Can J Neurol Sci 12, 296-302.
    • (1985) Can J Neurol Sci , vol.12 , pp. 296-302
    • Sarnat, H.B.1    Netsky, M.G.2
  • 54
    • 0036929716 scopus 로고    scopus 로고
    • When does a ganglion become a brain? Evolutionary origin of the central nervous system
    • Sarnat HB & Netsky MG (2002) When does a ganglion become a brain? Evolutionary origin of the central nervous system. Semin Pediatr Neurol 9, 240-253.
    • (2002) Semin Pediatr Neurol , vol.9 , pp. 240-253
    • Sarnat, H.B.1    Netsky, M.G.2
  • 55
    • 1942489678 scopus 로고    scopus 로고
    • Djeyes absent (Djeya) controls prototypic planarian eye regeneration by cooperating with the transcription factor Djsix-1
    • Mannini L, Rossi L, Den P, Gremigni V, Salvetti A, Salo E & Batistoni R (2004) Djeyes absent (Djeya) controls prototypic planarian eye regeneration by cooperating with the transcription factor Djsix-1. Dev Biol 269, 346-359.
    • (2004) Dev Biol , vol.269 , pp. 346-359
    • Mannini, L.1    Rossi, L.2    Den, P.3    Gremigni, V.4    Salvetti, A.5    Salo, E.6    Batistoni, R.7
  • 56
    • 0031804447 scopus 로고    scopus 로고
    • Rhodopsin-like proteins in planarian eye and auricle: Detection and functional analysis
    • Asano Y, Nakamura S, Ishida S, Azuma K & Shinozawa T (1998) Rhodopsin-like proteins in planarian eye and auricle: detection and functional analysis. J Exp Biol 201, 1263-1271.
    • (1998) J Exp Biol , vol.201 , pp. 1263-1271
    • Asano, Y.1    Nakamura, S.2    Ishida, S.3    Azuma, K.4    Shinozawa, T.5
  • 57
    • 0016173464 scopus 로고
    • Ultrastructure of the photoreceptor of the planarian Dugesia dorotocephala
    • Carpenter KS, Morita M & Best JB (1974) Ultrastructure of the photoreceptor of the planarian Dugesia dorotocephala. Cell Tissue Res 148, 143-158.
    • (1974) Cell Tissue Res , vol.148 , pp. 143-158
    • Carpenter, K.S.1    Morita, M.2    Best, J.B.3
  • 58
    • 0027323435 scopus 로고
    • POU-domain genes in planarian Dugesia japonica: The structure and expression
    • Orii H, Agata K & Watanabe K (1993) POU-domain genes in planarian Dugesia japonica: the structure and expression. Biochem Biophys Res Commun 192, 1395-1402.
    • (1993) Biochem Biophys Res Commun , vol.192 , pp. 1395-1402
    • Orii, H.1    Agata, K.2    Watanabe, K.3
  • 59
    • 0001939094 scopus 로고
    • RACE: Rapid amplification of cDNA ends
    • (Innis MA, Gelfand DH, Sninsky JJ & White TJ, eds). Academic Press, San Diego, Tokyo.
    • Frohman MA (1990) RACE: rapid amplification of cDNA ends. In PCR Protocols - a Guide to Methods and Applications (Innis MA, Gelfand DH, Sninsky JJ & White TJ, eds), pp. 28-38. Academic Press, San Diego, Tokyo.
    • (1990) PCR Protocols - A Guide to Methods and Applications , pp. 28-38
    • Frohman, M.A.1
  • 60
    • 0030972511 scopus 로고    scopus 로고
    • Stepwise dilution screening of a cDNA library by polymerase chain reaction
    • Watanabe K, Sakai F & Orii H (1997) Stepwise dilution screening of a cDNA library by polymerase chain reaction. Anal Biochem 252, 213-214.
    • (1997) Anal Biochem , vol.252 , pp. 213-214
    • Watanabe, K.1    Sakai, F.2    Orii, H.3
  • 61
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S & von Heijne G (1997) Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10, 1-6.
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 62
    • 0036939053 scopus 로고    scopus 로고
    • The body margin of the planarian Dugesia japonica: Characterization by the expression of an intermediate filament gene
    • Tazaki A, Kato K, Orii H, Agata K & Watanabe K (2002) The body margin of the planarian Dugesia japonica: characterization by the expression of an intermediate filament gene. Dev Genes Evol 212, 365-373.
    • (2002) Dev Genes Evol , vol.212 , pp. 365-373
    • Tazaki, A.1    Kato, K.2    Orii, H.3    Agata, K.4    Watanabe, K.5
  • 63
    • 0041192909 scopus 로고    scopus 로고
    • Identification of two distinct muscles in the planarian Dugesia japonica by their expression of myosin heavy chain genes
    • Kobayashi C, Kobayashi S, Orii H, Watanabe K & Agata K (1998) Identification of two distinct muscles in the planarian Dugesia japonica by their expression of myosin heavy chain genes. Zool Sci 15, 861-869.
    • (1998) Zool Sci , vol.15 , pp. 861-869
    • Kobayashi, C.1    Kobayashi, S.2    Orii, H.3    Watanabe, K.4    Agata, K.5
  • 64
    • 0036826121 scopus 로고    scopus 로고
    • Anatomy of the planarian Dugesia japonica I. The muscular system revealed by antisera against myosin heavy chains
    • Orii H, Ito H & Watanabe K (2002) Anatomy of the planarian Dugesia japonica I. The muscular system revealed by antisera against myosin heavy chains. Zool Sci 19, 1123-1131.
    • (2002) Zool Sci , vol.19 , pp. 1123-1131
    • Orii, H.1    Ito, H.2    Watanabe, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.