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Volumn 83, Issue 1, 2002, Pages 37-47

Kinetics of nitric oxide-cyclic GMP signalling in CNS cells and its possible regulation by cyclic GMP

Author keywords

Cyclic GMP; Nitric oxide; Phosphodiesterase; Soluble guanylyl cycase; Striatum

Indexed keywords

CYCLIC GMP; NITRIC OXIDE; PHOSPHODIESTERASE;

EID: 0036788270     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2002.01106.x     Document Type: Article
Times cited : (41)

References (48)
  • 1
    • 0030615278 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent cyclic GMP phosphodiesterase activity in granule neurons and astrocytes from rat cerebellum
    • 2+/calmodulin-dependent cyclic GMP phosphodiesterase activity in granule neurons and astrocytes from rat cerebellum. Eur. J. Pharmacol. 323, 119-125.
    • (1997) Eur. J. Pharmacol. , vol.323 , pp. 119-125
    • Agullo, L.1    Garcia, A.2
  • 2
    • 0024454868 scopus 로고
    • Effects of selective inhibitors on cyclic nucleotide phosphodiesterases of rabbit aorta
    • Ahn H. S., Crim W., Romano M., Sybertz E. and Pitts B. (1989) Effects of selective inhibitors on cyclic nucleotide phosphodiesterases of rabbit aorta. Biochem. Pharmacol. 38, 3331-3339.
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 3331-3339
    • Ahn, H.S.1    Crim, W.2    Romano, M.3    Sybertz, E.4    Pitts, B.5
  • 3
    • 0032550199 scopus 로고    scopus 로고
    • Glutamate neurotoxicity is associated with nitric oxide-mediated mitochondrial dysfunction and glutathione depletion
    • Almeida A., Heales S. J., Bolanos J. P. and Medina J. M. (1998) Glutamate neurotoxicity is associated with nitric oxide-mediated mitochondrial dysfunction and glutathione depletion. Brain Res. 790, 209-216.
    • (1998) Brain Res. , vol.790 , pp. 209-216
    • Almeida, A.1    Heales, S.J.2    Bolanos, J.P.3    Medina, J.M.4
  • 4
    • 0035889980 scopus 로고    scopus 로고
    • Expression of cGMP-specific phosphodiesterase 9A mRNA in the rat brain
    • Andreeva S. G., Dikkes P., Epstein P. M. and Rosenberg P. A. (2001) Expression of cGMP-specific phosphodiesterase 9A mRNA in the rat brain. J. Neurosci. 21, 9068-9076.
    • (2001) J. Neurosci. , vol.21 , pp. 9068-9076
    • Andreeva, S.G.1    Dikkes, P.2    Epstein, P.M.3    Rosenberg, P.A.4
  • 5
    • 0028802726 scopus 로고
    • Cyclic nucleotide phosphodiesterases: Functional implications of multiple isoforms
    • Beavo J. A. (1995) Cyclic nucleotide phosphodiesterases: functional implications of multiple isoforms. Physiol. Rev. 75, 725-748.
    • (1995) Physiol. Rev. , vol.75 , pp. 725-748
    • Beavo, J.A.1
  • 6
    • 0035830921 scopus 로고    scopus 로고
    • Sub-second kinetics of the nitric oxide receptor, soluble guanylyl cyclase, in intact cerebellar cells
    • Bellamy T. C. and Garthwaite J. (2001a) Sub-second kinetics of the nitric oxide receptor, soluble guanylyl cyclase, in intact cerebellar cells. J. Biol. Chem. 276, 4297-4292.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4287-4292
    • Bellamy, T.C.1    Garthwaite, J.2
  • 7
    • 0035164908 scopus 로고    scopus 로고
    • 'cAMP-specific' phosphodiesterase contributes to cGMP degradation in cerebellar cells exposed to nitric oxide
    • Bellamy T. C. and Garthwaite J. (2001b) 'cAMP-specific' phosphodiesterase contributes to cGMP degradation in cerebellar cells exposed to nitric oxide. Mol. Pharmacol. 59, 54-61.
    • (2001) Mol. Pharmacol. , vol.59 , pp. 54-61
    • Bellamy, T.C.1    Garthwaite, J.2
  • 8
    • 0034646418 scopus 로고    scopus 로고
    • Rapid desensitization of the nitric oxide receptor, soluble guanylyl cyclase, underlies diversity of cellular cGMP responses
    • Bellamy T. C., Wood J., Goodwin D. A. and Garthwaite J. (2000) Rapid desensitization of the nitric oxide receptor, soluble guanylyl cyclase, underlies diversity of cellular cGMP responses. Proc. Natl Acad. Sci. USA 97, 2928-2933.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2928-2933
    • Bellamy, T.C.1    Wood, J.2    Goodwin, D.A.3    Garthwaite, J.4
  • 10
    • 0035866058 scopus 로고    scopus 로고
    • Stimulation of nitric oxide-cGMP pathway excites striatal cholinergic intemeurons via protein kinase G activation
    • Centonze D., Pisani A., Bonsi P., Giacomini P., Bemardi G. and Calabresi P. (2001) Stimulation of nitric oxide-cGMP pathway excites striatal cholinergic intemeurons via protein kinase G activation. J. Neurosci. 21, 1393-1400.
    • (2001) J. Neurosci. , vol.21 , pp. 1393-1400
    • Centonze, D.1    Pisani, A.2    Bonsi, P.3    Giacomini, P.4    Bemardi, G.5    Calabresi, P.6
  • 11
    • 0034003405 scopus 로고    scopus 로고
    • Regulation of adenylyl cyclase in the central nervous system
    • Chem Y. (2000) Regulation of adenylyl cyclase in the central nervous system. Cell. Signal. 12, 195-204.
    • (2000) Cell. Signal. , vol.12 , pp. 195-204
    • Chem, Y.1
  • 12
    • 0033519275 scopus 로고    scopus 로고
    • Cyclic AMP phosphodiesterases are localized in regions of the mouse brain associated with reinforcement, movement, and affect
    • Cherry J. A. and Davis R. L. (1999) Cyclic AMP phosphodiesterases are localized in regions of the mouse brain associated with reinforcement, movement, and affect. J. Comp. Neurol. 407, 287-301.
    • (1999) J. Comp. Neurol. , vol.407 , pp. 287-301
    • Cherry, J.A.1    Davis, R.L.2
  • 13
    • 0034103659 scopus 로고    scopus 로고
    • Roles of NMDA receptor activity and nitric oxide production in brain development
    • Contestabile A. (2000) Roles of NMDA receptor activity and nitric oxide production in brain development. Brain Res. Rev. 32, 476-509.
    • (2000) Brain Res. Rev. , vol.32 , pp. 476-509
    • Contestabile, A.1
  • 15
    • 0030944876 scopus 로고    scopus 로고
    • Ionotropic glutamate receptors and nitric oxide synthesis in the rat striatum
    • East S. J., Parry-Jones A. and Brotchie J. M. (1996) Ionotropic glutamate receptors and nitric oxide synthesis in the rat striatum. Neuroreport 8, 71-75.
    • (1996) Neuroreport , vol.8 , pp. 71-75
    • East, S.J.1    Parry-Jones, A.2    Brotchie, J.M.3
  • 16
    • 0015971996 scopus 로고
    • Statistical estimations in enzyme kinetics. The integrated Michaelis equation
    • Femley H. N. (1974) Statistical estimations in enzyme kinetics. The integrated Michaelis equation. Eur. J. Biochem. 43, 377-378.
    • (1974) Eur. J. Biochem. , vol.43 , pp. 377-378
    • Femley, H.N.1
  • 17
    • 0033785602 scopus 로고    scopus 로고
    • Nitric oxide-sensitive guanylyl cyclase activity inhibition through cyclic GMP-dependent dephosphorylation
    • Ferrero R., Rodriguez-Pascual F., Miras-Portugal M. T. and Torres M. (2000) Nitric oxide-sensitive guanylyl cyclase activity inhibition through cyclic GMP-dependent dephosphorylation. J. Neurochem. 75, 2029-2039.
    • (2000) J. Neurochem. , vol.75 , pp. 2029-2039
    • Ferrero, R.1    Rodriguez-Pascual, F.2    Miras-Portugal, M.T.3    Torres, M.4
  • 18
    • 0033572982 scopus 로고    scopus 로고
    • Striatum- and testis-specific phosphodiesterase PDE10A
    • Fujishige K., Kotera J. and Omori K. (1999) Striatum- and testis-specific phosphodiesterase PDE10A. Eur. J. Biochem. 266, 1118-1127.
    • (1999) Eur. J. Biochem. , vol.266 , pp. 1118-1127
    • Fujishige, K.1    Kotera, J.2    Omori, K.3
  • 19
    • 0027332626 scopus 로고
    • Localizations of α1 and β1 subunits of soluble guanylate cyclase in the rat brain
    • Furuyama T., Inagaki S. and Takagi H. (1993) Localizations of α1 and β1 subunits of soluble guanylate cyclase in the rat brain. Brain Res. Mol. Brain Res. 20, 335-344.
    • (1993) Brain Res. Mol. Brain Res. , vol.20 , pp. 335-344
    • Furuyama, T.1    Inagaki, S.2    Takagi, H.3
  • 20
    • 0022002328 scopus 로고
    • Cellular uptake disguises action of L-glutamate on N-methyl-D-aspartate receptors
    • Garthwaite J. (1985) Cellular uptake disguises action of L-glutamate on N-methyl-D-aspartate receptors. Br. J. Pharmacol. 85, 297-307.
    • (1985) Br. J. Pharmacol. , vol.85 , pp. 297-307
    • Garthwaite, J.1
  • 21
    • 0026077959 scopus 로고
    • Glutamate, nitric oxide and cell-cell signalling in the nervous system
    • Garthwaite J. (1991) Glutamate, nitric oxide and cell-cell signalling in the nervous system. Trends Neurosci. 14, 60-67.
    • (1991) Trends Neurosci. , vol.14 , pp. 60-67
    • Garthwaite, J.1
  • 22
    • 0000495909 scopus 로고    scopus 로고
    • The physiological roles of nitric oxide in the central nervous system
    • (Mayer B., ed.). Springer, Berlin
    • Garthwaite J. (2000) The physiological roles of nitric oxide in the central nervous system, in Handbook of Experimental Pharmacology, vol. 143 (Mayer B., ed.), pp. 259-275. Springer, Berlin.
    • (2000) Handbook of Experimental Pharmacology , vol.143 , pp. 259-275
    • Garthwaite, J.1
  • 23
    • 0023101760 scopus 로고
    • Cellular origins of cyclic GMP responses to excitatory amino acid receptor agonists in rat cerebellum in vitro
    • Garthwaite J. and Garthwaite G. (1987) Cellular origins of cyclic GMP responses to excitatory amino acid receptor agonists in rat cerebellum in vitro. J. Neurochem. 48, 29-39.
    • (1987) J. Neurochem. , vol.48 , pp. 29-39
    • Garthwaite, J.1    Garthwaite, G.2
  • 24
    • 0035131718 scopus 로고    scopus 로고
    • Subunits of the nitric oxide receptor, soluble guanylyl cyclase, expressed in rat brain
    • Gibb B. J. and Garthwaite J. (2001) Subunits of the nitric oxide receptor, soluble guanylyl cyclase, expressed in rat brain. Eur. J. Neurosci. 13, 539-544.
    • (2001) Eur. J. Neurosci. , vol.13 , pp. 539-544
    • Gibb, B.J.1    Garthwaite, J.2
  • 25
    • 0018119495 scopus 로고
    • Enzymic regulation of the concentration of cyclic GMP in mouse brain
    • Greenberg L. H., Troyer E., Ferrendelli J. A. and Weiss B. (1978) Enzymic regulation of the concentration of cyclic GMP in mouse brain. Neuropharmacology 17, 737-745.
    • (1978) Neuropharmacology , vol.17 , pp. 737-745
    • Greenberg, L.H.1    Troyer, E.2    Ferrendelli, J.A.3    Weiss, B.4
  • 26
    • 0036455192 scopus 로고    scopus 로고
    • Dynamics of nitric oxide during simulated ischaemia-reperfusion in rat striatal slices measured using an intrinsic biosensor, soluble guanylyl cyclase
    • Griffiths C., Garthwaite J., Goodwin D. A. and Garthwaite J. (2002) Dynamics of nitric oxide during simulated ischaemia-reperfusion in rat striatal slices measured using an intrinsic biosensor, soluble guanylyl cyclase. Eur. J. Neurosci. 15, 962-968.
    • (2002) Eur. J. Neurosci. , vol.15 , pp. 962-968
    • Griffiths, C.1    Garthwaite, J.2    Goodwin, D.A.3    Garthwaite, J.4
  • 27
    • 0032615901 scopus 로고    scopus 로고
    • Cyclic GMP as substrate and regulator of cyclic nucleotide phosphodiesterases (PDEs)
    • Juilfs D. M., Soderling S., Burns F. and Beavo J. A. (1999) Cyclic GMP as substrate and regulator of cyclic nucleotide phosphodiesterases (PDEs). Rev. Physiol. Biochem. Pharmacol. 135, 67-104.
    • (1999) Rev. Physiol. Biochem. Pharmacol. , vol.135 , pp. 67-104
    • Juilfs, D.M.1    Soderling, S.2    Burns, F.3    Beavo, J.A.4
  • 28
    • 0034718509 scopus 로고    scopus 로고
    • Human recombinant soluble guanylyl cyclase: Expression, purification, and regulation
    • Lee Y. C., Martin E. and Murad F. (2000) Human recombinant soluble guanylyl cyclase: expression, purification, and regulation. Proc. Natl Acad. Sci. USA 97, 10763-10768.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10763-10768
    • Lee, Y.C.1    Martin, E.2    Murad, F.3
  • 29
    • 0019978517 scopus 로고
    • Properties of purified soluble guanylate cyclase activated by nitric oxide and sodium nitroprusside
    • Lewicki J. A., Brandwein H. J., Mittal C. K., Arnold W. P. and Murad F. (1982) Properties of purified soluble guanylate cyclase activated by nitric oxide and sodium nitroprusside. J. Cyclic Nucleotide Res. 8, 17-25.
    • (1982) J. Cyclic Nucleotide Res. , vol.8 , pp. 17-25
    • Lewicki, J.A.1    Brandwein, H.J.2    Mittal, C.K.3    Arnold, W.P.4    Murad, F.5
  • 30
    • 0029075805 scopus 로고
    • Type III cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE3 gene family)
    • Manganiello V. C., Taira M., Degerman E. and Belfrage P. (1995) Type III cGMP-inhibited cyclic nucleotide phosphodiesterases (PDE3 gene family). Cell. Signal. 7, 445-455.
    • (1995) Cell. Signal. , vol.7 , pp. 445-455
    • Manganiello, V.C.1    Taira, M.2    Degerman, E.3    Belfrage, P.4
  • 31
    • 0031562370 scopus 로고    scopus 로고
    • Region-specific developmental patterns of atrial natriuretic factor-and nitric oxide-activated guanylyl cyclases in the postnatal frontal rat brain
    • Markerink-van Ittersum M., Steinbusch H. W. and de Vente J. (1997) Region-specific developmental patterns of atrial natriuretic factor-and nitric oxide-activated guanylyl cyclases in the postnatal frontal rat brain. Neuroscience 78, 571-587.
    • (1997) Neuroscience , vol.78 , pp. 571-587
    • Markerink-van Ittersum, M.1    Steinbusch, H.W.2    De Vente, J.3
  • 32
    • 0029962380 scopus 로고    scopus 로고
    • Rapid regulation of PDE-2 and PDE-4 cyclic AMP phosphodiesterase activity following ligation of the T cell antigen receptor on thymocytes: Analysis using the selective inhibitors erythro-9-(2-hydroxy-3-nonyl)-adenine (EHNA) and rolipram
    • Michie A. M., Lobban M., Muller T., Harnett M. M. and Houslay M. D. (1996) Rapid regulation of PDE-2 and PDE-4 cyclic AMP phosphodiesterase activity following ligation of the T cell antigen receptor on thymocytes: analysis using the selective inhibitors erythro-9-(2-hydroxy-3-nonyl)-adenine (EHNA) and rolipram. Cell. Signal. 8, 97-110.
    • (1996) Cell. Signal. , vol.8 , pp. 97-110
    • Michie, A.M.1    Lobban, M.2    Muller, T.3    Harnett, M.M.4    Houslay, M.D.5
  • 33
    • 0035889091 scopus 로고    scopus 로고
    • Rapid nitric oxide-induced desensitization of the cGMP response is caused by increased activity of phosphodiesterase type 5 paralleled by phosphorylation of the enzyme
    • Mullershausen F., Russwurm M., Thompson W. J., Liu L., Koesling D. and Friebe A. (2001) Rapid nitric oxide-induced desensitization of the cGMP response is caused by increased activity of phosphodiesterase type 5 paralleled by phosphorylation of the enzyme. J. Cell. Biol. 155, 271-278.
    • (2001) J. Cell. Biol. , vol.155 , pp. 271-278
    • Mullershausen, F.1    Russwurm, M.2    Thompson, W.J.3    Liu, L.4    Koesling, D.5    Friebe, A.6
  • 34
    • 0028196632 scopus 로고
    • Expression of a calmodulin-dependent phosphodiesterase isoform (PDE1B1) correlates with brain regions having extensive dopaminergic innervation
    • Polli J. W. and Kincaid R. L. (1994) Expression of a calmodulin-dependent phosphodiesterase isoform (PDE1B1) correlates with brain regions having extensive dopaminergic innervation. J. Neurosci. 14, 1251-1261.
    • (1994) J. Neurosci. , vol.14 , pp. 1251-1261
    • Polli, J.W.1    Kincaid, R.L.2
  • 35
    • 0028176041 scopus 로고
    • Protein kinase C-dependent desensitization of the atrial natriuretic peptide receptor is mediated by dephosphorylation
    • Potter L. R. and Garbers D. L. (1994) Protein kinase C-dependent desensitization of the atrial natriuretic peptide receptor is mediated by dephosphorylation. J. Biol. Chem. 269, 14636-14642.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14636-14642
    • Potter, L.R.1    Garbers, D.L.2
  • 36
    • 0035101782 scopus 로고    scopus 로고
    • Nitric oxide as modulator of neuronal function
    • Prast H. and Philippu A. (2001) Nitric oxide as modulator of neuronal function. Prog. Neurobiol. 64, 51-68.
    • (2001) Prog. Neurobiol. , vol.64 , pp. 51-68
    • Prast, H.1    Philippu, A.2
  • 37
    • 0029876116 scopus 로고    scopus 로고
    • Differential cellular pattern of gene expression for two distinct cGMP-inhibited cyclic nucleotide phosphodiesterases in developing and mature rat brain
    • Reinhardt R. R. and Bondy C. A. (1996) Differential cellular pattern of gene expression for two distinct cGMP-inhibited cyclic nucleotide phosphodiesterases in developing and mature rat brain. Neuroscience 72, 567-578.
    • (1996) Neuroscience , vol.72 , pp. 567-578
    • Reinhardt, R.R.1    Bondy, C.A.2
  • 38
  • 39
    • 0010613882 scopus 로고    scopus 로고
    • cGMP-inhibitied phosphodiesterases (PDE-3)
    • Academic Press, London, UK
    • Schudt D. A., Dent G. and Rabe K. F. (1996a) cGMP-inhibitied phosphodiesterases (PDE-3), in Phosphodiesterase Inhibitors, pp. 89-109. Academic Press, London, UK.
    • (1996) Phosphodiesterase Inhibitors , pp. 89-109
    • Schudt, D.A.1    Dent, G.2    Rabe, K.F.3
  • 40
    • 0003338738 scopus 로고    scopus 로고
    • Interaction of PDE4 inhibitors with enzymes
    • Academic Press, London
    • Schudt D. A., Dent G. and Rabe K. F. (1996b) Interaction of PDE4 inhibitors with enzymes, in Phosphodiesterase Inhibitors, pp. 110-126. Academic Press, London.
    • (1996) Phosphodiesterase Inhibitors , pp. 110-126
    • Schudt, D.A.1    Dent, G.2    Rabe, K.F.3
  • 41
    • 0034009080 scopus 로고    scopus 로고
    • Regulation of cAMP and cGMP signaling: New phosphodiesterases and new functions
    • Soderling S. H. and Beavo J. A. (2000) Regulation of cAMP and cGMP signaling: new phosphodiesterases and new functions. Curr. Opin. Cell Biol. 12, 174-179.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 174-179
    • Soderling, S.H.1    Beavo, J.A.2
  • 42
    • 0027384515 scopus 로고
    • The nitric oxide-cyclic GMP signalling pathway in rat brain
    • Southam E. and Garthwaite J. (1993) The nitric oxide-cyclic GMP signalling pathway in rat brain. Neuropharmacology 32, 1267-1277.
    • (1993) Neuropharmacology , vol.32 , pp. 1267-1277
    • Southam, E.1    Garthwaite, J.2
  • 43
    • 0035847253 scopus 로고    scopus 로고
    • The effects of phosphodiesterase inhibition on cyclic GMP and cyclic AMP accumulation in the hippocampus of the rat
    • van Staveren W. C., Markerink-van Ittersum M., Steinbusch H. W. and de Vente J. (2001) The effects of phosphodiesterase inhibition on cyclic GMP and cyclic AMP accumulation in the hippocampus of the rat. Brain Res. 888, 275-286.
    • (2001) Brain Res. , vol.888 , pp. 275-286
    • Van Staveren, W.C.1    Markerink-van Ittersum, M.2    Steinbusch, H.W.3    De Vente, J.4
  • 44
    • 0033818302 scopus 로고    scopus 로고
    • Nitric oxide can differentially modulate striatal neurotransmitter concentrations via soluble guanylate cyclase and peroxynitrite formation
    • Trabace L. and Kendrick K. M. (2000) Nitric oxide can differentially modulate striatal neurotransmitter concentrations via soluble guanylate cyclase and peroxynitrite formation. J. Neurochem. 75, 1664-1674.
    • (2000) J. Neurochem. , vol.75 , pp. 1664-1674
    • Trabace, L.1    Kendrick, K.M.2
  • 45
    • 0032993016 scopus 로고    scopus 로고
    • Inhibition of cyclic GMP-binding cyclic GMP-specific phosphodiesterase (Type 5) by sildenafil and related compounds
    • Turko I. V., Ballard S. A., Francis S. H. and Corbin J. D. (1999) Inhibition of cyclic GMP-binding cyclic GMP-specific phosphodiesterase (Type 5) by sildenafil and related compounds. Mol. Pharmacol. 56, 124-130.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 124-130
    • Turko, I.V.1    Ballard, S.A.2    Francis, S.H.3    Corbin, J.D.4
  • 46
    • 0026531143 scopus 로고
    • Histochemical mapping of nitric oxide synthase in the rat brain
    • Vincent S. R. and Kimura H. (1992) Histochemical mapping of nitric oxide synthase in the rat brain. Neuroscience 46, 755-784.
    • (1992) Neuroscience , vol.46 , pp. 755-784
    • Vincent, S.R.1    Kimura, H.2
  • 47
    • 0028218265 scopus 로고
    • Differential expression of the 61 kDa and 63 kDa calmodulindependent phosphodiesterases in the mouse brain
    • Yan C., Bentley J. K., Sonnenburg W. K. and Beavo J. A. (1994) Differential expression of the 61 kDa and 63 kDa calmodulindependent phosphodiesterases in the mouse brain. J. Neurosci. 14, 973-984.
    • (1994) J. Neurosci. , vol.14 , pp. 973-984
    • Yan, C.1    Bentley, J.K.2    Sonnenburg, W.K.3    Beavo, J.A.4
  • 48
    • 0034819381 scopus 로고    scopus 로고
    • Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A) Comparison of rat and human PDE11A splicing variants
    • Yuasa K., Ohgaru T., Asahina M. and Omori K. (2001) Identification of rat cyclic nucleotide phosphodiesterase 11A (PDE11A) Comparison of rat and human PDE11A splicing variants. Eur. J. Biochem. 268, 4440-4448.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 4440-4448
    • Yuasa, K.1    Ohgaru, T.2    Asahina, M.3    Omori, K.4


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