메뉴 건너뛰기




Volumn 21, Issue 1, 2005, Pages 17-21

Parasite nucleotide-metabolizing enzymes and host purinergic signalling

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDE; PURINE RECEPTOR;

EID: 11444268861     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2004.10.005     Document Type: Article
Times cited : (44)

References (54)
  • 1
    • 0027962545 scopus 로고
    • Purinoceptors: Are there families of P2X and P2Y purinoceptors?
    • M.P. Abbracchio, and G. Burnstock Purinoceptors: are there families of P2X and P2Y purinoceptors? Pharmacol. Ther. 64 1994 445 475
    • (1994) Pharmacol. Ther. , vol.64 , pp. 445-475
    • Abbracchio, M.P.1    Burnstock, G.2
  • 2
    • 0035253835 scopus 로고    scopus 로고
    • Nucleotide receptors: An emerging family of regulatory molecules in blood cells
    • F. Di Virgilio Nucleotide receptors: an emerging family of regulatory molecules in blood cells Blood 97 2001 587 600
    • (2001) Blood , vol.97 , pp. 587-600
    • Di Virgilio, F.1
  • 3
    • 0035040532 scopus 로고    scopus 로고
    • Molecular approach to adenosine receptors: Receptor-mediated mechanisms of tissue protection
    • J. Linden Molecular approach to adenosine receptors: receptor-mediated mechanisms of tissue protection Annu. Rev. Pharmacol. Toxicol. 41 2001 775 787
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 775-787
    • Linden, J.1
  • 4
    • 0035924320 scopus 로고    scopus 로고
    • Role of G-protein-coupled adenosine receptors in downregulation of inflammation and protection from tissue damage
    • A. Ohta, and M. Sitkovsky Role of G-protein-coupled adenosine receptors in downregulation of inflammation and protection from tissue damage Nature 414 2001 916 920
    • (2001) Nature , vol.414 , pp. 916-920
    • Ohta, A.1    Sitkovsky, M.2
  • 5
    • 0038603203 scopus 로고    scopus 로고
    • Adenosine affects expression of membrane molecules, cytokine and chemokine release, and the T-cell stimulatory capacity of human dendritic cells
    • E. Panther Adenosine affects expression of membrane molecules, cytokine and chemokine release, and the T-cell stimulatory capacity of human dendritic cells Blood 101 2003 3985 3990
    • (2003) Blood , vol.101 , pp. 3985-3990
    • Panther, E.1
  • 6
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine: An endogenous regulator of innate immunity
    • G. Hasko, and B.N. Cronstein Adenosine: an endogenous regulator of innate immunity Trends Immunol. 25 2004 33 39
    • (2004) Trends Immunol. , vol.25 , pp. 33-39
    • Hasko, G.1    Cronstein, B.N.2
  • 7
    • 0021989615 scopus 로고
    • Antihemostatic, antiinflammatory, and immunosuppressive properties of the saliva of a tick, Ixodes dammini
    • J.M. Ribeiro Antihemostatic, antiinflammatory, and immunosuppressive properties of the saliva of a tick, Ixodes dammini J. Exp. Med. 161 1985 332 344
    • (1985) J. Exp. Med. , vol.161 , pp. 332-344
    • Ribeiro, J.M.1
  • 8
    • 0037208861 scopus 로고    scopus 로고
    • Role of arthropod saliva in blood feeding: Sialome and post-sialome perspectives
    • J.M. Ribeiro, and I.M. Francischetti Role of arthropod saliva in blood feeding: sialome and post-sialome perspectives Annu. Rev. Entomol. 48 2003 73 88
    • (2003) Annu. Rev. Entomol. , vol.48 , pp. 73-88
    • Ribeiro, J.M.1    Francischetti, I.M.2
  • 9
    • 0036720235 scopus 로고    scopus 로고
    • Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis
    • K. Gounaris Nucleotidase cascades are catalyzed by secreted proteins of the parasitic nematode Trichinella spiralis Infect. Immun. 70 2002 4917 4924
    • (2002) Infect. Immun. , vol.70 , pp. 4917-4924
    • Gounaris, K.1
  • 10
    • 0033021431 scopus 로고    scopus 로고
    • Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: Sequestration of ATP from macrophage P2Z receptors?
    • O. Zaborina Secretion of ATP-utilizing enzymes, nucleoside diphosphate kinase and ATPase, by Mycobacterium bovis BCG: sequestration of ATP from macrophage P2Z receptors? Mol. Microbiol. 31 1999 1333 1343
    • (1999) Mol. Microbiol. , vol.31 , pp. 1333-1343
    • Zaborina, O.1
  • 11
    • 0032857065 scopus 로고    scopus 로고
    • P2Z-independent and P2Z receptor-mediated macrophage killing by Pseudomonas aeruginosa isolated from cystic fibrosis patients
    • O. Zaborina P2Z-independent and P2Z receptor-mediated macrophage killing by Pseudomonas aeruginosa isolated from cystic fibrosis patients Infect. Immun. 67 1999 5231 5242
    • (1999) Infect. Immun. , vol.67 , pp. 5231-5242
    • Zaborina, O.1
  • 12
    • 0033855317 scopus 로고    scopus 로고
    • Phagocytic cell killing mediated by secreted cytotoxic factors of Vibrio cholerae
    • V. Punj Phagocytic cell killing mediated by secreted cytotoxic factors of Vibrio cholerae Infect. Immun. 68 2000 4930 4937
    • (2000) Infect. Immun. , vol.68 , pp. 4930-4937
    • Punj, V.1
  • 13
    • 0036713844 scopus 로고    scopus 로고
    • Toward a description of the sialome of the adult female mosquito Aedes aegypti
    • J.G. Valenzuela Toward a description of the sialome of the adult female mosquito Aedes aegypti Insect Biochem. Mol. Biol. 32 2002 1101 1122
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1101-1122
    • Valenzuela, J.G.1
  • 14
    • 0037211629 scopus 로고    scopus 로고
    • The salivary purine nucleosidase of the mosquito, Aedes aegypti
    • J.M. Ribeiro, and J.G. Valenzuela The salivary purine nucleosidase of the mosquito, Aedes aegypti Insect Biochem. Mol. Biol. 33 2003 13 22
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 13-22
    • Ribeiro, J.M.1    Valenzuela, J.G.2
  • 15
    • 0028859094 scopus 로고
    • The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotidase family
    • D.E. Champagne The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5′-nucleotidase family Proc. Natl. Acad. Sci. U. S. A. 92 1995 694 698
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 694-698
    • Champagne, D.E.1
  • 16
    • 2442574901 scopus 로고    scopus 로고
    • Triatoma infestans apyrases belong to the 5′-nucleotidase family
    • E. Faudry Triatoma infestans apyrases belong to the 5′-nucleotidase family J. Biol. Chem. 279 2004 19607 19613
    • (2004) J. Biol. Chem. , vol.279 , pp. 19607-19613
    • Faudry, E.1
  • 17
    • 0027571229 scopus 로고
    • The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli
    • P. Willadsen The nucleotidase of Boophilus microplus and its relationship to enzymes from the rat and Escherichia coli Insect Biochem. Mol. Biol. 23 1993 291 295
    • (1993) Insect Biochem. Mol. Biol. , vol.23 , pp. 291-295
    • Willadsen, P.1
  • 18
    • 0032515084 scopus 로고    scopus 로고
    • Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme
    • J.G. Valenzuela Purification, cloning, and expression of an apyrase from the bed bug Cimex lectularius. A new type of nucleotide-binding enzyme J. Biol. Chem. 273 1998 30583 30590
    • (1998) J. Biol. Chem. , vol.273 , pp. 30583-30590
    • Valenzuela, J.G.1
  • 19
    • 0035144334 scopus 로고    scopus 로고
    • The salivary apyrase of the blood-sucking sand fly Phlebotomus papatasi belongs to the novel Cimex family of apyrases
    • J.G. Valenzuela The salivary apyrase of the blood-sucking sand fly Phlebotomus papatasi belongs to the novel Cimex family of apyrases J. Exp. Biol. 204 2001 229 237
    • (2001) J. Exp. Biol. , vol.204 , pp. 229-237
    • Valenzuela, J.G.1
  • 20
    • 0036149221 scopus 로고    scopus 로고
    • Cell damage excites nociceptors through release of cytosolic ATP
    • S.P. Cook, and E.W. McCleskey Cell damage excites nociceptors through release of cytosolic ATP Pain 95 2002 41 47
    • (2002) Pain , vol.95 , pp. 41-47
    • Cook, S.P.1    McCleskey, E.W.2
  • 21
    • 0034977188 scopus 로고    scopus 로고
    • ADP and platelets: The end of the beginning
    • D. Woulfe ADP and platelets: the end of the beginning J. Clin. Invest. 107 2001 1503 1505
    • (2001) J. Clin. Invest. , vol.107 , pp. 1503-1505
    • Woulfe, D.1
  • 22
    • 1542346410 scopus 로고    scopus 로고
    • Clinical and molecular pharmacologic characteristics of adenosine-induced vasodilation
    • I. Biaggioni Clinical and molecular pharmacologic characteristics of adenosine-induced vasodilation Clin. Pharmacol. Ther. 75 2004 137 139
    • (2004) Clin. Pharmacol. Ther. , vol.75 , pp. 137-139
    • Biaggioni, I.1
  • 23
    • 0026502768 scopus 로고
    • Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide
    • E.A. Lerner, and C.B. Shoemaker Maxadilan. Cloning and functional expression of the gene encoding this potent vasodilator peptide J. Biol. Chem. 267 1992 1062 1066
    • (1992) J. Biol. Chem. , vol.267 , pp. 1062-1066
    • Lerner, E.A.1    Shoemaker, C.B.2
  • 24
    • 0033965558 scopus 로고    scopus 로고
    • Adenosine and inosine increase cutaneous vasopermeability by activating A(3) receptors on mast cells
    • S.L. Tilley Adenosine and inosine increase cutaneous vasopermeability by activating A(3) receptors on mast cells J. Clin. Invest. 105 2000 361 367
    • (2000) J. Clin. Invest. , vol.105 , pp. 361-367
    • Tilley, S.L.1
  • 25
    • 0035746062 scopus 로고    scopus 로고
    • The salivary adenosine deaminase activity of the mosquitoes Culex quinquefasciatus and Aedes aegypti
    • J.M. Ribeiro The salivary adenosine deaminase activity of the mosquitoes Culex quinquefasciatus and Aedes aegypti J. Exp. Biol. 204 2001 2001 2010
    • (2001) J. Exp. Biol. , vol.204 , pp. 2001-2010
    • Ribeiro, J.M.1
  • 26
    • 0035007318 scopus 로고    scopus 로고
    • Secreted variant of nucleoside diphosphate kinase from the intracellular parasitic nematode Trichinella spiralis
    • K. Gounaris Secreted variant of nucleoside diphosphate kinase from the intracellular parasitic nematode Trichinella spiralis Infect. Immun. 69 2001 3658 3662
    • (2001) Infect. Immun. , vol.69 , pp. 3658-3662
    • Gounaris, K.1
  • 27
    • 2942562559 scopus 로고    scopus 로고
    • A nucleotidase with unique catalytic properties is secreted by Trichinella spiralis
    • K. Gounaris A nucleotidase with unique catalytic properties is secreted by Trichinella spiralis Mol. Biochem. Parasitol. 136 2004 257 264
    • (2004) Mol. Biochem. Parasitol. , vol.136 , pp. 257-264
    • Gounaris, K.1
  • 28
    • 0033766981 scopus 로고    scopus 로고
    • Extracellular metabolism of ATP and other nucleotides
    • H. Zimmermann Extracellular metabolism of ATP and other nucleotides Naunyn Schmiedebergs Arch. Pharmacol. 362 2000 299 309
    • (2000) Naunyn Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 299-309
    • Zimmermann, H.1
  • 29
    • 0038608023 scopus 로고    scopus 로고
    • Comprehensive analysis of the secreted proteins of the parasite Haemonchus contortus reveals extensive sequence variation and differential immune recognition
    • A.P. Yatsuda Comprehensive analysis of the secreted proteins of the parasite Haemonchus contortus reveals extensive sequence variation and differential immune recognition J. Biol. Chem. 278 2003 16941 16951
    • (2003) J. Biol. Chem. , vol.278 , pp. 16941-16951
    • Yatsuda, A.P.1
  • 30
    • 0031754497 scopus 로고    scopus 로고
    • Receptors for purines and pyrimidines
    • V. Ralevic, and G. Burnstock Receptors for purines and pyrimidines Pharmacol. Rev. 50 1998 413 492
    • (1998) Pharmacol. Rev. , vol.50 , pp. 413-492
    • Ralevic, V.1    Burnstock, G.2
  • 31
    • 0033680583 scopus 로고    scopus 로고
    • P2 purinergic receptors: Modulation of cell function and therapeutic potential
    • G. Burnstock, and M. Williams P2 purinergic receptors: modulation of cell function and therapeutic potential J. Pharmacol. Exp. Ther. 295 2000 862 869
    • (2000) J. Pharmacol. Exp. Ther. , vol.295 , pp. 862-869
    • Burnstock, G.1    Williams, M.2
  • 32
    • 0035854734 scopus 로고    scopus 로고
    • P2Y(6) nucleotide receptor mediates monocyte interleukin-8 production in response to UDP or lipopolysaccharide
    • M. Warny P2Y(6) nucleotide receptor mediates monocyte interleukin-8 production in response to UDP or lipopolysaccharide J. Biol. Chem. 276 2001 26051 26056
    • (2001) J. Biol. Chem. , vol.276 , pp. 26051-26056
    • Warny, M.1
  • 33
    • 0037314348 scopus 로고    scopus 로고
    • P2Y6 receptor mediates colonic NaCl secretion via differential activation of cAMP-mediated transport
    • M. Kottgen P2Y6 receptor mediates colonic NaCl secretion via differential activation of cAMP-mediated transport J. Clin. Invest. 111 2003 371 379
    • (2003) J. Clin. Invest. , vol.111 , pp. 371-379
    • Kottgen, M.1
  • 34
    • 0037399429 scopus 로고    scopus 로고
    • "The force be with you": ATP in gut mechanosensory transduction
    • H.J. Cooke "The force be with you": ATP in gut mechanosensory transduction News Physiol. Sci. 18 2003 43 49
    • (2003) News Physiol. Sci. , vol.18 , pp. 43-49
    • Cooke, H.J.1
  • 35
    • 1342264245 scopus 로고    scopus 로고
    • Immunomodulatory and neuroprotective effects of inosine
    • G. Hasko Immunomodulatory and neuroprotective effects of inosine Trends Pharmacol. Sci. 25 2004 152 157
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 152-157
    • Hasko, G.1
  • 36
    • 0033565879 scopus 로고    scopus 로고
    • Chemotaxis of rat mast cells toward adenine nucleotides
    • M.A. McCloskey Chemotaxis of rat mast cells toward adenine nucleotides J. Immunol. 163 1999 970 977
    • (1999) J. Immunol. , vol.163 , pp. 970-977
    • McCloskey, M.A.1
  • 37
    • 0034684681 scopus 로고    scopus 로고
    • Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1
    • P.A. Knight Delayed expulsion of the nematode Trichinella spiralis in mice lacking the mucosal mast cell-specific granule chymase, mouse mast cell protease-1 J. Exp. Med. 192 2000 1849 1856
    • (2000) J. Exp. Med. , vol.192 , pp. 1849-1856
    • Knight, P.A.1
  • 38
    • 0037596643 scopus 로고    scopus 로고
    • Mast cells disrupt epithelial barrier function during enteric nematode infection
    • J.R. McDermott Mast cells disrupt epithelial barrier function during enteric nematode infection Proc. Natl. Acad. Sci. U. S. A. 100 2003 7761 7766
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7761-7766
    • McDermott, J.R.1
  • 39
    • 0031590303 scopus 로고    scopus 로고
    • Th2-mediated host protective immunity to intestinal nematode infections
    • R.K. Grencis Th2-mediated host protective immunity to intestinal nematode infections Philos. Trans. R. Soc. Lond. B Biol. Sci. 352 1997 1377 1384
    • (1997) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.352 , pp. 1377-1384
    • Grencis, R.K.1
  • 40
    • 0030185024 scopus 로고    scopus 로고
    • Nucleotide-induced mucin release from primary hamster tracheal surface epithelial cells involves the P2u purinoceptor
    • K.C. Kim Nucleotide-induced mucin release from primary hamster tracheal surface epithelial cells involves the P2u purinoceptor Eur. Respir. J. 9 1996 542 548
    • (1996) Eur. Respir. J. , vol.9 , pp. 542-548
    • Kim, K.C.1
  • 41
    • 0037380783 scopus 로고    scopus 로고
    • Loss of nucleotide regulation of epithelial chloride transport in the jejunum of P2Y4-null mice
    • B. Robaye Loss of nucleotide regulation of epithelial chloride transport in the jejunum of P2Y4-null mice Mol. Pharmacol. 63 2003 777 783
    • (2003) Mol. Pharmacol. , vol.63 , pp. 777-783
    • Robaye, B.1
  • 42
    • 1642296755 scopus 로고    scopus 로고
    • Purinergic regulation of epithelial transport
    • R.E. Bucheimer, and J. Linden Purinergic regulation of epithelial transport J. Physiol. 555 2004 311 321
    • (2004) J. Physiol. , vol.555 , pp. 311-321
    • Bucheimer, R.E.1    Linden, J.2
  • 43
    • 0034613299 scopus 로고    scopus 로고
    • Constitutive release of ATP and evidence for major contribution of ecto- nucleotide pyrophosphatase and nucleoside diphosphokinase to extracellular nucleotide concentrations
    • E.R. Lazarowski Constitutive release of ATP and evidence for major contribution of ecto- nucleotide pyrophosphatase and nucleoside diphosphokinase to extracellular nucleotide concentrations J. Biol. Chem. 275 2000 31061 31068
    • (2000) J. Biol. Chem. , vol.275 , pp. 31061-31068
    • Lazarowski, E.R.1
  • 44
    • 0031469951 scopus 로고    scopus 로고
    • Identification of serine/threonine protein kinases secreted by Trichinella spiralis infective larvae
    • S.R. Arden Identification of serine/threonine protein kinases secreted by Trichinella spiralis infective larvae Mol. Biochem. Parasitol. 90 1997 111 119
    • (1997) Mol. Biochem. Parasitol. , vol.90 , pp. 111-119
    • Arden, S.R.1
  • 45
    • 0034693289 scopus 로고    scopus 로고
    • A reversible protein phosphorylation system is present at the surface of infective larvae of the parasitic nematode Trichinella spiralis
    • V.P. Smith A reversible protein phosphorylation system is present at the surface of infective larvae of the parasitic nematode Trichinella spiralis FEBS Lett. 483 2000 104 108
    • (2000) FEBS Lett. , vol.483 , pp. 104-108
    • Smith, V.P.1
  • 46
    • 0032754759 scopus 로고    scopus 로고
    • Ecto-protein kinases: Ecto-domain phosphorylation as a novel target for pharmacological manipulation?
    • F.A. Redegeld Ecto-protein kinases: ecto-domain phosphorylation as a novel target for pharmacological manipulation? Trends Pharmacol. Sci. 20 1999 453 459
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 453-459
    • Redegeld, F.A.1
  • 47
    • 0033760251 scopus 로고    scopus 로고
    • Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: External-ATP-dependent, P2Z-receptor-mediated necrosis and ATP-independent, caspase-mediated apoptosis
    • O. Zaborina Secreted products of a nonmucoid Pseudomonas aeruginosa strain induce two modes of macrophage killing: external-ATP-dependent, P2Z-receptor-mediated necrosis and ATP-independent, caspase-mediated apoptosis Microbiology 146 2000 2521 2530
    • (2000) Microbiology , vol.146 , pp. 2521-2530
    • Zaborina, O.1
  • 48
    • 0033945304 scopus 로고    scopus 로고
    • Clinical and environmental isolates of Burkholderia cepacia exhibit differential cytotoxicity towards macrophages and mast cells
    • A. Melnikov Clinical and environmental isolates of Burkholderia cepacia exhibit differential cytotoxicity towards macrophages and mast cells Mol. Microbiol. 36 2000 1481 1493
    • (2000) Mol. Microbiol. , vol.36 , pp. 1481-1493
    • Melnikov, A.1
  • 49
    • 0030840444 scopus 로고    scopus 로고
    • ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors
    • D.A. Lammas ATP-induced killing of mycobacteria by human macrophages is mediated by purinergic P2Z(P2X7) receptors Immunity 7 1997 433 444
    • (1997) Immunity , vol.7 , pp. 433-444
    • Lammas, D.A.1
  • 50
    • 0035884993 scopus 로고    scopus 로고
    • ATP stimulates human macrophages to kill intracellular virulent Mycobacterium tuberculosis via calcium-dependent phagosome-lysosome fusion
    • D.J. Kusner, and J.A. Barton ATP stimulates human macrophages to kill intracellular virulent Mycobacterium tuberculosis via calcium-dependent phagosome-lysosome fusion J. Immunol. 167 2001 3308 3315
    • (2001) J. Immunol. , vol.167 , pp. 3308-3315
    • Kusner, D.J.1    Barton, J.A.2
  • 51
    • 0033565269 scopus 로고    scopus 로고
    • Cutting edge: Purinergic signaling regulates radical-mediated bacterial killing mechanisms in macrophages through a P2X7-independent mechanism
    • A. Sikora Cutting edge: purinergic signaling regulates radical-mediated bacterial killing mechanisms in macrophages through a P2X7-independent mechanism J. Immunol. 163 1999 558 561
    • (1999) J. Immunol. , vol.163 , pp. 558-561
    • Sikora, A.1
  • 52
    • 0032524883 scopus 로고    scopus 로고
    • Induced activation of the Toxoplasma gondii nucleoside triphosphate hydrolase leads to depletion of host cell ATP levels and rapid exit of intracellular parasites from infected cells
    • J.A. Silverman Induced activation of the Toxoplasma gondii nucleoside triphosphate hydrolase leads to depletion of host cell ATP levels and rapid exit of intracellular parasites from infected cells J. Biol. Chem. 273 1998 12352 12359
    • (1998) J. Biol. Chem. , vol.273 , pp. 12352-12359
    • Silverman, J.A.1
  • 53
    • 0035209620 scopus 로고    scopus 로고
    • International Union of Pharmacology. XXV. Nomenclature and classification of adenosine receptors
    • B.B. Fredholm International Union of Pharmacology. XXV. Nomenclature and classification of adenosine receptors rPharmacol. Rev. 53 2001 527 552
    • (2001) RPharmacol. Rev. , vol.53 , pp. 527-552
    • Fredholm, B.B.1
  • 54
    • 0033152549 scopus 로고    scopus 로고
    • Two novel families of ectonucleotidases: Molecular structures, catalytic properties and a search for function
    • H. Zimmermann Two novel families of ectonucleotidases: molecular structures, catalytic properties and a search for function Trends Pharmacol. Sci. 20 1999 231 236
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 231-236
    • Zimmermann, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.