메뉴 건너뛰기




Volumn 115, Issue 1, 2010, Pages 183-193

Mice treated with chlorpyrifos or chlorpyrifos oxon have organophosphorylated tubulin in the brain and disrupted microtubule structures, suggesting a role for tubulin in neurotoxicity associated with exposure to organophosphorus agents

Author keywords

Chlorpyrifos; Mass spectrometry; Nanoimaging; Neurotoxicity; Tubulin

Indexed keywords

ACETYLCHOLINESTERASE; ANAZOLENE SODIUM; BETA TUBULIN; CHLORPYRIFOS; CHLORPYRIFOS OXON; ORGANOPHOSPHORUS COMPOUND; TYROSINE; UNCLASSIFIED DRUG; CHOLINESTERASE; DRUG DERIVATIVE; INSECTICIDE; MICROTUBULE ASSOCIATED PROTEIN; O,O DIETHYL O 3,5,6 TRICHLORO 2 PYRIDYL PHOSPHATE; O,O-DIETHYL O-3,5,6-TRICHLORO-2-PYRIDYL PHOSPHATE; ORGANOPHOSPHATE; TUBULIN; TUBULIN MODULATOR;

EID: 79551685829     PISSN: 10966080     EISSN: 10960929     Source Type: Journal    
DOI: 10.1093/toxsci/kfq032     Document Type: Article
Times cited : (87)

References (52)
  • 1
    • 0027439722 scopus 로고
    • Enhanced calmodulin binding concurrent with increased kinase-dependent phosphorylation of cytoskeletal proteins following a single subcutaneous injection of diisopropyl phosphorofluoridate in hens
    • Abou-Donia, M. B., Viana, M. E., Gupta, R. P., and Anderson, J. K. (1993). Enhanced calmodulin binding concurrent with increased kinase-dependent phosphorylation of cytoskeletal proteins following a single subcutaneous injection of diisopropyl phosphorofluoridate in hens. Neurochem. Int. 22, 165-173.
    • (1993) Neurochem. Int. , vol.22 , pp. 165-173
    • Abou-Donia, M.B.1    Viana, M.E.2    Gupta, R.P.3    Anderson, J.K.4
  • 2
    • 0242539881 scopus 로고    scopus 로고
    • Serotonergic systems targeted by developmental exposure to chlorpyrifos: effects during different critical periods
    • Aldridge, J. E., Seidler, F. J., Meyer, A., Thillai, I., and Slotkin, T. A. (2003). Serotonergic systems targeted by developmental exposure to chlorpyrifos: effects during different critical periods. Environ. Health Perspect. 111, 1736-1743.
    • (2003) Environ. Health Perspect. , vol.111 , pp. 1736-1743
    • Aldridge, J.E.1    Seidler, F.J.2    Meyer, A.3    Thillai, I.4    Slotkin, T.A.5
  • 3
    • 0028227962 scopus 로고
    • Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease
    • Alonso, A. C., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1994). Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 91, 5562-5566.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 5562-5566
    • Alonso, A.C.1    Zaidi, T.2    Grundke-Iqbal, I.3    Iqbal, K.4
  • 4
    • 0031713093 scopus 로고    scopus 로고
    • Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon
    • Amitai, G., Moorad, D., Adani, R., and Doctor, B. P. (1998). Inhibition of acetylcholinesterase and butyrylcholinesterase by chlorpyrifos-oxon. Biochem. Pharmacol. 56, 293-299.
    • (1998) Biochem. Pharmacol. , vol.56 , pp. 293-299
    • Amitai, G.1    Moorad, D.2    Adani, R.3    Doctor, B.P.4
  • 5
    • 0035815482 scopus 로고    scopus 로고
    • Possible role of enhanced microtubule phosphorylation in dichlorvos induced delayed neurotoxicity in rat
    • Choudhary, S., Joshi, K., and Gill, K. D. (2001). Possible role of enhanced microtubule phosphorylation in dichlorvos induced delayed neurotoxicity in rat. Brain Res. 897, 60-70.
    • (2001) Brain Res , vol.897 , pp. 60-70
    • Choudhary, S.1    Joshi, K.2    Gill, K.D.3
  • 6
    • 65249107203 scopus 로고    scopus 로고
    • Microtubule assembly, organization and dynamics in axons and dendrites
    • Conde, C., and Caceres, A. (2009). Microtubule assembly, organization and dynamics in axons and dendrites. Nat. Rev. Neurosci. 10, 319-332.
    • (2009) Nat. Rev. Neurosci. , vol.10 , pp. 319-332
    • Conde, C.1    Caceres, A.2
  • 7
    • 0025779219 scopus 로고
    • Dependency of microtubule-associated proteins (MAPs) for tubulin stability and assembly; use of estramustine phosphate in the study of microtubules
    • Friden, B., and Wallin, M. (1991). Dependency of microtubule-associated proteins (MAPs) for tubulin stability and assembly; use of estramustine phosphate in the study of microtubules. Mol. Cell. Biochem. 105, 149-158.
    • (1991) Mol. Cell. Biochem. , vol.105 , pp. 149-158
    • Friden, B.1    Wallin, M.2
  • 8
    • 33846025142 scopus 로고    scopus 로고
    • Chlorpyrifos, chlorpyrifos-oxon, and diisopropylfluorophosphate inhibit kinesin-dependent microtubule motility
    • Gearhart, D. A., Sickles, D. W., Buccafusco, J. J., Prendergast, M. A., and Terry, A. V., Jr. (2007). Chlorpyrifos, chlorpyrifos-oxon, and diisopropylfluorophosphate inhibit kinesin-dependent microtubule motility. Toxicol. Appl. Pharmacol. 218, 20-29.
    • (2007) Toxicol. Appl. Pharmacol. , vol.218 , pp. 20-29
    • Gearhart, D.A.1    Sickles, D.W.2    Buccafusco, J.J.3    Prendergast, M.A.4    Terry Jr., A.V.5
  • 9
    • 67349155891 scopus 로고    scopus 로고
    • Covalent binding of the organophosphorus agent FP-biotin to tyrosine in eight proteins that have no active site serine
    • PMCID:2700782
    • Grigoryan, H., Li, B., Anderson, E. K., Xue, W., Nachon, F., Lockridge, O., and Schopfer, L. M. (2009a). Covalent binding of the organophosphorus agent FP-biotin to tyrosine in eight proteins that have no active site serine. Chem. Biol. Interact. 180, 492-498. PMCID:2700782.
    • (2009) Chem. Biol. Interact. , vol.180 , pp. 492-498
    • Grigoryan, H.1    Li, B.2    Anderson, E.K.3    Xue, W.4    Nachon, F.5    Lockridge, O.6    Schopfer, L.M.7
  • 10
  • 11
    • 70349247706 scopus 로고    scopus 로고
    • Nanoimages show disruption of tubulin polymerization by chlorpyrifos oxon: implications for neurotoxicity
    • NIHMS:134468
    • Grigoryan, H., and Lockridge, O. (2009). Nanoimages show disruption of tubulin polymerization by chlorpyrifos oxon: implications for neurotoxicity. Toxicol. Appl. Pharmacol. 240, 143-148. NIHMS:134468.
    • (2009) Toxicol. Appl. Pharmacol. , vol.240 , pp. 143-148
    • Grigoryan, H.1    Lockridge, O.2
  • 13
    • 50649103273 scopus 로고    scopus 로고
    • Mass spectrometry identifies covalent binding of soman, sarin, chlorpyrifos oxon, diisopropyl fluorophosphate, and FP-biotin to tyrosines on tubulin: a potential mechanism of long term toxicity by organophosphorus agents
    • Grigoryan, H., Schopfer, L. M., Thompson, C. M., Terry, A. V., Masson, P., and Lockridge, O. (2008). Mass spectrometry identifies covalent binding of soman, sarin, chlorpyrifos oxon, diisopropyl fluorophosphate, and FP-biotin to tyrosines on tubulin: a potential mechanism of long term toxicity by organophosphorus agents. Chem. Biol. Interact. 175, 180-186.
    • (2008) Chem. Biol. Interact. , vol.175 , pp. 180-186
    • Grigoryan, H.1    Schopfer, L.M.2    Thompson, C.M.3    Terry, A.V.4    Masson, P.5    Lockridge, O.6
  • 14
    • 0030841699 scopus 로고    scopus 로고
    • Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen
    • Gupta, R. P., Abdel-Rahman, A., Wilmarth, K. W., and Abou-Donia, M. B. (1997). Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen. Biochem. Pharmacol. 53, 1799-1806.
    • (1997) Biochem. Pharmacol. , vol.53 , pp. 1799-1806
    • Gupta, R.P.1    Abdel-Rahman, A.2    Wilmarth, K.W.3    Abou-Donia, M.B.4
  • 15
    • 0028017677 scopus 로고
    • In vivo and in vitro effects of diisopropyl phosphorofluoridate (DFP) on the rate of hen brain tubulin polymerization
    • Gupta, R. P., and Abou-Donia, M. B. (1994). In vivo and in vitro effects of diisopropyl phosphorofluoridate (DFP) on the rate of hen brain tubulin polymerization. Neurochem. Res. 19, 435-444.
    • (1994) Neurochem. Res. , vol.19 , pp. 435-444
    • Gupta, R.P.1    Abou-Donia, M.B.2
  • 16
    • 0033562166 scopus 로고    scopus 로고
    • Tau phosphorylation by diisopropyl phosphorofluoridate (DFP)-treated hen brain supernatant inhibits its binding with microtubules: role of Ca2+/Calmodulin-dependent protein kinase II in tau phosphorylation
    • Gupta, R. P., and Abou-Donia, M. B. (1999). Tau phosphorylation by diisopropyl phosphorofluoridate (DFP)-treated hen brain supernatant inhibits its binding with microtubules: role of Ca2+/Calmodulin-dependent protein kinase II in tau phosphorylation. Arch. Biochem. Biophys. 365, 268-278.
    • (1999) Arch. Biochem. Biophys. , vol.365 , pp. 268-278
    • Gupta, R.P.1    Abou-Donia, M.B.2
  • 17
    • 70349233759 scopus 로고    scopus 로고
    • Proteomic analysis of differentiating neuroblastoma cells treated with sub-lethal neurite inhibitory concentrations of diazinon: identification of novel biomarkers of effect
    • Harris, W., Sachana, M., Flaskos, J., and Hargreaves, A. J. (2009). Proteomic analysis of differentiating neuroblastoma cells treated with sub-lethal neurite inhibitory concentrations of diazinon: identification of novel biomarkers of effect. Toxicol. Appl. Pharmacol. 240, 159-165.
    • (2009) Toxicol. Appl. Pharmacol. , vol.240 , pp. 159-165
    • Harris, W.1    Sachana, M.2    Flaskos, J.3    Hargreaves, A.J.4
  • 18
    • 0041519060 scopus 로고    scopus 로고
    • Centrosomal microtubule plus end tracking proteins and their role in Dictyostelium cell dynamics
    • Hestermann, A., Rehberg, M., and Graf, R. (2002). Centrosomal microtubule plus end tracking proteins and their role in Dictyostelium cell dynamics. J. Muscle Res. Cell. Motil. 23, 621-630.
    • (2002) J. Muscle Res. Cell. Motil. , vol.23 , pp. 621-630
    • Hestermann, A.1    Rehberg, M.2    Graf, R.3
  • 20
    • 0036898465 scopus 로고    scopus 로고
    • Myosin-V, a versatile motor for short-range vesicle transport
    • Langford, G. M. (2002). Myosin-V, a versatile motor for short-range vesicle transport. Traffic 3, 859-865.
    • (2002) Traffic , vol.3 , pp. 859-865
    • Langford, G.M.1
  • 21
    • 0348011603 scopus 로고    scopus 로고
    • Functions of intermediate filaments in neuronal development and disease
    • Lariviere, R. C., and Julien, J. P. (2004). Functions of intermediate filaments in neuronal development and disease. J. Neurobiol. 58, 131-148.
    • (2004) J. Neurobiol. , vol.58 , pp. 131-148
    • Lariviere, R.C.1    Julien, J.P.2
  • 22
    • 58049194183 scopus 로고    scopus 로고
    • Tyrosines of human and mouse transferrin covalently labeled by organophosphorus agents: a new motif for binding to proteins that have no active site serine
    • PMCID:2638647
    • Li, B., Schopfer, L. M., Grigoryan, H., Thompson, C. M., Hinrichs, S. H., Masson, P., and Lockridge, O. (2009). Tyrosines of human and mouse transferrin covalently labeled by organophosphorus agents: a new motif for binding to proteins that have no active site serine. Toxicol. Sci. 107, 144-155. PMCID:2638647.
    • (2009) Toxicol. Sci. , vol.107 , pp. 144-155
    • Li, B.1    Schopfer, L.M.2    Grigoryan, H.3    Thompson, C.M.4    Hinrichs, S.H.5    Masson, P.6    Lockridge, O.7
  • 23
    • 0030802287 scopus 로고    scopus 로고
    • Molecular chaperones and the cytoskeleton
    • Liang, P., and MacRae, T. H. (1997). Molecular chaperones and the cytoskeleton. J. Cell. Sci. 110(Pt 13), 1431-1440.
    • (1997) J. Cell. Sci. , vol.110 , Issue.PART 13 , pp. 1431-1440
    • Liang, P.1    MacRae, T.H.2
  • 24
    • 59749090938 scopus 로고    scopus 로고
    • AFM for analysis of structure and dynamics of DNA and protein-DNA complexes
    • Lyubchenko, Y. L., and Shlyakhtenko, L. S. (2009). AFM for analysis of structure and dynamics of DNA and protein-DNA complexes. Methods 47, 206-213.
    • (2009) Methods , vol.47 , pp. 206-213
    • Lyubchenko, Y.L.1    Shlyakhtenko, L.S.2
  • 25
    • 0028845388 scopus 로고
    • Role of microtubule-associated proteins in the control of microtubule assembly
    • Maccioni, R. B., and Cambiazo, V. (1995). Role of microtubule-associated proteins in the control of microtubule assembly. Physiol. Rev. 75, 835-864.
    • (1995) Physiol. Rev. , vol.75 , pp. 835-864
    • Maccioni, R.B.1    Cambiazo, V.2
  • 26
    • 0030726679 scopus 로고    scopus 로고
    • Neuropharmacological mechanisms of nerve agent-induced seizure and neuropathology
    • McDonough, J. H., Jr, and Shih, T. M. (1997). Neuropharmacological mechanisms of nerve agent-induced seizure and neuropathology. Neurosci. Biobehav. Rev. 21, 559-579.
    • (1997) Neurosci. Biobehav. Rev. , vol.21 , pp. 559-579
    • McDonough Jr., J.H.1    Shih, T.M.2
  • 28
    • 51249117818 scopus 로고    scopus 로고
    • Tau-isoform dependent enhancement of taxol mobility through microtubules
    • Park, H., Kim, M., and Fygenson, D. K. (2008). Tau-isoform dependent enhancement of taxol mobility through microtubules. Arch. Biochem. Biophys. 478, 119-126.
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 119-126
    • Park, H.1    Kim, M.2    Fygenson, D.K.3
  • 30
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999). Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 32
    • 76749097989 scopus 로고    scopus 로고
    • Biomarkers of organophosphorus nerve agent exposure: comparison of phosphylated butyrylcholinesterase and phosphylated albumin after oxime therapy
    • Read, R. W., Riches, J. R., Stevens, J. A., Stubbs, S. J., and Black, R. M. (2010). Biomarkers of organophosphorus nerve agent exposure: comparison of phosphylated butyrylcholinesterase and phosphylated albumin after oxime therapy. Arch. Toxicol. 84, 25-36.
    • (2010) Arch. Toxicol. , vol.84 , pp. 25-36
    • Read, R.W.1    Riches, J.R.2    Stevens, J.A.3    Stubbs, S.J.4    Black, R.M.5
  • 34
    • 44749094910 scopus 로고    scopus 로고
    • Inhibition of extension outgrowth in differentiating rat C6 glioma cells by chlorpyrifos and chlorpyrifos oxon: effects on microtubule proteins
    • Sachana, M., Flaskos, J., Sidiropoulou, E., Yavari, C. A., and Hargreaves, A. J. (2008). Inhibition of extension outgrowth in differentiating rat C6 glioma cells by chlorpyrifos and chlorpyrifos oxon: effects on microtubule proteins. Toxicol. In Vitro 22, 1387-1391.
    • (2008) Toxicol. In Vitro , vol.22 , pp. 1387-1391
    • Sachana, M.1    Flaskos, J.2    Sidiropoulou, E.3    Yavari, C.A.4    Hargreaves, A.J.5
  • 36
    • 0348046513 scopus 로고    scopus 로고
    • Neuropsychiatric evaluation in subjects chronically exposed to organophosphate pesticides
    • Salvi, R. M., Lara, D. R., Ghisolfi, E. S., Portela, L. V., Dias, R. D., and Souza, D. O. (2003). Neuropsychiatric evaluation in subjects chronically exposed to organophosphate pesticides. Toxicol. Sci. 72, 267-271.
    • (2003) Toxicol. Sci. , vol.72 , pp. 267-271
    • Salvi, R.M.1    Lara, D.R.2    Ghisolfi, E.S.3    Portela, L.V.4    Dias, R.D.5    Souza, D.O.6
  • 37
    • 10644293868 scopus 로고    scopus 로고
    • Biotransformation of chlorpyrifos and diazinon by human liver microsomes and recombinant human cytochrome P450s (CYP)
    • Sams, C., Cocker, J., and Lennard, M. S. (2004). Biotransformation of chlorpyrifos and diazinon by human liver microsomes and recombinant human cytochrome P450s (CYP). Xenobiotica 34, 861-873.
    • (2004) Xenobiotica , vol.34 , pp. 861-873
    • Sams, C.1    Cocker, J.2    Lennard, M.S.3
  • 38
    • 0036353211 scopus 로고    scopus 로고
    • Noncholinesterase mechanisms of chlorpyrifos neurotoxicity: altered phosphorylation of Ca2+/cAMP response element binding protein in cultured neurons
    • Schuh, R. A., Lein, P. J., Beckles, R. A., and Jett, D. A. (2002). Noncholinesterase mechanisms of chlorpyrifos neurotoxicity: altered phosphorylation of Ca2+/cAMP response element binding protein in cultured neurons. Toxicol. Appl. Pharmacol. 182, 176-185.
    • (2002) Toxicol. Appl. Pharmacol. , vol.182 , pp. 176-185
    • Schuh, R.A.1    Lein, P.J.2    Beckles, R.A.3    Jett, D.A.4
  • 40
    • 0037841390 scopus 로고    scopus 로고
    • Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials
    • Shlyakhtenko, L. S., Gall, A. A., Filonov, A., Cerovac, Z., Lushnikov, A., and Lyubchenko, Y. L. (2003). Silatrane-based surface chemistry for immobilization of DNA, protein-DNA complexes and other biological materials. Ultramicroscopy 97, 279-287.
    • (2003) Ultramicroscopy , vol.97 , pp. 279-287
    • Shlyakhtenko, L.S.1    Gall, A.A.2    Filonov, A.3    Cerovac, Z.4    Lushnikov, A.5    Lyubchenko, Y.L.6
  • 41
    • 0031194056 scopus 로고    scopus 로고
    • Cellular mechanisms for developmental toxicity of chlorpyrifos: targeting the adenylyl cyclase signaling cascade
    • Song, X., Seidler, F. J., Saleh, J. L., Zhang, J., Padilla, S., and Slotkin, T. A. (1997). Cellular mechanisms for developmental toxicity of chlorpyrifos: targeting the adenylyl cyclase signaling cascade. Toxicol. Appl. Pharmacol. 145, 158-174.
    • (1997) Toxicol. Appl. Pharmacol. , vol.145 , pp. 158-174
    • Song, X.1    Seidler, F.J.2    Saleh, J.L.3    Zhang, J.4    Padilla, S.5    Slotkin, T.A.6
  • 43
    • 0034433637 scopus 로고    scopus 로고
    • Cytoplasmic dynein subunit heterogeneity: implications for axonal transport
    • Susalka, S. J., and Pfister, K. K. (2000). Cytoplasmic dynein subunit heterogeneity: implications for axonal transport. J. Neurocytol. 29, 819-829.
    • (2000) J. Neurocytol. , vol.29 , pp. 819-829
    • Susalka, S.J.1    Pfister, K.K.2
  • 44
    • 0034861252 scopus 로고    scopus 로고
    • Metabolism of chlorpyrifos by human cytochrome P450 isoforms and human, mouse, and rat liver microsomes
    • Tang, J., Cao, Y., Rose, R. L., Brimfield, A. A., Dai, D., Goldstein, J. A., and Hodgson, E. (2001). Metabolism of chlorpyrifos by human cytochrome P450 isoforms and human, mouse, and rat liver microsomes. Drug Metab. Dispos. 29, 1201-1204.
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1201-1204
    • Tang, J.1    Cao, Y.2    Rose, R.L.3    Brimfield, A.A.4    Dai, D.5    Goldstein, J.A.6    Hodgson, E.7
  • 47
    • 0024205197 scopus 로고
    • The sequential appearance of low- and high-molecular-weight forms of MAP2 in the developing cerebellum
    • Tucker, R. P., Binder, L. I., Viereck, C., Hemmings, B. A., and Matus, A. I. (1988). The sequential appearance of low- and high-molecular-weight forms of MAP2 in the developing cerebellum. J. Neurosci. 8, 4503-4512.
    • (1988) J. Neurosci. , vol.8 , pp. 4503-4512
    • Tucker, R.P.1    Binder, L.I.2    Viereck, C.3    Hemmings, B.A.4    Matus, A.I.5
  • 48
    • 0022827893 scopus 로고
    • Phosphorylation of tubulin by a calmodulin-dependent protein kinase
    • Wandosell, F., Serrano, L., Hernandez, M. A., and Avila, J. (1986). Phosphorylation of tubulin by a calmodulin-dependent protein kinase. J. Biol. Chem. 261, 10332-10339.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10332-10339
    • Wandosell, F.1    Serrano, L.2    Hernandez, M.A.3    Avila, J.4
  • 49
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann, S., and Weber, K. (2003). Post-translational modifications regulate microtubule function. Nat. Rev. Mol. Cell Biol. 4, 938-947.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 50
    • 64749112492 scopus 로고    scopus 로고
    • Biomarkers of HIV-1 associated dementia: proteomic investigation of sera
    • Wiederin, J., Rozek, W., Duan, F., and Ciborowski, P. (2009). Biomarkers of HIV-1 associated dementia: proteomic investigation of sera. Proteome Sci. 7, 8.
    • (2009) Proteome Sci , vol.7 , pp. 8
    • Wiederin, J.1    Rozek, W.2    Duan, F.3    Ciborowski, P.4
  • 52
    • 33750511285 scopus 로고    scopus 로고
    • Sarin experiences in Japan: acute toxicity and long-term effects
    • Yanagisawa, N., Morita, H., and Nakajima, T. (2006). Sarin experiences in Japan: acute toxicity and long-term effects. J. Neurol. Sci. 249, 76-85.
    • (2006) J. Neurol. Sci. , vol.249 , pp. 76-85
    • Yanagisawa, N.1    Morita, H.2    Nakajima, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.