메뉴 건너뛰기




Volumn 111, Issue 6, 2009, Pages 584-592

Enzymatic reduction of polyunsaturated lysophosphati-dylcholine hydroperoxides by glutathione peroxidase-1

Author keywords

Arachidonoyl lysoPC; Docosahexaenoyl lysoPC; Glutathione peroxidase; Hydroperoxides; Lipoxygenase; RBL

Indexed keywords

GLYCINE MAX;

EID: 69849105735     PISSN: 14387697     EISSN: 14389312     Source Type: Journal    
DOI: 10.1002/ejlt.200900023     Document Type: Article
Times cited : (10)

References (47)
  • 1
    • 0023242350 scopus 로고
    • The role of selenium peroxidases in the protection against oxidative damage
    • F. Ursini, A. Bindoli: The role of selenium peroxidases in the protection against oxidative damage. Chem Phys Lipids. 1987, 44, 255-276.
    • (1987) Chem Phys Lipids , vol.44 , pp. 255-276
    • Ursini, F.1    Bindoli, A.2
  • 2
    • 70449174079 scopus 로고
    • Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • G. C. Mills: Hemoglobin catabolism. I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J Biol Chem. 1957, 229, 189-197.
    • (1957) J Biol Chem , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 3
    • 0032523001 scopus 로고    scopus 로고
    • Inhibition of erythrocyte selenium-glutathione peroxidase by auranofin analogues and metabolites
    • J. R. Roberts, C. F. Shaw 3rd: Inhibition of erythrocyte selenium-glutathione peroxidase by auranofin analogues and metabolites. Biochem Pharmacol. 1998, 55, 1291-1299.
    • (1998) Biochem Pharmacol , vol.55 , pp. 1291-1299
    • Roberts, J.R.1    Shaw C.F 3rd2
  • 4
    • 22144442380 scopus 로고    scopus 로고
    • Structure, gene expression, and evolution of primate glutathione peroxidases
    • R. Fukuhara, T. Kageyama: Structure, gene expression, and evolution of primate glutathione peroxidases. Comp Biochem Physiol B Biochem Mol Biol. 2005, 141, 428-436.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.141 , pp. 428-436
    • Fukuhara, R.1    Kageyama, T.2
  • 5
    • 31344432053 scopus 로고    scopus 로고
    • Phospholipase A2, reactive oxygen species, and lipid peroxidation in cerebral ischemia
    • R. Muralikrishna Adibhatla, J. F. Hatcher: Phospholipase A2, reactive oxygen species, and lipid peroxidation in cerebral ischemia. Free Radic Biol Med. 2006, 40, 376-387.
    • (2006) Free Radic Biol Med , vol.40 , pp. 376-387
    • Muralikrishna Adibhatla, R.1    Hatcher, J.F.2
  • 6
    • 0020520287 scopus 로고
    • Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids
    • A. Grossman, A. Wendel: Non-reactivity of the selenoenzyme glutathione peroxidase with enzymatically hydroperoxidized phospholipids. Eur J Biochem. 1983, 135, 549-552.
    • (1983) Eur J Biochem , vol.135 , pp. 549-552
    • Grossman, A.1    Wendel, A.2
  • 7
    • 0028991435 scopus 로고
    • PHGPx and phospholipase A2/GPx: Comparative importance on the reduction of hydroperoxides in rat liver mitochondria
    • F. Antunes, A. Salvador, R. E. Pinto: PHGPx and phospholipase A2/GPx: Comparative importance on the reduction of hydroperoxides in rat liver mitochondria. Free Radic Biol Med. 1995, 19, 669-677.
    • (1995) Free Radic Biol Med , vol.19 , pp. 669-677
    • Antunes, F.1    Salvador, A.2    Pinto, R.E.3
  • 8
    • 0031018005 scopus 로고    scopus 로고
    • Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides
    • H. S. Marinho, F. Antunes, R. E. Pinto: Role of glutathione peroxidase and phospholipid hydroperoxide glutathione peroxidase in the reduction of lysophospholipid hydroperoxides. Free Radic Biol Med. 1997, 22, 871-883.
    • (1997) Free Radic Biol Med , vol.22 , pp. 871-883
    • Marinho, H.S.1    Antunes, F.2    Pinto, R.E.3
  • 10
    • 37549004312 scopus 로고    scopus 로고
    • Role of lysophosphatidylcholine (LPC) in atherosclerosis
    • T. Matsumoto, T. Kobayashi, K. Kamata: Role of lysophosphatidylcholine (LPC) in atherosclerosis. Curr Med Chem. 2007, 14, 3209-3220.
    • (2007) Curr Med Chem , vol.14 , pp. 3209-3220
    • Matsumoto, T.1    Kobayashi, T.2    Kamata, K.3
  • 11
    • 27744439641 scopus 로고    scopus 로고
    • High performance liquid chromatography-tandem mass spectrometry of phospholipid molecular species in eggs from hens fed diets enriched in seal blubber oil
    • D. Pacetti, E. Boselli, H. W. Hulan, N. G. Frega: High performance liquid chromatography-tandem mass spectrometry of phospholipid molecular species in eggs from hens fed diets enriched in seal blubber oil. J Chromatogr A. 2005, 1097, 66-73.
    • (2005) J Chromatogr A , vol.1097 , pp. 73
    • Pacetti, D.1    Boselli, E.2    Hulan, H.W.3    Frega, N.G.4
  • 13
    • 0033983832 scopus 로고    scopus 로고
    • Characterization of plasma unsaturated lysophosphatidylcholines in human and rat
    • M. Croset, N. Brossard, A. Polette, M. Lagarde: Characterization of plasma unsaturated lysophosphatidylcholines in human and rat. Biochem J. 2000, 345, 61-67.
    • (2000) Biochem J , vol.345 , pp. 61-67
    • Croset, M.1    Brossard, N.2    Polette, A.3    Lagarde, M.4
  • 14
    • 36749100667 scopus 로고    scopus 로고
    • Mass spectrometric identification of molecular species of phosphatidylcholine and lysophosphatidylcholine extracted from shark liver
    • S. Chen, K. W. Li: Mass spectrometric identification of molecular species of phosphatidylcholine and lysophosphatidylcholine extracted from shark liver. J Agric Food Chem. 2007, 55, 9670-9677.
    • (2007) J Agric Food Chem , vol.55 , pp. 9670-9677
    • Chen, S.1    Li, K.W.2
  • 15
    • 33750929923 scopus 로고    scopus 로고
    • Analysis of phosphatidylcholine oxidation products in human plasma using quadrupole time-of-flight mass spectrometry
    • J. Adachi, M. Asano, N. Yoshioka, H. Nushida, Y. Ueno: Analysis of phosphatidylcholine oxidation products in human plasma using quadrupole time-of-flight mass spectrometry. Kobe J Med Sci. 2006, 52, 127-140.
    • (2006) Kobe J Med Sci , vol.52 , pp. 127-140
    • Adachi, J.1    Asano, M.2    Yoshioka, N.3    Nushida, H.4    Ueno, Y.5
  • 16
    • 10944233553 scopus 로고    scopus 로고
    • LC-MS analysis of phospholipids and lysophospholipids in human bronchoalveolar lavage fluid
    • B. Barroso, R. Bischoff: LC-MS analysis of phospholipids and lysophospholipids in human bronchoalveolar lavage fluid. J Chromatogr B Anal Technol Biomed Life Sci. 2005, 814, 21-28.
    • (2005) J Chromatogr B Anal Technol Biomed Life Sci , vol.814 , pp. 21-28
    • Barroso, B.1    Bischoff, R.2
  • 17
    • 0028235406 scopus 로고
    • The multiple hydroperoxides of choline phospholipids in plasma after ischemiareperfusion in rat liver
    • F. Takayama, T. Egashira, Y. Yamanaka: The multiple hydroperoxides of choline phospholipids in plasma after ischemiareperfusion in rat liver. J Toxicol Sci. 1994, 19, 97-106.
    • (1994) J Toxicol Sci , vol.19 , pp. 97-106
    • Takayama, F.1    Egashira, T.2    Yamanaka, Y.3
  • 18
    • 0242299620 scopus 로고    scopus 로고
    • LC-MS/MS analysis of lysophospholipids associated with soy protein isolate
    • N. Fang, S. Yu, T. M. Badger: LC-MS/MS analysis of lysophospholipids associated with soy protein isolate. J Agric Food Chem. 2003, 51, 6676-6682.
    • (2003) J Agric Food Chem , vol.51 , pp. 6676-6682
    • Fang, N.1    Yu, S.2    Badger, T.M.3
  • 19
    • 34247632110 scopus 로고    scopus 로고
    • Linoleoyl lysophosphatidic acid and linoleoyl lysophosphatidylcholine are efficient substrates for mammalian lipoxygenases
    • L. S. Huang, M. R. Kim, T. S. Jeong, D. E. Sok: Linoleoyl lysophosphatidic acid and linoleoyl lysophosphatidylcholine are efficient substrates for mammalian lipoxygenases. Biochim Biophys Acta. 2007, 1770, 1062-1070.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 1062-1070
    • Huang, L.S.1    Kim, M.R.2    Jeong, T.S.3    Sok, D.E.4
  • 20
    • 36248976167 scopus 로고    scopus 로고
    • Oxygenation of 1-docosahexaenoyl lysophosphatidylcholine by lipoxygenases; conjugated hydroperoxydiene and dihydroxytriene derivatives
    • L. S. Huang, M. R. Kim, D. E. Sok: Oxygenation of 1-docosahexaenoyl lysophosphatidylcholine by lipoxygenases; conjugated hydroperoxydiene and dihydroxytriene derivatives. Lipids. 2007, 42, 981-990.
    • (2007) Lipids , vol.42 , pp. 981-990
    • Huang, L.S.1    Kim, M.R.2    Sok, D.E.3
  • 21
    • 40549112976 scopus 로고    scopus 로고
    • Oxygenation of arachidonoyl lysophospholipids by lipoxygenases from soybean, porcine leukocyte, or rabbit reticulocyte
    • L. S. Huang, J. S. Kang, M. R. Kim, D. E. Sok: Oxygenation of arachidonoyl lysophospholipids by lipoxygenases from soybean, porcine leukocyte, or rabbit reticulocyte. J Agric Food Chem. 2008, 56, 1224-1232.
    • (2008) J Agric Food Chem , vol.56 , pp. 1224-1232
    • Huang, L.S.1    Kang, J.S.2    Kim, M.R.3    Sok, D.E.4
  • 22
    • 33750692730 scopus 로고    scopus 로고
    • Linoleoyl lysophosphatidylcholine is an efficient substrate for soybean lipoxygenase-1
    • L. S. Huang, M. R. Kim, D. E. Sok: Linoleoyl lysophosphatidylcholine is an efficient substrate for soybean lipoxygenase-1. Arch Biochem Biophys. 2006, 455, 119-126.
    • (2006) Arch Biochem Biophys , vol.455 , pp. 119-126
    • Huang, L.S.1    Kim, M.R.2    Sok, D.E.3
  • 23
    • 35548986631 scopus 로고    scopus 로고
    • Inhibition of lysophospholipase D activity by unsaturated lysophosphatidic acids or seed extracts containing 1-linoleoyl and 1-oleoyl lysophosphatidic acid
    • X. W. Liu, D. E. Sok, H. S. Yook, C. B. Sohn, Y. J. Chung, M. R. Kim: Inhibition of lysophospholipase D activity by unsaturated lysophosphatidic acids or seed extracts containing 1linoleoyl and 1-oleoyl lysophosphatidic acid. J Agric Food Chem. 2007, 55, 8717-8722.
    • (2007) J Agric Food Chem , vol.55 , pp. 8717-8722
    • Liu, X.W.1    Sok, D.E.2    Yook, H.S.3    Sohn, C.B.4    Chung, Y.J.5    Kim, M.R.6
  • 24
    • 33748521513 scopus 로고    scopus 로고
    • Role of 5-lipoxygenase pathway in the regulation of RAW 264.7 macrophage proliferation
    • D. Nieves, J. J. Moreno: Role of 5-lipoxygenase pathway in the regulation of RAW 264.7 macrophage proliferation. Biochem Pharmacol. 2006, 72, 1022-1030.
    • (2006) Biochem Pharmacol. , vol.72 , pp. 1022-1030
    • Nieves, D.1    Moreno, J.J.2
  • 25
    • 0031941870 scopus 로고    scopus 로고
    • Anti-inflammatory effect of YPE-01, a novel diarylheptanoid derivative, on dermal inflammation in mice
    • R. Yamazaki, R. Aiyama, T. Matsuzaki, S. Hashimoto, T. Yokokura: Anti-inflammatory effect of YPE-01, a novel diarylheptanoid derivative, on dermal inflammation in mice. Inflamm Res. 1998, 47, 182-186.
    • (1998) Inflamm Res , vol.47 , pp. 182-186
    • Yamazaki, R.1    Aiyama, R.2    Matsuzaki, T.3    Hashimoto, S.4    Yokokura, T.5
  • 26
    • 0019740344 scopus 로고
    • Glutathione peroxidase
    • A. Wendel: Glutathione peroxidase. Methods Enzymol. 1981, 77, 393-397.
    • (1981) Methods Enzymol , vol.77 , pp. 393-397
    • Wendel, A.1
  • 27
    • 27744524363 scopus 로고    scopus 로고
    • Protection by petaslignolide A, a major neuroprotective compound in the butanol extract of Petasites japonicus leaves, against oxidative damage in the brains of mice challenged with kainic acid
    • H. S. Cui, M. R. Kim, D. E. Sok: Protection by petaslignolide A, a major neuroprotective compound in the butanol extract of Petasites japonicus leaves, against oxidative damage in the brains of mice challenged with kainic acid. J Agric Food Chem. 2005, 53, 8526-8532.
    • (2005) J Agric Food Chem , vol.53 , pp. 8526-8532
    • Cui, H.S.1    Kim, M.R.2    Sok, D.E.3
  • 28
    • 52649121837 scopus 로고    scopus 로고
    • Regulation of lipoxygenase activity by polyunsaturated lysophosphatidylcholines or their oxygenation derivatives
    • L. S. Huang, M. R. Kim, D. E. Sok: Regulation of lipoxygenase activity by polyunsaturated lysophosphatidylcholines or their oxygenation derivatives. J Agric Food Chem. 2008, 56, 7808-7814.
    • (2008) J Agric Food Chem , vol.56 , pp. 7808-7814
    • Huang, L.S.1    Kim, M.R.2    Sok, D.E.3
  • 29
    • 0029040174 scopus 로고
    • Characterization of specific subcellular 15-hydroxyeicosatetraenoic acid (15-HETE) binding sites on rat basophilic leukemia cells
    • L. T. Kang, J. Y. Vanderhoek: Characterization of specific subcellular 15-hydroxyeicosatetraenoic acid (15-HETE) binding sites on rat basophilic leukemia cells. Biochim Biophys Acta. 1995, 1256, 297-304.
    • (1995) Biochim Biophys Acta , vol.1256 , pp. 297-304
    • Kang, L.T.1    Vanderhoek, J.Y.2
  • 31
    • 0030585326 scopus 로고    scopus 로고
    • Overexpression of phospholipid hydroperoxide glutathione peroxidase suppressed cell death due to oxidative damage in rat basophile leukemia cells (RBL-2H3)
    • H. Imai, D. Sumi, H. Sakamoto, A. Hanamoto, M. Arai, N. Chiba, Y. Nakagawa: Overexpression of phospholipid hydroperoxide glutathione peroxidase suppressed cell death due to oxidative damage in rat basophile leukemia cells (RBL-2H3). Biochem Biophys Res Commun. 1996, 222, 432-438.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 432-438
    • Imai, H.1    Sumi, D.2    Sakamoto, H.3    Hanamoto, A.4    Arai, M.5    Chiba, N.6    Nakagawa, Y.7
  • 32
    • 0345337246 scopus 로고    scopus 로고
    • Oxidation of dilinoleoyl phosphatidylcholine by lipoxygenase 1 from soybeans
    • M. Pérez-Gilabert, G. A. Veldink, J. F. Vliegenthart: Oxidation of dilinoleoyl phosphatidylcholine by lipoxygenase 1 from soybeans. Arch Biochem Biophys. 1998, 354, 18-23.
    • (1998) Arch Biochem Biophys , vol.354 , pp. 18-23
    • Pérez-Gilabert, M.1    Veldink, G.A.2    Vliegenthart, J.F.3
  • 33
    • 3242699423 scopus 로고    scopus 로고
    • Mechanisms of lysophosphatidic acid production
    • J. Aoki: Mechanisms of lysophosphatidic acid production. Semin Cell Dev Biol. 2004, 15, 477-489.
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 477-489
    • Aoki, J.1
  • 34
    • 22544443973 scopus 로고    scopus 로고
    • Lipoprotein-associated phospholipase A2 as a target of therapy
    • C. H. Macphee, J. J. Nelson, A. Zalewski: Lipoprotein-associated phospholipase A2 as a target of therapy. Curr Opin Lipidol. 2005, 16, 442-446.
    • (2005) Curr Opin Lipidol , vol.16 , pp. 442-446
    • Macphee, C.H.1    Nelson, J.J.2    Zalewski, A.3
  • 35
    • 24744432338 scopus 로고    scopus 로고
    • Endothelial lipase releases saturated and unsaturated fatty acids of high density lipoprotein phosphatidylcholine
    • M. Gauster, G. Rechberger, A. Sovic, G. Hörl, E. Steyrer, W. Sattler, S. Frank: Endothelial lipase releases saturated and unsaturated fatty acids of high density lipoprotein phosphatidylcholine. J Lipid Res. 2005, 46, 1517-1525.
    • (2005) J Lipid Res , vol.46 , pp. 1517-1525
    • Gauster, M.1    Rechberger, G.2    Sovic, A.3    Hörl, G.4    Steyrer, E.5    Sattler, W.6    Frank, S.7
  • 37
    • 0026699797 scopus 로고
    • Unsaturated fatty acids esterified in 2-acyl-llysophosphatidylcholine bound to albumin are more efficiently taken up by the young rat brain than the unesterified form
    • F. Thies, M. C. Delachambre, M. Bentejac, M. Lagarde, J. Lecerf: Unsaturated fatty acids esterified in 2-acyl-llysophosphatidylcholine bound to albumin are more efficiently taken up by the young rat brain than the unesterified form. J Neurochem. 1992, 59, 1110-1116.
    • (1992) J Neurochem , vol.59 , pp. 1110-1116
    • Thies, F.1    Delachambre, M.C.2    Bentejac, M.3    Lagarde, M.4    Lecerf, J.5
  • 38
    • 47249160785 scopus 로고    scopus 로고
    • Glutathione peroxidase family an evolutionary overview
    • R. Margis, C. Dunand, F. K. Teixeira, M. Margis-Pinheiro: Glutathione peroxidase family an evolutionary overview. FEBS J. 2008, 275, 3959-3970.
    • (2008) FEBS J , vol.275 , pp. 3959-3970
    • Margis, R.1    Dunand, C.2    Teixeira, F.K.3    Margis-Pinheiro, M.4
  • 39
    • 0024350070 scopus 로고
    • Phospholipid hydroperoxide glutathione peroxidase: Specific activity in tissues of rats of different age and comparison with other glutathione peroxidases
    • L. Zhang, M. Maiorino, A. Rovelli, F. Ursini: Phospholipid hydroperoxide glutathione peroxidase: Specific activity in tissues of rats of different age and comparison with other glutathione peroxidases. Biochim Biophys Acta 1989, 1006, 140-143.
    • (1989) Biochim Biophys Acta , vol.1006 , pp. 140-143
    • Zhang, L.1    Maiorino, M.2    Rovelli, A.3    Ursini, F.4
  • 40
    • 0034659139 scopus 로고    scopus 로고
    • Bioactive products of phospholipid oxidation: Isolation, identification, measurement and activities
    • G. Subbanagounder, A. D. Watson, J. A. Berliner: Bioactive products of phospholipid oxidation: Isolation, identification, measurement and activities. Free Radic Biol Med. 2000, 28, 1751-1761.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1751-1761
    • Subbanagounder, G.1    Watson, A.D.2    Berliner, J.A.3
  • 41
    • 0026333959 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • J. L. Witztum, D. Steinberg: Role of oxidized low density lipoprotein in atherogenesis. J Clin Invest. 1991, 88, 1785-1792.
    • (1991) J Clin Invest , vol.88 , pp. 1785-1792
    • Witztum, J.L.1    Steinberg, D.2
  • 42
    • 39049113549 scopus 로고    scopus 로고
    • Role of oxidative stress in the development of vascular injury and its therapeutic intervention by nifedipine
    • S. Yamagishi, K. Nakamura, T. Matsui: Role of oxidative stress in the development of vascular injury and its therapeutic intervention by nifedipine. Curr Med Chem. 2008, 15, 172-177.
    • (2008) Curr Med Chem , vol.15 , pp. 172-177
    • Yamagishi, S.1    Nakamura, K.2    Matsui, T.3
  • 43
    • 33751185543 scopus 로고    scopus 로고
    • The role of cytosolic phospholipase A2-alfa in regulation of phagocytic functions
    • R. Levy: The role of cytosolic phospholipase A2-alfa in regulation of phagocytic functions. Biochim Biophys Acta. 2006, 1761, 1323-1334.
    • (2006) Biochim Biophys Acta , vol.1761 , pp. 1323-1334
    • Levy, R.1
  • 44
    • 60549092670 scopus 로고    scopus 로고
    • Lipoprotein-associated phospholipase A2 and high-sensitivity C-reactive protein improve the stratification of ischemic stroke risk in the Atherosclerosis Risk in Communities (ARIC) study
    • V. Nambi, R. C. Hoogeveen, L. Chambless, Y. Hu, H. Bang, J. Coresh, H. Ni, E. Boerwinkle, T. Mosley, R. Sharrett, A. R. Folsom, C. M. Ballantyne: Lipoprotein-associated phospholipase A2 and high-sensitivity C-reactive protein improve the stratification of ischemic stroke risk in the Atherosclerosis Risk in Communities (ARIC) study. Stroke 2009, 40, 376-381.
    • (2009) Stroke , vol.40 , pp. 376-381
    • Nambi, V.1    Hoogeveen, R.C.2    Chambless, L.3    Hu, Y.4    Bang, H.5    Coresh, J.6    Ni, H.7    Boerwinkle, E.8    Mosley, T.9    Sharrett, R.10    Folsom, A.R.11    Ballantyne, C.M.12
  • 45
    • 56149116581 scopus 로고    scopus 로고
    • Lipoprotein-associated phospholipase A2 activity and risk of recurrent stroke
    • M. S. Elkind, W. Tai, K. Coates, M. C. Paik, R. L. Sacco: Lipoprotein-associated phospholipase A2 activity and risk of recurrent stroke. Cerebrovasc Dis. 2009, 27, 42-50.
    • (2009) Cerebrovasc Dis , vol.27 , pp. 42-50
    • Elkind, M.S.1    Tai, W.2    Coates, K.3    Paik, M.C.4    Sacco, R.L.5
  • 46
    • 23444442916 scopus 로고    scopus 로고
    • Secretory phospholipase A2 enzymes in atherogenesis
    • N. R. Webb: Secretory phospholipase A2 enzymes in atherogenesis. Curr Opin Lipidol. 2005, 16, 341-344.
    • (2005) Curr Opin Lipidol , vol.16 , pp. 341-344
    • Webb, N.R.1
  • 47
    • 0142200309 scopus 로고    scopus 로고
    • Group V and X secretory phospholipase A(2)s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions
    • Y. Ishimoto, K. Yamada, S. Yamamoto, T. Ono, M. Notoya, K. Hanasaki: Group V and X secretory phospholipase A(2)s-induced modification of high-density lipoprotein linked to the reduction of its antiatherogenic functions. Biochim Biophys Acta. 2003, 1642, 129-138.
    • (2003) Biochim Biophys Acta , vol.1642 , pp. 129-138
    • Ishimoto, Y.1    Yamada, K.2    Yamamoto, S.3    Ono, T.4    Notoya, M.5    Hanasaki, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.