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Volumn 22, Issue 7, 2008, Pages 1726-1733

Protective effect of antioxidants against sarcoplasmic reticulum (SR) oxidation by Fenton reaction, however without prevention of Ca-pump activity

Author keywords

EGb 761; Fenton reaction; Pycnogenol; Sarcoplasmic reticulum; SERCA; Stobadine; Trolox

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ANTIOXIDANT; ASCORBIC ACID; CARBONYL DERIVATIVE; DINITROPHENYLHYDRAZINE; GINKGO BILOBA EXTRACT; HYDROGEN PEROXIDE; HYDROXYL RADICAL; IRON DERIVATIVE; LIPID; PHENYLHYDRAZINE DERIVATIVE; PYCNOGENOL; PYRIDOINDOLE STOBADINE; STOBADINE; TROLOX C; TRYPSIN; UNCLASSIFIED DRUG;

EID: 51749099571     PISSN: 08872333     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tiv.2008.07.010     Document Type: Article
Times cited : (14)

References (74)
  • 1
    • 0041825261 scopus 로고    scopus 로고
    • Pharmacological studies supporting the therapeutic use of Ginkgo biloba extract for Alzheimer's disease
    • Ahlemeyer B., and Krieglstein J. Pharmacological studies supporting the therapeutic use of Ginkgo biloba extract for Alzheimer's disease. Review. Pharmacopsychiatry 36 (2003) 8-14
    • (2003) Review. Pharmacopsychiatry , vol.36 , pp. 8-14
    • Ahlemeyer, B.1    Krieglstein, J.2
  • 4
    • 12844257477 scopus 로고    scopus 로고
    • Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins
    • Bigelow D.J., and Squier T.C. Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochimical Biophysical Acta 1703 (2005) 121-134
    • (2005) Biochimical Biophysical Acta , vol.1703 , pp. 121-134
    • Bigelow, D.J.1    Squier, T.C.2
  • 5
    • 0030910932 scopus 로고    scopus 로고
    • Buss, H., Chan, T.P., Sluis, K.B., Domigan, N.M., Winterbourn, C.C., 1997. Protein carbonyl measurement by a sensitive ELISA method. Free Radical Biology & Medicine 23, 361-366. Erratum in: 1998. Free Radical Biology & Medicine 24, 1352.
    • Buss, H., Chan, T.P., Sluis, K.B., Domigan, N.M., Winterbourn, C.C., 1997. Protein carbonyl measurement by a sensitive ELISA method. Free Radical Biology & Medicine 23, 361-366. Erratum in: 1998. Free Radical Biology & Medicine 24, 1352.
  • 7
    • 0033539641 scopus 로고    scopus 로고
    • The nucleotide-binding site of sarcoplasmic reticulum Ca-ATPase is conformationally altered in aged skeletal muscle
    • Chen B., Jones T.E., and Bigelow D.J. The nucleotide-binding site of sarcoplasmic reticulum Ca-ATPase is conformationally altered in aged skeletal muscle. Biochemistry 38 (1999) 14887-14896
    • (1999) Biochemistry , vol.38 , pp. 14887-14896
    • Chen, B.1    Jones, T.E.2    Bigelow, D.J.3
  • 11
    • 0023655531 scopus 로고
    • Protein damage and degradation by oxygen radicals: III: ion of secondary and tertiary structure
    • Davies K.J.A., and Delsignore M.E. Protein damage and degradation by oxygen radicals: III: ion of secondary and tertiary structure. The Journal of Biological Chemistry 262 (1987) 9908-9913
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 9908-9913
    • Davies, K.J.A.1    Delsignore, M.E.2
  • 13
    • 0022550514 scopus 로고
    • Preparation and definition of the extract of Ginkgo biloba
    • Drieu K. Preparation and definition of the extract of Ginkgo biloba. Presse Médicale 15 (1986) 1455-1457
    • (1986) Presse Médicale , vol.15 , pp. 1455-1457
    • Drieu, K.1
  • 14
    • 0021837375 scopus 로고
    • Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase
    • East J.M., Melville D., and Lee A.G. Exchange rates and numbers of annular lipids for the calcium and magnesium ion dependent adenosinetriphosphatase. Biochemistry 24 (1985) 2615-2623
    • (1985) Biochemistry , vol.24 , pp. 2615-2623
    • East, J.M.1    Melville, D.2    Lee, A.G.3
  • 16
    • 0034682741 scopus 로고    scopus 로고
    • The skeletal muscle calcium release channel: coupled O2 sensor and NO signaling functions
    • Eu J.P., Sun J., Xu L., Stamler J.S., and Meissner G. The skeletal muscle calcium release channel: coupled O2 sensor and NO signaling functions. Cell 102 (2000) 499-509
    • (2000) Cell , vol.102 , pp. 499-509
    • Eu, J.P.1    Sun, J.2    Xu, L.3    Stamler, J.S.4    Meissner, G.5
  • 17
    • 0031916191 scopus 로고    scopus 로고
    • Hypochlorous acid inhibits Ca(2+)-ATPase from skeletal muscle sarcoplasmic reticulum
    • Favero T.G., Colter D., Hooper P.F., and Abramson J.J. Hypochlorous acid inhibits Ca(2+)-ATPase from skeletal muscle sarcoplasmic reticulum. Journal of Applied Physiology 84 (1998) 425-430
    • (1998) Journal of Applied Physiology , vol.84 , pp. 425-430
    • Favero, T.G.1    Colter, D.2    Hooper, P.F.3    Abramson, J.J.4
  • 19
    • 0030886655 scopus 로고    scopus 로고
    • Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains
    • Goldshleger R., and Karlish S.J. Fe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domains. Proceedings of the National Academy of Sciences of the United States of America 94 (1997) 9596-9601
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , pp. 9596-9601
    • Goldshleger, R.1    Karlish, S.J.2
  • 20
    • 33747764829 scopus 로고    scopus 로고
    • Phagocyte-derived reactive species: salvation or suicide?
    • Halliwell B. Phagocyte-derived reactive species: salvation or suicide?. Trends in Biochemical Sciences 31 (2006) 509-515
    • (2006) Trends in Biochemical Sciences , vol.31 , pp. 509-515
    • Halliwell, B.1
  • 21
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • Halliwell B., and Gutteridge J.M.C. The importance of free radicals and catalytic metal ions in human diseases. Molecular Aspects of Medicine 8 (1985) 89-193
    • (1985) Molecular Aspects of Medicine , vol.8 , pp. 89-193
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 23
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: an overview
    • Halliwell B., and Gutteridge J.M.C. Role of free radicals and catalytic metal ions in human disease: an overview. Methods in Enzymology 186 (1990) 1-85
    • (1990) Methods in Enzymology , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 25
    • 0345676510 scopus 로고    scopus 로고
    • Antioxidant and pharmacodynamic effects of pyridoindole stobadine
    • Horakova L., and Stolc S. Antioxidant and pharmacodynamic effects of pyridoindole stobadine. General Pharmacology 30 (1998) 627-638
    • (1998) General Pharmacology , vol.30 , pp. 627-638
    • Horakova, L.1    Stolc, S.2
  • 26
    • 0028130552 scopus 로고
    • Antioxidant action of stobadine
    • Packer L. (Ed), Academic Press, San Diego
    • Horakova L., Sies H., and Steenken S. Antioxidant action of stobadine. In: Packer L. (Ed). Methods in Enzymology vol. 234(part D) (1994), Academic Press, San Diego 572-581
    • (1994) Methods in Enzymology , vol.234 PART D , pp. 572-581
    • Horakova, L.1    Sies, H.2    Steenken, S.3
  • 27
    • 0035865819 scopus 로고    scopus 로고
    • Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms
    • Ishige K., Schubert D., and Sagara Y. Flavonoids protect neuronal cells from oxidative stress by three distinct mechanisms. Free Radical Biology & Medicine 30 (2001) 433-446
    • (2001) Free Radical Biology & Medicine , vol.30 , pp. 433-446
    • Ishige, K.1    Schubert, D.2    Sagara, Y.3
  • 30
    • 0021099488 scopus 로고
    • Kinetic characterization of detergent-solubilized sarcoplasmic reticulum Adenosinetriphosphatase
    • Kosk-Kosicka D., Kurzmack M., and Inesi G. Kinetic characterization of detergent-solubilized sarcoplasmic reticulum Adenosinetriphosphatase. Biochemistry 22 (1983) 2559-2567
    • (1983) Biochemistry , vol.22 , pp. 2559-2567
    • Kosk-Kosicka, D.1    Kurzmack, M.2    Inesi, G.3
  • 31
    • 0031770290 scopus 로고    scopus 로고
    • The mechanism of detergent solubilization of liposomes and protein-containing membranes
    • Kragh-Hansen U., le Maire M., and Moller J.V. The mechanism of detergent solubilization of liposomes and protein-containing membranes. Biophysical Journal 75 (1998) 2932-2946
    • (1998) Biophysical Journal , vol.75 , pp. 2932-2946
    • Kragh-Hansen, U.1    le Maire, M.2    Moller, J.V.3
  • 33
    • 20444442574 scopus 로고    scopus 로고
    • Effect of the pyridoindole antioxidant stobadine on development of experimental diabetic cataract and on lens protein oxidation in rats: comparison with vitamin E and BHT
    • Kyselova Z., Gajdosik A., Gajdosikova A., Ulicna O., Mihalova D., Karasu C., and Stefek M. Effect of the pyridoindole antioxidant stobadine on development of experimental diabetic cataract and on lens protein oxidation in rats: comparison with vitamin E and BHT. Molecular Vision 11 (2005) 56-65
    • (2005) Molecular Vision , vol.11 , pp. 56-65
    • Kyselova, Z.1    Gajdosik, A.2    Gajdosikova, A.3    Ulicna, O.4    Mihalova, D.5    Karasu, C.6    Stefek, M.7
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 10644264370 scopus 로고    scopus 로고
    • Pharmacological modulation of sarcoplasmic reticulum function in smooth muscle
    • Laporte R., Hui A., and Laher I. Pharmacological modulation of sarcoplasmic reticulum function in smooth muscle. Pharmacological Reviews 56 (2004) 439-513
    • (2004) Pharmacological Reviews , vol.56 , pp. 439-513
    • Laporte, R.1    Hui, A.2    Laher, I.3
  • 36
    • 0024598763 scopus 로고
    • Molecular cloning and expression of cDNA encoding the 53, 000-dalton glycoprotein of rabbit skeletal muscle sarcoplasmic reticulum
    • Leberer E., Charuk J.H., Clarke D.M., Green N.M., Zubrzycka-Gaarn E., and MacLennan D.H. Molecular cloning and expression of cDNA encoding the 53, 000-dalton glycoprotein of rabbit skeletal muscle sarcoplasmic reticulum. Journal of Biological Chemistry 264 (1989) 3484-3493
    • (1989) Journal of Biological Chemistry , vol.264 , pp. 3484-3493
    • Leberer, E.1    Charuk, J.H.2    Clarke, D.M.3    Green, N.M.4    Zubrzycka-Gaarn, E.5    MacLennan, D.H.6
  • 37
    • 0031740283 scopus 로고    scopus 로고
    • How lipids interact with an intrinsic membrane protein: the case of the calcium pump
    • Lee A.G. How lipids interact with an intrinsic membrane protein: the case of the calcium pump. Biochimical Biophysical Acta 1376 (1998) 381-390
    • (1998) Biochimical Biophysical Acta , vol.1376 , pp. 381-390
    • Lee, A.G.1
  • 38
    • 0033212845 scopus 로고    scopus 로고
    • Membrane ion transport systems during oxidative stress in rodent brain: protective effect of stobadine and other antioxidants
    • Lehotsky J., Kaplan P., Racay P., Matejovicova M., Drgova A., and Mezesova V. Membrane ion transport systems during oxidative stress in rodent brain: protective effect of stobadine and other antioxidants. Life Sciences 65 (1999) 1951-1958
    • (1999) Life Sciences , vol.65 , pp. 1951-1958
    • Lehotsky, J.1    Kaplan, P.2    Racay, P.3    Matejovicova, M.4    Drgova, A.5    Mezesova, V.6
  • 43
    • 33751331864 scopus 로고    scopus 로고
    • Phenytoin administration in pregnancy-effect of antioxidants on biochemical variables in pre-and postnatal development of rats
    • Navarova J., Ujhazy E., Dubovicky M., and Mach M. Phenytoin administration in pregnancy-effect of antioxidants on biochemical variables in pre-and postnatal development of rats. Biologia 60 (2005) 51-55
    • (2005) Biologia , vol.60 , pp. 51-55
    • Navarova, J.1    Ujhazy, E.2    Dubovicky, M.3    Mach, M.4
  • 45
    • 0032839592 scopus 로고    scopus 로고
    • Antioxidant activity and biologic properties of a procyanidin-rich extract from pine (Pinus maritima) bark, pycnogenol
    • Packer L., Rimbach G., and Virgili F. Antioxidant activity and biologic properties of a procyanidin-rich extract from pine (Pinus maritima) bark, pycnogenol. Free Radical Biology & Medicine 27 (1999) 704-724
    • (1999) Free Radical Biology & Medicine , vol.27 , pp. 704-724
    • Packer, L.1    Rimbach, G.2    Virgili, F.3
  • 46
    • 0035146985 scopus 로고    scopus 로고
    • Molecular aspects of alpha-tocotrienol antioxidant action and cell signalling
    • Packer L., Weber S.U., and Rimbach G. Molecular aspects of alpha-tocotrienol antioxidant action and cell signalling. The Journal of Nutrition 131 (2001) 369-373
    • (2001) The Journal of Nutrition , vol.131 , pp. 369-373
    • Packer, L.1    Weber, S.U.2    Rimbach, G.3
  • 47
    • 0022374222 scopus 로고
    • The effect of mixed-function oxidation of enzymes on their susceptibility to degradation by a nonlysosomal cysteine proteinase
    • Rivett A.J. The effect of mixed-function oxidation of enzymes on their susceptibility to degradation by a nonlysosomal cysteine proteinase. Archives of Biochemistry and Biophysics 243 (1985) 624-632
    • (1985) Archives of Biochemistry and Biophysics , vol.243 , pp. 624-632
    • Rivett, A.J.1
  • 48
    • 0036219486 scopus 로고    scopus 로고
    • A review of the French maritime pine bark extract (Pycnogenol), a herbal medication with a diverse clinical pharmacology. Review
    • Rohdewald P. A review of the French maritime pine bark extract (Pycnogenol), a herbal medication with a diverse clinical pharmacology. Review. International Journal of Clinical Pharmacology and Therapeutics 40 (2002) 158-168
    • (2002) International Journal of Clinical Pharmacology and Therapeutics , vol.40 , pp. 158-168
    • Rohdewald, P.1
  • 52
    • 0022453245 scopus 로고
    • Oxidative stress impairs the function of sarcoplasmic reticulum by oxidation of sulfhydryl groups in the Ca-ATPase
    • Scherer N.M., and Deamer D.W. Oxidative stress impairs the function of sarcoplasmic reticulum by oxidation of sulfhydryl groups in the Ca-ATPase. Archives of Biochemistry and Biophysics 246 (1986) 589-601
    • (1986) Archives of Biochemistry and Biophysics , vol.246 , pp. 589-601
    • Scherer, N.M.1    Deamer, D.W.2
  • 53
    • 0002926180 scopus 로고
    • Oxidants, types, sources and mechanisms of injury
    • Crystal R.G., West J.B., Barnes P.J., Cherniak N.S., and Weibel E.R. (Eds), Raven, New York
    • Schraufstatter M.U., and Cochrane C.G. Oxidants, types, sources and mechanisms of injury. In: Crystal R.G., West J.B., Barnes P.J., Cherniak N.S., and Weibel E.R. (Eds). The Lung: Scientific Foundation (1991), Raven, New York 1803-1810
    • (1991) The Lung: Scientific Foundation , pp. 1803-1810
    • Schraufstatter, M.U.1    Cochrane, C.G.2
  • 54
    • 0034672517 scopus 로고    scopus 로고
    • Phenolic antioxidants attenuate neuronal cell death following uptake of oxidized low-density lipoprotein
    • Schroeter H., Williams R.J., Matin R., Iversen L., and Rice-Evans C.A. Phenolic antioxidants attenuate neuronal cell death following uptake of oxidized low-density lipoprotein. Free Radical Biology & Medicine 29 (2000) 1222-1233
    • (2000) Free Radical Biology & Medicine , vol.29 , pp. 1222-1233
    • Schroeter, H.1    Williams, R.J.2    Matin, R.3    Iversen, L.4    Rice-Evans, C.A.5
  • 55
    • 0030853496 scopus 로고    scopus 로고
    • 2+-ATPase from sarcoplasmic reticulum: solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine
    • 2+-ATPase from sarcoplasmic reticulum: solubilization and reconstitution by new short-chain phospholipid detergent 1,2-diheptanoyl-sn-phosphatidylcholine. Biochemical Journal 325 (1997) 533-542
    • (1997) Biochemical Journal , vol.325 , pp. 533-542
    • Shivanna, B.D.1    Rowe, E.S.2
  • 56
    • 2542467819 scopus 로고    scopus 로고
    • Studies on molecular mechanisms of Ginkgo biloba extract
    • Smith J.V., and Luo Y. Studies on molecular mechanisms of Ginkgo biloba extract. Applied Microbiology and Biotechnology 64 (2004) 465-472
    • (2004) Applied Microbiology and Biotechnology , vol.64 , pp. 465-472
    • Smith, J.V.1    Luo, Y.2
  • 57
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alterations in calcium homeostasis
    • Squier T.C., and Bigelow D.J. Protein oxidation and age-dependent alterations in calcium homeostasis. Frontiers in Bioscience 5 (2000) 504-526
    • (2000) Frontiers in Bioscience , vol.5 , pp. 504-526
    • Squier, T.C.1    Bigelow, D.J.2
  • 58
    • 0025674536 scopus 로고    scopus 로고
    • Stadtman, E.R., 1991. Metal ions catalyzed oxidation of proteins: biochemical mechanisms and biological consequences. Free Radical Biology & Medicine 9, 315-325. Erratum in: 1991 Free Radical Biology & Medicine 10, 249.
    • Stadtman, E.R., 1991. Metal ions catalyzed oxidation of proteins: biochemical mechanisms and biological consequences. Free Radical Biology & Medicine 9, 315-325. Erratum in: 1991 Free Radical Biology & Medicine 10, 249.
  • 59
    • 0029847580 scopus 로고    scopus 로고
    • Stimulation of the Ca(2+)-ATPase of sarcoplasmic reticulum by disulfiram
    • Starling A.P., East J.M., and Lee A.G. Stimulation of the Ca(2+)-ATPase of sarcoplasmic reticulum by disulfiram. Biochemical Journal 320 (1996) 101-105
    • (1996) Biochemical Journal , vol.320 , pp. 101-105
    • Starling, A.P.1    East, J.M.2    Lee, A.G.3
  • 60
    • 20444441235 scopus 로고    scopus 로고
    • Oxidative modification of rat eye lens proteins by peroxyl radicals in vitro: protection by the chain-breaking antioxidants stobadine and Trolox
    • Stefek M., Kyselova Z., Racková L., and Krizanova L. Oxidative modification of rat eye lens proteins by peroxyl radicals in vitro: protection by the chain-breaking antioxidants stobadine and Trolox. Biochimica et Biophysica Acta 1741 (2005) 183-190
    • (2005) Biochimica et Biophysica Acta , vol.1741 , pp. 183-190
    • Stefek, M.1    Kyselova, Z.2    Racková, L.3    Krizanova, L.4
  • 61
    • 51749107304 scopus 로고    scopus 로고
    • Stolc, S., Bauer, V., Benes, L., Tichy, M., 1983. Patents: CS 229 067, SWED 8204693-9, BBELG 891 148, SWISS 651 754, BRD P-3231088, SSPAIN 553 017, JAP 151 4040.
    • Stolc, S., Bauer, V., Benes, L., Tichy, M., 1983. Patents: CS 229 067, SWED 8204693-9, BBELG 891 148, SWISS 651 754, BRD P-3231088, SSPAIN 553 017, JAP 151 4040.
  • 62
    • 28644444652 scopus 로고    scopus 로고
    • 2+-ATPase sarcoplasmic reticulum by HOCl and HNE and protective effect of some antioxidants
    • 2+-ATPase sarcoplasmic reticulum by HOCl and HNE and protective effect of some antioxidants. Biofactors 23 (2005) 111-116
    • (2005) Biofactors , vol.23 , pp. 111-116
    • Strosova, M.1    Skuciova, M.2    Horakova, L.3
  • 64
    • 0035875154 scopus 로고    scopus 로고
    • 2+-ATPase of the sarcoplasmic reticulum. Review
    • 2+-ATPase of the sarcoplasmic reticulum. Review. Biochemical Journal 356 (2001) 685-704
    • (2001) Biochemical Journal , vol.356 , pp. 685-704
    • Sweadner, K.J.1    Donnet, C.2
  • 65
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum
    • Toyoshima C., Nakasake M., Nomura H., and Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum. Nature 405 (2000) 647-655
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasake, M.2    Nomura, H.3    Ogawa, H.4
  • 69
    • 0033592423 scopus 로고    scopus 로고
    • Peroxinitrite modification of protein thiols: oxidation, nitrosylation and s-glutathilations of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase
    • Viner R.I., Williams T.D., and Schoneich Ch. Peroxinitrite modification of protein thiols: oxidation, nitrosylation and s-glutathilations of functionally important cysteine residue(s) in the sarcoplasmic reticulum Ca-ATPase. Biochemistry 38 (1999) 12408-12415
    • (1999) Biochemistry , vol.38 , pp. 12408-12415
    • Viner, R.I.1    Williams, T.D.2    Schoneich, Ch.3
  • 71
    • 0015029362 scopus 로고
    • Lipid composition in rabbit sarcoplasmic reticulum and occurrence of alkyl ether phospholipids
    • Waku K., Uda Y., and Nakazawa Y. Lipid composition in rabbit sarcoplasmic reticulum and occurrence of alkyl ether phospholipids. Journal of Biochemistry 69 (1971) 483-491
    • (1971) Journal of Biochemistry , vol.69 , pp. 483-491
    • Waku, K.1    Uda, Y.2    Nakazawa, Y.3
  • 73
    • 0016312487 scopus 로고
    • Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes
    • Warren G.B., Toon P.A., Birdsall N.J., Lee A.G., and Metcalfe J.C. Reversible lipid titrations of the activity of pure adenosine triphosphatase-lipid complexes. Biochemistry 13 (1974) 5501-5507
    • (1974) Biochemistry , vol.13 , pp. 5501-5507
    • Warren, G.B.1    Toon, P.A.2    Birdsall, N.J.3    Lee, A.G.4    Metcalfe, J.C.5


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