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Volumn 9, Issue 5, 1998, Pages 211-222

Analysis of the active sites of copper/topa quinone-containing amine oxidases from Lathyrus odoratus and L. sativus seedlings

Author keywords

Amine oxidase; Fabaceae; Grass pea; Lathyrus odoratus; Lathyrus sativus; Sweet pea; Topa quinone

Indexed keywords

COPPER COMPOUNDS; ELECTRON SPIN RESONANCE SPECTROSCOPY; MANGANESE COMPOUNDS; PARAMAGNETIC RESONANCE; REDOX REACTIONS; SUBSTRATES;

EID: 0031661452     PISSN: 09580344     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1565(199809/10)9:5<211::AID-PCA407>3.0.CO;2-X     Document Type: Article
Times cited : (30)

References (60)
  • 1
    • 85053094549 scopus 로고
    • Copper amine oxidases and amines as regulators of cellular processes
    • (Mondovi, B., ed.), CRC Press, Boca Raton
    • Bachrach, U. (1985). Copper amine oxidases and amines as regulators of cellular processes. In Structure and Functions of Amine Oxidases (Mondovi, B., ed.), pp. 5-20, CRC Press, Boca Raton.
    • (1985) Structure and Functions of Amine Oxidases , pp. 5-20
    • Bachrach, U.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0006845086 scopus 로고
    • Copper determinations
    • (Estabrook, R. W and Pullman, M. E., eds.), Academic Press, New York
    • Brumby, P. E. and Massey, V. (1967). Copper determinations. In Methods in Enzymology (Estabrook, R. W and Pullman, M. E., eds.), Vol. 10, pp. 471-474, Academic Press, New York.
    • (1967) Methods in Enzymology , vol.10 , pp. 471-474
    • Brumby, P.E.1    Massey, V.2
  • 5
    • 0028605705 scopus 로고
    • Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase
    • Cai, D. and Klinman, J. P. (1994). Evidence for a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase. J. Biol. Chem. 269, 32039-32042.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32039-32042
    • Cai, D.1    Klinman, J.P.2
  • 6
    • 0016372799 scopus 로고
    • Mitochondrial monoamine oxidase. Inactivation by pargyline. Adduct formation
    • Chuang, H. Y. K., Patek, D. R. and Hellerman, L (1974), Mitochondrial monoamine oxidase. Inactivation by pargyline. Adduct formation. J. Biol. Chem. 249, 2381-2384.
    • (1974) J. Biol. Chem. , vol.249 , pp. 2381-2384
    • Chuang, H.Y.K.1    Patek, D.R.2    Hellerman, L.3
  • 7
    • 0024310284 scopus 로고
    • Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: Purification and properties
    • Cogoni, A., Farci, R., Medda, R., Rinaldi, A. and Floris, G. (1989). Amine oxidase from Lathyrus cicera and Phaseolus vulgaris: purification and properties. Prep. Biochem. 19, 95-112.
    • (1989) Prep. Biochem. , vol.19 , pp. 95-112
    • Cogoni, A.1    Farci, R.2    Medda, R.3    Rinaldi, A.4    Floris, G.5
  • 8
    • 0017195509 scopus 로고
    • Human placental diamine oxidase. Improved purification and characterization of a copper- and manganese-containing amine oxidase with novel substrate specificity
    • Crabbe, M. J., Waight, R. D., Bardsley, W. G., Barker, R. W., Kelly, I. D. and Knowles, P. F. (1976). Human placental diamine oxidase. Improved purification and characterization of a copper-and manganese-containing amine oxidase with novel substrate specificity. Biochem. J. 155, 679-687.
    • (1976) Biochem. J. , vol.155 , pp. 679-687
    • Crabbe, M.J.1    Waight, R.D.2    Bardsley, W.G.3    Barker, R.W.4    Kelly, I.D.5    Knowles, P.F.6
  • 10
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M., Gilles, K. A., Hamilton, J. K., Rebers, P. A. and Smith, F. (1956). Colorimetric method for determination of sugars and related substances. Anal. Chem. 28, 350-356.
    • (1956) Anal. Chem. , vol.28 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 11
    • 0029608781 scopus 로고
    • Copper/quinone-containing amine oxidases, an exciting class of ubiquitous enzymes
    • Frébort, I. and Adachi, O. (1995). Copper/quinone-containing amine oxidases, an exciting class of ubiquitous enzymes. J. Ferment. Bioeng. 80, 625-632.
    • (1995) J. Ferment. Bioeng. , vol.80 , pp. 625-632
    • Frébort, I.1    Adachi, O.2
  • 12
    • 0000407415 scopus 로고
    • Employment of guaiacol for the determination of activities of enzymes generating hydrogen peroxide and for the determination of glucose in blood and urine
    • Frébort, I., Haviger, A. and Peč, P. (1989). Employment of guaiacol for the determination of activities of enzymes generating hydrogen peroxide and for the determination of glucose in blood and urine. Biológia (Bratislava) 44, 729-737.
    • (1989) Biológia (Bratislava) , vol.44 , pp. 729-737
    • Frébort, I.1    Haviger, A.2    Peč, P.3
  • 13
    • 0028125310 scopus 로고
    • Active-site covalent modifications of quinoprotein amine oxidases from Aspergillus niger
    • Frébort, I., Peč, P., Luhová, L., Matsushita, K., Toyama, H. and Adachi, O. (1994). Active-site covalent modifications of quinoprotein amine oxidases from Aspergillus niger. Eur. J. Biochem. 225, 959-965.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 959-965
    • Frébort, I.1    Peč, P.2    Luhová, L.3    Matsushita, K.4    Toyama, H.5    Adachi, O.6
  • 14
    • 0029555568 scopus 로고
    • Half-site reactivity with p-nitrophenylhydrazine and sub-unit separation of the dimeric copper-containing amine oxidase from Aspergillus niger
    • Frébort, I., Toyama, H., Kazunobu, M. and Adachi, O. (1995). Half-site reactivity with p-nitrophenylhydrazine and sub-unit separation of the dimeric copper-containing amine oxidase from Aspergillus niger. Biochem. Mol. Biol. Int. 36, 1207-1216.
    • (1995) Biochem. Mol. Biol. Int. , vol.36 , pp. 1207-1216
    • Frébort, I.1    Toyama, H.2    Kazunobu, M.3    Adachi, O.4
  • 16
    • 0025887806 scopus 로고
    • Structure-function studies of substrate oxidation by bovine serum amine oxidase: Relationship to cofactor structure and mechanism
    • Hartman, C. and Klinman, J. P. (1991). Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism. Biochemistry 30, 4605-4611.
    • (1991) Biochemistry , vol.30 , pp. 4605-4611
    • Hartman, C.1    Klinman, J.P.2
  • 17
    • 0025824482 scopus 로고
    • An investigation of bovine serum amine oxidase active site stoichiometry: Evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimer
    • Janes, S. M. and Klinman, J. P. (1991). An investigation of bovine serum amine oxidase active site stoichiometry: evidence for an aminotransferase mechanism involving two carbonyl cofactors per enzyme dimer. Biochemistry 30, 4599-4605.
    • (1991) Biochemistry , vol.30 , pp. 4599-4605
    • Janes, S.M.1    Klinman, J.P.2
  • 18
    • 0025374783 scopus 로고
    • A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase
    • Janes, S. M., Mu, D., Wemmer, D., Smith, A. J., Kaur, S., Maltby, D., Burlingame, A. L and Klinman, J. P. (1990). A new redox cofactor in eukaryotic enzymes: 6-hydroxydopa at the active site of bovine serum amine oxidase. Science 248, 981-987.
    • (1990) Science , vol.248 , pp. 981-987
    • Janes, S.M.1    Mu, D.2    Wemmer, D.3    Smith, A.J.4    Kaur, S.5    Maltby, D.6    Burlingame, A.L.7    Klinman, J.P.8
  • 21
    • 0030586824 scopus 로고    scopus 로고
    • Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 Å resolution
    • Kumar, V., Dooley, D. M., Freeman, H. C., Guss, J. M., Harvey, I., McGuirl, M. A., Wilce, M. C. J. and Zubak, V. M. (1996). Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 Å resolution. Structure 4, 943-955.
    • (1996) Structure , vol.4 , pp. 943-955
    • Kumar, V.1    Dooley, D.M.2    Freeman, H.C.3    Guss, J.M.4    Harvey, I.5    McGuirl, M.A.6    Wilce, M.C.J.7    Zubak, V.M.8
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 650-685.
    • (1970) Nature , vol.227 , pp. 650-685
    • Laemmli, U.K.1
  • 23
    • 0027181337 scopus 로고
    • Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP
    • Löw, A., Sprinzl, M. and Faulhammer, H. G. (1993). Affinity labeling of c-H-ras p21 consensus elements with periodate-oxidized GDP and GTP. Eur. J. Biochem. 215, 473-479.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 473-479
    • Löw, A.1    Sprinzl, M.2    Faulhammer, H.G.3
  • 26
    • 0343538458 scopus 로고
    • Darstellung der 2-hydroxyderivative des cadaverins und putrescins
    • Macholán, L. (1965). Darstellung der 2-hydroxyderivative des cadaverins und putrescins. Collect. Czech. Chem. Commun. 30, 2074-2079.
    • (1965) Collect. Czech. Chem. Commun. , vol.30 , pp. 2074-2079
    • Macholán, L.1
  • 27
    • 0015526829 scopus 로고
    • 3-Hydroxycadaverine, a new substrate for diamine oxidase
    • Macholán, L. (1972). 3-Hydroxycadaverine, a new substrate for diamine oxidase. Enzymologia 42, 303-315.
    • (1972) Enzymologia , vol.42 , pp. 303-315
    • Macholán, L.1
  • 28
    • 0007933277 scopus 로고
    • Selective and reversible inhibition of diamine oxidase by 1,5-diamino-3-pentanone
    • Mocholán, L. (1974). Selective and reversible inhibition of diamine oxidase by 1,5-diamino-3-pentanone. Collect. Czech. Chem. Commun. 39, 653-661.
    • (1974) Collect. Czech. Chem. Commun. , vol.39 , pp. 653-661
    • Mocholán, L.1
  • 29
    • 0011367076 scopus 로고
    • Isolation and some characteristics of diamine oxidase from etiolated pea seedlings
    • Macholán, L. and Haubrová, J. (1976). Isolation and some characteristics of diamine oxidase from etiolated pea seedlings. Collect. Czech. Chem. Commun. 41, 2987-2996.
    • (1976) Collect. Czech. Chem. Commun. , vol.41 , pp. 2987-2996
    • Macholán, L.1    Haubrová, J.2
  • 30
    • 0001608050 scopus 로고
    • Oxidation of 1,4-diamino-2-butene to pyrrol, a sensitive test of diamine oxidase activity
    • Hubálek, L., Macholán, F. and Šubová, H. (1975). Oxidation of 1,4-diamino-2-butene to pyrrol, a sensitive test of diamine oxidase activity. Collect. Czech. Chem. Commun. 40, 1247-1256.
    • (1975) Collect. Czech. Chem. Commun. , vol.40 , pp. 1247-1256
    • Hubálek, L.1    Macholán, F.2    Šubová, H.3
  • 31
    • 0027965409 scopus 로고
    • Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue
    • Matsuzaki, R., Fukui, T., Sato, H., Ozaki, Y. and Tanizawa, K. (1994). Generation of the topa quinone cofactor in bacterial monoamine oxidase by cupric ion-dependent autooxidation of a specific tyrosyl residue. FEBS Lett. 351, 360-364.
    • (1994) FEBS Lett. , vol.351 , pp. 360-364
    • Matsuzaki, R.1    Fukui, T.2    Sato, H.3    Ozaki, Y.4    Tanizawa, K.5
  • 32
    • 0028914513 scopus 로고
    • Spectroscopic studies on the mechanism of the topa quinone generation in bacterial monoamine oxidase
    • Matsuzaki, R., Suzuki, S., Yamaguchi, K., Fukui, T. and Tanizawa, K. (1995). Spectroscopic studies on the mechanism of the topa quinone generation in bacterial monoamine oxidase. Biochemistry 34, 4524-4530.
    • (1995) Biochemistry , vol.34 , pp. 4524-4530
    • Matsuzaki, R.1    Suzuki, S.2    Yamaguchi, K.3    Fukui, T.4    Tanizawa, K.5
  • 33
    • 0016755153 scopus 로고
    • Novel inactivators of plasma amine oxidase
    • Maycock, A. L., Suva, R. H. and Abeles, R. H. (1975). Novel inactivators of plasma amine oxidase. J. Am. Chem. Soc. 97, 5613-5614.
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 5613-5614
    • Maycock, A.L.1    Suva, R.H.2    Abeles, R.H.3
  • 34
    • 0016411871 scopus 로고
    • Chromatography of nucleic acids, proteins and some phages on granulated hydroxyapatite
    • Mazin, A. L. and Sulimova, G. E. (1975). Chromatography of nucleic acids, proteins and some phages on granulated hydroxyapatite. Biokhimiya 40, 115-122.
    • (1975) Biokhimiya , vol.40 , pp. 115-122
    • Mazin, A.L.1    Sulimova, G.E.2
  • 35
    • 0003825255 scopus 로고
    • Copper-containing amine oxidases
    • (Davidson, V L., ed.), Marcel Dekker, New York
    • McIntire, W. S. and Hartmann, C. (1992). Copper-containing amine oxidases. In Principles and Applications of Quino-proteins. (Davidson, V L., ed.), pp. 97-171, Marcel Dekker, New York.
    • (1992) Principles and Applications of Quino-proteins , pp. 97-171
    • McIntire, W.S.1    Hartmann, C.2
  • 37
    • 0029071681 scopus 로고
    • Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy
    • Moënne-Locoz, P., Nakamura, N., Steinebach, V., Duine, J. A., Mure, M., Klinman, J. P. and Sanders-Loehr, J. (1995). Characterization of the topa quinone cofactor in amine oxidase from Escherichia coli by resonance Raman spectroscopy. Biochemistry 34, 7020-7026.
    • (1995) Biochemistry , vol.34 , pp. 7020-7026
    • Moënne-Locoz, P.1    Nakamura, N.2    Steinebach, V.3    Duine, J.A.4    Mure, M.5    Klinman, J.P.6    Sanders-Loehr, J.7
  • 39
    • 0026562320 scopus 로고
    • Bovine serum amine oxidase: Half-site reactivity with phenylhydrazine, semicarbazide and aromatic hydrazides
    • Morpurgo, L., Agostinelli, E., Mondovi, B., Avigliano, L., Silvestri, R., Stefancich, G. and Artico, M. (1992). Bovine serum amine oxidase: half-site reactivity with phenylhydrazine, semicarbazide and aromatic hydrazides. Biochemistry 31, 2615-2621.
    • (1992) Biochemistry , vol.31 , pp. 2615-2621
    • Morpurgo, L.1    Agostinelli, E.2    Mondovi, B.3    Avigliano, L.4    Silvestri, R.5    Stefancich, G.6    Artico, M.7
  • 41
  • 42
    • 84909650789 scopus 로고
    • In vitro method for testing the toxin-producing capacity of diphtheria bacteria
    • Ouchterlony, O. (1948). In vitro method for testing the toxin-producing capacity of diphtheria bacteria. Acta Pathol. Microbiol. Scand. 25, 186-191.
    • (1948) Acta Pathol. Microbiol. Scand. , vol.25 , pp. 186-191
    • Ouchterlony, O.1
  • 43
    • 0001436142 scopus 로고
    • Characterization of amine oxidases from Pisum, Lens, Lathyrus and Cicer
    • Padiglia, A., Cogoni, A. and Floris, G. (1991). Characterization of amine oxidases from Pisum, Lens, Lathyrus and Cicer. Phytochemistry 30, 3895-3897.
    • (1991) Phytochemistry , vol.30 , pp. 3895-3897
    • Padiglia, A.1    Cogoni, A.2    Floris, G.3
  • 44
    • 0027058097 scopus 로고
    • Lentil seedling amine oxidase: Interaction with carbonyl reagents
    • Padiglia, A., Medda, R. and Floris, G. (1992). Lentil seedling amine oxidase: Interaction with carbonyl reagents. Biochem. Int. 28, 1097-1107.
    • (1992) Biochem. Int. , vol.28 , pp. 1097-1107
    • Padiglia, A.1    Medda, R.2    Floris, G.3
  • 46
    • 0001366310 scopus 로고
    • Determination of the activity of diamine oxidase from pea with Z-1,4-diamino-2-butene as a substrate
    • Peč, P., Chudý, J. and Macholán, L (1991). Determination of the activity of diamine oxidase from pea with Z-1,4-diamino-2-butene as a substrate. Biológia (Bratislava) 46, 665-672.
    • (1991) Biológia (Bratislava) , vol.46 , pp. 665-672
    • Peč, P.1    Chudý, J.2    Macholán, L.3
  • 48
    • 0026605072 scopus 로고
    • cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase
    • Rossi, A., Petruzelli, R. and Finazzi-Agró, A. (1992). cDNA-derived amino-acid sequence of lentil seedlings' amine oxidase. FEBS Lett. 301, 253-257.
    • (1992) FEBS Lett. , vol.301 , pp. 253-257
    • Rossi, A.1    Petruzelli, R.2    Finazzi-Agró, A.3
  • 49
    • 85053099663 scopus 로고
    • Spectroscopic and chemical properties of the amine oxidase copper
    • (Mondovi, B., ed.), CRC Press, Boca Raton
    • Rotilio, G. (1985). Spectroscopic and chemical properties of the amine oxidase copper. In Structure and Functions of Amine Oxidases. (Mondovi, B., ed.), pp. 128-134, CRC Press, Boca Raton.
    • (1985) Structure and Functions of Amine Oxidases , pp. 128-134
    • Rotilio, G.1
  • 50
    • 0030463345 scopus 로고    scopus 로고
    • Differential pulse polarographic study of the redox centres in pea amine oxidase
    • Šebela, M., Studničková, M. and Wimmerová, M. (1996). Differential pulse polarographic study of the redox centres in pea amine oxidase. Bioelectrochem. Bioenerg. 41, 173-179.
    • (1996) Bioelectrochem. Bioenerg. , vol.41 , pp. 173-179
    • Šebela, M.1    Studničková, M.2    Wimmerová, M.3
  • 51
    • 3543074221 scopus 로고
    • Inhibition of pea diamine oxidase by aliphatic amino ketones and their reaction with pyridoxal 5-phosphate
    • Skyvová, M. and Macholán, L. (1970). Inhibition of pea diamine oxidase by aliphatic amino ketones and their reaction with pyridoxal 5-phosphate. Collect. Czech. Chem. Commun. 35, 2345-2354.
    • (1970) Collect. Czech. Chem. Commun. , vol.35 , pp. 2345-2354
    • Skyvová, M.1    Macholán, L.2
  • 53
    • 0029117707 scopus 로고
    • Identification of topa quinone as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase
    • Steinebach, V., Groen, B. W., Wijmenga, S. S., Niessen, W. M. A., Jongejan, J. A. and Duine, J. A. (1995). Identification of topa quinone as illustrated for pig kidney diamine oxidase and Escherichia coli amine oxidase. Anal. Biochem. 230, 159-166.
    • (1995) Anal. Biochem. , vol.230 , pp. 159-166
    • Steinebach, V.1    Groen, B.W.2    Wijmenga, S.S.3    Niessen, W.M.A.4    Jongejan, J.A.5    Duine, J.A.6
  • 54
    • 0029950157 scopus 로고    scopus 로고
    • Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme
    • Steinebach, V., Benen, J. A. E., Postma, P. W., De Vries, S. and Duine, J. (1996). Cloning of the maoA gene that encodes aromatic amine oxidase of Escherichia coli W3350 and characterization of the overexpressed enzyme. Eur. J. Biochem. 237, 584-591.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 584-591
    • Steinebach, V.1    Benen, J.A.E.2    Postma, P.W.3    De Vries, S.4    Duine, J.5
  • 55
    • 0342668232 scopus 로고
    • Diamine oxidase of Lathyrus sativus seedlings
    • Suresh, M. R., Ramakrishna, S. and Adiga, P. R. (1976). Diamine oxidase of Lathyrus sativus seedlings. Phytochemistry 15, 483-485.
    • (1976) Phytochemistry , vol.15 , pp. 483-485
    • Suresh, M.R.1    Ramakrishna, S.2    Adiga, P.R.3
  • 56
    • 0020584806 scopus 로고
    • Reaction of aortic lysyl oxidase with β-aminopropionitrile
    • Tang, S.-S., Trackman, P. C. and Kagan, H. M. (1983). Reaction of aortic lysyl oxidase with β-aminopropionitrile. J. Biol. Chem. 258, 4331-4338.
    • (1983) J. Biol. Chem. , vol.258 , pp. 4331-4338
    • Tang, S.-S.1    Trackman, P.C.2    Kagan, H.M.3
  • 57
    • 0029040435 scopus 로고
    • Cloning and molecular analysis of the pea seedling copper amine oxidase
    • Tipping, A. J. and McPherson, M. J. (1995). Cloning and molecular analysis of the pea seedling copper amine oxidase. J. Biol. Chem. 270, 16939-16946.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16939-16946
    • Tipping, A.J.1    McPherson, M.J.2
  • 58
    • 0027250458 scopus 로고
    • Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase
    • Turowski, P. N., McGuirl, M. A. and Dooley, D. M. (1993). Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase. J. Biol. Chem. 268, 17680-17682.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17680-17682
    • Turowski, P.N.1    McGuirl, M.A.2    Dooley, D.M.3
  • 59
    • 0027651508 scopus 로고
    • Improved Chromatographic purification of pea seedlings diamine oxidase
    • Wimmerová, M., Glatz, Z., Janiczek, O. and Macholán, L. (1993). Improved Chromatographic purification of pea seedlings diamine oxidase. Prep. Biochem. 23, 303-319.
    • (1993) Prep. Biochem. , vol.23 , pp. 303-319
    • Wimmerová, M.1    Glatz, Z.2    Janiczek, O.3    Macholán, L.4


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