메뉴 건너뛰기




Volumn 42, Issue 6, 2014, Pages 1796-1801

Protein moonlighting in iron metabolism: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH)

Author keywords

glyceraldehyde 3 phosphate dehydrogenase (GAPDH); higher order multifunctionality; iron; transferrin; transferrin receptor 3 (TfR3)

Indexed keywords

ACONITATE HYDRATASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LACTOFERRIN; TRANSFERRIN RECEPTOR; TRANSFERRIN RECEPTOR 3; UNCLASSIFIED DRUG; IRON;

EID: 84911912713     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140220     Document Type: Article
Times cited : (42)

References (49)
  • 2
    • 0027402608 scopus 로고
    • The development of awareness of iron-withholding defense
    • PubMed
    • Weinberg, E.D. (1993) The development of awareness of iron-withholding defense. Perspect. Biol. Med. 36, 215-221 PubMed
    • (1993) Perspect. Biol. Med. , vol.36 , pp. 215-221
    • Weinberg, E.D.1
  • 4
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • CrossRef PubMed
    • Henderson, B. and Martin, A. (2011) Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect. Immun. 79, 3476-3491 CrossRef PubMed
    • (2011) Infect. Immun. , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 5
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehydes-3-phosphate dehydrogenase: Biochemical mechanisms and regulatory control
    • CrossRef PubMed
    • Sirover, M.A. (2011) On the functional diversity of glyceraldehydes-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 1810, 741-751 CrossRef PubMed
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 7
    • 83555162529 scopus 로고    scopus 로고
    • Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor
    • CrossRef PubMed
    • Kumar, S., Sheokand, N., Mhadeshwar, M.A., Raje, C.I. and Raje, M. (2012) Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor. Int. J. Biochem. Cell Biol. 44, 189-199 CrossRef PubMed
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 189-199
    • Kumar, S.1    Sheokand, N.2    Mhadeshwar, M.A.3    Raje, C.I.4    Raje, M.5
  • 8
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • PubMed
    • Modun, B. and Williams, P. (1999) The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect. Immun. 67, 1086-1092 PubMed
    • (1999) Infect. Immun. , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 9
    • 34047254111 scopus 로고    scopus 로고
    • The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor
    • CrossRef PubMed
    • Raje, C.I., Kumar, S., Harle, A., Nanda, J.S. and Raje, M. (2007) The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor. J. Biol. Chem. 282, 3252-3261 CrossRef PubMed
    • (2007) J. Biol. Chem. , vol.282 , pp. 3252-3261
    • Raje, C.I.1    Kumar, S.2    Harle, A.3    Nanda, J.S.4    Raje, M.5
  • 10
    • 84861386961 scopus 로고    scopus 로고
    • The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor
    • CrossRef PubMed
    • Rawat, P., Kumar, S., Sheokand, N., Raje, C.I. and Raje, M. (2012) The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor. Biochem. Cell Biol. 90, 329-338 CrossRef PubMed
    • (2012) Biochem. Cell Biol. , vol.90 , pp. 329-338
    • Rawat, P.1    Kumar, S.2    Sheokand, N.3    Raje, C.I.4    Raje, M.5
  • 11
    • 84876161526 scopus 로고    scopus 로고
    • Secreted glyceraldehyde-3-phosphate dehydrogenase is a multifunctional autocrine transferrin receptor for cellular iron acquisition
    • CrossRef PubMed
    • Sheokand, N., Kumar, S., Malhotra, H., Tillu, V., Raje, C.I. and Raje, M. (2013) Secreted glyceraldehyde-3-phosphate dehydrogenase is a multifunctional autocrine transferrin receptor for cellular iron acquisition. Biochim. Biophys. Acta 1830, 3816-3827 CrossRef PubMed
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3816-3827
    • Sheokand, N.1    Kumar, S.2    Malhotra, H.3    Tillu, V.4    Raje, C.I.5    Raje, M.6
  • 12
    • 84857355874 scopus 로고    scopus 로고
    • Molecular evolution of the transferrin family and associated receptors
    • CrossRef PubMed
    • Lambert, L.A. (2012) Molecular evolution of the transferrin family and associated receptors. Biochim. Biophys. Acta 1820, 244-255 CrossRef PubMed
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 244-255
    • Lambert, L.A.1
  • 13
    • 84911921884 scopus 로고    scopus 로고
    • Moonlighting cell-surface GAPDH recruits apotransferrin to effect iron egress from mammalian cells
    • PubMed
    • Sheokand, N., Malhotra, H., Kumar, S., Tillu, V.A., Chauhan, A.S., Raje, C.I. and Raje, M. (2014) Moonlighting cell-surface GAPDH recruits apotransferrin to effect iron egress from mammalian cells. J. Cell Sci. 127, 4279-4291 PubMed
    • (2014) J. Cell Sci. , vol.127 , pp. 4279-4291
    • Sheokand, N.1    Malhotra, H.2    Kumar, S.3    Tillu, V.A.4    Chauhan, A.S.5    Raje, C.I.6    Raje, M.7
  • 14
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • CrossRef PubMed
    • Jeffery, C.J. (1999) Moonlighting proteins. Trends Biochem. Sci. 24, 8-11 CrossRef PubMed
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 15
    • 0020758755 scopus 로고
    • A porcine brain protein (35K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase
    • CrossRef PubMed
    • Kumagai, H. and Sakai, H. (1983) A porcine brain protein (35K protein) which bundles microtubules and its identification as glyceraldehyde 3-phosphate dehydrogenase. J. Biochem. 93, 1259-1269 CrossRef PubMed
    • (1983) J. Biochem. , vol.93 , pp. 1259-1269
    • Kumagai, H.1    Sakai, H.2
  • 16
    • 0021854754 scopus 로고
    • Fusion of phospholipid vesicles induced by muscle glyceraldehyde-3-phosphate dehydrogenase in the absence of calcium
    • CrossRef PubMed
    • Morero, R.D., Viñals, A.L., Bloj, B. and Farías, R.N. (1985) Fusion of phospholipid vesicles induced by muscle glyceraldehyde-3-phosphate dehydrogenase in the absence of calcium. Biochemistry 24, 1904-1909 CrossRef PubMed
    • (1985) Biochemistry , vol.24 , pp. 1904-1909
    • Morero, R.D.1    Viñals, A.L.2    Bloj, B.3    Farías, R.N.4
  • 18
    • 70449525136 scopus 로고    scopus 로고
    • Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation
    • CrossRef PubMed
    • Demarse, N.A., Ponnusamy, S., Spicer, E.K., Apohan, E., Baatz, J.E., Ogretmen, B. and Davies, C. (2009) Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation. J. Mol. Biol. 394, 789-803 CrossRef PubMed
    • (2009) J. Mol. Biol. , vol.394 , pp. 789-803
    • Demarse, N.A.1    Ponnusamy, S.2    Spicer, E.K.3    Apohan, E.4    Baatz, J.E.5    Ogretmen, B.6    Davies, C.7
  • 19
    • 0000241799 scopus 로고
    • PH and the recycling of transferrin during receptor-mediated endocytosis
    • CrossRef PubMed
    • Dautry-Varsat, A., Ciechanover, A. and Lodish, H.F. (1983) pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl. Acad. Sci. U.S.A. 80, 2258-2262 CrossRef PubMed
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 20
    • 84857363315 scopus 로고    scopus 로고
    • Regulation of iron transport and the role of transferrin
    • CrossRef PubMed
    • Gkouvatsos, K., Papanikolaou, G. and Pantopoulos, K. (2012) Regulation of iron transport and the role of transferrin. Biochim. Biophys. Acta 1820, 188-202 CrossRef PubMed
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 188-202
    • Gkouvatsos, K.1    Papanikolaou, G.2    Pantopoulos, K.3
  • 22
    • 28344453346 scopus 로고    scopus 로고
    • Mammalian lactoferrin receptors: Structure and function
    • CrossRef PubMed
    • Suzuki, Y.A., Lopez, V. and Lönnerdal, B. (2005) Mammalian lactoferrin receptors: structure and function. Cell. Mol. Life Sci. 62, 2560-2575 CrossRef PubMed
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2560-2575
    • Suzuki, Y.A.1    Lopez, V.2    Lönnerdal, B.3
  • 23
    • 28344447990 scopus 로고    scopus 로고
    • Multifunctional roles of lactoferrin: A critical overview
    • CrossRef PubMed
    • Ward, P.P., Paz, E. and Conneely, O.M. (2005) Multifunctional roles of lactoferrin: a critical overview. Cell. Mol. Life Sci. 62, 2540-2548 CrossRef PubMed
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 2540-2548
    • Ward, P.P.1    Paz, E.2    Conneely, O.M.3
  • 24
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2: A new member of the transferrin receptor-like family
    • CrossRef PubMed
    • Kawabata, H., Yang, R., Hirama, T., Vuong, P.T., Kawano, S., Gombart, A.F. and Koeffler, H.P. (1999) Molecular cloning of transferrin receptor 2: a new member of the transferrin receptor-like family. J. Biol. Chem. 274, 20826-20832 CrossRef PubMed
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6    Koeffler, H.P.7
  • 25
    • 0032959574 scopus 로고    scopus 로고
    • Transferrin receptor is necessary for development of erythrocytes and the nervous system
    • CrossRef PubMed
    • Levy, J.E., Jin, O.U., Fujiwara, Y., Kuo, F. and Andrews, N. (1999) Transferrin receptor is necessary for development of erythrocytes and the nervous system. Nat. Genet. 21, 396-399 CrossRef PubMed
    • (1999) Nat. Genet. , vol.21 , pp. 396-399
    • Levy, J.E.1    Jin, O.U.2    Fujiwara, Y.3    Kuo, F.4    Andrews, N.5
  • 26
    • 0029953577 scopus 로고    scopus 로고
    • Transferrin receptor-independent uptake of differic transferrin by human hepatoma cells with antisense inhibition of receptor expression
    • CrossRef PubMed
    • Trinder, D., Zak, O. and Aisen, P. (1996) Transferrin receptor-independent uptake of differic transferrin by human hepatoma cells with antisense inhibition of receptor expression. Hepatology 23, 1512-1520 CrossRef PubMed
    • (1996) Hepatology , vol.23 , pp. 1512-1520
    • Trinder, D.1    Zak, O.2    Aisen, P.3
  • 27
    • 0344845282 scopus 로고    scopus 로고
    • Recycling, degradation and sensitivity to the synergistic anion of transferrin in the receptor-independent route of iron uptake by human hepatoma (HuH-7) cells
    • CrossRef PubMed
    • Ikuta, K., Zak, O. and Aisen, P. (2004) Recycling, degradation and sensitivity to the synergistic anion of transferrin in the receptor-independent route of iron uptake by human hepatoma (HuH-7) cells. Int. J. Biochem. Cell Biol. 36, 340-352 CrossRef PubMed
    • (2004) Int. J. Biochem. Cell Biol. , vol.36 , pp. 340-352
    • Ikuta, K.1    Zak, O.2    Aisen, P.3
  • 28
    • 30344443077 scopus 로고    scopus 로고
    • Non-conventional protein secretion in yeast
    • CrossRef PubMed
    • Nombela, C., Gil, C. and Chaffin, W.L. (2006) Non-conventional protein secretion in yeast. Trends Microbiol. 14, 15-21 CrossRef PubMed
    • (2006) Trends Microbiol. , vol.14 , pp. 15-21
    • Nombela, C.1    Gil, C.2    Chaffin, W.L.3
  • 30
    • 27944448840 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase in the extracellular space inhibits cell spreading
    • CrossRef PubMed
    • Yamaji, R., Chatani, E., Harada, N., Sugimoto, K., Inui, H. and Nakano, Y. (2005) Glyceraldehyde-3-phosphate dehydrogenase in the extracellular space inhibits cell spreading. Biochim. Biophys. Acta 1726, 261-271 CrossRef PubMed
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 261-271
    • Yamaji, R.1    Chatani, E.2    Harada, N.3    Sugimoto, K.4    Inui, H.5    Nakano, Y.6
  • 31
    • 0017341543 scopus 로고
    • Glyceraldehyde-phosphate dehydrogenase (total and isoenzyme activity) in the early diagnosis of myocardial infarction
    • PubMed
    • Griffiths, J. and Shaw, S. (1977) Glyceraldehyde-phosphate dehydrogenase (total and isoenzyme activity) in the early diagnosis of myocardial infarction. Clin. Chem. 23, 245-249 PubMed
    • (1977) Clin. Chem. , vol.23 , pp. 245-249
    • Griffiths, J.1    Shaw, S.2
  • 33
    • 28444488323 scopus 로고    scopus 로고
    • Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin
    • CrossRef PubMed
    • Delaby, C., Pilard, N., Gonçalves, A.S., Beaumont, C. and Canonne-Hergaux, F. (2005) Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin. Blood 106, 3979-3984 CrossRef PubMed
    • (2005) Blood , vol.106 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Gonçalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 34
    • 33846650973 scopus 로고    scopus 로고
    • Molecular control of iron transport
    • CrossRef PubMed
    • Ganz, T. (2007) Molecular control of iron transport. J. Am. Soc. Nephrol. 18, 394-400 CrossRef PubMed
    • (2007) J. Am. Soc. Nephrol. , vol.18 , pp. 394-400
    • Ganz, T.1
  • 35
    • 84884534252 scopus 로고    scopus 로고
    • Structure-function analysis of the human ferroportin iron exporter (SLC40A1): Effect of hemochromatosis type 4 disease mutations and identification of critical residues
    • CrossRef PubMed
    • Le Gac, G., Ka, C., Joubrel, R., Gourlaouen, I., Lehn, P., Mornon, J.P., Férec, C. and Callebaut, I. (2013) Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues. Hum. Mutat. 34, 1371-1380 CrossRef PubMed
    • (2013) Hum. Mutat. , vol.34 , pp. 1371-1380
    • Le Gac, G.1    Ka, C.2    Joubrel, R.3    Gourlaouen, I.4    Lehn, P.5    Mornon, J.P.6    Férec, C.7    Callebaut, I.8
  • 36
    • 33644792074 scopus 로고    scopus 로고
    • Iron imports. III. Transfer of iron from the mucosa into circulation
    • CrossRef PubMed
    • Wessling-Resnick, M. (2006) Iron imports. III. Transfer of iron from the mucosa into circulation. Am. J. Physiol. Gastrointest. Liver Physiol. 290, G1-G6 CrossRef PubMed
    • (2006) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.290 , pp. G1-G6
    • Wessling-Resnick, M.1
  • 37
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: Discrimination between glycolytic and fusogenic roles of individual isoforms
    • CrossRef PubMed
    • Glaser, P.E. and Gross, R.W. (1995) Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry 34, 12193-12203 CrossRef PubMed
    • (1995) Biochemistry , vol.34 , pp. 12193-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 40
    • 33744901493 scopus 로고    scopus 로고
    • Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils
    • CrossRef PubMed
    • Terao, Y., Yamaguchi, M., Hamada, S. and Kawabata, S. (2006) Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils. J. Biol. Chem. 281, 14215-14223 CrossRef PubMed
    • (2006) J. Biol. Chem. , vol.281 , pp. 14215-14223
    • Terao, Y.1    Yamaguchi, M.2    Hamada, S.3    Kawabata, S.4
  • 41
    • 0030055892 scopus 로고    scopus 로고
    • Epidermal growth factor-binding protein in Mycobacterium avium and Mycobacterium tuberculosis: A possible role in the mechanism of infection
    • PubMed
    • Bermudez, L.E., Petrofsky, M. and Shelton, K. (1996) Epidermal growth factor-binding protein in Mycobacterium avium and Mycobacterium tuberculosis: a possible role in the mechanism of infection. Infect. Immun. 64, 2917-2922 PubMed
    • (1996) Infect. Immun. , vol.64 , pp. 2917-2922
    • Bermudez, L.E.1    Petrofsky, M.2    Shelton, K.3
  • 42
    • 0031811939 scopus 로고    scopus 로고
    • Patho-ecological implications of microbial acquisition of host iron
    • CrossRef
    • Weinberg, E.D. (1998) Patho-ecological implications of microbial acquisition of host iron. Rev. Med. Microbiol. 9, 171 CrossRef
    • (1998) Rev. Med. Microbiol. , vol.9 , pp. 171
    • Weinberg, E.D.1
  • 43
    • 0036275173 scopus 로고    scopus 로고
    • Transferrin binding in Staphylococcus aureus: Involvement of a cell wall-anchored protein
    • CrossRef PubMed
    • Taylor, J.M. and Heinrichs, D.E. (2002) Transferrin binding in Staphylococcus aureus: involvement of a cell wall-anchored protein. Mol. Microbiol. 43, 1603-1614 CrossRef PubMed
    • (2002) Mol. Microbiol. , vol.43 , pp. 1603-1614
    • Taylor, J.M.1    Heinrichs, D.E.2
  • 44
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • CrossRef PubMed
    • Gray-Owen, S.D. and Schyvers, A.B. (1996) Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 4, 185-191 CrossRef PubMed
    • (1996) Trends Microbiol. , vol.4 , pp. 185-191
    • Gray-Owen, S.D.1    Schyvers, A.B.2
  • 46
    • 79953151566 scopus 로고    scopus 로고
    • Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG
    • CrossRef PubMed
    • Carroll, M.V., Sim, R.B., Bigi, F., Jäkel, A., Antrobus, R. and Mitchell, D.A. (2010) Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG. Protein Cell 1, 859-870 CrossRef PubMed
    • (2010) Protein Cell , vol.1 , pp. 859-870
    • Carroll, M.V.1    Sim, R.B.2    Bigi, F.3    Jäkel, A.4    Antrobus, R.5    Mitchell, D.A.6
  • 47
    • 70349873656 scopus 로고    scopus 로고
    • +-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase
    • PubMed
    • +-dependent post-translational modification of Escherichia coli glyceraldehyde-3-phosphate dehydrogenase. Int. Microbiol. 12, 187-192PubMed
    • (2009) Int. Microbiol. , vol.12 , pp. 187-192
    • Aguilera, L.1    Giménez, R.2    Badia, J.3    Aguilar, J.4    Baldoma, L.5
  • 48
    • 34249332380 scopus 로고    scopus 로고
    • Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: Interaction of the extracellular enzyme with human plasminogen and fibrinogen
    • CrossRef PubMed
    • Egea, L., Aguilera, L., Giménez, R., Sorolla, M.A., Aguilar, J., Badía, J. and Baldoma, L. (2007) Role of secreted glyceraldehyde-3-phosphate dehydrogenase in the infection mechanism of enterohemorrhagic and enteropathogenic Escherichia coli: interaction of the extracellular enzyme with human plasminogen and fibrinogen. Int. J. Biochem. Cell Biol. 39, 1190-1203 CrossRef PubMed
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1190-1203
    • Egea, L.1    Aguilera, L.2    Giménez, R.3    Sorolla, M.A.4    Aguilar, J.5    Badía, J.6    Baldoma, L.7
  • 49
    • 84861065569 scopus 로고    scopus 로고
    • Subcellular dynamics of multifunctional protein regulation: Mechanisms of GAPDH intracellular translocation
    • CrossRef PubMed
    • Sirover, M.A. (2012) Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J. Cell. Biochem. 113, 2193-2200 CrossRef PubMed
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2193-2200
    • Sirover, M.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.