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Volumn 1852, Issue 10, 2015, Pages 2170-2182

Differential roles of MMP-9 in early and late stages of dystrophic muscles in a mouse model of Duchenne muscular dystrophy

Author keywords

Dystrophin; Fibrosis; MCP 1; MIP 2; MMP 9; Osteopontin

Indexed keywords

CXCL3 CHEMOKINE; GELATINASE A; GELATINASE B; MESSENGER RNA; MONOCYTE CHEMOTACTIC PROTEIN 1; MYOGENIC FACTOR 5; OSTEOPONTIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; TRANSCRIPTION FACTOR PAX3;

EID: 84938691920     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2015.07.008     Document Type: Article
Times cited : (20)

References (66)
  • 2
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman E.P., Brown R.H., Kunkel L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987, 51:919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 3
    • 0024600620 scopus 로고
    • Association of dystrophin and an integral membrane glycoprotein
    • Campbell K.P., Kahl S.D. Association of dystrophin and an integral membrane glycoprotein. Nature 1989, 338:259-262.
    • (1989) Nature , vol.338 , pp. 259-262
    • Campbell, K.P.1    Kahl, S.D.2
  • 4
    • 33749015734 scopus 로고    scopus 로고
    • Molecular mechanisms of muscular dystrophies: old and new players
    • Davies K.E., Nowak K.J. Molecular mechanisms of muscular dystrophies: old and new players. Nat. Rev. Mol. Cell Biol. 2006, 7:762-773.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 762-773
    • Davies, K.E.1    Nowak, K.J.2
  • 6
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A., Ewald A.J., Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat. Rev. Mol. Cell Biol. 2007, 8:221-233.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 7
    • 0037832412 scopus 로고    scopus 로고
    • The basement membrane/basal lamina of skeletal muscle
    • Sanes J.R. The basement membrane/basal lamina of skeletal muscle. J. Biol. Chem. 2003, 278:12601-12604.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12601-12604
    • Sanes, J.R.1
  • 8
    • 1642313674 scopus 로고    scopus 로고
    • Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading
    • Kjaer M. Role of extracellular matrix in adaptation of tendon and skeletal muscle to mechanical loading. Physiol. Rev. 2004, 84:649-698.
    • (2004) Physiol. Rev. , vol.84 , pp. 649-698
    • Kjaer, M.1
  • 9
    • 36049005089 scopus 로고    scopus 로고
    • Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation
    • Van Lint P., Libert C. Chemokine and cytokine processing by matrix metalloproteinases and its effect on leukocyte migration and inflammation. J. Leukoc. Biol. 2007, 82:1375-1381.
    • (2007) J. Leukoc. Biol. , vol.82 , pp. 1375-1381
    • Van Lint, P.1    Libert, C.2
  • 10
    • 77954582762 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitor batimastat alleviates pathology and improves skeletal muscle function in dystrophin-deficient mdx mice
    • Kumar A., Bhatnagar S. Matrix metalloproteinase inhibitor batimastat alleviates pathology and improves skeletal muscle function in dystrophin-deficient mdx mice. Am. J. Pathol. 2010, 177:248-260.
    • (2010) Am. J. Pathol. , vol.177 , pp. 248-260
    • Kumar, A.1    Bhatnagar, S.2
  • 11
  • 12
    • 20444386565 scopus 로고    scopus 로고
    • Up-regulation of mitogen activated protein kinases in mdx skeletal muscle following chronic treadmill exercise
    • Nakamura A., Yoshida K., Ueda H., Takeda S., Ikeda S. Up-regulation of mitogen activated protein kinases in mdx skeletal muscle following chronic treadmill exercise. Biochim. Biophys. Acta 2005, 1740:326-331.
    • (2005) Biochim. Biophys. Acta , vol.1740 , pp. 326-331
    • Nakamura, A.1    Yoshida, K.2    Ueda, H.3    Takeda, S.4    Ikeda, S.5
  • 13
    • 34447620885 scopus 로고    scopus 로고
    • Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ)
    • Fukushima K., Nakamura A., Ueda H., Yuasa K., Yoshida K., Takeda S., Ikeda S. Activation and localization of matrix metalloproteinase-2 and -9 in the skeletal muscle of the muscular dystrophy dog (CXMDJ). BMC Musculoskelet. Disord. 2007, 8:54.
    • (2007) BMC Musculoskelet. Disord. , vol.8 , pp. 54
    • Fukushima, K.1    Nakamura, A.2    Ueda, H.3    Yuasa, K.4    Yoshida, K.5    Takeda, S.6    Ikeda, S.7
  • 15
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: effectors of development and normal physiology
    • Vu T.H., Werb Z. Matrix metalloproteinases: effectors of development and normal physiology. Genes Dev. 2000, 14:2123-2133.
    • (2000) Genes Dev. , vol.14 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 16
    • 4444304939 scopus 로고    scopus 로고
    • Regulation of matrix biology by matrix metalloproteinases
    • Mott J.D., Werb Z. Regulation of matrix biology by matrix metalloproteinases. Curr. Opin. Cell Biol. 2004, 16:558-564.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 558-564
    • Mott, J.D.1    Werb, Z.2
  • 17
    • 84865285291 scopus 로고    scopus 로고
    • Matrix metalloproteinases in skeletal muscles: friends or foes?
    • Alameddine H.S. Matrix metalloproteinases in skeletal muscles: friends or foes?. Neurobiol. Dis. 2012, 48:508-518.
    • (2012) Neurobiol. Dis. , vol.48 , pp. 508-518
    • Alameddine, H.S.1
  • 18
    • 79954499665 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 ablation in dystrophin-deficient mdx muscles reduces angiogenesis resulting in impaired growth of regenerated muscle fibers
    • Miyazaki D., Nakamura A., Fukushima K., Yoshida K., Takeda S., Ikeda S. Matrix metalloproteinase-2 ablation in dystrophin-deficient mdx muscles reduces angiogenesis resulting in impaired growth of regenerated muscle fibers. Hum. Mol. Genet. 2011, 20:1787-1799.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 1787-1799
    • Miyazaki, D.1    Nakamura, A.2    Fukushima, K.3    Yoshida, K.4    Takeda, S.5    Ikeda, S.6
  • 19
    • 0035878554 scopus 로고    scopus 로고
    • Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • Yamada H., Saito F., Fukuta-Ohi H., Zhong D., Hase A., Arai K., Okuyama A., Maekawa R., Shimizu T., Matsumura K. Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum. Mol. Genet. 2001, 10:1563-1569.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5    Arai, K.6    Okuyama, A.7    Maekawa, R.8    Shimizu, T.9    Matsumura, K.10
  • 20
  • 21
    • 67649851014 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy
    • Li H., Mittal A., Makonchuk D.Y., Bhatnagar S., Kumar A. Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum. Mol. Genet. 2009, 18:2584-2598.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2584-2598
    • Li, H.1    Mittal, A.2    Makonchuk, D.Y.3    Bhatnagar, S.4    Kumar, A.5
  • 22
    • 84881594834 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 inhibition improves proliferation and engraftment of myogenic cells in dystrophic muscle of mdx mice
    • Hindi S.M., Shin J., Ogura Y., Li H., Kumar A. Matrix metalloproteinase-9 inhibition improves proliferation and engraftment of myogenic cells in dystrophic muscle of mdx mice. PLoS One 2013, 8:e72121.
    • (2013) PLoS One , vol.8 , pp. e72121
    • Hindi, S.M.1    Shin, J.2    Ogura, Y.3    Li, H.4    Kumar, A.5
  • 23
    • 80052668815 scopus 로고    scopus 로고
    • Osteopontin-stimulated expression of matrix metalloproteinase-9 causes cardiomyopathy in the mdx model of Duchenne muscular dystrophy
    • Dahiya S., Givvimani S., Bhatnagar S., Qipshidze N., Tyagi S.C., Kumar A. Osteopontin-stimulated expression of matrix metalloproteinase-9 causes cardiomyopathy in the mdx model of Duchenne muscular dystrophy. J. Immunol. 2011, 187:2723-2731.
    • (2011) J. Immunol. , vol.187 , pp. 2723-2731
    • Dahiya, S.1    Givvimani, S.2    Bhatnagar, S.3    Qipshidze, N.4    Tyagi, S.C.5    Kumar, A.6
  • 24
    • 84872063624 scopus 로고    scopus 로고
    • Osteopontin deficiency delays inflammatory infiltration and the onset of muscle regeneration in a mouse model of muscle injury
    • Uaesoontrachoon K., Wasgewatte Wijesinghe D.K., Mackie E.J., Pagel C.N. Osteopontin deficiency delays inflammatory infiltration and the onset of muscle regeneration in a mouse model of muscle injury. Dis. Model. Mech. 2013, 6:197-205.
    • (2013) Dis. Model. Mech. , vol.6 , pp. 197-205
    • Uaesoontrachoon, K.1    Wasgewatte Wijesinghe, D.K.2    Mackie, E.J.3    Pagel, C.N.4
  • 27
    • 1042268862 scopus 로고    scopus 로고
    • Temporal gene expression profiling of dystrophin-deficient (mdx) mouse diaphragm identifies conserved and muscle group-specific mechanisms in the pathogenesis of muscular dystrophy
    • Porter J.D., Merriam A.P., Leahy P., Gong B., Feuerman J., Cheng G., Khanna S. Temporal gene expression profiling of dystrophin-deficient (mdx) mouse diaphragm identifies conserved and muscle group-specific mechanisms in the pathogenesis of muscular dystrophy. Hum. Mol. Genet. 2004, 13:257-269.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 257-269
    • Porter, J.D.1    Merriam, A.P.2    Leahy, P.3    Gong, B.4    Feuerman, J.5    Cheng, G.6    Khanna, S.7
  • 30
    • 0029827468 scopus 로고    scopus 로고
    • The mdx-amplification-resistant mutation system assay, a simple and rapid polymerase chain reaction-based detection of the mdx allele
    • Amalfitano A., Chamberlain J.S. The mdx-amplification-resistant mutation system assay, a simple and rapid polymerase chain reaction-based detection of the mdx allele. Muscle Nerve 1996, 19:1549-1553.
    • (1996) Muscle Nerve , vol.19 , pp. 1549-1553
    • Amalfitano, A.1    Chamberlain, J.S.2
  • 31
    • 0007006712 scopus 로고    scopus 로고
    • Muscle regeneration in mdx mice: resistance to repeated necrosis is compatible with myofiber maturity
    • Massa R., Silvestri G., Zeng Y.C., Martorana A., Sancesario G., Bernardi G. Muscle regeneration in mdx mice: resistance to repeated necrosis is compatible with myofiber maturity. Basic Appl. Myol. 1997, 7:387-394.
    • (1997) Basic Appl. Myol. , vol.7 , pp. 387-394
    • Massa, R.1    Silvestri, G.2    Zeng, Y.C.3    Martorana, A.4    Sancesario, G.5    Bernardi, G.6
  • 32
    • 84880339278 scopus 로고    scopus 로고
    • Initial pulmonary respiration causes massive diaphragm damage and hyper-CKemia in Duchenne muscular dystrophy dog
    • Nakamura A., Kobayashi M., Kuraoka M., Yuasa K., Yugeta N., Okada T., Takeda S. Initial pulmonary respiration causes massive diaphragm damage and hyper-CKemia in Duchenne muscular dystrophy dog. Sci. Rep. 2013, 3:2183.
    • (2013) Sci. Rep. , vol.3 , pp. 2183
    • Nakamura, A.1    Kobayashi, M.2    Kuraoka, M.3    Yuasa, K.4    Yugeta, N.5    Okada, T.6    Takeda, S.7
  • 34
    • 81355147868 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 deficiency results in decreased fiber cross-sectional area and alters fiber type distribution in mouse hindlimb skeletal muscle
    • Mehan R.S., Greybeck B.J., Emmons K., Byrnes W.C., Allen D.L. Matrix metalloproteinase-9 deficiency results in decreased fiber cross-sectional area and alters fiber type distribution in mouse hindlimb skeletal muscle. Cells Tissues Organs 2011, 194:510-520.
    • (2011) Cells Tissues Organs , vol.194 , pp. 510-520
    • Mehan, R.S.1    Greybeck, B.J.2    Emmons, K.3    Byrnes, W.C.4    Allen, D.L.5
  • 35
    • 45049087094 scopus 로고    scopus 로고
    • Towards developing standard operating procedures for pre-clinical testing in the mdx mouse model of Duchenne muscular dystrophy
    • Grounds M.D., Radley H.G., Lynch G.S., Nagaraju K., De Luca A. Towards developing standard operating procedures for pre-clinical testing in the mdx mouse model of Duchenne muscular dystrophy. Neurobiol. Dis. 2008, 31:1-19.
    • (2008) Neurobiol. Dis. , vol.31 , pp. 1-19
    • Grounds, M.D.1    Radley, H.G.2    Lynch, G.S.3    Nagaraju, K.4    De Luca, A.5
  • 36
    • 58749098598 scopus 로고    scopus 로고
    • Shifts in macrophage phenotypes and macrophage competition for arginine metabolism affect the severity of muscle pathology in muscular dystrophy
    • Villalta S.A., Nguyen H.X., Deng B., Gotoh T., Tidball J.G. Shifts in macrophage phenotypes and macrophage competition for arginine metabolism affect the severity of muscle pathology in muscular dystrophy. Hum. Mol. Genet. 2009, 18:482-496.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 482-496
    • Villalta, S.A.1    Nguyen, H.X.2    Deng, B.3    Gotoh, T.4    Tidball, J.G.5
  • 40
    • 58649114969 scopus 로고
    • Cytokines derived from cultured skeletal muscle cells after mechanical strain promote neutrophil chemotaxis in vitro
    • Peterson J.M., Pizza F.X. Cytokines derived from cultured skeletal muscle cells after mechanical strain promote neutrophil chemotaxis in vitro. J. Appl. Physiol. 1985, 106(2009):130-137.
    • (1985) J. Appl. Physiol. , vol.106 , Issue.2009 , pp. 130-137
    • Peterson, J.M.1    Pizza, F.X.2
  • 41
    • 84864283300 scopus 로고    scopus 로고
    • Muscles, exercise and obesity: skeletal muscle as a secretory organ
    • Pedersen B.K., Febbraio M.A. Muscles, exercise and obesity: skeletal muscle as a secretory organ. Nat. Rev. Endocrinol. 2012, 8:457-465.
    • (2012) Nat. Rev. Endocrinol. , vol.8 , pp. 457-465
    • Pedersen, B.K.1    Febbraio, M.A.2
  • 44
    • 33748519220 scopus 로고    scopus 로고
    • Reduced necrosis of dystrophic muscle by depletion of host neutrophils, or blocking TNFalpha function with Etanercept in mdx mice
    • Hodgetts S., Radley H., Davies M., Grounds M.D. Reduced necrosis of dystrophic muscle by depletion of host neutrophils, or blocking TNFalpha function with Etanercept in mdx mice. Neuromuscul. Disord. 2006, 16:591-602.
    • (2006) Neuromuscul. Disord. , vol.16 , pp. 591-602
    • Hodgetts, S.1    Radley, H.2    Davies, M.3    Grounds, M.D.4
  • 45
    • 77951700255 scopus 로고    scopus 로고
    • Regulatory interactions between muscle and the immune system during muscle regeneration
    • Tidball J.G., Villalta S.A. Regulatory interactions between muscle and the immune system during muscle regeneration. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2010, 298:R1173-R1187.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.298 , pp. R1173-R1187
    • Tidball, J.G.1    Villalta, S.A.2
  • 46
    • 78751682676 scopus 로고    scopus 로고
    • Interleukin-10 reduces the pathology of mdx muscular dystrophy by deactivating M1 macrophages and modulating macrophage phenotype
    • Villalta S.A., Rinaldi C., Deng B., Liu G., Fedor B., Tidball J.G. Interleukin-10 reduces the pathology of mdx muscular dystrophy by deactivating M1 macrophages and modulating macrophage phenotype. Hum. Mol. Genet. 2011, 20:790-805.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 790-805
    • Villalta, S.A.1    Rinaldi, C.2    Deng, B.3    Liu, G.4    Fedor, B.5    Tidball, J.G.6
  • 48
    • 0042570554 scopus 로고    scopus 로고
    • The inflammatory response: friend or enemy for muscle injury?
    • Toumi H., Best T.M. The inflammatory response: friend or enemy for muscle injury?. Br. J. Sports Med. 2003, 37:284-286.
    • (2003) Br. J. Sports Med. , vol.37 , pp. 284-286
    • Toumi, H.1    Best, T.M.2
  • 49
    • 21044449794 scopus 로고    scopus 로고
    • Null mutation of myeloperoxidase in mice prevents mechanical activation of neutrophil lysis of muscle cell membranes in vitro and in vivo
    • Nguyen H.X., Lusis A.J., Tidball J.G. Null mutation of myeloperoxidase in mice prevents mechanical activation of neutrophil lysis of muscle cell membranes in vitro and in vivo. J. Physiol. 2005, 565:403-413.
    • (2005) J. Physiol. , vol.565 , pp. 403-413
    • Nguyen, H.X.1    Lusis, A.J.2    Tidball, J.G.3
  • 52
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact
    • Van den Steen P.E., Proost P., Wuyts A., Van Damme J., Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-alpha and leaves RANTES and MCP-2 intact. Blood 2000, 96:2673-2681.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van den Steen, P.E.1    Proost, P.2    Wuyts, A.3    Van Damme, J.4    Opdenakker, G.5
  • 59
    • 84882731713 scopus 로고    scopus 로고
    • Interleukin-6 myokine signaling in skeletal muscle: a double-edged sword?
    • Munoz-Canoves P., Scheele C., Pedersen B.K., Serrano A.L. Interleukin-6 myokine signaling in skeletal muscle: a double-edged sword?. FEBS J. 2013, 280:4131-4148.
    • (2013) FEBS J. , vol.280 , pp. 4131-4148
    • Munoz-Canoves, P.1    Scheele, C.2    Pedersen, B.K.3    Serrano, A.L.4
  • 61
    • 0031656460 scopus 로고    scopus 로고
    • Matrix metalloproteinases: structures, evolution, and diversification
    • Massova I., Kotra L.P., Fridman R., Mobashery S. Matrix metalloproteinases: structures, evolution, and diversification. FASEB J. 1998, 12:1075-1095.
    • (1998) FASEB J. , vol.12 , pp. 1075-1095
    • Massova, I.1    Kotra, L.P.2    Fridman, R.3    Mobashery, S.4
  • 62
    • 80054950719 scopus 로고    scopus 로고
    • Elevated levels of active matrix metalloproteinase-9 cause hypertrophy in skeletal muscle of normal and dystrophin-deficient mdx mice
    • Dahiya S., Bhatnagar S., Hindi S.M., Jiang C., Paul P.K., Kuang S., Kumar A. Elevated levels of active matrix metalloproteinase-9 cause hypertrophy in skeletal muscle of normal and dystrophin-deficient mdx mice. Hum. Mol. Genet. 2011, 20:4345-4359.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 4345-4359
    • Dahiya, S.1    Bhatnagar, S.2    Hindi, S.M.3    Jiang, C.4    Paul, P.K.5    Kuang, S.6    Kumar, A.7
  • 63
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q., Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000, 14:163-176.
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2
  • 65
    • 33745119413 scopus 로고    scopus 로고
    • Corticosteroid and doxycycline suppress MMP-9 and inflammatory cytokine expression, MAPK activation in the corneal epithelium in experimental dry eye
    • De Paiva C.S., Corrales R.M., Villarreal A.L., Farley W.J., Li D.Q., Stern M.E., Pflugfelder S.C. Corticosteroid and doxycycline suppress MMP-9 and inflammatory cytokine expression, MAPK activation in the corneal epithelium in experimental dry eye. Exp. Eye Res. 2006, 83:526-535.
    • (2006) Exp. Eye Res. , vol.83 , pp. 526-535
    • De Paiva, C.S.1    Corrales, R.M.2    Villarreal, A.L.3    Farley, W.J.4    Li, D.Q.5    Stern, M.E.6    Pflugfelder, S.C.7
  • 66
    • 39049112077 scopus 로고    scopus 로고
    • Serum gelatinases (MMP-2 and MMP-9) and VCAM-1 as a guideline in a therapeutic approach in Graves' ophthalmopathy
    • Mysliwiec J., Adamczyk M., Pawlowski P., Nikolajuk A., Gorska M. Serum gelatinases (MMP-2 and MMP-9) and VCAM-1 as a guideline in a therapeutic approach in Graves' ophthalmopathy. Endokrynol. Pol. 2007, 58:105-109.
    • (2007) Endokrynol. Pol. , vol.58 , pp. 105-109
    • Mysliwiec, J.1    Adamczyk, M.2    Pawlowski, P.3    Nikolajuk, A.4    Gorska, M.5


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