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Volumn 150, Issue 1, 2017, Pages 74-86

Modulation of infection-mediated migration of neutrophils and CXCR2 trafficking by osteopontin

Author keywords

CXCR2; endodontic infection; integrin v; osteopontin; receptor recycling

Indexed keywords

CHEMOKINE RECEPTOR CXCR2; CXCL1 CHEMOKINE; OSTEOPONTIN; ALPHA5 INTEGRIN;

EID: 84990975271     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/imm.12668     Document Type: Article
Times cited : (26)

References (58)
  • 2
    • 84927709900 scopus 로고    scopus 로고
    • On the dynamics of root canal infections – what we understand and what we don't
    • Zehnder M, Belibasakis GN. On the dynamics of root canal infections – what we understand and what we don't. Virulence 2015; 6:216–22.
    • (2015) Virulence , vol.6 , pp. 216-222
    • Zehnder, M.1    Belibasakis, G.N.2
  • 3
    • 70350381756 scopus 로고    scopus 로고
    • Diversity of endodontic microbiota revisited
    • Siqueira JF Jr, Rocas IN. Diversity of endodontic microbiota revisited. J Dent Res 2009; 88:969–81.
    • (2009) J Dent Res , vol.88 , pp. 969-981
    • Siqueira, J.F.1    Rocas, I.N.2
  • 4
    • 0034292422 scopus 로고    scopus 로고
    • IL-10, but not IL-4, suppresses infection-stimulated bone resorption in vivo
    • Sasaki H, Hou L, Belani A, Wang CY, Uchiyama T, Muller R et al. IL-10, but not IL-4, suppresses infection-stimulated bone resorption in vivo. J Immunol 2000; 165:3626–30.
    • (2000) J Immunol , vol.165 , pp. 3626-3630
    • Sasaki, H.1    Hou, L.2    Belani, A.3    Wang, C.Y.4    Uchiyama, T.5    Muller, R.6
  • 5
    • 0035139890 scopus 로고    scopus 로고
    • Interleukin-6 deficiency increases inflammatory bone destruction
    • Balto K, Sasaki H, Stashenko P. Interleukin-6 deficiency increases inflammatory bone destruction. Infect Immun 2001; 69:744–50.
    • (2001) Infect Immun , vol.69 , pp. 744-750
    • Balto, K.1    Sasaki, H.2    Stashenko, P.3
  • 6
    • 3242804261 scopus 로고    scopus 로고
    • MIP-1γ promotes receptor-activator-of-NF-κB-ligand-induced osteoclast formation and survival
    • Okamatsu Y, Kim D, Battaglino R, Sasaki H, Spate U, Stashenko P. MIP-1γ promotes receptor-activator-of-NF-κB-ligand-induced osteoclast formation and survival. J Immunol 2004; 173:2084–90.
    • (2004) J Immunol , vol.173 , pp. 2084-2090
    • Okamatsu, Y.1    Kim, D.2    Battaglino, R.3    Sasaki, H.4    Spate, U.5    Stashenko, P.6
  • 7
    • 0346497862 scopus 로고    scopus 로고
    • Gamma interferon (IFN-γ) and IFN-γ-inducing cytokines interleukin-12 (IL-12) and IL-18 do not augment infection-stimulated bone resorption in vivo
    • Sasaki H, Balto K, Kawashima N, Eastcott J, Hoshino K, Akira S et al. Gamma interferon (IFN-γ) and IFN-γ-inducing cytokines interleukin-12 (IL-12) and IL-18 do not augment infection-stimulated bone resorption in vivo. Clin Diagn Lab Immunol 2004; 11:106–10.
    • (2004) Clin Diagn Lab Immunol , vol.11 , pp. 106-110
    • Sasaki, H.1    Balto, K.2    Kawashima, N.3    Eastcott, J.4    Hoshino, K.5    Akira, S.6
  • 8
    • 84881400367 scopus 로고    scopus 로고
    • IL-17 receptor A signaling is protective in infection-stimulated periapical bone destruction
    • AlShwaimi E, Berggreen E, Furusho H, Rossall JC, Dobeck J, Yoganathan S et al. IL-17 receptor A signaling is protective in infection-stimulated periapical bone destruction. J Immunol 2013; 191:1785–91.
    • (2013) J Immunol , vol.191 , pp. 1785-1791
    • AlShwaimi, E.1    Berggreen, E.2    Furusho, H.3    Rossall, J.C.4    Dobeck, J.5    Yoganathan, S.6
  • 10
    • 51649127081 scopus 로고    scopus 로고
    • The phagocytes: neutrophils and monocytes
    • Dale DC, Boxer L, Liles WC. The phagocytes: neutrophils and monocytes. Blood 2008; 112:935–45.
    • (2008) Blood , vol.112 , pp. 935-945
    • Dale, D.C.1    Boxer, L.2    Liles, W.C.3
  • 11
    • 0032936191 scopus 로고    scopus 로고
    • Infection-stimulated infraosseus inflammation and bone destruction is increased in P-/E-selectin knockout mice
    • Kawashima N, Niederman R, Hynes RO, Ullmann-Cullere M, Stashenko P. Infection-stimulated infraosseus inflammation and bone destruction is increased in P-/E-selectin knockout mice. Immunology 1999; 97:117–23.
    • (1999) Immunology , vol.97 , pp. 117-123
    • Kawashima, N.1    Niederman, R.2    Hynes, R.O.3    Ullmann-Cullere, M.4    Stashenko, P.5
  • 12
    • 84907092888 scopus 로고    scopus 로고
    • Pathogenic bacterial species associated with endodontic infection evade innate immune control by disabling neutrophils
    • Matsui A, Jin JO, Johnston CD, Yamazaki H, Houri-Haddad Y, Rittling SR. Pathogenic bacterial species associated with endodontic infection evade innate immune control by disabling neutrophils. Infect Immun 2014; 82:4068–79.
    • (2014) Infect Immun , vol.82 , pp. 4068-4079
    • Matsui, A.1    Jin, J.O.2    Johnston, C.D.3    Yamazaki, H.4    Houri-Haddad, Y.5    Rittling, S.R.6
  • 14
    • 33748142935 scopus 로고    scopus 로고
    • ELR+ CXC chemokines and their receptors (CXC chemokine receptor 1 and CXC chemokine receptor 2) as new therapeutic targets
    • Bizzarri C, Beccari AR, Bertini R, Cavicchia MR, Giorgini S, Allegretti M. ELR+ CXC chemokines and their receptors (CXC chemokine receptor 1 and CXC chemokine receptor 2) as new therapeutic targets. Pharmacol Ther 2006; 112:139–49.
    • (2006) Pharmacol Ther , vol.112 , pp. 139-149
    • Bizzarri, C.1    Beccari, A.R.2    Bertini, R.3    Cavicchia, M.R.4    Giorgini, S.5    Allegretti, M.6
  • 15
    • 34147126728 scopus 로고    scopus 로고
    • An essential role for IL-17 in preventing pathogen-initiated bone destruction: recruitment of neutrophils to inflamed bone requires IL-17 receptor-dependent signals
    • Yu JJ, Ruddy MJ, Wong GC, Sfintescu C, Baker PJ, Smith JB et al. An essential role for IL-17 in preventing pathogen-initiated bone destruction: recruitment of neutrophils to inflamed bone requires IL-17 receptor-dependent signals. Blood 2007; 109:3794–802.
    • (2007) Blood , vol.109 , pp. 3794-3802
    • Yu, J.J.1    Ruddy, M.J.2    Wong, G.C.3    Sfintescu, C.4    Baker, P.J.5    Smith, J.B.6
  • 16
  • 17
    • 77952705167 scopus 로고    scopus 로고
    • Importance of CXC chemokine receptor 2 in alveolar neutrophil and exudate macrophage recruitment in response to pneumococcal lung infection
    • Herbold W, Maus R, Hahn I, Ding N, Srivastava M, Christman JW et al. Importance of CXC chemokine receptor 2 in alveolar neutrophil and exudate macrophage recruitment in response to pneumococcal lung infection. Infect Immun 2010; 78:2620–30.
    • (2010) Infect Immun , vol.78 , pp. 2620-2630
    • Herbold, W.1    Maus, R.2    Hahn, I.3    Ding, N.4    Srivastava, M.5    Christman, J.W.6
  • 18
    • 84940688678 scopus 로고    scopus 로고
    • Early cytokine response to infection with pathogenic vs non-pathogenic organisms in a mouse model of endodontic infection
    • Matsui A, Stephens D, Kantarci A, Rittling SR. Early cytokine response to infection with pathogenic vs non-pathogenic organisms in a mouse model of endodontic infection. PLoS ONE 2015; 10:e0132752.
    • (2015) PLoS ONE , vol.10
    • Matsui, A.1    Stephens, D.2    Kantarci, A.3    Rittling, S.R.4
  • 19
    • 79956157867 scopus 로고    scopus 로고
    • Osteopontin in macrophage function
    • Rittling SR. Osteopontin in macrophage function. Expert Rev Mol Med 2011; 13:e15.
    • (2011) Expert Rev Mol Med , vol.13
    • Rittling, S.R.1
  • 20
    • 79955029805 scopus 로고    scopus 로고
    • Osteopontin, intrinsic tissue regulator of intractable inflammatory diseases
    • Uede T. Osteopontin, intrinsic tissue regulator of intractable inflammatory diseases. Pathol Int 2011; 61:265–80.
    • (2011) Pathol Int , vol.61 , pp. 265-280
    • Uede, T.1
  • 22
    • 84862988248 scopus 로고    scopus 로고
    • NLRP3 inflammasome induces chemotactic immune cell migration to the CNS in experimental autoimmune encephalomyelitis
    • Inoue M, Williams KL, Gunn MD, Shinohara ML. NLRP3 inflammasome induces chemotactic immune cell migration to the CNS in experimental autoimmune encephalomyelitis. Proc Natl Acad Sci U S A 2012; 109:10480–5.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10480-10485
    • Inoue, M.1    Williams, K.L.2    Gunn, M.D.3    Shinohara, M.L.4
  • 23
    • 84875178124 scopus 로고    scopus 로고
    • Osteopontin mediates macrophage chemotaxis via α4 and α9 integrins and survival via the α4 integrin
    • Lund SA, Wilson CL, Raines EW, Tang J, Giachelli CM, Scatena M. Osteopontin mediates macrophage chemotaxis via α4 and α9 integrins and survival via the α4 integrin. J Cell Biochem 2013; 114:1194–202.
    • (2013) J Cell Biochem , vol.114 , pp. 1194-1202
    • Lund, S.A.1    Wilson, C.L.2    Raines, E.W.3    Tang, J.4    Giachelli, C.M.5    Scatena, M.6
  • 24
    • 84948441210 scopus 로고    scopus 로고
    • Osteopontin in immune-mediated diseases
    • Rittling SR, Singh R. Osteopontin in immune-mediated diseases. J Dent Res 2015; 94:1638–45.
    • (2015) J Dent Res , vol.94 , pp. 1638-1645
    • Rittling, S.R.1    Singh, R.2
  • 27
    • 0031836772 scopus 로고    scopus 로고
    • Mice lacking osteopontin show normal development and bone structure but display altered osteoclast formation in vitro
    • Rittling SR, Matsumoto HN, McKee MD, Nanci A, An XR, Novick KE et al. Mice lacking osteopontin show normal development and bone structure but display altered osteoclast formation in vitro. J Bone Miner Res 1998; 13:1101–11.
    • (1998) J Bone Miner Res , vol.13 , pp. 1101-1111
    • Rittling, S.R.1    Matsumoto, H.N.2    McKee, M.D.3    Nanci, A.4    An, X.R.5    Novick, K.E.6
  • 28
    • 0037251307 scopus 로고    scopus 로고
    • Novel murine mammary epithelial cell lines that form osteolytic bone metastases: effect of strain background on tumor homing
    • Chen Y, Rittling SR. Novel murine mammary epithelial cell lines that form osteolytic bone metastases: effect of strain background on tumor homing. Clin Exp Metastasis 2003; 20:111–20.
    • (2003) Clin Exp Metastasis , vol.20 , pp. 111-120
    • Chen, Y.1    Rittling, S.R.2
  • 30
    • 84895751609 scopus 로고    scopus 로고
    • Isolation, purification and labeling of mouse bone marrow neutrophils for functional studies and adoptive transfer experiments
    • Swamydas M, Lionakis MS. Isolation, purification and labeling of mouse bone marrow neutrophils for functional studies and adoptive transfer experiments. J Vis Exp 2013; 77:e50586.
    • (2013) J Vis Exp , vol.77
    • Swamydas, M.1    Lionakis, M.S.2
  • 32
    • 35649014332 scopus 로고    scopus 로고
    • Characterization of anti-osteopontin monoclonal antibodies: binding sensitivity to post-translational modifications
    • Kazanecki CC, Kowalski AJ, Ding T, Rittling SR, Denhardt DT. Characterization of anti-osteopontin monoclonal antibodies: binding sensitivity to post-translational modifications. J Cell Biochem 2007; 102:925–35.
    • (2007) J Cell Biochem , vol.102 , pp. 925-935
    • Kazanecki, C.C.1    Kowalski, A.J.2    Ding, T.3    Rittling, S.R.4    Denhardt, D.T.5
  • 33
    • 0032544465 scopus 로고    scopus 로고
    • Detection of mouse osteopontin by western blotting
    • Rittling SR, Feng F. Detection of mouse osteopontin by western blotting. Biochem Biophys Res Commun 1998; 250:287–92.
    • (1998) Biochem Biophys Res Commun , vol.250 , pp. 287-292
    • Rittling, S.R.1    Feng, F.2
  • 34
    • 0041766160 scopus 로고    scopus 로고
    • Air-pouch models of inflammation and modifications for the study of granuloma-mediated cartilage degradation
    • Colville-Nash P, Lawrence T. Air-pouch models of inflammation and modifications for the study of granuloma-mediated cartilage degradation. Methods Mol Biol 2003; 225:181–9.
    • (2003) Methods Mol Biol , vol.225 , pp. 181-189
    • Colville-Nash, P.1    Lawrence, T.2
  • 35
    • 70349773144 scopus 로고    scopus 로고
    • Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis
    • Sharif SA, Du X, Myles T, Song JJ, Price E, Lee DM et al. Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis. Arthritis Rheum 2009; 60:2902–12.
    • (2009) Arthritis Rheum , vol.60 , pp. 2902-2912
    • Sharif, S.A.1    Du, X.2    Myles, T.3    Song, J.J.4    Price, E.5    Lee, D.M.6
  • 36
    • 33748857158 scopus 로고    scopus 로고
    • Neutrophil infiltration and chemokines
    • Kobayashi Y. Neutrophil infiltration and chemokines. Crit Rev Immunol 2006; 26:307–16.
    • (2006) Crit Rev Immunol , vol.26 , pp. 307-316
    • Kobayashi, Y.1
  • 37
    • 67649336941 scopus 로고    scopus 로고
    • Polymeric osteopontin employs integrin α9β1 as a receptor and attracts neutrophils by presenting a de novo binding site
    • Nishimichi N, Higashikawa F, Kinoh HH, Tateishi Y, Matsuda H, Yokosaki Y. Polymeric osteopontin employs integrin α9β1 as a receptor and attracts neutrophils by presenting a de novo binding site. J Biol Chem 2009; 284:14769–76.
    • (2009) J Biol Chem , vol.284 , pp. 14769-14776
    • Nishimichi, N.1    Higashikawa, F.2    Kinoh, H.H.3    Tateishi, Y.4    Matsuda, H.5    Yokosaki, Y.6
  • 38
    • 53749092962 scopus 로고    scopus 로고
    • Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments
    • Caswell PT, Chan M, Lindsay AJ, McCaffrey MW, Boettiger D, Norman JC. Rab-coupling protein coordinates recycling of α5β1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J Cell Biol 2008; 183:143–55.
    • (2008) J Cell Biol , vol.183 , pp. 143-155
    • Caswell, P.T.1    Chan, M.2    Lindsay, A.J.3    McCaffrey, M.W.4    Boettiger, D.5    Norman, J.C.6
  • 39
    • 33644669749 scopus 로고    scopus 로고
    • Higher neutrophil infiltration mediated by osteopontin is a likely contributing factor to the increased susceptibility of females to alcoholic liver disease
    • Banerjee A, Apte UM, Smith R, Ramaiah SK. Higher neutrophil infiltration mediated by osteopontin is a likely contributing factor to the increased susceptibility of females to alcoholic liver disease. J Pathol 2006; 208:473–85.
    • (2006) J Pathol , vol.208 , pp. 473-485
    • Banerjee, A.1    Apte, U.M.2    Smith, R.3    Ramaiah, S.K.4
  • 40
    • 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 DK, Mackie EJ, Pagel CN. 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
  • 41
    • 84924258751 scopus 로고    scopus 로고
    • Neutralization of osteopontin attenuates neutrophil migration in sepsis-induced acute lung injury
    • Hirano Y, Aziz M, Yang WL, Wang Z, Zhou M, Ochani M et al. Neutralization of osteopontin attenuates neutrophil migration in sepsis-induced acute lung injury. Crit Care 2015; 19:53.
    • (2015) Crit Care , vol.19 , pp. 53
    • Hirano, Y.1    Aziz, M.2    Yang, W.L.3    Wang, Z.4    Zhou, M.5    Ochani, M.6
  • 43
    • 84948441210 scopus 로고    scopus 로고
    • Osteopontin in immune-mediated diseases
    • Rittling SR, Singh R. Osteopontin in immune-mediated diseases. J Dent Res 2015; 94:1638–45.
    • (2015) J Dent Res , vol.94 , pp. 1638-1645
    • Rittling, S.R.1    Singh, R.2
  • 44
    • 84921813332 scopus 로고    scopus 로고
    • The multifactorial role of neutrophils in rheumatoid arthritis
    • Wright HL, Moots RJ, Edwards SW. The multifactorial role of neutrophils in rheumatoid arthritis. Nat Rev Rheumatol 2014; 10:593–601.
    • (2014) Nat Rev Rheumatol , vol.10 , pp. 593-601
    • Wright, H.L.1    Moots, R.J.2    Edwards, S.W.3
  • 45
    • 23044454592 scopus 로고    scopus 로고
    • Role of osteopontin in hepatic neutrophil infiltration during alcoholic steatohepatitis
    • Apte UM, Banerjee A, McRee R, Wellberg E, Ramaiah SK. Role of osteopontin in hepatic neutrophil infiltration during alcoholic steatohepatitis. Toxicol Appl Pharmacol 2005; 207:25–38.
    • (2005) Toxicol Appl Pharmacol , vol.207 , pp. 25-38
    • Apte, U.M.1    Banerjee, A.2    McRee, R.3    Wellberg, E.4    Ramaiah, S.K.5
  • 46
    • 0028986791 scopus 로고
    • Calcium suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αvβ3
    • Hu DD, Hoyer JR, Smith JW. Calcium suppresses cell adhesion to osteopontin by attenuating binding affinity for integrin αvβ3. J Biol Chem 1995; 270:9917–25.
    • (1995) J Biol Chem , vol.270 , pp. 9917-9925
    • Hu, D.D.1    Hoyer, J.R.2    Smith, J.W.3
  • 47
    • 0033583322 scopus 로고    scopus 로고
    • The integrin α9β1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1
    • Taooka Y, Chen J, Yednock T, Sheppard D. The integrin α9β1 mediates adhesion to activated endothelial cells and transendothelial neutrophil migration through interaction with vascular cell adhesion molecule-1. J Cell Biol 1999; 145:413–20.
    • (1999) J Cell Biol , vol.145 , pp. 413-420
    • Taooka, Y.1    Chen, J.2    Yednock, T.3    Sheppard, D.4
  • 49
    • 84874240557 scopus 로고    scopus 로고
    • Aspects of VLA-4 and LFA-1 regulation that may contribute to rolling and firm adhesion
    • Chigaev A, Sklar LA. Aspects of VLA-4 and LFA-1 regulation that may contribute to rolling and firm adhesion. Front Immunol 2012; 3:242.
    • (2012) Front Immunol , vol.3 , pp. 242
    • Chigaev, A.1    Sklar, L.A.2
  • 50
    • 84922735977 scopus 로고    scopus 로고
    • Osteopontin binding to the alpha 4 integrin requires highest affinity integrin conformation, but is independent of post-translational modifications of osteopontin
    • Hui T, Sorensen ES, Rittling SR. Osteopontin binding to the alpha 4 integrin requires highest affinity integrin conformation, but is independent of post-translational modifications of osteopontin. Matrix Biol 2015; 41:19–25.
    • (2015) Matrix Biol , vol.41 , pp. 19-25
    • Hui, T.1    Sorensen, E.S.2    Rittling, S.R.3
  • 52
    • 0037088640 scopus 로고    scopus 로고
    • Tumor-derived osteopontin is soluble, not matrix associated
    • Rittling SR, Chen Y, Feng F, Wu Y. Tumor-derived osteopontin is soluble, not matrix associated. J Biol Chem 2002; 277:9175–82.
    • (2002) J Biol Chem , vol.277 , pp. 9175-9182
    • Rittling, S.R.1    Chen, Y.2    Feng, F.3    Wu, Y.4
  • 54
    • 0032562614 scopus 로고    scopus 로고
    • Identification of a potent, selective non-peptide CXCR2 antagonist that inhibits interleukin-8-induced neutrophil migration
    • White JR, Lee JM, Young PR, Hertzberg RP, Jurewicz AJ, Chaikin MA et al. Identification of a potent, selective non-peptide CXCR2 antagonist that inhibits interleukin-8-induced neutrophil migration. J Biol Chem 1998; 273:10095–8.
    • (1998) J Biol Chem , vol.273 , pp. 10095-10098
    • White, J.R.1    Lee, J.M.2    Young, P.R.3    Hertzberg, R.P.4    Jurewicz, A.J.5    Chaikin, M.A.6
  • 55
    • 84866149276 scopus 로고    scopus 로고
    • The chemokine receptors CXCR1 and CXCR2 couple to distinct G protein-coupled receptor kinases to mediate and regulate leukocyte functions
    • Raghuwanshi SK, Su Y, Singh V, Haynes K, Richmond A, Richardson RM. The chemokine receptors CXCR1 and CXCR2 couple to distinct G protein-coupled receptor kinases to mediate and regulate leukocyte functions. J Immunol 2012; 189:2824–32.
    • (2012) J Immunol , vol.189 , pp. 2824-2832
    • Raghuwanshi, S.K.1    Su, Y.2    Singh, V.3    Haynes, K.4    Richmond, A.5    Richardson, R.M.6
  • 56
    • 84896523366 scopus 로고    scopus 로고
    • G Protein-coupled receptor kinase-6 interacts with activator of G protein signaling-3 to regulate CXCR2-mediated cellular functions
    • Singh V, Raghuwanshi SK, Smith N, Rivers EJ, Richardson RM. G Protein-coupled receptor kinase-6 interacts with activator of G protein signaling-3 to regulate CXCR2-mediated cellular functions. J Immunol 2014; 192:2186–94.
    • (2014) J Immunol , vol.192 , pp. 2186-2194
    • Singh, V.1    Raghuwanshi, S.K.2    Smith, N.3    Rivers, E.J.4    Richardson, R.M.5
  • 57
    • 84890235263 scopus 로고    scopus 로고
    • Endocytic trafficking of chemokine receptors
    • Marchese A. Endocytic trafficking of chemokine receptors. Curr Opin Cell Biol 2014; 27:72–7.
    • (2014) Curr Opin Cell Biol , vol.27 , pp. 72-77
    • Marchese, A.1
  • 58


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