메뉴 건너뛰기




Volumn 113, Issue 10, 2009, Pages 2363-2369

Degradation of soluble VEGF receptor-1 by MMP-7 allows VEGF access to endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

MATRILYSIN; SOLUBLE VASCULOTROPIN RECEPTOR 1; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN RECEPTOR 1; VASCULOTROPIN RECEPTOR 2;

EID: 63849229054     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2008-08-172742     Document Type: Article
Times cited : (84)

References (45)
  • 1
    • 0037699954 scopus 로고    scopus 로고
    • The biology of VEGF and its receptors
    • Ferrara N, Gerber HP, LeCouter J. The biology of VEGF and its receptors. Nat Med. 2003;9:669-676.
    • (2003) Nat Med , vol.9 , pp. 669-676
    • Ferrara, N.1    Gerber, H.P.2    LeCouter, J.3
  • 2
    • 25144511910 scopus 로고    scopus 로고
    • The vascular endothelial growth factor (VEGF)/VEGF receptor system and its role under physiological and pathological conditions
    • Takahashi H, Shibuya M. The vascular endothelial growth factor (VEGF)/VEGF receptor system and its role under physiological and pathological conditions. Clin Sci (Lond). 2005;109:227-241.
    • (2005) Clin Sci (Lond) , vol.109 , pp. 227-241
    • Takahashi, H.1    Shibuya, M.2
  • 3
    • 0030576517 scopus 로고    scopus 로고
    • Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis
    • Hanahan D, Folkman J. Patterns and emerging mechanisms of the angiogenic switch during tumorigenesis. Cell. 1996;86:353-364.
    • (1996) Cell , vol.86 , pp. 353-364
    • Hanahan, D.1    Folkman, J.2
  • 4
    • 0035060498 scopus 로고    scopus 로고
    • Pitfalls in the measurement of circulating vascular endothelial growth factor
    • Jelkmann W. Pitfalls in the measurement of circulating vascular endothelial growth factor. Clin Chem. 2001;47:617-623.
    • (2001) Clin Chem , vol.47 , pp. 617-623
    • Jelkmann, W.1
  • 5
    • 0036481769 scopus 로고    scopus 로고
    • Connective tissue growth factor binds vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis
    • Inoki I, Shiomi T, Hashimoto G, et al. Connective tissue growth factor binds vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis. FASEB J. 2002;16:219-221.
    • (2002) FASEB J , vol.16 , pp. 219-221
    • Inoki, I.1    Shiomi, T.2    Hashimoto, G.3
  • 6
    • 0027421333 scopus 로고
    • Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor
    • Kendall RL, Thomas KA. Inhibition of vascular endothelial cell growth factor activity by an endogenously encoded soluble receptor. Proc Natl Acad Sci U S A. 1993;90:10705-10709.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10705-10709
    • Kendall, R.L.1    Thomas, K.A.2
  • 7
    • 0029025873 scopus 로고
    • Platelet factor-4 inhibits the mitogenic activity of VEGF121 and VEGF165 using several concurrent mechanisms
    • Gengrinovitch S, Greenberg SM, Cohen T, et al. Platelet factor-4 inhibits the mitogenic activity of VEGF121 and VEGF165 using several concurrent mechanisms. J Biol Chem.1995;270:15059-15065.
    • (1995) J Biol Chem , vol.270 , pp. 15059-15065
    • Gengrinovitch, S.1    Greenberg, S.M.2    Cohen, T.3
  • 8
    • 0038109791 scopus 로고    scopus 로고
    • ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165
    • Luque A, Carpizo DR, Iruela-Arispe ML. ADAMTS1/METH1 inhibits endothelial cell proliferation by direct binding and sequestration of VEGF165. J Biol Chem. 2003;278:23656-23665.
    • (2003) J Biol Chem , vol.278 , pp. 23656-23665
    • Luque, A.1    Carpizo, D.R.2    Iruela-Arispe, M.L.3
  • 9
    • 0009849965 scopus 로고    scopus 로고
    • Binding and displacement of vascular endothelial growth factor (VEGF) by thrombospondin: Effect on human microvascular endothelial cell proliferation and angiogenesis
    • Gupta K, Gupta P, Wild R, Ramakrishnan S, Hebbel RP. Binding and displacement of vascular endothelial growth factor (VEGF) by thrombospondin: effect on human microvascular endothelial cell proliferation and angiogenesis. Angiogenesis. 1999;3:147-158.
    • (1999) Angiogenesis , vol.3 , pp. 147-158
    • Gupta, K.1    Gupta, P.2    Wild, R.3    Ramakrishnan, S.4    Hebbel, R.P.5
  • 10
    • 1642303371 scopus 로고    scopus 로고
    • Héroult M, Bernard-Pierrot l, Delbe J, et al. Heparin affin regulatory peptide binds to vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis. Oncogene. 2004;23:1745-1753.
    • Héroult M, Bernard-Pierrot l, Delbe J, et al. Heparin affin regulatory peptide binds to vascular endothelial growth factor (VEGF) and inhibits VEGF-induced angiogenesis. Oncogene. 2004;23:1745-1753.
  • 11
    • 33750430869 scopus 로고    scopus 로고
    • Corneal avascularity is due to soluble VEGF receptor-1
    • Ambati BK, Nozaki M, Singh N, et al. Corneal avascularity is due to soluble VEGF receptor-1. Nature. 2006;443:993-997.
    • (2006) Nature , vol.443 , pp. 993-997
    • Ambati, B.K.1    Nozaki, M.2    Singh, N.3
  • 12
    • 0037373006 scopus 로고    scopus 로고
    • Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia
    • Maynard SE, Min JY, Merchan J, et al. Excess placental soluble fms-like tyrosine kinase 1 (sFlt1) may contribute to endothelial dysfunction, hypertension, and proteinuria in preeclampsia. J Clin Invest. 2003;111:649-658.
    • (2003) J Clin Invest , vol.111 , pp. 649-658
    • Maynard, S.E.1    Min, J.Y.2    Merchan, J.3
  • 13
    • 0031771617 scopus 로고    scopus 로고
    • Avascular endothelial growth factor antagonist is produced by the human placenta and released into the maternal circulation
    • Clark DE, Smith SK, He Y, et al. Avascular endothelial growth factor antagonist is produced by the human placenta and released into the maternal circulation. Biol Reprod. 1998;59:1540-1548.
    • (1998) Biol Reprod , vol.59 , pp. 1540-1548
    • Clark, D.E.1    Smith, S.K.2    He, Y.3
  • 14
    • 0030582384 scopus 로고    scopus 로고
    • Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR
    • Kendall RL, Wang G, Thomas KA. Identification of a natural soluble form of the vascular endothelial growth factor receptor, FLT-1, and its heterodimerization with KDR. Biochem Biophys Res Commun. 1996;226:324-328.
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 324-328
    • Kendall, R.L.1    Wang, G.2    Thomas, K.A.3
  • 15
    • 0042328366 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-1 is deposited in the extracellular matrix by endothelial cells and is a ligand for the alpha 5 beta 1 integrin
    • Orecchia A, Lacal PM, Schietroma C, Morea V, Zambruno G, Failla CM. Vascular endothelial growth factor receptor-1 is deposited in the extracellular matrix by endothelial cells and is a ligand for the alpha 5 beta 1 integrin. J Cell Sci. 2003;116:3479-3489.
    • (2003) J Cell Sci , vol.116 , pp. 3479-3489
    • Orecchia, A.1    Lacal, P.M.2    Schietroma, C.3    Morea, V.4    Zambruno, G.5    Failla, C.M.6
  • 16
    • 0034007818 scopus 로고    scopus 로고
    • Release and complex formation of soluble VEGFR-1 from endothelial cells and biological fluids
    • Hornig C, Barleon B, Ahmad S, Vuorela P, Ahmed A, Weich HA. Release and complex formation of soluble VEGFR-1 from endothelial cells and biological fluids. Lab Invest. 2000;80:443-454.
    • (2000) Lab Invest , vol.80 , pp. 443-454
    • Hornig, C.1    Barleon, B.2    Ahmad, S.3    Vuorela, P.4    Ahmed, A.5    Weich, H.A.6
  • 17
    • 33644545381 scopus 로고    scopus 로고
    • Tumour microenvironment-opinion: Validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy
    • Overall CM, Kleifeld O. Tumour microenvironment-opinion: validating matrix metalloproteinases as drug targets and anti-targets for cancer therapy. Nat Rev Cancer. 2006;6:227-239.
    • (2006) Nat Rev Cancer , vol.6 , pp. 227-239
    • Overall, C.M.1    Kleifeld, O.2
  • 18
    • 33344466450 scopus 로고    scopus 로고
    • Making the cut: Pro-tease-mediated regulation of angiogenesis
    • Roy R, Zhang B, Moses MA. Making the cut: pro-tease-mediated regulation of angiogenesis. Exp Cell Res. 2006;312:608-622.
    • (2006) Exp Cell Res , vol.312 , pp. 608-622
    • Roy, R.1    Zhang, B.2    Moses, M.A.3
  • 19
    • 0036127647 scopus 로고    scopus 로고
    • MMPs in the eye: Emerging roles for matrix metalloproteinases in ocular physiology
    • Sivak JM, Fini ME. MMPs in the eye: emerging roles for matrix metalloproteinases in ocular physiology. Prog Retin Eye Res. 2002;21:1-14.
    • (2002) Prog Retin Eye Res , vol.21 , pp. 1-14
    • Sivak, J.M.1    Fini, M.E.2
  • 20
    • 33846785537 scopus 로고    scopus 로고
    • Matrix met-alloproteinases in lung: Multiple, multifarious, and multifaceted
    • Greenlee KJ, Werb Z, Kheradmand F. Matrix met-alloproteinases in lung: multiple, multifarious, and multifaceted. Physiol Rev. 2007;87:69-98.
    • (2007) Physiol Rev , vol.87 , pp. 69-98
    • Greenlee, K.J.1    Werb, Z.2    Kheradmand, F.3
  • 22
    • 37349082926 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease
    • Raffetto JD, Khalil RA. Matrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease. Biochem Pharmacol. 2008;75:346-359.
    • (2008) Biochem Pharmacol , vol.75 , pp. 346-359
    • Raffetto, J.D.1    Khalil, R.A.2
  • 23
    • 0041352075 scopus 로고    scopus 로고
    • The matrix metalloproteinase system: Changes, regulation, and impact throughout the ovarian and uterine reproductive cycle
    • Curry TE, Jr., Osteen KG. The matrix metalloproteinase system: changes, regulation, and impact throughout the ovarian and uterine reproductive cycle. Endocr Rev. 2003;24:428-465.
    • (2003) Endocr Rev , vol.24 , pp. 428-465
    • Curry Jr., T.E.1    Osteen, K.G.2
  • 24
    • 0000391746 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis
    • Bergers G, Brekken R, McMahon G, et al. Matrix metalloproteinase-9 triggers the angiogenic switch during carcinogenesis. Nat Cell Biol. 2000;2:737-744.
    • (2000) Nat Cell Biol , vol.2 , pp. 737-744
    • Bergers, G.1    Brekken, R.2    McMahon, G.3
  • 25
    • 33645744014 scopus 로고    scopus 로고
    • Role of matrix metalloproteinases in delayed cortical responses after stroke
    • Zhao BQ, Wang S, Kim HY, et al. Role of matrix metalloproteinases in delayed cortical responses after stroke. Nat Med. 2006;12:441-445.
    • (2006) Nat Med , vol.12 , pp. 441-445
    • Zhao, B.Q.1    Wang, S.2    Kim, H.Y.3
  • 26
    • 44849137555 scopus 로고    scopus 로고
    • Gene transfer of matrix metalloproteinase-9 induces tumor regression of breast cancer in vivo
    • Bendrik C, Robertson J, Gauldie J, Dabrosin C. Gene transfer of matrix metalloproteinase-9 induces tumor regression of breast cancer in vivo. Cancer Res. 2008;68:3405-3412.
    • (2008) Cancer Res , vol.68 , pp. 3405-3412
    • Bendrik, C.1    Robertson, J.2    Gauldie, J.3    Dabrosin, C.4
  • 27
    • 22344437713 scopus 로고    scopus 로고
    • Processing of VEGF-Aby matrix metalloproteinases regulates bioavailability and vascular patterning in tumors
    • Lee S, Jilani SM, Nikolova GV, Carpizo D, Iruela-Arispe ML. Processing of VEGF-Aby matrix metalloproteinases regulates bioavailability and vascular patterning in tumors. J Cell Biol. 2005;169:681-691.
    • (2005) J Cell Biol , vol.169 , pp. 681-691
    • Lee, S.1    Jilani, S.M.2    Nikolova, G.V.3    Carpizo, D.4    Iruela-Arispe, M.L.5
  • 28
    • 0037183997 scopus 로고    scopus 로고
    • Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165
    • Hashimoto G, Inoki I, Fujii Y, Aoki T, Ikeda E, Okada Y. Matrix metalloproteinases cleave connective tissue growth factor and reactivate angiogenic activity of vascular endothelial growth factor 165. J Biol Chem. 2002;277:36288-36295.
    • (2002) J Biol Chem , vol.277 , pp. 36288-36295
    • Hashimoto, G.1    Inoki, I.2    Fujii, Y.3    Aoki, T.4    Ikeda, E.5    Okada, Y.6
  • 29
    • 0029937679 scopus 로고    scopus 로고
    • The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency
    • Keyt BA, Berleau LT, Nguyen HV, et al. The carboxyl-terminal domain (111-165) of vascular endothelial growth factor is critical for its mitogenic potency. J Biol Chem. 1996;271:7788-7795.
    • (1996) J Biol Chem , vol.271 , pp. 7788-7795
    • Keyt, B.A.1    Berleau, L.T.2    Nguyen, H.V.3
  • 30
    • 37549068908 scopus 로고    scopus 로고
    • Identification of candidate angiogenic inhibitors processed by matrix metalloproteinase 2 (MMP-2) in cell-based proteomic screens: Disruption of vascular endothelial growth factor (VEGF)/ heparin affin regulatory peptide (pleiotrophin) and VEGF/Connective tissue growth factor angiogenic inhibitory complexes by MMP-2 proteolysis
    • Dean RA, Butler GS, Hamma-Kourbali Y, et al. Identification of candidate angiogenic inhibitors processed by matrix metalloproteinase 2 (MMP-2) in cell-based proteomic screens: disruption of vascular endothelial growth factor (VEGF)/ heparin affin regulatory peptide (pleiotrophin) and VEGF/Connective tissue growth factor angiogenic inhibitory complexes by MMP-2 proteolysis. Mol Cell Biol. 2007;27:8454-8465.
    • (2007) Mol Cell Biol , vol.27 , pp. 8454-8465
    • Dean, R.A.1    Butler, G.S.2    Hamma-Kourbali, Y.3
  • 31
    • 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
    • 31
    • 31.Van den Steen PE, 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
  • 32
    • 36048938981 scopus 로고    scopus 로고
    • The VEGF angiogenic switch of fibroblasts is regulated by MMP-7 from cancer cells
    • Ito TK, Ishii G, Chiba H, Ochiai A. The VEGF angiogenic switch of fibroblasts is regulated by MMP-7 from cancer cells. Oncogene. 2007;26:7194-7203.
    • (2007) Oncogene , vol.26 , pp. 7194-7203
    • Ito, T.K.1    Ishii, G.2    Chiba, H.3    Ochiai, A.4
  • 33
    • 20744457595 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 degrades all insulin-like growth factor binding proteins and facilitates insulin-like growth factor bioavailability
    • Nakamura M, Miyamoto S, Maeda H, et al. Matrix metalloproteinase-7 degrades all insulin-like growth factor binding proteins and facilitates insulin-like growth factor bioavailability. Biochem Biophys Res Commun. 2005;333:1011-1016.
    • (2005) Biochem Biophys Res Commun , vol.333 , pp. 1011-1016
    • Nakamura, M.1    Miyamoto, S.2    Maeda, H.3
  • 34
    • 9144232874 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7 facilitates insulin-like growth factor bioavailability through its proteinase activity on insulin-like growth factor binding protein 3
    • Miyamoto S, Yano K, Sugimoto S, et al. Matrix metalloproteinase-7 facilitates insulin-like growth factor bioavailability through its proteinase activity on insulin-like growth factor binding protein 3. Cancer Res. 2004;64:665-671.
    • (2004) Cancer Res , vol.64 , pp. 665-671
    • Miyamoto, S.1    Yano, K.2    Sugimoto, S.3
  • 35
    • 1942509392 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7): A new promising drug target in cancer and inflammation?
    • Wielockx B, Libert C, Wilson C. Matrilysin (matrix metalloproteinase-7): a new promising drug target in cancer and inflammation? Cytokine Growth Factor Rev. 2004;15:111-115.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 111-115
    • Wielockx, B.1    Libert, C.2    Wilson, C.3
  • 36
    • 0030630628 scopus 로고    scopus 로고
    • Matrix metalloproteinases as mediators of reproductive function
    • Hulboy DL, Rudolph LA, Matrisian LM. Matrix metalloproteinases as mediators of reproductive function. Mol Hum Reprod. 1997;3:27-45.
    • (1997) Mol Hum Reprod , vol.3 , pp. 27-45
    • Hulboy, D.L.1    Rudolph, L.A.2    Matrisian, L.M.3
  • 37
    • 0035865438 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human pancreatic adenocarcinomas: Clinicopathologic and prognostic significance of matrilysin expression
    • Yamamoto H, Itoh F, Iku S, et al. Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human pancreatic adenocarcinomas: clinicopathologic and prognostic significance of matrilysin expression. J Clin Oncol. 2001;19:1118-1127.
    • (2001) J Clin Oncol , vol.19 , pp. 1118-1127
    • Yamamoto, H.1    Itoh, F.2    Iku, S.3
  • 38
    • 0036233880 scopus 로고    scopus 로고
    • Prognostic significance of matrix metalloproteinase-7 (MMP-7) expression at the invasive front in gastric carcinoma
    • Liu XP, Kawauchi S, Oga A, et al. Prognostic significance of matrix metalloproteinase-7 (MMP-7) expression at the invasive front in gastric carcinoma. Jpn J Cancer Res. 2002;93:291-295.
    • (2002) Jpn J Cancer Res , vol.93 , pp. 291-295
    • Liu, X.P.1    Kawauchi, S.2    Oga, A.3
  • 39
    • 0036142231 scopus 로고    scopus 로고
    • Oncogenic beta-catenin and MMP-7 (matrilysin) cosegregate in late-stage clinical colon cancer
    • OugolkovAV, YamashitaK, Mai M, Minamoto T. Oncogenic beta-catenin and MMP-7 (matrilysin) cosegregate in late-stage clinical colon cancer. Gastroenterology. 2002;122:60-71.
    • (2002) Gastroenterology , vol.122 , pp. 60-71
    • Ougolkov, A.V.1    Yamashita, K.2    Mai, M.3    Minamoto, T.4
  • 40
    • 0030844495 scopus 로고    scopus 로고
    • Expression of matrilysin in vascular endothelial cells adjacent to matrilysin-producing tumors
    • NagashimaY, HasegawaS, KoshikawaN, et al. Expression of matrilysin in vascular endothelial cells adjacent to matrilysin-producing tumors. Int J Cancer. 1997;72:441-445.
    • (1997) Int J Cancer , vol.72 , pp. 441-445
    • Nagashima, Y.1    Hasegawa, S.2    Koshikawa, N.3
  • 41
    • 40749120338 scopus 로고    scopus 로고
    • Endothelium specific matrilysin (MMP-7) expression in human cancers
    • Sier CF, Hawinkels LJ, Zijlmans HJ, et al. Endothelium specific matrilysin (MMP-7) expression in human cancers. Matrix Biol. 2008;27:267-271.
    • (2008) Matrix Biol , vol.27 , pp. 267-271
    • Sier, C.F.1    Hawinkels, L.J.2    Zijlmans, H.J.3
  • 42
    • 23844470235 scopus 로고    scopus 로고
    • A high peripheral microvessel density count correlates with a poor prognosis in pancreatic cancer
    • Takagi K, Takada T, Amano H. A high peripheral microvessel density count correlates with a poor prognosis in pancreatic cancer. J Gastroenterol. 2005;40:402-408.
    • (2005) J Gastroenterol , vol.40 , pp. 402-408
    • Takagi, K.1    Takada, T.2    Amano, H.3
  • 43
    • 0032868402 scopus 로고    scopus 로고
    • Relationships between vascularization and proliferation in invasive breast cancer
    • Beliën JA, van Diest PJ, Baak JP. Relationships between vascularization and proliferation in invasive breast cancer. J Pathol. 1999;189:309-318.
    • (1999) J Pathol , vol.189 , pp. 309-318
    • Beliën, J.A.1    van Diest, P.J.2    Baak, J.P.3
  • 44
    • 0343051765 scopus 로고    scopus 로고
    • In situ detection of matrix metalloproteinase-2 (MMP2) and the metalloproteinase inhibitor TIMP2 transcripts in human primary hepatocellular carcinoma and in liver metastasis
    • Musso O, Theret N, Campion JP, et al. In situ detection of matrix metalloproteinase-2 (MMP2) and the metalloproteinase inhibitor TIMP2 transcripts in human primary hepatocellular carcinoma and in liver metastasis. J Hepatol. 1997;26:593-605.
    • (1997) J Hepatol , vol.26 , pp. 593-605
    • Musso, O.1    Theret, N.2    Campion, J.P.3
  • 45
    • 34249744576 scopus 로고    scopus 로고
    • Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells
    • Yana I, Sagara H, Takaki S, et al. Crosstalk between neovessels and mural cells directs the site-specific expression of MT1-MMP to endothelial tip cells. J Cell Sci. 2007;120:1607-1614.
    • (2007) J Cell Sci , vol.120 , pp. 1607-1614
    • Yana, I.1    Sagara, H.2    Takaki, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.