메뉴 건너뛰기




Volumn 5, Issue 4, 2013, Pages 389-398

Synergistic protection of MLC 1 against cardiac ischemia/reperfusion- induced degradation: A novel therapeutic concept for the future

Author keywords

[No Author keywords available]

Indexed keywords

5 ETHOXYMETHOXY N HYDROXY 2 METHYL 4 (4 PHENOXYBENZAMIDO)PENTANAMIDE; BATIMASTAT; CONTRACTILE PROTEIN; DOXYCYCLINE; GELATINASE A; GELATINASE B; ILOMASTAT; MARIMASTAT; MLC1 PROTEIN; PD 166793; TETRACYCLINE; UNCLASSIFIED DRUG;

EID: 84875157276     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.19     Document Type: Review
Times cited : (9)

References (93)
  • 1
    • 10944239058 scopus 로고    scopus 로고
    • ACC/AHA guidelines for the management of patients with ST-elevation myocardial infarction: A report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines (Committee to Revise the 1999 Guidelines for the Management of Patients with Acute Myocardial Infarction)
    • Antman EM, Anbe DT, Armstrong PW et al. ACC/AHA guidelines for the management of patients with ST-elevation myocardial infarction: a report of the American College of Cardiology/American Heart Association Task Force on Practice Guidelines (Committee to Revise the 1999 Guidelines for the Management of Patients with Acute Myocardial Infarction). Circulation 110 (9), e82-e292 (2004).
    • (2004) Circulation , vol.110 , Issue.9
    • Antman, E.M.1    Anbe, D.T.2    Armstrong, P.W.3
  • 2
    • 84862507917 scopus 로고    scopus 로고
    • Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2
    • Cadete VJ, Sawicka J, Jaswal JS et al. Ischemia/reperfusion-induced myosin light chain 1 phosphorylation increases its degradation by matrix metalloproteinase 2. FEBS J. 279(13), 2444-2454 (2012).
    • (2012) FEBS J. , vol.279 , Issue.13 , pp. 2444-2454
    • Cadete, V.J.1    Sawicka, J.2    Jaswal, J.S.3
  • 3
    • 78649631500 scopus 로고    scopus 로고
    • Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction
    • Doroszko A, Polewicz D, Cadete VJ et al. Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction. Shock 34(6), 592-600 (2010).
    • (2010) Shock , vol.34 , Issue.6 , pp. 592-600
    • Doroszko, A.1    Polewicz, D.2    Cadete, V.J.3
  • 4
    • 70349652283 scopus 로고    scopus 로고
    • Cardiac dysfunction in an animal model of neonatal asphyxia is associated with increased degradation of MLC1 by MMP-2
    • Doroszko A, Polewicz D, Sawicka J et al. Cardiac dysfunction in an animal model of neonatal asphyxia is associated with increased degradation of MLC1 by MMP-2. Basic Res. Cardiol. 104(6), 669-679 (2009).
    • (2009) Basic Res. Cardiol. , vol.104 , Issue.6 , pp. 669-679
    • Doroszko, A.1    Polewicz, D.2    Sawicka, J.3
  • 5
    • 0035860834 scopus 로고    scopus 로고
    • Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1
    • Arrell DK, Neverova I, Fraser H, Marban E, Van Eyk JE. Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1. Circ. Res. 89(6), 480-487 (2001).
    • (2001) Circ. Res. , vol.89 , Issue.6 , pp. 480-487
    • Arrell, D.K.1    Neverova, I.2    Fraser, H.3    Marban, E.4    Van Eyk, J.E.5
  • 6
    • 84155164866 scopus 로고    scopus 로고
    • Early measurements of plasma matrix metalloproteinase-2 predict infarct size and ventricular dysfunction in ST-elevation myocardial infarction
    • Nilsson L, Hallen J, Atar D, Jonasson L, Swahn E. Early measurements of plasma matrix metalloproteinase-2 predict infarct size and ventricular dysfunction in ST-elevation myocardial infarction. Heart 98(1), 31-36 (2012).
    • (2012) Heart , vol.98 , Issue.1 , pp. 31-36
    • Nilsson, L.1    Hallen, J.2    Atar, D.3    Jonasson, L.4    Swahn, E.5
  • 7
    • 0014945041 scopus 로고
    • Three-dimensional reconstruction of F-Actin, thin flaments and decorated thin flaments
    • Moore PB, Huxley HE, Derosier DJ. Three-dimensional reconstruction of F-Actin, thin flaments and decorated thin flaments. J. Mol. Biol. 50(2), 279-295 (1970).
    • (1970) J. Mol. Biol. , vol.50 , Issue.2 , pp. 279-295
    • Moore, P.B.1    Huxley, H.E.2    Derosier, D.J.3
  • 8
    • 0027279669 scopus 로고
    • Molecular muscle
    • Taylor EW. Molecular muscle. Science 261(5117), 35-36 (1993).
    • (1993) Science , vol.261 , Issue.5117 , pp. 35-36
    • Taylor, E.W.1
  • 9
    • 0015914687 scopus 로고
    • Substructure of the myosin molecule. i V. Interactions of myosin and its subfragments with adenosine triphosphate and F-Actin
    • Margossian SS, Lowey S. Substructure of the myosin molecule. I V. Interactions of myosin and its subfragments with adenosine triphosphate and F-Actin. J. Mol. Biol. 74 (3), 313-330 (1973).
    • (1973) J. Mol. Biol. , vol.74 , Issue.3 , pp. 313-330
    • Margossian, S.S.1    Lowey, S.2
  • 10
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I, Holden HM, Whittaker M et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science 261(5117), 58-65 (1993).
    • (1993) Science , vol.261 , Issue.5117 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3
  • 11
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction; Interference microscopy of living muscle fbers
    • Huxley A F, Niedergerke R. Structural changes in muscle during contraction; interference microscopy of living muscle fbers. Nature 173(4412), 971-973 (1954).
    • (1954) Nature , vol.173 , Issue.4412 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 13
    • 49549162361 scopus 로고
    • Substructure of the myosin molecule. 3. Preparation of single-headed derivatives of myosin
    • Margossian SS, Lowey S. Substructure of the myosin molecule. 3. Preparation of single-headed derivatives of myosin. J. Mol. Biol. 74(3), 301-311 (1973).
    • (1973) J. Mol. Biol. , vol.74 , Issue.3 , pp. 301-311
    • Margossian, S.S.1    Lowey, S.2
  • 14
    • 0018789449 scopus 로고
    • The limited tryptic cleavage of chymotryptic S-1: An approach to the characterization of the actin site in myosin heads
    • Mornet D, Pantel P, Audemard E, Kassab R. The limited tryptic cleavage of chymotryptic S-1: an approach to the characterization of the actin site in myosin heads. Biochem. Biophys. Res. Commun. 89(3), 925-932 (1979).
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , Issue.3 , pp. 925-932
    • Mornet, D.1    Pantel, P.2    Audemard, E.3    Kassab, R.4
  • 15
    • 0027194702 scopus 로고
    • Three-dimensional structure of myosin subfragment-1: A molecular motor
    • Rayment I, Rypniewski WR, Schmidt-Base K et al. Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 261(5117), 50-58 (1993).
    • (1993) Science , vol.261 , Issue.5117 , pp. 50-58
    • Rayment, I.1    Rypniewski, W.R.2    Schmidt-Base, K.3
  • 17
    • 17044378603 scopus 로고    scopus 로고
    • Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems
    • White MY, Cordwell SJ, Mccarron HC et al. Proteomics of ischemia/reperfusion injury in rabbit myocardium reveals alterations to proteins of essential functional systems. Proteomics 5(5), 1395-1410 (2005).
    • (2005) Proteomics , vol.5 , Issue.5 , pp. 1395-1410
    • White, M.Y.1    Cordwell, S.J.2    McCarron, H.C.3
  • 18
    • 79957598460 scopus 로고    scopus 로고
    • Ischemia induced peroxynitrite dependent modifcations of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction
    • Polewicz D, Cadete VJ, Doroszko A et al. Ischemia induced peroxynitrite dependent modifcations of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction. J. Cell. Mol. Med. 15 (5), 1136-1147 (2011).
    • (2011) J. Cell. Mol. Med. , vol.15 , Issue.5 , pp. 1136-1147
    • Polewicz, D.1    Cadete, V.J.2    Doroszko, A.3
  • 19
    • 23044497564 scopus 로고    scopus 로고
    • Degradation of myosin light chain in isolated rat hearts subjected to ischemia-reperfusion injury: A new intracellular target for matrix metalloproteinase-2
    • Sawicki G, Leon H, Sawicka J et al. Degradation of myosin light chain in isolated rat hearts subjected to ischemia-reperfusion injury: a new intracellular target for matrix metalloproteinase-2. Circulation 112(4), 544-552 (2005).
    • (2005) Circulation , vol.112 , Issue.4 , pp. 544-552
    • Sawicki, G.1    Leon, H.2    Sawicka, J.3
  • 20
    • 0030444538 scopus 로고    scopus 로고
    • Muscle proteins-their actions and interactions
    • Holmes KC. Muscle proteins-their actions and interactions. Curr. Opin. Struct. Biol. 6(6), 781-789 (1996).
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , Issue.6 , pp. 781-789
    • Holmes, K.C.1
  • 21
    • 0013790350 scopus 로고
    • A new protein factor promoting aggregation of tropomyosin
    • Ebashi S, Kodama A. A new protein factor promoting aggregation of tropomyosin. J. Biochem. 58(1), 107-108 (1965).
    • (1965) J. Biochem. , vol.58 , Issue.1 , pp. 107-108
    • Ebashi, S.1    Kodama, A.2
  • 22
    • 84934435729 scopus 로고    scopus 로고
    • Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin
    • Murakami K, Yumoto F, Ohki SY et al. Structural basis for calcium-regulated relaxation of striated muscles at interaction sites of troponin with actin and tropomyosin. Adv. Exp. Med. Biol. 592, 71-86 (2007).
    • (2007) Adv. Exp. Med. Biol. , vol.592 , pp. 71-86
    • Murakami, K.1    Yumoto, F.2    Ohki, S.Y.3
  • 23
    • 0015218120 scopus 로고
    • Reconstitution of troponin activity from three protein components
    • Greaser ML, Gergely J. Reconstitution of troponin activity from three protein components. J. Biol. Chem. 246(13), 4226-4233 (1971).
    • (1971) J. Biol. Chem. , vol.246 , Issue.13 , pp. 4226-4233
    • Greaser, M.L.1    Gergely, J.2
  • 24
    • 84934440414 scopus 로고    scopus 로고
    • Tropomyosin and troponin cooperativity on the thin flament
    • Boussouf SE, Geeves M.A. Tropomyosin and troponin cooperativity on the thin flament. Adv. Exp. Med. Biol. 592, 99-109 (2007).
    • (2007) Adv. Exp. Med. Biol. , vol.592 , pp. 99-109
    • Boussouf, S.E.1    Geeves, M.A.2
  • 25
    • 33645064302 scopus 로고    scopus 로고
    • Partial replacement of cardiac troponin i with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation
    • Scruggs SB, Walker LA, Lyu T et al. Partial replacement of cardiac troponin I with a non-phosphorylatable mutant at serines 43/45 attenuates the contractile dysfunction associated with PKCepsilon phosphorylation. J. Mol. Cell. Cardiol. 40(4), 465-473 (2006).
    • (2006) J. Mol. Cell. Cardiol. , vol.40 , Issue.4 , pp. 465-473
    • Scruggs, S.B.1    Walker, L.A.2    Lyu, T.3
  • 26
    • 12244311161 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 mediates cytokine-induced myocardial contractile dysfunction
    • Gao CQ, Sawicki G, Suarez-Pinzon WL et al. Matrix metalloproteinase-2 mediates cytokine-induced myocardial contractile dysfunction. Cardiovasc. Res. 57(2), 426-433 (2003).
    • (2003) Cardiovasc. Res. , vol.57 , Issue.2 , pp. 426-433
    • Gao, C.Q.1    Sawicki, G.2    Suarez-Pinzon, W.L.3
  • 27
    • 0037126045 scopus 로고    scopus 로고
    • Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury
    • Wang W, Schulze CJ, Suarez-Pinzon WL et al. Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 106(12), 1543-1549 (2002).
    • (2002) Circulation , vol.106 , Issue.12 , pp. 1543-1549
    • Wang, W.1    Schulze, C.J.2    Suarez-Pinzon, W.L.3
  • 28
    • 4544291412 scopus 로고    scopus 로고
    • Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin i gene
    • Gomes AV, Potter JD. Cellular and molecular aspects of familial hypertrophic cardiomyopathy caused by mutations in the cardiac troponin I gene. Mol. Cell. Biochem. 263(1-2), 99-114 (2004).
    • (2004) Mol. Cell. Biochem. , vol.263 , Issue.1-2 , pp. 99-114
    • Gomes, A.V.1    Potter, J.D.2
  • 29
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier HL, Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94(3), 284-295 (2004).
    • (2004) Circ. Res. , vol.94 , Issue.3 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 31
    • 45349086526 scopus 로고    scopus 로고
    • Physiological functions of the giant elastic protein titin in mammalian striated muscle
    • Fukuda N, Granzier HL, Ishiwata S, Kurihara S. Physiological functions of the giant elastic protein titin in mammalian striated muscle. J. Physiol. Sci. 58 (3), 151-159 (2008).
    • (2008) J. Physiol. Sci. , vol.58 , Issue.3 , pp. 151-159
    • Fukuda, N.1    Granzier, H.L.2    Ishiwata, S.3    Kurihara, S.4
  • 32
    • 34250368734 scopus 로고    scopus 로고
    • Proteasome inhibition attenuates infarct size and preserves cardiac function in a murine model of myocardial ischemia-reperfusion injury
    • Stansfeld WE, Moss NC, Willis MS, Tang R, Selzman CH. Proteasome inhibition attenuates infarct size and preserves cardiac function in a murine model of myocardial ischemia-reperfusion injury. Ann. Thorac. Surg. 84(1), 120-125 (2007).
    • (2007) Ann. Thorac. Surg. , vol.84 , Issue.1 , pp. 120-125
    • Stansfeld, W.E.1    Moss, N.C.2    Willis, M.S.3    Tang, R.4    Selzman, C.H.5
  • 33
    • 0032923593 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of myocardial stunning
    • Bolli R, Marban E. Molecular and cellular mechanisms of myocardial stunning. Physiol. Rev. 79(2), 609-634 (1999).
    • (1999) Physiol. Rev. , vol.79 , Issue.2 , pp. 609-634
    • Bolli, R.1    Marban, E.2
  • 34
    • 78549277458 scopus 로고    scopus 로고
    • Titin is a target of matrix metalloproteinase-2: Implications in myocardial ischemia/reperfusion injury
    • Ali MA, Cho WJ, Hudson B et al. Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury. Circulation 122(20), 2039-2047 (2010).
    • (2010) Circulation , vol.122 , Issue.20 , pp. 2039-2047
    • Ali, M.A.1    Cho, W.J.2    Hudson, B.3
  • 35
    • 2542455498 scopus 로고    scopus 로고
    • Abnormal liver function tests in the symptomatic pregnant patient: The local experience in Singapore
    • Wong HY, Tan JY, Lim CC. Abnormal liver function tests in the symptomatic pregnant patient: the local experience in Singapore. Ann. Acad. Med. Singap. 33(2), 204-208 (2004).
    • (2004) Ann. Acad. Med. Singap. , vol.33 , Issue.2 , pp. 204-208
    • Wong, H.Y.1    Tan, J.Y.2    Lim, C.C.3
  • 36
    • 63049084664 scopus 로고    scopus 로고
    • PKC and MLCK-dependent, cytokine-induced rat coronary endothelial dysfunction
    • Tinsley JH, Hunter FA, Childs EW. PKC and MLCK-dependent, cytokine-induced rat coronary endothelial dysfunction. J. Surg. Res. 152(1), 76-83 (2009).
    • (2009) J. Surg. Res. , vol.152 , Issue.1 , pp. 76-83
    • Tinsley, J.H.1    Hunter, F.A.2    Childs, E.W.3
  • 37
    • 0035190054 scopus 로고    scopus 로고
    • Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction
    • Gao Y, Ye LH, Kishi H et al. Myosin light chain kinase as a multifunctional regulatory protein of smooth muscle contraction. IUBMB Life 51(6), 337-344 (2001).
    • (2001) IUBMB Life , vol.51 , Issue.6 , pp. 337-344
    • Gao, Y.1    Ye, L.H.2    Kishi, H.3
  • 38
    • 0029614896 scopus 로고
    • Myosin light chain phosphorylation in cardiac hypertrophy and failure due to myocardial infarction
    • Liu X, Shao Q, Dhalla NS. Myosin light chain phosphorylation in cardiac hypertrophy and failure due to myocardial infarction. J. Mol. Cell. Cardiol. 27(12), 2613-2621 (1995).
    • (1995) J. Mol. Cell. Cardiol. , vol.27 , Issue.12 , pp. 2613-2621
    • Liu, X.1    Shao, Q.2    Dhalla, N.S.3
  • 39
    • 0037076782 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation in neutrophil-stimulated coronary microvascular leakage
    • Yuan SY, Wu MH, Ustinova EE et al. Myosin light chain phosphorylation in neutrophil-stimulated coronary microvascular leakage. Circ. Res. 90(11), 1214-1221 (2002).
    • (2002) Circ. Res. , vol.90 , Issue.11 , pp. 1214-1221
    • Yuan, S.Y.1    Wu, M.H.2    Ustinova, E.E.3
  • 40
    • 84865532057 scopus 로고    scopus 로고
    • Effect of the myosin light chain kinase inhibitor ML-7 on the proteome of hearts subjected to ischemia-reperfusion inju r y
    • Lin HB, Cadete VJ, Sawicka J, Wozniak M, Sawicki G. Effect of the myosin light chain kinase inhibitor ML-7 on the proteome of hearts subjected to ischemia-reperfusion inju r y. J. Proteomics 75(17), 5386-5395 (2012).
    • (2012) J. Proteomics , vol.75 , Issue.17 , pp. 5386-5395
    • Lin, H.B.1    Cadete, V.J.2    Sawicka, J.3    Wozniak, M.4    Sawicki, G.5
  • 41
    • 0023915403 scopus 로고
    • K-252a, a novel microbial product, inhibits smooth muscle myosin light chain kinase
    • Nakanishi S, Yamada K, Kase H, Nakamura S, Nonomura Y. K-252a, a novel microbial product, inhibits smooth muscle myosin light chain kinase. J. Biol. Chem. 263(13), 6215-6219 (1988).
    • (1988) J. Biol. Chem. , vol.263 , Issue.13 , pp. 6215-6219
    • Nakanishi, S.1    Yamada, K.2    Kase, H.3    Nakamura, S.4    Nonomura, Y.5
  • 42
    • 0034328036 scopus 로고    scopus 로고
    • Candidate inhibitor of the volume-sensitive kinase regulating K-Cl cotransport: The myosin light chain kinase inhibitor ML-7
    • Kelley SJ, Thomas R, Dunham PB. Candidate inhibitor of the volume-sensitive kinase regulating K-Cl cotransport: the myosin light chain kinase inhibitor ML-7. J. Membr. Biol. 178(1), 31-41 (2000).
    • (2000) J. Membr. Biol. , vol.178 , Issue.1 , pp. 31-41
    • Kelley, S.J.1    Thomas, R.2    Dunham, P.B.3
  • 43
    • 0026409760 scopus 로고
    • Myosin light chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fbronectin substratum
    • Isemura M, Mita T, Satoh K, Narumi K, Motomiya M. Myosin light chain kinase inhibitors ML-7 and ML-9 inhibit mouse lung carcinoma cell attachment to the fbronectin substratum. Cell Biol. Int. Rep. 15(10), 965-972 (1991).
    • (1991) Cell Biol. Int. Rep. , vol.15 , Issue.10 , pp. 965-972
    • Isemura, M.1    Mita, T.2    Satoh, K.3    Narumi, K.4    Motomiya, M.5
  • 44
    • 12944279217 scopus 로고    scopus 로고
    • Role of MAP kinase and myosin light chain kinase in chromosome-induced development of mouse egg polarity
    • Deng M, Williams CJ, Schultz RM. Role of MAP kinase and myosin light chain kinase in chromosome-induced development of mouse egg polarity. Dev. Biol. 278(2), 358-366 (2005).
    • (2005) Dev. Biol. , vol.278 , Issue.2 , pp. 358-366
    • Deng, M.1    Williams, C.J.2    Schultz, R.M.3
  • 45
    • 75149195436 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase reduces brain edema formation after traumatic brain injury
    • Luh C, Kuhlmann CR, Ackermann B et al. Inhibition of myosin light chain kinase reduces brain edema formation after traumatic brain injury. J. Neurochem. 112 (4), 1015-1025 (2010).
    • (2010) J. Neurochem. , vol.112 , Issue.4 , pp. 1015-1025
    • Luh, C.1    Kuhlmann, C.R.2    Ackermann, B.3
  • 46
    • 20444431240 scopus 로고    scopus 로고
    • Effects of ML-7 and Y-27632 on carbachol-And endothelin-1-induced contraction of bovine trabecular meshwork
    • Rosenthal R, Choritz L, Schlott S et al. Effects of ML-7 and Y-27632 on carbachol-And endothelin-1-induced contraction of bovine trabecular meshwork. Exp. Eye Res. 80(6), 837-845 (2005).
    • (2005) Exp. Eye Res. , vol.80 , Issue.6 , pp. 837-845
    • Rosenthal, R.1    Choritz, L.2    Schlott, S.3
  • 47
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr. Matrix metalloproteinases. J. Biol. Chem. 274 (31), 21491-21494 (1999).
    • (1999) J. Biol. Chem. , vol.274 , Issue.31 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 48
    • 0028262145 scopus 로고
    • Expression of matrix metalloproteinase-2 and-9 during early human wound healing
    • Salo T, Makela M, Kylmaniemi M, Autio-Harmainen H, Larjava H. Expression of matrix metalloproteinase-2 and-9 during early human wound healing. Lab Invest. 70(2), 176-182 (1994).
    • (1994) Lab Invest. , vol.70 , Issue.2 , pp. 176-182
    • Salo, T.1    Makela, M.2    Kylmaniemi, M.3    Autio-Harmainen, H.4    Larjava, H.5
  • 49
    • 34447312482 scopus 로고    scopus 로고
    • Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth
    • Mosig RA, Dowling O, Difeo A et al. Loss of MMP-2 disrupts skeletal and craniofacial development and results in decreased bone mineralization, joint erosion and defects in osteoblast and osteoclast growth. Hum. Mol. Genet. 16 (9), 1113-1123 (2007).
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.9 , pp. 1113-1123
    • Mosig, R.A.1    Dowling, O.2    Difeo, A.3
  • 50
    • 0033134622 scopus 로고    scopus 로고
    • Matrix metalloproteinases in angiogenesis: A moving target for therapeutic intervention
    • Stetler-Stevenson WG. Matrix metalloproteinases in angiogenesis: a moving target for therapeutic intervention. J. Clin. Invest. 103(9), 1237-1241 (1999).
    • (1999) J. Clin. Invest. , vol.103 , Issue.9 , pp. 1237-1241
    • Stetler-Stevenson, W.G.1
  • 51
    • 47049095760 scopus 로고    scopus 로고
    • Elevated circulatory MMP-2 and MMP-9 levels and activities in patients with rheumatoid arthritis and systemic lupus erythematosus
    • Chang YH, Lin IL, Tsay GJ et al. Elevated circulatory MMP-2 and MMP-9 levels and activities in patients with rheumatoid arthritis and systemic lupus erythematosus. Clin. Biochem. 41(12), 955-959 (2008).
    • (2008) Clin. Biochem. , vol.41 , Issue.12 , pp. 955-959
    • Chang, Y.H.1    Lin, I.L.2    Tsay, G.J.3
  • 52
    • 61849164425 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 and matrix metalloproteinase-2 as biomarkers of various courses in multiple sclerosis
    • Benesova Y, Vasku A, Novotna H et al. Matrix metalloproteinase-9 and matrix metalloproteinase-2 as biomarkers of various courses in multiple sclerosis. Mult. Scler. 15(3), 316-322 (2009).
    • (2009) Mult. Scler. , vol.15 , Issue.3 , pp. 316-322
    • Benesova, Y.1    Vasku, A.2    Novotna, H.3
  • 53
    • 0032431941 scopus 로고    scopus 로고
    • Expression and role of matrix metalloproteinases MMP-2 and MMP-9 in human spinal column tumors
    • Gokaslan ZL, Chintala SK, York JE et al. Expression and role of matrix metalloproteinases MMP-2 and MMP-9 in human spinal column tumors. Clin. Exp. Metastasis 16(8), 721-728 (1998).
    • (1998) Clin. Exp. Metastasis , vol.16 , Issue.8 , pp. 721-728
    • Gokaslan, Z.L.1    Chintala, S.K.2    York, J.E.3
  • 54
    • 0035800880 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition after myocardial infarction: A new approach to prevent heart failure?
    • Creemers EE, Cleutjens JP, Smits JF, Daemen MJ. Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure? Circ. Res. 89(3), 201-210 (2001).
    • (2001) Circ. Res. , vol.89 , Issue.3 , pp. 201-210
    • Creemers, E.E.1    Cleutjens, J.P.2    Smits, J.F.3    Daemen, M.J.4
  • 55
    • 0028792509 scopus 로고
    • Matrix metalloproteinases and cardiovascular disease
    • Dollery CM, Mcewan JR, Henney AM. Matrix metalloproteinases and cardiovascular disease. Circ. Res. 77(5), 863-868 (1995).
    • (1995) Circ. Res. , vol.77 , Issue.5 , pp. 863-868
    • Dollery, C.M.1    McEwan, J.R.2    Henney, A.M.3
  • 56
    • 0034127659 scopus 로고    scopus 로고
    • Myocardial matrix degradation and metalloproteinase activation in the failing heart: A potential therapeutic target
    • Spinale FG, Coker ML, Bond BR, Zellner JL. Myocardial matrix degradation and metalloproteinase activation in the failing heart: a potential therapeutic target. Cardiovasc. Res. 46(2), 225-238 (2000).
    • (2000) Cardiovasc. Res. , vol.46 , Issue.2 , pp. 225-238
    • Spinale, F.G.1    Coker, M.L.2    Bond, B.R.3    Zellner, J.L.4
  • 57
    • 0034785723 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition and the prevention of heart failure
    • Lee RT. Matrix metalloproteinase inhibition and the prevention of heart failure. Trends Cardiovasc. Med. 11(5), 202-205 (2001).
    • (2001) Trends Cardiovasc. Med. , vol.11 , Issue.5 , pp. 202-205
    • Lee, R.T.1
  • 58
    • 77956784544 scopus 로고    scopus 로고
    • Intracellular substrate cleavage: A novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases
    • Cauwe B, Opdenakker G. Intracellular substrate cleavage: a novel dimension in the biochemistry, biology and pathology of matrix metalloproteinases. Crit. Rev. Biochem. Mol. Biol. 45(5), 351-423 (2010).
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , Issue.5 , pp. 351-423
    • Cauwe, B.1    Opdenakker, G.2
  • 59
    • 34548820960 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-Actinin in peroxynitrite mediated myocardial injury
    • Sung MM, Schulz CG, Wang W et al. Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-Actinin in peroxynitrite mediated myocardial injury. J. Mol. Cell. Cardiol. 43(4), 429-436 (2007).
    • (2007) J. Mol. Cell. Cardiol. , vol.43 , Issue.4 , pp. 429-436
    • Sung, M.M.1    Schulz, C.G.2    Wang, W.3
  • 60
    • 0034221875 scopus 로고    scopus 로고
    • Role of gelatinases MMP-2 and MMP-9 in tissue remodeling following acute lung injury
    • Corbel M, Boichot E, Lagente V. Role of gelatinases MMP-2 and MMP-9 in tissue remodeling following acute lung injury. Braz J. Med. Biol. Res. 33(7), 749-754 (2000).
    • (2000) Braz J. Med. Biol. Res. , vol.33 , Issue.7 , pp. 749-754
    • Corbel, M.1    Boichot, E.2    Lagente, V.3
  • 61
    • 84863257882 scopus 로고    scopus 로고
    • Vaporized perfuorocarbon confers protection against acute lung injury by inhibiting MMP-9 expression without protective effects in other organs
    • Han B, Zhao X, Huang X, Xie L. Vaporized perfuorocarbon confers protection against acute lung injury by inhibiting MMP-9 expression without protective effects in other organs. J. Int. Med. Res. 40(1), 115-125 (2012).
    • (2012) J. Int. Med. Res. , vol.40 , Issue.1 , pp. 115-125
    • Han, B.1    Zhao, X.2    Huang, X.3    Xie, L.4
  • 62
    • 77349121392 scopus 로고    scopus 로고
    • Effects of MMP-9 inhibition by doxycycline on proteome of lungs in high tidal volume mechanical ventilation-induced acute lung inju r y
    • Doroszko A, Hurst TS, Polewicz D et al. Effects of MMP-9 inhibition by doxycycline on proteome of lungs in high tidal volume mechanical ventilation-induced acute lung inju r y. Proteome Sci. 8, 3 (2010).
    • (2010) Proteome Sci. , vol.8 , Issue.3
    • Doroszko, A.1    Hurst, T.S.2    Polewicz, D.3
  • 63
    • 5444259378 scopus 로고    scopus 로고
    • Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and infammatory diseases
    • St-Pierre Y, Couillard J, Van Themsche C. Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and infammatory diseases. Expert Opin. Ther. Targets 8(5), 473-489 (2004).
    • (2004) Expert Opin. Ther. Targets , vol.8 , Issue.5 , pp. 473-489
    • St-Pierre, Y.1    Couillard, J.2    Van Themsche, C.3
  • 64
    • 33845910687 scopus 로고    scopus 로고
    • A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fbronectin or zinc binding domains
    • Martens E, Leyssen A, Van Aelst I et al. A monoclonal antibody inhibits gelatinase B/MMP-9 by selective binding to part of the catalytic domain and not to the fbronectin or zinc binding domains. Biochim. Biophys. Acta 1770(2), 178-186 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1770 , Issue.2 , pp. 178-186
    • Martens, E.1    Leyssen, A.2    Van Aelst, I.3
  • 65
    • 84055190462 scopus 로고    scopus 로고
    • Pioglitazone reduces peritoneal fbrosis via inhibition of TGF-beta, MMP-2, and MMP-9 in a model of encapsulating peritoneal sclerosis
    • Saglam F, Cavdar Z, Sarioglu S et al. Pioglitazone reduces peritoneal fbrosis via inhibition of TGF-beta, MMP-2, and MMP-9 in a model of encapsulating peritoneal sclerosis. Ren. Fail. 34(1), 95-102 (2012).
    • (2012) Ren. Fail. , vol.34 , Issue.1 , pp. 95-102
    • Saglam, F.1    Cavdar, Z.2    Sarioglu, S.3
  • 66
    • 83455245483 scopus 로고    scopus 로고
    • Plasma levels of matrix metalloproteinases and their inhibitors in hypertension: A systematic review and meta-Analysis
    • Marchesi C, Dentali F, Nicolini E et al. Plasma levels of matrix metalloproteinases and their inhibitors in hypertension: a systematic review and meta-Analysis. J. Hypertens. 30(1), 3-16 (2012).
    • (2012) J. Hypertens. , vol.30 , Issue.1 , pp. 3-16
    • Marchesi, C.1    Dentali, F.2    Nicolini, E.3
  • 67
    • 67349094937 scopus 로고    scopus 로고
    • Effects of doxycycline on serum and endometrial levels of MMP-2, MMP-9 and TIMP-1 in women using a levonorgestrel-releasing subcutaneous implant
    • Zhao S, Choksuchat C, Zhao Y et al. Effects of doxycycline on serum and endometrial levels of MMP-2, MMP-9 and TIMP-1 in women using a levonorgestrel-releasing subcutaneous implant. Contraception 79(6), 469-478 (2009).
    • (2009) Contraception , vol.79 , Issue.6 , pp. 469-478
    • Zhao, S.1    Choksuchat, C.2    Zhao, Y.3
  • 68
    • 21644489724 scopus 로고    scopus 로고
    • Dilating the degradome: Matrix metalloproteinase 2 (MMP-2) cuts to the heart of the matter
    • Overall CM. Dilating the degradome: matrix metalloproteinase 2 (MMP-2) cuts to the heart of the matter. Biochem J. 383(Pt 3), e5-e7 (2004).
    • (2004) Biochem J. , vol.383 , Issue.PART 3
    • Overall, C.M.1
  • 69
    • 5444259378 scopus 로고    scopus 로고
    • Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and infammatory diseases
    • St-Pierre Y, Couillard J, Van Themsche C. Regulation of MMP-9 gene expression for the development of novel molecular targets against cancer and infammatory diseases. Expert Opin. Ther. Targets 8(5), 473-489 (2004).
    • (2004) Expert Opin. Ther. Targets , vol.8 , Issue.5 , pp. 473-489
    • St-Pierre, Y.1    Couillard, J.2    Van Themsche, C.3
  • 70
    • 63849264551 scopus 로고    scopus 로고
    • Activation of MMP-2 as a key event in oxidative stress injury to the heart
    • Ali MA, Schulz R. Activation of MMP-2 as a key event in oxidative stress injury to the heart. Front. Biosci. 14, 699-716 (2009).
    • (2009) Front. Biosci. , vol.14 , pp. 699-716
    • Ali, M.A.1    Schulz, R.2
  • 71
    • 59749095843 scopus 로고    scopus 로고
    • Activation and modulation of 72 kDa matrix metalloproteinase-2 by peroxynitrite and glutathione
    • Viappiani S, Nicolescu AC, Holt A et al. Activation and modulation of 72 kDa matrix metalloproteinase-2 by peroxynitrite and glutathione. Biochem. Pharmacol. 77(5), 826-834 (2009).
    • (2009) Biochem. Pharmacol. , vol.77 , Issue.5 , pp. 826-834
    • Viappiani, S.1    Nicolescu, A.C.2    Holt, A.3
  • 72
    • 0036135119 scopus 로고    scopus 로고
    • Peroxynitrite-induced myocardial injury is mediated through matrix metalloproteinase-2
    • Wang W, Sawicki G, Schulz R. Peroxynitrite-induced myocardial injury is mediated through matrix metalloproteinase-2. Cardiovasc. Res. 53(1), 165-174 (2002).
    • (2002) Cardiovasc. Res. , vol.53 , Issue.1 , pp. 165-174
    • Wang, W.1    Sawicki, G.2    Schulz, R.3
  • 73
    • 34547815193 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation
    • Sariahmetoglu M, Crawford BD, Leon H et al. Regulation of matrix metalloproteinase-2 (MMP-2) activity by phosphorylation. FASEB J. 21(10), 2486-2495 (2007).
    • (2007) FASEB J. , vol.21 , Issue.10 , pp. 2486-2495
    • Sariahmetoglu, M.1    Crawford, B.D.2    Leon, H.3
  • 74
    • 77049113770 scopus 로고    scopus 로고
    • The tissue inhibitors of metalloproteinases (TIMPs): An ancient family with structural and functional diversit y
    • Brew K, Nagase H. The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversit y. Biochim. Biophys. Acta 1803(1), 55-71 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1803 , Issue.1 , pp. 55-71
    • Brew, K.1    Nagase, H.2
  • 75
    • 0036305443 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases and effect of MMP-inhibition in heart transplant related reperfusion injury
    • Falk V, Soccal PM, Grunenfelder J et al. Regulation of matrix metalloproteinases and effect of MMP-inhibition in heart transplant related reperfusion injury. Eur. J. Cardiothorac. Surg. 22(1), 53-58 (2002).
    • (2002) Eur. J. Cardiothorac. Surg. , vol.22 , Issue.1 , pp. 53-58
    • Falk, V.1    Soccal, P.M.2    Grunenfelder, J.3
  • 76
    • 31344456635 scopus 로고    scopus 로고
    • The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors
    • Peterson JT. The importance of estimating the therapeutic index in the development of matrix metalloproteinase inhibitors. Cardiovasc. Res. 69(3), 677-687 (2006).
    • (2006) Cardiovasc. Res. , vol.69 , Issue.3 , pp. 677-687
    • Peterson, J.T.1
  • 77
    • 0034814434 scopus 로고    scopus 로고
    • Topical synthetic inhibitor of matrix metalloproteinases delays epidermal regeneration of human wounds
    • Agren MS, Mirastschijski U, Karlsmark T, Saarialho-Kere UK. Topical synthetic inhibitor of matrix metalloproteinases delays epidermal regeneration of human wounds. Exp. Dermatol. 10(5), 337-348 (2001).
    • (2001) Exp. Dermatol. , vol.10 , Issue.5 , pp. 337-348
    • Agren, M.S.1    Mirastschijski, U.2    Karlsmark, T.3    Saarialho-Kere, U.K.4
  • 78
    • 0034681937 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 contributes to ischemia-reperfusion injury in the heart
    • Cheung PY, Sawicki G, Wozniak M et al. Matrix metalloproteinase-2 contributes to ischemia-reperfusion injury in the heart. Circulation 101(15), 1833-1839 (2000).
    • (2000) Circulation , vol.101 , Issue.15 , pp. 1833-1839
    • Cheung, P.Y.1    Sawicki, G.2    Wozniak, M.3
  • 79
    • 39449123099 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases prevents peroxynitrite-induced contractile dysfunction in the isolated cardiac myocyte
    • Leon H, Baczko I, Sawicki G, Light PE, Schulz R. Inhibition of matrix metalloproteinases prevents peroxynitrite-induced contractile dysfunction in the isolated cardiac myocyte. Br. J. Pharmacol. 153(4), 676-683 (2008).
    • (2008) Br. J. Pharmacol. , vol.153 , Issue.4 , pp. 676-683
    • Leon, H.1    Baczko, I.2    Sawicki, G.3    Light, P.E.4    Schulz, R.5
  • 80
    • 50249125886 scopus 로고    scopus 로고
    • Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effuent from isolated rat hearts during ischemia-reperfusion
    • Fert-Bober J, Leon H, Sawicka J et al. Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effuent from isolated rat hearts during ischemia-reperfusion. Basic Res. Cardiol. 103 (5), 431-443 (2008).
    • (2008) Basic Res. Cardiol. , vol.103 , Issue.5 , pp. 431-443
    • Fert-Bober, J.1    Leon, H.2    Sawicka, J.3
  • 81
    • 0032200444 scopus 로고    scopus 로고
    • Tetracyclines inhibit connective tissue breakdown by multiple non-Antimicrobial mechanisms
    • Golub LM, Lee HM, Ryan ME et al. Tetracyclines inhibit connective tissue breakdown by multiple non-Antimicrobial mechanisms. Adv. Dent. Res. 12(2), 12-26 (1998).
    • (1998) Adv. Dent. Res. , vol.12 , Issue.2 , pp. 12-26
    • Golub, L.M.1    Lee, H.M.2    Ryan, M.E.3
  • 82
    • 32444441006 scopus 로고    scopus 로고
    • Effect of matrix metalloproteinase inhibition by doxycycline on myocardial healing and remodeling after myocardial infarction
    • Tessone A, Feinberg MS, Barbash IM et al. Effect of matrix metalloproteinase inhibition by doxycycline on myocardial healing and remodeling after myocardial infarction. Cardiovasc. Drugs Ther. 19(6), 383-390 (2005).
    • (2005) Cardiovasc. Drugs Ther. , vol.19 , Issue.6 , pp. 383-390
    • Tessone, A.1    Feinberg, M.S.2    Barbash, I.M.3
  • 83
    • 77950356699 scopus 로고    scopus 로고
    • Electron paramagnetic resonance oximetry and redoximetry
    • He G. Electron paramagnetic resonance oximetry and redoximetry. Methods Mol. Biol. 594, 85-105 (2010).
    • (2010) Methods Mol. Biol. , vol.594 , pp. 85-105
    • He, G.1
  • 85
    • 84855372880 scopus 로고    scopus 로고
    • Infammation in myocardial diseases
    • Marchant DJ, Boyd JH, Lin DC et al. Infammation in myocardial diseases. Circ. Res. 110(1), 126-144 (2012).
    • (2012) Circ. Res. , vol.110 , Issue.1 , pp. 126-144
    • Marchant, D.J.1    Boyd, J.H.2    Lin, D.C.3
  • 86
    • 21244492310 scopus 로고    scopus 로고
    • Myocardial substrate metabolism in the normal and failing heart
    • Stanley WC, Recchia FA, Lopaschuk GD. Myocardial substrate metabolism in the normal and failing heart. Physiol. Rev. 85(3), 1093-1129 (2005).
    • (2005) Physiol. Rev. , vol.85 , Issue.3 , pp. 1093-1129
    • Stanley, W.C.1    Recchia, F.A.2    Lopaschuk, G.D.3
  • 87
    • 84860278698 scopus 로고    scopus 로고
    • Cell death and survival signaling in the cardiovascular system
    • Tucka J, Bennett M, Littlewood T. Cell death and survival signaling in the cardiovascular system. Front. Biosci. 17, 248-261 (2012).
    • (2012) Front. Biosci. , vol.17 , pp. 248-261
    • Tucka, J.1    Bennett, M.2    Littlewood, T.3
  • 88
    • 80051535614 scopus 로고    scopus 로고
    • How and when do myocytes die during ischemia and reperfusion: The late phase
    • Baines CP. How and when do myocytes die during ischemia and reperfusion: the late phase. J. Cardiovasc. Pharmacol. Ther. 16(3-4), 239-243 (2011).
    • (2011) J. Cardiovasc. Pharmacol. Ther. , vol.16 , Issue.3-4 , pp. 239-243
    • Baines, C.P.1
  • 89
    • 0033510439 scopus 로고    scopus 로고
    • Altered balance between matrix gelatinases (MMP-2 and MMP-9) and their tissue inhibitors in human dilated cardiomyopathy: Potential role of MMP-9 in myosin-heavy chain degradation
    • Rouet-Benzineb P, Buhler JM, Dreyfus P et al. Altered balance between matrix gelatinases (MMP-2 and MMP-9) and their tissue inhibitors in human dilated cardiomyopathy: potential role of MMP-9 in myosin-heavy chain degradation. Eur. J. Heart Fail. 1(4), 337-352 (1999).
    • (1999) Eur. J. Heart Fail. , vol.1 , Issue.4 , pp. 337-352
    • Rouet-Benzineb, P.1    Buhler, J.M.2    Dreyfus, P.3
  • 90
    • 3042771387 scopus 로고    scopus 로고
    • Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: Functional proteomics studies
    • Sawicki G, Jugdutt BI. Detection of regional changes in protein levels in the in vivo canine model of acute heart failure following ischemia-reperfusion injury: functional proteomics studies. Proteomics 4(7), 2195-2202 (2004).
    • (2004) Proteomics , vol.4 , Issue.7 , pp. 2195-2202
    • Sawicki, G.1    Jugdutt, B.I.2
  • 91
    • 77958086724 scopus 로고    scopus 로고
    • Cardiac functional improvement in rats with myocardial infarction by up-regulating cardiac myosin light chain kinase with neuregulin
    • Gu X, Liu X, Xu D et al. Cardiac functional improvement in rats with myocardial infarction by up-regulating cardiac myosin light chain kinase with neuregulin. Cardiovasc. Res. 88(2), 334-343 (2010).
    • (2010) Cardiovasc. Res. , vol.88 , Issue.2 , pp. 334-343
    • Gu, X.1    Liu, X.2    Xu, D.3
  • 92
    • 84867740025 scopus 로고    scopus 로고
    • Third universal defnition of myocardial infarction
    • Thygesen K, Alpert JS, Jaffe AS et al. Third universal defnition of myocardial infarction. Eur. Heart J. 33(20), 2551-2567 (2012).
    • (2012) Eur. Heart J. , vol.33 , Issue.20 , pp. 2551-2567
    • Thygesen, K.1    Alpert, J.S.2    Jaffe, A.S.3
  • 93
    • 34948891653 scopus 로고    scopus 로고
    • A cardiac myosin light chain kinase regulates sarcomere assembly in the vertebrate heart
    • Seguchi O, Takashima S, Yamazaki S et al. A cardiac myosin light chain kinase regulates sarcomere assembly in the vertebrate heart. J. Clin. Invest. 117(10), 2812-2824 (2007).
    • (2007) J. Clin. Invest. , vol.117 , Issue.10 , pp. 2812-2824
    • Seguchi, O.1    Takashima, S.2    Yamazaki, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.