메뉴 건너뛰기




Volumn 9, Issue 4, 2015, Pages

Tissue Localization and Extracellular Matrix Degradation by PI, PII and PIII Snake Venom Metalloproteinases: Clues on the Mechanisms of Venom-Induced Hemorrhage

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN TYPE 1; COLLAGEN TYPE 14; COLLAGEN TYPE 15; COLLAGEN TYPE 3; ENTACTIN; FIBRONECTIN; LUMICAN; METALLOPROTEINASE; P I METALLOPROTEINASE; P II METALLOPROTEINASE; P III METALLOPROTEINASE; SNAKE VENOM; SNAKE VENOM METALLOPROTEINASE; TENASCIN; THROMBOSPONDIN; UNCLASSIFIED DRUG; VITRONECTIN; HEMORRHAGIC METALLOPROTEINASE;

EID: 84929493856     PISSN: 19352727     EISSN: 19352735     Source Type: Journal    
DOI: 10.1371/journal.pntd.0003731     Document Type: Article
Times cited : (87)

References (41)
  • 1
    • 19544382337 scopus 로고    scopus 로고
    • Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases
    • Fox JW, Serrano SM, Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon. 2005; 45: 969–985. 15922769
    • (2005) Toxicon , vol.45 , pp. 969-985
    • Fox, J.W.1    Serrano, S.M.2
  • 2
    • 84863779320 scopus 로고    scopus 로고
    • On the ancestral recruitment of metalloproteinases into the venom of snakes
    • Casewell NR, On the ancestral recruitment of metalloproteinases into the venom of snakes. Toxicon. 2012; 60: 449–454. doi: 10.1016/j.toxicon.2012.02.006 22406471
    • (2012) Toxicon , vol.60 , pp. 449-454
    • Casewell, N.R.1
  • 3
    • 39749125478 scopus 로고    scopus 로고
    • Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia)
    • Fry BG, Scheib H, van der Weerd L, Young B, McNaughtan J, Ramjan SF, et al. Evolution of an arsenal: structural and functional diversification of the venom system in the advanced snakes (Caenophidia). Mol Cell Proteomics. 2008; 7: 215–246. 17855442
    • (2008) Mol Cell Proteomics , vol.7 , pp. 215-246
    • Fry, B.G.1    Scheib, H.2    van der Weerd, L.3    Young, B.4    McNaughtan, J.5    Ramjan, S.F.6
  • 4
    • 0029814973 scopus 로고    scopus 로고
    • Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution
    • Moura-da-Silva AM, Theakston RD, Crampton JM, Evolution of disintegrin cysteine-rich and mammalian matrix-degrading metalloproteinases: gene duplication and divergence of a common ancestor rather than convergent evolution. J Mol Evol. 1996; 43: 263–269. 8703092
    • (1996) J Mol Evol , vol.43 , pp. 263-269
    • Moura-da-Silva, A.M.1    Theakston, R.D.2    Crampton, J.M.3
  • 5
    • 79960307199 scopus 로고    scopus 로고
    • Domain loss facilitates accelerated evolution and neofunctionalization of duplicate snake venom metalloproteinase toxin genes
    • Casewell NR, Wagstaff SC, Harrison RA, Renjifo C, Wüster W, Domain loss facilitates accelerated evolution and neofunctionalization of duplicate snake venom metalloproteinase toxin genes. Mol Biol Evol. 2011; 28: 2637–2649. doi: 10.1093/molbev/msr091 21478373
    • (2011) Mol Biol Evol , vol.28 , pp. 2637-2649
    • Casewell, N.R.1    Wagstaff, S.C.2    Harrison, R.A.3    Renjifo, C.4    Wüster, W.5
  • 6
    • 84903465784 scopus 로고    scopus 로고
    • Medically important differences in snake venom composition are dictated by distinct postgenomic mechanisms
    • Casewell NR, Wagstaff SC, Wüster W, Cook DA, Bolton FM, King SI, et al. Medically important differences in snake venom composition are dictated by distinct postgenomic mechanisms. Proc Natl Acad Sci U S A. 2014; 111: 9205–9210. doi: 10.1073/pnas.1405484111 24927555
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 9205-9210
    • Casewell, N.R.1    Wagstaff, S.C.2    Wüster, W.3    Cook, D.A.4    Bolton, F.M.5    King, S.I.6
  • 8
    • 77956986903 scopus 로고    scopus 로고
    • Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: tissue distribution and in situ hydrolysis
    • Baldo C, Jamora C, Yamanouye N, Zorn TM, Moura-da-Silva AM, Mechanisms of vascular damage by hemorrhagic snake venom metalloproteinases: tissue distribution and in situ hydrolysis. PLoS Negl Trop Dis. 2010; 4: e727. doi: 10.1371/journal.pntd.0000727 20614020
    • (2010) PLoS Negl Trop Dis , vol.4 , pp. 727
    • Baldo, C.1    Jamora, C.2    Yamanouye, N.3    Zorn, T.M.4    Moura-da-Silva, A.M.5
  • 9
    • 39149086659 scopus 로고    scopus 로고
    • Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases
    • Moura-da-Silva AM, Ramos OH, Baldo C, Niland S, Hansen U, Ventura JS, et al. Collagen binding is a key factor for the hemorrhagic activity of snake venom metalloproteinases. Biochimie. 2008; 90: 484–492. 18096518
    • (2008) Biochimie , vol.90 , pp. 484-492
    • Moura-da-Silva, A.M.1    Ramos, O.H.2    Baldo, C.3    Niland, S.4    Hansen, U.5    Ventura, J.S.6
  • 10
    • 77956624674 scopus 로고    scopus 로고
    • New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases
    • Oliveira AK, Paes Leme AF, Asega AF, Camargo AC, Fox JW, Serrano SM, New insights into the structural elements involved in the skin haemorrhage induced by snake venom metalloproteinases. Thromb Haemost. 2010; 104: 485–497. doi: 10.1160/TH09-12-0855 20664911
    • (2010) Thromb Haemost , vol.104 , pp. 485-497
    • Oliveira, A.K.1    Paes Leme, A.F.2    Asega, A.F.3    Camargo, A.C.4    Fox, J.W.5    Serrano, S.M.6
  • 11
    • 33845693751 scopus 로고    scopus 로고
    • Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain
    • Pinto AF, Terra RM, Guimaraes JA, Fox JW, Mapping von Willebrand factor A domain binding sites on a snake venom metalloproteinase cysteine-rich domain. Arch Biochem Biophys. 2007; 457: 41–46. 17118332
    • (2007) Arch Biochem Biophys , vol.457 , pp. 41-46
    • Pinto, A.F.1    Terra, R.M.2    Guimaraes, J.A.3    Fox, J.W.4
  • 12
    • 26844537946 scopus 로고    scopus 로고
    • Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor
    • Serrano SM, Jia LG, Wang D, Shannon JD, Fox JW, Function of the cysteine-rich domain of the haemorrhagic metalloproteinase atrolysin A: targeting adhesion proteins collagen I and von Willebrand factor. Biochem J. 2005; 391: 69–76. 15929722
    • (2005) Biochem J , vol.391 , pp. 69-76
    • Serrano, S.M.1    Jia, L.G.2    Wang, D.3    Shannon, J.D.4    Fox, J.W.5
  • 13
    • 33845984058 scopus 로고    scopus 로고
    • The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: role in substrate targeting
    • Serrano SM, Kim J, Wang D, Dragulev B, Shannon JD, Mann HH, et al. The cysteine-rich domain of snake venom metalloproteinases is a ligand for von Willebrand factor A domains: role in substrate targeting. J Biol Chem. 2006; 281: 39746–39756. 17040908
    • (2006) J Biol Chem , vol.281 , pp. 39746-39756
    • Serrano, S.M.1    Kim, J.2    Wang, D.3    Dragulev, B.4    Shannon, J.D.5    Mann, H.H.6
  • 14
    • 34447309053 scopus 로고    scopus 로고
    • Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation
    • Serrano SM, Wang D, Shannon JD, Pinto AF, Polanowska-Grabowska RK, Fox JW, Interaction of the cysteine-rich domain of snake venom metalloproteinases with the A1 domain of von Willebrand factor promotes site-specific proteolysis of von Willebrand factor and inhibition of von Willebrand factor-mediated platelet aggregation. FEBS J. 2007; 274: 3611–3621. 17578514
    • (2007) FEBS J , vol.274 , pp. 3611-3621
    • Serrano, S.M.1    Wang, D.2    Shannon, J.D.3    Pinto, A.F.4    Polanowska-Grabowska, R.K.5    Fox, J.W.6
  • 15
    • 0025023540 scopus 로고
    • Interaction of hemorrhagic metalloproteinases with human alpha 2-macroglobulin
    • Baramova EN, Shannon JD, Bjarnason JB, Gonias SL, Fox JW, Interaction of hemorrhagic metalloproteinases with human alpha 2-macroglobulin. Biochemistry.1990; 29: 1069–1074. 1692735
    • (1990) Biochemistry , vol.29 , pp. 1069-1074
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Gonias, S.L.4    Fox, J.W.5
  • 16
    • 84899428805 scopus 로고    scopus 로고
    • Understanding structural and functional aspects of PII snake venom metalloproteinases: characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralis
    • Camacho E, Villalobos E, Sanz L, Pérez A, Escalante T, Lomonte B, et al. (2014) Understanding structural and functional aspects of PII snake venom metalloproteinases: characterization of BlatH1, a hemorrhagic dimeric enzyme from the venom of Bothriechis lateralis. Biochimie. 2014; 101: 145–155. doi: 10.1016/j.biochi.2014.01.008 24457155
    • (2014) Biochimie , vol.101 , pp. 145-155
    • Camacho, E.1    Villalobos, E.2    Sanz, L.3    Pérez, A.4    Escalante, T.5    Lomonte, B.6
  • 17
    • 80051665013 scopus 로고    scopus 로고
    • Key events in microvascular damage induced by snake venom hemorrhagic metalloproteinases
    • Escalante T, Rucavado A, Fox JW, Gutiérrez JM, Key events in microvascular damage induced by snake venom hemorrhagic metalloproteinases. J Proteomics. 2011; 74: 1781–1794. doi: 10.1016/j.jprot.2011.03.026 21447411
    • (2011) J Proteomics , vol.74 , pp. 1781-1794
    • Escalante, T.1    Rucavado, A.2    Fox, J.W.3    Gutiérrez, J.M.4
  • 18
    • 19544381172 scopus 로고    scopus 로고
    • Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage
    • Gutiérrez JM, Rucavado A, Escalante T, Díaz C, Hemorrhage induced by snake venom metalloproteinases: biochemical and biophysical mechanisms involved in microvessel damage. Toxicon. 2005; 45: 997–1011. 15922771
    • (2005) Toxicon , vol.45 , pp. 997-1011
    • Gutiérrez, J.M.1    Rucavado, A.2    Escalante, T.3    Díaz, C.4
  • 19
    • 0034213348 scopus 로고    scopus 로고
    • Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom
    • Nikai T, Taniguchi K, Komori Y, Masuda K, Fox JW, Sugihara H, Primary structure and functional characterization of bilitoxin-1, a novel dimeric P-II snake venom metalloproteinase from Agkistrodon bilineatus venom. Arch Biochem Biophys. 2000; 378: 6–15. 10871038
    • (2000) Arch Biochem Biophys , vol.378 , pp. 6-15
    • Nikai, T.1    Taniguchi, K.2    Komori, Y.3    Masuda, K.4    Fox, J.W.5    Sugihara, H.6
  • 20
    • 0024452930 scopus 로고
    • Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases
    • Baramova EN, Shannon JD, Bjarnason JB, Fox JW, Degradation of extracellular matrix proteins by hemorrhagic metalloproteinases. Arch Biochem Biophys. 1989; 275: 63–71. 2817904
    • (1989) Arch Biochem Biophys , vol.275 , pp. 63-71
    • Baramova, E.N.1    Shannon, J.D.2    Bjarnason, J.B.3    Fox, J.W.4
  • 21
    • 0025942230 scopus 로고
    • Proteolytic digestion of non-collagenous basement membrane proteins by the hemorrhagic metalloproteinase Ht-e from Crotalus atrox venom
    • Baramova EN, Shannon JD, Fox JW, Bjarnason JB, Proteolytic digestion of non-collagenous basement membrane proteins by the hemorrhagic metalloproteinase Ht-e from Crotalus atrox venom. Biomed Biochim Acta. 1991; 50: 763–768. 1801753
    • (1991) Biomed Biochim Acta , vol.50 , pp. 763-768
    • Baramova, E.N.1    Shannon, J.D.2    Fox, J.W.3    Bjarnason, J.B.4
  • 22
    • 82955187846 scopus 로고    scopus 로고
    • Role of collagens and perlecan in microvascular stability: exploring the mechanism of capillary vessel damage by snake venom metalloproteinases
    • Escalante T, Ortiz N, Rucavado A, Sánchez EF, Richardson M, Fox JW, et al. Role of collagens and perlecan in microvascular stability: exploring the mechanism of capillary vessel damage by snake venom metalloproteinases. PLoS One. 2011; 6: e28017. doi: 10.1371/journal.pone.0028017 22174764
    • (2011) PLoS One , vol.6 , pp. 28017
    • Escalante, T.1    Ortiz, N.2    Rucavado, A.3    Sánchez, E.F.4    Richardson, M.5    Fox, J.W.6
  • 23
    • 0015834958 scopus 로고
    • Action of snake venom hemorrhagic principles on isolated glomerular basement membrane
    • Osaka A, Just M, Habermann E, Action of snake venom hemorrhagic principles on isolated glomerular basement membrane. Biochim Biophys Acta. 1973; 323: 415–428. 4357021
    • (1973) Biochim Biophys Acta , vol.323 , pp. 415-428
    • Osaka, A.1    Just, M.2    Habermann, E.3
  • 24
    • 0028639246 scopus 로고
    • Basement membrane (type IV) collagen
    • Kühn K, Basement membrane (type IV) collagen. Matrix Biol. 1995; 14: 439–445. 7795882
    • (1995) Matrix Biol , vol.14 , pp. 439-445
    • Kühn, K.1
  • 26
    • 0019781637 scopus 로고
    • A network model for the organization of type IV collagen molecules in basement membranes
    • Timpl R, Wiedemann H, van Delden V, Furthmayr H, Kühn K, A network model for the organization of type IV collagen molecules in basement membranes. Eur J Biochem. 1981; 120: 203–211. 6274634
    • (1981) Eur J Biochem , vol.120 , pp. 203-211
    • Timpl, R.1    Wiedemann, H.2    van Delden, V.3    Furthmayr, H.4    Kühn, K.5
  • 27
    • 1442310569 scopus 로고    scopus 로고
    • Basement membrane assembly, stability and activities observed through a developmental lens
    • Yurchenco PD, Amenta PS, Patton BL, Basement membrane assembly, stability and activities observed through a developmental lens. Matrix Biol. 2004; 22: 521–538. 14996432
    • (2004) Matrix Biol , vol.22 , pp. 521-538
    • Yurchenco, P.D.1    Amenta, P.S.2    Patton, B.L.3
  • 28
    • 70449428630 scopus 로고    scopus 로고
    • Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins
    • Escalante T, Rucavado A, Pinto AF, Terra RM, Gutiérrez JM, Fox JW, Wound exudate as a proteomic window to reveal different mechanisms of tissue damage by snake venom toxins. J Proteome Res. 2009; 8: 5120–5131. doi: 10.1021/pr900489m 19764775
    • (2009) J Proteome Res , vol.8 , pp. 5120-5131
    • Escalante, T.1    Rucavado, A.2    Pinto, A.F.3    Terra, R.M.4    Gutiérrez, J.M.5    Fox, J.W.6
  • 29
    • 79953678991 scopus 로고    scopus 로고
    • Proteomics of wound exudate in snake venom-induced pathology: search for biomarkers to assess tissue damage and therapeutic success
    • Rucavado A, Escalante T, Shannon J, Gutiérrez JM, Fox JW, Proteomics of wound exudate in snake venom-induced pathology: search for biomarkers to assess tissue damage and therapeutic success. J Proteome Res. 2011; 10: 1987–2005. doi: 10.1021/pr101208f 21306181
    • (2011) J Proteome Res , vol.10 , pp. 1987-2005
    • Rucavado, A.1    Escalante, T.2    Shannon, J.3    Gutiérrez, J.M.4    Fox, J.W.5
  • 30
    • 0028924054 scopus 로고
    • Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo)
    • Gutiérrez JM, Romero M, Díaz C, Borkow G, Ovadia M, Isolation and characterization of a metalloproteinase with weak hemorrhagic activity from the venom of the snake Bothrops asper (terciopelo). Toxicon. 1995; 33: 19–29. 7778126
    • (1995) Toxicon , vol.33 , pp. 19-29
    • Gutiérrez, J.M.1    Romero, M.2    Díaz, C.3    Borkow, G.4    Ovadia, M.5
  • 31
    • 10744232219 scopus 로고    scopus 로고
    • Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities
    • Watanabe L, Shannon JD, Valente RH, Rucavado A, Alape-Girón A, Kamiguti AS, et al. Amino acid sequence and crystal structure of BaP1, a metalloproteinase from Bothrops asper snake venom that exerts multiple tissue-damaging activities. Protein Sci. 2003; 12: 2273–2281. 14500885
    • (2003) Protein Sci , vol.12 , pp. 2273-2281
    • Watanabe, L.1    Shannon, J.D.2    Valente, R.H.3    Rucavado, A.4    Alape-Girón, A.5    Kamiguti, A.S.6
  • 32
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227: 680–685. 5432063
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 4744363468 scopus 로고    scopus 로고
    • A novel P-I class metalloproteinase with broad substrate-cleaving activity, agkislysin, from Agkistrodon acutus venom
    • Wang WJ, Shih CH, Huang TF, A novel P-I class metalloproteinase with broad substrate-cleaving activity, agkislysin, from Agkistrodon acutus venom. Biochem Biophys Res Commun. 2004; 324: 224–230. 15465006
    • (2004) Biochem Biophys Res Commun , vol.324 , pp. 224-230
    • Wang, W.J.1    Shih, C.H.2    Huang, T.F.3
  • 34
    • 0022354215 scopus 로고
    • Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom
    • Gutiérrez JM, Gene JA, Rojas G, Cerdas L, Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom. Toxicon, 1985; 23: 887–893. 3913055
    • (1985) Toxicon , vol.23 , pp. 887-893
    • Gutiérrez, J.M.1    Gene, J.A.2    Rojas, G.3    Cerdas, L.4
  • 35
    • 79956224874 scopus 로고    scopus 로고
    • Profiling the venom gland transcriptomes of Costa Rican snakes by 454 pyrosequencing
    • Durban J, Juárez P, Angulo Y, Lomonte B, Flores-Díaz M, Alape-Girón A, et al. (2011) Profiling the venom gland transcriptomes of Costa Rican snakes by 454 pyrosequencing. BMC Genomics. 2011; 12: 259. doi: 10.1186/1471-2164-12-259 21605378
    • (2011) BMC Genomics , vol.12 , pp. 259
    • Durban, J.1    Juárez, P.2    Angulo, Y.3    Lomonte, B.4    Flores-Díaz, M.5    Alape-Girón, A.6
  • 36
    • 0029432140 scopus 로고
    • Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (Terciopelo) snake venom
    • Rucavado A, Lomonte B, Ovadia M, Gutiérrez JM, Local tissue damage induced by BaP1, a metalloproteinase isolated from Bothrops asper (Terciopelo) snake venom. Exp Mol Pathol. 1995; 63: 186–199. 9062552
    • (1995) Exp Mol Pathol , vol.63 , pp. 186-199
    • Rucavado, A.1    Lomonte, B.2    Ovadia, M.3    Gutiérrez, J.M.4
  • 37
    • 2942642590 scopus 로고    scopus 로고
    • Automatic and quantitative measurement of protein-protein colocalization in live cells
    • Costes SV, Daelemans D, Cho EH, Dobbin Z, Pavlakis G, Lockett S, Automatic and quantitative measurement of protein-protein colocalization in live cells. Biophys J. 2004; 86: 3993–4003. 15189895
    • (2004) Biophys J , vol.86 , pp. 3993-4003
    • Costes, S.V.1    Daelemans, D.2    Cho, E.H.3    Dobbin, Z.4    Pavlakis, G.5    Lockett, S.6
  • 38
    • 65649130436 scopus 로고    scopus 로고
    • Developmental and pathogenic mechanisms of basement membrane assembly
    • Yurchenco PD, Patton BL, Developmental and pathogenic mechanisms of basement membrane assembly. Curr Pharm Des. 2009; 15: 1277–1294. 19355968
    • (2009) Curr Pharm Des , vol.15 , pp. 1277-1294
    • Yurchenco, P.D.1    Patton, B.L.2
  • 40
    • 51749090417 scopus 로고    scopus 로고
    • Skin pathology induced by snake venom metalloproteinase: acute damage, revascularization, and re-epithelization in a mouse ear model
    • Jiménez N, Escalante T, Gutiérrez JM, Rucavado A, Skin pathology induced by snake venom metalloproteinase: acute damage, revascularization, and re-epithelization in a mouse ear model. J Invest Dermatol. 2008; 128: 2421–2428. doi: 10.1038/jid.2008.118 18449209
    • (2008) J Invest Dermatol , vol.128 , pp. 2421-2428
    • Jiménez, N.1    Escalante, T.2    Gutiérrez, J.M.3    Rucavado, A.4
  • 41
    • 0028848625 scopus 로고
    • Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (Terciopelo)
    • Gutiérrez JM, Romero M, Nuñez J, Chaves F, Borkow G, Ovadia M, Skeletal muscle necrosis and regeneration after injection of BaH1, a hemorrhagic metalloproteinase isolated from the venom of the snake Bothrops asper (Terciopelo). Exp Mol Pathol. 1995; 62: 28–41. 7556589
    • (1995) Exp Mol Pathol , vol.62 , pp. 28-41
    • Gutiérrez, J.M.1    Romero, M.2    Nuñez, J.3    Chaves, F.4    Borkow, G.5    Ovadia, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.