메뉴 건너뛰기




Volumn 19, Issue R1, 2010, Pages

Parkinson's disease: Insights from pathways

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; DJ 1 PROTEIN; GENE PRODUCT; LEUCINE RICH REPEAT KINASE 2; PARKIN; PROTEIN PINK1; UNCLASSIFIED DRUG;

EID: 77953890085     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddq167     Document Type: Article
Times cited : (139)

References (82)
  • 3
    • 69149089036 scopus 로고    scopus 로고
    • Molecular pathogenesis of Parkinson disease: insights from genetic studies
    • Gasser, T. (2009) Molecular pathogenesis of Parkinson disease: insights from genetic studies. Expert Rev. Mol. Med., 11, e22.
    • (2009) Expert Rev. Mol. Med. , vol.11
    • Gasser, T.1
  • 5
    • 70350759686 scopus 로고    scopus 로고
    • Pathogenesis of familial Parkinson's disease: new insights based on monogenic forms of Parkinson's disease
    • Hatano, T., Kubo, S., Sato, S. and Hattori, N. (2009) Pathogenesis of familial Parkinson's disease: new insights based on monogenic forms of Parkinson's disease. J. Neurochem., 111, 1075-1093.
    • (2009) J. Neurochem. , vol.111 , pp. 1075-1093
    • Hatano, T.1    Kubo, S.2    Sato, S.3    Hattori, N.4
  • 6
    • 63149090431 scopus 로고    scopus 로고
    • Parkinson's disease: from monogenic forms to genetic susceptibility factors
    • Lesage, S. and Brice, A. (2009) Parkinson's disease: from monogenic forms to genetic susceptibility factors. Hum. Mol. Genet., 18, R48-R59.
    • (2009) Hum. Mol. Genet. , vol.18
    • Lesage, S.1    Brice, A.2
  • 13
    • 37349129281 scopus 로고    scopus 로고
    • The parkin protein as a therapeutic target in Parkinson's disease
    • Winklhofer, K.F. (2007) The parkin protein as a therapeutic target in Parkinson's disease. Expert Opin. Ther. Targets, 11, 1543-1552.
    • (2007) Expert Opin. Ther. Targets , vol.11 , pp. 1543-1552
    • Winklhofer, K.F.1
  • 14
    • 41149114560 scopus 로고    scopus 로고
    • Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1)
    • Mills, R.D., Sim, C.H., Mok, S.S., Mulhern, T.D., Culvenor, J.G. and Cheng, H.C. (2008) Biochemical aspects of the neuroprotective mechanism of PTEN-induced kinase-1 (PINK1). J. Neurochem., 105, 18-33.
    • (2008) J. Neurochem. , vol.105 , pp. 18-33
    • Mills, R.D.1    Sim, C.H.2    Mok, S.S.3    Mulhern, T.D.4    Culvenor, J.G.5    Cheng, H.C.6
  • 16
    • 70350002152 scopus 로고    scopus 로고
    • DJ-1 and prevention of oxidative stress in Parkinson's disease and other age-related disorders
    • Kahle, P.J., Waak, J. and Gasser, T. (2009) DJ-1 and prevention of oxidative stress in Parkinson's disease and other age-related disorders. Free Radic. Biol. Med., 47, 1354-1361.
    • (2009) Free Radic. Biol. Med. , vol.47 , pp. 1354-1361
    • Kahle, P.J.1    Waak, J.2    Gasser, T.3
  • 18
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark, I.E., Dodson, M.W., Jiang, C., Cao, J.H., Huh, J.R., Seol, J.H., Yoo, S.J., Hay, B.A. and Guo, M. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature, 441, 1162-1166.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 19
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park, J., Lee, S.B., Lee, S., Kim, Y., Song, S., Kim, S., Bae, E., Kim, J., Shong, M., Kim, J.M. et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature, 441, 1157-1161.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10
  • 20
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda, R.K., Cherra, S.J. 3rd, Kulich, S.M., Tandon, A., Park, D. and Chu, C.T. (2009) Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J. Biol. Chem., 284, 13843-13855.
    • (2009) J. Biol. Chem. , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra S.J. 3rd2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 22
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng, H., Dodson, M.W., Huang, H. and Guo, M. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl Acad. Sci. USA, 105, 14503-14508.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 24
    • 44349195101 scopus 로고    scopus 로고
    • Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery
    • Yang, Y., Ouyang, Y., Yang, L., Beal, M.F., McQuibban, A., Vogel, H. and Lu, B. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl Acad. Sci. USA, 105, 7070-7075.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 7070-7075
    • Yang, Y.1    Ouyang, Y.2    Yang, L.3    Beal, M.F.4    McQuibban, A.5    Vogel, H.6    Lu, B.7
  • 25
    • 77951235489 scopus 로고    scopus 로고
    • Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1
    • Cui, M., Tang, X., Christian, W.V., Yoon, Y. and Tieu, K. (2010) Perturbations in mitochondrial dynamics induced by human mutant PINK1 can be rescued by the mitochondrial division inhibitor mdivi-1. J. Biol. Chem, 285, 11740-11752.
    • (2010) J. Biol. Chem. , vol.285 , pp. 11740-11752
    • Cui, M.1    Tang, X.2    Christian, W.V.3    Yoon, Y.4    Tieu, K.5
  • 29
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • Gautier, C.A., Kitada, T. and Shen, J. (2008) Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress. Proc. Natl Acad. Sci. USA, 105, 11364-11369.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 30
    • 62749113469 scopus 로고    scopus 로고
    • Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells
    • Gegg, M.E., Cooper, J.M., Schapira, A.H. and Taanman, J.W. (2009) Silencing of PINK1 expression affects mitochondrial DNA and oxidative phosphorylation in dopaminergic cells. PLoS One, 4, e4756.
    • (2009) PLoS One , vol.4
    • Gegg, M.E.1    Cooper, J.M.2    Schapira, A.H.3    Taanman, J.W.4
  • 32
    • 67649413521 scopus 로고    scopus 로고
    • Complex I deficiency and dopaminergic neuronal cell loss in parkin-deficient zebrafish (Danio rerio)
    • Flinn, L., Mortiboys, H., Volkmann, K., Koster, R.W., Ingham, P.W. and Bandmann, O. (2009) Complex I deficiency and dopaminergic neuronal cell loss in parkin-deficient zebrafish (Danio rerio). Brain, 132, 1613-1623.
    • (2009) Brain , vol.132 , pp. 1613-1623
    • Flinn, L.1    Mortiboys, H.2    Volkmann, K.3    Koster, R.W.4    Ingham, P.W.5    Bandmann, O.6
  • 34
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D.F. and Youle, R.J. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol., 183, 795-803.
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 38
    • 73449111577 scopus 로고    scopus 로고
    • Mitochondrial autophagy as a compensatory response to PINK1 deficiency
    • Cherra, S.J. 3rd, Dagda, R.K., Tandon, A. and Chu, C.T. (2009) Mitochondrial autophagy as a compensatory response to PINK1 deficiency. Autophagy, 5, 1213-1214.
    • (2009) Autophagy , vol.5 , pp. 1213-1214
    • Cherra S.J. 3rd1    Dagda, R.K.2    Tandon, A.3    Chu, C.T.4
  • 41
    • 65249159732 scopus 로고    scopus 로고
    • Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1
    • Blackinton, J., Lakshminarasimhan, M., Thomas, K.J., Ahmad, R., Greggio, E., Raza, A.S., Cookson, M.R. and Wilson, M.A. (2009) Formation of a stabilized cysteine sulfinic acid is critical for the mitochondrial function of the parkinsonism protein DJ-1. J. Biol. Chem., 284, 6476-6485.
    • (2009) J. Biol. Chem. , vol.284 , pp. 6476-6485
    • Blackinton, J.1    Lakshminarasimhan, M.2    Thomas, K.J.3    Ahmad, R.4    Greggio, E.5    Raza, A.S.6    Cookson, M.R.7    Wilson, M.A.8
  • 42
    • 63049138430 scopus 로고    scopus 로고
    • Mitochondrial localization of DJ-1 leads to enhanced neuroprotection
    • Junn, E., Jang, W.H., Zhao, X., Jeong, B.S. and Mouradian, M.M. (2009) Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J. Neurosci. Res., 87, 123-129.
    • (2009) J. Neurosci. Res. , vol.87 , pp. 123-129
    • Junn, E.1    Jang, W.H.2    Zhao, X.3    Jeong, B.S.4    Mouradian, M.M.5
  • 43
    • 30044434872 scopus 로고    scopus 로고
    • Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans
    • Ved, R., Saha, S., Westlund, B., Perier, C., Burnam, L., Sluder, A., Hoener, M., Rodrigues, C.M., Alfonso, A., Steer, C. et al. (2005) Similar patterns of mitochondrial vulnerability and rescue induced by genetic modification of alpha-synuclein, parkin, and DJ-1 in Caenorhabditis elegans. J. Biol. Chem., 280, 42655-42668.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42655-42668
    • Ved, R.1    Saha, S.2    Westlund, B.3    Perier, C.4    Burnam, L.5    Sluder, A.6    Hoener, M.7    Rodrigues, C.M.8    Alfonso, A.9    Steer, C.10
  • 48
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling
    • Sha, D., Chin, L.S. and Li, L. (2010) Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum. Mol. Genet., 19, 352-363.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 352-363
    • Sha, D.1    Chin, L.S.2    Li, L.3
  • 49
    • 70349923087 scopus 로고    scopus 로고
    • Absence of nigral degeneration in aged parkin/DJ-1/PINK1 triple knockout mice
    • Kitada, T., Tong, Y., Gautier, C.A. and Shen, J. (2009) Absence of nigral degeneration in aged parkin/DJ-1/PINK1 triple knockout mice. J. Neurochem., 111, 696-702.
    • (2009) J. Neurochem. , vol.111 , pp. 696-702
    • Kitada, T.1    Tong, Y.2    Gautier, C.A.3    Shen, J.4
  • 50
    • 26444445118 scopus 로고    scopus 로고
    • Abundant neuritic inclusions and microvacuolar changes in a case of diffuse Lewy body disease with the A53T mutation in the alpha-synuclein gene
    • Yamaguchi, K., Cochran, E.J., Murrell, J.R., Polymeropoulos, M.H., Shannon, K.M., Crowther, R.A., Goedert, M. and Ghetti, B. (2005) Abundant neuritic inclusions and microvacuolar changes in a case of diffuse Lewy body disease with the A53T mutation in the alpha-synuclein gene. Acta Neuropathol., 110, 298-305.
    • (2005) Acta Neuropathol. , vol.110 , pp. 298-305
    • Yamaguchi, K.1    Cochran, E.J.2    Murrell, J.R.3    Polymeropoulos, M.H.4    Shannon, K.M.5    Crowther, R.A.6    Goedert, M.7    Ghetti, B.8
  • 57
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein
    • Uversky, V.N. and Eliezer, D. (2009) Biophysics of Parkinson's disease: structure and aggregation of alpha-synuclein. Curr. Protein Pept. Sci., 10, 483-499.
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 58
    • 37549030985 scopus 로고    scopus 로고
    • In vivo alpha-synuclein overexpression in rodents: a useful model of Parkinson's disease?
    • Chesselet, M.F. (2008) In vivo alpha-synuclein overexpression in rodents: a useful model of Parkinson's disease? Exp. Neurol., 209, 22-27.
    • (2008) Exp. Neurol. , vol.209 , pp. 22-27
    • Chesselet, M.F.1
  • 59
    • 47049084912 scopus 로고    scopus 로고
    • Viral vectors, animal models and new therapies for Parkinson's disease
    • Schneider, B., Zufferey, R. and Aebischer, P. (2008) Viral vectors, animal models and new therapies for Parkinson's disease. Parkinsonism Relat. Disord., 14(Suppl. 2), S169-S171.
    • (2008) Parkinsonism Relat. Disord. , vol.14 , Issue.SUPPL. 2
    • Schneider, B.1    Zufferey, R.2    Aebischer, P.3
  • 60
    • 77953395313 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions
    • pii
    • Greggio, E. and Cookson, M.R. (2009) Leucine-rich repeat kinase 2 mutations and Parkinson's disease: three questions. ASN Neuro, 1, pii: e00002.
    • (2009) ASN Neuro , vol.1
    • Greggio, E.1    Cookson, M.R.2
  • 61
    • 77649105209 scopus 로고    scopus 로고
    • Mechanisms in dominant parkinsonism: the toxic triangle of LRRK2, alpha-synuclein, and tau
    • Taymans, J.M. and Cookson, M.R. (2010) Mechanisms in dominant parkinsonism: the toxic triangle of LRRK2, alpha-synuclein, and tau. Bioessays, 32, 227-235.
    • (2010) Bioessays , vol.32 , pp. 227-235
    • Taymans, J.M.1    Cookson, M.R.2
  • 64
    • 34248574535 scopus 로고    scopus 로고
    • Loss of LRRK2/PARK8 induces degeneration of dopaminergic neurons in Drosophila
    • Lee, S.B., Kim, W., Lee, S. and Chung, J. (2007) Loss of LRRK2/PARK8 induces degeneration of dopaminergic neurons in Drosophila. Biochem. Biophys. Res. Commun., 358, 534-539.
    • (2007) Biochem. Biophys. Res. Commun. , vol.358 , pp. 534-539
    • Lee, S.B.1    Kim, W.2    Lee, S.3    Chung, J.4
  • 65
    • 41549124987 scopus 로고    scopus 로고
    • Dispensable role of Drosophila ortholog of LRRK2 kinase activity in survival of dopaminergic neurons
    • Wang, D., Tang, B., Zhao, G., Pan, Q., Xia, K., Bodmer, R. and Zhang, Z. (2008) Dispensable role of Drosophila ortholog of LRRK2 kinase activity in survival of dopaminergic neurons. Mol. Neurodegener., 3,3.
    • (2008) Mol. Neurodegener. , vol.3 , pp. 3
    • Wang, D.1    Tang, B.2    Zhao, G.3    Pan, Q.4    Xia, K.5    Bodmer, R.6    Zhang, Z.7
  • 66
    • 72449198522 scopus 로고    scopus 로고
    • Unexpected lack of hypersensitivity in LRRK2 knock-out mice to MPTP (1-methyl- 4-phenyl-1,2,3,6-tetrahydropyridine)
    • Andres-Mateos, E., Mejias, R., Sasaki, M., Li, X., Lin, B.M., Biskup, S., Zhang, L., Banerjee, R., Thomas, B., Yang, L. et al. (2009) Unexpected lack of hypersensitivity in LRRK2 knock-out mice to MPTP (1-methyl- 4-phenyl-1,2,3,6-tetrahydropyridine). J. Neurosci., 29, 15846-15850.
    • (2009) J. Neurosci. , vol.29 , pp. 15846-15850
    • Andres-Mateos, E.1    Mejias, R.2    Sasaki, M.3    Li, X.4    Lin, B.M.5    Biskup, S.6    Zhang, L.7    Banerjee, R.8    Thomas, B.9    Yang, L.10
  • 67
    • 68249104469 scopus 로고    scopus 로고
    • Emerging role of LRRK2 in human neural progenitor cell cycle progression, survival and differentiation
    • Milosevic, J., Schwarz, S.C., Ogunlade, V., Meyer, A.K., Storch, A. and Schwarz, J. (2009) Emerging role of LRRK2 in human neural progenitor cell cycle progression, survival and differentiation. Mol. Neurodegener., 4, 25.
    • (2009) Mol. Neurodegener. , vol.4 , pp. 25
    • Milosevic, J.1    Schwarz, S.C.2    Ogunlade, V.3    Meyer, A.K.4    Storch, A.5    Schwarz, J.6
  • 70
    • 72149087091 scopus 로고    scopus 로고
    • Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein
    • Lin, X., Parisiadou, L., Gu, X.L., Wang, L., Shim, H., Sun, L., Xie, C., Long, C.X., Yang, W.J., Ding, J. et al. (2009) Leucine-rich repeat kinase 2 regulates the progression of neuropathology induced by Parkinson's-disease-related mutant alpha-synuclein. Neuron, 64, 807-827.
    • (2009) Neuron , vol.64 , pp. 807-827
    • Lin, X.1    Parisiadou, L.2    Gu, X.L.3    Wang, L.4    Shim, H.5    Sun, L.6    Xie, C.7    Long, C.X.8    Yang, W.J.9    Ding, J.10
  • 73
    • 10644281090 scopus 로고    scopus 로고
    • Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease
    • Lo Bianco, C., Schneider, B.L., Bauer, M., Sajadi, A., Brice, A., Iwatsubo, T. and Aebischer, P. (2004) Lentiviral vector delivery of parkin prevents dopaminergic degeneration in an alpha-synuclein rat model of Parkinson's disease. Proc. Natl Acad. Sci. USA, 101, 17510-17515.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 17510-17515
    • Lo Bianco, C.1    Schneider, B.L.2    Bauer, M.3    Sajadi, A.4    Brice, A.5    Iwatsubo, T.6    Aebischer, P.7
  • 74
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli, L., O'Farrell, C., Lockhart, P.J., Baptista, M., Kehoe, K., Vink, L., Choi, P., Wolozin, B., Farrer, M., Hardy, J. et al. (2002) Parkin protects against the toxicity associated with mutant alpha-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron, 36, 1007-1019.
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3    Baptista, M.4    Kehoe, K.5    Vink, L.6    Choi, P.7    Wolozin, B.8    Farrer, M.9    Hardy, J.10
  • 78
    • 51949090816 scopus 로고    scopus 로고
    • Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila
    • Imai, Y., Gehrke, S., Wang, H.Q., Takahashi, R., Hasegawa, K., Oota, E. and Lu, B. (2008) Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. EMBO J., 27, 2432-2443.
    • (2008) EMBO J. , vol.27 , pp. 2432-2443
    • Imai, Y.1    Gehrke, S.2    Wang, H.Q.3    Takahashi, R.4    Hasegawa, K.5    Oota, E.6    Lu, B.7
  • 80
    • 77649328234 scopus 로고    scopus 로고
    • The Parkinson's disease associated LRRK2 exhibits weaker in vitro phosphorylation of 4E-BP compared to autophosphorylation
    • Kumar, A., Greggio, E., Beilina, A., Kaganovich, A., Chan, D., Taymans, J.M., Wolozin, B. and Cookson, M.R. (2010) The Parkinson's disease associated LRRK2 exhibits weaker in vitro phosphorylation of 4E-BP compared to autophosphorylation. PLoS One, 5, e8730.
    • (2010) PLoS One , vol.5
    • Kumar, A.1    Greggio, E.2    Beilina, A.3    Kaganovich, A.4    Chan, D.5    Taymans, J.M.6    Wolozin, B.7    Cookson, M.R.8
  • 82
    • 73549085595 scopus 로고    scopus 로고
    • Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis
    • Nemani, V.M., Lu, W., Berge, V., Nakamura, K., Onoa, B., Lee, M.K., Chaudhry, F.A., Nicoll, R.A. and Edwards, R.H. (2010) Increased expression of alpha-synuclein reduces neurotransmitter release by inhibiting synaptic vesicle reclustering after endocytosis. Neuron, 65, 66-79.
    • (2010) Neuron , vol.65 , pp. 66-79
    • Nemani, V.M.1    Lu, W.2    Berge, V.3    Nakamura, K.4    Onoa, B.5    Lee, M.K.6    Chaudhry, F.A.7    Nicoll, R.A.8    Edwards, R.H.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.