메뉴 건너뛰기




Volumn 287, Issue 15, 2012, Pages 11788-11797

Biological and structural characterization of Trypanosoma cruzi phosphodiesterase C and implications for design of parasite selective inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; CATALYTIC DOMAINS; CHAGAS DISEASE; DIRECT INTERACTIONS; DRUG TARGETS; ENZYMATIC ACTIVITIES; ENZYMATIC PROPERTIES; N-TERMINALS; PARASITE-; PHOSPHODIESTERASES; SELECTIVE INHIBITORS; SILDENAFIL; STRUCTURAL CHARACTERIZATION; STRUCTURAL STUDIES; TRYPANOSOMA BRUCEI; TRYPANOSOMA CRUZI;

EID: 84859478891     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.326777     Document Type: Article
Times cited : (31)

References (53)
  • 4
    • 79953322829 scopus 로고    scopus 로고
    • Cyclic-nucleotide signalling in protozoa
    • Gould, M. K., and de Koning, H. P. (2011) Cyclic-nucleotide signalling in protozoa. FEMS Microbiol. Rev. 35, 515-541
    • (2011) FEMS Microbiol. Rev. , vol.35 , pp. 515-541
    • Gould, M.K.1    De Koning, H.P.2
  • 5
    • 34548728165 scopus 로고    scopus 로고
    • Cyclic nucleotide signaling mechanisms in trypanosomes: Possible targets for therapeutic agents
    • DOI 10.1124/mi.7.4.7
    • Laxman, S., and Beavo, J. A. (2007) Cyclic nucleotide signaling mechanisms in trypanosomes. Possible targets for therapeutic agents. Mol. Interv. 7, 203-215 (Pubitemid 47437267)
    • (2007) Molecular Interventions , vol.7 , Issue.4 , pp. 203-215
    • Laxman, S.1    Beavo, J.A.2
  • 6
    • 0842322479 scopus 로고    scopus 로고
    • cAMP signalling in the kinetoplastid protozoa
    • DOI 10.2174/1566524043360113
    • Seebeck, T., Schaub, R., and Johner, A. (2004) cAMP signalling in the kinetoplastid protozoa. Curr. Mol. Med. 4, 585-599 (Pubitemid 39172365)
    • (2004) Current Molecular Medicine , vol.4 , Issue.6 , pp. 585-599
    • Seebeck, T.1    Schaub, R.2    Johner, A.3
  • 7
    • 10644277792 scopus 로고    scopus 로고
    • Acidocalcisomes and the contractile vacuole complex are involved in osmoregulation in Trypanosoma cruzi
    • DOI 10.1074/jbc.M410372200
    • Rohloff, P., Montalvetti, A., and Docampo, R. (2004) Acidocalcisomes and the contractile vacuole complex are involved in osmoregulation in Trypanosoma cruzi. J. Biol. Chem. 279, 52270-52281 (Pubitemid 39656601)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.50 , pp. 52270-52281
    • Rohloff, P.1    Montalvetti, A.2    Docampo, R.3
  • 8
    • 78650245392 scopus 로고    scopus 로고
    • Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi
    • Schoijet, A. C., Miranda, K., Medeiros, L. C., de Souza, W., Flawiá, M. M., Torres, H. N., Pignataro, O. P., Docampo, R., and Alonso, G. D. (2011) Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi. Mol. Microbiol. 79, 50-62
    • (2011) Mol. Microbiol. , vol.79 , pp. 50-62
    • Schoijet, A.C.1    Miranda, K.2    Medeiros, L.C.3    De Souza, W.4    Flawiá, M.M.5    Torres, H.N.6    Pignataro, O.P.7    Docampo, R.8    Alonso, G.D.9
  • 9
    • 33847368239 scopus 로고    scopus 로고
    • The Trypanosoma brucei cAMP phosphodiesterases TbrPDEB1 and TbrPDEB2: Flagellar enzymes that are essential for parasite virulence
    • DOI 10.1096/fj.06-6818com
    • Oberholzer, M., Marti, G., Baresic, M., Kunz, S., Hemphill, A., and Seebeck, T. (2007) The Trypanosoma brucei cAMP phosphodiesterases TbrPDEB1 and TbrPDEB2. Flagellar enzymes that are essential for parasite virulence. FASEB J. 21, 720-731 (Pubitemid 46348248)
    • (2007) FASEB Journal , vol.21 , Issue.3 , pp. 720-731
    • Oberholzer, M.1    Marti, G.2    Baresic, M.3    Kunz, S.4    Hemphill, A.5    Seebeck, T.6
  • 10
    • 33846339421 scopus 로고    scopus 로고
    • TcrPDEA1, a cAMP-specific phosphodiesterase with atypical pharmacological properties from Trypanosoma cruzi
    • DOI 10.1016/j.molbiopara.2006.12.002, PII S0166685106003495
    • Alonso, G. D., Schoijet, A. C., Torres, H. N., and Flawiá, M. M. (2007) TcrPDEA1, a cAMP-specific phosphodiesterase with atypical pharmacological properties from Trypanosoma cruzi. Mol. Biochem. Parasitol. 152, 72-79 (Pubitemid 46127525)
    • (2007) Molecular and Biochemical Parasitology , vol.152 , Issue.1 , pp. 72-79
    • Alonso, G.D.1    Schoijet, A.C.2    Torres, H.N.3    Flawia, M.M.4
  • 11
    • 33750005401 scopus 로고    scopus 로고
    • Characterization of a novel cAMP-binding, cAMP-specific cyclic nucleotide phosphodiesterase (TcrPDEB1) from Trypanosoma cruzi
    • Díaz-Benjumea, R., Laxman, S., Hinds, T. R., Beavo, J. A., and Rascón, A. (2006) Characterization of a novel cAMP-binding, cAMP-specific cyclic nucleotide phosphodiesterase (TcrPDEB1) from Trypanosoma cruzi. Biochem. J. 399, 305-314
    • (2006) Biochem. J. , vol.399 , pp. 305-314
    • Díaz-Benjumea, R.1    Laxman, S.2    Hinds, T.R.3    Beavo, J.A.4    Rascón, A.5
  • 12
    • 28044464526 scopus 로고    scopus 로고
    • TcPDE4, a novel membrane-associated cAMP-specific phosphodiesterase from Trypanosoma cruzi
    • DOI 10.1016/j.molbiopara.2005.09.005, PII S0166685105002665
    • Alonso, G. D., Schoijet, A. C., Torres, H. N., and Flawiá, M. M. (2006) TcPDE4, a novel membrane-associated cAMP-specific phosphodiesterase from Trypanosoma cruzi. Mol. Biochem. Parasitol. 145, 40-49 (Pubitemid 41691853)
    • (2006) Molecular and Biochemical Parasitology , vol.145 , Issue.1 , pp. 40-49
    • Alonso, G.D.1    Schoijet, A.C.2    Torres, H.N.3    Flawia, M.M.4
  • 13
    • 29144477132 scopus 로고    scopus 로고
    • A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi
    • DOI 10.1111/j.1742-4658.2005.05039.x
    • Kunz, S., Oberholzer, M., and Seebeck, T. (2005) A FYVE-containing unusual cyclic nucleotide phosphodiesterase from Trypanosoma cruzi. FEBS J. 272, 6412-6422 (Pubitemid 41815628)
    • (2005) FEBS Journal , vol.272 , Issue.24 , pp. 6412-6422
    • Kunz, S.1    Oberholzer, M.2    Seebeck, T.3
  • 14
    • 1542374655 scopus 로고    scopus 로고
    • Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi
    • DOI 10.1042/BJ20031147
    • D'Angelo, M. A., Sanguineti, S., Reece, J. M., Birnbaumer, L., Torres, H. N., and Flawiá, M. M. (2004) Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi. Biochem. J. 378, 63-72 (Pubitemid 38299544)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 63-72
    • D'Angelo, M.A.1    Sanguineti, S.2    Reece, J.M.3    Birnbaumer, L.4    Torres, H.N.5    Flawia, M.M.6
  • 15
    • 77956131207 scopus 로고    scopus 로고
    • Chemical validation of phosphodiesterase C as a chemotherapeutic target in Trypanosoma cruzi, the etiological agent of Chagas' disease
    • King-Keller, S., Li, M., Smith, A., Zheng, S., Kaur, G., Yang, X., Wang, B., and Docampo, R. (2010) Chemical validation of phosphodiesterase C as a chemotherapeutic target in Trypanosoma cruzi, the etiological agent of Chagas' disease. Antimicrob. Agents Chemother. 54, 3738-3745
    • (2010) Antimicrob. Agents Chemother. , vol.54 , pp. 3738-3745
    • King-Keller, S.1    Li, M.2    Smith, A.3    Zheng, S.4    Kaur, G.5    Yang, X.6    Wang, B.7    Docampo, R.8
  • 17
    • 71249129667 scopus 로고    scopus 로고
    • Cyclic nucleotide binding GAF domains from phosphodiesterases. Structural and mechanistic insights
    • Heikaus, C. C., Pandit, J., and Klevit, R. E. (2009) Cyclic nucleotide binding GAF domains from phosphodiesterases. Structural and mechanistic insights. Structure 17, 1551-1557
    • (2009) Structure , vol.17 , pp. 1551-1557
    • Heikaus, C.C.1    Pandit, J.2    Klevit, R.E.3
  • 18
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • Lemmon, M. A. (2003) Phosphoinositide recognition domains. Traffic 4, 201-213
    • (2003) Traffic , vol.4 , pp. 201-213
    • Lemmon, M.A.1
  • 19
    • 82555177172 scopus 로고    scopus 로고
    • Phosphodiesterase inhibitors as a new generation of antiprotozoan drugs. Exploiting the benefit of enzymes that are highly conserved between host and parasite
    • Seebeck, T., Sterk, G. J., and Ke, H. (2011) Phosphodiesterase inhibitors as a new generation of antiprotozoan drugs. Exploiting the benefit of enzymes that are highly conserved between host and parasite. Future Med. Chem. 3, 1289-1306
    • (2011) Future Med. Chem. , vol.3 , pp. 1289-1306
    • Seebeck, T.1    Sterk, G.J.2    Ke, H.3
  • 20
    • 78751549573 scopus 로고    scopus 로고
    • Natural and synthetic naphthoquinones active against Trypanosoma cruzi. An initial step towards new drugs for Chagas disease
    • Salas, C. O., Faúndez, M., Morello, A., Maya, J. D., and Tapia, R. A. (2011) Natural and synthetic naphthoquinones active against Trypanosoma cruzi. An initial step towards new drugs for Chagas disease. Curr. Med. Chem. 18, 144-161
    • (2011) Curr. Med. Chem. , vol.18 , pp. 144-161
    • Salas, C.O.1    Faúndez, M.2    Morello, A.3    Maya, J.D.4    Tapia, R.A.5
  • 22
    • 78349274397 scopus 로고    scopus 로고
    • Advances in Chagas disease drug development. 2009-2010
    • Buckner, F. S., and Navabi, N. (2010) Advances in Chagas disease drug development. 2009-2010. Curr. Opin. Infect. Dis. 23, 609-616
    • (2010) Curr. Opin. Infect. Dis. , vol.23 , pp. 609-616
    • Buckner, F.S.1    Navabi, N.2
  • 23
    • 78751534394 scopus 로고    scopus 로고
    • Trypanocidal drugs. Mechanisms, resistance and new targets
    • Wilkinson, S. R., and Kelly, J. M. (2009) Trypanocidal drugs. Mechanisms, resistance and new targets. Expert Rev. Mol. Med. 11, e31
    • (2009) Expert Rev. Mol. Med. , vol.11
    • Wilkinson, S.R.1    Kelly, J.M.2
  • 25
  • 26
    • 33645558859 scopus 로고    scopus 로고
    • Cyclic nucleotide specific phosphodiesterases of Leishmania major
    • Johner, A., Kunz, S., Linder, M., Shakur, Y., and Seebeck, T. (2006) Cyclic nucleotide specific phosphodiesterases of Leishmania major.BMCMicrobiol. 6, 25
    • (2006) BMCMicrobiol. , vol.6 , pp. 25
    • Johner, A.1    Kunz, S.2    Linder, M.3    Shakur, Y.4    Seebeck, T.5
  • 27
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublié, S. (1997) Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublié, S.1
  • 28
    • 24744456706 scopus 로고    scopus 로고
    • Multiple elements jointly determine inhibitor selectivity of cyclic nucleotide phosphodiesterases 4 and 7
    • DOI 10.1074/jbc.M504398200
    • Wang, H., Liu, Y., Chen, Y., Robinson, H., and Ke, H. (2005) Multiple elements jointly determine inhibitor selectivity of cyclic nucleotide phosphodiesterases 4 and 7. J. Biol. Chem. 280, 30949-30955 (Pubitemid 41291827)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.35 , pp. 30949-30955
    • Wang, H.1    Liu, Y.2    Chen, Y.3    Robinson, H.4    Ke, H.5
  • 30
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0031058883 scopus 로고    scopus 로고
    • Phase determination from multiwavelength anomalous diffraction measurements
    • DOI 10.1016/S0076-6879(97)76074-9
    • Hendrickson, W. A., and Ogata, C. M. (1997) Phase determination from multiwavelength anomalous diffraction measurements. Methods Enzymol. 276, 494-523 (Pubitemid 27085619)
    • (1997) Methods in Enzymology , vol.276 , pp. 494-523
    • Hendrickson, W.A.1    Ogata, C.M.2
  • 32
    • 77950793231 scopus 로고    scopus 로고
    • Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification
    • Sheldrick, G. M. (2010) Experimental phasing with SHELXC/D/E. Combining chain tracing with density modification. Acta Crystallogr. D Biol. Crystallogr. 66, 479-485
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 479-485
    • Sheldrick, G.M.1
  • 34
    • 0031053055 scopus 로고    scopus 로고
    • AMoRe: An automated molecular replacement program package
    • DOI 10.1016/S0076-6879(97)76079-8
    • Navaza, J., and Saludjian, P. (1997) AMoRe: an automated molecular replacement program package. Methods Enzymol. 276, 581-594 (Pubitemid 27085624)
    • (1997) Methods in Enzymology , vol.276 , pp. 581-594
    • Navaza, J.1    Saludjian, P.2
  • 35
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 38
    • 0035687612 scopus 로고    scopus 로고
    • Evolutionary rate differences in trypanosomes
    • DOI 10.1016/S1567-1348(01)00018-1, PII S1567134801000181
    • Stevens, J., and Rambaut, A. (2001) Evolutionary rate differences in trypanosomes. Infect. Genet. Evol. 1, 143-150 (Pubitemid 34051519)
    • (2001) Infection, Genetics and Evolution , vol.1 , Issue.2 , pp. 143-150
    • Stevens, J.1    Rambaut, A.2
  • 39
    • 77958123318 scopus 로고    scopus 로고
    • Spliced leader trapping reveals widespread alternative splicing patterns in the highly dynamic transcriptome of Trypanosoma brucei
    • Nilsson, D., Gunasekera, K., Mani, J., Osteras, M., Farinelli, L., Baerlocher, L., Roditi, I., and Ochsenreiter, T. (2010) Spliced leader trapping reveals widespread alternative splicing patterns in the highly dynamic transcriptome of Trypanosoma brucei. PLoS Pathog. 6, e1001037
    • (2010) PLoS Pathog. , vol.6
    • Nilsson, D.1    Gunasekera, K.2    Mani, J.3    Osteras, M.4    Farinelli, L.5    Baerlocher, L.6    Roditi, I.7    Ochsenreiter, T.8
  • 40
    • 70349731776 scopus 로고    scopus 로고
    • Genome-wide expression profiling of in vivo-derived bloodstream parasite stages and dynamic analysis of mRNA alterations during synchronous differentiation in Trypanosoma brucei
    • Kabani, S., Fenn, K., Ross, A., Ivens, A., Smith, T. K., Ghazal, P., and Matthews, K. (2009) Genome-wide expression profiling of in vivo-derived bloodstream parasite stages and dynamic analysis of mRNA alterations during synchronous differentiation in Trypanosoma brucei. BMC Genomics 10, 427
    • (2009) BMC Genomics , vol.10 , pp. 427
    • Kabani, S.1    Fenn, K.2    Ross, A.3    Ivens, A.4    Smith, T.K.5    Ghazal, P.6    Matthews, K.7
  • 41
    • 31344479863 scopus 로고    scopus 로고
    • Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei
    • DOI 10.1002/pmic.200500119
    • Jones, A., Faldas, A., Foucher, A., Hunt, E., Tait, A., Wastling, J. M., and Turner, C. M. (2006) Visualisation and analysis of proteomic data from the procyclic form of Trypanosoma brucei. Proteomics 6, 259-267 (Pubitemid 43142950)
    • (2006) Proteomics , vol.6 , Issue.1 , pp. 259-267
    • Jones, A.1    Faldas, A.2    Foucher, A.3    Hunt, E.4    Tait, A.5    Wastling, J.M.6    Turner, C.M.7
  • 42
    • 33847689816 scopus 로고    scopus 로고
    • Crystal structures of phosphodiesterases and implications on substrate specificity and inhibitor selectivity
    • DOI 10.2174/156802607779941242
    • Ke, H., and Wang, H. (2007) Crystal structures of phosphodiesterases and implications on substrate specificity and inhibitor selectivity. Curr. Top. Med. Chem. 7, 391-403 (Pubitemid 46358652)
    • (2007) Current Topics in Medicinal Chemistry , vol.7 , Issue.4 , pp. 391-403
    • Ke, H.1    Wang, H.2
  • 43
    • 35748936134 scopus 로고    scopus 로고
    • Crystal structure of the Leishmania major phosphodiesterase LmjPDEB1 and insight into the design of the parasite-selective inhibitors
    • DOI 10.1111/j.1365-2958.2007.05976.x
    • Wang, H., Yan, Z., Geng, J., Kunz, S., Seebeck, T., and Ke, H. (2007) Crystal structure of the Leishmania major phosphodiesterase LmjPDEB1 and insight into the design of the parasite-selective inhibitors. Mol. Microbiol. 66, 1029-1038 (Pubitemid 350050428)
    • (2007) Molecular Microbiology , vol.66 , Issue.4 , pp. 1029-1038
    • Wang, H.1    Yan, Z.2    Geng, J.3    Kunz, S.4    Seebeck, T.5    Ke, H.6
  • 46
    • 37349101070 scopus 로고    scopus 로고
    • Conformational variations of both phosphodiesterase-5 and inhibitors provide the structural basis for the physiological effects of vardenafil and sildenafil
    • DOI 10.1124/mol.107.040212
    • Wang, H., Ye, M., Robinson, H., Francis S. H., and Ke, H. (2008) Conformational variations of both phosphodiesterase-5 and inhibitors provide the structural basis for the physiological effects of vardenafil and sildenafil. Mol. Pharmacol. 73, 104-110 (Pubitemid 350294201)
    • (2008) Molecular Pharmacology , vol.73 , Issue.1 , pp. 104-110
    • Wang, H.1    Ye, M.2    Robinson, H.3    Francis, S.H.4    Ke, H.5
  • 47
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • DOI 10.1126/science.1075762
    • Manning, G., Whyte, D. B., Martinez, R., Hunter, T., and Sudarsanam, S. (2002) The protein kinase complement of the human genome. Science 298, 1912-1934 (Pubitemid 35425239)
    • (2002) Science , vol.298 , Issue.5600 , pp. 1912-1934
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3    Hunter, T.4    Sudarsanam, S.5
  • 48
    • 1842609697 scopus 로고    scopus 로고
    • Evolution of the Multifunctional Protein Tyrosine Phosphatase Family
    • DOI 10.1093/molbev/msh055
    • Pils, B., and Schultz, J. (2004) Evolution of the multifunctional protein tyrosine phosphatase family. Mol. Biol. Evol. 21, 625-631 (Pubitemid 38452095)
    • (2004) Molecular Biology and Evolution , vol.21 , Issue.4 , pp. 625-631
    • Pils, B.1    Schultz, J.2
  • 49
    • 79953269767 scopus 로고    scopus 로고
    • Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling
    • Zettl, M., Adrain, C., Strisovsky, K., Lastun, V., and Freeman, M. (2011) Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling. Cell 145, 79-91
    • (2011) Cell , vol.145 , pp. 79-91
    • Zettl, M.1    Adrain, C.2    Strisovsky, K.3    Lastun, V.4    Freeman, M.5
  • 50
    • 76049128717 scopus 로고    scopus 로고
    • Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3
    • Jura, N., Shan, Y., Cao, X., Shaw, D. E., and Kuriyan, J. (2009) Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3. Proc. Natl. Acad. Sci. U.S.A. 106, 21608-21613
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 21608-21613
    • Jura, N.1    Shan, Y.2    Cao, X.3    Shaw, D.E.4    Kuriyan, J.5
  • 51
    • 2942700177 scopus 로고    scopus 로고
    • Inactive enzyme-homologues find new function in regulatory processes
    • DOI 10.1016/j.jmb.2004.04.063, PII S0022283604005248
    • Pils, B., and Schultz, J. (2004) Inactive enzyme-homologues find new function in regulatory processes. J. Mol. Biol. 340, 399-404 (Pubitemid 38797988)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.3 , pp. 399-404
    • Pils, B.1    Schultz, J.2
  • 52
    • 57049103481 scopus 로고    scopus 로고
    • Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity
    • Wang, H., Yan, Z., Yang, S., Cai, J., Robinson, H., and Ke, H. (2008) Kinetic and structural studies of phosphodiesterase-8A and implication on the inhibitor selectivity. Biochemistry 47, 12760-12768
    • (2008) Biochemistry , vol.47 , pp. 12760-12768
    • Wang, H.1    Yan, Z.2    Yang, S.3    Cai, J.4    Robinson, H.5    Ke, H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.