메뉴 건너뛰기




Volumn 8, Issue 4, 2004, Pages 365-370

High-throughput docking as a source of novel drug leads

Author keywords

high throughput docking; high throughput screening; HTD; HTS; IMPDH; inosine 5 monophosphate dehydrogenase; MASC; Multiple Active Site Correction; PfDHFR; Plasmodium falciparum dihydrofolate reductase; SAR; structure activity relationship; VS

Indexed keywords

BETA LACTAMASE INHIBITOR; CYCLOPHILIN; ENZYME INHIBITOR; INDOLE DERIVATIVE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE INHIBITOR; PYRIMIDINE; QUINAZOLINE DERIVATIVE;

EID: 3242884966     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2004.05.001     Document Type: Review
Times cited : (154)

References (51)
  • 1
    • 0036835460 scopus 로고    scopus 로고
    • Integration of virtual and high-throughput screening
    • Bajorath J. Integration of virtual and high-throughput screening. Nat Rev Drug Discov. 1:2002;882-894
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 882-894
    • Bajorath, J.1
  • 3
    • 1542635664 scopus 로고    scopus 로고
    • Retrospect and prospect of virtual screening in drug discovery
    • Xu H., Agrafiotis D.K. Retrospect and prospect of virtual screening in drug discovery. Curr Top Med Chem. 2:2002;1305-1320
    • (2002) Curr Top Med Chem , vol.2 , pp. 1305-1320
    • Xu, H.1    Agrafiotis, D.K.2
  • 4
    • 3242888975 scopus 로고    scopus 로고
    • Integrating virtual screening in lead discovery
    • in press.
    • Oprea TI, Matter H: Integrating virtual screening in lead discovery. Curr Opin Chem Biol 2004, 8:in press.
    • Curr Opin Chem Biol 2004 , pp. 8
    • Oprea, T.I.1    Matter, H.2
  • 5
    • 84892166712 scopus 로고
    • Einfluss der Configuration auf die wirkung der Enzyme
    • Fischer E. Einfluss der Configuration auf die wirkung der Enzyme. Ber Dt Chem Ges. 27:1894;2985-2993
    • (1894) Ber Dt Chem Ges , vol.27 , pp. 2985-2993
    • Fischer, E.1
  • 6
    • 0042353897 scopus 로고    scopus 로고
    • Molecular recognition and docking algorithms
    • An outstanding review on most of the technical aspects of molecular docking.
    • Brooijmans N., Kuntz I.D. Molecular recognition and docking algorithms. Annu Rev Biophys Biomol Struct. 32:2003;335-373 An outstanding review on most of the technical aspects of molecular docking.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 335-373
    • Brooijmans, N.1    Kuntz, I.D.2
  • 7
    • 0037262054 scopus 로고    scopus 로고
    • Ligand-protein docking: Cancer research at the interface between biology and chemistry
    • Glen R.C., Allen S.C. Ligand-protein docking: cancer research at the interface between biology and chemistry. Curr Med Chem. 10:2003;763-777
    • (2003) Curr Med Chem , vol.10 , pp. 763-777
    • Glen, R.C.1    Allen, S.C.2
  • 8
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: An overview of search algorithms and a guide to scoring functions
    • Halperin I., Ma B., Wolfson H., Nussinov R. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins. 47:2002;409-443
    • (2002) Proteins , vol.47 , pp. 409-443
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 9
    • 0037763817 scopus 로고    scopus 로고
    • Comparative evaluation of 11 scoring functions for molecular docking
    • Wang R., Lu Y., Wang S. Comparative evaluation of 11 scoring functions for molecular docking. J Med Chem. 46:2003;2287-2303
    • (2003) J Med Chem , vol.46 , pp. 2287-2303
    • Wang, R.1    Lu, Y.2    Wang, S.3
  • 10
    • 2942564021 scopus 로고    scopus 로고
    • Pursuing the leadlikeness concept in pharmaceutical research
    • in press.
    • Hann M, Oprea TI: Pursuing the leadlikeness concept in pharmaceutical research. Curr Opin Chem Biol 2004, 8:in press.
    • (2004) Curr Opin Chem Biol , pp. 8
    • Hann, M.1    Oprea, T.I.2
  • 11
    • 0035438391 scopus 로고    scopus 로고
    • Is there a difference between leads and drugs? a historical perspective
    • Oprea T.I., Davis A.M., Teague S.J., Leeson P.D. Is there a difference between leads and drugs? A historical perspective. J Chem Inf Comput Sci. 41:2001;1308-1315
    • (2001) J Chem Inf Comput Sci , vol.41 , pp. 1308-1315
    • Oprea, T.I.1    Davis, A.M.2    Teague, S.J.3    Leeson, P.D.4
  • 12
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski C.A., Lombardo F., Dominy B.W., Feeney P.J. Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings. Adv Drug Deliv Rev. 46:1997;3-26
    • (1997) Adv Drug Deliv Rev , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 13
    • 0038792292 scopus 로고    scopus 로고
    • Discovery of a potent and selective protein kinase CK2 inhibitor by high-throughput docking
    • Vangrevelinghe E., Zimmermann K., Schoepfer J., Portmann R., Fabbro D., Furet P. Discovery of a potent and selective protein kinase CK2 inhibitor by high-throughput docking. J Med Chem. 46:2003;2656-2662
    • (2003) J Med Chem , vol.46 , pp. 2656-2662
    • Vangrevelinghe, E.1    Zimmermann, K.2    Schoepfer, J.3    Portmann, R.4    Fabbro, D.5    Furet, P.6
  • 14
    • 0035025191 scopus 로고    scopus 로고
    • DOCK 4.0: Search strategies for automated molecular docking of flexible molecule databases
    • Ewing T.J., Makino S., Skillman A.G., Kuntz I.D. DOCK 4.0: search strategies for automated molecular docking of flexible molecule databases. J Comput Aided Mol Des. 15:2001;411-428
    • (2001) J Comput Aided Mol des , vol.15 , pp. 411-428
    • Ewing, T.J.1    Makino, S.2    Skillman, A.G.3    Kuntz, I.D.4
  • 15
    • 0346214475 scopus 로고    scopus 로고
    • Discovery of a novel family of CDK inhibitors with the program LIDAEUS: Structural basis for ligand-induced disordering of the activation loop
    • Wu S.Y., McNae I., Kontopidis G., McClue S.J., McInnes C., Stewart K.J., Wang S., Zheleva D.I., Marriage H., Lane D.P., et al. Discovery of a novel family of CDK inhibitors with the program LIDAEUS: structural basis for ligand-induced disordering of the activation loop. Structure. 11:2003;399-410
    • (2003) Structure , vol.11 , pp. 399-410
    • Wu, S.Y.1    McNae, I.2    Kontopidis, G.3    McClue, S.J.4    McInnes, C.5    Stewart, K.J.6    Wang, S.7    Zheleva, D.I.8    Marriage, H.9    Lane, D.P.10
  • 16
    • 0036076470 scopus 로고    scopus 로고
    • Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase
    • Powers R.A., Morandi F., Shoichet B.K. Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase. Structure (Camb). 10:2002;1013-1023
    • (2002) Structure (Camb) , vol.10 , pp. 1013-1023
    • Powers, R.A.1    Morandi, F.2    Shoichet, B.K.3
  • 17
    • 0037493019 scopus 로고    scopus 로고
    • Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough
    • The authors went through significant effort to validate the hits from the virtual screen, eliminating the possibility that the inhibition observed is due to a spurious mechanism.
    • Soelaiman S., Wei B.Q., Bergson P., Lee Y.S., Shen Y., Mrksich M., Shoichet B.K., Tang W.J. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. J Biol Chem. 278:2003;25990-25997 The authors went through significant effort to validate the hits from the virtual screen, eliminating the possibility that the inhibition observed is due to a spurious mechanism.
    • (2003) J Biol Chem , vol.278 , pp. 25990-25997
    • Soelaiman, S.1    Wei, B.Q.2    Bergson, P.3    Lee, Y.S.4    Shen, Y.5    Mrksich, M.6    Shoichet, B.K.7    Tang, W.J.8
  • 18
    • 0031965676 scopus 로고    scopus 로고
    • Flexible ligand docking using conformational ensembles
    • Lorber D.M., Shoichet B.K. Flexible ligand docking using conformational ensembles. Protein Sci. 7:1998;938-950
    • (1998) Protein Sci , vol.7 , pp. 938-950
    • Lorber, D.M.1    Shoichet, B.K.2
  • 19
    • 0037431421 scopus 로고    scopus 로고
    • Kinase inhibitors: Not just for kinases anymore
    • McGovern S.L., Shoichet B.K. Kinase inhibitors: not just for kinases anymore. J Med Chem. 46:2003;1478-1483
    • (2003) J Med Chem , vol.46 , pp. 1478-1483
    • McGovern, S.L.1    Shoichet, B.K.2
  • 20
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • McGovern S.L., Caselli E., Grigorieff N., Shoichet B.K. A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening. J Med Chem. 45:2002;1712-1722
    • (2002) J Med Chem , vol.45 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 21
    • 0141923641 scopus 로고    scopus 로고
    • Identification and prediction of promiscuous aggregating inhibitors among known drugs
    • Seidler J., McGovern S.L., Doman T.N., Shoichet B.K. Identification and prediction of promiscuous aggregating inhibitors among known drugs. J Med Chem. 46:2003;4477-4486
    • (2003) J Med Chem , vol.46 , pp. 4477-4486
    • Seidler, J.1    McGovern, S.L.2    Doman, T.N.3    Shoichet, B.K.4
  • 22
    • 0141792701 scopus 로고    scopus 로고
    • A specific mechanism of nonspecific inhibition
    • A continuation of the characterization of non-specific inhibition (also see [18]). The addition of detergent reverses the action of inhibitory aggregates, providing a simple and practical solution to reducing the number of false positives found by HTS and VS.
    • McGovern S.L., Helfand B.T., Feng B., Shoichet B.K. A specific mechanism of nonspecific inhibition. J Med Chem. 46:2003;4265-4272 A continuation of the characterization of non-specific inhibition (also see [18]). The addition of detergent reverses the action of inhibitory aggregates, providing a simple and practical solution to reducing the number of false positives found by HTS and VS.
    • (2003) J Med Chem , vol.46 , pp. 4265-4272
    • McGovern, S.L.1    Helfand, B.T.2    Feng, B.3    Shoichet, B.K.4
  • 24
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using an incremental construction algorithm
    • Rarey M., Kramer B., Lengauer T., Klebe G. A fast flexible docking method using an incremental construction algorithm. J Mol Biol. 261:1996;470-489
    • (1996) J Mol Biol , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 25
    • 0035966871 scopus 로고    scopus 로고
    • Detailed analysis of scoring functions for virtual screening
    • Stahl M., Rarey M. Detailed analysis of scoring functions for virtual screening. J Med Chem. 44:2001;1035-1042
    • (2001) J Med Chem , vol.44 , pp. 1035-1042
    • Stahl, M.1    Rarey, M.2
  • 26
    • 0345269288 scopus 로고    scopus 로고
    • Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis
    • Brenk R., Naerum L., Gradler U., Gerber H-D., Garcia G.A., Reuter K., Stubbs M.T., Klebe G. Virtual screening for submicromolar leads of tRNA-guanine transglycosylase based on a new unexpected binding mode detected by crystal structure analysis. J Med Chem. 46:2003;1133-1143
    • (2003) J Med Chem , vol.46 , pp. 1133-1143
    • Brenk, R.1    Naerum, L.2    Gradler, U.3    Gerber, H.-D.4    Garcia, G.A.5    Reuter, K.6    Stubbs, M.T.7    Klebe, G.8
  • 29
    • 0037784010 scopus 로고    scopus 로고
    • Docking and database screening reveal new classes of Plasmodium falciparum dihydrofolate reductase inhibitors
    • Rastelli G., Pacchioni S., Sirawaraporn W., Sirawaraporn R., Parenti M.D., Ferrari A.M. Docking and database screening reveal new classes of Plasmodium falciparum dihydrofolate reductase inhibitors. J Med Chem. 46:2003;2834-2845
    • (2003) J Med Chem , vol.46 , pp. 2834-2845
    • Rastelli, G.1    Pacchioni, S.2    Sirawaraporn, W.3    Sirawaraporn, R.4    Parenti, M.D.5    Ferrari, A.M.6
  • 31
    • 0036680063 scopus 로고    scopus 로고
    • Protein flexibility and drug design: How to hit a moving target
    • Carlson H.A. Protein flexibility and drug design: how to hit a moving target. Curr Opin Chem Biol. 6:2002;447-452
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 447-452
    • Carlson, H.A.1
  • 33
    • 0033576680 scopus 로고    scopus 로고
    • Consensus scoring: A method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins
    • Charifson P.S., Corkery J.J., Murcko M.A., Walters W.P. Consensus scoring: a method for obtaining improved hit rates from docking databases of three-dimensional structures into proteins. J Med Chem. 42:1999;5100-5109
    • (1999) J Med Chem , vol.42 , pp. 5100-5109
    • Charifson, P.S.1    Corkery, J.J.2    Murcko, M.A.3    Walters, W.P.4
  • 35
    • 0037208312 scopus 로고    scopus 로고
    • Consideration of molecular weight during compound selection in virtual target-based database screening
    • Pan Y., Huang N., Cho S., MacKerell A.D. Jr. Consideration of molecular weight during compound selection in virtual target-based database screening. J Chem Inf Comput Sci. 43:2003;267-272
    • (2003) J Chem Inf Comput Sci , vol.43 , pp. 267-272
    • Pan, Y.1    Huang, N.2    Cho, S.3    Mackerell Jr., A.D.4
  • 36
    • 0346731233 scopus 로고    scopus 로고
    • Multiple active site corrections for docking and virtual screening
    • Vigers G.P.A., Rizzi J.P. Multiple active site corrections for docking and virtual screening. J Med Chem. 47:2004;80-89
    • (2004) J Med Chem , vol.47 , pp. 80-89
    • Vigers, G.P.A.1    Rizzi, J.P.2
  • 37
    • 0037402105 scopus 로고    scopus 로고
    • Pharmacophore-based molecular docking to account for ligand flexibility
    • The authors describe a new method for HTD consisting of constrained rigid docking of conformer ensembles using theoretical pharmacophoric sites on the target protein, The method is extremely fast due to the efficient coverage of ligand conformer and orientational space.
    • Joseph-McCarthy D., Thomas B.E. IV, Belmarsh M., Moustakas D., Alvarez J.C. Pharmacophore-based molecular docking to account for ligand flexibility. Proteins. 51:2003;172-188 The authors describe a new method for HTD consisting of constrained rigid docking of conformer ensembles using theoretical pharmacophoric sites on the target protein, The method is extremely fast due to the efficient coverage of ligand conformer and orientational space.
    • (2003) Proteins , vol.51 , pp. 172-188
    • Joseph-Mccarthy, D.1    Thomas IV, B.E.2    Belmarsh, M.3    Moustakas, D.4    Alvarez, J.C.5
  • 38
    • 0025916872 scopus 로고
    • Functionality maps of binding sites: A multiple copy simultaneous search method
    • Miranker A., Karplus M. Functionality maps of binding sites: a multiple copy simultaneous search method. Proteins. 11:1991;29-34
    • (1991) Proteins , vol.11 , pp. 29-34
    • Miranker, A.1    Karplus, M.2
  • 39
    • 0037402655 scopus 로고    scopus 로고
    • Automated generation of MCSS-derived pharmacophoric DOCK site points for searching multiconformation databases
    • Joseph-McCarthy D., Alvarez J.C. Automated generation of MCSS-derived pharmacophoric DOCK site points for searching multiconformation databases. Proteins. 51:2003;189-202
    • (2003) Proteins , vol.51 , pp. 189-202
    • Joseph-Mccarthy, D.1    Alvarez, J.C.2
  • 40
    • 0027385177 scopus 로고
    • Matching chemistry and shape in molecular docking
    • Shoichet B.K., Kuntz I.D. Matching chemistry and shape in molecular docking. Protein Eng. 6:1993;723-732
    • (1993) Protein Eng , vol.6 , pp. 723-732
    • Shoichet, B.K.1    Kuntz, I.D.2
  • 41
    • 12444278563 scopus 로고    scopus 로고
    • Analysis and optimization of structure-based virtual screening protocols 2. Examination of docked ligand orientation sampling methodology: Mapping a pharmacophore for success
    • Good A.C., Cheney D.L., Sitkoff D.F., Tokarski J.S., Stouch T.R., Bassolino D.A., Krystek S.R., Yi L., Masonb J.S., Perkins T.D.J. Analysis and optimization of structure-based virtual screening protocols 2. Examination of docked ligand orientation sampling methodology: mapping a pharmacophore for success. J Mol Graph Model. 22:2003;31-40
    • (2003) J Mol Graph Model , vol.22 , pp. 31-40
    • Good, A.C.1    Cheney, D.L.2    Sitkoff, D.F.3    Tokarski, J.S.4    Stouch, T.R.5    Bassolino, D.A.6    Krystek, S.R.7    Yi, L.8    Masonb, J.S.9    Perkins, T.D.J.10
  • 42
    • 0347361642 scopus 로고    scopus 로고
    • Lessons in molecular recognition: The effects of ligand and protein flexibility on molecular docking accuracy
    • Erickson J.A., Jalaie M., Robertson D.H., Lewis R.A., Vieth M. Lessons in molecular recognition: the effects of ligand and protein flexibility on molecular docking accuracy. J Med Chem. 47:2004;45-55
    • (2004) J Med Chem , vol.47 , pp. 45-55
    • Erickson, J.A.1    Jalaie, M.2    Robertson, D.H.3    Lewis, R.A.4    Vieth, M.5
  • 43
    • 0037424605 scopus 로고    scopus 로고
    • Efficient conformational sampling of local side-chain flexibility
    • Kallblad P., Dean P.M. Efficient conformational sampling of local side-chain flexibility. J Mol Biol. 326:2003;1651-1665
    • (2003) J Mol Biol , vol.326 , pp. 1651-1665
    • Kallblad, P.1    Dean, P.M.2
  • 44
    • 0038460858 scopus 로고    scopus 로고
    • Information decay in molecular docking screens against holo, apo, and modeled conformations of enzymes
    • McGovern S.L., Shoichet B.K. Information decay in molecular docking screens against holo, apo, and modeled conformations of enzymes. J Med Chem. 46:2003;2895-2907
    • (2003) J Med Chem , vol.46 , pp. 2895-2907
    • McGovern, S.L.1    Shoichet, B.K.2
  • 45
    • 0037806022 scopus 로고    scopus 로고
    • Sensitivity of molecular docking to induced fit effects in influenza virus neuraminidase
    • An excellent study highlighting the sensitivity of docking methodologies to protein structure through cross-docking experiments.
    • Birch L., Murray C.W., Hartshorn M.J., Tickle I.J., Verdonk M.L. Sensitivity of molecular docking to induced fit effects in influenza virus neuraminidase. J Comput Aided Mol Des. 16:2002;855-869 An excellent study highlighting the sensitivity of docking methodologies to protein structure through cross-docking experiments.
    • (2002) J Comput Aided Mol des , vol.16 , pp. 855-869
    • Birch, L.1    Murray, C.W.2    Hartshorn, M.J.3    Tickle, I.J.4    Verdonk, M.L.5
  • 46
    • 0038336897 scopus 로고    scopus 로고
    • Application and limitations of X-ray crystallographic data in structure-based ligand and drug design
    • Davis A.M., Teague S.J., Kleywegt G.J. Application and limitations of X-ray crystallographic data in structure-based ligand and drug design. Angew Chem Int Ed Engl. 42:2003;2718-2736
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 2718-2736
    • Davis, A.M.1    Teague, S.J.2    Kleywegt, G.J.3
  • 47
    • 0034811498 scopus 로고    scopus 로고
    • Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA
    • Wang J., Morin P., Wang W., Kollman P.A. Use of MM-PBSA in reproducing the binding free energies to HIV-1 RT of TIBO derivatives and predicting the binding mode to HIV-1 RT of efavirenz by docking and MM-PBSA. J Am Chem Soc. 123:2001;5221-5230
    • (2001) J Am Chem Soc , vol.123 , pp. 5221-5230
    • Wang, J.1    Morin, P.2    Wang, W.3    Kollman, P.A.4
  • 48
    • 0037187412 scopus 로고    scopus 로고
    • Molecular dynamics and free energy analyses of cathepsin D-inhibitor interactions: Insight into structure-based ligand design
    • The authors use a molecular dynamics-based, continuum solvent method (MM-PBSA) to reproduce the experimental binding affinity for a set of seven inhibitors to cathepsin-D. The integration of these types of calculations into the HTD paradigm will significantly increase the accuracy of the methods.
    • Huo S., Wang J., Cieplak P., Kollman P.A., Kuntz I.D. Molecular dynamics and free energy analyses of cathepsin D-inhibitor interactions: insight into structure-based ligand design. J Med Chem. 45:2002;1412-1419 The authors use a molecular dynamics-based, continuum solvent method (MM-PBSA) to reproduce the experimental binding affinity for a set of seven inhibitors to cathepsin-D. The integration of these types of calculations into the HTD paradigm will significantly increase the accuracy of the methods.
    • (2002) J Med Chem , vol.45 , pp. 1412-1419
    • Huo, S.1    Wang, J.2    Cieplak, P.3    Kollman, P.A.4    Kuntz, I.D.5
  • 49
    • 0141545126 scopus 로고    scopus 로고
    • Identification of novel inhibitors of BCR-ABL tyrosine kinase via virtual screening
    • Peng H., Huang N., Qi J., Xie P., Xu C., Wang J., Yang C. Identification of novel inhibitors of BCR-ABL tyrosine kinase via virtual screening. Bioorg Med Chem Lett. 13:2003;3693-3699
    • (2003) Bioorg Med Chem Lett , vol.13 , pp. 3693-3699
    • Peng, H.1    Huang, N.2    Qi, J.3    Xie, P.4    Xu, C.5    Wang, J.6    Yang, C.7
  • 50
    • 0345099649 scopus 로고    scopus 로고
    • Structure-based discovery of potassium channel blockers from natural products: Virtual screening and electrophysiological assay testing
    • Liu H., Li Y., Song M., Tan X., Cheng F., Zheng S., Shen J., Luo X., Ji R., Yue J., et al. Structure-based discovery of potassium channel blockers from natural products: virtual screening and electrophysiological assay testing. Chem Biol. 10:2003;1103-1113
    • (2003) Chem Biol , vol.10 , pp. 1103-1113
    • Liu, H.1    Li, Y.2    Song, M.3    Tan, X.4    Cheng, F.5    Zheng, S.6    Shen, J.7    Luo, X.8    Ji, R.9    Yue, J.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.