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Volumn , Issue , 2009, Pages 11-38

Target Profiling of Small Molecules

Author keywords

Qualitative and semiquantitative interaction screening methodologies; SM interaction profiling experimental approaches; Small molecules (SMs) vital in regulatory and neuronal networks

Indexed keywords


EID: 84890768846     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470495018.ch2     Document Type: Chapter
Times cited : (1)

References (62)
  • 2
    • 33846288924 scopus 로고    scopus 로고
    • Multiplexing molecular diagnostics and immunoassays using emerging microarray technologies
    • Ling, M. M., Ricks, C., Lea, P. (2007). Multiplexing molecular diagnostics and immunoassays using emerging microarray technologies. Expert Rev. Mol. Diagn., 7, 87-98.
    • (2007) Expert Rev. Mol. Diagn., , vol.7 , pp. 87-98
    • Ling, M.M.1    Ricks, C.2    Lea, P.3
  • 4
    • 35448962899 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions
    • Freyer, M. W., Lewis, E. A. (2008). Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions. Methods Cell Biol., 84, 79-113.
    • (2008) Methods Cell Biol., , vol.84 , pp. 79-113
    • Freyer, M.W.1    Lewis, E.A.2
  • 5
    • 0034012952 scopus 로고    scopus 로고
    • Biosensor chip mass spectrometry: a chip-based proteomics approach
    • Nelson, R. W., Nedelkov, D., Tubbs, K. A. (2000). Biosensor chip mass spectrometry: a chip-based proteomics approach. Electrophoresis, 21, 1155-1163.
    • (2000) Electrophoresis, , vol.21 , pp. 1155-1163
    • Nelson, R.W.1    Nedelkov, D.2    Tubbs, K.A.3
  • 6
    • 0037016352 scopus 로고    scopus 로고
    • A scintillation proximity assay for studying inhibitors of human tau protein kinase II/cdk5 using a 96-well format
    • Evans, D. B., Rank, K. B., Sharma, S. K. (2002). A scintillation proximity assay for studying inhibitors of human tau protein kinase II/cdk5 using a 96-well format. J. Biochem. Biophys. Methods, 50, 151-161.
    • (2002) J. Biochem. Biophys. Methods, , vol.50 , pp. 151-161
    • Evans, D.B.1    Rank, K.B.2    Sharma, S.K.3
  • 7
    • 14844329503 scopus 로고    scopus 로고
    • A Drosophila proteininteraction map centered on cell-cycle regulators
    • Stanyon, C. A., Liu, G., Mangiola, B. A., et al. (2004). A Drosophila proteininteraction map centered on cell-cycle regulators. Genome Biol., 5, R96.
    • (2004) Genome Biol., , vol.5
    • Stanyon, C.A.1    Liu, G.2    Mangiola, B.A.3
  • 8
    • 33746753342 scopus 로고    scopus 로고
    • Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast
    • Parsons, A. B., Lopez, A., Givoni, I. E., et al. (2006). Exploring the mode-of-action of bioactive compounds by chemical-genetic profiling in yeast. Cell, 126, 611-625.
    • (2006) Cell, , vol.126 , pp. 611-625
    • Parsons, A.B.1    Lopez, A.2    Givoni, I.E.3
  • 9
    • 1542290057 scopus 로고    scopus 로고
    • A three-hybrid approach to scanning the proteome for targets of small molecule kinase inhibitors
    • Becker, F., Murthi, K., Smith, C., et al. (2004). A three-hybrid approach to scanning the proteome for targets of small molecule kinase inhibitors. Chem. Biol., 11, 211-223.
    • (2004) Chem. Biol., , vol.11 , pp. 211-223
    • Becker, F.1    Murthi, K.2    Smith, C.3
  • 11
    • 9144268287 scopus 로고    scopus 로고
    • Chemogenomic profiling: identifying the functional interactions of small molecules in yeast
    • Giaever, G., Flaherty, P., Kumm, J., et al. (2004). Chemogenomic profiling: identifying the functional interactions of small molecules in yeast. Proc. Natl. Acad. Sci. USA, 101, 793-798.
    • (2004) Proc. Natl. Acad. Sci. USA, , vol.101 , pp. 793-798
    • Giaever, G.1    Flaherty, P.2    Kumm, J.3
  • 12
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature, 340, 245-246.
    • (1989) Nature, , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 14
    • 33646874523 scopus 로고    scopus 로고
    • Two-hybrid protein-protein interaction analysis in Arabidopsis protoplasts: establishment of a heterodimerization map of group C and group S bZIP transcription factors
    • Ehlert, A., Weltmeier, F., Wang, X., et al. (2006). Two-hybrid protein-protein interaction analysis in Arabidopsis protoplasts: establishment of a heterodimerization map of group C and group S bZIP transcription factors. Plant J., 46, 890-900.
    • (2006) Plant J., , vol.46 , pp. 890-900
    • Ehlert, A.1    Weltmeier, F.2    Wang, X.3
  • 15
    • 0029824170 scopus 로고    scopus 로고
    • A three-hybrid system for detecting small ligand-protein receptor interactions
    • Licitra, E. J., Liu, J. O. (1996). A three-hybrid system for detecting small ligand-protein receptor interactions. Proc. Natl. Acad. Sci. USA, 93, 12817-12821.
    • (1996) Proc. Natl. Acad. Sci. USA, , vol.93 , pp. 12817-12821
    • Licitra, E.J.1    Liu, J.O.2
  • 16
    • 0036569568 scopus 로고    scopus 로고
    • A GAL4-based yeast three-hybrid system for the identification of small molecule-target protein interactions
    • Henthorn, D. C., Jaxa-Chamiec, A. A., Meldrum, E. (2002). A GAL4-based yeast three-hybrid system for the identification of small molecule-target protein interactions. Biochem. Pharmacol., 63, 1619-1628.
    • (2002) Biochem. Pharmacol., , vol.63 , pp. 1619-1628
    • Henthorn, D.C.1    Jaxa-Chamiec, A.A.2    Meldrum, E.3
  • 18
    • 0033048778 scopus 로고    scopus 로고
    • Genomic profiling of drug sensitivities via induced haploinsufficiency
    • Giaever, G., Shoemaker, D. D., Jones, T. W., et al. (1999). Genomic profiling of drug sensitivities via induced haploinsufficiency. Nat. Genet., 21, 278-283.
    • (1999) Nat. Genet., , vol.21 , pp. 278-283
    • Giaever, G.1    Shoemaker, D.D.2    Jones, T.W.3
  • 19
    • 10744225364 scopus 로고    scopus 로고
    • Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes
    • Lum, P. Y., Armour, C. D., Stepaniants, S. B., et al. (2004). Discovering modes of action for therapeutic compounds using a genome-wide screen of yeast heterozygotes. Cell, 116, 121-137.
    • (2004) Cell, , vol.116 , pp. 121-137
    • Lum, P.Y.1    Armour, C.D.2    Stepaniants, S.B.3
  • 20
    • 34447556014 scopus 로고    scopus 로고
    • Chemical proteomics for drug discovery based on compound-immobilized affinity chromatography
    • Katayama, H., Oda, Y. (2007). Chemical proteomics for drug discovery based on compound-immobilized affinity chromatography. J. Chromatogr. B, 855, 21-27.
    • (2007) J. Chromatogr. B, , vol.855 , pp. 21-27
    • Katayama, H.1    Oda, Y.2
  • 21
    • 33847628853 scopus 로고    scopus 로고
    • Automated multiple ligand screening by frontal affinity chromatography- mass spectrometry (FAC-MS)
    • Ng, W., Dai, J. R., Slon-Usakiewicz, J. J., Redden, P. R., Pasternak, A., Reid, N. (2007). Automated multiple ligand screening by frontal affinity chromatography- mass spectrometry (FAC-MS). J. Biomol. Screen., 12, 167-174.
    • (2007) J. Biomol. Screen., , vol.12 , pp. 167-174
    • Ng, W.1    Dai, J.R.2    Slon-Usakiewicz, J.J.3    Redden, P.R.4    Pasternak, A.5    Reid, N.6
  • 22
    • 42949096479 scopus 로고    scopus 로고
    • Assaying small-molecule-receptor interactions by continuous flow competitive displacement chromatography/mass spectrometry
    • Sharma, J., Besanger, T. R., Brennan, J. D. (2008). Assaying small-molecule-receptor interactions by continuous flow competitive displacement chromatography/mass spectrometry. Anal. Chem., 80, 3213-3220.
    • (2008) Anal. Chem., , vol.80 , pp. 3213-3220
    • Sharma, J.1    Besanger, T.R.2    Brennan, J.D.3
  • 23
    • 34447498398 scopus 로고    scopus 로고
    • A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions
    • Cooper, M. A., Singleton, V. T. (2007). A survey of the 2001 to 2005 quartz crystal microbalance biosensor literature: applications of acoustic physics to the analysis of biomolecular interactions. J. Mol. Recognit., 20, 154-184.
    • (2007) J. Mol. Recognit., , vol.20 , pp. 154-184
    • Cooper, M.A.1    Singleton, V.T.2
  • 24
    • 1542315193 scopus 로고    scopus 로고
    • Direct monitoring of enzymatic glucan hydrolysis on a 27-MHz quartz-crystal microbalance
    • Nishino, H., Nihira, T., Mori, T., Okahata, Y. (2004). Direct monitoring of enzymatic glucan hydrolysis on a 27-MHz quartz-crystal microbalance. J. Am. Chem. Soc., 126, 2264-2265.
    • (2004) J. Am. Chem. Soc., , vol.126 , pp. 2264-2265
    • Nishino, H.1    Nihira, T.2    Mori, T.3    Okahata, Y.4
  • 25
    • 33847377003 scopus 로고    scopus 로고
    • Profiling of molecular interactions in real time using acoustic detection
    • Godber, B., Frogley, M., Rehak, M., et al. (2007). Profiling of molecular interactions in real time using acoustic detection. Biosens. Bioelectron., 22, 2382-2386.
    • (2007) Biosens. Bioelectron., , vol.22 , pp. 2382-2386
    • Godber, B.1    Frogley, M.2    Rehak, M.3
  • 26
    • 33845540132 scopus 로고    scopus 로고
    • Rapid and simultaneous quantification of four urinary proteins by piezoelectric quartz crystal microbalance immunosensor array
    • Luo, Y., Chen, M., Wen, Q., et al. (2006). Rapid and simultaneous quantification of four urinary proteins by piezoelectric quartz crystal microbalance immunosensor array. Clin. Chem., 52, 2273-2280.
    • (2006) Clin. Chem., , vol.52 , pp. 2273-2280
    • Luo, Y.1    Chen, M.2    Wen, Q.3
  • 27
    • 41549137931 scopus 로고    scopus 로고
    • Electrochemical biosensors: sensor principles and architectures
    • Grieshaber, D., MacKenzie, R., Vörös, J., Reimhult, E. (2008). Electrochemical biosensors: sensor principles and architectures. Sensors, 8, 1400-1458.
    • (2008) Sensors, , vol.8 , pp. 1400-1458
    • Grieshaber, D.1    MacKenzie, R.2    Vörös, J.3    Reimhult, E.4
  • 28
    • 30744473476 scopus 로고    scopus 로고
    • Reagentless, reusable, ultrasensitive electrochemical molecular beacon aptasensor
    • Radi, A. E., Acero Sánchez, J. L., Baldrich, E., O'Sullivan, C. K. (2006). Reagentless, reusable, ultrasensitive electrochemical molecular beacon aptasensor. J. Am. Chem. Soc., 128, 117-124.
    • (2006) J. Am. Chem. Soc., , vol.128 , pp. 117-124
    • Radi, A.E.1    Acero Sánchez, J.L.2    Baldrich, E.3    O'Sullivan, C.K.4
  • 29
    • 33845762941 scopus 로고    scopus 로고
    • Carbon nanotube multi-channeled field-effect transistors
    • Chen, C., Zhang, Y. (2006). Carbon nanotube multi-channeled field-effect transistors. J. Nanosci. Nanotechnol., 6, 3789-3793.
    • (2006) J. Nanosci. Nanotechnol., , vol.6 , pp. 3789-3793
    • Chen, C.1    Zhang, Y.2
  • 30
    • 41849092997 scopus 로고    scopus 로고
    • Use of photolithography to encode cell adhesive domains into protein microarrays
    • Lee, J. Y., Shah, S. S., Zimmer, C. C., Liu, G. Y., Revzin, A. (2008). Use of photolithography to encode cell adhesive domains into protein microarrays. Langmuir, 24, 2232-2239.
    • (2008) Langmuir, , vol.24 , pp. 2232-2239
    • Lee, J.Y.1    Shah, S.S.2    Zimmer, C.C.3    Liu, G.Y.4    Revzin, A.5
  • 31
    • 38149067498 scopus 로고    scopus 로고
    • An electrochemical impedance biosensor with aptamer-modified pyrolyzed carbon electrode for label-free protein detection
    • Lee, J. A., Hwang, S., Kwak, J., Park, S. I., Lee, S. S., Lee, K.-C. (2007). An electrochemical impedance biosensor with aptamer-modified pyrolyzed carbon electrode for label-free protein detection. Sens. Actuat. B, 1, 372-379.
    • (2007) Sens. Actuat. B, , vol.1 , pp. 372-379
    • Lee, J.A.1    Hwang, S.2    Kwak, J.3    Park, S.I.4    Lee, S.S.5    Lee, K.-C.6
  • 32
    • 38849093973 scopus 로고    scopus 로고
    • Electrical protein detection in cell lysates using high-density peptide-aptamer microarrays
    • Evans, D., Johnson, S., Laurenson, S., Davies, A. G., Ko Ferrigno, P., Wälti, C. (2008). Electrical protein detection in cell lysates using high-density peptide-aptamer microarrays. J. Biol., 7, 3.
    • (2008) J. Biol., , vol.7 , pp. 3
    • Evans, D.1    Johnson, S.2    Laurenson, S.3    Davies, A.G.4    Ko Ferrigno, P.5    Wälti, C.6
  • 33
    • 34547459511 scopus 로고    scopus 로고
    • Simultaneous quartz crystal microbalance-electrochemical impedance spectroscopy study on the adsorption of anti-human immunoglobulin G and its immunoreaction at nanomaterial-modified Au electrode surfaces
    • Jia, X., Xie, Q., Zhang, Y., Yao, S. (2007). Simultaneous quartz crystal microbalance-electrochemical impedance spectroscopy study on the adsorption of anti-human immunoglobulin G and its immunoreaction at nanomaterial-modified Au electrode surfaces. Anal. Sci., 23, 689-696.
    • (2007) Anal. Sci., , vol.23 , pp. 689-696
    • Jia, X.1    Xie, Q.2    Zhang, Y.3    Yao, S.4
  • 34
    • 34547103538 scopus 로고    scopus 로고
    • Potential of label-free detection in high-content-screening applications
    • Proll, G., Steinle, L., Pröll, F., et al. (2007). Potential of label-free detection in high-content-screening applications. J. Chromatogr. A, 1161, 2-8.
    • (2007) J. Chromatogr. A, , vol.1161 , pp. 2-8
    • Proll, G.1    Steinle, L.2    Pröll, F.3
  • 35
    • 23944480584 scopus 로고    scopus 로고
    • Reflectometric interference spectroscopy combined with MALDI-TOF mass spectrometry to determine quantitative and qualitative binding of mixtures of vancomycin derivatives
    • Mehlmann, M., Garvin, A. M., Steinwand, M., Gauglitz, G. (2005). Reflectometric interference spectroscopy combined with MALDI-TOF mass spectrometry to determine quantitative and qualitative binding of mixtures of vancomycin derivatives. Anal. Bioanal. Chem., 382, 1942-1948.
    • (2005) Anal. Bioanal. Chem., , vol.382 , pp. 1942-1948
    • Mehlmann, M.1    Garvin, A.M.2    Steinwand, M.3    Gauglitz, G.4
  • 36
    • 33750595486 scopus 로고    scopus 로고
    • Label-free detection methods for protein microarrays
    • Yu, X., Xu, D., Cheng, Q. (2006). Label-free detection methods for protein microarrays. Proteomics, 6, 5493-5503.
    • (2006) Proteomics, , vol.6 , pp. 5493-5503
    • Yu, X.1    Xu, D.2    Cheng, Q.3
  • 37
    • 37049019245 scopus 로고    scopus 로고
    • Extracting kinetic rate constants from surface plasmon resonance array systems
    • Rich, R. L., Cannon, M. J., Jenkins, J., et al. (2008). Extracting kinetic rate constants from surface plasmon resonance array systems. Anal. Biochem., 373, 112-120.
    • (2008) Anal. Biochem., , vol.373 , pp. 112-120
    • Rich, R.L.1    Cannon, M.J.2    Jenkins, J.3
  • 38
    • 21644470727 scopus 로고    scopus 로고
    • Detection and quantification of on-chip phosphorylated peptides by surface plasmon resonance imaging techniques using a phosphate capture molecule
    • Inamori, K., Kyo, M., Nishiya, Y., et al. (2005). Detection and quantification of on-chip phosphorylated peptides by surface plasmon resonance imaging techniques using a phosphate capture molecule. Anal. Chem., 77, 3979-3985.
    • (2005) Anal. Chem., , vol.77 , pp. 3979-3985
    • Inamori, K.1    Kyo, M.2    Nishiya, Y.3
  • 39
    • 33645286751 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging analysis of protein-protein interactions using on-chip-expressed capture protein
    • Kim, M., Park, K., Jeong, E. J., Shin, Y. B., Chung, B. H. (2006). Surface plasmon resonance imaging analysis of protein-protein interactions using on-chip-expressed capture protein. Anal. Biochem., 351, 298-304.
    • (2006) Anal. Biochem., , vol.351 , pp. 298-304
    • Kim, M.1    Park, K.2    Jeong, E.J.3    Shin, Y.B.4    Chung, B.H.5
  • 41
    • 84890715622 scopus 로고    scopus 로고
    • Generation of F(0)F(1)-ATPase nanoarray by dip-pen nanolithography and its application as biosensors
    • in press
    • Liu, X., Yue, J., Zhang, Z. (2008). Generation of F(0)F(1)-ATPase nanoarray by dip-pen nanolithography and its application as biosensors. Arch. Biochem. Biophys., (in press).
    • (2008) Arch. Biochem. Biophys.
    • Liu, X.1    Yue, J.2    Zhang, Z.3
  • 42
    • 0029008438 scopus 로고
    • Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector
    • Gershon, P. D., Khilko, S. (1995). Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance detector. J. Immunol. Methods, 183, 65-76.
    • (1995) J. Immunol. Methods, , vol.183 , pp. 65-76
    • Gershon, P.D.1    Khilko, S.2
  • 43
  • 44
    • 84890633398 scopus 로고    scopus 로고
    • Biacore.
    • Biacore. http://www.biacore.com/lifesciences/index.html.
  • 45
    • 84890686934 scopus 로고    scopus 로고
    • GWC Technologies, Inc.
    • GWC Technologies, Inc. http://www.gwctechnologies.com
  • 46
    • 84890709081 scopus 로고    scopus 로고
    • Lumera.
    • Lumera. http://www.lumera.com
  • 47
    • 33847051684 scopus 로고    scopus 로고
    • Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction
    • Yan, Y., Liu, Y., Sorci, M., et al. (2007). Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction. Biochemistry, 46, 1724-1731.
    • (2007) Biochemistry, , vol.46 , pp. 1724-1731
    • Yan, Y.1    Liu, Y.2    Sorci, M.3
  • 48
    • 0037173001 scopus 로고    scopus 로고
    • Kinetic analysis of estrogen receptor/ligand interactions
    • Rich, R. L., Hoth, L. R., Geoghegan, K. F., et al. (2002). Kinetic analysis of estrogen receptor/ligand interactions. Proc. Natl. Acad. Sci. USA, 99, 8562-8567.
    • (2002) Proc. Natl. Acad. Sci. USA, , vol.99 , pp. 8562-8567
    • Rich, R.L.1    Hoth, L.R.2    Geoghegan, K.F.3
  • 49
    • 28444469838 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors
    • Jung, S. O., Ro, H. S., Kho, B. H., Shin, Y. B., Kim, M. G., Chung, B. H. (2005). Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors. Proteomics, 5, 4427-4431.
    • (2005) Proteomics, , vol.5 , pp. 4427-4431
    • Jung, S.O.1    Ro, H.S.2    Kho, B.H.3    Shin, Y.B.4    Kim, M.G.5    Chung, B.H.6
  • 50
    • 43749113794 scopus 로고    scopus 로고
    • Rapid characterization of drug-drug interaction in plasma protein binding using a surface plasmon resonance biosensor
    • Kuroda, Y., Saito, M., Sakai, H., Yamaoka, T. (2008). Rapid characterization of drug-drug interaction in plasma protein binding using a surface plasmon resonance biosensor. Drug Metab. Pharmacokinet., 23, 120-127.
    • (2008) Drug Metab. Pharmacokinet., , vol.23 , pp. 120-127
    • Kuroda, Y.1    Saito, M.2    Sakai, H.3    Yamaoka, T.4
  • 51
    • 37549010341 scopus 로고    scopus 로고
    • Survey of the year 2006 commercial optical biosensor literature
    • Rich, R. L., Myszka, D. G. (2007). Survey of the year 2006 commercial optical biosensor literature. J. Mol. Recognit., 20, 300-366.
    • (2007) J. Mol. Recognit., , vol.20 , pp. 300-366
    • Rich, R.L.1    Myszka, D.G.2
  • 54
    • 21044444449 scopus 로고    scopus 로고
    • Pocketome via comprehensive identification and classification of ligand binding envelopes
    • An, J., Totrov, M., Abagyan, R. (2005). Pocketome via comprehensive identification and classification of ligand binding envelopes. Mol. Cell. Proteom., 4, 752-761.
    • (2005) Mol. Cell. Proteom., , vol.4 , pp. 752-761
    • An, J.1    Totrov, M.2    Abagyan, R.3
  • 55
    • 34447617178 scopus 로고    scopus 로고
    • Using structural motif descriptors for sequence-based binding site prediction
    • Henschel, A., Winter, C., Kim, W. K., Schroeder, M. (2007). Using structural motif descriptors for sequence-based binding site prediction. BMC Bioinformatics, 8 (Suppl. 4), S5.
    • (2007) BMC Bioinformatics , vol.8 , Issue.SUPPL 4
    • Henschel, A.1    Winter, C.2    Kim, W.K.3    Schroeder, M.4
  • 56
    • 18744394070 scopus 로고    scopus 로고
    • Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites
    • Laurie, A. T., Jackson, R. M. (2005). Q-SiteFinder: an energy-based method for the prediction of protein-ligand binding sites. Bioinformatics, 21, 1908-1916.
    • (2005) Bioinformatics, , vol.21 , pp. 1908-1916
    • Laurie, A.T.1    Jackson, R.M.2
  • 57
    • 84890638047 scopus 로고    scopus 로고
    • AutoDock.
    • AutoDock. http://autodock.scripps.edu/
  • 58
    • 84890645743 scopus 로고    scopus 로고
    • GROMACS.
    • GROMACS. http://www.gromacs.org/
  • 59
    • 84890645055 scopus 로고    scopus 로고
    • M.O.E.
    • MOE. http://www.chemcomp.com/
  • 60
    • 3042806401 scopus 로고    scopus 로고
    • A detailed comparison of current docking and scoring methods on systems of pharmaceutical relevance
    • Perola, E., Walters, W. P., Charifson, P. S. (2004). A detailed comparison of current docking and scoring methods on systems of pharmaceutical relevance. Proteins, 56, 235-249.
    • (2004) Proteins, , vol.56 , pp. 235-249
    • Perola, E.1    Walters, W.P.2    Charifson, P.S.3
  • 62
    • 24044545913 scopus 로고    scopus 로고
    • CO: a chemical ontology for identification of functional groups and semantic comparison of small molecules
    • Feldman, H. J., Dumontier, M., Ling, S., Haider, N., Hogue, C. W. (2005). CO: a chemical ontology for identification of functional groups and semantic comparison of small molecules. FEBS Lett., 579, 4685-4691.
    • (2005) FEBS Lett., , vol.579 , pp. 4685-4691
    • Feldman, H.J.1    Dumontier, M.2    Ling, S.3    Haider, N.4    Hogue, C.W.5


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