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Volumn 61, Issue , 2004, Pages 97-126

Proteomic approaches in drug discovery and development

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER;

EID: 16544391825     PISSN: 00747742     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7742(04)61005-1     Document Type: Article
Times cited : (11)

References (101)
  • 1
    • 0037174635 scopus 로고    scopus 로고
    • Treatment of ischemic brain damage by perturbing NMDA receptor-PSD-95 protein interactions
    • Aarts, M., Liu, Y., Liu, L., Besshoh, S., Arundine, M., Gurd, J. W., Wang, Y. T., Salter, M. W., and Tymianski, M. (2002). Treatment of ischemic brain damage by perturbing NMDA receptor-PSD-95 protein interactions. Science 298(5594), 846-850.
    • (2002) Science , vol.298 , Issue.5594 , pp. 846-850
    • Aarts, M.1    Liu, Y.2    Liu, L.3    Besshoh, S.4    Arundine, M.5    Gurd, J.W.6    Wang, Y.T.7    Salter, M.W.8    Tymianski, M.9
  • 2
    • 0001426432 scopus 로고    scopus 로고
    • Chemical strategies for functional proteomics
    • Adam, G. C., Sorensen, E. J., and Cravatt, B. F. (2002a). Chemical strategies for functional proteomics. Mol. Cell Proteomics 1(10), 781-790.
    • (2002) Mol. Cell Proteomics , vol.1 , Issue.10 , pp. 781-790
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 3
    • 0036022519 scopus 로고    scopus 로고
    • Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype
    • Adam, G. C., Sorensen, E. J., and Cravatt, B. F. (2002b). Proteomic profiling of mechanistically distinct enzyme classes using a common chemotype. Nat. Biotechnol. 20(8), 805-809.
    • (2002) Nat. Biotechnol. , vol.20 , Issue.8 , pp. 805-809
    • Adam, G.C.1    Sorensen, E.J.2    Cravatt, B.F.3
  • 4
    • 0038488193 scopus 로고    scopus 로고
    • A mass spectrometric journey into protein and proteome research
    • Aebersold, R. (2003). A mass spectrometric journey into protein and proteome research. J. Am. Soc. Mass. Spectrom. 14, 685-695.
    • (2003) J. Am. Soc. Mass. Spectrom. , vol.14 , pp. 685-695
    • Aebersold, R.1
  • 6
    • 0037986653 scopus 로고    scopus 로고
    • A correlation between a proteomic evaluation and conventional measurements in the assessment of renal proximal tubular toxicity
    • Bandara, L. R., Kelly, M. D., Lock, E. A., and Kennedy, S. (2003). A correlation between a proteomic evaluation and conventional measurements in the assessment of renal proximal tubular toxicity. Toxicol. Sci. 73(1), 195-206.
    • (2003) Toxicol. Sci. , vol.73 , Issue.1 , pp. 195-206
    • Bandara, L.R.1    Kelly, M.D.2    Lock, E.A.3    Kennedy, S.4
  • 7
    • 0030045605 scopus 로고    scopus 로고
    • A protein linkage map of Escherichia coli bacteriophage T7
    • Bartel, P. L., Roecklein, J. A., SenGupta, D., and Fields, S. (1996). A protein linkage map of Escherichia coli bacteriophage T7. Nat. Genet. 12(1), 72-77.
    • (1996) Nat. Genet. , vol.12 , Issue.1 , pp. 72-77
    • Bartel, P.L.1    Roecklein, J.A.2    Sengupta, D.3    Fields, S.4
  • 8
    • 0028871458 scopus 로고
    • Chromogranin a in cerebrospinal fluid: A biochemical marker for synaptic degeneration in Alzheimer's disease?
    • Blennow, K., Davidsson, P., Wallin, A., and Ekman, R. (1995). Chromogranin A in cerebrospinal fluid: A biochemical marker for synaptic degeneration in Alzheimer's disease? Dementia 6(6), 306-311.
    • (1995) Dementia , vol.6 , Issue.6 , pp. 306-311
    • Blennow, K.1    Davidsson, P.2    Wallin, A.3    Ekman, R.4
  • 9
    • 0037434977 scopus 로고    scopus 로고
    • Biomedical informatics for proteomics
    • Boguski, M. S., and McIntosh, M. W. (2003). Biomedical informatics for proteomics. Nature 422(6928), 233-237.
    • (2003) Nature , vol.422 , Issue.6928 , pp. 233-237
    • Boguski, M.S.1    McIntosh, M.W.2
  • 10
    • 0036775490 scopus 로고    scopus 로고
    • Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family
    • Borodovsky, A., Ovaa, H., Kolli, N., Gan-Erdene, T., Wilkinson, K. D., Ploegh, H. L., and Kessler, B. M. (2002). Chemistry-based functional proteomics reveals novel members of the deubiquitinating enzyme family. Chem. Biol. 9(10), 1149-1159.
    • (2002) Chem. Biol. , vol.9 , Issue.10 , pp. 1149-1159
    • Borodovsky, A.1    Ovaa, H.2    Kolli, N.3    Gan-Erdene, T.4    Wilkinson, K.D.5    Ploegh, H.L.6    Kessler, B.M.7
  • 12
    • 0037208170 scopus 로고    scopus 로고
    • Application of chemometrics to 1H NMR spectroscopic data to investigate a relationship between human serum metabolic profiles and hypertension
    • Brindle, J. T., Nicholson, J. K., Schofield, P. M., Grainger, D. J., and Holmes, E. (2003). Application of chemometrics to 1H NMR spectroscopic data to investigate a relationship between human serum metabolic profiles and hypertension. Analyst 128(1), 32-36.
    • (2003) Analyst , vol.128 , Issue.1 , pp. 32-36
    • Brindle, J.T.1    Nicholson, J.K.2    Schofield, P.M.3    Grainger, D.J.4    Holmes, E.5
  • 13
    • 0034660083 scopus 로고    scopus 로고
    • Methods for projecting the incidence and prevalence of chronic diseases in aging populations: Application to Alzheimer's disease
    • Brookmeyer, R., and Gray, S. (2000). Methods for projecting the incidence and prevalence of chronic diseases in aging populations: Application to Alzheimer's disease. Stat. Med. 19(11-12), 1481-1493.
    • (2000) Stat. Med. , vol.19 , Issue.11-12 , pp. 1481-1493
    • Brookmeyer, R.1    Gray, S.2
  • 15
    • 0242391293 scopus 로고    scopus 로고
    • Application of random peptide phage display to the study of nuclear hormone receptors
    • Chang, C. Y., Norris, J. D. Jansen, M., Huang, H. J., and McDonnell, D. P. (2003). Application of random peptide phage display to the study of nuclear hormone receptors. Methods Enzymol. 364, 118-142.
    • (2003) Methods Enzymol. , vol.364 , pp. 118-142
    • Chang, C.Y.1    Norris, J.D.2    Jansen, M.3    Huang, H.J.4    McDonnell, D.P.5
  • 17
    • 0036802247 scopus 로고    scopus 로고
    • Imaging mass spectrometry. A new tool to investigate the spatial organization of peptides and proteins in mammalian tissue sections
    • Chaurand, P., Schwartz, S. A., and Caprioli, R. M. (2002). Imaging mass spectrometry. A new tool to investigate the spatial organization of peptides and proteins in mammalian tissue sections. Curr. Opin. Chem. Biol. 6(5), 676-681.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.5 , pp. 676-681
    • Chaurand, P.1    Schwartz, S.A.2    Caprioli, R.M.3
  • 18
    • 0019874210 scopus 로고
    • Towards a total human protein map
    • Clark, B. F. (1981). Towards a total human protein map. Nature 292(5823), 491-492.
    • (1981) Nature , vol.292 , Issue.5823 , pp. 491-492
    • Clark, B.F.1
  • 20
    • 0037374498 scopus 로고    scopus 로고
    • The price of innovation: New estimates of drug development costs
    • DiMasi, J. A., Hansen, R. W., and Grabowski, H. G. (2003). The price of innovation: New estimates of drug development costs. J. Health Econ. 22(2), 151-185.
    • (2003) J. Health Econ. , vol.22 , Issue.2 , pp. 151-185
    • Dimasi, J.A.1    Hansen, R.W.2    Grabowski, H.G.3
  • 22
    • 0035099794 scopus 로고    scopus 로고
    • A method for estimating progression rates in Alzheimer disease
    • Doody, R. S., Massman, P., and Dunn, J. K. (2001). A method for estimating progression rates in Alzheimer disease. Arch. Neurol. 58(3), 449-454.
    • (2001) Arch. Neurol. , vol.58 , Issue.3 , pp. 449-454
    • Doody, R.S.1    Massman, P.2    Dunn, J.K.3
  • 25
    • 0037607633 scopus 로고    scopus 로고
    • Informatics and data management in proteomics
    • Fenyo, D., and Beavis, R. C. (2002). Informatics and data management in proteomics. Trends Biotechnol. 20(Suppl. 12), S35-S38.
    • (2002) Trends Biotechnol. , vol.20 , Issue.SUPPL. 12
    • Fenyo, D.1    Beavis, R.C.2
  • 26
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature 340(6230), 245-246.
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 28
    • 0034647505 scopus 로고    scopus 로고
    • Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display
    • Fuh, G., Pisabarro, M. T., Li, Y., Quan, C., Lasky, L. A., and Sidhu, S. S. (2000). Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display. J. Biol. Chem. 275(28), 21486-21491.
    • (2000) J. Biol. Chem. , vol.275 , Issue.28 , pp. 21486-21491
    • Fuh, G.1    Pisabarro, M.T.2    Li, Y.3    Quan, C.4    Lasky, L.A.5    Sidhu, S.S.6
  • 29
    • 0036022528 scopus 로고    scopus 로고
    • "Fishing" for the functional proteome
    • Gerlt, J. A. (2002). "Fishing" for the functional proteome Nat. Biotechnol. 20(8), 786-787.
    • (2002) Nat. Biotechnol. , vol.20 , Issue.8 , pp. 786-787
    • Gerlt, J.A.1
  • 30
    • 0142138236 scopus 로고    scopus 로고
    • Metabonomics: NMR spectroscopy and pattern recognition analysis of body fluids and tissues for characterisation of xenobiotic toxicity and disease diagnosis
    • Griffin, J. L. (2003). Metabonomics: NMR spectroscopy and pattern recognition analysis of body fluids and tissues for characterisation of xenobiotic toxicity and disease diagnosis. Curr. Opin. Chem. Biol. 7(5), 648-654.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , Issue.5 , pp. 648-654
    • Griffin, J.L.1
  • 31
    • 1842430173 scopus 로고    scopus 로고
    • Defining a metabolic phenotype in the brain of a transgenic mouse model of spinocerebellar ataxia 3
    • Griffin, J. L., Cemal, C. K., and Pook, M. A. (2003). Defining a metabolic phenotype in the brain of a transgenic mouse model of spinocerebellar ataxia 3. Physiol. Genomics. 16, 16.
    • (2003) Physiol. Genomics , vol.16 , pp. 16
    • Griffin, J.L.1    Cemal, C.K.2    Pook, M.A.3
  • 33
    • 0033772588 scopus 로고    scopus 로고
    • Mass spectrometry and proteomics
    • Gygi, S. P., and Aebersold, R. (2000). Mass spectrometry and proteomics. Curr. Opin. Chem. Biol. 4(5), 489-494.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , Issue.5 , pp. 489-494
    • Gygi, S.P.1    Aebersold, R.2
  • 34
    • 0034662907 scopus 로고    scopus 로고
    • Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology
    • Gygi, S. P., Corthals, G. L., Zhang, Y., Rochon, Y., and Aebersold, R. (2000). Evaluation of two-dimensional gel electrophoresis-based proteome analysis technology. Proc. Natl. Acad. Sci. USA 97(17), 9390-9395.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.17 , pp. 9390-9395
    • Gygi, S.P.1    Corthals, G.L.2    Zhang, Y.3    Rochon, Y.4    Aebersold, R.5
  • 35
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi, S. P., Rist, B., Gerber, S. A., Turecek, F., Gelb, M. H., and Aebersold, R. (1999). Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol. 17(10), 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , Issue.10 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 36
    • 0242523659 scopus 로고    scopus 로고
    • Methods and applications of antibody microarrays in cancer research
    • Haab, B. B. (2003). Methods and applications of antibody microarrays in cancer research. Proteomics 3(11), 2116-2122.
    • (2003) Proteomics , vol.3 , Issue.11 , pp. 2116-2122
    • Haab, B.B.1
  • 37
  • 38
    • 0242523667 scopus 로고    scopus 로고
    • The emerging field of protein microarrays
    • Hanash, S. (2003). The emerging field of protein microarrays. Proteomics 3(11), 2075.
    • (2003) Proteomics , vol.3 , Issue.11 , pp. 2075
    • Hanash, S.1
  • 41
    • 0033499631 scopus 로고    scopus 로고
    • Phage display of cDNA repertoires: The pVI display system and its applications for the selection of immunogenic ligands
    • Hufton, S. E., Moerkerk, P. T., Meulemans, E. V., de Bruine, A., Arends, J. W., and Hoogenboom, H. R. (1999). Phage display of cDNA repertoires: The pVI display system and its applications for the selection of immunogenic ligands. J. Immunol. Methods 231(1-2), 39-51.
    • (1999) J. Immunol. Methods , vol.231 , Issue.1-2 , pp. 39-51
    • Hufton, S.E.1    Moerkerk, P.T.2    Meulemans, E.V.3    De Bruine, A.4    Arends, J.W.5    Hoogenboom, H.R.6
  • 43
    • 0142244518 scopus 로고    scopus 로고
    • Profiling of the cell surface proteome
    • Jang, J. H., and Hanash, S. (2003). Profiling of the cell surface proteome. Proteomics 3(10), 1947-1954.
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1947-1954
    • Jang, J.H.1    Hanash, S.2
  • 44
    • 0036795576 scopus 로고    scopus 로고
    • In vivo functional proteomics: Mammalian genome annotation using CD-tagging
    • 856, 858-860 passim
    • Jarvik, J. W., Fisher, G. W., Shi, C., Hennen, L., Hauser, C., Adler, S., and Berget, P. B. (2002). In vivo functional proteomics: Mammalian genome annotation using CD-tagging. Biotechniques 33(4), 852-854, 856, 858-860 passim.
    • (2002) Biotechniques , vol.33 , Issue.4 , pp. 852-854
    • Jarvik, J.W.1    Fisher, G.W.2    Shi, C.3    Hennen, L.4    Hauser, C.5    Adler, S.6    Berget, P.B.7
  • 46
    • 0036678119 scopus 로고    scopus 로고
    • Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness
    • Jessani, N., Liu, Y., Humphrey, M., and Cravatt, B. F. (2002). Enzyme activity profiles of the secreted and membrane proteome that depict cancer cell invasiveness. Proc. Natl. Acad. Sci. USA 99(16), 10335-10340.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.16 , pp. 10335-10340
    • Jessani, N.1    Liu, Y.2    Humphrey, M.3    Cravatt, B.F.4
  • 50
    • 0038746584 scopus 로고    scopus 로고
    • The role of chromogranin a and the control of secretory granule genesis and maturation
    • Kim, T., Tao-Cheng, J. H., Eiden, L. E., and Peng Loh, Y. (2003). The role of chromogranin A and the control of secretory granule genesis and maturation. Trends Endocrinol. Metab. 14(2), 56-57.
    • (2003) Trends Endocrinol. Metab. , vol.14 , Issue.2 , pp. 56-57
    • Kim, T.1    Tao-Cheng, J.H.2    Eiden, L.E.3    Peng Loh, Y.4
  • 51
    • 0016637146 scopus 로고
    • Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals
    • Klose, J. (1975). Protein mapping by combined isoelectric focusing and electrophoresis of mouse tissues. A novel approach to testing for induced point mutations in mammals. Humangenetik 26(3), 231-243.
    • (1975) Humangenetik , vol.26 , Issue.3 , pp. 231-243
    • Klose, J.1
  • 52
    • 0037306722 scopus 로고    scopus 로고
    • Activity-based proteomics: Enzyme chemistry redux
    • Kozarich, J. W. (2003). Activity-based proteomics: Enzyme chemistry redux. Curr. Opin. Chem. Biol. 7(1), 78-83.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , Issue.1 , pp. 78-83
    • Kozarich, J.W.1
  • 54
    • 0037709383 scopus 로고    scopus 로고
    • Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (QTRAP) used for high sensitivity proteomics applications
    • Le Blanc, J. C., Hager, J. W., Ilisiu, A. M., Hunter, C., Zhong, F., and Chu, I. (2003). Unique scanning capabilities of a new hybrid linear ion trap mass spectrometer (QTRAP) used for high sensitivity proteomics applications. Proteomics 3(6), 859-869.
    • (2003) Proteomics , vol.3 , Issue.6 , pp. 859-869
    • Le Blanc, J.C.1    Hager, J.W.2    Ilisiu, A.M.3    Hunter, C.4    Zhong, F.5    Chu, I.6
  • 56
    • 0043198426 scopus 로고    scopus 로고
    • Proteomic tools for quantitation by mass spectrometry
    • Lill, J. (2003). Proteomic tools for quantitation by mass spectrometry. Mass. Spectrom. Rev. 22(3), 182-194.
    • (2003) Mass. Spectrom. Rev. , vol.22 , Issue.3 , pp. 182-194
    • Lill, J.1
  • 57
    • 85016229161 scopus 로고    scopus 로고
    • Large-scale protein identification using mass spectrometry
    • Lin, D., Tabb, D. L., and Yates, J. R., III (2003). Large-scale protein identification using mass spectrometry. Biochim. Biophys. Acta. 1646, 1-10.
    • (2003) Biochim. Biophys. Acta. , vol.1646 , pp. 1-10
    • Lin, D.1    Tabb, D.L.2    Yates III, J.R.3
  • 59
    • 0037168784 scopus 로고    scopus 로고
    • Fine-needle, negative-pressure lumbar puncture: A safe technique for collecting CSF
    • Linker, G., Mirza, N., Meyer, M., Putnam, K. T., and Sunderland, T. (2002). Fine-needle, negative-pressure lumbar puncture: A safe technique for collecting CSF. Neurology 59(12), 2008-2009.
    • (2002) Neurology , vol.59 , Issue.12 , pp. 2008-2009
    • Linker, G.1    Mirza, N.2    Meyer, M.3    Putnam, K.T.4    Sunderland, T.5
  • 60
    • 0033593013 scopus 로고    scopus 로고
    • Activity-based protein profiling: The serine hydrolases
    • Liu, Y., Patricelli, M. P., and Cravatt, B. F. (1999). Activity-based protein profiling: The serine hydrolases. Proc. Natl. Acad. Sci. USA 96, 14964-14699.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14964-114699
    • Liu, Y.1    Patricelli, M.P.2    Cravatt, B.F.3
  • 61
    • 0036391485 scopus 로고    scopus 로고
    • Design and synthesis of class-selective activity probes for protein tyrosine phosphatases
    • Lo, L. C., Pang, T. L., Kuo, C. H., Chiang, Y. L., Wang, H. Y., and Lin, J. J. (2002). Design and synthesis of class-selective activity probes for protein tyrosine phosphatases. J. Proteome Res. 1(1), 35-40.
    • (2002) J. Proteome Res. , vol.1 , Issue.1 , pp. 35-40
    • Lo, L.C.1    Pang, T.L.2    Kuo, C.H.3    Chiang, Y.L.4    Wang, H.Y.5    Lin, J.J.6
  • 64
    • 0034712955 scopus 로고    scopus 로고
    • Genome-wide analysis of vaccinia virus protein-protein interactions
    • McCraith, S., Holtzman, T., Moss, B., and Fields, S. (2000). Genome-wide analysis of vaccinia virus protein-protein interactions. Proc. Natl. Acad. Sci. USA 97(9), 4879-4884.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.9 , pp. 4879-4884
    • McCraith, S.1    Holtzman, T.2    Moss, B.3    Fields, S.4
  • 65
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D., and Stadlan, E. M. (1984). Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology 34(7), 939-944.
    • (1984) Neurology , vol.34 , Issue.7 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 66
    • 0017696571 scopus 로고
    • High resolution two-dimensional electrophoresis of basic as well as acidic proteins
    • O'Farrell, P. Z., Goodman, H. M., and O'Farrell, P. H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12(4), 1133-1141.
    • (1977) Cell , vol.12 , Issue.4 , pp. 1133-1141
    • O'Farrell, P.Z.1    Goodman, H.M.2    O'Farrell, P.H.3
  • 67
    • 0037326081 scopus 로고    scopus 로고
    • Mass spectrometric-based approaches in quantitative proteomics
    • Ong, S. E., Foster, L. J., and Mann, M. (2003). Mass spectrometric-based approaches in quantitative proteomics. Methods 29, 124-130.
    • (2003) Methods , vol.29 , pp. 124-130
    • Ong, S.E.1    Foster, L.J.2    Mann, M.3
  • 69
    • 0035469599 scopus 로고    scopus 로고
    • Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active stie-directed probes
    • Patricelli, M. P., Giang, D. K., Stamp, L. M., and Burbaum, J. J. (2001). Direct visualization of serine hydrolase activities in complex proteomes using fluorescent active stie-directed probes. Proteomics 1, 1067-1071.
    • (2001) Proteomics , vol.1 , pp. 1067-1071
    • Patricelli, M.P.1    Giang, D.K.2    Stamp, L.M.3    Burbaum, J.J.4
  • 72
    • 0142121432 scopus 로고    scopus 로고
    • Trends in development and approval times for new therapeutics in the United States
    • Reichert, J. M. (2003). Trends in development and approval times for new therapeutics in the United States. Nat. Rev. Drug Discov. 2(9), 695-702.
    • (2003) Nat. Rev. Drug Discov. , vol.2 , Issue.9 , pp. 695-702
    • Reichert, J.M.1
  • 73
    • 0037277752 scopus 로고    scopus 로고
    • Drug metabolism and pharmacokinetics in drug discovery
    • Roberts, S. A. (2003). Drug metabolism and pharmacokinetics in drug discovery. Curr. Opin. Drug Discov. Devel. 6(1), 66-80.
    • (2003) Curr. Opin. Drug Discov. Devel. , vol.6 , Issue.1 , pp. 66-80
    • Roberts, S.A.1
  • 77
    • 0037416207 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations
    • Sekar, R. B., and Periasamy, A. (2003). Fluorescence resonance energy transfer (FRET) microscopy imaging of live cell protein localizations. J. Cell Biol. 160(5), 629-633.
    • (2003) J. Cell Biol. , vol.160 , Issue.5 , pp. 629-633
    • Sekar, R.B.1    Periasamy, A.2
  • 78
    • 0141991166 scopus 로고    scopus 로고
    • Yin and Yang: Complement activation and regulation in Alzheimer's disease
    • Shen, Y., and Meri, S. (2003). Yin and Yang: Complement activation and regulation in Alzheimer's disease. Prog. Neurobiol. 70(6), 463-472.
    • (2003) Prog. Neurobiol. , vol.70 , Issue.6 , pp. 463-472
    • Shen, Y.1    Meri, S.2
  • 79
    • 0037305940 scopus 로고    scopus 로고
    • Functional genomics of intracellular peptide recognition domains with combinatorial biology methods
    • Sidhu, S. S., Bader, G. D., and Boone, C. (2003). Functional genomics of intracellular peptide recognition domains with combinatorial biology methods. Curr. Opin. Chem. Biol. 7(1), 97-102.
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , Issue.1 , pp. 97-102
    • Sidhu, S.S.1    Bader, G.D.2    Boone, C.3
  • 80
  • 81
    • 0012618726 scopus 로고    scopus 로고
    • Trends in mass spectrometry instrumentation for proteomics
    • Smith, R. D. (2002). Trends in mass spectrometry instrumentation for proteomics. Trends Biotechnol. 20(Suppl. 12), S3-S7.
    • (2002) Trends Biotechnol. , vol.20 , Issue.SUPPL. 12
    • Smith, R.D.1
  • 82
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli, M., Chaurand, P., Hallahan, D. E., and Caprioli, R. M. (2001). Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues. Nat. Med. 7(4), 493-496.
    • (2001) Nat. Med. , vol.7 , Issue.4 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3    Caprioli, R.M.4
  • 83
    • 0036903299 scopus 로고    scopus 로고
    • Molecular imaging of amyloid beta peptides in mouse brain sections using mass spectrometry
    • Stoeckli, M., Staab, D., Staufenbiel, M., Wiederhold, K. H., and Signor, L. (2002). Molecular imaging of amyloid beta peptides in mouse brain sections using mass spectrometry. Anal. Biochem. 311(1), 33-39.
    • (2002) Anal. Biochem. , vol.311 , Issue.1 , pp. 33-39
    • Stoeckli, M.1    Staab, D.2    Staufenbiel, M.3    Wiederhold, K.H.4    Signor, L.5
  • 84
    • 0036624335 scopus 로고    scopus 로고
    • Large-scale open bioinformatics data resources
    • Stupka, E. (2002). Large-scale open bioinformatics data resources. Curr. Opin. Mol. Ther. 4(3), 265-274.
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , Issue.3 , pp. 265-274
    • Stupka, E.1
  • 86
    • 0142143227 scopus 로고    scopus 로고
    • Current developments in SELDI affinity technology
    • Tang, N., Tornatore, P., and Weinberger, S. R. (2004). Current developments in SELDI affinity technology. Mass. Spectrom. Rev. 23(1), 34-44.
    • (2004) Mass. Spectrom. Rev. , vol.23 , Issue.1 , pp. 34-44
    • Tang, N.1    Tornatore, P.2    Weinberger, S.R.3
  • 87
    • 0033953722 scopus 로고    scopus 로고
    • Three-year follow-up of cerebrospinal fluid tau, beta-amyloid 42 and 40 concentrations in Alzheimer's disease
    • Tapiola, T., Pirttila, T., Mikkonen, M., Mehta, P. D., Alafuzoff, I., Koivisto, K., and Soininen, H. (2000). Three-year follow-up of cerebrospinal fluid tau, beta-amyloid 42 and 40 concentrations in Alzheimer's disease. Neurosci. Lett. 280(2), 119-122.
    • (2000) Neurosci. Lett. , vol.280 , Issue.2 , pp. 119-122
    • Tapiola, T.1    Pirttila, T.2    Mikkonen, M.3    Mehta, P.D.4    Alafuzoff, I.5    Koivisto, K.6    Soininen, H.7
  • 88
    • 0037456743 scopus 로고    scopus 로고
    • The chromogranin-secretogranin family
    • Taupenot, L., Harper, K. L., and O'Connor, D. T. (2003). The chromogranin-secretogranin family. N. Engl. J. Med. 348(12), 1134-1149.
    • (2003) N. Engl. J. Med. , vol.348 , Issue.12 , pp. 1134-1149
    • Taupenot, L.1    Harper, K.L.2    O'Connor, D.T.3
  • 90
    • 0242608332 scopus 로고    scopus 로고
    • Protein microarrays: Promising tools for proteomic research
    • Templin, M. F., Stoll, D., Schwenk, J. M., Potz, O., Kramer, S., and Joos, T. O. (2003). Protein microarrays: Promising tools for proteomic research. Proteomics 3(11), 2155-2166.
    • (2003) Proteomics , vol.3 , Issue.11 , pp. 2155-2166
    • Templin, M.F.1    Stoll, D.2    Schwenk, J.M.3    Potz, O.4    Kramer, S.5    Joos, T.O.6
  • 91
    • 0035052023 scopus 로고    scopus 로고
    • Organic ion imaging of biological tissue with secondary ion mass spectrometry and matrix-assisted laser desorption/ionization
    • Todd, P. J., Schaaff, T. G., Chaurand, P., and Caprioli, R. M. (2001). Organic ion imaging of biological tissue with secondary ion mass spectrometry and matrix-assisted laser desorption/ionization. J. Mass. Spectrom. 36(4), 355-369.
    • (2001) J. Mass. Spectrom. , vol.36 , Issue.4 , pp. 355-369
    • Todd, P.J.1    Schaaff, T.G.2    Chaurand, P.3    Caprioli, R.M.4
  • 92
    • 0036469130 scopus 로고    scopus 로고
    • Two-hybrid arrays
    • Uetz, P. (2002). Two-hybrid arrays. Curr. Opin. Chem. Biol. 6(1), 57-62.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , Issue.1 , pp. 57-62
    • Uetz, P.1
  • 94
    • 0032610737 scopus 로고    scopus 로고
    • Generating a bacterial genome inventory. Identifying 2-D spots by comigrating products of the genome on 2-D gels
    • VanBogelen, R. A. (1999). Generating a bacterial genome inventory. Identifying 2-D spots by comigrating products of the genome on 2-D gels. Methods Mol. Biol. 112, 423-429.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 423-429
    • VanBogelen, R.A.1
  • 95
    • 0001818091 scopus 로고    scopus 로고
    • Yeast two-hybrid systems and protein interaction mapping projects for yeast and worm
    • Walhout, A. J., Boulton, S. J., and Vidal, M. (2000). Yeast two-hybrid systems and protein interaction mapping projects for yeast and worm. Yeast 17(2), 88-94.
    • (2000) Yeast , vol.17 , Issue.2 , pp. 88-94
    • Walhout, A.J.1    Boulton, S.J.2    Vidal, M.3
  • 96
    • 0036624293 scopus 로고    scopus 로고
    • Metabolomics and biochemical profiling in drug discovery and development
    • Watkins, S. M., and German, J. B. (2002). Metabolomics and biochemical profiling in drug discovery and development. Curr. Opin. Mol. Ther. 4(3), 224-228.
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , Issue.3 , pp. 224-228
    • Watkins, S.M.1    German, J.B.2
  • 97
    • 0033785587 scopus 로고    scopus 로고
    • Secretoneurin: A functional neuropeptide in health and disease
    • Wiedermann, C. J. (2000). Secretoneurin: A functional neuropeptide in health and disease. Peptides 21(8), 1289-1298.
    • (2000) Peptides , vol.21 , Issue.8 , pp. 1289-1298
    • Wiedermann, C.J.1
  • 99
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu, C. C., and Yates, J. R., 3rd (2003). The application of mass spectrometry to membrane proteomics. Nat. Biotechnol. 21(3), 262-267.
    • (2003) Nat. Biotechnol. , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 100
    • 0346031536 scopus 로고    scopus 로고
    • Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies
    • Zeytun, A., Jeromin, A., Scalettar, B. A., Waldo, G. S., and Bradbury, A. R. (2003). Fluorobodies combine GFP fluorescence with the binding characteristics of antibodies. Nat. Biotechnol. 21(12), 1473-1479.
    • (2003) Nat. Biotechnol. , vol.21 , Issue.12 , pp. 1473-1479
    • Zeytun, A.1    Jeromin, A.2    Scalettar, B.A.3    Waldo, G.S.4    Bradbury, A.R.5
  • 101


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