메뉴 건너뛰기




Volumn 19, Issue 11, 2008, Pages 2212-2220

Quantification of isotope encoded proteins in 2-D gels using surface enhanced resonance Raman

Author keywords

[No Author keywords available]

Indexed keywords

ENCODING (SYMBOLS); FLUORESCENCE IMAGING; ISOTOPES; PROTEINS; SIGNAL ENCODING; SPECTROSCOPY; STANDARDIZATION;

EID: 56749160530     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc800325k     Document Type: Article
Times cited : (6)

References (52)
  • 1
    • 18944374155 scopus 로고    scopus 로고
    • Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells
    • MacKeigan, J. P., Murphy, L. O., Dimitri, C. A., and Blenis, J. (2005) Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells. Mol. Cell. Biol. 25, 4676-4682.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4676-4682
    • MacKeigan, J.P.1    Murphy, L.O.2    Dimitri, C.A.3    Blenis, J.4
  • 2
    • 8644266706 scopus 로고    scopus 로고
    • Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways
    • Whitehurst, A., Cobb, M. H., and White, M. A. (2004) Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways. Mol. Cell. Biol. 24, 10145-10150.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 10145-10150
    • Whitehurst, A.1    Cobb, M.H.2    White, M.A.3
  • 4
    • 36348977585 scopus 로고    scopus 로고
    • Generation of an analog-sensitive Syk tyrosine kinase for the study of signaling dynamics from the B cell antigen receptor
    • Oh, H., Ozkirimli, E., Shah, K., Harrison, M. L., and Geahlen, R. L. (2007) Generation of an analog-sensitive Syk tyrosine kinase for the study of signaling dynamics from the B cell antigen receptor. J. Biol. Chem. 282, 33760-33768.
    • (2007) J. Biol. Chem , vol.282 , pp. 33760-33768
    • Oh, H.1    Ozkirimli, E.2    Shah, K.3    Harrison, M.L.4    Geahlen, R.L.5
  • 5
    • 33746214828 scopus 로고    scopus 로고
    • Kinetics of B cell receptor signaling in human B cell subsets mapped by phosphospecific flow cytometry
    • Irish, J. M., Czerwinski, D. K., Nolan, G. P., and Levy, R. (2006) Kinetics of B cell receptor signaling in human B cell subsets mapped by phosphospecific flow cytometry. J. Immunol. 177, 1581-1589.
    • (2006) J. Immunol , vol.177 , pp. 1581-1589
    • Irish, J.M.1    Czerwinski, D.K.2    Nolan, G.P.3    Levy, R.4
  • 6
    • 23844494402 scopus 로고    scopus 로고
    • The duration, magnitude and compartmentalization of ERK MAP kinase activity: Mechanisms for providing signaling specificity
    • Ebisuya, M., Kondoh, K., and Nishida, E. (2005) The duration, magnitude and compartmentalization of ERK MAP kinase activity: Mechanisms for providing signaling specificity. J. Cell Sci. 118, 2997-3002.
    • (2005) J. Cell Sci , vol.118 , pp. 2997-3002
    • Ebisuya, M.1    Kondoh, K.2    Nishida, E.3
  • 7
    • 33644845741 scopus 로고    scopus 로고
    • Extracellular signal-regulated mitogen-activated protein kinase inhibitors decrease amphetamine-induced behavior and neuropeptide gene expression in the striatum
    • Shi, X., and McGinty, J. F. (2006) Extracellular signal-regulated mitogen-activated protein kinase inhibitors decrease amphetamine-induced behavior and neuropeptide gene expression in the striatum. Neuroscience 138, 1289-1298.
    • (2006) Neuroscience , vol.138 , pp. 1289-1298
    • Shi, X.1    McGinty, J.F.2
  • 8
    • 38349014380 scopus 로고    scopus 로고
    • Src family kinases: Regulation of their activities, levels and identification of new pathways
    • Ingley, E. (2008) Src family kinases: Regulation of their activities, levels and identification of new pathways. Biochim. Biophys. Acta 1784, 56-65.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 56-65
    • Ingley, E.1
  • 9
    • 0036479109 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ci/l and plays a role in microtubule dynamics in the early secretory pathway
    • Tisdale, E. J. (2002) Glyceraldehyde-3-phosphate dehydrogenase is phosphorylated by protein kinase Ci/l and plays a role in microtubule dynamics in the early secretory pathway. J. Biol. Chem. 277, 3334-3341.
    • (2002) J. Biol. Chem , vol.277 , pp. 3334-3341
    • Tisdale, E.J.1
  • 10
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: Application to glyceraldehyde-3-phosphate dehydrogenase
    • Seo, J., Jeong, J., Kim, Y., Hwang, N., Paek, E., and Lee, K.-J. (2008) Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J. Proteome Res. 7, 587-602.
    • (2008) J. Proteome Res , vol.7 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Kim, Y.3    Hwang, N.4    Paek, E.5    Lee, K.-J.6
  • 11
    • 23844452781 scopus 로고    scopus 로고
    • New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells
    • Sirover, M. A. (2005) New nuclear functions of the glycolytic protein, glyceraldehyde-3-phosphate dehydrogenase, in mammalian cells. J. Cell. Biochem. 95, 45-52.
    • (2005) J. Cell. Biochem , vol.95 , pp. 45-52
    • Sirover, M.A.1
  • 13
    • 0037253267 scopus 로고    scopus 로고
    • A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard
    • Alban, A., David, S. O., Bjorkesten, L., ersson, C., Sloge, E., Lewis, S., and Currie, I. (2003) A novel experimental design for comparative two-dimensional gel analysis: Two-dimensional difference gel electrophoresis incorporating a pooled internal standard. Proteomics 3, 36-44.
    • (2003) Proteomics , vol.3 , pp. 36-44
    • Alban, A.1    David, S.O.2    Bjorkesten, L.3    ersson, C.4    Sloge, E.5    Lewis, S.6    Currie, I.7
  • 14
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • Zhang, R., Sioma, C. S., Wang, S., and Regnier, F. E. (2001) Fractionation of isotopically labeled peptides in quantitative proteomics. Anal. Chem. 73, 5142-5149.
    • (2001) Anal. Chem , vol.73 , pp. 5142-5149
    • Zhang, R.1    Sioma, C.S.2    Wang, S.3    Regnier, F.E.4
  • 15
    • 34250722602 scopus 로고    scopus 로고
    • Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks
    • Wolf-Yadlin, A., Hautaniemi, S., Lauffenburger, D. A., and White, F. M. (2007) Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl. Acad. Sci. U.S.A. 104, 5860-5865.
    • (2007) Proc Natl. Acad. Sci. U.S.A , vol.104 , pp. 5860-5865
    • Wolf-Yadlin, A.1    Hautaniemi, S.2    Lauffenburger, D.A.3    White, F.M.4
  • 16
    • 39449112983 scopus 로고    scopus 로고
    • Microscale solution IEF combined with 2-D DIGE substantially enhances analysis depth of complex proteomes such as mammalian cell and tissue extracts
    • Han, M. J., Herlyn, M., Fisher, A. B., and Speicher, D. W. (2008) Microscale solution IEF combined with 2-D DIGE substantially enhances analysis depth of complex proteomes such as mammalian cell and tissue extracts. Electrophoresis 29, 695-705.
    • (2008) Electrophoresis , vol.29 , pp. 695-705
    • Han, M.J.1    Herlyn, M.2    Fisher, A.B.3    Speicher, D.W.4
  • 17
    • 56749107122 scopus 로고    scopus 로고
    • Proteomic Analysis by Two-Dimensional Polyacrylamide Gel Electrophoresis
    • Veenstra, T. D, and Yates, J. R, III, Eds, pp, Chapter 2, John Wiley & Sons, Hoboken, NJ
    • Gromov, P. S., Gromova, I., and Celis, J. E. (2006) Proteomic Analysis by Two-Dimensional Polyacrylamide Gel Electrophoresis, In Proteomics for Biological Discovery (Veenstra, T. D., and Yates, J. R., III, Eds.) pp 19-46, Chapter 2, John Wiley & Sons, Hoboken, NJ.
    • (2006) Proteomics for Biological Discovery , pp. 19-46
    • Gromov, P.S.1    Gromova, I.2    Celis, J.E.3
  • 18
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • Cordials, G. L., Wasinger, V. C., Hochstrasser, D. F., and Sanchez, J. C. (2000) The dynamic range of protein expression: a challenge for proteomic research. Electrophoresis 21, 1104-1115.
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Cordials, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 19
    • 48249152987 scopus 로고    scopus 로고
    • Detection and relative quantification of proteins by SERRS using isotopic labels
    • Deb, S. K., Davis, B., Knudsen, G. M., Gudihal, R., Ben Amotz, D., and Davisson, V. J. (2008) Detection and relative quantification of proteins by SERRS using isotopic labels. J. Am. Chem. Soc. 130, 9624-9625.
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 9624-9625
    • Deb, S.K.1    Davis, B.2    Knudsen, G.M.3    Gudihal, R.4    Ben Amotz, D.5    Davisson, V.J.6
  • 20
    • 44449164078 scopus 로고    scopus 로고
    • Protein quantitation in 2-D gels using fluorescence with water raman as an internal standard
    • Loethen, Y. L., Knudsen, G. M., Davis, B., Gudihal, R., Davisson, V. J., and Ben-Amotz, D. (2008) Protein quantitation in 2-D gels using fluorescence with water raman as an internal standard. J. Proteome Res. 7, 1341-1345.
    • (2008) J. Proteome Res , vol.7 , pp. 1341-1345
    • Loethen, Y.L.1    Knudsen, G.M.2    Davis, B.3    Gudihal, R.4    Davisson, V.J.5    Ben-Amotz, D.6
  • 22
    • 0032360290 scopus 로고    scopus 로고
    • Surface-enhanced Raman scattering
    • Campion, A., and Kambhampati, P. (1998) Surface-enhanced Raman scattering. Chem. Soc. Rev. 27, 241-250.
    • (1998) Chem. Soc. Rev , vol.27 , pp. 241-250
    • Campion, A.1    Kambhampati, P.2
  • 23
    • 0033168130 scopus 로고    scopus 로고
    • Quantitative SERS measurements on dielectric-overcoated silver-island films by solution-deposition control of surface concentrations
    • Lacy, W. B., Olson, L. G., and Harris, J. M. (1999) Quantitative SERS measurements on dielectric-overcoated silver-island films by solution-deposition control of surface concentrations. Anal. Chem. 71, 2564-2570.
    • (1999) Anal. Chem , vol.71 , pp. 2564-2570
    • Lacy, W.B.1    Olson, L.G.2    Harris, J.M.3
  • 24
    • 20444398181 scopus 로고    scopus 로고
    • Isotope edited internal standard method for quantitative surface-enhanced Raman spectroscopy
    • Zhang, D. M., Xie, Y., Deb, S. K., Davisson, V. J., and Ben-Amotz, D. (2005) Isotope edited internal standard method for quantitative surface-enhanced Raman spectroscopy. Anal. Chem. 77, 3563-3569.
    • (2005) Anal. Chem , vol.77 , pp. 3563-3569
    • Zhang, D.M.1    Xie, Y.2    Deb, S.K.3    Davisson, V.J.4    Ben-Amotz, D.5
  • 26
    • 47749144375 scopus 로고    scopus 로고
    • Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters
    • Kalkhof, S., and Sinz, A. (2008) Chances and pitfalls of chemical cross-linking with amine-reactive N-hydroxysuccinimide esters. Anal. Bioanal. Chem. 392, 305-312.
    • (2008) Anal. Bioanal. Chem , vol.392 , pp. 305-312
    • Kalkhof, S.1    Sinz, A.2
  • 27
    • 0036204066 scopus 로고    scopus 로고
    • Development of improved cell lysis, solubilization and imaging approaches for proteomic analyses
    • Leimgruber, R. M., Malone, J. P., Radabaugh, M. R., LaPorte, M. L., Violand, B. N., and Monahan, J. B. (2002) Development of improved cell lysis, solubilization and imaging approaches for proteomic analyses. Proteomics 2, 135-144.
    • (2002) Proteomics , vol.2 , pp. 135-144
    • Leimgruber, R.M.1    Malone, J.P.2    Radabaugh, M.R.3    LaPorte, M.L.4    Violand, B.N.5    Monahan, J.B.6
  • 28
    • 0035525595 scopus 로고    scopus 로고
    • Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis
    • Mortz, E., Krogh, T. N., Vorum, H., and Gorg, A. (2001) Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis. Proteomics 1, 1359-1363.
    • (2001) Proteomics , vol.1 , pp. 1359-1363
    • Mortz, E.1    Krogh, T.N.2    Vorum, H.3    Gorg, A.4
  • 29
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained Polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., and Mann, M. (1996) Mass spectrometric sequencing of proteins from silver stained Polyacrylamide gels. Anal. Chem. 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 30
    • 23044437571 scopus 로고    scopus 로고
    • Detection of amino acid and peptide phosphate protonation using Raman spectroscopy
    • Xie, Y., Jiang, Y., and Ben-Amotz, D. (2005) Detection of amino acid and peptide phosphate protonation using Raman spectroscopy. Anal. Biochem. 343, 223-230.
    • (2005) Anal. Biochem , vol.343 , pp. 223-230
    • Xie, Y.1    Jiang, Y.2    Ben-Amotz, D.3
  • 31
    • 1642586932 scopus 로고    scopus 로고
    • Second-derivative variance minimization method for automated spectral subtraction
    • Loethen, Y. L., Zhang, D., Favors, R. N., Basiaga, S. B. G., and Ben-Amotz, D. (2004) Second-derivative variance minimization method for automated spectral subtraction. Appl. Spectrosc. 58, 272-278.
    • (2004) Appl. Spectrosc , vol.58 , pp. 272-278
    • Loethen, Y.L.1    Zhang, D.2    Favors, R.N.3    Basiaga, S.B.G.4    Ben-Amotz, D.5
  • 32
    • 0042553279 scopus 로고
    • Smoothing and differentiation of data by simplified least squares procedures
    • Savitzky, A., and Golay, M. J. E. (1964) Smoothing and differentiation of data by simplified least squares procedures. Anal. Chem. 36, 1627-1639.
    • (1964) Anal. Chem , vol.36 , pp. 1627-1639
    • Savitzky, A.1    Golay, M.J.E.2
  • 33
    • 0242498775 scopus 로고    scopus 로고
    • Automated method for subtraction of fluorescence from biological Raman spectra
    • Lieber, C. A., and Mahadevan-Jansen, A. (2003) Automated method for subtraction of fluorescence from biological Raman spectra. Appl. Spectrosc. 57, 1363-1367.
    • (2003) Appl. Spectrosc , vol.57 , pp. 1363-1367
    • Lieber, C.A.1    Mahadevan-Jansen, A.2
  • 34
    • 33846368499 scopus 로고    scopus 로고
    • Fluorescent immunoprecipitation analysis of cell surface proteins: A methodology compatible with mass-spectrometry
    • Filatov Alexander, V., Krotov Grigory, I., Zgoda Victor, G., and Volkov, Y. (2007) Fluorescent immunoprecipitation analysis of cell surface proteins: a methodology compatible with mass-spectrometry. J. Immunol. Methods 319, 21-33.
    • (2007) J. Immunol. Methods , vol.319 , pp. 21-33
    • Filatov Alexander, V.1    Krotov Grigory, I.2    Zgoda Victor, G.3    Volkov, Y.4
  • 35
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Urdu, M., Morgan, M. E., and Minden, J. S. (1997) Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18, 2071-2077.
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Urdu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 36
    • 0032511419 scopus 로고    scopus 로고
    • Direct observation of size-dependent optical enhancement in single metal nanoparticles
    • Emory, S. R., Haskins, W. E., and Nie, S. (1998) Direct observation of size-dependent optical enhancement in single metal nanoparticles. J. Am. Chem. Soc. 120, 8009-8010.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 8009-8010
    • Emory, S.R.1    Haskins, W.E.2    Nie, S.3
  • 37
    • 0023703933 scopus 로고
    • Coloration of silver-stained protein bands in polyacrylamide gels is caused by light scattering from silver grains of characteristic sizes
    • Merril, C. R., Bisher, M. E., Harrington, M., and Steven, A. C. (1988) Coloration of silver-stained protein bands in polyacrylamide gels is caused by light scattering from silver grains of characteristic sizes. Proc. Natl. Acad. Sci. U.S.A. 85, 453-457.
    • (1988) Proc. Natl. Acad. Sci. U.S.A , vol.85 , pp. 453-457
    • Merril, C.R.1    Bisher, M.E.2    Harrington, M.3    Steven, A.C.4
  • 38
    • 22444440911 scopus 로고    scopus 로고
    • Synthesis and optical properties of silver nanoparticles and arrays
    • Evanoff, D. D., Jr., and Chumanov, G. (2005) Synthesis and optical properties of silver nanoparticles and arrays. ChemPhysChem 6, 1221-1231.
    • (2005) ChemPhysChem , vol.6 , pp. 1221-1231
    • Evanoff Jr., D.D.1    Chumanov, G.2
  • 39
    • 2842588851 scopus 로고
    • Adsorption and surface-enhanced Raman of dyes on silver and gold sols
    • Lee, P., and Meisel, D. (1982) Adsorption and surface-enhanced Raman of dyes on silver and gold sols. J. Phys. Chem. 86, 3391-3395.
    • (1982) J. Phys. Chem , vol.86 , pp. 3391-3395
    • Lee, P.1    Meisel, D.2
  • 40
    • 0027934707 scopus 로고
    • Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA
    • Hirst, M., Haliday, E., Nakamura, J., and Lou, L. (1994) Human GMP synthetase. Protein purification, cloning, and functional expression of cDNA. J. Biol. Chem. 269, 23830-23837.
    • (1994) J. Biol. Chem , vol.269 , pp. 23830-23837
    • Hirst, M.1    Haliday, E.2    Nakamura, J.3    Lou, L.4
  • 41
    • 0028978721 scopus 로고
    • High-level production from a baculovirus expression system and biochemical characterization of human GMP synthetase
    • Lou, L., Nakamura, J., Tsing, S., Nguyen, B., Chow, J., Straub, K., Chan, H., and Barnett, J. (1995) High-level production from a baculovirus expression system and biochemical characterization of human GMP synthetase. Protein Expression Purif. 6, 487-495.
    • (1995) Protein Expression Purif , vol.6 , pp. 487-495
    • Lou, L.1    Nakamura, J.2    Tsing, S.3    Nguyen, B.4    Chow, J.5    Straub, K.6    Chan, H.7    Barnett, J.8
  • 43
    • 32944478288 scopus 로고    scopus 로고
    • Proteomics of xenografted human breast cancer indicates novel targets related to tamoxifen resistance
    • Besada, V., Diaz, M., Becker, M., Ramos, Y., Castellanos-Serra, L., and Fichtner, I. (2006) Proteomics of xenografted human breast cancer indicates novel targets related to tamoxifen resistance. Proteomics 6, 1038-1048.
    • (2006) Proteomics , vol.6 , pp. 1038-1048
    • Besada, V.1    Diaz, M.2    Becker, M.3    Ramos, Y.4    Castellanos-Serra, L.5    Fichtner, I.6
  • 45
    • 0041871026 scopus 로고    scopus 로고
    • Evaluation of two-dimensional difference gel electrophoresis for protein profiling
    • Gade, D., Thiermann, J., Markowsky, D., and Rabus, R. (2003) Evaluation of two-dimensional difference gel electrophoresis for protein profiling. J. Mol. Microbiol. Biotechnol. 5, 240-251.
    • (2003) J. Mol. Microbiol. Biotechnol , vol.5 , pp. 240-251
    • Gade, D.1    Thiermann, J.2    Markowsky, D.3    Rabus, R.4
  • 46
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling
    • Lopez, M. F., Berggren, K., Chernokalskaya, E., Lazarev, A., Robinson, M., and Patten, W. F. (2000) A comparison of silver stain and SYPRO ruby protein gel stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling. Electrophoresis 21, 3673-3683.
    • (2000) Electrophoresis , vol.21 , pp. 3673-3683
    • Lopez, M.F.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patten, W.F.6
  • 47
    • 44449162195 scopus 로고    scopus 로고
    • Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level
    • Hanke, S., Besir, H., Oesterhelt, D., and Mann, M. (2008) Absolute SILAC for accurate quantitation of proteins in complex mixtures down to the attomole level. J. Proteome Res. 7, 1118-1130.
    • (2008) J. Proteome Res , vol.7 , pp. 1118-1130
    • Hanke, S.1    Besir, H.2    Oesterhelt, D.3    Mann, M.4
  • 49
    • 0001281668 scopus 로고    scopus 로고
    • Extremely large enhancement factors in surface-enhanced Raman scattering for molecules on colloidal gold clusters
    • Kneipp, K., Kneipp, H., Manoharan, R., Hanlon, E. B., Itzkan, I., Dasari, R. R., and Feld, M. S. (1998) Extremely large enhancement factors in surface-enhanced Raman scattering for molecules on colloidal gold clusters. Appl. Spectrosc 52, 1493-1497.
    • (1998) Appl. Spectrosc , vol.52 , pp. 1493-1497
    • Kneipp, K.1    Kneipp, H.2    Manoharan, R.3    Hanlon, E.B.4    Itzkan, I.5    Dasari, R.R.6    Feld, M.S.7
  • 50
    • 0031037501 scopus 로고    scopus 로고
    • Probing single molecules and single nanoparticles by surface-enhanced raman scattering
    • Nie, S., and Emory, S. R. (1997) Probing single molecules and single nanoparticles by surface-enhanced raman scattering. Science 275, 1102-1106.
    • (1997) Science , vol.275 , pp. 1102-1106
    • Nie, S.1    Emory, S.R.2
  • 51
    • 56749154324 scopus 로고    scopus 로고
    • Isotopic dye pairs for accurate optical concentration measurements using SERRS
    • in press
    • Deb, S. K., Davis, B., Ben Amotz, D., Davisson, V. J. Isotopic dye pairs for accurate optical concentration measurements using SERRS Appl. Spectrosc. in press.
    • Appl. Spectrosc
    • Deb, S.K.1    Davis, B.2    Ben Amotz, D.3    Davisson, V.J.4
  • 52
    • 0036500712 scopus 로고    scopus 로고
    • Simple multiplex genotyping by surface-enhanced resonance Raman scattering
    • Graham, D., Mallinder, B. J., Whitcombe, D., Watson, N. D., and Smith, W. E. (2002) Simple multiplex genotyping by surface-enhanced resonance Raman scattering. Anal. Chem. 74, 1069-1074.
    • (2002) Anal. Chem , vol.74 , pp. 1069-1074
    • Graham, D.1    Mallinder, B.J.2    Whitcombe, D.3    Watson, N.D.4    Smith, W.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.