메뉴 건너뛰기




Volumn 4, Issue 7, 2003, Pages 605-613

Microarrays and mass spectrometry - The future of proteomics

Author keywords

[No Author keywords available]

Indexed keywords

APTAMER; DNA; GENE PRODUCT; PROTEIN; RNA;

EID: 0141505015     PISSN: 13892029     EISSN: None     Source Type: Journal    
DOI: 10.2174/1389202033490213     Document Type: Review
Times cited : (3)

References (70)
  • 1
    • 0037177855 scopus 로고    scopus 로고
    • Transcript abundance in yeast varies over six orders of magnitude
    • Holland, M. J. Transcript abundance in yeast varies over six orders of magnitude. J. Biol. Chem., 2002, 277: 14363-14366.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14363-14366
    • Holland, M.J.1
  • 3
    • 0034056940 scopus 로고    scopus 로고
    • The dynamic range of protein expression: A challenge for proteomic research
    • Corthals, G. L., Wasinger, V. C., Hochstrasser, D. F., Sanchez, J. C. The dynamic range of protein expression: a challenge for proteomic research. Electrophoresis, 2000, 21: 1104-1115.
    • (2000) Electrophoresis , vol.21 , pp. 1104-1115
    • Corthals, G.L.1    Wasinger, V.C.2    Hochstrasser, D.F.3    Sanchez, J.C.4
  • 5
    • 0034923505 scopus 로고    scopus 로고
    • Analysis of proteins and proteomes by mass spectrometry
    • Mann, M., Hendrickson, R. C., Pandey, A. Analysis of proteins and proteomes by mass spectrometry. Annu. Rev. Biochem., 2001, 70: 437-473.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 437-473
    • Mann, M.1    Hendrickson, R.C.2    Pandey, A.3
  • 6
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold, R. C., Goodlett, D. R. Mass spectrometry in proteomics. Chem. Rev., 2001, 101: 269-295.
    • (2001) Chem. Rev. , vol.101 , pp. 269-295
    • Aebersold, R.C.1    Goodlett, D.R.2
  • 7
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • Yates, J. R., 3rd Mass spectrometry and the age of the proteome. J. Mass. Spectrom., 1998, 33: 1-19.
    • (1998) J. Mass. Spectrom. , vol.33 , pp. 1-19
    • Yates J.R. III1
  • 8
    • 0030720249 scopus 로고    scopus 로고
    • Analysis of peptide synthesis products by electrospray ionization mass spectrometry
    • Burdick, D. J., Stults, J. T. Analysis of peptide synthesis products by electrospray ionization mass spectrometry. Methods Enzymol., 1997, 289: 499-519.
    • (1997) Methods Enzymol. , vol.289 , pp. 499-519
    • Burdick, D.J.1    Stults, J.T.2
  • 9
    • 0036199586 scopus 로고    scopus 로고
    • A perspective on protein microarrays
    • Mitchell, P. A perspective on protein microarrays. Nat. Biotechnol., 2002, 20: 225-229.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 225-229
    • Mitchell, P.1
  • 12
  • 13
    • 10644222762 scopus 로고    scopus 로고
    • Protein arrays: A high-throughput solution for proteomics research?
    • Cahill, D. J. Protein arrays: a high-throughput solution for proteomics research? Proteomics: A Trends Guide, 2000, 1: 47-51.
    • (2000) Proteomics: A Trends Guide , vol.1 , pp. 47-51
    • Cahill, D.J.1
  • 14
    • 0035499601 scopus 로고    scopus 로고
    • Microarrays go live-new prospects for proteomics
    • Blagoev, B., Pandey, A. Microarrays go live-new prospects for proteomics. Trends Biochem. Sci., 2001, 26: 639-641.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 639-641
    • Blagoev, B.1    Pandey, A.2
  • 16
    • 0035799654 scopus 로고    scopus 로고
    • Microarrays of cells expressing defined cDNAs
    • Ziauddin, J., Sabatini, D. M. Microarrays of cells expressing defined cDNAs. Nature, 2001, 411: 107-110.
    • (2001) Nature , vol.411 , pp. 107-110
    • Ziauddin, J.1    Sabatini, D.M.2
  • 17
    • 0036629182 scopus 로고    scopus 로고
    • Towards quantitative assays with peptide chips: A surface engineering approach
    • Houseman, B. T., Mrksich, M. Towards quantitative assays with peptide chips: a surface engineering approach. Trends Biotechnol., 2002, 20: 279-281.
    • (2002) Trends Biotechnol. , vol.20 , pp. 279-281
    • Houseman, B.T.1    Mrksich, M.2
  • 18
    • 0036199649 scopus 로고    scopus 로고
    • Peptide chips for the quantitative evaluation of protein kinase activity
    • Houseman, B. T., Huh, J. H., Kron, S. J., Mrksich, M. Peptide chips for the quantitative evaluation of protein kinase activity. Nat. Biotechnol., 2002, 20: 270-274.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 270-274
    • Houseman, B.T.1    Huh, J.H.2    Kron, S.J.3    Mrksich, M.4
  • 21
    • 0035221240 scopus 로고    scopus 로고
    • Protein microarrays for highly parallel detection and quantitation of specific proteins and antibodies in complex solutions
    • research0004.0001-research0004.0013
    • Haab, B. B., Dunham, M. J., Brown, P. O. Protein microarrays for highly parallel detection and quantitation of specific proteins and antibodies in complex solutions. Genome Biol., 2001, 2: research0004.0001-research0004.0013.
    • (2001) Genome Biol. , vol.2
    • Haab, B.B.1    Dunham, M.J.2    Brown, P.O.3
  • 23
    • 0034177001 scopus 로고    scopus 로고
    • Chemical ligands, genomics and drug discovery
    • Lenz, G. R., Nash, H. M., Jindal, S. Chemical ligands, genomics and drug discovery. Drug Discov. Today, 2000, 5: 145-156.
    • (2000) Drug Discov. Today , vol.5 , pp. 145-156
    • Lenz, G.R.1    Nash, H.M.2    Jindal, S.3
  • 24
    • 0037061492 scopus 로고    scopus 로고
    • Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays
    • Kuruvilla, F. G., Shamji, A. F., Sternson, S. M., Hergenrother, P. J., Schreiber, S. L. Dissecting glucose signalling with diversity-oriented synthesis and small-molecule microarrays. Nature, 2002, 416: 653-657.
    • (2002) Nature , vol.416 , pp. 653-657
    • Kuruvilla, F.G.1    Shamji, A.F.2    Sternson, S.M.3    Hergenrother, P.J.4    Schreiber, S.L.5
  • 25
    • 0025194307 scopus 로고
    • Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase
    • Tuerk, C., Gold, L. Systematic evolution of ligands by exponential enrichment: RNA ligands to bacteriophage T4 DNA polymerase. Science, 1990, 249: 505-510.
    • (1990) Science , vol.249 , pp. 505-510
    • Tuerk, C.1    Gold, L.2
  • 26
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • Ellington, A. D., Szostak, J. W. In vitro selection of RNA molecules that bind specific ligands. Nature, 1990, 346: 818-822.
    • (1990) Nature , vol.346 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 27
    • 0034603154 scopus 로고    scopus 로고
    • Adaptive recognition by nucleic acid aptamers
    • Hermann, T., Patel, D. J. Adaptive recognition by nucleic acid aptamers. Science, 2000, 287: 820-825.
    • (2000) Science , vol.287 , pp. 820-825
    • Hermann, T.1    Patel, D.J.2
  • 28
    • 0032860385 scopus 로고    scopus 로고
    • Aptamers: An emerging class of molecules that rival antibodies in diagnostics
    • Jayasena, S. D. Aptamers: an emerging class of molecules that rival antibodies in diagnostics. Clin. Chem., 1999, 45: 1628-1650.
    • (1999) Clin. Chem. , vol.45 , pp. 1628-1650
    • Jayasena, S.D.1
  • 29
    • 0037099536 scopus 로고    scopus 로고
    • Identification and Characterization of Nuclease-stabilized RNA Molecules That Bind Human Prostate Cancer Cells via the Prostate-specific Membrane Antigen
    • Lupold, S. E., Hicke, B. J., Lin, Y., Coffey, D. S. Identification and Characterization of Nuclease-stabilized RNA Molecules That Bind Human Prostate Cancer Cells via the Prostate-specific Membrane Antigen. Cancer Res., 2002, 62: 4029-4033.
    • (2002) Cancer Res. , vol.62 , pp. 4029-4033
    • Lupold, S.E.1    Hicke, B.J.2    Lin, Y.3    Coffey, D.S.4
  • 31
    • 0035070585 scopus 로고    scopus 로고
    • Immobilized RNA switches for the analysis of complex chemical and biological mixtures
    • Seetharaman, S., Zivarts, M., Sudarsan, N., Breaker, R. R. Immobilized RNA switches for the analysis of complex chemical and biological mixtures. Nat. Biotechnol., 2001, 19: 336-341.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 336-341
    • Seetharaman, S.1    Zivarts, M.2    Sudarsan, N.3    Breaker, R.R.4
  • 33
    • 0035480005 scopus 로고    scopus 로고
    • Tissue microarrays (TMAs) for high-throughput molecular pathology research
    • Nocito, A., Kononen, J., Kallioniemi, O. P., Sauter, G. Tissue microarrays (TMAs) for high-throughput molecular pathology research. Int. J. Cancer, 2001, 94: 1-5.
    • (2001) Int. J. Cancer , vol.94 , pp. 1-5
    • Nocito, A.1    Kononen, J.2    Kallioniemi, O.P.3    Sauter, G.4
  • 37
    • 0037081179 scopus 로고    scopus 로고
    • Alterations of Smad signaling in human breast carcinoma are associated with poor outcome: A tissue microarray study
    • Xie, W., Mertens, J. C., Reiss, D. J., Rimm, D. L., Camp, R. L., Haffty, B. G., Reiss, M. Alterations of Smad signaling in human breast carcinoma are associated with poor outcome: a tissue microarray study. Cancer Res., 2002, 62: 497-505.
    • (2002) Cancer Res. , vol.62 , pp. 497-505
    • Xie, W.1    Mertens, J.C.2    Reiss, D.J.3    Rimm, D.L.4    Camp, R.L.5    Haffty, B.G.6    Reiss, M.7
  • 39
    • 0037117516 scopus 로고    scopus 로고
    • Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands
    • Hodneland, C. D., Lee, Y. S., Min, D. H., Mrksich, M. Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands. Proc. Natl. Acad. Sci. USA, 2002, 99: 5048-5052.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5048-5052
    • Hodneland, C.D.1    Lee, Y.S.2    Min, D.H.3    Mrksich, M.4
  • 40
    • 0036057919 scopus 로고    scopus 로고
    • Is mass spectrometry ready for proteome-wide protein expression analysis?
    • comment2008.2001-comment2008.2005
    • Rappsilber, J., Mann, M. Is mass spectrometry ready for proteome-wide protein expression analysis? Genome Biol., 2002, 3: comment2008.2001-comment2008.2005.
    • (2002) Genome Biol. , vol.3
    • Rappsilber, J.1    Mann, M.2
  • 41
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey, A., Mann, M. Proteomics to study genes and genomes. Nature, 2000, 405: 837-846.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 42
    • 0034786119 scopus 로고    scopus 로고
    • An evaluation of the use of two-dimensional gel electrophoresis in proteomics
    • Ong, S. E., Pandey, A. An evaluation of the use of two-dimensional gel electrophoresis in proteomics. Biomol. Eng., 2001, 18: 195-205.
    • (2001) Biomol. Eng. , vol.18 , pp. 195-205
    • Ong, S.E.1    Pandey, A.2
  • 45
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn, M. P., Wolters, D., Yates, J. R., 3rd Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat. Biotechnol., 2001, 19: 242-247.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates J.R. III3
  • 47
    • 0033565503 scopus 로고    scopus 로고
    • Immobilized gallium(III) affinity chromatography of phosphopeptides
    • Posewitz, M. C., Tempst, P. Immobilized gallium(III) affinity chromatography of phosphopeptides. Anal. Chem., 1999, 71: 2883-2892.
    • (1999) Anal. Chem. , vol.71 , pp. 2883-2892
    • Posewitz, M.C.1    Tempst, P.2
  • 48
    • 0033810757 scopus 로고    scopus 로고
    • Mapping the phosphorylation sites of proteins using on-line immobilized metal affinity chromatography/capillary electrophoresis/electrospray ionization multiple stage tandem mass spectrometry
    • Cao, P., Stults, J. T. Mapping the phosphorylation sites of proteins using on-line immobilized metal affinity chromatography/capillary electrophoresis/electrospray ionization multiple stage tandem mass spectrometry. Rapid Commun. Mass Spectrom., 2000, 14: 1600-1606.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1600-1606
    • Cao, P.1    Stults, J.T.2
  • 49
    • 0036468952 scopus 로고    scopus 로고
    • Phosphoprotein isotope-coded affinity tags: Application to the enrichment and identification of low-abundance phosphoproteins
    • Goshe, M. B., Veenstra, T. D., Panisko, E. A., Conrads, T. P., Angell, N. H., Smith, R. D. Phosphoprotein isotope-coded affinity tags: application to the enrichment and identification of low-abundance phosphoproteins. Anal. Chem., 2002, 74: 607-616.
    • (2002) Anal. Chem. , vol.74 , pp. 607-616
    • Goshe, M.B.1    Veenstra, T.D.2    Panisko, E.A.3    Conrads, T.P.4    Angell, N.H.5    Smith, R.D.6
  • 50
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda, Y., Nagasu, T., Chait, B. T. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat. Biotechnol., 2001, 19: 379-382.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 51
    • 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., Aebersold, R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat. Biotechnol., 1999, 17: 994-999.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 52
    • 0036171359 scopus 로고    scopus 로고
    • De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging
    • Cagney, G., Emili, A. De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging. Nat. Biotechnol., 2002, 20: 163-170.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 163-170
    • Cagney, G.1    Emili, A.2
  • 53
    • 0034282457 scopus 로고    scopus 로고
    • Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety
    • Munchbach, M., Quadroni, M., Miotto, G., James, P. Quantitation and facilitated de novo sequencing of proteins by isotopic N-terminal labeling of peptides with a fragmentation-directing moiety. Anal. Chem., 2000, 72: 4047-4057.
    • (2000) Anal. Chem. , vol.72 , pp. 4047-4057
    • Munchbach, M.1    Quadroni, M.2    Miotto, G.3    James, P.4
  • 54
    • 0033535961 scopus 로고    scopus 로고
    • Accurate quantitation of protein expression and site-specific phosphorylation
    • Oda, Y., Huang, K., Cross, F. R., Cowburn, D., Chait, B. T. Accurate quantitation of protein expression and site-specific phosphorylation. Proc. Natl. Acad. Sci. USA, 1999, 96: 6591-6596.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6591-6596
    • Oda, Y.1    Huang, K.2    Cross, F.R.3    Cowburn, D.4    Chait, B.T.5
  • 56
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong, S. E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., Mann, M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics, 2002, 1: 376-386.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 57
    • 0027198862 scopus 로고
    • Identifying proteins from two-dimensional gels by polecular mass searching of peptide fragments in protein sequence databases
    • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Watanabe, C. Identifying proteins from two-dimensional gels by polecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. USA, 1993, 90: 5011-5015.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5011-5015
    • Henzel, W.J.1    Billeci, T.M.2    Stults, J.T.3    Wong, S.C.4    Grimley, C.5    Watanabe, C.6
  • 58
    • 0031298696 scopus 로고    scopus 로고
    • Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching
    • Jensen, O. N., Podtelejnikov, A. V., Mann, M. Identification of the components of simple protein mixtures by high-accuracy peptide mass mapping and database searching. Anal. Chem., 1997, 69: 4741-4750.
    • (1997) Anal. Chem. , vol.69 , pp. 4741-4750
    • Jensen, O.N.1    Podtelejnikov, A.V.2    Mann, M.3
  • 61
    • 0030999705 scopus 로고    scopus 로고
    • An introduction to quadruple ion trap mass spectrometry
    • March, R. E. An introduction to quadruple ion trap mass spectrometry. J. Mass. Spectrom., 1997, 32: 351-369.
    • (1997) J. Mass. Spectrom. , vol.32 , pp. 351-369
    • March, R.E.1
  • 62
    • 0030960366 scopus 로고    scopus 로고
    • Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer
    • Shevchenko, A., Chernushevich, I., Eris, W., Standing, K. G., Thomson, B., Wilm, M., Mann, M. Rapid 'de novo' peptide sequencing by a combination of nanoelectrospray, isotopic labeling and a quadrupole/time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom., 1997, 11: 1015-1024.
    • (1997) Rapid Commun. Mass Spectrom. , vol.11 , pp. 1015-1024
    • Shevchenko, A.1    Chernushevich, I.2    Eris, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 63
    • 0029717657 scopus 로고    scopus 로고
    • High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer
    • Morris, H. R., Paxton, T., Dell, A., Langhorne, J., Berg, M., Bordoli, R. S., Hoyes, J., Bateman, R. H. High sensitivity collisionally-activated decomposition tandem mass spectrometry on a novel quadrupole/orthogonal-acceleration time-of-flight mass spectrometer. Rapid Commun. Mass Spectrom., 1996, 10: 889-896.
    • (1996) Rapid Commun. Mass Spectrom. , vol.10 , pp. 889-896
    • Morris, H.R.1    Paxton, T.2    Dell, A.3    Langhorne, J.4    Berg, M.5    Bordoli, R.S.6    Hoyes, J.7    Bateman, R.H.8
  • 64
    • 0033642816 scopus 로고    scopus 로고
    • Direct analysis of proteins in mixtures. Application to protein complexes
    • Yates, J. R., 3rd, Link, A. J., Schieltz, D. Direct analysis of proteins in mixtures. Application to protein complexes. Methods Mol. Biol., 2000, 146: 17-26.
    • (2000) Methods Mol. Biol. , vol.146 , pp. 17-26
    • Yates J.R. III1    Link, A.J.2    Schieltz, D.3
  • 65
    • 0037133237 scopus 로고    scopus 로고
    • Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue
    • Sze, S. K., Ge, Y., Oh, H., McLafferty, F. W. Top-down mass spectrometry of a 29-kDa protein for characterization of any posttranslational modification to within one residue. Proc. Natl. Acad. Sci. USA, 2002, 99: 1774-1779.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1774-1779
    • Sze, S.K.1    Ge, Y.2    Oh, H.3    McLafferty, F.W.4
  • 66
    • 0034132537 scopus 로고    scopus 로고
    • The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer
    • Medzihradszky, K. F., Campbell, J. M., Baldwin, M. A., Falick, A. M., Juhasz, P., Vestal, M. L., Burlingame, A. L. The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer. Anal. Chem., 2000, 72: 552-558.
    • (2000) Anal. Chem. , vol.72 , pp. 552-558
    • Medzihradszky, K.F.1    Campbell, J.M.2    Baldwin, M.A.3    Falick, A.M.4    Juhasz, P.5    Vestal, M.L.6    Burlingame, A.L.7
  • 67
    • 0030152785 scopus 로고    scopus 로고
    • A practical ion trap mass spectrometer for the analysis of peptides by matrix-assisted laser desorption/ionization
    • Qin, J., Ruud, J., Chait, B. T. A practical ion trap mass spectrometer for the analysis of peptides by matrix-assisted laser desorption/ionization. Anal. Chem., 1996, 68: 1784-1791.
    • (1996) Anal. Chem. , vol.68 , pp. 1784-1791
    • Qin, J.1    Ruud, J.2    Chait, B.T.3
  • 68
    • 0034194446 scopus 로고    scopus 로고
    • MALDI quadrupole time-of-flight mass spectrometry: A powerful tool for proteomic research
    • Shevchenko, A., Loboda, A., Ens, W., Standing, K. G. MALDI quadrupole time-of-flight mass spectrometry: a powerful tool for proteomic research. Anal. Chem., 2000, 72: 2132-2141.
    • (2000) Anal. Chem. , vol.72 , pp. 2132-2141
    • Shevchenko, A.1    Loboda, A.2    Ens, W.3    Standing, K.G.4
  • 69
    • 0034811750 scopus 로고    scopus 로고
    • A combined linear ion trap time-of-flight system with improved performance and MS(n) capabilities
    • Collings, B. A., Campbell, J. M., Mao, D., Douglas, D. J. A combined linear ion trap time-of-flight system with improved performance and MS(n) capabilities. Rapid Commun. Mass Spectrom., 2001, 15: 1777-1795.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 1777-1795
    • Collings, B.A.1    Campbell, J.M.2    Mao, D.3    Douglas, D.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.