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Volumn 3, Issue 3, 2004, Pages 364-382

Human serum proteins preseparated by electrophoresis or chromatography followed by tandem mass spectrometry

Author keywords

Chromatography; Electrophoresis; Human; Mass spectrometer; Protein; Proteome; Serum; Tandem

Indexed keywords

CELL PROTEIN; CHYMOTRYPSIN; PLASMA PROTEIN; TRYPSIN;

EID: 4444275799     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr034039p     Document Type: Article
Times cited : (82)

References (65)
  • 1
    • 0036615478 scopus 로고    scopus 로고
    • The Human Proteome Organization: A mission to advance proteome knowledge
    • Hanash, S.; Celis, J. E. The Human Proteome Organization: a mission to advance proteome knowledge. Mol. Cell Proteomics 2002, 1, 413-414.
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 413-414
    • Hanash, S.1    Celis, J.E.2
  • 2
    • 4344560157 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson, N. L.; Anderson, N. G. The human plasma proteome: history, character, and diagnostic prospects. Mol. Cell Proteomics 2003, 2, 50.
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 50
    • Anderson, N.L.1    Anderson, N.G.2
  • 3
    • 0036745679 scopus 로고    scopus 로고
    • Methods for fractionation, separation and profiling of proteins and peptides
    • Issaq, H. J.; Conrads, T. P.; Janini, G. M.; Veenstra, T. D. Methods for fractionation, separation and profiling of proteins and peptides. Electrophoresis 2002, 23, 3048-61.
    • (2002) Electrophoresis , vol.23 , pp. 3048-3061
    • Issaq, H.J.1    Conrads, T.P.2    Janini, G.M.3    Veenstra, T.D.4
  • 4
    • 0016216815 scopus 로고
    • The literature on affinity chromatography
    • Wilchek, M.; Jakoby, W. B. The literature on affinity chromatography. Methods Enzymol. 1974, 34, 3-10.
    • (1974) Methods Enzymol. , vol.34 , pp. 3-10
    • Wilchek, M.1    Jakoby, W.B.2
  • 5
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm, M.; Shevchenko, A.; Houthaeve, T.; Breit, S.; Schweigerer, L.; Fotsis, T.; Mann, M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996, 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 7
    • 0035404418 scopus 로고    scopus 로고
    • Continuous free-flow electrophoresis separation of cytosolic proteins from the human colon carcinoma cell line LIM 1215: A non two- dimensional gel electrophoresis-based proteome analysis strategy
    • Hoffmann, P.; Ji, H.; Moritz, R. L.; Connolly, L. M.; Frecklington, D. F.; Layton, M. J.; Eddes, J. S.; Simpson, R. J. Continuous free-flow electrophoresis separation of cytosolic proteins from the human colon carcinoma cell line LIM 1215: a non two- dimensional gel electrophoresis-based proteome analysis strategy. Proteomics 2001, 1, 807-818.
    • (2001) Proteomics , vol.1 , pp. 807-818
    • Hoffmann, P.1    Ji, H.2    Moritz, R.L.3    Connolly, L.M.4    Frecklington, D.F.5    Layton, M.J.6    Eddes, J.S.7    Simpson, R.J.8
  • 8
    • 0036253023 scopus 로고    scopus 로고
    • Detection of low-molecular-mass plasma peptides in the cavernous and systemic blood of healthy men during penile flaccidity and rigidity - An experimental approach using the novel differential peptide display technology
    • Tammen, H.; Hess, R.; Uckert, S.; Becker, A. J.; Stief, C. G.; Knappe, P. S.; Schrader, M.; Jonas, U. Detection of low-molecular-mass plasma peptides in the cavernous and systemic blood of healthy men during penile flaccidity and rigidity - an experimental approach using the novel differential peptide display technology. Urology 2002, 59, 784-789.
    • (2002) Urology , vol.59 , pp. 784-789
    • Tammen, H.1    Hess, R.2    Uckert, S.3    Becker, A.J.4    Stief, C.G.5    Knappe, P.S.6    Schrader, M.7    Jonas, U.8
  • 9
    • 0035977840 scopus 로고    scopus 로고
    • Proteomic profiling from human samples: The body fluid alternative
    • Kennedy, S. Proteomic profiling from human samples: the body fluid alternative. Toxicol. Lett. 2001, 120, 379-384.
    • (2001) Toxicol. Lett. , vol.120 , pp. 379-384
    • Kennedy, S.1
  • 10
    • 0031807041 scopus 로고    scopus 로고
    • Proteins of rat serum: I. Establishing a reference two-dimensional electrophoresis map by immunodetection and microbore high performance liquid chromatography-electrospray mass spectrometry
    • Haynes, P.; Miller, I.; Aebersold, R.; Gemeiner, M.; Eberini, I.; Lovati, M. R.; Manzoni, C.; Vignati, M.; Gianazza, E. Proteins of rat serum: I. Establishing a reference two-dimensional electrophoresis map by immunodetection and microbore high performance liquid chromatography-electrospray mass spectrometry. Electrophoresis 1998, 19, 1484-1492.
    • (1998) Electrophoresis , vol.19 , pp. 1484-1492
    • Haynes, P.1    Miller, I.2    Aebersold, R.3    Gemeiner, M.4    Eberini, I.5    Lovati, M.R.6    Manzoni, C.7    Vignati, M.8    Gianazza, E.9
  • 11
    • 0034848903 scopus 로고    scopus 로고
    • Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison
    • Wait, R.; Gianazza, E.; Eberini, I.; Sironi, L.; Dunn, M. J.; Gemeiner, M.; Miller, I. Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison. Electrophoresis 2001, 22, 3043-3052.
    • (2001) Electrophoresis , vol.22 , pp. 3043-3052
    • Wait, R.1    Gianazza, E.2    Eberini, I.3    Sironi, L.4    Dunn, M.J.5    Gemeiner, M.6    Miller, I.7
  • 13
    • 0036767470 scopus 로고    scopus 로고
    • Targeted proteomics of low-level proteins in human plasma by LC/MSn: Using human growth hormone as a model system
    • Wu, S. L.; Amato, H.; Biringer, R.; Choudhary, G.; Shieh, P.; Hancock, W. S. Targeted proteomics of low-level proteins in human plasma by LC/MSn: using human growth hormone as a model system. J. Proteome Res. 2002, 1, 459-465.
    • (2002) J. Proteome Res. , vol.1 , pp. 459-465
    • Wu, S.L.1    Amato, H.2    Biringer, R.3    Choudhary, G.4    Shieh, P.5    Hancock, W.S.6
  • 14
    • 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 III, J.R.3
  • 16
    • 0036746523 scopus 로고    scopus 로고
    • Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry
    • Andon, N. L.; Hollingworth, S.; Koller, A.; Greenland, A. J.; Yates, J. R., 3rd; Haynes, P. A. Proteomic characterization of wheat amyloplasts using identification of proteins by tandem mass spectrometry. Proteomics 2002, 2, 1156-1168.
    • (2002) Proteomics , vol.2 , pp. 1156-1168
    • Andon, N.L.1    Hollingworth, S.2    Koller, A.3    Greenland, A.J.4    Yates III, J.R.5    Haynes, P.A.6
  • 17
    • 0030022858 scopus 로고    scopus 로고
    • Peptide-mass profiles of poly(vinylidene difluoride)-bound proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in the presence of nonionic detergents
    • Gharahdaghi, F.; Kirchner, M.; Fernandez, J.; Mische, S. M. Peptide-mass profiles of poly(vinylidene difluoride)-bound proteins by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry in the presence of nonionic detergents. Anal. Biochem. 1996, 233, 94-99.
    • (1996) Anal. Biochem. , vol.233 , pp. 94-99
    • Gharahdaghi, F.1    Kirchner, M.2    Fernandez, J.3    Mische, S.M.4
  • 18
    • 0033931001 scopus 로고    scopus 로고
    • Phenotyping apolipoprotein E*3-leiden transgenic mice by two- dimensional polyacrylamide gel electrophoresis and mass spectrometric identification
    • Skehel, J. M.; Schneider, K.; Murphy, N.; Graham, A.; Benson, G. M.; Cutler, P.; Camilleri, P. Phenotyping apolipoprotein E*3-leiden transgenic mice by two- dimensional polyacrylamide gel electrophoresis and mass spectrometric identification. Electrophoresis 2000, 21, 2540-2545.
    • (2000) Electrophoresis , vol.21 , pp. 2540-2545
    • Skehel, J.M.1    Schneider, K.2    Murphy, N.3    Graham, A.4    Benson, G.M.5    Cutler, P.6    Camilleri, P.7
  • 19
    • 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
  • 20
    • 0036788583 scopus 로고    scopus 로고
    • Gas-phase separations of protein and peptide ion fragments generated by collision-induced dissociation in an ion trap
    • Badman, E. R.; Myung, S.; Clemmer, D. E. Gas-phase separations of protein and peptide ion fragments generated by collision-induced dissociation in an ion trap. Anal. Chem. 2002, 74, 4889-4894.
    • (2002) Anal. Chem. , vol.74 , pp. 4889-4894
    • Badman, E.R.1    Myung, S.2    Clemmer, D.E.3
  • 21
    • 0034124238 scopus 로고    scopus 로고
    • A tandem quadrupole/time-of-flight mass spectrometer with a matrix- assisted laser desorption/ionization source: Design and performance
    • Loboda, A. V.; Krutchinsky, A. N.; Bromirski, M.; Ens, W.; Standing, K. G. A tandem quadrupole/time-of-flight mass spectrometer with a matrix- assisted laser desorption/ionization source: design and performance. Rapid Commun. Mass Spectrom. 2000, 14, 1047-1057.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 1047-1057
    • Loboda, A.V.1    Krutchinsky, A.N.2    Bromirski, M.3    Ens, W.4    Standing, K.G.5
  • 22
    • 0019030843 scopus 로고
    • Instrumental aspects of positive and negative ion chemical ionization mass spectrometry
    • Stafford, G. C. Instrumental aspects of positive and negative ion chemical ionization mass spectrometry. Environ. Health Perspect 1980, 36, 85-88.
    • (1980) Environ. Health Perspect. , vol.36 , pp. 85-88
    • Stafford, G.C.1
  • 23
    • 0038409059 scopus 로고    scopus 로고
    • Product ion scanning using a Q-q-Qlinear ion trap (Q TRAPTM) mass spectrometer
    • Hager, J. W.; Yves Le Blanc, J. C. Product ion scanning using a Q-q-Qlinear ion trap (Q TRAPTM) mass spectrometer. Rapid Commun. Mass Spectrom. 2003, 17, 1056-1064.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 1056-1064
    • Hager, J.W.1    Yves Le Blanc, J.C.2
  • 24
  • 25
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann, M.; Wilm, M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal. Chem. 1994, 66, 4390-4399.
    • (1994) Anal. Chem. , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 26
    • 0031814022 scopus 로고    scopus 로고
    • Database searching using mass spectrometry data
    • Yates, J. R., 3rd Database searching using mass spectrometry data. Electrophoresis 1998, 19, 893-900.
    • (1998) Electrophoresis , vol.19 , pp. 893-900
    • Yates III, J.R.1
  • 27
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • pii
    • Perkins, D. N.; Pappin, D. J.; Creasy, D. M.; Cottrell, J. S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20, 3551-3567. [pii].
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 28
    • 0037274605 scopus 로고    scopus 로고
    • Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS
    • Choudhary, G.; Wu, S. L.; Shieh, P.; Hancock, W. S. Multiple enzymatic digestion for enhanced sequence coverage of proteins in complex proteomic mixtures using capillary LC with ion trap MS/MS. J. Proteome Res. 2003, 2, 59-67.
    • (2003) J. Proteome Res. , vol.2 , pp. 59-67
    • Choudhary, G.1    Wu, S.L.2    Shieh, P.3    Hancock, W.S.4
  • 29
    • 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.; Ens, 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    Ens, W.3    Standing, K.G.4    Thomson, B.5    Wilm, M.6    Mann, M.7
  • 31
    • 0037236038 scopus 로고    scopus 로고
    • A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry
    • Kruppa, G. H.; Schoeniger, J.; Young, M. M. A top down approach to protein structural studies using chemical cross-linking and Fourier transform mass spectrometry. Rapid Commun. Mass Spectrom. 2003, 17, 155-162.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 155-162
    • Kruppa, G.H.1    Schoeniger, J.2    Young, M.M.3
  • 33
    • 0036748309 scopus 로고    scopus 로고
    • Fourier transform mass spectrometry for automated fragmentation and identification of 5-20 kDa proteins in mixtures
    • Johnson, J. R.; Meng, F.; Forbes, A. J.; Cargile, B. J.; Kelleher, N. L. Fourier transform mass spectrometry for automated fragmentation and identification of 5-20 kDa proteins in mixtures. Electrophoresis 2002, 23, 3217-3223.
    • (2002) Electrophoresis , vol.23 , pp. 3217-3223
    • Johnson, J.R.1    Meng, F.2    Forbes, A.J.3    Cargile, B.J.4    Kelleher, N.L.5
  • 35
    • 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. U. S. A. 2002, 99, 1774-1779.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1774-1779
    • Sze, S.K.1    Ge, Y.2    Oh, H.3    McLafferty, F.W.4
  • 36
    • 0037987698 scopus 로고    scopus 로고
    • Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Marekov, L. N.; Steinert, P. M. Charge derivatization by 4-sulfophenyl isothiocyanate enhances peptide sequencing by post-source decay matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Mass Spectrom. 2003, 38, 373-377.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 373-377
    • Marekov, L.N.1    Steinert, P.M.2
  • 37
    • 0036873926 scopus 로고    scopus 로고
    • Application of a novel protein biochip technology for detection and identification of rheumatoid arthritis biomarkers in synovial fluid
    • Uchida, T.; Fukawa, A.; Uchida, M.; Fujita, K.; Saito, K. Application of a novel protein biochip technology for detection and identification of rheumatoid arthritis biomarkers in synovial fluid. J. Proteome Res. 2002, 1, 495-499.
    • (2002) J. Proteome Res. , vol.1 , pp. 495-499
    • Uchida, T.1    Fukawa, A.2    Uchida, M.3    Fujita, K.4    Saito, K.5
  • 38
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10 000 dallons
    • Karas, M.; Hillenkamp, F. Laser desorption ionization of proteins with molecular masses exceeding 10 000 dallons. Anal. Chem. 1988, 60, 2299-2301.
    • (1988) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 39
    • 0028167062 scopus 로고
    • Laser desorption time-of-flight mass spectrometric analysis of transferrin precipitated with antiserum: A unique simple method to identify molecular weight variants
    • Nakanishi, T.; Okamoto, N.; Tanaka, K.; Shimizu, A. Laser desorption time-of-flight mass spectrometric analysis of transferrin precipitated with antiserum: a unique simple method to identify molecular weight variants. Biol. Mass Spectrom. 1994, 23, 230-233.
    • (1994) Biol. Mass Spectrom. , vol.23 , pp. 230-233
    • Nakanishi, T.1    Okamoto, N.2    Tanaka, K.3    Shimizu, A.4
  • 40
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn, J. B.; Mann, M.; Meng, C. K.; Wong, S. F.; Whitehouse, C. M. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246, 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 43
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters, D. A.; Washburn, M. P.; Yates, J. R., 3rd An automated multidimensional protein identification technology for shotgun proteomics. Anal. Chem. 2001, 73, 5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 44
    • 0023801174 scopus 로고
    • Coomassie blue-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for direct visualization of polypeptides during electrophoresis
    • Schagger, H.; Aquila, H.; Von Jagow, G. Coomassie blue-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for direct visualization of polypeptides during electrophoresis. Anal. Biochem. 1988, 173, 201-205.
    • (1988) Anal. Biochem. , vol.173 , pp. 201-205
    • Schagger, H.1    Aquila, H.2    Von Jagow, G.3
  • 45
    • 0037176211 scopus 로고    scopus 로고
    • Surface-enhanced laser desorption-ionization retentate chromatography mass spectrometry (SELDI-RC-MS): A new method for rapid development of process chromatography conditions
    • Weinberger, S. R.; Boschetti, E.; Santambien, P.; Brenac, V. Surface-enhanced laser desorption-ionization retentate chromatography mass spectrometry (SELDI-RC-MS): a new method for rapid development of process chromatography conditions. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2002, 782, 307-316.
    • (2002) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.782 , pp. 307-316
    • Weinberger, S.R.1    Boschetti, E.2    Santambien, P.3    Brenac, V.4
  • 46
    • 0036033976 scopus 로고    scopus 로고
    • A robust microelectrospray ionization technique for high-throughput liquid chromatography/mass spectrometry proteomics using a sanded metal needle as an emitter
    • Guzzetta, A. W.; Thakur, R. A.; Mylchreest, I. C. A robust microelectrospray ionization technique for high-throughput liquid chromatography/mass spectrometry proteomics using a sanded metal needle as an emitter. Rapid Commun. Mass Spectrom. 2002, 16, 2067-2072.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 2067-2072
    • Guzzetta, A.W.1    Thakur, R.A.2    Mylchreest, I.C.3
  • 50
    • 0036624292 scopus 로고    scopus 로고
    • Peptidomic approaches in proteomic research
    • Jurgens, M.; Schrader, M. Peptidomic approaches in proteomic research. Curr. Opin. Mol. Ther. 2002, 4, 236-241.
    • (2002) Curr. Opin. Mol. Ther. , vol.4 , pp. 236-241
    • Jurgens, M.1    Schrader, M.2
  • 51
    • 0035238444 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: An elegant tool for peptidomics
    • Verhaert, P.; Uttenweiler-Joseph, S.; de Vries, M.; Loboda, A.; Ens, W.; Standing, K. G. Matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry: an elegant tool for peptidomics. Proteomics 2001, 1, 118-131.
    • (2001) Proteomics , vol.1 , pp. 118-131
    • Verhaert, P.1    Uttenweiler-Joseph, S.2    De Vries, M.3    Loboda, A.4    Ens, W.5    Standing, K.G.6
  • 52
    • 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
  • 53
    • 0036518996 scopus 로고    scopus 로고
    • Phosphotyrosine-binding domains in signal transduction
    • Yaffe, M. B. Phosphotyrosine-binding domains in signal transduction. Nat. Rev. Mol. Cell Biol. 2002, 3, 177-186.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 177-186
    • Yaffe, M.B.1
  • 54
    • 0037453510 scopus 로고    scopus 로고
    • Assembly of cell regulatory systems through protein interaction domains
    • Pawson, T.; Nash, P. Assembly of cell regulatory systems through protein interaction domains. Science 2003, 300, 445-452.
    • (2003) Science , vol.300 , pp. 445-452
    • Pawson, T.1    Nash, P.2
  • 55
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold, R.; Mann, M. Mass spectrometry-based proteomics. Nature 2003, 422, 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 56
    • 0036020072 scopus 로고    scopus 로고
    • Clinical potential of proteomics in the diagnosis of ovarian cancer
    • Ardekani, A. M.; Liotta, L. A.; Petricoin, E. F., 3rd Clinical potential of proteomics in the diagnosis of ovarian cancer. Expert Rev. Mol. Diagn. 2002, 2, 312-320.
    • (2002) Expert Rev. Mol. Diagn. , vol.2 , pp. 312-320
    • Ardekani, A.M.1    Liotta, L.A.2    Petricoin III, E.F.3
  • 57
    • 0036324715 scopus 로고    scopus 로고
    • Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer
    • Li, J.; Zhang, Z.; Rosenzweig, J.; Wang, Y. Y.; Chan, D. W. Proteomics and bioinformatics approaches for identification of serum biomarkers to detect breast cancer. Clin. Chem. 2002, 48, 1296-1304.
    • (2002) Clin. Chem. , vol.48 , pp. 1296-1304
    • Li, J.1    Zhang, Z.2    Rosenzweig, J.3    Wang, Y.Y.4    Chan, D.W.5
  • 61
    • 0034625260 scopus 로고    scopus 로고
    • Drosophila Dscam is an axon guidance receptor exhibiting extraordinary molecular diversity
    • Schmucker, D.; Clemens, J. C.; Shu, H.; Worby, C. A.; Xiao, J.; Muda, M.; Dixon, J. E.; Zipursky, S. L. Drosophila Dscam is an axon guidance receptor exhibiting extraordinary molecular diversity. Cell 2000, 101, 671-684.
    • (2000) Cell , vol.101 , pp. 671-684
    • Schmucker, D.1    Clemens, J.C.2    Shu, H.3    Worby, C.A.4    Xiao, J.5    Muda, M.6    Dixon, J.E.7    Zipursky, S.L.8
  • 64
    • 0036493224 scopus 로고    scopus 로고
    • A question of size: The eukaryotic proteome and the problems in defining it
    • Harrison, P. M.; Kumar, A.; Lang, N.; Snyder, M.; Gerstein, M. A question of size: the eukaryotic proteome and the problems in defining it. Nucleic Acids Res. 2002, 30, 1083-1090.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1083-1090
    • Harrison, P.M.1    Kumar, A.2    Lang, N.3    Snyder, M.4    Gerstein, M.5
  • 65
    • 0037338297 scopus 로고    scopus 로고
    • Data analysis-the Achilles heel of proteomics
    • Patterson, S. D. Data analysis-the Achilles heel of proteomics. Nat. Biotechnol. 2003, 21, 221-222.
    • (2003) Nat. Biotechnol. , vol.21 , pp. 221-222
    • Patterson, S.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.