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Volumn 8, Issue 3, 2009, Pages 1143-1155

Human serum proteins fractionated by preparative partition chromatography prior to LC-ESI-MS/MS

Author keywords

Human serum; LC MS MS; Liquid chromatography; Preparative chromatography; Tryptic digest; XITANDEM

Indexed keywords

2 DIETHYLAMINOETHANOL; AMINE; CONCANAVALIN A; HEPARIN; HYDROXYAPATITE; PHENOL; PLASMA PROTEIN; PROTEIN G; RESIN;

EID: 65249161694     PISSN: 15353893     EISSN: None     Source Type: Journal    
DOI: 10.1021/pr8005217     Document Type: Article
Times cited : (43)

References (83)
  • 1
    • 13844271205 scopus 로고    scopus 로고
    • Biomarker discovery in biological fluids
    • Gao, J.; et al. Biomarker discovery in biological fluids. Methods 2005, 35, 291-302.
    • (2005) Methods , vol.35 , pp. 291-302
    • Gao, J.1
  • 2
    • 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
  • 3
    • 34248578524 scopus 로고    scopus 로고
    • Sample preparation for serum/ plasma profiling and biomarker identification by mass spectrometry
    • Luque-Garcia, J. L.; Neubert, T. A. Sample preparation for serum/ plasma profiling and biomarker identification by mass spectrometry. J. Chromatosr., A 2007, 1153, 259-76.
    • (2007) J. Chromatosr., A , vol.1153 , pp. 259-276
    • Luque-Garcia, J.L.1    Neubert, T.A.2
  • 4
    • 0037015062 scopus 로고    scopus 로고
    • Proteomic survey of metabolic pathways in rice
    • Koller, A.; et al. Proteomic survey of metabolic pathways in rice. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 11969-74.
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 11969-11974
    • Koller, A.1
  • 5
    • 4444275799 scopus 로고    scopus 로고
    • Human serum proteins preseparated by electrophoresis or chromatography followed by tandem mass spectrometry
    • Marshall, J.; et al. Human serum proteins preseparated by electrophoresis or chromatography followed by tandem mass spectrometry. J. Proteome Res. 2004, 3, 364-82.
    • (2004) J. Proteome Res , vol.3 , pp. 364-382
    • Marshall, J.1
  • 7
    • 34447547727 scopus 로고
    • Purification and physiological properties of factor VII from plasma and serum; separation from prothrombin
    • Duckert, F.; Koller, F.; Matter, M. Purification and physiological properties of factor VII from plasma and serum; separation from prothrombin. Proc. Soc. Exp. Biol. Med. 1953, 82, 259-61.
    • (1953) Proc. Soc. Exp. Biol. Med , vol.82 , pp. 259-261
    • Duckert, F.1    Koller, F.2    Matter, M.3
  • 8
    • 0020321012 scopus 로고
    • Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma
    • Tollefsen, D. M.; Majerus, D. W.; Blank, M. K. Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma. J. Biol. Chem. 1982, 257, 2162-9.
    • (1982) J. Biol. Chem , vol.257 , pp. 2162-2169
    • Tollefsen, D.M.1    Majerus, D.W.2    Blank, M.K.3
  • 9
    • 0014336534 scopus 로고
    • Retinol-binding protein: The transport protein for vitamin A in human plasma
    • Kanai, M.; Raz, A.; Goodman, D. S. Retinol-binding protein: the transport protein for vitamin A in human plasma. J. Clin. Invest. 1968, 47, 2025-4.
    • (1968) J. Clin. Invest , vol.47 , pp. 2025-2034
    • Kanai, M.1    Raz, A.2    Goodman, D.S.3
  • 10
    • 0014784309 scopus 로고
    • The isolation of human plasma prekallikrein
    • McConnell, D. J.; Mason, B. The isolation of human plasma prekallikrein. Br. J. Pharmacol. 1970, 38, 490-502.
    • (1970) Br. J. Pharmacol , vol.38 , pp. 490-502
    • McConnell, D.J.1    Mason, B.2
  • 11
    • 0019891557 scopus 로고
    • Application of ion-exchange chromatography for the production of human albumin
    • Vasileva, R.; Jakab, M.; Hasko, F. Application of ion-exchange chromatography for the production of human albumin. J. Chromatosr. 1981, 216, 279-84.
    • (1981) J. Chromatosr , vol.216 , pp. 279-284
    • Vasileva, R.1    Jakab, M.2    Hasko, F.3
  • 12
    • 0016836426 scopus 로고
    • The purification and partial characterization of an insulin-like protein from human serum
    • Poffenbarger, P. L. The purification and partial characterization of an insulin-like protein from human serum. J. Clin. Invest. 1975, 56, 1455-63.
    • (1975) J. Clin. Invest , vol.56 , pp. 1455-1463
    • Poffenbarger, P.L.1
  • 13
    • 0015635265 scopus 로고
    • Purification of human alpha 1-antitrypsin by affinity chromatography on sepharose bound concanavalin A
    • Murthy, R. J.; Hercz, A. Purification of human alpha 1-antitrypsin by affinity chromatography on sepharose bound concanavalin A. FEBS Lett. 1973, 32, 243-6.
    • (1973) FEBS Lett , vol.32 , pp. 243-246
    • Murthy, R.J.1    Hercz, A.2
  • 14
    • 46649086117 scopus 로고    scopus 로고
    • Comparison of protein expression lists from mass spectrometry of human blood fluids using exact peptide sequences versus BLAST
    • Zhu, P.; et al. Comparison of protein expression lists from mass spectrometry of human blood fluids using exact peptide sequences versus BLAST. Clin. Proteomics 2007, 2, 185.
    • (2007) Clin. Proteomics , vol.2 , pp. 185
    • Zhu, P.1
  • 15
    • 12444339443 scopus 로고    scopus 로고
    • The human serum proteome: Display of nearly 3700 chromatographically separated protein spots on two dimensional electrophoresis gels and identification of 325 distinct proteins
    • Pieper, R.; et al. The human serum proteome: display of nearly 3700 chromatographically separated protein spots on two dimensional electrophoresis gels and identification of 325 distinct proteins. Proteomics 2003, 3, 1345-64.
    • (2003) Proteomics , vol.3 , pp. 1345-1364
    • Pieper, R.1
  • 16
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen, J. V.; Ong, S. E.; Mann, M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol. Cell. Proteomics 2004, 3, 608-14.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 17
    • 0003206867 scopus 로고    scopus 로고
    • Toward a human blood serum proteome: Analysis by multidimensional separation coupled with mass spectrometry
    • Adkins, J. N.; et al. Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. Mol. Cell. Proteomics 2002, 1, 947-55.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 947-955
    • Adkins, J.N.1
  • 18
    • 0346364695 scopus 로고    scopus 로고
    • Characterization of the low molecular weight human serum proteome
    • Tirumalai, R. S.; et al. Characterization of the low molecular weight human serum proteome. Mol. Cell. Proteomics 2003, 2, 1096-103.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1096-1103
    • Tirumalai, R.S.1
  • 19
    • 1242316198 scopus 로고    scopus 로고
    • Ultra-high-efficiency strong cation exchange LC/ RPLC/MS/MS for high dynamic range characterization of the human plasma proteome
    • Shen, Y.; et al. Ultra-high-efficiency strong cation exchange LC/ RPLC/MS/MS for high dynamic range characterization of the human plasma proteome. Anal. Chem. 2004, 76, 1134-44.
    • (2004) Anal. Chem , vol.76 , pp. 1134-1144
    • Shen, Y.1
  • 20
    • 27144497658 scopus 로고    scopus 로고
    • Characterization of the human blood plasma proteome
    • Shen, Y.; et al. Characterization of the human blood plasma proteome. Proteomics 2005.
    • (2005) Proteomics
    • Shen, Y.1
  • 22
    • 0036209134 scopus 로고    scopus 로고
    • Qscore: An algorithm for evaluating SEQUEST database search results
    • Moore, R. E.; Young, M. K.; Lee, T. D. Qscore: an algorithm for evaluating SEQUEST database search results. J. Am. Soc. Mass Spectrom. 2002, 13, 378-86.
    • (2002) J. Am. Soc. Mass Spectrom , vol.13 , pp. 378-386
    • Moore, R.E.1    Young, M.K.2    Lee, T.D.3
  • 23
    • 0036873939 scopus 로고    scopus 로고
    • Analysis of the adenovirus type 5 proteome by liquid chromatography and tandem mass spectrometry methods
    • Chelius, D.; et al. Analysis of the adenovirus type 5 proteome by liquid chromatography and tandem mass spectrometry methods. J. Proteome Res. 2002, 1, 501-13.
    • (2002) J. Proteome Res , vol.1 , pp. 501-513
    • Chelius, D.1
  • 25
    • 17444421940 scopus 로고    scopus 로고
    • Human plasma proteome analysis by multidimensional chromatography prefractionation and linear ion trap mass spectrometry identification
    • Jin, W. H.; et al. Human plasma proteome analysis by multidimensional chromatography prefractionation and linear ion trap mass spectrometry identification. J. Proteome Res. 2005, 4, 613-9.
    • (2005) J. Proteome Res , vol.4 , pp. 613-619
    • Jin, W.H.1
  • 26
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO Plasma Proteome Project: Results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn, G. S.; et al. Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics 2005, 5, 3226-45.
    • (2005) Proteomics , vol.5 , pp. 3226-3245
    • Omenn, G.S.1
  • 27
    • 33644864034 scopus 로고    scopus 로고
    • Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study
    • States, D. J.; et al. Challenges in deriving high-confidence protein identifications from data gathered by a HUPO plasma proteome collaborative study. Nat. Biotechnol. 2006, 24, 333-8.
    • (2006) Nat. Biotechnol , vol.24 , pp. 333-338
    • States, D.J.1
  • 28
    • 33750682085 scopus 로고    scopus 로고
    • Evaluation of multiprotein immunoaffinity subtraction for plasma proteomics and candidate biomarker discovery using mass spectrometry
    • Liu, T.; et al. Evaluation of multiprotein immunoaffinity subtraction for plasma proteomics and candidate biomarker discovery using mass spectrometry. Mol. Cell. Proteomics 2006, 5, 2167-74.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 2167-2174
    • Liu, T.1
  • 29
    • 33847408371 scopus 로고    scopus 로고
    • Head-to-head comparison of serum fractionation techniques
    • Whiteaker, J. R.; et al. Head-to-head comparison of serum fractionation techniques. J. Proteome Res. 2007, 6, 828-36.
    • (2007) J. Proteome Res , vol.6 , pp. 828-836
    • Whiteaker, J.R.1
  • 30
    • 34948876373 scopus 로고    scopus 로고
    • Contribution of protein fractionation to depth of analysis of the serum and plasma proteomes
    • Faca, V.; et al. Contribution of protein fractionation to depth of analysis of the serum and plasma proteomes. J. Proteome Res. 2007, 6, 3558-65.
    • (2007) J. Proteome Res , vol.6 , pp. 3558-3565
    • Faca, V.1
  • 31
    • 35649018789 scopus 로고    scopus 로고
    • Proteomic analysis of human blood serum using peptide library beads
    • Sennels, L.; et al. Proteomic analysis of human blood serum using peptide library beads. J. Proteome Res. 2007, 6, 4055-62.
    • (2007) J. Proteome Res , vol.6 , pp. 4055-4062
    • Sennels, L.1
  • 32
    • 0032892697 scopus 로고    scopus 로고
    • Composition of the peptide fraction in human blood plasma: Database of circulating human peptides
    • Richter, R.; et al. Composition of the peptide fraction in human blood plasma: database of circulating human peptides. J. Chromatosr., B: Biomed. Sci. Appl. 1999, 726, 25-35.
    • (1999) J. Chromatosr., B: Biomed. Sci. Appl , vol.726 , pp. 25-35
    • Richter, R.1
  • 33
    • 33748575600 scopus 로고    scopus 로고
    • A novel approach and protocol for discovering extremely low-abundance proteins in serum
    • Tanaka, Y.; et al. A novel approach and protocol for discovering extremely low-abundance proteins in serum. Proteomics 2006, 6, 4845-55.
    • (2006) Proteomics , vol.6 , pp. 4845-4855
    • Tanaka, Y.1
  • 34
    • 33750728385 scopus 로고    scopus 로고
    • Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications
    • Qian, W. J.; Jacobs, J. M.; Liu, T.; Camp, D. G., II.; Smith, R. D. Advances and challenges in liquid chromatography-mass spectrometry-based proteomics profiling for clinical applications. Mol. Cell. Proteomics 2006, 5, 1727-44.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 1727-1744
    • Qian, W.J.1    Jacobs, J.M.2    Liu, T.3    Camp II, D.G.4    Smith, R.D.5
  • 35
    • 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, 16,2067-72.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 2067-2072
    • Guzzetta, A.W.1    Thakur, R.A.2    Mylchreest, I.C.3
  • 37
    • 0034652001 scopus 로고    scopus 로고
    • Involvement of cytosolic phospholipase A2 and secretory phospholipase A2 in arachidonic acid release from human neutrophils
    • Marshall, J.; et al. Involvement of cytosolic phospholipase A2 and secretory phospholipase A2 in arachidonic acid release from human neutrophils. J. Immunol. 2000, 164, 2084-91.
    • (2000) J. Immunol , vol.164 , pp. 2084-2091
    • Marshall, J.1
  • 38
    • 12444330378 scopus 로고    scopus 로고
    • Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction
    • Marshall, J.; et al. Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction. J. Proteome Res. 2003, 2, 361-72.
    • (2003) J. Proteome Res , vol.2 , pp. 361-372
    • Marshall, J.1
  • 39
    • 33644498846 scopus 로고    scopus 로고
    • Coelution of other proteins with albumin during size-exclusion HPLC: Implications for analysis of urinary albumin
    • Sviridov, D.; Meilinger, B.; Drake, S. K.; Hoehn, G. T.; Hortin, G. L. Coelution of other proteins with albumin during size-exclusion HPLC: Implications for analysis of urinary albumin. Clin. Chem. 2006, 52, 389-97.
    • (2006) Clin. Chem , vol.52 , pp. 389-397
    • Sviridov, D.1    Meilinger, B.2    Drake, S.K.3    Hoehn, G.T.4    Hortin, G.L.5
  • 40
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification data
    • Craig, R.; Cortens, J. P.; Beavis, R. C. Open source system for analyzing, validating, and storing protein identification data. J Proteome Res. 2004, 3, 1234-2.
    • (2004) J Proteome Res , vol.3 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 41
    • 0348203675 scopus 로고    scopus 로고
    • A relational model of data for large shared data banks. 1970
    • Codd, E. F. A relational model of data for large shared data banks. 1970. MD Comput. 1998, 15, 162-6.
    • (1998) MD Comput , vol.15 , pp. 162-166
    • Codd, E.F.1
  • 42
    • 0036211823 scopus 로고    scopus 로고
    • Field, H. I.; Fenyo, D.; Beavis, R. C. RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database. Proteomics 2002, 2, 36-47.
    • Field, H. I.; Fenyo, D.; Beavis, R. C. RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database. Proteomics 2002, 2, 36-47.
  • 43
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul, S. F.; et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 1997, 25, 3389-402.
    • (1997) Nucleic Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 44
    • 33645721632 scopus 로고    scopus 로고
    • Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins
    • Anderson, L.; Hunter, C. L. Quantitative mass spectrometric multiple reaction monitoring assays for major plasma proteins. Mol. Cell. Proteomics 2006, 5, 573-88.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 573-588
    • Anderson, L.1    Hunter, C.L.2
  • 45
    • 0942276226 scopus 로고    scopus 로고
    • Mining biomarkers in human sera using proteomic tools
    • Zhang, R.; et al. Mining biomarkers in human sera using proteomic tools. Proteomics 2004, 4, 244-56.
    • (2004) Proteomics , vol.4 , pp. 244-256
    • Zhang, R.1
  • 46
    • 33846665857 scopus 로고    scopus 로고
    • Antibody-based enrichment of peptides on magnetic beads for mass-spectrometry-based quantification of serum biomarkers
    • Whiteaker, J. R.; et al. Antibody-based enrichment of peptides on magnetic beads for mass-spectrometry-based quantification of serum biomarkers. Anal. Biochem. 2007, 362, 44-54.
    • (2007) Anal. Biochem , vol.362 , pp. 44-54
    • Whiteaker, J.R.1
  • 47
    • 0023945526 scopus 로고
    • Use of a scanning densitometer or an ELISA plate reader for measurement of nanogram amounts of protein in crude extracts from biological tissues
    • Ghosh, S.; Gepstein, S.; Heikkila, J. J.; Dumbroff, E. B. Use of a scanning densitometer or an ELISA plate reader for measurement of nanogram amounts of protein in crude extracts from biological tissues. Anal. Biochem. 1988, 169, 227-33.
    • (1988) Anal. Biochem , vol.169 , pp. 227-233
    • Ghosh, S.1    Gepstein, S.2    Heikkila, J.J.3    Dumbroff, E.B.4
  • 48
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H.; von Jagow, G. Tricine-sodium dodecyl sulfatepolyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166, 368-79.
    • (1987) Anal. Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 49
    • 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, 201-5.
    • (1988) Anal. Biochem , vol.173 , pp. 201-205
    • Schagger, H.1    Aquila, H.2    Von Jagow, G.3
  • 50
    • 0028210740 scopus 로고
    • Electrophoretic method for separating small peptides in serum without extraction of macromolecules: Application to the detection of preeclampsia
    • Dionne, R.; Forest, J. C.; Moutquin, J. M.; De Grandpre, P.; Masse, J. Electrophoretic method for separating small peptides in serum without extraction of macromolecules: application to the detection of preeclampsia. Clin. Biochem. 1994, 27, 99-103.
    • (1994) Clin. Biochem , vol.27 , pp. 99-103
    • Dionne, R.1    Forest, J.C.2    Moutquin, J.M.3    De Grandpre, P.4    Masse, J.5
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 52
    • 0032759676 scopus 로고    scopus 로고
    • Capillary electrophoresis/tandem mass spectrometry for analysis of proteins from two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis
    • Jin, X.; Chen, Y.; Lubman, D. M.; Misek, D.; Hanash, S. M. Capillary electrophoresis/tandem mass spectrometry for analysis of proteins from two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis. Rapid Commun. Mass Spectrom. 1999, 13, 232734.
    • (1999) Rapid Commun. Mass Spectrom , vol.13 , pp. 232734
    • Jin, X.1    Chen, Y.2    Lubman, D.M.3    Misek, D.4    Hanash, S.M.5
  • 53
    • 0037252705 scopus 로고    scopus 로고
    • Database resources of the National Center for Biotechnology
    • Wheeler, D. L.; et al. Database resources of the National Center for Biotechnology. Nucleic Acids Res. 2003, 31, 28-33.
    • (2003) Nucleic Acids Res , vol.31 , pp. 28-33
    • Wheeler, D.L.1
  • 54
    • 33846057724 scopus 로고    scopus 로고
    • NCBI reference sequences (RefSeq): A curated non-redundant sequence database of genomes, transcripts and proteins
    • Pruitt, K. D.; Tatusova, T.; Maglott, D. R. NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res. 2007, 35, D61-5.
    • (2007) Nucleic Acids Res , vol.35
    • Pruitt, K.D.1    Tatusova, T.2    Maglott, D.R.3
  • 56
    • 0033051101 scopus 로고    scopus 로고
    • ink, A. J.; et al. Direct analysis of protein complexes using mass pectrometry. Nat. Biotechnol. 1999, 17, 676-82.
    • ink, A. J.; et al. Direct analysis of protein complexes using mass pectrometry. Nat. Biotechnol. 1999, 17, 676-82.
  • 57
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem ass spectra
    • raig, R.; Beavis, R. C. TANDEM: matching proteins with tandem ass spectra. Bioinformatics 2004, 20, 1466-7.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • raig, R.1    Beavis, R.C.2
  • 58
    • 0038699625 scopus 로고    scopus 로고
    • Identification and uantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • hang, H.; Li, X. J.; Martin, D. B.; Aebersold, R. Identification and uantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat. Biotechnol. 2003, 21, 660-6.
    • (2003) Nat. Biotechnol , vol.21 , pp. 660-666
    • hang, H.1    Li, X.J.2    Martin, D.B.3    Aebersold, R.4
  • 59
    • 7044272787 scopus 로고    scopus 로고
    • Potential for false ositive identifications from large databases through tandem mass pectrometry
    • argile, B. J.; Bundy, J. L.; Stephenson, J. L., Jr. Potential for false ositive identifications from large databases through tandem mass pectrometry. J. Proteome Res. 2004, 3, 1082-5.
    • (2004) J. Proteome Res , vol.3 , pp. 1082-1085
    • argile, B.J.1    Bundy, J.L.2    Stephenson Jr, J.L.3
  • 60
    • 23944451618 scopus 로고    scopus 로고
    • app, E. A.; et al. An evaluation, comparison, and accurate enchmarking of several publicly available MS/MS search algorithms: sensitivity and specificity analysis. Proteomics 2005, 5, 3475-90.
    • app, E. A.; et al. An evaluation, comparison, and accurate enchmarking of several publicly available MS/MS search algorithms: sensitivity and specificity analysis. Proteomics 2005, 5, 3475-90.
  • 61
    • 43849101253 scopus 로고    scopus 로고
    • Comparison of mascot and X!tandem performance for low and high accuracy mass spectrometry and the development of an adjusted mascot threshold
    • Brosch, M.; Swamy, S.; Hubbard, T.; Choudhary, J. Comparison of mascot and X!tandem performance for low and high accuracy mass spectrometry and the development of an adjusted mascot threshold. Mol. Cell. Proteomics 2008.
    • (2008) Mol. Cell. Proteomics
    • Brosch, M.1    Swamy, S.2    Hubbard, T.3    Choudhary, J.4
  • 62
    • 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
  • 63
    • 0034848903 scopus 로고    scopus 로고
    • Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison
    • Wait, R. Proteins of rat serum, urine, and cerebrospinal fluid: VI. Further protein identifications and interstrain comparison. Electrophoresis 2001, 22, 3043-52.
    • (2001) Electrophoresis , vol.22 , pp. 3043-3052
    • Wait, R.1
  • 64
    • 0035984343 scopus 로고    scopus 로고
    • Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Bergquist, J.; Palmblad, M.; Wetterhall, M.; Hakansson, P.; Markides, K. E. Peptide mapping of proteins in human body fluids using electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Mass Spectrom. Rev. 2002, 21, 2-15.
    • (2002) Mass Spectrom. Rev , vol.21 , pp. 2-15
    • Bergquist, J.1    Palmblad, M.2    Wetterhall, M.3    Hakansson, P.4    Markides, K.E.5
  • 65
    • 33750364830 scopus 로고    scopus 로고
    • The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins
    • Adachi, J.; Kumar, C.; Zhang, Y.; Olsen, J. V.; Mann, M. The human urinary proteome contains more than 1500 proteins, including a large proportion of membrane proteins. GenomeBiolosy2006, 7, R80.
    • (2006) GenomeBiolosy , vol.7
    • Adachi, J.1    Kumar, C.2    Zhang, Y.3    Olsen, J.V.4    Mann, M.5
  • 66
    • 33745442821 scopus 로고    scopus 로고
    • The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome
    • Hortin, G. L. The MALDI-TOF mass spectrometric view of the plasma proteome and peptidome. Clin. Chem. 2006, 52, 1223-37.
    • (2006) Clin. Chem , vol.52 , pp. 1223-1237
    • Hortin, G.L.1
  • 67
    • 39749174515 scopus 로고    scopus 로고
    • Product ion monitoring assay for prostate specific antigen in serum using a linear ion-trap
    • Kulasingam, V.; et al. "Product ion monitoring" assay for prostate specific antigen in serum using a linear ion-trap. J. Proteome Res. 2008, 7, 640-647.
    • (2008) J. Proteome Res , vol.7 , pp. 640-647
    • Kulasingam, V.1
  • 68
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H.; Addona, T.; Burgess, M.; Kuhn, E.; Carr, S. A. Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 2007, 6, 2212-29.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 69
    • 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, 1056-64.
    • (2003) Rapid Commun. Mass Spectrom , vol.17 , pp. 1056-1064
    • Hager, J.W.1    Yves Le Blanc, J.C.2
  • 70
    • 0034130561 scopus 로고    scopus 로고
    • Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays
    • Brenner, S.; et al. Gene expression analysis by massively parallel signature sequencing (MPSS) on microbead arrays. Nat. Biotechnol. 2000, 18, 630-4.
    • (2000) Nat. Biotechnol , vol.18 , pp. 630-634
    • Brenner, S.1
  • 71
    • 0016272563 scopus 로고
    • A method for selective cloning of eukaryotic DNA fragments in Escherichia coli by repeated transformation
    • Cohen, S. N.; Chang, A. C. A method for selective cloning of eukaryotic DNA fragments in Escherichia coli by repeated transformation. Mol. Gen. Genet. 1974, 134, 133-41.
    • (1974) Mol. Gen. Genet , vol.134 , pp. 133-141
    • Cohen, S.N.1    Chang, A.C.2
  • 72
    • 10744231402 scopus 로고    scopus 로고
    • Whole-genome shotgun assembly and comparison of human genome assemblies
    • Istrail, S.; et al. Whole-genome shotgun assembly and comparison of human genome assemblies. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 1916-21.
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 1916-1921
    • Istrail, S.1
  • 74
    • 0030139470 scopus 로고    scopus 로고
    • Genome analysis with gene expression microarrays
    • Schena, M. Genome analysis with gene expression microarrays. BioEssays 1996, 18, 427-31.
    • (1996) BioEssays , vol.18 , pp. 427-431
    • Schena, M.1
  • 75
    • 0023047540 scopus 로고
    • Fluorescence detection in automated DNA sequence analysis
    • Smith, L. M.; et al. Fluorescence detection in automated DNA sequence analysis. Nature 1986, 321, 674-9.
    • (1986) Nature , vol.321 , pp. 674-679
    • Smith, L.M.1
  • 76
    • 0025202162 scopus 로고
    • Target amplification for DNA analysis by the poly merase chain reaction
    • Mullis, K. B. Target amplification for DNA analysis by the poly merase chain reaction. Ann. Biol. Clin. 1990, 48, 579-82.
    • (1990) Ann. Biol. Clin , vol.48 , pp. 579-582
    • Mullis, K.B.1
  • 77
    • 0035918027 scopus 로고    scopus 로고
    • Rapid separation of peptides and proteins by isocratic capillary electrochromatography at elevated temperature
    • Zhang, S.; Zhang, J.; Horvath, C. Rapid separation of peptides and proteins by isocratic capillary electrochromatography at elevated temperature. J. Chromatogr., A 2001, 914, 189-200.
    • (2001) J. Chromatogr., A , vol.914 , pp. 189-200
    • Zhang, S.1    Zhang, J.2    Horvath, C.3
  • 78
    • 37049003330 scopus 로고    scopus 로고
    • Two-dimensional separation of human plasma proteins using iterative free-flow electrophoresis
    • Nissum, M.; et al. Two-dimensional separation of human plasma proteins using iterative free-flow electrophoresis. Proteomics 2007, 7, 4218-27.
    • (2007) Proteomics , vol.7 , pp. 4218-4227
    • Nissum, M.1
  • 79
    • 33746225435 scopus 로고    scopus 로고
    • Design considerations for high speed quantitative mass spectrometry with MALDI ionization
    • Corr, J. J.; et al. Design considerations for high speed quantitative mass spectrometry with MALDI ionization. J. Am. Soc. Mass Spectrom. 2006, 17, 1129-41.
    • (2006) J. Am. Soc. Mass Spectrom , vol.17 , pp. 1129-1141
    • Corr, J.J.1
  • 80
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov, I. V.; et al. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-55.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1
  • 81
    • 34748898371 scopus 로고    scopus 로고
    • Endogenous peptides from biophysical and biochemical fractionation of serum analyzed by matrix-assisted laser desorption/ionization and electrospray ionization hybrid quadrupole time-of-flight
    • Tucholska, M.; et al. Endogenous peptides from biophysical and biochemical fractionation of serum analyzed by matrix-assisted laser desorption/ionization and electrospray ionization hybrid quadrupole time-of-flight. Anal. Biochem. 2007, 370, 228-45.
    • (2007) Anal. Biochem , vol.370 , pp. 228-245
    • Tucholska, M.1
  • 82
    • 23944523358 scopus 로고    scopus 로고
    • A functional annotation of subproteomes in human plasma
    • Ping, P.; et al. A functional annotation of subproteomes in human plasma. Proteomics 2005, 5, 3506-19.
    • (2005) Proteomics , vol.5 , pp. 3506-3519
    • Ping, P.1
  • 83
    • 13244279455 scopus 로고    scopus 로고
    • Comparison of different depletion strategies for improved resolution in proteomic analysis of human serum samples
    • Bjorhall, K.; Miliotis, T.; Davidsson, P. Comparison of different depletion strategies for improved resolution in proteomic analysis of human serum samples. Proteomics 2005, 5, 307-17.
    • (2005) Proteomics , vol.5 , pp. 307-317
    • Bjorhall, K.1    Miliotis, T.2    Davidsson, P.3


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