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Volumn 103, Issue 10, 2004, Pages 3624-3634

Proteomics techniques and their application to hematology

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTIC METHOD; GENE SEQUENCE; GENOMICS; HEMATOLOGY; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEOMICS; REVIEW; TRANSLATION REGULATION;

EID: 2342541676     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-09-3295     Document Type: Review
Times cited : (107)

References (99)
  • 1
    • 0026791936 scopus 로고
    • Post-translational chemical modification(s) of proteins
    • Han KK, Martinage A. Post-translational chemical modification(s) of proteins. Int J Biochem. 1992; 24:19-28.
    • (1992) Int J Biochem , vol.24 , pp. 19-28
    • Han, K.K.1    Martinage, A.2
  • 2
    • 0034646232 scopus 로고    scopus 로고
    • Gene microarray identification of redox and mitochondrial elements that control resistance or sensitivity to apoptosis
    • Voehringer DW, Hirschberg DL, Xiao J, et al. Gene microarray identification of redox and mitochondrial elements that control resistance or sensitivity to apoptosis. Proc Natl Acad Sci U S A. 2000;;97:2680-2695.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 2680-2695
    • Voehringer, D.W.1    Hirschberg, D.L.2    Xiao, J.3
  • 5
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygl SP, Rochon Y, Franza BR, Aebersold R. Correlation between protein and mRNA abundance in yeast. Mol Cell Biol. 1999;19:1720-1730.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygl, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 6
    • 0036839597 scopus 로고    scopus 로고
    • Genomic and proteomic analysis of the myeloid differentiation program: Global analysis of gene expression during induced differentiation in the MPRO cell line
    • Lian Z, Kluger Y, Greenbaum DS, et al. Genomic and proteomic analysis of the myeloid differentiation program: global analysis of gene expression during induced differentiation in the MPRO cell line. Blood. 2002;100:3209-3220.
    • (2002) Blood , vol.100 , pp. 3209-3220
    • Lian, Z.1    Kluger, Y.2    Greenbaum, D.S.3
  • 7
    • 0037294859 scopus 로고    scopus 로고
    • Proteome analysis at the level of subcellular structures
    • Dreger M. Proteome analysis at the level of subcellular structures. Eur J Biochem. 2003;270:569-599.
    • (2003) Eur J Biochem , vol.270 , pp. 569-599
    • Dreger, M.1
  • 8
    • 0038364020 scopus 로고    scopus 로고
    • Organelle proteomics: Implications for subcellular fractionation in proteomics
    • Huber LA, Pfaller K, Vietor I. Organelle proteomics: implications for subcellular fractionation in proteomics. Circ Res. 2003;92:962-966.
    • (2003) Circ Res , vol.92 , pp. 962-966
    • Huber, L.A.1    Pfaller, K.2    Vietor, I.3
  • 9
    • 0034095972 scopus 로고    scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Gorg A, Obermaier C, Boguth G, et al. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis. 2000; 21:1037-1053.
    • (2000) Electrophoresis , vol.21 , pp. 1037-1053
    • Gorg, A.1    Obermaier, C.2    Boguth, G.3
  • 11
    • 0033572464 scopus 로고    scopus 로고
    • A luminescent ruthenium complex for ultrasensitive detection of proteins immobilized on membrane supports
    • Berggren K, Steinberg TH, Lauber WM, et al. A luminescent ruthenium complex for ultrasensitive detection of proteins immobilized on membrane supports. Anal Biochem. 1999;276:129-143.
    • (1999) Anal Biochem , vol.276 , pp. 129-143
    • Berggren, K.1    Steinberg, T.H.2    Lauber, W.M.3
  • 12
    • 0035289178 scopus 로고    scopus 로고
    • Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology
    • Tonge R, Shaw J, Middleton B, et al. Validation and development of fluorescence two-dimensional differential gel electrophoresis proteomics technology. Proteomics. 2001;1:377-396.
    • (2001) Proteomics , vol.1 , pp. 377-396
    • Tonge, R.1    Shaw, J.2    Middleton, B.3
  • 13
  • 14
    • 1942459748 scopus 로고    scopus 로고
    • Proteomic analysis of chronic lymphocytic leukemia subtypes with mutated or unmutated Ig VH genes
    • Cochran DAE, Evans CA, Blinco D, et al. Proteomic analysis of chronic lymphocytic leukemia subtypes with mutated or unmutated Ig VH genes. Mol Cell Proteomics. 2004;2:1331-1341.
    • (2004) Mol Cell Proteomics , vol.2 , pp. 1331-1341
    • Cochran, D.A.E.1    Evans, C.A.2    Blinco, D.3
  • 15
    • 0033838003 scopus 로고    scopus 로고
    • Towards high performance two-dimensional gel electrophoresis using ultrazoom gels
    • Hoving S, Voshol H, van Oostrum J. Towards high performance two-dimensional gel electrophoresis using ultrazoom gels. Electrophoresis. 2000;21:2617-2621.
    • (2000) Electrophoresis , vol.21 , pp. 2617-2621
    • Hoving, S.1    Voshol, H.2    Van Oostrum, J.3
  • 16
    • 0003206867 scopus 로고    scopus 로고
    • Toward a human blood serum proteome: Analysis by multidimensional separation coupled with mass spectrometry
    • Adkins JN, Vamum SM, Auberry KJ, et al. Toward a human blood serum proteome: analysis by multidimensional separation coupled with mass spectrometry. Mol Cell Proteomics. 2002;1947-955.
    • (2002) Mol Cell Proteomics , pp. 1947-1955
    • Adkins, J.N.1    Vamum, S.M.2    Auberry, K.J.3
  • 17
    • 0027427931 scopus 로고
    • Two-dimensional gel electrophoresis of four serum samples from patients with IgD myeloma
    • Stulik J, Tichy M, Kovarova H. Two-dimensional gel electrophoresis of four serum samples from patients with IgD myeloma. Clin Chim Acta. 1993; 218:149-158.
    • (1993) Clin Chim Acta , vol.218 , pp. 149-158
    • Stulik, J.1    Tichy, M.2    Kovarova, H.3
  • 18
    • 0035895071 scopus 로고    scopus 로고
    • Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin
    • Skibeli V, Nissen-Lie G, Torjesen P. Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin. Blood. 2001;98:3626-3634.
    • (2001) Blood , vol.98 , pp. 3626-3634
    • Skibeli, V.1    Nissen-Lie, G.2    Torjesen, P.3
  • 19
    • 0035289185 scopus 로고    scopus 로고
    • Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells
    • Csar XF, Wilson NJ, Strike P, et al. Copper/zinc superoxide dismutase is phosphorylated and modulated specifically by granulocyte-colony stimulating factor in myeloid cells. Proteomics. 2001;1:435-443.
    • (2001) Proteomics , vol.1 , pp. 435-443
    • Csar, X.F.1    Wilson, N.J.2    Strike, P.3
  • 20
    • 0034517388 scopus 로고    scopus 로고
    • Identification of novel MAP kinase pathway signaling targets by functional proteomics and mass spectrometry
    • Lewis TS, Hunt JB, Aveline LD, et al. Identification of novel MAP kinase pathway signaling targets by functional proteomics and mass spectrometry. Mol Cell. 2000;6:1343-1354.
    • (2000) Mol Cell , vol.6 , pp. 1343-1354
    • Lewis, T.S.1    Hunt, J.B.2    Aveline, L.D.3
  • 21
    • 0041663987 scopus 로고    scopus 로고
    • Quantitative analysis of protein phosphorylation status and protein kinase activity on microarrays using a novel fluorescent phosphorylation sensor dye
    • Martin K, Steinberg TH, Cooley LA, Gee KR, Beechem JM, Patton WF. Quantitative analysis of protein phosphorylation status and protein kinase activity on microarrays using a novel fluorescent phosphorylation sensor dye. Proteomics. 2003;3: 1244-1255.
    • (2003) Proteomics , vol.3 , pp. 1244-1255
    • Martin, K.1    Steinberg, T.H.2    Cooley, L.A.3    Gee, K.R.4    Beechem, J.M.5    Patton, W.F.6
  • 22
    • 0037337310 scopus 로고    scopus 로고
    • A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling
    • Blagoev B, Kratchmarova I, Ong SE, Nielsen M, Foster LJ, Mann M. A proteomics strategy to elucidate functional protein-protein interactions applied to EGF signaling. Nat Biotechnol. 2003;21: 315-316.
    • (2003) Nat Biotechnol , vol.21 , pp. 315-316
    • Blagoev, B.1    Kratchmarova, I.2    Ong, S.E.3    Nielsen, M.4    Foster, L.J.5    Mann, M.6
  • 23
    • 0037332128 scopus 로고    scopus 로고
    • Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion
    • van Anken E, Romijn EP, Maggioni C, et al. Sequential waves of functionally related proteins are expressed when B cells prepare for antibody secretion. Immunity. 2003;16:243-253.
    • (2003) Immunity , vol.16 , pp. 243-253
    • Van Anken, E.1    Romijn, E.P.2    Maggioni, C.3
  • 24
    • 0036241045 scopus 로고    scopus 로고
    • Identification of novel targets for cancer therapy using expression proteomics
    • Hanash SM, Madoz-Gurpide J, Misek DE. Identification of novel targets for cancer therapy using expression proteomics. Leukemia. 2002;16:476-485.
    • (2002) Leukemia , vol.16 , pp. 476-485
    • Hanash, S.M.1    Madoz-Gurpide, J.2    Misek, D.E.3
  • 26
    • 0036276743 scopus 로고    scopus 로고
    • Cytotoxicity of flutamide and 2-hydroxyflutamide and their effects on CYP1A2 mRNA in primary rat hepatocytes
    • Wang HX, Ma XC, Deng QL, Li D. Cytotoxicity of flutamide and 2-hydroxyflutamide and their effects on CYP1A2 mRNA in primary rat hepatocytes. Acta Pharmacol Sin. 2002;23:562-566.
    • (2002) Acta Pharmacol Sin , vol.23 , pp. 562-566
    • Wang, H.X.1    Ma, X.C.2    Deng, Q.L.3    Li, D.4
  • 27
    • 0036857628 scopus 로고    scopus 로고
    • Proteomic analysis of human eosinophil activation mediated by mast cells, granulocyte macrophage colony stimulating factor and tumor necrosis factor alpha
    • Levi-Schaffer F, Temkin V, Simon HU, Kettman JR, Frey JR, Lefkovits I. Proteomic analysis of human eosinophil activation mediated by mast cells, granulocyte macrophage colony stimulating factor and tumor necrosis factor alpha. Proteomics. 2002;2:1616-1626.
    • (2002) Proteomics , vol.2 , pp. 1616-1626
    • Levi-Schaffer, F.1    Temkin, V.2    Simon, H.U.3    Kettman, J.R.4    Frey, J.R.5    Lefkovits, I.6
  • 28
    • 0035895890 scopus 로고    scopus 로고
    • Proteomics characterization of abundant Golgi membrone brane proteins
    • Bell AW, Ward MA, Blackstock WP, et al. Proteomics characterization of abundant Golgi membrone brane proteins. J Biol Chem. 2001;276:5152-5165.
    • (2001) J Biol Chem , vol.276 , pp. 5152-5165
    • Bell, A.W.1    Ward, M.A.2    Blackstock, W.P.3
  • 29
    • 0037039159 scopus 로고    scopus 로고
    • Directed proteomic analysis of the human nucleolus
    • Andersen JS, Lyon CE, Fox AH, et al. Directed proteomic analysis of the human nucleolus. Curr Biol. 2002;12:1-11.
    • (2002) Curr Biol , vol.12 , pp. 1-11
    • Andersen, J.S.1    Lyon, C.E.2    Fox, A.H.3
  • 30
    • 0035825154 scopus 로고    scopus 로고
    • The phagosome proteome: Insight into phagosome functions
    • Garin J, Diez R, Kieffer S, et al. The phagosome proteome: insight into phagosome functions. J Cell Biol. 2001;152:165-160.
    • (2001) J Cell Biol , vol.152 , pp. 165-160
    • Garin, J.1    Diez, R.2    Kieffer, S.3
  • 31
    • 0038316341 scopus 로고    scopus 로고
    • ER-mediated phagocytosis: A new membrane for new functions
    • Desjardins M. ER-mediated phagocytosis: a new membrane for new functions. Nat Rev Immunol. 2003;3:280-291.
    • (2003) Nat Rev Immunol , vol.3 , pp. 280-291
    • Desjardins, M.1
  • 32
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link AJ, Eng J, Schieltz DM, et al. Direct analysis of protein complexes using mass spectrometry. Nat Biotechnol. 1999;17:676-682.
    • (1999) Nat Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1    Eng, J.2    Schieltz, D.M.3
  • 33
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washbum MP, Wolters D, Yates JR 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
    • Washbum, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 34
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R, Mann M. Mass spectrometry-based proteomics. Nature. 2003;422:196-207.
    • (2003) Nature , vol.422 , pp. 196-207
    • Aebersold, R.1    Mann, M.2
  • 35
    • 8944258107 scopus 로고    scopus 로고
    • A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (beta 67[E11] Val-Met → Asp)
    • Rees DC, Rochette J, Schofield C, et al. A novel silent posttranslational mechanism converts methionine to aspartate in hemoglobin Bristol (beta 67[E11] Val-Met → Asp). Blood. 1996;66:341-348.
    • (1996) Blood , vol.66 , pp. 341-348
    • Rees, D.C.1    Rochette, J.2    Schofield, C.3
  • 36
    • 18444392397 scopus 로고    scopus 로고
    • Detection of a novel variant human hemoglobin by electrospray ionization mass spectrometry
    • Troxler H, Neuheiser F, Kleinert P, et al. Detection of a novel variant human hemoglobin by electrospray ionization mass spectrometry. Biochem Biophys Res Commun. 2002;292:1044-1047.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 1044-1047
    • Troxler, H.1    Neuheiser, F.2    Kleinert, P.3
  • 37
    • 0035892131 scopus 로고    scopus 로고
    • Direct evidence that leukemic cells present HLA-associated immunogenic peptides derived from the BCR-ABL b3a2 fusion protein
    • Clark RE, Dodi IA, Hill SC, et al. Direct evidence that leukemic cells present HLA-associated immunogenic peptides derived from the BCR-ABL b3a2 fusion protein. Blood. 2001;98:2887-2893.
    • (2001) Blood , vol.98 , pp. 2887-2893
    • Clark, R.E.1    Dodi, I.A.2    Hill, S.C.3
  • 38
    • 0037015610 scopus 로고    scopus 로고
    • Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry
    • Lasonder E, Ishihama Y, Andersen JS, et al. Analysis of the Plasmodium falciparum proteome by high-accuracy mass spectrometry. Nature. 2002; 419:537-542.
    • (2002) Nature , vol.419 , pp. 537-542
    • Lasonder, E.1    Ishihama, Y.2    Andersen, J.S.3
  • 40
    • 0038015626 scopus 로고    scopus 로고
    • Changes in the proteome associated with the action of bcr-abl tyrosine kinase are not related to transcriptional regulation
    • Smith DL, Evans CA, Pierce A, Gaskell SJ, Whetton AD. Changes in the proteome associated with the action of bcr-abl tyrosine kinase are not related to transcriptional regulation. Mol Cell Proteomics. 2002;1:676-664.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 676-664
    • Smith, D.L.1    Evans, C.A.2    Pierce, A.3    Gaskell, S.J.4    Whetton, A.D.5
  • 41
    • 0036079692 scopus 로고    scopus 로고
    • The SELDI-TOF MS approach to proteomics: Protein profiling and biomarker identification
    • Issaq HJ, Veenstra TD, Conrads TP, Felschow D. The SELDI-TOF MS approach to proteomics: protein profiling and biomarker identification. Biochem Biophys Res Commun. 2002;292:567-592.
    • (2002) Biochem Biophys Res Commun , vol.292 , pp. 567-592
    • Issaq, H.J.1    Veenstra, T.D.2    Conrads, T.P.3    Felschow, D.4
  • 42
    • 0037116832 scopus 로고    scopus 로고
    • Use of proteomic patterns in serum to identify ovarian cancer
    • Petricoin EF, Ardekani AM, Hitt BA, et al. Use of proteomic patterns in serum to identify ovarian cancer. Lancet. 2002;359:572-577.
    • (2002) Lancet , vol.359 , pp. 572-577
    • Petricoin, E.F.1    Ardekani, A.M.2    Hitt, B.A.3
  • 44
    • 0037683738 scopus 로고    scopus 로고
    • Discovery of distinct protein profiles specific for lung tumors and premalignant lung lesions by SELDI mass spectrometry
    • Zhukov TA, Johanson RA, Cantor AB, Clark RA, Tockman MS. Discovery of distinct protein profiles specific for lung tumors and premalignant lung lesions by SELDI mass spectrometry. Lung Cancer. 2003;40:267-279.
    • (2003) Lung Cancer , vol.40 , pp. 267-279
    • Zhukov, T.A.1    Johanson, R.A.2    Cantor, A.B.3    Clark, R.A.4    Tockman, M.S.5
  • 45
    • 0036665376 scopus 로고    scopus 로고
    • ProteinChip technology: A new and facile method for the identification and measurement of high-density lipoproteins apoA-I and apoA-II and their glycosylated products in patients with diabetes and cardiovascular disease
    • Dayal B, Ertel NH. ProteinChip technology: a new and facile method for the identification and measurement of high-density lipoproteins apoA-I and apoA-II and their glycosylated products in patients with diabetes and cardiovascular disease. J Proteome Res. 2002;1:375-380.
    • (2002) J Proteome Res , vol.1 , pp. 375-380
    • Dayal, B.1    Ertel, N.H.2
  • 46
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli RM, Farmer TB, Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem. 1997;69:4751-4760.
    • (1997) Anal Chem , vol.69 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 47
    • 0041735992 scopus 로고    scopus 로고
    • Proteornic patterns of tumour subsets in non-small-cell lung cancer
    • Yanagisawa K, Shyr Y, Xu BJ, et al. Proteornic patterns of tumour subsets in non-small-cell lung cancer. Lancet. 2003;362:433-439.
    • (2003) Lancet , vol.362 , pp. 433-439
    • Yanagisawa, K.1    Shyr, Y.2    Xu, B.J.3
  • 49
    • 0027344077 scopus 로고
    • Edman degradation sequence analysis of resin-bound peptides synthesized by 9-fluorenylmethoxycarbonyl chemistry
    • Fields CG, VanDrisse VL, Fields GB. Edman degradation sequence analysis of resin-bound peptides synthesized by 9-fluorenylmethoxycarbonyl chemistry. Pept Res. 1993;6:39-47.
    • (1993) Pept Res , vol.6 , pp. 39-47
    • Fields, C.G.1    VanDrisse, V.L.2    Fields, G.B.3
  • 50
    • 0030200905 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ion trap mass spectrometry: Efficient isolation and effective fragmentation of peptide ions
    • Qin J, Chait BT. Matrix-assisted laser desorption ion trap mass spectrometry: efficient isolation and effective fragmentation of peptide ions. Anal Chem. 1996;66:2106-2112.
    • (1996) Anal Chem , vol.66 , pp. 2106-2112
    • Qin, J.1    Chait, B.T.2
  • 51
    • 0034132537 scopus 로고    scopus 로고
    • The characteristics of peptide collision-induced dissociation using a high-performance MALDI-TOF/TOF tandem mass spectrometer
    • Medzihradszky KF, Campbell JM, Baldwin MA, et al. 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
  • 52
    • 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 AV, Krutchinsky AN, Bromirski M, Ens W, Standing KG. 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
  • 53
    • 0027608882 scopus 로고
    • Use of mass spectrometric molecular weight information to identify proteins in sequence databases
    • Mann M, Hoirup P, Roepstorff P. Use of mass spectrometric molecular weight information to identify proteins in sequence databases. Biol Mass Spectrom. 1993;22:338-345.
    • (1993) Biol Mass Spectrom , vol.22 , pp. 338-345
    • Mann, M.1    Hoirup, P.2    Roepstorff, P.3
  • 54
    • 0027375364 scopus 로고
    • Peptide mass maps: A highly informative approach to protein identification
    • Yates JR 3rd, Speicher S, Griffin PR, Hunkapiller T. Peptide mass maps: a highly informative approach to protein identification. Anal Biochem. 1993;214:397-408.
    • (1993) Anal Biochem , vol.214 , pp. 397-408
    • Yates III, J.R.1    Speicher, S.2    Griffin, P.R.3    Hunkapiller, T.4
  • 55
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR 3rd. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994;5:976-989.
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 56
    • 0031865293 scopus 로고    scopus 로고
    • Protein identification using mass spectrometric information
    • Fenyo D, Qin J, Chait BT. Protein identification using mass spectrometric information. Electrophoresis. 1998;19:998-1005.
    • (1998) Electrophoresis , vol.19 , pp. 998-1005
    • Fenyo, D.1    Qin, J.2    Chait, B.T.3
  • 57
    • 0035563749 scopus 로고    scopus 로고
    • Gas-phase cleavage of PTC-derivatized electrosprayed tryptic peptides in an FT-ICR trapped-ion cell: Mass-based protein identification without liquid chromatographic separation
    • van der Rest G, He F, Emmett MR, Marshall AG, Gaskell SJ. Gas-phase cleavage of PTC-derivatized electrosprayed tryptic peptides in an FT-ICR trapped-ion cell: mass-based protein identification without liquid chromatographic separation. J Am Soc Mass Spectrom. 2001;12:288-295.
    • (2001) J Am Soc Mass Spectrom , vol.12 , pp. 288-295
    • Van Der Rest, G.1    He, F.2    Emmett, M.R.3    Marshall, A.G.4    Gaskell, S.J.5
  • 58
    • 0033783397 scopus 로고    scopus 로고
    • Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides
    • Brancia FL, Oliver SG, Gaskell SJ. Improved matrix-assisted laser desorption/ionization mass spectrometric analysis of tryptic hydrolysates of proteins following guanidination of lysine-containing peptides. Rapid Commun Mass Spectrom. 2000;14:2070-2073.
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 2070-2073
    • Brancia, F.L.1    Oliver, S.G.2    Gaskell, S.J.3
  • 59
    • 0036708081 scopus 로고    scopus 로고
    • Proteomics goes quantitative: Measuring protein abundance
    • Steen H, Pandey A. Proteomics goes quantitative: measuring protein abundance. Trends Biotechnol. 2002;20:361-364.
    • (2002) Trends Biotechnol , vol.20 , pp. 361-364
    • Steen, H.1    Pandey, A.2
  • 60
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han DK, Eng J, Zhou H, Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol. 2001;19:946-951.
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 61
    • 0031052452 scopus 로고    scopus 로고
    • Protein molecular mass to 1 Da by 13C 15N double depletion and FT-ICR mass spectrometry
    • Marshall AG, Senko MW, Li W, et al. Protein molecular mass to 1 Da by 13C 15N double depletion and FT-ICR mass spectrometry. J Am Chem Soc. 1997;119:433-434.
    • (1997) J Am Chem Soc , vol.119 , pp. 433-434
    • Marshall, A.G.1    Senko, M.W.2    Li, W.3
  • 62
    • 18344389894 scopus 로고    scopus 로고
    • Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprinting
    • Pratt JM, Robertson DH, Gaskell SJ, et al. Stable isotope labelling in vivo as an aid to protein identification in peptide mass fingerprinting. Proteomics. 2002;2:157-163.
    • (2002) Proteomics , vol.2 , pp. 157-163
    • Pratt, J.M.1    Robertson, D.H.2    Gaskell, S.J.3
  • 63
    • 2342654848 scopus 로고    scopus 로고
    • [doctoral dissertation]. Manchester, United Kingdom: University of Manchester Institute of Science and Technology
    • Cristea IM. Proteome changes during early stages of cell injury [doctoral dissertation]. Manchester, United Kingdom: University of Manchester Institute of Science and Technology. 2002.
    • (2002) Proteome Changes during Early Stages of Cell Injury
    • Cristea, I.M.1
  • 64
    • 0037417791 scopus 로고    scopus 로고
    • Quantitation of changes in protein phosphorylation: A simple method based on stable isotope labeling and mass spectrometry
    • Bonenfant D, Schmeizie T, Jacinto E, et al. Quantitation of changes in protein phosphorylation: a simple method based on stable isotope labeling and mass spectrometry. Proc Natl Acad Sci U S A. 2003;100:880-885.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 880-885
    • Bonenfant, D.1    Schmeizie, T.2    Jacinto, E.3
  • 65
    • 0035282172 scopus 로고    scopus 로고
    • Quantitative proteomic analysis using a MALDI quadrupole time-of-flight mass spectrometer
    • Griffin TJ, Gygi SP, Rist B, et al. Quantitative proteomic analysis using a MALDI quadrupole time-of-flight mass spectrometer. Anal Chem. 2001;73: 978-988.
    • (2001) Anal Chem , vol.73 , pp. 978-988
    • Griffin, T.J.1    Gygi, S.P.2    Rist, B.3
  • 66
    • 0036669447 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis; better than a poke in the ICAT?
    • Patton WF, Schulenberg B, Steinberg TH. Two-dimensional gel electrophoresis; better than a poke in the ICAT? Curr Opin Biotechnol. 2002;13: 321-328.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 321-328
    • Patton, W.F.1    Schulenberg, B.2    Steinberg, T.H.3
  • 68
    • 0346668199 scopus 로고    scopus 로고
    • Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards
    • Barnidge DR, Dratz EA, Martin T, Bonilla LE, Moran LB, Lindall A. Absolute quantification of the G protein-coupled receptor rhodopsin by LC/MS/MS using proteolysis product peptides and synthetic peptide standards. Anal Chem. 2003;75:445-451.
    • (2003) Anal Chem , vol.75 , pp. 445-451
    • Barnidge, D.R.1    Dratz, E.A.2    Martin, T.3    Bonilla, L.E.4    Moran, L.B.5    Lindall, A.6
  • 69
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci U S A. 2003;100:6940-6945.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 70
    • 0031127851 scopus 로고    scopus 로고
    • Cell biology and the genome projects - A concerted strategy for characterizing multiprotein complexes by using mass spectrometry
    • Lamond AI, Mann M. Cell biology and the genome projects - a concerted strategy for characterizing multiprotein complexes by using mass spectrometry. Trends Cell Biol. 1998;7:135-174.
    • (1998) Trends Cell Biol , vol.7 , pp. 135-174
    • Lamond, A.I.1    Mann, M.2
  • 71
    • 0035860499 scopus 로고    scopus 로고
    • Global analysis of protein activities using proteome chips
    • Zhu H, Bilgin M, Bangham R, et al. Global analysis of protein activities using proteome chips. Science. 2001;293:2101-2105.
    • (2001) Science , vol.293 , pp. 2101-2105
    • Zhu, H.1    Bilgin, M.2    Bangham, R.3
  • 72
    • 0036230933 scopus 로고    scopus 로고
    • Zeptosens' protein microarrays: A novel high performance microarray platform for low abundance protein analysis
    • Pawiak M, Schick E, Bopp MA, Schneider MJ, Oroszlan P, Ehrat M. Zeptosens' protein microarrays: a novel high performance microarray platform for low abundance protein analysis. Proteomics. 2002;2:383-393.
    • (2002) Proteomics , vol.2 , pp. 383-393
    • Pawiak, M.1    Schick, E.2    Bopp, M.A.3    Schneider, M.J.4    Oroszlan, P.5    Ehrat, M.6
  • 73
    • 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
  • 74
    • 0035159659 scopus 로고    scopus 로고
    • Protein arrays: Issues to be addressed: The chairperson's introduction to the session peptide and protein chips from the ESF workshop Proteomics: Focus on protein interactions
    • Taussig MJ. Protein arrays: issues to be addressed: The chairperson's introduction to the session peptide and protein chips from the ESF workshop Proteomics: focus on protein interactions. Comp Functional Genomics. 2001;2:298-300.
    • (2001) Comp Functional Genomics , vol.2 , pp. 298-300
    • Taussig, M.J.1
  • 75
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath G, Schreiber SL. Printing proteins as microarrays for high-throughput function determination. Science. 2000;289:1760-1783.
    • (2000) Science , vol.289 , pp. 1760-1783
    • MacBeath, G.1    Schreiber, S.L.2
  • 77
    • 0035489334 scopus 로고    scopus 로고
    • Proteomics: An holistic analysis of nature's proteins
    • Hebestreit HF. Proteomics: an holistic analysis of nature's proteins. Curr Opin Pharmacol. 2001;1: 513-520.
    • (2001) Curr Opin Pharmacol , vol.1 , pp. 513-520
    • Hebestreit, H.F.1
  • 80
    • 0031563773 scopus 로고    scopus 로고
    • Oligonucleotide inhibitors of human thrombin that bind distinct epitopes
    • Tasset DM, Kubik MF, Steiner W. Oligonucleotide inhibitors of human thrombin that bind distinct epitopes. J Mol Biol. 1997;272:688-698.
    • (1997) J Mol Biol , vol.272 , pp. 688-698
    • Tasset, D.M.1    Kubik, M.F.2    Steiner, W.3
  • 82
    • 0031241394 scopus 로고    scopus 로고
    • Identification and characterization of posttranslational modifications of proteins by MALDI ion trap mass spectrometry
    • Qin J, Chait BT. Identification and characterization of posttranslational modifications of proteins by MALDI ion trap mass spectrometry. Anal Chem. 1997;69:4002-4009.
    • (1997) Anal Chem , vol.69 , pp. 4002-4009
    • Qin, J.1    Chait, B.T.2
  • 83
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts JD, Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol. 2001;19:375-378.
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3
  • 84
    • 0035478709 scopus 로고    scopus 로고
    • Analysis of phosphorylated proteins and peptides by mass spectrometry
    • McLachlin DT, Chait BT. Analysis of phosphorylated proteins and peptides by mass spectrometry. Curr Opin Chem Biol. 2001;5:591-602.
    • (2001) Curr Opin Chem Biol , vol.5 , pp. 591-602
    • McLachlin, D.T.1    Chait, B.T.2
  • 85
    • 0346999590 scopus 로고    scopus 로고
    • Phosphotyrosine mapping in Bcr/Abl oncoprotein using phosphotyrosine-specific immonium ion scanning
    • Steen H, Fernandez M, Ghaffari S, Pandey A, Mann M. Phosphotyrosine mapping in Bcr/Abl oncoprotein using phosphotyrosine-specific immonium ion scanning. Mol Cell Proteomics. 2003; 2:138-145.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 138-145
    • Steen, H.1    Fernandez, M.2    Ghaffari, S.3    Pandey, A.4    Mann, M.5
  • 86
    • 0037458030 scopus 로고    scopus 로고
    • Profiling of tyrosine phosphorylation pathways in human calls using mass spectrometry
    • Salomon AR, Ficarro SB, Brill LM, et al. Profiling of tyrosine phosphorylation pathways in human calls using mass spectrometry. Proc Natl Acad Sci U S A. 2003;100:443-448.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 443-448
    • Salomon, A.R.1    Ficarro, S.B.2    Brill, L.M.3
  • 87
    • 0037337307 scopus 로고    scopus 로고
    • A systematic approach to modeling, capturing, and disseminating proteomics experimental data
    • Taylor CF, Paton NW, Garwood KL, et al. A systematic approach to modeling, capturing, and disseminating proteomics experimental data. Nat Biotechnol. 2003;21:247-254.
    • (2003) Nat Biotechnol , vol.21 , pp. 247-254
    • Taylor, C.F.1    Paton, N.W.2    Garwood, K.L.3
  • 88
    • 18344396568 scopus 로고    scopus 로고
    • Minimum information about a microarray experiment (MIAME)-toward standards for microarray data
    • Brazma A, Hingamp P, Quackenbush J, et al. Minimum information about a microarray experiment (MIAME)-toward standards for microarray data. Nat Genet. 2001;29:365-371.
    • (2001) Nat Genet , vol.29 , pp. 365-371
    • Brazma, A.1    Hingamp, P.2    Quackenbush, J.3
  • 90
    • 0033919787 scopus 로고    scopus 로고
    • Proteomics: Applications and opportunities in preclinical drug development
    • Steiner S, Witzmann FA. Proteomics: applications and opportunities in preclinical drug development. Electrophoresis. 2000;21:2099-2104.
    • (2000) Electrophoresis , vol.21 , pp. 2099-2104
    • Steiner, S.1    Witzmann, F.A.2
  • 91
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • Shaw J, Rowlinson R, Nickson J, et al. Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes. Proteomics. 2003;3:1181-1195.
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3
  • 92
    • 0025677738 scopus 로고
    • Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization
    • Hillenkamp F, Karas M. Mass spectrometry of peptides and proteins by matrix-assisted ultraviolet laser desorption/ionization. Methods Enzymol. 1990;193:280-295.
    • (1990) Methods Enzymol , vol.193 , pp. 280-295
    • Hillenkamp, F.1    Karas, M.2
  • 94
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y, Nagasu T, Chait BT. 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
  • 95
    • 0036164157 scopus 로고    scopus 로고
    • Selective incorporation of isotopically labeled amino acids for identification of intact proteins on a proteome-wide level
    • Martinovic S, Veenstra TD, Anderson GA, Pasa-Tolic L, Smith RD. Selective incorporation of isotopically labeled amino acids for identification of intact proteins on a proteome-wide level. J Mass Spectrom. 2002;37:99-107.
    • (2002) J Mass Spectrom , vol.37 , pp. 99-107
    • Martinovic, S.1    Veenstra, T.D.2    Anderson, G.A.3    Pasa-Tolic, L.4    Smith, R.D.5
  • 96
    • 0035499083 scopus 로고    scopus 로고
    • Fractionation of isotopically labeled peptides in quantitative proteomics
    • Zhang R, Sioma CS, Wang S, Regnier FE. Fractionation of isotopically labeled peptides in quantitative proteomics. Anal Chem. 2001;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
  • 98
    • 0036605185 scopus 로고    scopus 로고
    • Analysis of protein phosphorylation using mass spectrometry: Deciphering the phosphoproteome
    • Mann M, Ong SE, Gronborg M, Steen H, Jensen ON, Pandey A. Analysis of protein phosphorylation using mass spectrometry: deciphering the phosphoproteome. Trends Biotechnol. 2002;20: 261-268.
    • (2002) Trends Biotechnol , vol.20 , pp. 261-268
    • Mann, M.1    Ong, S.E.2    Gronborg, M.3    Steen, H.4    Jensen, O.N.5    Pandey, A.6
  • 99
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal Chem. 1996; 68:850-858.
    • (1996) Anal Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4


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