메뉴 건너뛰기




Volumn 286, Issue 6 49-6, 2004, Pages

Proteomic research: Potential opportunities for clinical and physiological investigators

Author keywords

Mass spectrometry; Metabolic labeling; Protein modification; Protein quantification; Protein synthesis

Indexed keywords

CARBOHYDRATE; LIPID; PHOSPHATE; PROTEIN; SULFATE;

EID: 2442710587     PISSN: 01931849     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpendo.00370.2003     Document Type: Review
Times cited : (34)

References (96)
  • 1
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R and Mann M. Mass spectrometry-based proteomics. Nature 422: 198-207, 2003.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 2
    • 0035225284 scopus 로고    scopus 로고
    • Cancer-induced fatigue and skeletal muscle wasting: The role of exercise
    • Al-Majid S and McCarthy DO. Cancer-induced fatigue and skeletal muscle wasting: the role of exercise. Biol Res Nurs 2: 186-197, 2001.
    • (2001) Biol Res Nurs , vol.2 , pp. 186-197
    • Al-Majid, S.1    McCarthy, D.O.2
  • 3
    • 0033517106 scopus 로고    scopus 로고
    • Reg 1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cervisiae
    • Alms GR, Sanz P, Carlson M, and Haystead TA. Reg 1p targets protein phosphatase 1 to dephosphorylate hexokinase II in Saccharomyces cervisiae. EMBO J 18: 4157-4168, 1999.
    • (1999) EMBO J , vol.18 , pp. 4157-4168
    • Alms, G.R.1    Sanz, P.2    Carlson, M.3    Haystead, T.A.4
  • 6
    • 0034996561 scopus 로고    scopus 로고
    • Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise
    • Balagopal P, Schimke JC, Ades PA, Adey D, and Nair KS. Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise. Am J Physiol Endocrinol Metab 280: E203-E208, 2001.
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Balagopal, P.1    Schimke, J.C.2    Ades, P.A.3    Adey, D.4    Nair, K.S.5
  • 7
    • 0025380044 scopus 로고
    • Pancreatic extracts. 1922
    • Banting FG and Best BA. Pancreatic extracts. 1922. J Lab Clin Med 115: 254-272, 1990.
    • (1990) J Lab Clin Med , vol.115 , pp. 254-272
    • Banting, F.G.1    Best, B.A.2
  • 8
    • 0023377246 scopus 로고
    • An isotopic method for measurement of muscle protein synthesis and degradation in vivo
    • Barrett EJ, Revkin JH, Young LH, Zaret BL, Jacob R, and Gelfand RA. An isotopic method for measurement of muscle protein synthesis and degradation in vivo. Biochem J 245: 223-228, 1987.
    • (1987) Biochem J , vol.245 , pp. 223-228
    • Barrett, E.J.1    Revkin, J.H.2    Young, L.H.3    Zaret, B.L.4    Jacob, R.5    Gelfand, R.A.6
  • 10
    • 0027950135 scopus 로고
    • Protein synthesis and breakdown in skin and muscle: A leg model of amino acid kinetics
    • Biolo G, Gastaldelli A, Zhang XJ, and Wolfe RR. Protein synthesis and breakdown in skin and muscle: a leg model of amino acid kinetics. Am J Physiol Endocrinol Metab 267: E467-E474, 1994.
    • (1994) Am J Physiol Endocrinol Metab , vol.267
    • Biolo, G.1    Gastaldelli, A.2    Zhang, X.J.3    Wolfe, R.R.4
  • 12
    • 0029083530 scopus 로고
    • The turning point in genome research
    • Boguski MS. The turning point in genome research. Trends Biochem Sci 20: 295-296, 1995.
    • (1995) Trends Biochem Sci , vol.20 , pp. 295-296
    • Boguski, M.S.1
  • 13
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414: 813-820, 2001.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 14
    • 0031304362 scopus 로고    scopus 로고
    • Molecular imaging of biological samples: Localization of peptides and proteins using MALDI-TOF MS
    • Caprioli RM, Farmer TB, and Gile J. Molecular imaging of biological samples: localization of peptides and proteins using MALDI-TOF MS. Anal Chem 69: 4751-4760, 1997.
    • (1997) Anal Chem , vol.69 , pp. 4751-4760
    • Caprioli, R.M.1    Farmer, T.B.2    Gile, J.3
  • 15
    • 0036802247 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new tool to investigate the spatial organization of peptides and proteins in mammalian tissue sections
    • Chaurand P, Schwartz SA, and Caprioli RM. Imaging mass spectrometry: a new tool to investigate the spatial organization of peptides and proteins in mammalian tissue sections. Curr Opin Chem Biol 6: 676-681, 2002.
    • (2002) Curr Opin Chem Biol , vol.6 , pp. 676-681
    • Chaurand, P.1    Schwartz, S.A.2    Caprioli, R.M.3
  • 16
    • 0027476877 scopus 로고
    • Posttranslational regulation of insulin-like growth factor binding protein-4 in normal and transformed human fibroblasts
    • Conover CA, Kiefer MC, and Zapf J. Posttranslational regulation of insulin-like growth factor binding protein-4 in normal and transformed human fibroblasts. J Clin Invest 91: 1129-1137, 1993.
    • (1993) J Clin Invest , vol.91 , pp. 1129-1137
    • Conover, C.A.1    Kiefer, M.C.2    Zapf, J.3
  • 17
    • 0031849955 scopus 로고    scopus 로고
    • Cardiac protein abnormalities in dilated cardiomyopathy detected by two-dimensional polyacrylamide gel electrophoresis
    • Corbett JM, Why HJ, Wheeler CH, Richardson PJ, Archard LC, Yacoub MH, and Dunn MJ. Cardiac protein abnormalities in dilated cardiomyopathy detected by two-dimensional polyacrylamide gel electrophoresis. Electrophoresis 19: 2031-2042, 1998.
    • (1998) Electrophoresis , vol.19 , pp. 2031-2042
    • Corbett, J.M.1    Why, H.J.2    Wheeler, C.H.3    Richardson, P.J.4    Archard, L.C.5    Yacoub, M.H.6    Dunn, M.J.7
  • 18
    • 0026069777 scopus 로고
    • Differential effects of insulin deficiency on albumin and fibrinogen synthesis in humans
    • De Feo P, Gan Gaisano M, and Haymond MW. Differential effects of insulin deficiency on albumin and fibrinogen synthesis in humans. J Clin Invest 88: 833-840, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 833-840
    • De Feo, P.1    Gan Gaisano, M.2    Haymond, M.W.3
  • 19
    • 0033135747 scopus 로고    scopus 로고
    • Protein glycosylation in development and disease
    • Dennis JW, Granovsky M, and Warren CE. Protein glycosylation in development and disease. BioEssays 21: 412-421, 1999.
    • (1999) BioEssays , vol.21 , pp. 412-421
    • Dennis, J.W.1    Granovsky, M.2    Warren, C.E.3
  • 20
    • 0034425742 scopus 로고    scopus 로고
    • Antibody arrays for high-throughput screening of antibody-antigen interactions
    • DeWildt RM, Mundy CR, Gorick BD, and Tomlinson IM. Antibody arrays for high-throughput screening of antibody-antigen interactions. Nat Biotechnol 18: 989-994, 2000.
    • (2000) Nat Biotechnol , vol.18 , pp. 989-994
    • DeWildt, R.M.1    Mundy, C.R.2    Gorick, B.D.3    Tomlinson, I.M.4
  • 22
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields S and Song O. A novel genetic system to detect protein-protein interactions. Nature 340: 245-246, 1989.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 25
    • 0031149094 scopus 로고    scopus 로고
    • Sequential purification of human apolipoprotein B-100, albumin, and fibrinogen by immunoaffinity chromatography for measurement of protein synthesis
    • Fu A, Morris JC, Ford GC, and Nair KS. Sequential purification of human apolipoprotein B-100, albumin, and fibrinogen by immunoaffinity chromatography for measurement of protein synthesis. Anal Biochem 247: 228-236, 1996.
    • (1996) Anal Biochem , vol.247 , pp. 228-236
    • Fu, A.1    Morris, J.C.2    Ford, G.C.3    Nair, K.S.4
  • 26
    • 0032431232 scopus 로고    scopus 로고
    • Age effect on fibrinogen and albumin synthesis in humans
    • Fu A and Nair KS. Age effect on fibrinogen and albumin synthesis in humans. Am J Physiol Endocrinol Metab 275: E1023-E1030, 1998.
    • (1998) Am J Physiol Endocrinol Metab , vol.275
    • Fu, A.1    Nair, K.S.2
  • 27
    • 0032728399 scopus 로고    scopus 로고
    • Searching for drug targets in microbial genomes
    • Galperin MY and Coonin EG. Searching for drug targets in microbial genomes. Curr Opin Biotech 10: 571-578, 1999.
    • (1999) Curr Opin Biotech , vol.10 , pp. 571-578
    • Galperin, M.Y.1    Coonin, E.G.2
  • 28
    • 0031722559 scopus 로고    scopus 로고
    • Strategies for glycoconjugate analysis
    • Geyer H and Geyer R. Strategies for glycoconjugate analysis. Acta Anat 161: 18-35, 1998.
    • (1998) Acta Anat , vol.161 , pp. 18-35
    • Geyer, H.1    Geyer, R.2
  • 29
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat Cell Biol 5: 87-90, 2003.
    • (2003) Nat Cell Biol , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 30
    • 0035221502 scopus 로고    scopus 로고
    • Perspectives for mass spectrometry and functional proteomics
    • Godovac-Zimmerman J and Brown LR. Perspectives for mass spectrometry and functional proteomics. Mass Spectrom Rev 20: 1-57, 2001.
    • (2001) Mass Spectrom Rev , vol.20 , pp. 1-57
    • Godovac-Zimmerman, J.1    Brown, L.R.2
  • 31
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 426: 895-899, 2003.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 32
    • 0016908233 scopus 로고
    • Intracellular protein degradation in mammalian and bacterial cells: Part 2
    • edited by Snell EE, Boyer PD, Meister A, and Richardson CC. Palo Alto, CA: Annual Reviews
    • Goldberg AL and St. John AC. Intracellular protein degradation in mammalian and bacterial cells: Part 2. In: Annual Review of Biochemistry, edited by Snell EE, Boyer PD, Meister A, and Richardson CC. Palo Alto, CA: Annual Reviews, 1976, p. 747-803.
    • (1976) Annual Review of Biochemistry , pp. 747-803
    • Goldberg, A.L.1    St. John, A.C.2
  • 33
    • 0041807685 scopus 로고    scopus 로고
    • A functional proteomics approach to signal transduction
    • Graves PR and Haystead TA. A functional proteomics approach to signal transduction. Recent Prog Horm Res 58: 1-24, 2003.
    • (2003) Recent Prog Horm Res , vol.58 , pp. 1-24
    • Graves, P.R.1    Haystead, T.A.2
  • 34
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi SP, Rist B, Gerber SA, Turecek F, Gelb MH, and Aebersold R. Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17: 994-999, 1999.
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 35
    • 0036328175 scopus 로고    scopus 로고
    • Synthesis rate of muscle proteins, muscle functions, and amino acid kinetics in type 2 diabetes
    • Halvatsiotis P, Short KR, Bigelow ML, and Nair KS. Synthesis rate of muscle proteins, muscle functions, and amino acid kinetics in type 2 diabetes. Diabetes 51: 2395-2404, 2002.
    • (2002) Diabetes , vol.51 , pp. 2395-2404
    • Halvatsiotis, P.1    Short, K.R.2    Bigelow, M.L.3    Nair, K.S.4
  • 36
    • 0037434981 scopus 로고    scopus 로고
    • Disease proteomics
    • Hanash S. Disease proteomics. Nature 422: 226-232, 2003.
    • (2003) Nature , vol.422 , pp. 226-232
    • Hanash, S.1
  • 37
    • 0036227219 scopus 로고    scopus 로고
    • The challenges of developing a sound proteomics strategy
    • Hancock WS, Wu SL, and Shieh P. The challenges of developing a sound proteomics strategy. Proteomics 2: 352-359, 2002.
    • (2002) Proteomics , vol.2 , pp. 352-359
    • Hancock, W.S.1    Wu, S.L.2    Shieh, P.3
  • 38
    • 0028872358 scopus 로고
    • Causes of insulin resistance
    • Kahn CR. Causes of insulin resistance. Nature 373: 384-385, 1995.
    • (1995) Nature , vol.373 , pp. 384-385
    • Kahn, C.R.1
  • 39
    • 0035259538 scopus 로고    scopus 로고
    • Use of antibodies for detection of phosphorylated proteins separated by two-dimensional gel electrophoresis
    • Kaufmann H, Bailey JE, and Fussenegger M. Use of antibodies for detection of phosphorylated proteins separated by two-dimensional gel electrophoresis. Proteomics 1: 194-199, 2001.
    • (2001) Proteomics , vol.1 , pp. 194-199
    • Kaufmann, H.1    Bailey, J.E.2    Fussenegger, M.3
  • 40
    • 0024261265 scopus 로고
    • Cellular mechanisms involved in the action of insulin on protein synthesis
    • Kimball SR and Jefferson LS. Cellular mechanisms involved in the action of insulin on protein synthesis. Diabetes Metab Rev 4: 773-787, 1988.
    • (1988) Diabetes Metab Rev , vol.4 , pp. 773-787
    • Kimball, S.R.1    Jefferson, L.S.2
  • 42
    • 0034254939 scopus 로고    scopus 로고
    • Electrophoresis for the analysis of acidic oligosaccharides
    • Koketsu M and Linhardt RJ. Electrophoresis for the analysis of acidic oligosaccharides. Anal Biochem 283: 136-145, 2000.
    • (2000) Anal Biochem , vol.283 , pp. 136-145
    • Koketsu, M.1    Linhardt, R.J.2
  • 43
    • 0028899747 scopus 로고
    • Association of pretransplantation antiheart antibodies with clinical course after heart transplantation
    • Latif N, Rose ML, Yacoub MH, and Dunn MJ. Association of pretransplantation antiheart antibodies with clinical course after heart transplantation. J Heart Lung Transplant 14: 119-126, 1995.
    • (1995) J Heart Lung Transplant , vol.14 , pp. 119-126
    • Latif, N.1    Rose, M.L.2    Yacoub, M.H.3    Dunn, M.J.4
  • 46
    • 0042164959 scopus 로고    scopus 로고
    • Using standard positions and image fusion to create proteome maps from collections of two-dimensional gel electrophoresis images
    • Luhn S, Berth M, Hecker M, and Bernhardt J. Using standard positions and image fusion to create proteome maps from collections of two-dimensional gel electrophoresis images. Proteomics 3: 1117-1127, 2003.
    • (2003) Proteomics , vol.3 , pp. 1117-1127
    • Luhn, S.1    Berth, M.2    Hecker, M.3    Bernhardt, J.4
  • 48
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy MP. Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal Biochem 280: 1-10, 2000.
    • (2000) Anal Biochem , vol.280 , pp. 1-10
    • Molloy, M.P.1
  • 49
    • 0036208704 scopus 로고    scopus 로고
    • Differential gel exposure, a new methodology for the two-dimensional comparison of protein samples
    • Monribot-Espagne C and Boucherie H. Differential gel exposure, a new methodology for the two-dimensional comparison of protein samples. Proteomics 2: 229-240, 2002.
    • (2002) Proteomics , vol.2 , pp. 229-240
    • Monribot-Espagne, C.1    Boucherie, H.2
  • 50
    • 0027997185 scopus 로고
    • Coexpression of glucose transporters and glucokinase in Xenopus oocytes indicates that both glucose tranport and phosphorylation determine glucose utilization
    • Morita H, Yano Y, Niswender KD, May JM, Whitesell RR, Wu L, Printz RL, Granner DK, Magnuson MA, and Powers AC. Coexpression of glucose transporters and glucokinase in Xenopus oocytes indicates that both glucose tranport and phosphorylation determine glucose utilization. J Clin Invest 94: 1373-1382, 1994.
    • (1994) J Clin Invest , vol.94 , pp. 1373-1382
    • Morita, H.1    Yano, Y.2    Niswender, K.D.3    May, J.M.4    Whitesell, R.R.5    Wu, L.6    Printz, R.L.7    Granner, D.K.8    Magnuson, M.A.9    Powers, A.C.10
  • 53
    • 0028787009 scopus 로고
    • Muscle protein turnover: Methodological issues and the effect of aging
    • Nair KS. Muscle protein turnover: methodological issues and the effect of aging. J Gerontol Biol Med Sci 50A: 107-112, 1995.
    • (1995) J Gerontol Biol Med Sci , vol.50 A , pp. 107-112
    • Nair, K.S.1
  • 54
    • 0029073033 scopus 로고
    • Protein dynamics in whole body and in splanchnic and leg tissues in type I diabetic patients
    • Nair KS, Ford GC, Ekberg K, Fernqvist-Forbes E, and Wahren J. Protein dynamics in whole body and in splanchnic and leg tissues in type I diabetic patients. J Clin Invest 95: 2926-2937, 1995.
    • (1995) J Clin Invest , vol.95 , pp. 2926-2937
    • Nair, K.S.1    Ford, G.C.2    Ekberg, K.3    Fernqvist-Forbes, E.4    Wahren, J.5
  • 55
  • 56
    • 0023722892 scopus 로고
    • Effect of betahydroxybutyrate on whole-body leucine kinetics and fractional mixed skeletal muscle protein synthesis in humans
    • Nair KS, Welle SL, Halliday D, and Campbell RG. Effect of betahydroxybutyrate on whole-body leucine kinetics and fractional mixed skeletal muscle protein synthesis in humans. J Clin Invest 82: 198-205, 1988.
    • (1988) J Clin Invest , vol.82 , pp. 198-205
    • Nair, K.S.1    Welle, S.L.2    Halliday, D.3    Campbell, R.G.4
  • 58
    • 0035067251 scopus 로고    scopus 로고
    • Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome
    • Oda Y, Nagasu T, and Chait BT. Enrichment analysis of phosphorylated proteins as a tool for probing the phosphoproteome. Nat Biotechnol 19: 379-382, 2001.
    • (2001) Nat Biotechnol , vol.19 , pp. 379-382
    • Oda, Y.1    Nagasu, T.2    Chait, B.T.3
  • 59
    • 0016711037 scopus 로고
    • High resolution two-dimensional electrophoresis of proteins
    • O'Farrell PH. High resolution two-dimensional electrophoresis of proteins. J Biol Chem 250: 4007-4021, 1975.
    • (1975) J Biol Chem , vol.250 , pp. 4007-4021
    • O'Farrell, P.H.1
  • 60
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, Pandey A, and Mann M. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386, 2002.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Mann, M.7
  • 61
    • 0034659815 scopus 로고    scopus 로고
    • Proteomics to study genes and genomes
    • Pandey A and Mann M. Proteomics to study genes and genomes. Nature 405: 837-846, 2000.
    • (2000) Nature , vol.405 , pp. 837-846
    • Pandey, A.1    Mann, M.2
  • 62
    • 0030888807 scopus 로고    scopus 로고
    • Autoantibodies in sera of patients with myocarditis: Characterizaton of the corresponding proteins by isoelectric focusing and N-terminal sequence analysis
    • Pankuweit S, Portig I, Lottspeich F, and Maisch B. Autoantibodies in sera of patients with myocarditis: characterizaton of the corresponding proteins by isoelectric focusing and N-terminal sequence analysis. J Mol Cell Cardiol 29: 77-84, 1997.
    • (1997) J Mol Cell Cardiol , vol.29 , pp. 77-84
    • Pankuweit, S.1    Portig, I.2    Lottspeich, F.3    Maisch, B.4
  • 63
    • 0034111635 scopus 로고    scopus 로고
    • A thousand points of light: The application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics
    • Patton WF. A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics. Electrophoresis 21: 1123-1144, 2000.
    • (2000) Electrophoresis , vol.21 , pp. 1123-1144
    • Patton, W.F.1
  • 64
    • 0037023859 scopus 로고    scopus 로고
    • Detection technologies in proteome analysis
    • Patton WF. Detection technologies in proteome analysis. J Chromatogr 771: 3-31, 2002.
    • (2002) J Chromatogr , vol.771 , pp. 3-31
    • Patton, W.F.1
  • 65
    • 0036669447 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis; better than a poke in the ICAT?
    • Patton WF, Schulenberg B, and Steinberg TH. Two-dimensional gel electrophoresis; better than a poke in the ICAT? Curr Opin Biotechnol 13: 321-328, 2002.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 321-328
    • Patton, W.F.1    Schulenberg, B.2    Steinberg, T.H.3
  • 67
    • 0029814482 scopus 로고    scopus 로고
    • The construction of world wide web accessible myocardial two-dimensional gel electrophoresis protein database "HEART-2DPAGE": A practical approach
    • Pleissner KP, Sander S, Oswald H, Regitz-Zagrosek V, and Fleck E. The construction of world wide web accessible myocardial two-dimensional gel electrophoresis protein database "HEART-2DPAGE": a practical approach. Electrophoresis 17: 1386-1392, 1996.
    • (1996) Electrophoresis , vol.17 , pp. 1386-1392
    • Pleissner, K.P.1    Sander, S.2    Oswald, H.3    Regitz-Zagrosek, V.4    Fleck, E.5
  • 68
    • 0030704708 scopus 로고    scopus 로고
    • Identification of mitochondrial antigens recognized by antibodies in sera of patients with idiopathic dilated cardiomyopathy by two-dimensional gel electrophoresis and protein sequencing
    • Pohlner K, Portig I, Pankuweit S, Lottspeich F, and Maisch B. Identification of mitochondrial antigens recognized by antibodies in sera of patients with idiopathic dilated cardiomyopathy by two-dimensional gel electrophoresis and protein sequencing. Am J Cardiol 80: 1040-1045, 1997.
    • (1997) Am J Cardiol , vol.80 , pp. 1040-1045
    • Pohlner, K.1    Portig, I.2    Pankuweit, S.3    Lottspeich, F.4    Maisch, B.5
  • 72
    • 0035438393 scopus 로고    scopus 로고
    • On graphical and numerical characterization of proteomics maps
    • Randic M. On graphical and numerical characterization of proteomics maps. J Chem Inf Comput Sci 41: 1330-1338, 2001.
    • (2001) J Chem Inf Comput Sci , vol.41 , pp. 1330-1338
    • Randic, M.1
  • 74
    • 0030451773 scopus 로고    scopus 로고
    • Effect of age on in vivo rates of mitochondrial protein synthesis in human skeletal muscle
    • Rooyackers OE, Adey DB, Ades PA, and Nair KS. Effect of age on in vivo rates of mitochondrial protein synthesis in human skeletal muscle. Proc Natl Acad Sci USA 93: 15364-15369, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 15364-15369
    • Rooyackers, O.E.1    Adey, D.B.2    Ades, P.A.3    Nair, K.S.4
  • 75
    • 0030783111 scopus 로고    scopus 로고
    • Measurement of synthesis rates of specific muscle proteins using needle biopsy samples
    • Rooyackers OE, Balagopal P, and Nair KS. Measurement of synthesis rates of specific muscle proteins using needle biopsy samples. Muscle Nerve Suppl 5: S93-S96, 1997.
    • (1997) Muscle Nerve Suppl , vol.5
    • Rooyackers, O.E.1    Balagopal, P.2    Nair, K.S.3
  • 77
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end-productions: A review
    • Singh R, Barden A, Mori T, and Beilin L. Advanced glycation end-productions: a review. Diabetologia 44: 129-146, 2001.
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 78
    • 0036266251 scopus 로고    scopus 로고
    • Gene expression profile in skeletal muscle of type 2 diabetes and the effect of insulin treatment
    • Sreekumar R, Halvatsiotis P, Schimke JC, and Nair KS. Gene expression profile in skeletal muscle of type 2 diabetes and the effect of insulin treatment. Diabetes 51: 1913-1920, 2002.
    • (2002) Diabetes , vol.51 , pp. 1913-1920
    • Sreekumar, R.1    Halvatsiotis, P.2    Schimke, J.C.3    Nair, K.S.4
  • 81
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli M, Chaurand P, Hallahan DE, and Caprioli RM. Imaging mass spectrometry: a new technology for the analysis of protein expression in mammalian tissues. Nat Med 7: 493-496, 2001.
    • (2001) Nat Med , vol.7 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3    Caprioli, R.M.4
  • 82
    • 0038271638 scopus 로고    scopus 로고
    • Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts
    • Stump CS, Short KR, Bigelow ML, Schimke JC, and Nair KS. Effect of insulin on human skeletal muscle mitochondrial ATP production, protein synthesis, and mRNA transcripts. Proc Natl Acad Sci USA 100: 7996-8001, 2003.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7996-8001
    • Stump, C.S.1    Short, K.R.2    Bigelow, M.L.3    Schimke, J.C.4    Nair, K.S.5
  • 83
    • 0035865087 scopus 로고    scopus 로고
    • A physical map of the human genome
    • The International Human Genome Mapping Consortium. A physical map of the human genome. Nature 409: 934-941, 2001.
    • (2001) Nature , vol.409 , pp. 934-941
  • 84
    • 0037434980 scopus 로고    scopus 로고
    • From genomics to proteomics
    • Tyers M and Mann M. From genomics to proteomics. Nature 422: 193-197, 2003.
    • (2003) Nature , vol.422 , pp. 193-197
    • Tyers, M.1    Mann, M.2
  • 86
    • 0032884023 scopus 로고    scopus 로고
    • Difference gel electrophoresis
    • Unlu M. Difference gel electrophoresis. Biochem Soc Trans 27: 547-549, 1999.
    • (1999) Biochem Soc Trans , vol.27 , pp. 547-549
    • Unlu, M.1
  • 90
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, and Yates JRI. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19: 242-247, 2001.
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.I.3
  • 91
    • 2442635280 scopus 로고
    • Protein turnover in the whole body
    • Waterlow JC. Protein turnover in the whole body. Nature 253: 157, 1975.
    • (1975) Nature , vol.253 , pp. 157
    • Waterlow, J.C.1
  • 95
    • 0035072715 scopus 로고    scopus 로고
    • A systematic approach to the analysis of protein phosphorylation
    • Zhou H, Watts JD, and Aebersold R. A systematic approach to the analysis of protein phosphorylation. Nat Biotechnol 19: 375-378, 2001.
    • (2001) Nat Biotechnol , vol.19 , pp. 375-378
    • Zhou, H.1    Watts, J.D.2    Aebersold, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.