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Volumn 17, Issue 6, 2010, Pages 455-468

Mass Spectrometry in Chronic Kidney Disease Research

Author keywords

Peptidome; Plasma; Proteome; Serum; Targeted proteomics; Urine

Indexed keywords

BIOLOGICAL MARKER; PEPTIDOME; PROTEOME; UNCLASSIFIED DRUG;

EID: 78049449702     PISSN: 15485595     EISSN: None     Source Type: Journal    
DOI: 10.1053/j.ackd.2010.09.003     Document Type: Review
Times cited : (10)

References (55)
  • 1
    • 0036176161 scopus 로고    scopus 로고
    • National Kidney Foundation K/DOQI clinical practice guidelines for chronic kidney disease: Evaluation, classification, and stratification
    • National Kidney Foundation K/DOQI clinical practice guidelines for chronic kidney disease: Evaluation, classification, and stratification. Am J Kidney Dis 2002, 39(2 Suppl 1):S1-S266.
    • (2002) Am J Kidney Dis , vol.39 , Issue.2 SUPPL. 1
  • 2
    • 74049151193 scopus 로고    scopus 로고
    • Clinical practice. Stage IV chronic kidney disease
    • Abboud H., Henrich W.L. Clinical practice. Stage IV chronic kidney disease. N Engl J Med 2010, 362:56-65.
    • (2010) N Engl J Med , vol.362 , pp. 56-65
    • Abboud, H.1    Henrich, W.L.2
  • 3
    • 35848968871 scopus 로고    scopus 로고
    • Prevalence of chronic kidney disease in the United States
    • Coresh J., Selvin E., Stevens L.A., et al. Prevalence of chronic kidney disease in the United States. JAMA 2007, 298:2038-2047.
    • (2007) JAMA , vol.298 , pp. 2038-2047
    • Coresh, J.1    Selvin, E.2    Stevens, L.A.3
  • 5
    • 1642413198 scopus 로고    scopus 로고
    • Longitudinal follow-up and outcomes among a population with chronic kidney disease in a large managed care organization
    • Keith D.S., Nichols G.A., Gullion C.M., et al. Longitudinal follow-up and outcomes among a population with chronic kidney disease in a large managed care organization. Arch Intern Med 2004, 164:659-663.
    • (2004) Arch Intern Med , vol.164 , pp. 659-663
    • Keith, D.S.1    Nichols, G.A.2    Gullion, C.M.3
  • 6
    • 33750744092 scopus 로고    scopus 로고
    • Chronic kidney disease progression
    • Eddy A.A., Neilson E.G. Chronic kidney disease progression. J Am Soc Nephrol 2006, 17:2964-2966.
    • (2006) J Am Soc Nephrol , vol.17 , pp. 2964-2966
    • Eddy, A.A.1    Neilson, E.G.2
  • 7
    • 77950955047 scopus 로고    scopus 로고
    • Multi-dimensional liquid chromatography in proteomics-A review
    • Zhang X., Fang A., Riley C.P., et al. Multi-dimensional liquid chromatography in proteomics-A review. Anal Chim Acta 2010, 664:101-113.
    • (2010) Anal Chim Acta , vol.664 , pp. 101-113
    • Zhang, X.1    Fang, A.2    Riley, C.P.3
  • 8
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates J.R., Ruse C.I., Nakorchevsky A. Proteomics by mass spectrometry: Approaches, advances, and applications. Annu Rev Biomed Eng 2009, 11:49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 9
    • 77953156634 scopus 로고    scopus 로고
    • Accurate mass tag retention time database for urine proteome analysis by chromatography-Mass spectrometry
    • Agron I.A., Avtonomov D.M., Kononikhin A.S., et al. Accurate mass tag retention time database for urine proteome analysis by chromatography-Mass spectrometry. Biochemistry (Mosc) 2010, 75:636-641.
    • (2010) Biochemistry (Mosc) , vol.75 , pp. 636-641
    • Agron, I.A.1    Avtonomov, D.M.2    Kononikhin, A.S.3
  • 10
    • 78049446171 scopus 로고    scopus 로고
    • Accurate mass measurement: Terminology and treatment of data. J Am Soc Mass Spectrom (in press)
    • Brenton AG, Godfrey AR: Accurate mass measurement: Terminology and treatment of data. J Am Soc Mass Spectrom (in press).
    • Brenton, A.G.1    Godfrey, A.R.2
  • 11
    • 14844360847 scopus 로고    scopus 로고
    • Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis: The human proteome
    • Qian W.J., Liu T., Monroe M.E., et al. Probability-based evaluation of peptide and protein identifications from tandem mass spectrometry and SEQUEST analysis: The human proteome. J Proteome Res 2005, 4:53-62.
    • (2005) J Proteome Res , vol.4 , pp. 53-62
    • Qian, W.J.1    Liu, T.2    Monroe, M.E.3
  • 12
    • 63049110388 scopus 로고    scopus 로고
    • Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions
    • Pan C., Kumar C., Bohl S., et al. Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Mol Cell Proteomics 2009, 8:443-450.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3
  • 13
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong S.E., Blagoev B., Kratchmarova I., et al. Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 2002, 1:376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 14
    • 30144444853 scopus 로고    scopus 로고
    • Bioinformatic methods to exploit mass spectrometric data for proteomic applications
    • Chalkley R.J., Hansen K.C., Baldwin M.A. Bioinformatic methods to exploit mass spectrometric data for proteomic applications. Methods Enzymol 2005, 402:289-312.
    • (2005) Methods Enzymol , vol.402 , pp. 289-312
    • Chalkley, R.J.1    Hansen, K.C.2    Baldwin, M.A.3
  • 15
    • 70949104487 scopus 로고    scopus 로고
    • Genome-wide analysis of immune activation in human T and B cells reveals distinct classes of alternatively spliced genes
    • Grigoryev Y.A., Kurian S.M., Nakorchevskiy A.A., et al. Genome-wide analysis of immune activation in human T and B cells reveals distinct classes of alternatively spliced genes. PLoS One 2009, 4:e7906.
    • (2009) PLoS One , vol.4
    • Grigoryev, Y.A.1    Kurian, S.M.2    Nakorchevskiy, A.A.3
  • 16
    • 67650564908 scopus 로고    scopus 로고
    • Biomarkers for early and late stage chronic allograft nephropathy by proteogenomic profiling of peripheral blood
    • Kurian S.M., Heilman R., Mondala T.S., et al. Biomarkers for early and late stage chronic allograft nephropathy by proteogenomic profiling of peripheral blood. PLoS One 2009, 4:e6212.
    • (2009) PLoS One , vol.4
    • Kurian, S.M.1    Heilman, R.2    Mondala, T.S.3
  • 17
    • 77949358460 scopus 로고    scopus 로고
    • Molecular mechanisms of chronic kidney transplant rejection via large-scale proteogenomic analysis of tissue biopsies
    • Nakorchevsky A., Hewel J.A., Kurian S.M., et al. Molecular mechanisms of chronic kidney transplant rejection via large-scale proteogenomic analysis of tissue biopsies. J Am Soc Nephrol 2010, 21:362-373.
    • (2010) J Am Soc Nephrol , vol.21 , pp. 362-373
    • Nakorchevsky, A.1    Hewel, J.A.2    Kurian, S.M.3
  • 18
    • 67649658244 scopus 로고    scopus 로고
    • M-type phospholipase A2 receptor as target antigen in idiopathic membranous nephropathy
    • Beck L.H., Bonegio R.G., Lambeau G., et al. M-type phospholipase A2 receptor as target antigen in idiopathic membranous nephropathy. N Engl J Med 2009, 361:11-21.
    • (2009) N Engl J Med , vol.361 , pp. 11-21
    • Beck, L.H.1    Bonegio, R.G.2    Lambeau, G.3
  • 19
    • 69849113129 scopus 로고    scopus 로고
    • Urinary peptidome may predict renal function decline in type 1 diabetes and microalbuminuria
    • Merchant M.L., Perkins B.A., Boratyn G.M., et al. Urinary peptidome may predict renal function decline in type 1 diabetes and microalbuminuria. J Am Soc Nephrol 2009, 20:2065-2074.
    • (2009) J Am Soc Nephrol , vol.20 , pp. 2065-2074
    • Merchant, M.L.1    Perkins, B.A.2    Boratyn, G.M.3
  • 20
    • 78049440203 scopus 로고    scopus 로고
    • et al: Naturally occurring human urinary peptides for use in diagnosis of chronic kidney disease. Mol Cell Proteomics (in press)
    • Good DM, Zurbig P, Argiles A, et al: Naturally occurring human urinary peptides for use in diagnosis of chronic kidney disease. Mol Cell Proteomics (in press).
    • Good, D.M.1    Zurbig, P.2    Argiles, A.3
  • 21
    • 48149087279 scopus 로고    scopus 로고
    • Urinary proteomics in diabetes and CKD
    • Rossing K., Mischak H., Dakna M., et al. Urinary proteomics in diabetes and CKD. J Am Soc Nephrol 2008, 19:1283-1290.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 1283-1290
    • Rossing, K.1    Mischak, H.2    Dakna, M.3
  • 22
    • 50849092540 scopus 로고    scopus 로고
    • CE-MS analysis of the human urinary proteome for biomarker discovery and disease diagnostics
    • Coon J.J., Zurbig P., Dakna M., et al. CE-MS analysis of the human urinary proteome for biomarker discovery and disease diagnostics. Proteomics Clin Appl 2008, 2:964.
    • (2008) Proteomics Clin Appl , vol.2 , pp. 964
    • Coon, J.J.1    Zurbig, P.2    Dakna, M.3
  • 23
    • 0028090455 scopus 로고
    • The emergence of mass spectrometry in biochemical research
    • Siuzdak G. The emergence of mass spectrometry in biochemical research. Proc Natl Acad Sci U S A 1994, 91:11290-11297.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 11290-11297
    • Siuzdak, G.1
  • 24
    • 77953362009 scopus 로고    scopus 로고
    • Coupling liquid chromatography to Orbitrap mass spectrometry
    • Makarov A., Scigelova M. Coupling liquid chromatography to Orbitrap mass spectrometry. J Chromatogr A 2010, 1217:3938-3945.
    • (2010) J Chromatogr A , vol.1217 , pp. 3938-3945
    • Makarov, A.1    Scigelova, M.2
  • 25
    • 77954195244 scopus 로고    scopus 로고
    • Evaluation of accurate mass and relative isotopic abundance measurements in the LTQ-orbitrap mass spectrometer for further metabolomics database building
    • Xu Y., Heilier J.F., Madalinski G., et al. Evaluation of accurate mass and relative isotopic abundance measurements in the LTQ-orbitrap mass spectrometer for further metabolomics database building. Anal Chem 2010, 82:5490-5501.
    • (2010) Anal Chem , vol.82 , pp. 5490-5501
    • Xu, Y.1    Heilier, J.F.2    Madalinski, G.3
  • 26
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn J.B., Mann M., Meng C.K., et al. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246:64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3
  • 27
    • 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
  • 28
    • 57449099068 scopus 로고    scopus 로고
    • Precision proteomics: The case for high resolution and high mass accuracy
    • Mann M., Kelleher N.L. Precision proteomics: The case for high resolution and high mass accuracy. Proc Natl Acad Sci U S A 2008, 105:18132-18138.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18132-18138
    • Mann, M.1    Kelleher, N.L.2
  • 29
    • 34247166848 scopus 로고    scopus 로고
    • Liquid chromatography electron capture dissociation tandem mass spectrometry (LC-ECD-MS/MS) versus liquid chromatography collision-induced dissociation tandem mass spectrometry (LC-CID-MS/MS) for the identification of proteins
    • Creese A.J., Cooper H.J. Liquid chromatography electron capture dissociation tandem mass spectrometry (LC-ECD-MS/MS) versus liquid chromatography collision-induced dissociation tandem mass spectrometry (LC-CID-MS/MS) for the identification of proteins. J Am Soc Mass Spectrom 2007, 18:891-897.
    • (2007) J Am Soc Mass Spectrom , vol.18 , pp. 891-897
    • Creese, A.J.1    Cooper, H.J.2
  • 30
    • 14744299376 scopus 로고    scopus 로고
    • The role of electron capture dissociation in biomolecular analysis
    • Cooper H.J., Hakansson K., Marshall A.G. The role of electron capture dissociation in biomolecular analysis. Mass Spectrom Rev 2005, 24:201-222.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 201-222
    • Cooper, H.J.1    Hakansson, K.2    Marshall, A.G.3
  • 31
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev R.A. Electron-capture dissociation tandem mass spectrometry. Curr Opin Biotechnol 2004, 15:12-16.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 32
    • 0036012895 scopus 로고    scopus 로고
    • Liquid chromatography and electron-capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry
    • Palmblad M., Tsybin Y.O., Ramstrom M., et al. Liquid chromatography and electron-capture dissociation in Fourier transform ion cyclotron resonance mass spectrometry. Rapid Commun Mass Spectrom 2002, 16:988-992.
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 988-992
    • Palmblad, M.1    Tsybin, Y.O.2    Ramstrom, M.3
  • 33
    • 0035416833 scopus 로고    scopus 로고
    • High-sensitivity electron capture dissociation tandem FTICR mass spectrometry of microelectrosprayed peptides
    • Hakansson K., Emmett M.R., Hendrickson C.L., et al. High-sensitivity electron capture dissociation tandem FTICR mass spectrometry of microelectrosprayed peptides. Anal Chem 2001, 73:3605-3610.
    • (2001) Anal Chem , vol.73 , pp. 3605-3610
    • Hakansson, K.1    Emmett, M.R.2    Hendrickson, C.L.3
  • 34
    • 77951857252 scopus 로고    scopus 로고
    • Sub-part-per-million precursor and product mass accuracy for high-throughput proteomics on an electron transfer dissociation-enabled orbitrap mass spectrometer
    • Wenger C.D., McAlister G.C., Xia Q., et al. Sub-part-per-million precursor and product mass accuracy for high-throughput proteomics on an electron transfer dissociation-enabled orbitrap mass spectrometer. Mol Cell Proteomics 2010, 9:754-763.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 754-763
    • Wenger, C.D.1    McAlister, G.C.2    Xia, Q.3
  • 35
    • 53049085542 scopus 로고    scopus 로고
    • A proteomics grade electron transfer dissociation-enabled hybrid linear ion trap-orbitrap mass spectrometer
    • McAlister G.C., Berggren W.T., Griep-Raming J., et al. A proteomics grade electron transfer dissociation-enabled hybrid linear ion trap-orbitrap mass spectrometer. J Proteome Res 2008, 7:3127-3136.
    • (2008) J Proteome Res , vol.7 , pp. 3127-3136
    • McAlister, G.C.1    Berggren, W.T.2    Griep-Raming, J.3
  • 36
    • 35448946118 scopus 로고    scopus 로고
    • Dual electrospray ion source for electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer
    • Williams D.K., McAlister G.C., Good D.M., et al. Dual electrospray ion source for electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer. Anal Chem 2007, 79:7916-7919.
    • (2007) Anal Chem , vol.79 , pp. 7916-7919
    • Williams, D.K.1    McAlister, G.C.2    Good, D.M.3
  • 37
    • 34249022000 scopus 로고    scopus 로고
    • Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer
    • McAlister G.C., Phanstiel D., Good D.M., et al. Implementation of electron-transfer dissociation on a hybrid linear ion trap-orbitrap mass spectrometer. Anal Chem 2007, 79:3525-3534.
    • (2007) Anal Chem , vol.79 , pp. 3525-3534
    • McAlister, G.C.1    Phanstiel, D.2    Good, D.M.3
  • 38
    • 33847174067 scopus 로고    scopus 로고
    • Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research
    • Wiese S., Reidegeld K.A., Meyer H.E., et al. Protein labeling by iTRAQ: A new tool for quantitative mass spectrometry in proteome research. Proteomics 2007, 7:340-350.
    • (2007) Proteomics , vol.7 , pp. 340-350
    • Wiese, S.1    Reidegeld, K.A.2    Meyer, H.E.3
  • 39
    • 27644543078 scopus 로고    scopus 로고
    • Comparison of label-free methods for quantifying human proteins by shotgun proteomics
    • Old W.M., Meyer-Arendt K., veline-Wolf L., et al. Comparison of label-free methods for quantifying human proteins by shotgun proteomics. Mol Cell Proteomics 2005, 4:1487-1502.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1487-1502
    • Old, W.M.1    Meyer-Arendt, K.2    veline-Wolf, L.3
  • 40
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link A.J., Eng J., Schieltz D.M., 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
  • 41
    • 0033642816 scopus 로고    scopus 로고
    • Direct analysis of proteins in mixtures. Application to protein complexes
    • Yates J.R., Link A.J., Schieltz D. Direct analysis of proteins in mixtures. Application to protein complexes. Methods Mol Biol 2000, 146:17-26.
    • (2000) Methods Mol Biol , vol.146 , pp. 17-26
    • Yates, J.R.1    Link, A.J.2    Schieltz, D.3
  • 42
    • 75749115605 scopus 로고    scopus 로고
    • Selected reaction monitoring-mass spectrometric immunoassay responsive to parathyroid hormone and related variants
    • Lopez M.F., Rezai T., Sarracino D.A., et al. Selected reaction monitoring-mass spectrometric immunoassay responsive to parathyroid hormone and related variants. Clin Chem 2010, 56:281-290.
    • (2010) Clin Chem , vol.56 , pp. 281-290
    • Lopez, M.F.1    Rezai, T.2    Sarracino, D.A.3
  • 43
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti P., Bodenmiller B., Mueller L.N., et al. Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 2009, 138:795-806.
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3
  • 44
    • 67650564834 scopus 로고    scopus 로고
    • Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma
    • Addona T.A., Abbatiello S.E., Schilling B., et al. Multi-site assessment of the precision and reproducibility of multiple reaction monitoring-based measurements of proteins in plasma. Nat Biotechnol 2009, 27:633-641.
    • (2009) Nat Biotechnol , vol.27 , pp. 633-641
    • Addona, T.A.1    Abbatiello, S.E.2    Schilling, B.3
  • 45
    • 0034999225 scopus 로고    scopus 로고
    • Survival improvement among patients with end-stage renal disease: Trends over time for transplant recipients and wait-listed patients
    • Meier-Kriesche H.U., Ojo A.O., Port F.K., et al. Survival improvement among patients with end-stage renal disease: Trends over time for transplant recipients and wait-listed patients. J Am Soc Nephrol 2001, 12:1293-1296.
    • (2001) J Am Soc Nephrol , vol.12 , pp. 1293-1296
    • Meier-Kriesche, H.U.1    Ojo, A.O.2    Port, F.K.3
  • 46
    • 0032844172 scopus 로고    scopus 로고
    • Chronic allograft nephropathy: An update
    • Paul L.C. Chronic allograft nephropathy: An update. Kidney Int 1999, 56:783-793.
    • (1999) Kidney Int , vol.56 , pp. 783-793
    • Paul, L.C.1
  • 47
    • 34548361710 scopus 로고    scopus 로고
    • SWOT analysis of Banff: Strengths, weaknesses, opportunities and threats of the international Banff consensus process and classification system for renal allograft pathology
    • Mengel M., Sis B., Halloran P.F. SWOT analysis of Banff: Strengths, weaknesses, opportunities and threats of the international Banff consensus process and classification system for renal allograft pathology. Am J Transplant 2007, 7:2221-2226.
    • (2007) Am J Transplant , vol.7 , pp. 2221-2226
    • Mengel, M.1    Sis, B.2    Halloran, P.F.3
  • 48
    • 17644375856 scopus 로고    scopus 로고
    • Kidney allograft fibrosis and atrophy early after living donor transplantation
    • Cosio F.G., Grande J.P., Larson T.S., et al. Kidney allograft fibrosis and atrophy early after living donor transplantation. Am J Transplant 2005, 5:1130-1136.
    • (2005) Am J Transplant , vol.5 , pp. 1130-1136
    • Cosio, F.G.1    Grande, J.P.2    Larson, T.S.3
  • 49
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • Wolters D.A., Washburn M.P., Yates J.R. An automated multidimensional protein identification technology for shotgun proteomics. Anal Chem 2001, 73:5683-5690.
    • (2001) Anal Chem , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates, J.R.3
  • 51
    • 44049108985 scopus 로고    scopus 로고
    • Staging of chronic kidney disease: Time for a course correction
    • Bauer C., Melamed M.L., Hostetter T.H. Staging of chronic kidney disease: Time for a course correction. J Am Soc Nephrol 2008, 19:844-846.
    • (2008) J Am Soc Nephrol , vol.19 , pp. 844-846
    • Bauer, C.1    Melamed, M.L.2    Hostetter, T.H.3
  • 52
    • 0035100888 scopus 로고    scopus 로고
    • Biomarkers Definitions Working Group Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework
    • Biomarkers Definitions Working Group Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework. Clin Pharmacol Ther 2001, 69:89-95.
    • (2001) Clin Pharmacol Ther , vol.69 , pp. 89-95
  • 53
    • 18844370547 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery
    • Kolch W., Neususs C., Pelzing M., et al. Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom Rev 2005, 24:959-977.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3
  • 54
    • 65349107657 scopus 로고    scopus 로고
    • The human urinary proteome reveals high similarity between kidney aging and chronic kidney disease
    • Zurbig P., Decramer S., Dakna M., et al. The human urinary proteome reveals high similarity between kidney aging and chronic kidney disease. Proteomics 2009, 9:2108-2117.
    • (2009) Proteomics , vol.9 , pp. 2108-2117
    • Zurbig, P.1    Decramer, S.2    Dakna, M.3
  • 55
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller L.N., Brusniak M.Y., Mani D.R., et al. An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J Proteome Res 2008, 7:51-61.
    • (2008) J Proteome Res , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.Y.2    Mani, D.R.3


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