메뉴 건너뛰기




Volumn 6, Issue 2, 2014, Pages 247-266

Classical MALDI-MS versus CE-based ESI-MS proteomic profiling in urine for clinical applications

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; PROTEOME; TUMOR MARKER;

EID: 84892712389     PISSN: 17576180     EISSN: 17576199     Source Type: Journal    
DOI: 10.4155/bio.13.313     Document Type: Review
Times cited : (19)

References (147)
  • 1
    • 84871297843 scopus 로고    scopus 로고
    • Next-generation proteomics: Towards an integrative view of proteome dynamics
    • Altelaar AF, Munoz J, Heck AJ. Next-generation proteomics: towards an integrative view of proteome dynamics. Nat. Rev. Genet. 14(1), 35-48 (2013).
    • (2013) Nat. Rev. Genet. , vol.14 , Issue.1 , pp. 35-48
    • Altelaar, A.F.1    Munoz, J.2    Heck, A.J.3
  • 2
    • 79952628909 scopus 로고    scopus 로고
    • Protein profiling for cancer biomarker discovery using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and infrared imaging: A review
    • Bakry R, Rainer M, Huck CW, Bonn GK: Protein profiling for cancer biomarker discovery using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry and infrared imaging: a review. Anal. Chim. Acta 690(1), 26-34 (2011).
    • (2011) Anal. Chim. Acta , vol.690 , Issue.1 , pp. 26-34
    • Bakry, R.1    Rainer, M.2    Huck, C.W.3    Bonn, G.K.4
  • 3
    • 0035100888 scopus 로고    scopus 로고
    • Biomarkers and surrogate endpoints: Preferred definitions and conceptual framework
    • Biomarkers Definitions Working Group
    • Biomarkers Definitions Working Group. Biomarkers and surrogate endpoints: preferred definitions and conceptual framework. Clin. Pharmacol. Ther. 69(3), 89-95 (2001).
    • (2001) Clin. Pharmacol. Ther. , vol.69 , Issue.3 , pp. 89-95
  • 4
    • 34047209848 scopus 로고    scopus 로고
    • Clinical proteomics: A need to define the field and to begin to set adequate standards
    • Mischak H, Apweiler R, Banks RE et al. Clinical proteomics: a need to define the field and to begin to set adequate standards. Proteomics. Clin. Appl. 1(2), 148-156 (2007).
    • (2007) Proteomics. Clin. Appl. , vol.1 , Issue.2 , pp. 148-156
    • Mischak, H.1    Apweiler, R.2    Banks, R.E.3
  • 5
    • 84877271000 scopus 로고    scopus 로고
    • Urinary biomarkers for prostate cancer: A review
    • Hessels D, Schalken JA. Urinary biomarkers for prostate cancer: a review. Asian J. Androl. 15(3), 333-339 (2013).
    • (2013) Asian J. Androl. , vol.15 , Issue.3 , pp. 333-339
    • Hessels, D.1    Schalken, J.A.2
  • 6
    • 75749101060 scopus 로고    scopus 로고
    • A recipe for proteomics diagnostic test development: The OVA1 test, from biomarker discovery to FDA clearance
    • Fung ET. A recipe for proteomics diagnostic test development: the OVA1 test, from biomarker discovery to FDA clearance. Clin. Chem. 56(2), 327-329 (2010).
    • (2010) Clin. Chem. , vol.56 , Issue.2 , pp. 327-329
    • Fung, E.T.1
  • 7
    • 79957624610 scopus 로고    scopus 로고
    • Profiling the proteome in renal transplantation
    • Sigdel TK, Lee S, Sarwal MM. Profiling the proteome in renal transplantation. Proteomics. Clin. Appl. 5(5-6), 269-280 (2011).
    • (2011) Proteomics. Clin. Appl. , vol.5 , Issue.5-6 , pp. 269-280
    • Sigdel, T.K.1    Lee, S.2    Sarwal, M.M.3
  • 8
    • 84898599851 scopus 로고    scopus 로고
    • Inconvenient truth: Cancer biomarker development by using proteomics
    • doi:10.1016/j.bbapap.2013.07.009 Epub ahead of print
    • Kondo T. Inconvenient truth: cancer biomarker development by using proteomics. Biochim. Biophys. Acta doi:10.1016/j.bbapap.2013.07.009 (2013) (Epub ahead of print).
    • (2013) Biochim. Biophys. Acta
    • Kondo, T.1
  • 9
    • 43149119293 scopus 로고    scopus 로고
    • Near infrared spectroscopy compared to liquid chromatography coupled to mass spectrometry and capillary electrophoresis as a detection tool for peptide reaction monitoring
    • Petter CH, Heigl N, Bachmann S et al. Near infrared spectroscopy compared to liquid chromatography coupled to mass spectrometry and capillary electrophoresis as a detection tool for peptide reaction monitoring. Amino. Acids 34(4), 605-616 (2008).
    • (2008) Amino. Acids , vol.34 , Issue.4 , pp. 605-616
    • Petter, C.H.1    Heigl, N.2    Bachmann, S.3
  • 10
    • 84872043509 scopus 로고    scopus 로고
    • Filter-based method for background removal in high-sensitivity wide-field-surface-enhanced Raman scattering imaging in vivo
    • Mallia RJ, McVeigh PZ, Veilleux I, Wilson BC. Filter-based method for background removal in high-sensitivity wide-field-surface-enhanced Raman scattering imaging in vivo. J. Biomed. Opt. 17(7), 076017 (2012).
    • (2012) J. Biomed. Opt. , vol.17 , Issue.7 , pp. 076017
    • Mallia, R.J.1    McVeigh, P.Z.2    Veilleux, I.3    Wilson, B.C.4
  • 11
    • 77957371887 scopus 로고    scopus 로고
    • Depletion of abundant plasma proteins and limitations of plasma proteomics
    • Tu C, Rudnick PA, Martinez MY et al. Depletion of abundant plasma proteins and limitations of plasma proteomics. J. Proteome. Res. 9(10), 4982-4991 (2010).
    • (2010) J. Proteome. Res. , vol.9 , Issue.10 , pp. 4982-4991
    • Tu, C.1    Rudnick, P.A.2    Martinez, M.Y.3
  • 12
    • 84863624457 scopus 로고    scopus 로고
    • Profiling plasma peptides for the identification of potential ageing biomarkers in Chinese Han adults
    • Lu J, Huang Y, Wang Y et al. Profiling plasma peptides for the identification of potential ageing biomarkers in Chinese Han adults. PLoS ONE 7(7), e39726 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.7
    • Lu, J.1    Huang, Y.2    Wang, Y.3
  • 13
    • 84861347338 scopus 로고    scopus 로고
    • Differential protein profiling of synovial fluid from rheumatoid arthritis and osteoarthritis patients using LC-MALDI TOF/TOF
    • Mateos J, Lourido L, Fernandez-Puente P et al. Differential protein profiling of synovial fluid from rheumatoid arthritis and osteoarthritis patients using LC-MALDI TOF/TOF. J. Proteomics. 75(10), 2869-2878 (2012).
    • (2012) J. Proteomics. , vol.75 , Issue.10 , pp. 2869-2878
    • Mateos, J.1    Lourido, L.2    Fernandez-Puente, P.3
  • 14
    • 79960125931 scopus 로고    scopus 로고
    • Plasma biomarker discovery using 3D protein profiling coupled with label-free quantitation
    • Beer LA, Tang HY, Barnhart KT, Speicher DW. Plasma biomarker discovery using 3D protein profiling coupled with label-free quantitation. Methods Mol. Biol. 728, 3-27 (2011).
    • (2011) Methods Mol. Biol. , vol.728 , pp. 3-27
    • Beer, L.A.1    Tang, H.Y.2    Barnhart, K.T.3    Speicher, D.W.4
  • 15
    • 79955034735 scopus 로고    scopus 로고
    • Time course proteomic profiling of human myocardial infarction plasma samples: An approach to new biomarker discovery
    • Silbiger VN, Luchessi AD, Hirata RD et al. Time course proteomic profiling of human myocardial infarction plasma samples: an approach to new biomarker discovery. Clin. Chim. Acta 412(11-12), 1086-1093 (2011).
    • (2011) Clin. Chim. Acta , vol.412 , Issue.11-12 , pp. 1086-1093
    • Silbiger, V.N.1    Luchessi, A.D.2    Hirata, R.D.3
  • 16
    • 79952753705 scopus 로고    scopus 로고
    • Markers of vascular disease in plasma from patients with chronic kidney disease identified by proteomic analysis
    • Schiffer E, Liabeuf S, Lacroix C et al. Markers of vascular disease in plasma from patients with chronic kidney disease identified by proteomic analysis. J. Hypertens. 29(4), 783-790 (2011).
    • (2011) J. Hypertens , vol.29 , Issue.4 , pp. 783-790
    • Schiffer, E.1    Liabeuf, S.2    Lacroix, C.3
  • 17
    • 84860325202 scopus 로고    scopus 로고
    • Candidate biomarker verification: Critical examination of a serum protein pattern for human colorectal cancer
    • Albrethsen J, Bogebo R, Moller CH, Olsen JA, Raskov HH, Gammeltoft S. Candidate biomarker verification: Critical examination of a serum protein pattern for human colorectal cancer. Proteomics. Clin. Appl. 6(3-4), 182-189 (2012).
    • (2012) Proteomics. Clin. Appl. , vol.6 , Issue.3-4 , pp. 182-189
    • Albrethsen, J.1    Bogebo, R.2    Moller, C.H.3    Olsen, J.A.4    Raskov, H.H.5    Gammeltoft, S.6
  • 18
    • 84877148563 scopus 로고    scopus 로고
    • Pre-analytical factors influencing the stability of cerebrospinal fluid proteins
    • Simonsen AH, Bahl JM, Danborg PBet al. Pre-analytical factors influencing the stability of cerebrospinal fluid proteins. J. Neurosci. Methods 215(2), 234-240 (2013).
    • (2013) J. Neurosci. Methods , vol.215 , Issue.2 , pp. 234-240
    • Simonsen, A.H.1    Bahl, J.M.2    Danborg, P.B.3
  • 19
    • 63649113691 scopus 로고    scopus 로고
    • Standardized peptidome profiling of human cerebrospinal fluid by magnetic bead separation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Bruegel M, Planert M, Baumann S et al. Standardized peptidome profiling of human cerebrospinal fluid by magnetic bead separation and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. J. Proteomics. 72(4), 608-615 (2009).
    • (2009) J. Proteomics , vol.72 , Issue.4 , pp. 608-615
    • Bruegel, M.1    Planert, M.2    Baumann, S.3
  • 20
    • 84880160226 scopus 로고    scopus 로고
    • High-resolution proteome/peptidome analysis of body fluids by capillary electrophoresis coupled with MS
    • Albalat A, Bitsika V, Zurbig P, Siwy J, Mullen W. High-resolution proteome/peptidome analysis of body fluids by capillary electrophoresis coupled with MS. Methods Mol. Biol. 984, 153-165 (2013).
    • (2013) Methods Mol. Biol. , vol.984 , pp. 153-165
    • Albalat, A.1    Bitsika, V.2    Zurbig, P.3    Siwy, J.4    Mullen, W.5
  • 21
    • 33847252481 scopus 로고    scopus 로고
    • CSF biomarker discovery using label-free nano-LC-MS based proteomic profiling: Technical aspects
    • Huang JT, McKenna T, Hughes C, Leweke FM, Schwarz E, Bahn S. CSF biomarker discovery using label-free nano-LC-MS based proteomic profiling: technical aspects. J. Sep. Sci. 30(2), 214-225 (2007).
    • (2007) J. Sep. Sci. , vol.30 , Issue.2 , pp. 214-225
    • Huang, J.T.1    McKenna, T.2    Hughes, C.3    Leweke, F.M.4    Schwarz, E.5    Bahn, S.6
  • 22
    • 79959504808 scopus 로고    scopus 로고
    • Identification of biomarkers for diagnosis and progression of MS by MALDI-TOF mass spectrometry
    • Teunissen CE, Koel-Simmelink MJ, Pham TV et al. Identification of biomarkers for diagnosis and progression of MS by MALDI-TOF mass spectrometry. Mult. Scler. 17(7), 838-850 (2011).
    • (2011) Mult. Scler. , vol.17 , Issue.7 , pp. 838-850
    • Teunissen, C.E.1    Koel-Simmelink, M.J.2    Pham, T.V.3
  • 23
    • 33947287762 scopus 로고    scopus 로고
    • Novel panel of cerebrospinal fluid biomarkers for the prediction of progression to Alzheimer dementia in patients with mild cognitive impairment
    • Simonsen AH, McGuire J, Hansson O et al. Novel panel of cerebrospinal fluid biomarkers for the prediction of progression to Alzheimer dementia in patients with mild cognitive impairment. Arch. Neurol. 64(3), 366-370 (2007).
    • (2007) Arch. Neurol. , vol.64 , Issue.3 , pp. 366-370
    • Simonsen, A.H.1    McGuire, J.2    Hansson, O.3
  • 24
    • 84857037858 scopus 로고    scopus 로고
    • Cerebrospinal fluid biomarkers for major depression confirm relevance of associated pathophysiology
    • Ditzen C, Tang N, Jastorff AM et al. Cerebrospinal fluid biomarkers for major depression confirm relevance of associated pathophysiology. Neuropsychopharmacology 37(4), 1013-1025 (2012).
    • (2012) Neuropsychopharmacology , vol.37 , Issue.4 , pp. 1013-1025
    • Ditzen, C.1    Tang, N.2    Jastorff, A.M.3
  • 25
    • 78650461840 scopus 로고    scopus 로고
    • Proteomic profiling of cerebrospinal fluid in Creutzfeldt-Jakob disease
    • Qualtieri A, Urso E, Le PM et al. Proteomic profiling of cerebrospinal fluid in Creutzfeldt-Jakob disease. Expert. Rev. Proteomics. 7(6), 907-917 (2010).
    • (2010) Expert. Rev. Proteomics. , vol.7 , Issue.6 , pp. 907-917
    • Qualtieri, A.1    Urso, E.2    Le, P.M.3
  • 26
    • 77956170603 scopus 로고    scopus 로고
    • Proteomic profiling of cerebrospinal fluid in parkinsonian disorders
    • Constantinescu R, Andreasson U, Li S et al. Proteomic profiling of cerebrospinal fluid in parkinsonian disorders. Parkinsonism. Relat. Disord. 16(8), 545-549 (2010).
    • (2010) Parkinsonism. Relat. Disord. , vol.16 , Issue.8 , pp. 545-549
    • Constantinescu, R.1    Andreasson, U.2    Li, S.3
  • 27
    • 84878640947 scopus 로고    scopus 로고
    • One decade of salivary proteomics: Current approaches and outstanding challenges
    • Amado FM, Ferreira RP, Vitorino R. One decade of salivary proteomics: current approaches and outstanding challenges. Clin. Biochem. 46(6), 506-517 (2013).
    • (2013) Clin. Biochem. , vol.46 , Issue.6 , pp. 506-517
    • Amado, F.M.1    Ferreira, R.P.2    Vitorino, R.3
  • 28
    • 51349132896 scopus 로고    scopus 로고
    • The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions
    • Denny P, Hagen FK, Hardt M et al. The proteomes of human parotid and submandibular/sublingual gland salivas collected as the ductal secretions. J. Proteome. Res. 7(5), 1994-2006 (2008).
    • (2008) J. Proteome. Res. , vol.7 , Issue.5 , pp. 1994-2006
    • Denny, P.1    Hagen, F.K.2    Hardt, M.3
  • 30
    • 17844368916 scopus 로고    scopus 로고
    • Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry
    • Hu S, Xie Y, Ramachandran P et al. Large-scale identification of proteins in human salivary proteome by liquid chromatography/mass spectrometry and two-dimensional gel electrophoresis-mass spectrometry. Proteomics 5(6), 1714-1728 (2005).
    • (2005) Proteomics , vol.5 , Issue.6 , pp. 1714-1728
    • Hu, S.1    Xie, Y.2    Ramachandran, P.3
  • 31
    • 79953737346 scopus 로고    scopus 로고
    • Saliva: Diagnostics and therapeutic perspectives
    • Spielmann N, Wong DT. Saliva: diagnostics and therapeutic perspectives. Oral Dis. 17(4), 345-354 (2011).
    • (2011) Oral Dis. , vol.17 , Issue.4 , pp. 345-354
    • Spielmann, N.1    Wong, D.T.2
  • 32
    • 34948866795 scopus 로고    scopus 로고
    • How shall we use the proteomics toolbox for biomarker discovery?
    • Lescuyer P, Hochstrasser D, Rabilloud T. How shall we use the proteomics toolbox for biomarker discovery? J. Proteome. Res. 6(9), 3371-3376 (2007).
    • (2007) J. Proteome. Res. , vol.6 , Issue.9 , pp. 3371-3376
    • Lescuyer, P.1    Hochstrasser, D.2    Rabilloud, T.3
  • 33
    • 84872176059 scopus 로고    scopus 로고
    • A quantitative proteomic analysis uncovers the relevance of CUL3 in bladder cancer aggressiveness
    • Grau L, Luque-Garcia JL, Gonzalez-Peramato P et al. A quantitative proteomic analysis uncovers the relevance of CUL3 in bladder cancer aggressiveness. PLoS ONE 8(1), e53328 (2013).
    • (2013) PLoS ONE , vol.8 , Issue.1
    • Grau, L.1    Luque-Garcia, J.L.2    Gonzalez-Peramato, P.3
  • 34
    • 84883158627 scopus 로고    scopus 로고
    • Individualised proteome profiling of human endometrial tumours improves detection of new prognostic markers
    • Attarha S, Andersson S, Mints M, Souchelnytskyi S. Individualised proteome profiling of human endometrial tumours improves detection of new prognostic markers. Br. J. Cancer 109(3), 704-713 (2013).
    • (2013) Br. J. Cancer , vol.109 , Issue.3 , pp. 704-713
    • Attarha, S.1    Andersson, S.2    Mints, M.3    Souchelnytskyi, S.4
  • 35
    • 47549119495 scopus 로고    scopus 로고
    • Urinary proteomics: Towards biomarker discovery, diagnostics and prognostics
    • Thongboonkerd V. Urinary proteomics: towards biomarker discovery, diagnostics and prognostics. Mol. Biosyst. 4(8), 810-815 (2008).
    • (2008) Mol. Biosyst. , vol.4 , Issue.8 , pp. 810-815
    • Thongboonkerd, V.1
  • 36
    • 69249154604 scopus 로고    scopus 로고
    • Proteomics in uremia and renal disease
    • Mischak H, Massy ZA, Jankowski J. Proteomics in uremia and renal disease. Semin. Dial. 22(4), 409-416 (2009).
    • (2009) Semin. Dial. , vol.22 , Issue.4 , pp. 409-416
    • Mischak, H.1    Massy, Z.A.2    Jankowski, J.3
  • 37
    • 0000415976 scopus 로고
    • Constancy of urinary creatinine excretion
    • Vestergaard P, Leverett R. Constancy of urinary creatinine excretion. J. Lab. Clin. Med. 51(2), 211-218 (1958).
    • (1958) J. Lab. Clin. Med. , vol.51 , Issue.2 , pp. 211-218
    • Vestergaard, P.1    Leverett, R.2
  • 38
    • 77953722868 scopus 로고    scopus 로고
    • Comprehensive human urine standards for comparability and standardization in clinical proteome analysis
    • Mischak H, Kolch W, Aivaliotis M et al. Comprehensive human urine standards for comparability and standardization in clinical proteome analysis. Proteomics. Clin. Appl. 4(4), 464-478 (2010).
    • (2010) Proteomics. Clin. Appl. , vol.4 , Issue.4 , pp. 464-478
    • Mischak, H.1    Kolch, W.2    Aivaliotis, M.3
  • 39
    • 84856479041 scopus 로고    scopus 로고
    • Analysis of the urine proteome via a combination of multi-dimensional approaches
    • Zerefos PG, Aivaliotis M, Baumann M, Vlahou A. Analysis of the urine proteome via a combination of multi-dimensional approaches. Proteomics 12(3), 391-400 (2012).
    • (2012) Proteomics , vol.12 , Issue.3 , pp. 391-400
    • Zerefos, P.G.1    Aivaliotis, M.2    Baumann, M.3    Vlahou, A.4
  • 40
    • 84874525984 scopus 로고    scopus 로고
    • Discovery of potential bladder cancer biomarkers by comparative urine proteomics and analysis
    • Lei T, Zhao X, Jin S, Meng Q, Zhou H, Zhang M: Discovery of potential bladder cancer biomarkers by comparative urine proteomics and analysis. Clin. Genitourin. Cancer 11(1), 56-62 (2013).
    • (2013) Clin. Genitourin. Cancer , vol.11 , Issue.1 , pp. 56-62
    • Lei, T.1    Zhao, X.2    Jin, S.3    Meng, Q.4    Zhou, H.5    Zhang, M.6
  • 41
    • 84877956744 scopus 로고    scopus 로고
    • Urine proteins identified by two-dimensional differential gel electrophoresis facilitate the differential diagnoses of scrapie
    • Lamoureux L, Simon SL, Plews M et al. Urine proteins identified by two-dimensional differential gel electrophoresis facilitate the differential diagnoses of scrapie. PLoS ONE 8(5), e64044 (2013).
    • (2013) PLoS ONE , vol.8 , Issue.5
    • Lamoureux, L.1    Simon, S.L.2    Plews, M.3
  • 42
    • 77950610129 scopus 로고    scopus 로고
    • Shotgun proteomics identifies proteins specific for acute renal transplant rejection
    • Sigdel TK, Kaushal A, Gritsenko M et al. Shotgun proteomics identifies proteins specific for acute renal transplant rejection. Proteomics. Clin. Appl. 4(1), 32-47 (2010).
    • (2010) Proteomics. Clin. Appl. , vol.4 , Issue.1 , pp. 32-47
    • Sigdel, T.K.1    Kaushal, A.2    Gritsenko, M.3
  • 43
    • 79957622297 scopus 로고    scopus 로고
    • Proteomic analysis of urinary upper gastrointestinal cancer markers
    • Husi H, Stephens N, Cronshaw A et al. Proteomic analysis of urinary upper gastrointestinal cancer markers. Proteomics. Clin. Appl. 5(5-6), 289-299 (2011).
    • (2011) Proteomics. Clin. Appl. , vol.5 , Issue.5-6 , pp. 289-299
    • Husi, H.1    Stephens, N.2    Cronshaw, A.3
  • 44
    • 84885417510 scopus 로고    scopus 로고
    • Improving peptide relative quantification in MALDI-TOF MS for biomarker assessment
    • Albalat A, Stalmach A, Bitsika V et al. Improving peptide relative quantification in MALDI-TOF MS for biomarker assessment. Proteomics 13(20), 2967-2975 (2013).
    • (2013) Proteomics , vol.13 , Issue.20 , pp. 2967-2975
    • Albalat, A.1    Stalmach, A.2    Bitsika, V.3
  • 45
    • 84890122630 scopus 로고    scopus 로고
    • Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: Focus on bladder cancer
    • doi:10.1002/prca.201300038 Epub ahead of print
    • Latosinska A, Frantzi M, Vlahou A, Mischak H. Clinical applications of capillary electrophoresis coupled to mass spectrometry in biomarker discovery: focus on bladder cancer. Proteomics. Clin. Appl. doi:10.1002/prca.201300038 (2013) (Epub ahead of print).
    • (2013) Proteomics. Clin. Appl.
    • Latosinska, A.1    Frantzi, M.2    Vlahou, A.3    Mischak, H.4
  • 46
    • 79251560313 scopus 로고    scopus 로고
    • CE-MS in biomarker discovery, validation, and clinical application
    • Mischak H, Schanstra JP. CE-MS in biomarker discovery, validation, and clinical application. Proteomics. Clin. Appl. 5(1-2), 9-23 (2011).
    • (2011) Proteomics. Clin. Appl. , vol.5 , Issue.1-2 , pp. 9-23
    • Mischak, H.1    Schanstra, J.P.2
  • 47
    • 33750040863 scopus 로고    scopus 로고
    • Preanalytical and analytical variation of surface-enhanced laser desorption-ionization time-of-flight mass spectrometry of human serum
    • Albrethsen J, Bogebo R, Olsen J, Raskov H, Gammeltoft S. Preanalytical and analytical variation of surface-enhanced laser desorption-ionization time-of-flight mass spectrometry of human serum. Clin. Chem. Lab. Med. 44(10), 1243-1252 (2006).
    • (2006) Clin. Chem. Lab. Med. , vol.44 , Issue.10 , pp. 1243-1252
    • Albrethsen, J.1    Bogebo, R.2    Olsen, J.3    Raskov, H.4    Gammeltoft, S.5
  • 48
    • 10744221488 scopus 로고    scopus 로고
    • Mass spectrometry for the detection of differentially expressed proteins: A comparison of surface-enhanced laser desorption/ionization and capillary electrophoresis/mass spectrometry
    • Neuhoff N, Kaiser T, Wittke S et al. Mass spectrometry for the detection of differentially expressed proteins: a comparison of surface-enhanced laser desorption/ionization and capillary electrophoresis/mass spectrometry. Rapid Commun. Mass Spectrom. 18(2), 149-156 (2004).
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , Issue.2 , pp. 149-156
    • Neuhoff, N.1    Kaiser, T.2    Wittke, S.3
  • 49
    • 84861341375 scopus 로고    scopus 로고
    • Reproducibility of mass spectrometry based protein profiles for diagnosis of ovarian cancer across clinical studies: A systematic review
    • Callesen AK, Mogensen O, Jensen AK et al. Reproducibility of mass spectrometry based protein profiles for diagnosis of ovarian cancer across clinical studies: a systematic review. J. Proteomics 75(10), 2758-2772 (2012).
    • (2012) J. Proteomics , vol.75 , Issue.10 , pp. 2758-2772
    • Callesen, A.K.1    Mogensen, O.2    Jensen, A.K.3
  • 50
    • 77951623830 scopus 로고    scopus 로고
    • Integrating high-throughput technologies in the quest for effective biomarkers for ovarian cancer
    • Kulasingam V, Pavlou MP, Diamandis EP. Integrating high-throughput technologies in the quest for effective biomarkers for ovarian cancer. Nat. Rev. Cancer 10(5), 371-378 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , Issue.5 , pp. 371-378
    • Kulasingam, V.1    Pavlou, M.P.2    Diamandis, E.P.3
  • 51
    • 84862866916 scopus 로고    scopus 로고
    • Expanding the zebrafish embryo proteome using multiple fractionation approaches and tandem mass spectrometry
    • Lossner C, Wee S, Ler SG et al. Expanding the zebrafish embryo proteome using multiple fractionation approaches and tandem mass spectrometry. Proteomics 12(11), 1879-1882 (2012).
    • (2012) Proteomics , vol.12 , Issue.11 , pp. 1879-1882
    • Lossner, C.1    Wee, S.2    Ler, S.G.3
  • 52
    • 84855369410 scopus 로고    scopus 로고
    • Robust analysis of the yeast proteome under 50 kDa by molecular-mass-based fractionation and top-down mass spectrometry
    • Kellie JF, Catherman AD, Durbin KR et al. Robust analysis of the yeast proteome under 50 kDa by molecular-mass-based fractionation and top-down mass spectrometry. Anal. Chem. 84(1), 209-215 (2012).
    • (2012) Anal. Chem. , vol.84 , Issue.1 , pp. 209-215
    • Kellie, J.F.1    Catherman, A.D.2    Durbin, K.R.3
  • 53
    • 79952201760 scopus 로고    scopus 로고
    • Identification of chemical-adducted proteins in urine by multi-dimensional protein identification technology (LC/LC-MS/MS)
    • Labenski MT, Fisher AA, Monks TJ, Lau SS. Identification of chemical-adducted proteins in urine by multi-dimensional protein identification technology (LC/LC-MS/MS). Methods Mol. Biol. 691, 339-347 (2011).
    • (2011) Methods Mol. Biol. , vol.691 , pp. 339-347
    • Labenski, M.T.1    Fisher, A.A.2    Monks, T.J.3    Lau, S.S.4
  • 54
    • 84858972964 scopus 로고    scopus 로고
    • Performance of different separation methods interfaced in the same MS-reflection TOF detector: A comparison of performance between CE versus HPLC for biomarker analysis
    • Mullen W, Albalat A, Gonzalez J et al. Performance of different separation methods interfaced in the same MS-reflection TOF detector: a comparison of performance between CE versus HPLC for biomarker analysis. Electrophoresis 33(4), 567-574 (2012).
    • (2012) Electrophoresis , vol.33 , Issue.4 , pp. 567-574
    • Mullen, W.1    Albalat, A.2    Gonzalez, J.3
  • 55
    • 77957287523 scopus 로고    scopus 로고
    • High-efficiency liquid chromatography-mass spectrometry separations with 50 mm, 250 mm, and 1 m long polymer-based monolithic capillary columns for the characterization of complex proteolytic digests
    • Eeltink S, Dolman S, Detobel F, Swart R, Ursem M, Schoenmakers PJ. High-efficiency liquid chromatography-mass spectrometry separations with 50 mm, 250 mm, and 1 m long polymer-based monolithic capillary columns for the characterization of complex proteolytic digests. J. Chromatogr. A 1217(43), 6610-6615 (2010).
    • (2010) J. Chromatogr. A , vol.1217 , Issue.43 , pp. 6610-6615
    • Eeltink, S.1    Dolman, S.2    Detobel, F.3    Swart, R.4    Ursem, M.5    Schoenmakers, P.J.6
  • 56
    • 84885916658 scopus 로고    scopus 로고
    • Absolute quantification of selected proteins in the human osteoarthritic secretome
    • Peffers MJ, Beynon RJ, Clegg PD. Absolute quantification of selected proteins in the human osteoarthritic secretome. Int. J. Mol. Sci. 14(10), 20658-20681 (2013).
    • (2013) Int. J. Mol. Sci. , vol.14 , Issue.10 , pp. 20658-20681
    • Peffers, M.J.1    Beynon, R.J.2    Clegg, P.D.3
  • 57
    • 84886028630 scopus 로고    scopus 로고
    • Multi-profile Bayesian alignment model for LC-MS data analysis with integration of internal standards
    • Tsai TH, Tadesse MG, Di PC et al. Multi-profile Bayesian alignment model for LC-MS data analysis with integration of internal standards. Bioinformatics 29(21), 2774-2780 (2013).
    • (2013) Bioinformatics , vol.29 , Issue.21 , pp. 2774-2780
    • Tsai, T.H.1    Tadesse, M.G.2    Di, P.C.3
  • 58
    • 0029841119 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption ionization mass-spectrometry of proteins
    • Beavis RC, Chait BT. Matrix-assisted laser desorption ionization mass-spectrometry of proteins. Methods Enzymol. 270, 519-551 (1996).
    • (1996) Methods Enzymol. , vol.270 , pp. 519-551
    • Beavis, R.C.1    Chait, B.T.2
  • 59
    • 0024772621 scopus 로고
    • Cinnamic acid derivatives as matrices for ultraviolet laser desorption mass spectrometry of proteins
    • Beavis RC, Chait BT. Cinnamic acid derivatives as matrices for ultraviolet laser desorption mass spectrometry of proteins. Rapid Commun. Mass Spectrom. 3(12), 432-435 (1989).
    • (1989) Rapid Commun. Mass Spectrom. , vol.3 , Issue.12 , pp. 432-435
    • Beavis, R.C.1    Chait, B.T.2
  • 60
    • 0028470545 scopus 로고
    • Comparative mapping of recombinant proteins and glycoproteins by plasma desorption and matrix-assisted laser desorption/ionization mass spectrometry
    • Tsarbopoulos A, Karas M, Strupat K, Pramanik BN, Nagabhushan TL, Hillenkamp F. Comparative mapping of recombinant proteins and glycoproteins by plasma desorption and matrix-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 66(13), 2062-2070 (1994).
    • (1994) Anal. Chem. , vol.66 , Issue.13 , pp. 2062-2070
    • Tsarbopoulos, A.1    Karas, M.2    Strupat, K.3    Pramanik, B.N.4    Nagabhushan, T.L.5    Hillenkamp, F.6
  • 61
    • 50449099939 scopus 로고    scopus 로고
    • 4-Chloro-alpha-cyanocinnamic acid is an advanced, rationally designed MALDI matrix
    • Jaskolla TW, Lehmann WD, Karas M. 4-Chloro-alpha-cyanocinnamic acid is an advanced, rationally designed MALDI matrix. Proc. Natl Acad. Sci. USA 105(34), 12200-12205 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.34 , pp. 12200-12205
    • Jaskolla, T.W.1    Lehmann, W.D.2    Karas, M.3
  • 62
    • 2442513210 scopus 로고    scopus 로고
    • Dried-droplet probe preparation on AnchorChip targets for navigating the acquisition of matrix-assisted laser desorption/ionization time-of-flight spectra by fluorescence of matrix/analyte crystals
    • Thomas H, Havlis J, Peychl J, Shevchenko A. Dried-droplet probe preparation on AnchorChip targets for navigating the acquisition of matrix-assisted laser desorption/ionization time-of-flight spectra by fluorescence of matrix/analyte crystals. Rapid Commun. Mass Spectrom. 18(9), 923-930 (2004).
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , Issue.9 , pp. 923-930
    • Thomas, H.1    Havlis, J.2    Peychl, J.3    Shevchenko, A.4
  • 63
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M, Hillenkamp F. Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal. Chem. 60(20), 2299-2301 (1988).
    • (1988) Anal. Chem. , vol.60 , Issue.20 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 64
    • 0001305955 scopus 로고
    • Improved mass accuracy in matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry of peptides
    • Vorm O, Mann M. Improved mass accuracy in matrix-assisted laser desorption/ionisation time-of-flight mass spectrometry of peptides. J. Am. Soc. Mass Spectrom. 5(11), 955-958 (1994).
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , Issue.11 , pp. 955-958
    • Vorm, O.1    Mann, M.2
  • 65
    • 79955462941 scopus 로고    scopus 로고
    • The first decade of MALDI protein profiling: A lesson in translational biomarker research
    • Albrethsen J. The first decade of MALDI protein profiling: a lesson in translational biomarker research. J. Proteomics 74(6), 765-773 (2011).
    • (2011) J. Proteomics , vol.74 , Issue.6 , pp. 765-773
    • Albrethsen, J.1
  • 66
    • 84868250682 scopus 로고    scopus 로고
    • Graphite supported preparation (GSP) of alpha-cyano-4-hydroxycinnamic acid (CHCA) for matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) for peptides and proteins
    • Gorka J, Bahr U, Karas M. Graphite supported preparation (GSP) of alpha-cyano-4-hydroxycinnamic acid (CHCA) for matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) for peptides and proteins. J. Am. Soc. Mass Spectrom. 23(11), 1949-1954 (2012).
    • (2012) J. Am. Soc. Mass Spectrom. , vol.23 , Issue.11 , pp. 1949-1954
    • Gorka, J.1    Bahr, U.2    Karas, M.3
  • 67
    • 67650394372 scopus 로고    scopus 로고
    • Comparison between the matrices alpha-cyano-4-hydroxycinnamic acid and 4-chloro-alpha-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry
    • Jaskolla TW, Papasotiriou DG, Karas M. Comparison between the matrices alpha-cyano-4-hydroxycinnamic acid and 4-chloro-alpha-cyanocinnamic acid for trypsin, chymotrypsin, and pepsin digestions by MALDI-TOF mass spectrometry. J. Proteome. Res. 8(7), 3588-3597 (2009).
    • (2009) J. Proteome. Res. , vol.8 , Issue.7 , pp. 3588-3597
    • Jaskolla, T.W.1    Papasotiriou, D.G.2    Karas, M.3
  • 68
    • 33845645547 scopus 로고    scopus 로고
    • Recent developments in methods and technology for analysis of biological samples by MALDI-TOF-MS
    • Pan C, Xu S, Zhou H, Fu Y, Ye M, Zou H. Recent developments in methods and technology for analysis of biological samples by MALDI-TOF-MS. Anal. Bioanal. Chem. 387(1), 193-204 (2007).
    • (2007) Anal. Bioanal. Chem. , vol.387 , Issue.1 , pp. 193-204
    • Pan, C.1    Xu, S.2    Zhou, H.3    Fu, Y.4    Ye, M.5    Zou, H.6
  • 69
    • 62149095745 scopus 로고    scopus 로고
    • Modern MALDI time-of-flight mass spectrometry
    • Vestal ML. Modern MALDI time-of-flight mass spectrometry. J. Mass Spectrom. 44(3), 303-317 (2009).
    • (2009) J. Mass Spectrom. , vol.44 , Issue.3 , pp. 303-317
    • Vestal, M.L.1
  • 71
    • 23944436422 scopus 로고    scopus 로고
    • Proteomics: From basic research to diagnostic application.A review of requirements and needs
    • Vitzthum F, Behrens F, Anderson NL,Shaw JH. Proteomics: from basic research to diagnostic application. A review of requirements and needs. J. Proteome. Res. 4(4), 1086-1097 (2005).
    • (2005) J. Proteome. Res. , vol.4 , Issue.4 , pp. 1086-1097
    • Vitzthum, F.1    Behrens, F.2    Anderson Nlshaw, J.H.3
  • 72
    • 58149287747 scopus 로고    scopus 로고
    • Investigating the quantitative nature of MALDI-TOF MS
    • Szajli E, Feher T, Medzihradszky KF. Investigating the quantitative nature of MALDI-TOF MS. Mol. Cell Proteomics 7(12), 2410-2418 (2008).
    • (2008) Mol. Cell Proteomics , vol.7 , Issue.12 , pp. 2410-2418
    • Szajli, E.1    Feher, T.2    Medzihradszky, K.F.3
  • 73
    • 0029979976 scopus 로고    scopus 로고
    • Influence of matrix solution conditions on the MALDI-MS analysis of peptides and proteins
    • Cohen SL, Chait BT. Influence of matrix solution conditions on the MALDI-MS analysis of peptides and proteins. Anal. Chem. 68(1), 31-37 (1996).
    • (1996) Anal. Chem. , vol.68 , Issue.1 , pp. 31-37
    • Cohen, S.L.1    Chait, B.T.2
  • 74
    • 0033214277 scopus 로고    scopus 로고
    • The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins
    • Krause E, Wenschuh H, Jungblut PR. The dominance of arginine-containing peptides in MALDI-derived tryptic mass fingerprints of proteins. Anal. Chem. 71(19), 4160-4165 (1999).
    • (1999) Anal. Chem. , vol.71 , Issue.19 , pp. 4160-4165
    • Krause, E.1    Wenschuh, H.2    Jungblut, P.R.3
  • 76
    • 34047235457 scopus 로고    scopus 로고
    • Advances in urinary proteome analysis and biomarker discovery
    • Fliser D, Novak J, Thongboonkerd V et al. Advances in urinary proteome analysis and biomarker discovery. J. Am. Soc. Nephrol. 18(4), 1057-1071 (2007).
    • (2007) J. Am. Soc. Nephrol. , vol.18 , Issue.4 , pp. 1057-1071
    • Fliser, D.1    Novak, J.2    Thongboonkerd, V.3
  • 77
    • 34447262161 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry for the analysis of intact proteins
    • Haselberg R, de Jong GJ, Somsen GW. Capillary electrophoresis-mass spectrometry for the analysis of intact proteins. J. Chromatogr. A 1159(1-2), 81-109 (2007).
    • (2007) J. Chromatogr. A , vol.1159 , Issue.1-2 , pp. 81-109
    • Haselberg, R.1    De Jong, G.J.2    Somsen, G.W.3
  • 78
    • 18444393438 scopus 로고    scopus 로고
    • Combining capillary electrophoresis with mass spectrometry for applications in proteomics
    • Simpson DC, Smith RD. Combining capillary electrophoresis with mass spectrometry for applications in proteomics. Electrophoresis 26(7-8), 1291-1305 (2005).
    • (2005) Electrophoresis , vol.26 , Issue.7-8 , pp. 1291-1305
    • Simpson, D.C.1    Smith, R.D.2
  • 79
    • 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, Mischak H. Capillary electrophoresis-mass spectrometry as a powerful tool in clinical diagnosis and biomarker discovery. Mass Spectrom. Rev. 24(6), 959-977 (2005).
    • (2005) Mass Spectrom. Rev. , vol.24 , Issue.6 , pp. 959-977
    • Kolch, W.1    Neususs, C.2    Pelzing, M.3    Mischak, H.4
  • 80
    • 84892757841 scopus 로고    scopus 로고
    • Basic principles and modes of Capillary Electrophoresis
    • Petersen RJ, Mohammad AA (Eds.). Humana Press Inc., NY, USA
    • Whatley H. Basic principles and modes of Capillary Electrophoresis. In: Clinical and Forensic Application of Capillary Electrophoresis. Petersen RJ, Mohammad AA (Eds.). Humana Press Inc., NY, USA 21-58 (2001).
    • (2001) Clinical and Forensic Application of Capillary Electrophoresis , pp. 21-58
    • Whatley, H.1
  • 81
    • 38349107355 scopus 로고    scopus 로고
    • Peptidomic analysis of rat urine using capillary electrophoresis coupled to mass spectrometry
    • Frommberger M, Zurbig P, Jantos J et al. Peptidomic analysis of rat urine using capillary electrophoresis coupled to mass spectrometry. Proteomics Clin. Appl. 1(7), 650-660 (2007).
    • (2007) Proteomics Clin. Appl. , vol.1 , Issue.7 , pp. 650-660
    • Frommberger, M.1    Zurbig, P.2    Jantos, J.3
  • 82
    • 79957592170 scopus 로고    scopus 로고
    • Human urinary peptide database for multiple disease biomarker discovery
    • Siwy J, Mullen W, Golovko I, Franke J, Zurbig P. Human urinary peptide database for multiple disease biomarker discovery. Proteomics Clin. Appl. 5(5-6), 367-374 (2011).
    • (2011) Proteomics Clin. Appl. , vol.5 , Issue.5-6 , pp. 367-374
    • Siwy, J.1    Mullen, W.2    Golovko, I.3    Franke, J.4    Zurbig, P.5
  • 83
    • 69849106821 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in biomarker discovery and clinical diagnosis: An update of recent developments
    • Mischak H, Coon JJ, Novak J, Weissinger EM, Schanstra JP, Dominiczak AF. Capillary electrophoresis-mass spectrometry as a powerful tool in biomarker discovery and clinical diagnosis: an update of recent developments. Mass Spectrom. Rev. 28(5), 703-724 (2009).
    • (2009) Mass Spectrom. Rev. , vol.28 , Issue.5 , pp. 703-724
    • Mischak, H.1    Coon, J.J.2    Novak, J.3    Weissinger, E.M.4    Schanstra, J.P.5    Dominiczak, A.F.6
  • 84
    • 0025837003 scopus 로고
    • Selective effect of ethanol on norepinephrine-and nicotine-induced emesis in cats
    • Beleslin DB, Jovanovic-Micic D, Nikolic SB, Samardzic R. Selective effect of ethanol on norepinephrine-and nicotine-induced emesis in cats. Alcohol 8(6), 499-501 (1991).
    • (1991) Alcohol , vol.8 , Issue.6 , pp. 499-501
    • Beleslin, D.B.1    Jovanovic-Micic, D.2    Nikolic, S.B.3    Samardzic, R.4
  • 85
    • 51249098520 scopus 로고    scopus 로고
    • Twenty years of interface development for capillary electrophoresis- electrospray ionization-mass spectrometry
    • Maxwell EJ, Chen DD. Twenty years of interface development for capillary electrophoresis-electrospray ionization-mass spectrometry. Anal. Chim. Acta 627(1), 25-33 (2008).
    • (2008) Anal. Chim. Acta , vol.627 , Issue.1 , pp. 25-33
    • Maxwell, E.J.1    Chen, D.D.2
  • 86
    • 84894903134 scopus 로고    scopus 로고
    • Novel sheathless CE-MS interface as an original and powerful infusion platform for nanoESI study: From intact proteins to high molecular mass noncovalent complexes
    • doi:10.1007/s00216-013-7226-1 Epub ahead of print
    • Gahoual R, Busnel JM, Wolff P, Francois YN, Leize-Wagner E. Novel sheathless CE-MS interface as an original and powerful infusion platform for nanoESI study: from intact proteins to high molecular mass noncovalent complexes. Anal. Bioanal. Chem. doi:10.1007/s00216-013-7226-1 (2013) (Epub ahead of print).
    • (2013) Anal. Bioanal. Chem.
    • Gahoual, R.1    Busnel, J.M.2    Wolff, P.3    Francois, Y.N.4    Leize-Wagner, E.5
  • 87
    • 33745335841 scopus 로고    scopus 로고
    • Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation
    • Zurbig P, Renfrow MB, Schiffer E et al. Biomarker discovery by CE-MS enables sequence analysis via MS/MS with platform-independent separation. Electrophoresis 27(11), 2111-2125 (2006).
    • (2006) Electrophoresis , vol.27 , Issue.11 , pp. 2111-2125
    • Zurbig, P.1    Renfrow, M.B.2    Schiffer, E.3
  • 88
    • 33847286435 scopus 로고    scopus 로고
    • Recent advances in capillary electrophoresis for biomarker discovery
    • Bakry R, Huck CW, Najam-ul-Haq M, Rainer M, Bonn GK. Recent advances in capillary electrophoresis for biomarker discovery. J. Sep. Sci. 30(2), 192-201 (2007).
    • (2007) J. Sep. Sci. , vol.30 , Issue.2 , pp. 192-201
    • Bakry, R.1    Huck, C.W.2    Najam-Ul-Haq, M.3    Rainer, M.4    Bonn, G.K.5
  • 90
    • 65349086126 scopus 로고    scopus 로고
    • Electrolyte systems for on-line CE-MS: Detection requirements and separation possibilities
    • Pantuckova P, Gebauer P, Bocek P, Krivankova L. Electrolyte systems for on-line CE-MS: detection requirements and separation possibilities. Electrophoresis 30(1), 203-214 (2009).
    • (2009) Electrophoresis , vol.30 , Issue.1 , pp. 203-214
    • Pantuckova, P.1    Gebauer, P.2    Bocek, P.3    Krivankova, L.4
  • 91
    • 84862873837 scopus 로고    scopus 로고
    • Capillary electrophoresis/mass spectrometry relevant to pharmaceutical and biotechnological applications
    • Pioch M, Bunz SC, Neususs C. Capillary electrophoresis/mass spectrometry relevant to pharmaceutical and biotechnological applications. Electrophoresis 33(11), 1517-1530 (2012).
    • (2012) Electrophoresis , vol.33 , Issue.11 , pp. 1517-1530
    • Pioch, M.1    Bunz, S.C.2    Neususs, C.3
  • 92
    • 3543063251 scopus 로고    scopus 로고
    • Capillary electrophoresis coupled to mass spectrometer for automated and robust polypeptide determination in body fluids for clinical use
    • Kaiser T, Wittke S, Just I et al. Capillary electrophoresis coupled to mass spectrometer for automated and robust polypeptide determination in body fluids for clinical use. Electrophoresis 25(13), 2044-2055 (2004).
    • (2004) Electrophoresis , vol.25 , Issue.13 , pp. 2044-2055
    • Kaiser, T.1    Wittke, S.2    Just, I.3
  • 93
    • 10744228656 scopus 로고    scopus 로고
    • Determination of peptides and proteins in human urine with capillary electrophoresis-mass spectrometry, a suitable tool for the establishment of new diagnostic markers
    • Wittke S, Fliser D, Haubitz M et al. Determination of peptides and proteins in human urine with capillary electrophoresis-mass spectrometry, a suitable tool for the establishment of new diagnostic markers. J. Chromatogr. A 1013(1-2), 173-181(2003).
    • (2003) J. Chromatogr. A , vol.1013 , Issue.1-2 , pp. 173-181
    • Wittke, S.1    Fliser, D.2    Haubitz, M.3
  • 94
    • 84878643645 scopus 로고    scopus 로고
    • Technical aspects and inter-laboratory variability in native peptide profiling: The CE-MS experience
    • Mischak H, Vlahou A, Ioannidis JP. Technical aspects and inter-laboratory variability in native peptide profiling: the CE-MS experience. Clin. Biochem. 46(6), 432-443 (2013).
    • (2013) Clin. Biochem. , vol.46 , Issue.6 , pp. 432-443
    • Mischak, H.1    Vlahou, A.2    Ioannidis, J.P.3
  • 95
    • 84878666313 scopus 로고    scopus 로고
    • Recent advances in capillary electrophoresis coupled to mass spectrometry for clinical proteomic applications
    • Stalmach A, Albalat A, Mullen W, Mischak H. Recent advances in capillary electrophoresis coupled to mass spectrometry for clinical proteomic applications. Electrophoresis 34(11), 1452-1464 (2013).
    • (2013) Electrophoresis , vol.34 , Issue.11 , pp. 1452-1464
    • Stalmach, A.1    Albalat, A.2    Mullen, W.3    Mischak, H.4
  • 96
    • 84898858336 scopus 로고    scopus 로고
    • MALDI mass spectrometry in prostate cancer biomarker discovery
    • doi:10.1016/j.bbapap.2013.06.015 Epub ahead of print
    • Flatley B, Malone P, Cramer R. MALDI mass spectrometry in prostate cancer biomarker discovery. Biochim. Biophys. Acta doi:10.1016/j.bbapap.2013.06.015 (2013) (Epub ahead of print).
    • (2013) Biochim. Biophys. Acta
    • Flatley, B.1    Malone, P.2    Cramer, R.3
  • 97
    • 33846027431 scopus 로고    scopus 로고
    • Detection of pre-neoplastic and neoplastic prostate disease by MALDI profiling of urine
    • M'Koma AE, Blum DL, Norris JL et al. Detection of pre-neoplastic and neoplastic prostate disease by MALDI profiling of urine. Biochem. Biophys. Res. Commun. 353(3), 829-834 (2007).
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , Issue.3 , pp. 829-834
    • M'Koma, A.E.1    Blum, D.L.2    Norris, J.L.3
  • 99
    • 84878298880 scopus 로고    scopus 로고
    • Non-invasive detection of drug toxicity in rats by solid-phase extraction and MALDI-TOF analysis of urine samples
    • Iloro I, Gonzalez E, Gutierrez-de Juan V, Mato JM, Falcon-Perez JM, Elortza F. Non-invasive detection of drug toxicity in rats by solid-phase extraction and MALDI-TOF analysis of urine samples. Anal. Bioanal. Chem. 405(7), 2311-2320 (2013).
    • (2013) Anal. Bioanal. Chem. , vol.405 , Issue.7 , pp. 2311-2320
    • Iloro, I.1    Gonzalez, E.2    Gutierrez-De Juan, V.3    Mato, J.M.4    Falcon-Perez, J.M.5    Elortza, F.6
  • 100
    • 72149116700 scopus 로고    scopus 로고
    • Optimization of analytical and pre-analytical conditions for MALDI-TOF-MS human urine protein profiles
    • Calvano CD, Aresta A, Iacovone M et al. Optimization of analytical and pre-analytical conditions for MALDI-TOF-MS human urine protein profiles. J. Pharm. Biomed. Anal. 51(4), 907-914 (2010).
    • (2010) J. Pharm. Biomed. Anal. , vol.51 , Issue.4 , pp. 907-914
    • Calvano, C.D.1    Aresta, A.2    Iacovone, M.3
  • 101
    • 19944362482 scopus 로고    scopus 로고
    • Enhancement of sensitivity and resolution of surface-enhanced laser desorption/ionization time-of-flight mass spectrometric records for serum peptides using time-series analysis techniques
    • Malyarenko DI, Cooke WE, Adam BL et al. Enhancement of sensitivity and resolution of surface-enhanced laser desorption/ionization time-of-flight mass spectrometric records for serum peptides using time-series analysis techniques. Clin. Chem. 51(1), 65-74 (2005).
    • (2005) Clin. Chem. , vol.51 , Issue.1 , pp. 65-74
    • Malyarenko, D.I.1    Cooke, W.E.2    Adam, B.L.3
  • 103
    • 69249139037 scopus 로고    scopus 로고
    • Optimal preparation methods for automated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry profiling of low molecular weight proteins and peptides
    • Penno MA, Ernst M, Hoffmann P. Optimal preparation methods for automated matrix-assisted laser desorption/ionization time-of-flight mass spectrometry profiling of low molecular weight proteins and peptides. Rapid Commun. Mass Spectrom. 23(17), 2656-2662 (2009).
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , Issue.17 , pp. 2656-2662
    • Penno, M.A.1    Ernst, M.2    Hoffmann, P.3
  • 104
    • 70349758752 scopus 로고    scopus 로고
    • Capillary electrophoresis coupled to mass spectrometry for proteomic profiling of human urine and biomarker discovery
    • Zurbig P, Schiffer E, Mischak H. Capillary electrophoresis coupled to mass spectrometry for proteomic profiling of human urine and biomarker discovery. Methods Mol.Biol. 564, 105-121 (2009).
    • (2009) Methods Mol.Biol. , vol.564 , pp. 105-121
    • Zurbig, P.1    Schiffer, E.2    Mischak, H.3
  • 105
    • 34248334942 scopus 로고    scopus 로고
    • Reproducibility in protein profiling by MALDI-TOF mass spectrometry
    • Albrethsen J. Reproducibility in protein profiling by MALDI-TOF mass spectrometry. Clin. Chem. 53(5), 852-858 (2007).
    • (2007) Clin. Chem. , vol.53 , Issue.5 , pp. 852-858
    • Albrethsen, J.1
  • 106
    • 58149383790 scopus 로고    scopus 로고
    • Quantitative matrix-assisted laser desorption/ionization mass spectrometry
    • Duncan MW, Roder H, Hunsucker SW. Quantitative matrix-assisted laser desorption/ionization mass spectrometry. Brief. Funct. Genomic. Proteomic. 7(5), 355-370 (2008).
    • (2008) Brief. Funct. Genomic. Proteomic. , vol.7 , Issue.5 , pp. 355-370
    • Duncan, M.W.1    Roder, H.2    Hunsucker, S.W.3
  • 107
    • 34347393745 scopus 로고    scopus 로고
    • Mass spectrometry to classify non-small-cell lung cancer patients for clinical outcome after treatment with epidermal growth factor receptor tyrosine kinase inhibitors: A multicohort cross-institutional study
    • Taguchi F, Solomon B, Gregorc V et al. Mass spectrometry to classify non-small-cell lung cancer patients for clinical outcome after treatment with epidermal growth factor receptor tyrosine kinase inhibitors: a multicohort cross-institutional study. J. Natl. Cancer Inst. 99(11), 838-846 (2007).
    • (2007) J. Natl. Cancer Inst. , vol.99 , Issue.11 , pp. 838-846
    • Taguchi, F.1    Solomon, B.2    Gregorc, V.3
  • 108
    • 60849087391 scopus 로고    scopus 로고
    • Quantitative urinary proteome analysis for biomarker evaluation in chronic kidney disease
    • Jantos-Siwy J, Schiffer E, Brand K et al. Quantitative urinary proteome analysis for biomarker evaluation in chronic kidney disease. J. Proteome. Res. 8(1), 268-281 (2009).
    • (2009) J. Proteome. Res. , vol.8 , Issue.1 , pp. 268-281
    • Jantos-Siwy, J.1    Schiffer, E.2    Brand, K.3
  • 109
    • 84866492752 scopus 로고    scopus 로고
    • A comparison between MALDI-MS and CE-MS data for biomarker assessment in chronic kidney diseases
    • Molin L, Seraglia R, Lapolla A et al. A comparison between MALDI-MS and CE-MS data for biomarker assessment in chronic kidney diseases. J. Proteomics 75(18), 5888-5897 (2012).
    • (2012) J. Proteomics , vol.75 , Issue.18 , pp. 5888-5897
    • Molin, L.1    Seraglia, R.2    Lapolla, A.3
  • 110
    • 84883289789 scopus 로고    scopus 로고
    • Bottom-up proteome analysis of E. Coli using capillary zone electrophoresis-tandem mass spectrometry with an electrokinetic sheath-flow electrospray interface
    • Yan X, Essaka DC, Sun L, Zhu G, Dovichi NJ. Bottom-up proteome analysis of E. coli using capillary zone electrophoresis-tandem mass spectrometry with an electrokinetic sheath-flow electrospray interface. Proteomics 13(17), 2546-2551 (2013).
    • (2013) Proteomics , vol.13 , Issue.17 , pp. 2546-2551
    • Yan, X.1    Essaka, D.C.2    Sun, L.3    Zhu, G.4    Dovichi, N.J.5
  • 111
    • 84897410743 scopus 로고    scopus 로고
    • Comparison of CE-MS/MS and LC-MS/MS sequencing demonstrates significant complementarity in natural peptide identification in human urine
    • doi: 10.1002/elps.201300327 Epub ahead of print
    • Klein J, Papadopoulos T, Mischak H, Mullen W. Comparison of CE-MS/MS and LC-MS/MS sequencing demonstrates significant complementarity in natural peptide identification in human urine. Electrophoresis doi: 10.1002/elps.201300327 (2013) (Epub ahead of print).
    • (2013) Electrophoresis
    • Klein, J.1    Papadopoulos, T.2    Mischak, H.3    Mullen, W.4
  • 112
    • 84874755802 scopus 로고    scopus 로고
    • Identification of a novel biomarker for biliary tract cancer using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Article ID 108609
    • Kikkawa S, Sogawa K, Satoh M et al. Identification of a novel biomarker for biliary tract cancer using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Int. J. Proteomics, Article ID 108609 (2012).
    • (2012) Int. J. Proteomics
    • Kikkawa, S.1    Sogawa, K.2    Satoh, M.3
  • 113
    • 84875910524 scopus 로고    scopus 로고
    • MALDI in-source decay, from sequencing to imaging
    • Debois D, Smargiasso N, Demeure K et al. MALDI in-source decay, from sequencing to imaging. Top. Curr. Chem. 331, 117-141 (2013).
    • (2013) Top. Curr. Chem. , vol.331 , pp. 117-141
    • Debois, D.1    Smargiasso, N.2    Demeure, K.3
  • 114
    • 84867057236 scopus 로고    scopus 로고
    • Analysing signalling networks by mass spectrometry
    • Jorgensen C, Locard-Paulet M: Analysing signalling networks by mass spectrometry. Amino. Acids 43(3), 1061-1074 (2012).
    • (2012) Amino. Acids , vol.43 , Issue.3 , pp. 1061-1074
    • Jorgensen, C.1    Locard-Paulet, M.2
  • 115
    • 84865804312 scopus 로고    scopus 로고
    • Metabolome 2.0: Quantitative genetics and network biology of metabolic phenotypes
    • Dumas ME. Metabolome 2.0: quantitative genetics and network biology of metabolic phenotypes. Mol.Biosyst. 8(10), 2494-2502 (2012).
    • (2012) Mol.Biosyst. , vol.8 , Issue.10 , pp. 2494-2502
    • Dumas, M.E.1
  • 116
    • 84890547928 scopus 로고    scopus 로고
    • A practical data processing workflow for multi-OMICS projects
    • doi:10.1016/j.bbapap.2013.02.029 Epub ahead of print
    • Kohl M, Megger DA, Trippler M et al. A practical data processing workflow for multi-OMICS projects. Biochim. Biophys. Acta doi:10.1016/j.bbapap.2013.02. 029 (2013) (Epub ahead of print).
    • (2013) Biochim. Biophys. Acta
    • Kohl, M.1    Megger, D.A.2    Trippler, M.3
  • 117
    • 84864818817 scopus 로고    scopus 로고
    • Revolutionizing medicine in the 21st century through systems approaches
    • Hood L, Balling R, Auffray C. Revolutionizing medicine in the 21st century through systems approaches. Biotechnol. J. 7(8), 992-1001 (2012).
    • (2012) Biotechnol. J. , vol.7 , Issue.8 , pp. 992-1001
    • Hood, L.1    Balling, R.2    Auffray, C.3
  • 118
    • 4644335402 scopus 로고    scopus 로고
    • Systems biology, proteomics, and the future of health care: Toward predictive, preventative, and personalized medicine
    • Weston AD, Hood L. Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine. J. Proteome. Res. 3(2), 179-196 (2004).
    • (2004) J. Proteome. Res. , vol.3 , Issue.2 , pp. 179-196
    • Weston, A.D.1    Hood, L.2
  • 120
    • 77952932817 scopus 로고    scopus 로고
    • Harnessing systems biology approaches to engineer functional microvascular networks
    • Sefcik LS, Wilson JL, Papin JA, Botchwey EA. Harnessing systems biology approaches to engineer functional microvascular networks. Tissue Eng. Part B Rev. 16(3), 361-370 (2010).
    • (2010) Tissue Eng. Part B Rev. , vol.16 , Issue.3 , pp. 361-370
    • Sefcik, L.S.1    Wilson, J.L.2    Papin, J.A.3    Botchwey, E.A.4
  • 121
    • 33645961885 scopus 로고    scopus 로고
    • Bioinformatics for cancer management in the post-genome era
    • Katoh M, Katoh M. Bioinformatics for cancer management in the post-genome era. Technol. Cancer Res. Treat. 5(2), 169-175 (2006).
    • (2006) Technol. Cancer Res. Treat. , vol.5 , Issue.2 , pp. 169-175
    • Katoh, M.1    Katoh, M.2
  • 122
    • 2342628481 scopus 로고    scopus 로고
    • Data standards for 'omic' science
    • Quackenbush J. Data standards for 'omic' science. Nat. Biotechnol. 22(5), 613-614 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , Issue.5 , pp. 613-614
    • Quackenbush, J.1
  • 123
    • 33344479181 scopus 로고    scopus 로고
    • Discovery and validation of new protein biomarkers for urothelial cancer: A prospective analysis
    • Theodorescu D, Wittke S, Ross MM et al. Discovery and validation of new protein biomarkers for urothelial cancer: a prospective analysis. Lancet Oncol. 7(3), 230-240 (2006).
    • (2006) Lancet Oncol. , vol.7 , Issue.3 , pp. 230-240
    • Theodorescu, D.1    Wittke, S.2    Ross, M.M.3
  • 124
    • 68049131450 scopus 로고    scopus 로고
    • Prediction of muscle-invasive bladder cancer using urinary proteomics
    • Schiffer E, Vlahou A, Petrolekas A et al. Prediction of muscle-invasive bladder cancer using urinary proteomics. Clin. Cancer Res. 15(15), 4935-4943 (2009).
    • (2009) Clin. Cancer Res. , vol.15 , Issue.15 , pp. 4935-4943
    • Schiffer, E.1    Vlahou, A.2    Petrolekas, A.3
  • 125
    • 80053647484 scopus 로고    scopus 로고
    • Assessment of high-throughput high-resolution MALDI-TOF-MS of urinary peptides for the detection of muscle-invasive bladder cancer
    • Bryan RT, Wei W, Shimwell NJ et al. Assessment of high-throughput high-resolution MALDI-TOF-MS of urinary peptides for the detection of muscle-invasive bladder cancer. Proteomics Clin. Appl. 5(9-10), 493-503 (2011).
    • (2011) Proteomics Clin. Appl. , vol.5 , Issue.9-10 , pp. 493-503
    • Bryan, R.T.1    Wei, W.2    Shimwell, N.J.3
  • 126
    • 23144461504 scopus 로고    scopus 로고
    • Pilot study of capillary electrophoresis coupled to mass spectrometry as a tool to define potential prostate cancer biomarkers in urine
    • Theodorescu D, Fliser D, Wittke S et al. Pilot study of capillary electrophoresis coupled to mass spectrometry as a tool to define potential prostate cancer biomarkers in urine. Electrophoresis 26(14), 2797-2808 (2005).
    • (2005) Electrophoresis , vol.26 , Issue.14 , pp. 2797-2808
    • Theodorescu, D.1    Fliser, D.2    Wittke, S.3
  • 127
  • 128
    • 42449130178 scopus 로고    scopus 로고
    • Discovery and validation of urinary biomarkers for prostate cancer
    • Theodorescu D, Schiffer E, Bauer HW et al. Discovery and validation of urinary biomarkers for prostate cancer. Proteomics. Clin. Appl. 2(4), 556-570 (2008).
    • (2008) Proteomics. Clin. Appl. , vol.2 , Issue.4 , pp. 556-570
    • Theodorescu, D.1    Schiffer, E.2    Bauer, H.W.3
  • 129
    • 84879224082 scopus 로고    scopus 로고
    • Molecular profiling of cholangiocarcinoma shows potential for targeted therapy treatment decisions
    • Voss JS, Holtegaard LM, Kerr SE et al. Molecular profiling of cholangiocarcinoma shows potential for targeted therapy treatment decisions. Hum. Pathol. 44(7), 1216-1222 (2013).
    • (2013) Hum. Pathol. , vol.44 , Issue.7 , pp. 1216-1222
    • Voss, J.S.1    Holtegaard, L.M.2    Kerr, S.E.3
  • 130
    • 84855415036 scopus 로고    scopus 로고
    • Proteomics analysis and evaluation of biomarkers for detection of cholangiocarcinoma
    • Sriwanitchrak P, Viyanant V, Chaijaroenkul W et al. Proteomics analysis and evaluation of biomarkers for detection of cholangiocarcinoma. Asian Pac. J. Cancer Prev. 12(6), 1503-1510 (2011).
    • (2011) Asian Pac. J. Cancer Prev. , vol.12 , Issue.6 , pp. 1503-1510
    • Sriwanitchrak, P.1    Viyanant, V.2    Chaijaroenkul, W.3
  • 131
    • 84862567956 scopus 로고    scopus 로고
    • Proteomics-based identification of alpha-enolase as a potential prognostic marker in cholangiocarcinoma
    • Yonglitthipagon P, Pairojkul C, Bhudhisawasdi V, Mulvenna J, Loukas A, Sripa B. Proteomics-based identification of alpha-enolase as a potential prognostic marker in cholangiocarcinoma. Clin. Biochem. 45(10-11), 827-834 (2012).
    • (2012) Clin. Biochem. , vol.45 , Issue.10-11 , pp. 827-834
    • Yonglitthipagon, P.1    Pairojkul, C.2    Bhudhisawasdi, V.3    Mulvenna, J.4    Loukas, A.5    Sripa, B.6
  • 132
    • 84871143909 scopus 로고    scopus 로고
    • Urine proteomic analysis differentiates cholangiocarcinoma from primary sclerosing cholangitis and other benign biliary disorders
    • Metzger J, Negm AA, Plentz RR et al. Urine proteomic analysis differentiates cholangiocarcinoma from primary sclerosing cholangitis and other benign biliary disorders. Gut 62(1), 122-130 (2013).
    • (2013) Gut , vol.62 , Issue.1 , pp. 122-130
    • Metzger, J.1    Negm, A.A.2    Plentz, R.R.3
  • 133
    • 45949095467 scopus 로고    scopus 로고
    • All-cause mortality attributable to chronic kidney disease: A prospective cohort study based on 462 293 adults in Taiwan
    • Wen CP, Cheng TY, Tsai MK et al. All-cause mortality attributable to chronic kidney disease: a prospective cohort study based on 462 293 adults in Taiwan. Lancet 371(9631), 2173-2182 (2008).
    • (2008) Lancet , vol.371 , Issue.9631 , pp. 2173-2182
    • Wen, C.P.1    Cheng, T.Y.2    Tsai, M.K.3
  • 134
    • 78149291420 scopus 로고    scopus 로고
    • Naturally occurring human urinary peptides for use in diagnosis of chronic kidney disease
    • Good DM, Zurbig P, Argiles A et al. Naturally occurring human urinary peptides for use in diagnosis of chronic kidney disease. Mol. Cell Proteomics. 9(11), 2424-2437 (2010).
    • (2010) Mol. Cell Proteomics , vol.9 , Issue.11 , pp. 2424-2437
    • Good, D.M.1    Zurbig, P.2    Argiles, A.3
  • 135
    • 62149085888 scopus 로고    scopus 로고
    • Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: A MALDI study
    • Lapolla A, Seraglia R, Molin L et al.Low molecular weight proteins in urines from healthy subjects as well as diabetic, nephropathic and diabetic-nephropathic patients: a MALDI study. J. Mass Spectrom. 44(3), 419-425 (2009).
    • (2009) J. Mass Spectrom. , vol.44 , Issue.3 , pp. 419-425
    • Lapolla, A.1    Seraglia, R.2    Molin, L.3
  • 136
    • 72449143576 scopus 로고    scopus 로고
    • A further investigation on a MALDI-based method for evaluation of markers of renal damage
    • Lapolla A, Molin L, Sechi A et al. A further investigation on a MALDI-based method for evaluation of markers of renal damage. J. Mass Spectrom. 44(12), 1754-1760 (2009).
    • (2009) J. Mass Spectrom. , vol.44 , Issue.12 , pp. 1754-1760
    • Lapolla, A.1    Molin, L.2    Sechi, A.3
  • 137
    • 84866492752 scopus 로고    scopus 로고
    • A comparison between MALDI-MS and CE-MS data for biomarker assessment in chronic kidney diseases
    • Molin L, Seraglia R, Lapolla A et al. A comparison between MALDI-MS and CE-MS data for biomarker assessment in chronic kidney diseases. J. Proteomics 75(18), 5888-5897 (2012).
    • (2012) J. Proteomics , vol.75 , Issue.18 , pp. 5888-5897
    • Molin, L.1    Seraglia, R.2    Lapolla, A.3
  • 138
    • 84925938529 scopus 로고    scopus 로고
    • Study of diabetic nephropathy in the proteomic era
    • Thongboonkerd V. Study of diabetic nephropathy in the proteomic era. Contrib.Nephrol. 170, 172-183 (2011).
    • (2011) Contrib.Nephrol , vol.170 , pp. 172-183
    • Thongboonkerd, V.1
  • 139
    • 21344467291 scopus 로고    scopus 로고
    • Identification of urinary protein pattern in Type 1 diabetic adolescents with early diabetic nephropathy by a novel combined proteome analysis
    • Meier M, Kaiser T, Herrmann A et al. Identification of urinary protein pattern in Type 1 diabetic adolescents with early diabetic nephropathy by a novel combined proteome analysis. J. Diabetes Complications 19(4), 223-232 (2005).
    • (2005) J. Diabetes Complications , vol.19 , Issue.4 , pp. 223-232
    • Meier, M.1    Kaiser, T.2    Herrmann, A.3
  • 140
    • 8644277000 scopus 로고    scopus 로고
    • Proteomic analysis for the assessment of diabetic renal damage in humans
    • (Lond)
    • Mischak H, Kaiser T, Walden M et al. Proteomic analysis for the assessment of diabetic renal damage in humans. Clin. Sci.(Lond) 107(5), 485-495 (2004).
    • (2004) Clin. Sci. , vol.107 , Issue.5 , pp. 485-495
    • Mischak, H.1    Kaiser, T.2    Walden, M.3
  • 141
    • 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. 19(7), 1283-1290 (2008).
    • (2008) J. Am. Soc. Nephrol. , vol.19 , Issue.7 , pp. 1283-1290
    • Rossing, K.1    Mischak, H.2    Dakna, M.3
  • 142
    • 78149479774 scopus 로고    scopus 로고
    • Multicentric validation of proteomic biomarkers in urine specific for diabetic nephropathy
    • Alkhalaf A, Zurbig P, Bakker SJ et al. Multicentric validation of proteomic biomarkers in urine specific for diabetic nephropathy. PLoS ONE 5(10), e13421 (2010).
    • (2010) PLoS ONE , vol.5 , Issue.10
    • Alkhalaf, A.1    Zurbig, P.2    Bakker, S.J.3
  • 143
    • 41149148161 scopus 로고    scopus 로고
    • Increased hepcidin expression in colorectal carcinogenesis
    • Ward DG, Roberts K, Brookes MJ et al. Increased hepcidin expression in colorectal carcinogenesis. World J. Gastroenterol. 14(9), 1339-1345 (2008).
    • (2008) World J. Gastroenterol. , vol.14 , Issue.9 , pp. 1339-1345
    • Ward, D.G.1    Roberts, K.2    Brookes, M.J.3
  • 144
    • 84870328390 scopus 로고    scopus 로고
    • Urinary proteomics for early diagnosis in diabetic nephropathy
    • Zurbig P, Jerums G, Hovind P et al. Urinary proteomics for early diagnosis in diabetic nephropathy. Diabetes 61(12), 3304-3313 (2012).
    • (2012) Diabetes , vol.61 , Issue.12 , pp. 3304-3313
    • Zurbig, P.1    Jerums, G.2    Hovind, P.3
  • 145
    • 84875597573 scopus 로고    scopus 로고
    • A urinary peptide biomarker set predicts worsening of albuminuria in Type 2 diabetes mellitus
    • Roscioni SS, de ZD, Hellemons ME et al. A urinary peptide biomarker set predicts worsening of albuminuria in Type 2 diabetes mellitus. Diabetologia 56(2), 259-267 (2013).
    • (2013) Diabetologia , vol.56 , Issue.2 , pp. 259-267
    • Roscioni, S.S.1    De Zd Hellemons, M.E.2
  • 146
    • 78649641356 scopus 로고    scopus 로고
    • Urinary excretion of twenty peptides forms an early and accurate diagnostic pattern of acute kidney injury
    • Metzger J, Kirsch T, Schiffer E et al. Urinary excretion of twenty peptides forms an early and accurate diagnostic pattern of acute kidney injury. Kidney Int. 78(12), 1252-1262 (2010).
    • (2010) Kidney Int. , vol.78 , Issue.12 , pp. 1252-1262
    • Metzger, J.1    Kirsch, T.2    Schiffer, E.3
  • 147
    • 84856521374 scopus 로고    scopus 로고
    • Urinary proteome analysis to exclude severe vesicoureteral reflux
    • Drube J, Schiffer E, Lau E et al. Urinary proteome analysis to exclude severe vesicoureteral reflux. Pediatrics 129(2), e356-e363 (2012).
    • (2012) Pediatrics , vol.129 , Issue.2
    • Drube, J.1    Schiffer, E.2    Lau, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.