메뉴 건너뛰기




Volumn 85, Issue 1, 2012, Pages 59-73

Mass spectrometry-based proteomics for translational research: A technical overview

Author keywords

Biomarkers; Chronic pancreatitis; Mass spectrometry; Pancreas

Indexed keywords

BIOLOGICAL MARKER;

EID: 84859301166     PISSN: 00440086     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (27)

References (101)
  • 1
    • 0031398974 scopus 로고    scopus 로고
    • Protein identification in the postgenome era: The rapid rise of proteomics
    • James P. Protein identification in the postgenome era: the rapid rise of proteomics. Q Rev Biophys. 1997;30(4):279-331.
    • (1997) Q Rev Biophys , vol.30 , Issue.4 , pp. 279-331
    • James, P.1
  • 3
    • 0036603768 scopus 로고    scopus 로고
    • Alternative splicing: Combinatorial output from the genome
    • Roberts GC, Smith CW. Alternative splicing: combinatorial output from the genome. Curr Opin Chem Biol. 2002;6(3):375-83.
    • (2002) Curr Opin Chem Biol , vol.6 , Issue.3 , pp. 375-383
    • Roberts, G.C.1    Smith, C.W.2
  • 4
    • 0033546122 scopus 로고    scopus 로고
    • Highthroughput mass spectrometric discovery of protein post-translational modifications
    • Wilkins MR, Gasteiger E, Gooley AA, Herbert BR, Molloy MP, Binz PA, et al. Highthroughput mass spectrometric discovery of protein post-translational modifications. J Mol Biol. 1999;289(3):645-57.
    • (1999) J Mol Biol , vol.289 , Issue.3 , pp. 645-657
    • Wilkins, M.R.1    Gasteiger, E.2    Gooley, A.A.3    Herbert, B.R.4    Molloy, M.P.5    Binz, P.A.6
  • 6
    • 0033455550 scopus 로고    scopus 로고
    • Separation of human cerebrospinal fluid proteins by capillary isoelectric focusing in the absence of denaturing agents
    • Manabe T, Miyamoto H, Inoue K, Nakatsu M, Arai M. Separation of human cerebrospinal fluid proteins by capillary isoelectric focusing in the absence of denaturing agents. Electrophoresis. 1999;20(18):3677-83.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3677-3683
    • Manabe, T.1    Miyamoto, H.2    Inoue, K.3    Nakatsu, M.4    Arai, M.5
  • 8
    • 0345550275 scopus 로고    scopus 로고
    • Comparison of protein precipitation methods for sample preparation prior to proteomic analysis
    • Jiang L, He L, Fountoulakis M. Comparison of protein precipitation methods for sample preparation prior to proteomic analysis. J Chromatogr A. 2004;1023(2):317-20.
    • (2004) J Chromatogr A , vol.1023 , Issue.2 , pp. 317-320
    • Jiang, L.1    He, L.2    Fountoulakis, M.3
  • 9
    • 0036379687 scopus 로고    scopus 로고
    • Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation
    • Thongboonkerd V, McLeish KR, Arthur JM, Klein JB. Proteomic analysis of normal human urinary proteins isolated by acetone precipitation or ultracentrifugation. Kidney Int. 2002;62(4):1461-9.
    • (2002) Kidney Int , vol.62 , Issue.4 , pp. 1461-1469
    • Thongboonkerd, V.1    McLeish, K.R.2    Arthur, J.M.3    Klein, J.B.4
  • 10
    • 0033571082 scopus 로고    scopus 로고
    • Isolation and characterization of hydrophobic polypeptides in human bile
    • Stark M, Jornvall H, Johansson J. Isolation and characterization of hydrophobic polypeptides in human bile. Eur J Biochem. 1999;266(1):209-14.
    • (1999) Eur J Biochem , vol.266 , Issue.1 , pp. 209-214
    • Stark, M.1    Jornvall, H.2    Johansson, J.3
  • 11
    • 0020687017 scopus 로고
    • Staining of proteins on gels: Comparisons of dyes and procedures
    • Wilson CM. Staining of proteins on gels: comparisons of dyes and procedures. Methods Enzymol. 1983;91:236-47.
    • (1983) Methods Enzymol , vol.91 , pp. 236-247
    • Wilson, C.M.1
  • 12
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver- stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins silver- stained polyacrylamide gels. Anal Chem. 1996;68(5):850-8.
    • (1996) Anal Chem , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 13
    • 0033667456 scopus 로고    scopus 로고
    • A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling
    • Lopez MF, Berggren K, Chernokalskaya E, Lazarev A, Robinson M, Patton WF. A comparison of silver stain and SYPRO Ruby Protein Gel Stain with respect to protein detection in two-dimensional gels and identification by peptide mass profiling. Electrophoresis. 2000;21(17):3673-83.
    • (2000) Electrophoresis , vol.21 , Issue.17 , pp. 3673-3683
    • Lopez, M.F.1    Berggren, K.2    Chernokalskaya, E.3    Lazarev, A.4    Robinson, M.5    Patton, W.F.6
  • 14
    • 3242773844 scopus 로고    scopus 로고
    • Proteomic capacity of recent fluorescent dyes for protein staining
    • Chevalier F, Rofidal V, Vanova P, Bergoin A, Rossignol M. Proteomic capacity of recent fluorescent dyes for protein staining. Phytochemistry. 2004;65(11):1499-506.
    • (2004) Phytochemistry , vol.65 , Issue.11 , pp. 1499-1506
    • Chevalier, F.1    Rofidal, V.2    Vanova, P.3    Bergoin, A.4    Rossignol, M.5
  • 15
    • 33748571491 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry
    • Wittmann-Liebold B, Graack HR, Pohl T. Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry. Proteomics. 2006;6(17):4688-703.
    • (2006) Proteomics , vol.6 , Issue.17 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 17
    • 17144362794 scopus 로고    scopus 로고
    • Two-stage Off-Gel isoelectric focusing: Protein followed by peptide fractionation and application to proteome analysis of human plasma
    • Heller M, Michel PE, Morier P, Crettaz D, Wenz C, Tissot JD, et al. Two-stage Off-Gel isoelectric focusing: protein followed by peptide fractionation and application to proteome analysis of human plasma. Electrophoresis. 2005;26(6):1174-88.
    • (2005) Electrophoresis , vol.26 , Issue.6 , pp. 1174-1188
    • Heller, M.1    Michel, P.E.2    Morier, P.3    Crettaz, D.4    Wenz, C.5    Tissot, J.D.6
  • 18
    • 39749166988 scopus 로고    scopus 로고
    • Capillary electrophoresis of proteins and peptides
    • Chapter 10:Unit 10
    • Burgi D, Smith AJ. Capillary electrophoresis of proteins and peptides. Curr Protoc Protein Sci. 2001;Chapter 10:Unit 10.9.
    • (2001) Curr Protoc Protein Sci , pp. 9
    • Burgi, D.1    Smith, A.J.2
  • 19
    • 42649090169 scopus 로고    scopus 로고
    • Rapid capillary electrophoresis time-of-flight mass spectrometry separations of peptides and proteins using a monoquaternarized piperazine compound (M7C4I) for capillary coatings
    • Elhamili A, Wetterhall M, Arvidsson B, Sebastiano R, Righetti PG, Bergquist J. Rapid capillary electrophoresis time-of-flight mass spectrometry separations of peptides and proteins using a monoquaternarized piperazine compound (M7C4I) for capillary coatings. Electrophoresis. 2008;29(8):1619-25.
    • (2008) Electrophoresis , vol.29 , Issue.8 , pp. 1619-1625
    • Elhamili, A.1    Wetterhall, M.2    Arvidsson, B.3    Sebastiano, R.4    Righetti, P.G.5    Bergquist, J.6
  • 20
    • 12944322218 scopus 로고    scopus 로고
    • On-line multidimensional liquid chromatography and capillary electrophoresis systems for peptides and proteins
    • Stroink T, Ortiz MC, Bult A, Lingeman H, de Jong GJ, Underberg WJ. On-line multidimensional liquid chromatography and capillary electrophoresis systems for peptides and proteins. J Chromatogr A. 2005;817(1):49-66.
    • (2005) J Chromatogr A , vol.817 , Issue.1 , pp. 49-66
    • Stroink, T.1    Ortiz, M.C.2    Bult, A.3    Lingeman, H.4    de Jong, G.J.5    Underberg, W.J.6
  • 21
    • 0023083636 scopus 로고
    • Isoelectric focusing in immobilized pH gradients: Theory and newer methodology
    • Righetti PG, Gianazza E. Isoelectric focusing in immobilized pH gradients: theory and newer methodology. Methods Biochem Anal. 1987;32:215-78.
    • (1987) Methods Biochem Anal , vol.32 , pp. 215-278
    • Righetti, P.G.1    Gianazza, E.2
  • 22
    • 34247627759 scopus 로고    scopus 로고
    • Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling
    • Tannu NS, Hemby SE. Two-dimensional fluorescence difference gel electrophoresis for comparative proteomics profiling. Nat Protoc. 2006;1(4):1732-42.
    • (2006) Nat Protoc , vol.1 , Issue.4 , pp. 1732-1742
    • Tannu, N.S.1    Hemby, S.E.2
  • 23
    • 0037337308 scopus 로고    scopus 로고
    • The application of mass spectrometry to membrane proteomics
    • Wu CC, Yates JR, 3rd. The application of mass spectrometry to membrane proteomics. Nat Biotechnol. 2003;21(3):262-7.
    • (2003) Nat Biotechnol , vol.21 , Issue.3 , pp. 262-267
    • Wu, C.C.1    Yates III, J.R.2
  • 24
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • Molloy MP, Brzezinski EE, Hang J, McDowell MT, VanBogelen RA. Overcoming technical variation and biological variation in quantitative proteomics. Proteomics. 2003;3(10):1912-9.
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.3    McDowell, M.T.4    Vanbogelen, R.A.5
  • 25
    • 27744583045 scopus 로고    scopus 로고
    • All about DIGE: Quantification technology for differential-display 2D-gel proteomics
    • Lilley KS, Friedman DB. All about DIGE: quantification technology for differential-display 2D-gel proteomics. Expert Rev Proteomics. 2004;1(4):401-9.
    • (2004) Expert Rev Proteomics , vol.1 , Issue.4 , pp. 401-409
    • Lilley, K.S.1    Friedman, D.B.2
  • 26
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS. Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis. 1997;18(11):2071-7.
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 30
    • 0024537204 scopus 로고
    • Cyanine dye labeling reagents containing isothiocyanate groups
    • Mujumdar RB, Ernst LA, Mujumdar SR, Waggoner AS. Cyanine dye labeling reagents containing isothiocyanate groups. Cytometry. 1989;10(1):11-9.
    • (1989) Cytometry , vol.10 , Issue.1 , pp. 11-19
    • Mujumdar, R.B.1    Ernst, L.A.2    Mujumdar, S.R.3    Waggoner, A.S.4
  • 32
    • 0017163433 scopus 로고
    • Reverse-phase chromatography of polar biological substances: Separation of catechol compounds by highperformance liquid chromatography
    • Molnar I, Horvath C. Reverse-phase chromatography of polar biological substances: separation of catechol compounds by highperformance liquid chromatography. Clin Chem. 1976;22(9):1497-502.
    • (1976) Clin Chem , vol.22 , Issue.9 , pp. 1497-1502
    • Molnar, I.1    Horvath, C.2
  • 34
    • 33748919316 scopus 로고
    • Gel filtration: A method for desalting and group separation
    • Porath J, Flodin P. Gel filtration: a method for desalting and group separation. Nature. 1959;183(4676):1657-9.
    • (1959) Nature , vol.183 , Issue.4676 , pp. 1657-1659
    • Porath, J.1    Flodin, P.2
  • 36
    • 36749004371 scopus 로고    scopus 로고
    • Top-down MS, a powerful complement to the high capabilities of proteolysis proteomics
    • McLafferty FW, Breuker K, Jin M, Han X, Infusini G, Jiang H, et al. Top-down MS, a powerful complement to the high capabilities of proteolysis proteomics. FEBS J. 2007;274(24):6256-68.
    • (2007) FEBS J , vol.274 , Issue.24 , pp. 6256-6268
    • McLafferty, F.W.1    Breuker, K.2    Jin, M.3    Han, X.4    Infusini, G.5    Jiang, H.6
  • 37
    • 34249302758 scopus 로고    scopus 로고
    • Emerging methods in proteomics: Top-down protein characterization by multistage tandem mass spectrometry
    • Scherperel G, Reid GE. Emerging methods in proteomics: top-down protein characterization by multistage tandem mass spectrometry. Analyst. 2007;132(6):500-6.
    • (2007) Analyst , vol.132 , Issue.6 , pp. 500-506
    • Scherperel, G.1    Reid, G.E.2
  • 38
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • Kelleher NL. Top-down proteomics. Anal Chem. 2004;76(11):197A-203A.
    • (2004) Anal Chem , vol.76 , Issue.11
    • Kelleher, N.L.1
  • 39
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, Olsen JV, Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc. 2006;1(6):2856-60.
    • (2006) Nat Protoc , vol.1 , Issue.6 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 40
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to arginine and lysine residues
    • Olsen JV, Ong SE, Mann M. Trypsin cleaves exclusively C-terminal to arginine and lysine residues. Mol Cell Proteomics. 2004;3(6):608-14.
    • (2004) Mol Cell Proteomics , vol.3 , Issue.6 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 41
    • 0036127937 scopus 로고    scopus 로고
    • Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix- assisted laser desorption/ionization timeof- flight mass spectrometry
    • van Montfort BA, Canas B, Duurkens R, Godovac-Zimmermann J, Robillard GT. Improved in-gel approaches to generate peptide maps of integral membrane proteins with matrix- assisted laser desorption/ionization timeof- flight mass spectrometry. J Mass Spectrom. 2002;37(3):322-30.
    • (2002) J Mass Spectrom , vol.37 , Issue.3 , pp. 322-330
    • van Montfort, B.A.1    Canas, B.2    Duurkens, R.3    Godovac-Zimmermann, J.4    Robillard, G.T.5
  • 42
    • 0028817274 scopus 로고
    • Internal sequences from proteins digested in polyacrylamide gels
    • Jeno P, Mini T, Moes S, Hintermann E, Horst M. Internal sequences from proteins digested in polyacrylamide gels. Anal Biochem. 1995;224(1):75-82.
    • (1995) Anal Biochem , vol.224 , Issue.1 , pp. 75-82
    • Jeno, P.1    Mini, T.2    Moes, S.3    Hintermann, E.4    Horst, M.5
  • 43
    • 25144508697 scopus 로고    scopus 로고
    • A new approach in proteomics of wheat gluten: Combining chymotrypsin cleavage and matrix-assisted laser desorption/ ionization quadrupole ion trap reflectron tandem mass spectrometry
    • Salplachta J, Marchetti M, Chmelik J, Allmaier G. A new approach in proteomics of wheat gluten: combining chymotrypsin cleavage and matrix-assisted laser desorption/ ionization quadrupole ion trap reflectron tandem mass spectrometry. Rapid Commun Mass Spectrom. 2005;19(18):2725-8.
    • (2005) Rapid Commun Mass Spectrom , vol.19 , Issue.18 , pp. 2725-2728
    • Salplachta, J.1    Marchetti, M.2    Chmelik, J.3    Allmaier, G.4
  • 44
    • 0023867452 scopus 로고
    • Structural characterization of recombinant hepatitis B surface antigen protein by mass spectrometry
    • Hemling ME, Carr SA, Capiau C, Petre J. Structural characterization of recombinant hepatitis B surface antigen protein by mass spectrometry. Biochemistry. 1988;27(2):699-705.
    • (1988) Biochemistry , vol.27 , Issue.2 , pp. 699-705
    • Hemling, M.E.1    Carr, S.A.2    Capiau, C.3    Petre, J.4
  • 45
    • 70949086044 scopus 로고    scopus 로고
    • Comparative analysis of OFFGel, strong cation exchange with pH gradient, and RP at high pH for first-dimensional separation of peptides from a membrane-enriched protein fraction
    • Manadas B, English JA, Wynne KJ, Cotter DR, Dunn MJ. Comparative analysis of OFFGel, strong cation exchange with pH gradient, and RP at high pH for first-dimensional separation of peptides from a membrane-enriched protein fraction. Proteomics. 2009;9(22):5194-8.
    • (2009) Proteomics , vol.9 , Issue.22 , pp. 5194-5198
    • Manadas, B.1    English, J.A.2    Wynne, K.J.3    Cotter, D.R.4    Dunn, M.J.5
  • 46
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for largescale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for largescale protein analysis: the yeast proteome. J Proteome Res. 2003;2(1):43-50.
    • (2003) J Proteome Res , vol.2 , Issue.1 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 47
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D, Yates JR, 3rd. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol. 2001;19(3):242-7.
    • (2001) Nat Biotechnol , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 48
    • 71549117585 scopus 로고    scopus 로고
    • Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome
    • Wisniewski JR, Zougman A, Mann M. Combination of FASP and StageTip-based fractionation allows in-depth analysis of the hippocampal membrane proteome. J Proteome Res. 2009;8(12):5674-8.
    • (2009) J Proteome Res , vol.8 , Issue.12 , pp. 5674-5678
    • Wisniewski, J.R.1    Zougman, A.2    Mann, M.3
  • 49
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski JR, Zougman A, Nagaraj N, Mann M. Universal sample preparation method for proteome analysis. Nature Methods. 2009;6(5):359-62.
    • (2009) Nature Methods , vol.6 , Issue.5 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 50
    • 36348936820 scopus 로고    scopus 로고
    • Two-dimensional reversedphase x ion-pair reversed-phase HPLC: An alternative approach to high-resolution peptide separation for shotgun proteome analysis
    • Delmotte N, Lasaosa M, Tholey A, Heinzle E, Huber CG. Two-dimensional reversedphase x ion-pair reversed-phase HPLC: an alternative approach to high-resolution peptide separation for shotgun proteome analysis. J Proteome Res. 2007;6(11):4363-73.
    • (2007) J Proteome Res , vol.6 , Issue.11 , pp. 4363-4373
    • Delmotte, N.1    Lasaosa, M.2    Tholey, A.3    Heinzle, E.4    Huber, C.G.5
  • 51
    • 51949083217 scopus 로고    scopus 로고
    • Practical implementation of 2D HPLC scheme with accurate peptide retention prediction in both dimensions for high-throughput bottom-up proteomics
    • Dwivedi RC, Spicer V, Harder M, Antonovici M, Ens W, Standing KG, et al. Practical implementation of 2D HPLC scheme with accurate peptide retention prediction in both dimensions for high-throughput bottom-up proteomics. Anal Chem. 2008;80(18):7036-42.
    • (2008) Anal Chem , vol.80 , Issue.18 , pp. 7036-7042
    • Dwivedi, R.C.1    Spicer, V.2    Harder, M.3    Antonovici, M.4    Ens, W.5    Standing, K.G.6
  • 52
    • 70349974833 scopus 로고    scopus 로고
    • Peptide separations by on-line MudPIT compared to isoelectric focusing in an off-gel format: Application to a membrane-enriched fraction from C2C12 mouse skeletal muscle cells
    • Elschenbroich S, Ignatchenko V, Sharma P, Schmitt-Ulms G, Gramolini AO, Kislinger T. Peptide separations by on-line MudPIT compared to isoelectric focusing in an off-gel format: application to a membrane-enriched fraction from C2C12 mouse skeletal muscle cells. J Proteome Res. 2009;8(10):4860-9.
    • (2009) J Proteome Res , vol.8 , Issue.10 , pp. 4860-4869
    • Elschenbroich, S.1    Ignatchenko, V.2    Sharma, P.3    Schmitt-Ulms, G.4    Gramolini, A.O.5    Kislinger, T.6
  • 53
    • 0036684101 scopus 로고    scopus 로고
    • Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: Single- dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT
    • McDonald WH, Ohi R, Miyamoto DT, Mitchison TJ, Yates JR. Comparison of three directly coupled HPLC MS/MS strategies for identification of proteins from complex mixtures: single- dimension LC-MS/MS, 2-phase MudPIT, and 3-phase MudPIT. International Journal of Mass Spectrometry. 2002;219(1):245-51.
    • (2002) International Journal of Mass Spectrometry , vol.219 , Issue.1 , pp. 245-251
    • McDonald, W.H.1    Ohi, R.2    Miyamoto, D.T.3    Mitchison, T.J.4    Yates, J.R.5
  • 54
    • 54749158155 scopus 로고    scopus 로고
    • Multidimensional LC separations in shotgun proteomics
    • Motoyama A, Yates JR, 3rd. Multidimensional LC separations in shotgun proteomics. Anal Chem. 2008;80(19):7187-93.
    • (2008) Anal Chem , vol.80 , Issue.19 , pp. 7187-7193
    • Motoyama, A.1    Yates 3rd., J.R.2
  • 55
    • 0037317228 scopus 로고    scopus 로고
    • Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics
    • Rappsilber J, Ishihama Y, Mann M. Stop and go extraction tips for matrix-assisted laser desorption/ionization, nanoelectrospray, and LC/MS sample pretreatment in proteomics. Anal Chem. 2003;75(3):663-70.
    • (2003) Anal Chem , vol.75 , Issue.3 , pp. 663-670
    • Rappsilber, J.1    Ishihama, Y.2    Mann, M.3
  • 56
    • 1542302553 scopus 로고    scopus 로고
    • Fractionation of peptides in proteomics with the use of pI-based approach and ZipTip pipette tips
    • Baczek T. Fractionation of peptides in proteomics with the use of pI-based approach and ZipTip pipette tips. J Pharm Biomed Anal. 2004;34(5):851-60.
    • (2004) J Pharm Biomed Anal , vol.34 , Issue.5 , pp. 851-860
    • Baczek, T.1
  • 57
    • 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, Kristensen DB, Steen H, Pandey A, 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(5):376-86.
    • (2002) Mol Cell Proteomics , vol.1 , Issue.5 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 59
    • 12444345515 scopus 로고    scopus 로고
    • Tandem mass tags: A novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS
    • Thompson A, Schafer J, Kuhn K, Kienle S, Schwarz J, Schmidt G, et al. Tandem mass tags: a novel quantification strategy for comparative analysis of complex protein mixtures by MS/MS. Anal Chem. 2003;75(8):1895-904.
    • (2003) Anal Chem , vol.75 , Issue.8 , pp. 1895-1904
    • Thompson, A.1    Schafer, J.2    Kuhn, K.3    Kienle, S.4    Schwarz, J.5    Schmidt, G.6
  • 60
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross PL, Huang YN, Marchese JN, Williamson B, Parker K, Hattan S, et al. Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol Cell Proteomics. 2004;3(12):1154-69.
    • (2004) Mol Cell Proteomics , vol.3 , Issue.12 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4    Parker, K.5    Hattan, S.6
  • 61
    • 34250379924 scopus 로고    scopus 로고
    • The absolute quantification strategy: Application to phosphorylation profiling of human separase serine 1126
    • Gerber SA, Kettenbach AN, Rush J, Gygi SP. The absolute quantification strategy: application to phosphorylation profiling of human separase serine 1126. Methods Mol Biol. 2007;359:71-86.
    • (2007) Methods Mol Biol , vol.359 , pp. 71-86
    • Gerber, S.A.1    Kettenbach, A.N.2    Rush, J.3    Gygi, S.P.4
  • 62
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick DS, Gerber SA, Gygi SP. The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods. 2005;35(3):265-73.
    • (2005) Methods , vol.35 , Issue.3 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 63
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP. Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA. 2003;100(12):6940-5.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.12 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 65
    • 0032835756 scopus 로고    scopus 로고
    • Optimization of an ion-to-photon detector for large molecules in mass spectrometry
    • Dubois F, Knochenmuss R, Zenobi R. Optimization of an ion-to-photon detector for large molecules in mass spectrometry. Rapid Commun Mass Spectrom. 1999;13(19):1958-67.
    • (1999) Rapid Commun Mass Spectrom , vol.13 , Issue.19 , pp. 1958-1967
    • Dubois, F.1    Knochenmuss, R.2    Zenobi, R.3
  • 66
    • 4444335470 scopus 로고    scopus 로고
    • The ABC's (and XYZ's) of peptide sequencing
    • Steen H, Mann M. The ABC's (and XYZ's) of peptide sequencing. Nat Rev Mol Cell Biol. 2004;5(9):699-711.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.9 , pp. 699-711
    • Steen, H.1    Mann, M.2
  • 67
    • 29244448703 scopus 로고    scopus 로고
    • Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap
    • Olsen JV, de Godoy LM, Li G, Macek B, Mortensen P, Pesch R, et al. Parts per million mass accuracy on an Orbitrap mass spectrometer via lock mass injection into a C-trap. Mol Cell Proteomics. 2005;4(12):2010-21.
    • (2005) Mol Cell Proteomics , vol.4 , Issue.12 , pp. 2010-2021
    • Olsen, J.V.1    de Godoy, L.M.2    Li, G.3    Macek, B.4    Mortensen, P.5    Pesch, R.6
  • 68
    • 0035241690 scopus 로고    scopus 로고
    • Mass spectrometry in proteomics
    • Aebersold R, Goodlett DR. Mass spectrometry in proteomics. Chem Rev. 2001;101(2):269-95.
    • (2001) Chem Rev , vol.101 , Issue.2 , pp. 269-295
    • Aebersold, R.1    Goodlett, D.R.2
  • 69
    • 33750319346 scopus 로고    scopus 로고
    • Orbitrap mass analyzer - overview and applications in proteomics
    • Scigelova M, Makarov A. Orbitrap mass analyzer - overview and applications in proteomics. Proteomics. 2006;6(Suppl 2):16-21.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 2 , pp. 16-21
    • Scigelova, M.1    Makarov, A.2
  • 71
    • 0000857494 scopus 로고
    • An Approach to Correlate Tandem Mass-Spectral Data of Peptides with Amino-Acid-Sequences in a Protein Database
    • Eng JK, Mccormack AL, Yates JR. An Approach to Correlate Tandem Mass-Spectral Data of Peptides with Amino-Acid-Sequences in a Protein Database. J Am Soc Mass Spectrom. 1994;5(11):976-89.
    • (1994) J Am Soc Mass Spectrom , vol.5 , Issue.11 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 72
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJC, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis. 1999;20(18):3551-67.
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 73
    • 0041358793 scopus 로고    scopus 로고
    • OLAV: Towards high-throughput tandem mass spectrometry data identification
    • Colinge J, Masselot A, Giron M, Dessingy T, Magnin J. OLAV: towards high-throughput tandem mass spectrometry data identification. Proteomics. 2003;3(8):1454-63.
    • (2003) Proteomics , vol.3 , Issue.8 , pp. 1454-1463
    • Colinge, J.1    Masselot, A.2    Giron, M.3    Dessingy, T.4    Magnin, J.5
  • 74
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov IV, Seymour SL, Patel AA, Loboda A, Tang WH, Keating SP, et al. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics. 2007;6(9):1638-55.
    • (2007) Mol Cell Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 75
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: Matching proteins with tandem mass spectra
    • Craig R, Beavis RC. TANDEM: matching proteins with tandem mass spectra. Bioinformatics. 2004;20(9):1466-7.
    • (2004) Bioinformatics , vol.20 , Issue.9 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 76
    • 0033565832 scopus 로고    scopus 로고
    • Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching
    • Clauser KR, Baker P, Burlingame AL. Role of accurate mass measurement (+/- 10 ppm) in protein identification strategies employing MS or MS/MS and database searching. Anal Chem. 1999;71(14):2871-82.
    • (1999) Anal Chem , vol.71 , Issue.14 , pp. 2871-2882
    • Clauser, K.R.1    Baker, P.2    Burlingame, A.L.3
  • 77
    • 38649090064 scopus 로고    scopus 로고
    • False discovery rates and related statistical concepts in mass spectrometry- based proteomics
    • Choi H, Nesvizhskii AI. False discovery rates and related statistical concepts in mass spectrometry- based proteomics. J Proteome Res. 2008;7(1):47-50.
    • (2008) J Proteome Res , vol.7 , Issue.1 , pp. 47-50
    • Choi, H.1    Nesvizhskii, A.I.2
  • 78
    • 38649083118 scopus 로고    scopus 로고
    • Assigning significance to peptides identified by tandem mass spectrometry using decoy databases
    • Kall L, Storey JD, MacCoss MJ, Noble WS. Assigning significance to peptides identified by tandem mass spectrometry using decoy databases. J Proteome Res. 2008;7(1):29-34.
    • (2008) J Proteome Res , vol.7 , Issue.1 , pp. 29-34
    • Kall, L.1    Storey, J.D.2    Maccoss, M.J.3    Noble, W.S.4
  • 79
    • 77953016667 scopus 로고    scopus 로고
    • Estimating the confidence of peptide identifications without decoy databases
    • Renard BY, Timm W, Kirchner M, Steen JA, Hamprecht FA, Steen H. Estimating the confidence of peptide identifications without decoy databases. Anal Chem. 2010;82(11):4314-8.
    • (2010) Anal Chem , vol.82 , Issue.11 , pp. 4314-4318
    • Renard, B.Y.1    Timm, W.2    Kirchner, M.3    Steen, J.A.4    Hamprecht, F.A.5    Steen, H.6
  • 80
    • 77449146854 scopus 로고    scopus 로고
    • Target-decoy search strategy for mass spectrometry-based proteomics
    • Elias JE, Gygi SP. Target-decoy search strategy for mass spectrometry-based proteomics. Methods Mol Biol. 2010;604:55-71.
    • (2010) Methods Mol Biol , vol.604 , pp. 55-71
    • Elias, J.E.1    Gygi, S.P.2
  • 81
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE, Gygi SP. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods. 2007;4(3):207-14.
    • (2007) Nat Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 82
    • 79953123184 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics of endoscopically collected pancreatic fluid in chronic pancreatitis research
    • Paulo JA, Lee LS, Wu B, Banks PA, Steen H, Conwell DL. Mass spectrometry-based proteomics of endoscopically collected pancreatic fluid in chronic pancreatitis research. Proteomics Clin Appl. 2011;5(3-4):109-20.
    • (2011) Proteomics Clin Appl , vol.5 , Issue.3-4 , pp. 109-120
    • Paulo, J.A.1    Lee, L.S.2    Wu, B.3    Banks, P.A.4    Steen, H.5    Conwell, D.L.6
  • 85
    • 77955186669 scopus 로고    scopus 로고
    • Identification of pancreas- specific proteins in endoscopically (endoscopic pancreatic function test) collected pancreatic fluid with liquid chromatographytandem mass spectrometry
    • Paulo JA, Lee LS, Wu B, Repas K, Mortele KJ, Banks PA, et al. Identification of pancreas- specific proteins in endoscopically (endoscopic pancreatic function test) collected pancreatic fluid with liquid chromatographytandem mass spectrometry. Pancreas. 2010;39(6):889-96.
    • (2010) Pancreas , vol.39 , Issue.6 , pp. 889-896
    • Paulo, J.A.1    Lee, L.S.2    Wu, B.3    Repas, K.4    Mortele, K.J.5    Banks, P.A.6
  • 86
    • 77954713265 scopus 로고    scopus 로고
    • Optimized sample preparation of endoscopic collected pancreatic fluid for SDS-PAGE analysis
    • Paulo JA, Lee LS, Wu B, Repas K, Banks PA, Conwell DL, et al. Optimized sample preparation of endoscopic collected pancreatic fluid for SDS-PAGE analysis. Electrophoresis. 2010;31(14):2377-87.
    • (2010) Electrophoresis , vol.31 , Issue.14 , pp. 2377-2387
    • Paulo, J.A.1    Lee, L.S.2    Wu, B.3    Repas, K.4    Banks, P.A.5    Conwell, D.L.6
  • 87
    • 78650477405 scopus 로고    scopus 로고
    • Proteomic analysis of endoscopically (endoscopic pancreatic function test) collected gastroduodenal fluid using in-gel tryptic digestion followed by LCMS/ MS
    • Paulo JA, Lee LS, Wu B, Repas K, Banks PA, Conwell DL, et al. Proteomic analysis of endoscopically (endoscopic pancreatic function test) collected gastroduodenal fluid using in-gel tryptic digestion followed by LCMS/ MS. Proteomics Clin Appl. 2010;4(8- 9):715-25.
    • (2010) Proteomics Clin Appl , vol.4 , Issue.8-9 , pp. 715-725
    • Paulo, J.A.1    Lee, L.S.2    Wu, B.3    Repas, K.4    Banks, P.A.5    Conwell, D.L.6
  • 88
    • 79960713878 scopus 로고    scopus 로고
    • Difference gel electrophoresis identifies differentially expressed proteins in endoscopically collected pancreatic fluid
    • Paulo JA, Lee LS, Banks PA, Steen H, Conwell DL. Difference gel electrophoresis identifies differentially expressed proteins in endoscopically collected pancreatic fluid. Electrophoresis. 2011;32(15):1939-51.
    • (2011) Electrophoresis , vol.32 , Issue.15 , pp. 1939-1951
    • Paulo, J.A.1    Lee, L.S.2    Banks, P.A.3    Steen, H.4    Conwell, D.L.5
  • 89
    • 80053923393 scopus 로고    scopus 로고
    • Proteomic Analysis of an Immortalized Mouse Pancreatic Stellate Cell Line Identifies Differentially-Expressed Proteins in Activated vs Nonproliferating Cell States
    • Paulo JA, Urrutia R, Banks PA, Conwell DL, Steen H. Proteomic Analysis of an Immortalized Mouse Pancreatic Stellate Cell Line Identifies Differentially-Expressed Proteins in Activated vs Nonproliferating Cell States. J Proteome Res. 2011;10(10):4835-44.
    • (2011) J Proteome Res , vol.10 , Issue.10 , pp. 4835-4844
    • Paulo, J.A.1    Urrutia, R.2    Banks, P.A.3    Conwell, D.L.4    Steen, H.5
  • 91
    • 0037114993 scopus 로고    scopus 로고
    • Proteolysis during the isoelectric focusing step of two-dimensional gel electrophoresis may be a common problem
    • Finnie C, Svensson B. Proteolysis during the isoelectric focusing step of two-dimensional gel electrophoresis may be a common problem. Anal Biochem. 2002;311(2):182-6.
    • (2002) Anal Biochem , vol.311 , Issue.2 , pp. 182-186
    • Finnie, C.1    Svensson, B.2
  • 92
    • 23944520883 scopus 로고    scopus 로고
    • HUPO Plasma Proteome Project specimen collection and handling: Towards the standardization of parameters for plasma proteome samples
    • Rai AJ, Gelfand CA, Haywood BC, Warunek DJ, Yi J, Schuchard MD, et al. HUPO Plasma Proteome Project specimen collection and handling: towards the standardization of parameters for plasma proteome samples. Proteomics. 2005;5(13):3262-77.
    • (2005) Proteomics , vol.5 , Issue.13 , pp. 3262-3277
    • Rai, A.J.1    Gelfand, C.A.2    Haywood, B.C.3    Warunek, D.J.4    Yi, J.5    Schuchard, M.D.6
  • 93
    • 12444330378 scopus 로고    scopus 로고
    • Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction
    • Marshall J, Kupchak P, Zhu W, Yantha J, Vrees T, Furesz S, et al. Processing of serum proteins underlies the mass spectral fingerprinting of myocardial infarction. J Proteome Res. 2003;2(4):361-72.
    • (2003) J Proteome Res , vol.2 , Issue.4 , pp. 361-372
    • Marshall, J.1    Kupchak, P.2    Zhu, W.3    Yantha, J.4    Vrees, T.5    Furesz, S.6
  • 94
    • 63849290925 scopus 로고    scopus 로고
    • Fibrinogen induces cytokine and collagen production in pancreatic stellate cells
    • Masamune A, Kikuta K, Watanabe T, Satoh K, Hirota M, Hamada S, et al. Fibrinogen induces cytokine and collagen production in pancreatic stellate cells. Gut. 2009;58(4):550-9.
    • (2009) Gut , vol.58 , Issue.4 , pp. 550-559
    • Masamune, A.1    Kikuta, K.2    Watanabe, T.3    Satoh, K.4    Hirota, M.5    Hamada, S.6
  • 95
    • 37249092998 scopus 로고    scopus 로고
    • Pancreatic stellate cells: New target in the treatment of chronic pancreatitis
    • Talukdar R, Tandon RK. Pancreatic stellate cells: new target in the treatment of chronic pancreatitis. J Gastroenterol Hepatol. 2008;23(1):34-41.
    • (2008) J Gastroenterol Hepatol , vol.23 , Issue.1 , pp. 34-41
    • Talukdar, R.1    Tandon, R.K.2
  • 96
    • 20444500034 scopus 로고    scopus 로고
    • Cytokines and peroxisome proliferator-activated receptor gamma ligand regulate phagocytosis by pancreatic stellate cells
    • Shimizu K, Kobayashi M, Tahara J, Shiratori K. Cytokines and peroxisome proliferator-activated receptor gamma ligand regulate phagocytosis by pancreatic stellate cells. Gastroenterology. 2005;128(7):2105-18.
    • (2005) Gastroenterology , vol.128 , Issue.7 , pp. 2105-2118
    • Shimizu, K.1    Kobayashi, M.2    Tahara, J.3    Shiratori, K.4
  • 97
    • 0036282292 scopus 로고    scopus 로고
    • Pancreatic stellate cells respond to inflammatory cytokines: Potential role in chronic pancreatitis
    • Mews P, Phillips P, Fahmy R, Korsten M, Pirola R, Wilson J, et al. Pancreatic stellate cells respond to inflammatory cytokines: potential role in chronic pancreatitis. Gut. 2002;50(4):535-41.
    • (2002) Gut , vol.50 , Issue.4 , pp. 535-541
    • Mews, P.1    Phillips, P.2    Fahmy, R.3    Korsten, M.4    Pirola, R.5    Wilson, J.6
  • 99
    • 66949174113 scopus 로고    scopus 로고
    • From proteomics research to clinical practice
    • Tsangaris GT. From proteomics research to clinical practice. Expert Rev Proteomics. 2009;6(3):235-8.
    • (2009) Expert Rev Proteomics , vol.6 , Issue.3 , pp. 235-238
    • Tsangaris, G.T.1
  • 100
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • Yates JR, Ruse CI, 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
  • 101
    • 56949086651 scopus 로고    scopus 로고
    • Proteomics: New technologies and clinical applications
    • Latterich M, Abramovitz M, Leyland-Jones B. Proteomics: new technologies and clinical applications. Eur J Cancer. 2008;44(18):2737-41.
    • (2008) Eur J Cancer , vol.44 , Issue.18 , pp. 2737-2741
    • Latterich, M.1    Abramovitz, M.2    Leyland-Jones, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.