메뉴 건너뛰기




Volumn 70, Issue 3, 2011, Pages 351-364

Nutriproteomics: Technologies and applications for identification and quantification of biomarkers and ingredients

Author keywords

Biomarkers; Ingredients; Nutriproteomics

Indexed keywords

BETA LACTOGLOBULIN; BIOLOGICAL MARKER; ESSENTIAL AMINO ACID; FOOD ALLERGEN; PEPSIN A; PEPTIDES AND PROTEINS; PROBIOTIC AGENT; TRYPSIN;

EID: 80054881621     PISSN: 00296651     EISSN: 14752719     Source Type: Journal    
DOI: 10.1017/S0029665111000528     Document Type: Conference Paper
Times cited : (17)

References (190)
  • 1
    • 0028141935 scopus 로고
    • Adult amino acid requirements: The case for a major revision in current recommendations
    • Young VR (1994) Adult amino acid requirements: The case for a major revision in current recommendations. J Nutr 124, 1517S-1523S
    • (1994) J Nutr , vol.124
    • Young, V.R.1
  • 2
    • 80054918540 scopus 로고    scopus 로고
    • Proteins
    • [M Dekker, editor]. New York: CRC Press
    • Desai B (2000) Proteins. In Handbook of Nutrition and Diet, pp. 1-816 [M Dekker, editor]. New York: CRC Press
    • (2000) Handbook of Nutrition and Diet , pp. 1-816
    • Desai, B.1
  • 3
    • 34948866795 scopus 로고    scopus 로고
    • How shall we use the proteomics toolbox for biomarker discovery?
    • Lescuyer P, Hochstrasser D & Rabilloud T (2007) How shall we use the proteomics toolbox for biomarker discovery? J Proteome Res 6, 3371-3376
    • (2007) J Proteome Res , vol.6 , pp. 3371-3376
    • Lescuyer, P.1    Hochstrasser, D.2    Rabilloud, T.3
  • 4
    • 34447283809 scopus 로고    scopus 로고
    • What does it need to be a biomarker? Relationships between resolution, differential quantification and statistical validation of protein surrogate biomarkers
    • Schrattenholz A & Groebe K (2007) What does it need to be a biomarker? Relationships between resolution, differential quantification and statistical validation of protein surrogate biomarkers. Electrophoresis 28, 1970-1979
    • (2007) Electrophoresis , vol.28 , pp. 1970-1979
    • Schrattenholz, A.1    Groebe, K.2
  • 5
    • 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, et al. (2009) Capillary electrophoresis-mass spectrometry as a powerful tool in biomarker discovery and clinical diagnosis: An update of recent developments. Mass Spectrom Rev 28, 703-724
    • (2009) Mass Spectrom Rev , vol.28 , pp. 703-724
    • Mischak, H.1    Coon, J.J.2    Novak, J.3
  • 6
    • 24044440791 scopus 로고    scopus 로고
    • Discovery of biomarker candidates within disease by protein profiling: Principles and concepts
    • Marko-Varga G, Lindberg H, Lofdahl CG, et al. (2005) Discovery of biomarker candidates within disease by protein profiling: Principles and concepts. J Proteome Res 4, 1200-1212
    • (2005) J Proteome Res , vol.4 , pp. 1200-1212
    • Marko-Varga, G.1    Lindberg, H.2    Lofdahl, C.G.3
  • 7
    • 23944436422 scopus 로고    scopus 로고
    • Proteomics: From basic research to diagnostic application. A review of requirements and needs
    • Vitzthum F, Behrens F, Anderson NL, et al. (2005) Proteomics: From basic research to diagnostic application. A review of requirements and needs. J Proteome Res 4, 1086-1097
    • (2005) J Proteome Res , vol.4 , pp. 1086-1097
    • Vitzthum, F.1    Behrens, F.2    Anderson, N.L.3
  • 8
    • 34547131554 scopus 로고    scopus 로고
    • Analysis of protein complexes using mass spectrometry
    • Gingras AC, Gstaiger M, Raught B, et al. (2007) Analysis of protein complexes using mass spectrometry. Nat Rev Mol Cell Biol 8, 645-654
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 645-654
    • Gingras, A.C.1    Gstaiger, M.2    Raught, B.3
  • 9
    • 34249310964 scopus 로고    scopus 로고
    • Diversity of cAMP-dependent protein kinase isoforms and their anchoring proteins in mouse ventricular tissue
    • Scholten A, van Veen TA, Vos MA, et al. (2007) Diversity of cAMP-dependent protein kinase isoforms and their anchoring proteins in mouse ventricular tissue. J Proteome Res 6, 1705-1717
    • (2007) J Proteome Res , vol.6 , pp. 1705-1717
    • Scholten, A.1    Van Veen, T.A.2    Vos, M.A.3
  • 10
    • 33745659440 scopus 로고    scopus 로고
    • Proteomics and its role in nutrition research
    • Wang J, Li D, Dangott LJ, et al. (2006) Proteomics and its role in nutrition research. J Nutr 136, 1759-1762
    • (2006) J Nutr , vol.136 , pp. 1759-1762
    • Wang, J.1    Li, D.2    Dangott, L.J.3
  • 11
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R & Mann M (2003) Mass spectrometry-based proteomics. Nature 422, 198-207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 12
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, et al. (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246, 64-71
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3
  • 13
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons
    • Karas M & Hillenkamp F (1988) Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Anal Chem 60, 2299-2301
    • (1988) Anal Chem , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 14
    • 23944480893 scopus 로고    scopus 로고
    • Utilizing human blood plasma for proteomic biomarker discovery
    • Jacobs JM, Adkins JN, Qian WJ, et al. (2005) Utilizing human blood plasma for proteomic biomarker discovery. J Proteome Res 4, 1073-1085
    • (2005) J Proteome Res , vol.4 , pp. 1073-1085
    • Jacobs, J.M.1    Adkins, J.N.2    Qian, W.J.3
  • 15
    • 33744996070 scopus 로고    scopus 로고
    • Different immunoaffinity fractionation strategies to characterize the human plasma proteome
    • Gong Y, Li X, Yang B, et al. (2006) Different immunoaffinity fractionation strategies to characterize the human plasma proteome. J Proteome Res 5, 1379-1387
    • (2006) J Proteome Res , vol.5 , pp. 1379-1387
    • Gong, Y.1    Li, X.2    Yang, B.3
  • 16
    • 44049093407 scopus 로고    scopus 로고
    • Glycoprotein enrichment through lectin affinity techniques
    • Mechref Y, Madera M & Novotny MV (2008) Glycoprotein enrichment through lectin affinity techniques. Methods Mol Biol 424, 373-396
    • (2008) Methods Mol Biol , vol.424 , pp. 373-396
    • Mechref, Y.1    Madera, M.2    Novotny, M.V.3
  • 17
    • 63049113651 scopus 로고    scopus 로고
    • Analytical strategies for phosphoproteomics
    • Thingholm TE, Jensen ON & Larsen MR (2009) Analytical strategies for phosphoproteomics. Proteomics 9, 1451-1468
    • (2009) Proteomics , vol.9 , pp. 1451-1468
    • Thingholm, T.E.1    Jensen, O.N.2    Larsen, M.R.3
  • 18
    • 64349089985 scopus 로고    scopus 로고
    • Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins
    • Wollscheid B, Bausch-Fluck D, Henderson C, et al. (2009) Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol 27, 378-386
    • (2009) Nat Biotechnol , vol.27 , pp. 378-386
    • Wollscheid, B.1    Bausch-Fluck, D.2    Henderson, C.3
  • 19
    • 33644755630 scopus 로고    scopus 로고
    • Improved protein recovery in reversed-phase liquid chromatography by the use of ultrahigh pressures
    • Eschelbach JW & Jorgenson JW (2006) Improved protein recovery in reversed-phase liquid chromatography by the use of ultrahigh pressures. Anal Chem 78, 1697-1706
    • (2006) Anal Chem , vol.78 , pp. 1697-1706
    • Eschelbach, J.W.1    Jorgenson, J.W.2
  • 20
    • 0035106351 scopus 로고    scopus 로고
    • Largescale analysis of the yeast proteome by multidimensional protein identification technology
    • Washburn MP, Wolters D & Yates JR, 3rd (2001) Largescale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19, 242-247
    • (2001) Nat Biotechnol , vol.19 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates III, J.R.3
  • 21
    • 1842457041 scopus 로고    scopus 로고
    • Proteomic investigation of natural killer cell microsomes using gas-phase fractionation by mass spectrometry
    • Blonder J, Rodriguez-Galan MC, Lucas DA, et al. (2004) Proteomic investigation of natural killer cell microsomes using gas-phase fractionation by mass spectrometry. Biochim Biophys Acta 1698, 87-95
    • (2004) Biochim Biophys Acta , vol.1698 , pp. 87-95
    • Blonder, J.1    Rodriguez-Galan, M.C.2    Lucas, D.A.3
  • 22
    • 39449111536 scopus 로고    scopus 로고
    • Genomespecific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides
    • Scherl A, Shaffer SA, Taylor GK, et al. (2008) Genomespecific gas-phase fractionation strategy for improved shotgun proteomic profiling of proteotypic peptides. Anal Chem 80, 1182-1191
    • (2008) Anal Chem , vol.80 , pp. 1182-1191
    • Scherl, A.1    Shaffer, S.A.2    Taylor, G.K.3
  • 23
    • 0036747350 scopus 로고    scopus 로고
    • Approaching complete peroxisome characterization by gas-phase fractionation
    • Yi EC, Marelli M, Lee H, et al. (2002) Approaching complete peroxisome characterization by gas-phase fractionation. Electrophoresis 23, 3205-3216
    • (2002) Electrophoresis , vol.23 , pp. 3205-3216
    • Yi, E.C.1    Marelli, M.2    Lee, H.3
  • 24
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel lecture)
    • Fenn JB (2003) Electrospray wings for molecular elephants (Nobel lecture). Angew Chem Int Ed Engl 42, 3871-3894
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3871-3894
    • Fenn, J.B.1
  • 25
    • 0042318496 scopus 로고    scopus 로고
    • The origin of macromolecule ionization by laser irradiation (Nobel lecture)
    • Tanaka K (2003) The origin of macromolecule ionization by laser irradiation (Nobel lecture). Angew Chem Int Ed Engl 42, 3860-3870
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3860-3870
    • Tanaka, K.1
  • 26
    • 33645654439 scopus 로고    scopus 로고
    • Performance evaluation of a hybrid linear ion trap/orbitrap mass spectrometer
    • Makarov A, Denisov E, Kholomeev A, et al. (2006) Performance evaluation of a hybrid linear ion trap/orbitrap mass spectrometer. Anal Chem 78, 2113-2120
    • (2006) Anal Chem , vol.78 , pp. 2113-2120
    • Makarov, A.1    Denisov, E.2    Kholomeev, A.3
  • 27
    • 21044441542 scopus 로고    scopus 로고
    • Improving protein identification using complementary fragmentation techniques in Fourier transform mass spectrometry
    • Nielsen ML, Savitski MM & Zubarev RA (2005) Improving protein identification using complementary fragmentation techniques in Fourier transform mass spectrometry. Mol Cell Proteomics 4, 835-845
    • (2005) Mol Cell Proteomics , vol.4 , pp. 835-845
    • Nielsen, M.L.1    Savitski, M.M.2    Zubarev, R.A.3
  • 28
    • 68049114653 scopus 로고    scopus 로고
    • Precursor acquisition independent from ion count: How to dive deeper into the proteomics ocean
    • Panchaud A, Scherl A, Shaffer SA, et al. (2009) Precursor acquisition independent from ion count: How to dive deeper into the proteomics ocean. Anal Chem 81, 6481-6488
    • (2009) Anal Chem , vol.81 , pp. 6481-6488
    • Panchaud, A.1    Scherl, A.2    Shaffer, S.A.3
  • 29
    • 41349096900 scopus 로고    scopus 로고
    • Data analysis and bioinformatics tools for tandem mass spectrometry in proteomics
    • Deutsch EW, Lam H & Aebersold R (2008) Data analysis and bioinformatics tools for tandem mass spectrometry in proteomics. Physiol Genomics 33, 18-25
    • (2008) Physiol Genomics , vol.33 , pp. 18-25
    • Deutsch, E.W.1    Lam, H.2    Aebersold, R.3
  • 30
    • 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 (1994) An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom 5, 976-989
    • (1994) J Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 31
    • 0033434080 scopus 로고    scopus 로고
    • Probability- based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, et al. (1999) Probability- based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3
  • 32
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A, Nesvizhskii AI, Kolker E, et al. (2002) Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 74, 5383-5392
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3
  • 33
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii AI, Keller A, Kolker E, et al. (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75, 4646-4658
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3
  • 34
    • 33750362838 scopus 로고    scopus 로고
    • Statistics for proteomics: A review of tools for analyzing experimental data
    • Urfer W, Grzegorczyk M & Jung K (2006) Statistics for proteomics: A review of tools for analyzing experimental data. Proteomics 6 Suppl. 2, 48-55
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 2 , pp. 48-55
    • Urfer, W.1    Grzegorczyk, M.2    Jung, K.3
  • 35
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias JE & Gygi SP (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4, 207-214
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 36
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME & Minden JS (1997) Difference gel electrophoresis: A single gel method for detecting changes in protein extracts. Electrophoresis 18, 2071-2077
    • (1997) Electrophoresis , vol.18 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 37
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • Gygi SP, Rist B, Gerber SA, et al. (1999) Quantitative analysis of complex protein mixtures using isotope-coded affinity tags. Nat Biotechnol 17, 994-999
    • (1999) Nat Biotechnol , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3
  • 38
    • 2542486702 scopus 로고    scopus 로고
    • Determination of endogenous and supplied deuterated abscisic acid in plant tissues by high-performance liquid chromatographyelectrospray ionization tandem mass spectrometry with multiple reaction monitoring
    • Ross AR, Ambrose SJ, Cutler AJ, et al. (2004) Determination of endogenous and supplied deuterated abscisic acid in plant tissues by high-performance liquid chromatographyelectrospray ionization tandem mass spectrometry with multiple reaction monitoring. Anal Biochem 329, 324-333
    • (2004) Anal Biochem , vol.329 , pp. 324-333
    • Ross, A.R.1    Ambrose, S.J.2    Cutler, A.J.3
  • 39
    • 13244260803 scopus 로고    scopus 로고
    • A novel strategy for quantitative proteomics using isotope-coded protein labels
    • Schmidt A, Kellermann J & Lottspeich F (2005) A novel strategy for quantitative proteomics using isotope-coded protein labels. Proteomics 5, 4-15
    • (2005) Proteomics , vol.5 , pp. 4-15
    • Schmidt, A.1    Kellermann, J.2    Lottspeich, F.3
  • 40
    • 42649098635 scopus 로고    scopus 로고
    • ANIBAL, stable isotope-based quantitative proteomics by aniline and benzoic acid labeling of amino and carboxylic groups
    • Panchaud A, Hansson J, Affolter M, et al. (2008) ANIBAL, stable isotope-based quantitative proteomics by aniline and benzoic acid labeling of amino and carboxylic groups. Mol Cell Proteomics 7, 800-812
    • (2008) Mol Cell Proteomics , vol.7 , pp. 800-812
    • Panchaud, A.1    Hansson, J.2    Affolter, M.3
  • 41
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, et al. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1, 376-386
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3
  • 42
    • 0038699625 scopus 로고    scopus 로고
    • Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry
    • Zhang H, Li XJ, Martin DB, et al. (2003) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol 21, 660-666
    • (2003) Nat Biotechnol , vol.21 , pp. 660-666
    • Zhang, H.1    Li, X.J.2    Martin, D.B.3
  • 43
    • 3543121341 scopus 로고    scopus 로고
    • Quantification in proteomics through stable isotope coding: A review
    • Julka S & Regnier F (2004) Quantification in proteomics through stable isotope coding: A review. J Proteome Res 3, 350-363
    • (2004) J Proteome Res , vol.3 , pp. 350-363
    • Julka, S.1    Regnier, F.2
  • 44
    • 0038371369 scopus 로고    scopus 로고
    • Quantitative chemical proteomics for identifying candidate drug targets
    • Oda Y, Owa T, Sato T, et al. (2003) Quantitative chemical proteomics for identifying candidate drug targets. Anal Chem 75, 2159-2165
    • (2003) Anal Chem , vol.75 , pp. 2159-2165
    • Oda, Y.1    Owa, T.2    Sato, T.3
  • 45
    • 0036789268 scopus 로고    scopus 로고
    • Acid-labile isotope-coded extractants: A class of reagents for quantitative mass spectrometric analysis of complex protein mixtures
    • Qiu Y, Sousa EA, Hewick RM, et al. (2002) Acid-labile isotope-coded extractants: A class of reagents for quantitative mass spectrometric analysis of complex protein mixtures. Anal Chem 74, 4969-4979
    • (2002) Anal Chem , vol.74 , pp. 4969-4979
    • Qiu, Y.1    Sousa, E.A.2    Hewick, R.M.3
  • 46
    • 0035983628 scopus 로고    scopus 로고
    • A method to identify and simultaneously determine the relative quantities of proteins isolated by gel electrophoresis
    • Sechi S (2002) A method to identify and simultaneously determine the relative quantities of proteins isolated by gel electrophoresis. Rapid Commun Mass Spectrom 16, 1416-1424
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 1416-1424
    • Sechi, S.1
  • 47
    • 0036023992 scopus 로고    scopus 로고
    • Quantitative analysis of two-dimensional gel-separated proteins using isotopically marked alkylating agents and matrix-assisted laser desorption/ionization mass spectrometry
    • Gehanne S, Cecconi D, Carboni L, et al. (2002) Quantitative analysis of two-dimensional gel-separated proteins using isotopically marked alkylating agents and matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 16, 1692-1698
    • (2002) Rapid Commun Mass Spectrom , vol.16 , pp. 1692-1698
    • Gehanne, S.1    Cecconi, D.2    Carboni, L.3
  • 48
    • 1642412734 scopus 로고    scopus 로고
    • Isolation and isotope labeling of cysteine- and methionine-containing tryptic peptides: Application to the study of cell surface proteolysis
    • Shen M, Guo L, Wallace A, et al. (2003) Isolation and isotope labeling of cysteine- and methionine-containing tryptic peptides: Application to the study of cell surface proteolysis. Mol Cell Proteomics 2, 315-324
    • (2003) Mol Cell Proteomics , vol.2 , pp. 315-324
    • Shen, M.1    Guo, L.2    Wallace, A.3
  • 49
    • 0038608603 scopus 로고    scopus 로고
    • An approach to quantitative proteome analysis by labeling tryptophan residues
    • Kuyama H, Watanabe M, Toda C, et al. (2003) An approach to quantitative proteome analysis by labeling tryptophan residues. Rapid Commun Mass Spectrom 17, 1642-1650
    • (2003) Rapid Commun Mass Spectrom , vol.17 , pp. 1642-1650
    • Kuyama, H.1    Watanabe, M.2    Toda, C.3
  • 50
    • 33646725310 scopus 로고    scopus 로고
    • Combining protein identification and quantification: C-terminal isotope-coded tagging using sulfanilic acid
    • Panchaud A, Guillaume E, Affolter M, et al. (2006) Combining protein identification and quantification: C-terminal isotope-coded tagging using sulfanilic acid. Rapid Commun Mass Spectrom 20, 1585-1594
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 1585-1594
    • Panchaud, A.1    Guillaume, E.2    Affolter, M.3
  • 51
    • 0035384687 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus
    • Yao X, Freas A, Ramirez J, et al. (2001) Proteolytic 18O labeling for comparative proteomics: Model studies with two serotypes of adenovirus. Anal Chem 73, 2836-2842
    • (2001) Anal Chem , vol.73 , pp. 2836-2842
    • Yao, X.1    Freas, A.2    Ramirez, J.3
  • 52
    • 0034654476 scopus 로고    scopus 로고
    • Identification and C-terminal characterization of proteins from twodimensional polyacrylamide gels by a combination of isotopic labeling and nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Kosaka T, Takazawa T & Nakamura T (2000) Identification and C-terminal characterization of proteins from twodimensional polyacrylamide gels by a combination of isotopic labeling and nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal Chem 72, 1179-1185
    • (2000) Anal Chem , vol.72 , pp. 1179-1185
    • Kosaka, T.1    Takazawa, T.2    Nakamura, T.3
  • 53
    • 0036391333 scopus 로고    scopus 로고
    • Proteolytic 18O labeling for comparative proteomics: Evaluation of endoprotease Glu-C as the catalytic agent
    • Reynolds KJ, Yao X & Fenselau C (2002) Proteolytic 18O labeling for comparative proteomics: Evaluation of endoprotease Glu-C as the catalytic agent. J Proteome Res 1, 27-33
    • (2002) J Proteome Res , vol.1 , pp. 27-33
    • Reynolds, K.J.1    Yao, X.2    Fenselau, C.3
  • 54
    • 0034921817 scopus 로고    scopus 로고
    • Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation
    • Goodlett DR, Keller A, Watts JD, et al. (2001) Differential stable isotope labeling of peptides for quantitation and de novo sequence derivation. Rapid Commun Mass Spectrom 15, 1214-1221
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 1214-1221
    • Goodlett, D.R.1    Keller, A.2    Watts, J.D.3
  • 55
    • 0035543071 scopus 로고    scopus 로고
    • A novel multifunctional labeling reagent for enhanced protein characterization with mass spectrometry
    • Peters EC, Horn DM, Tully DC, et al. (2001) A novel multifunctional labeling reagent for enhanced protein characterization with mass spectrometry. Rapid Commun Mass Spectrom 15, 2387-2392
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 2387-2392
    • Peters, E.C.1    Horn, D.M.2    Tully, D.C.3
  • 56
    • 0033647183 scopus 로고    scopus 로고
    • Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry
    • Beardsley RL, Karty JA & Reilly JP (2000) Enhancing the intensities of lysine-terminated tryptic peptide ions in matrix-assisted laser desorption/ionization mass spectrometry. Rapid Commun Mass Spectrom 14, 2147-2153
    • (2000) Rapid Commun Mass Spectrom , vol.14 , pp. 2147-2153
    • Beardsley, R.L.1    Karty, J.A.2    Reilly, J.P.3
  • 57
    • 0344608889 scopus 로고    scopus 로고
    • Defining absolute confidence limits in the identification of Caulobacter proteins by peptide mass mapping
    • Karty JA, Ireland MM, Brun YV, et al. (2002) Defining absolute confidence limits in the identification of Caulobacter proteins by peptide mass mapping. J Proteome Res 1, 325-335
    • (2002) J Proteome Res , vol.1 , pp. 325-335
    • Karty, J.A.1    Ireland, M.M.2    Brun, Y.V.3
  • 58
    • 0036171359 scopus 로고    scopus 로고
    • De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging
    • Cagney G & Emili A (2002) De novo peptide sequencing and quantitative profiling of complex protein mixtures using mass-coded abundance tagging. Nat Biotechnol 20, 163-170
    • (2002) Nat Biotechnol , vol.20 , pp. 163-170
    • Cagney, G.1    Emili, A.2
  • 59
    • 33646254857 scopus 로고    scopus 로고
    • Differentially isotope-coded N-terminal protein sulphonation: Combining protein identification and quantification
    • Guillaume E, Panchaud A, Affolter M, et al. (2006) Differentially isotope-coded N-terminal protein sulphonation: Combining protein identification and quantification. Proteomics 6, 2338-2349
    • (2006) Proteomics , vol.6 , pp. 2338-2349
    • Guillaume, E.1    Panchaud, A.2    Affolter, M.3
  • 60
    • 0033543508 scopus 로고    scopus 로고
    • Protein crosslinks: Universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry
    • Chen X, Chen YH & Anderson VE (1999) Protein crosslinks: Universal isolation and characterization by isotopic derivatization and electrospray ionization mass spectrometry. Anal Biochem 273, 192-203
    • (1999) Anal Biochem , vol.273 , pp. 192-203
    • Chen, X.1    Chen, Y.H.2    Anderson, V.E.3
  • 61
    • 0041877476 scopus 로고    scopus 로고
    • Quantitative analysis of modified proteins by LC-MS/MS of peptides labeled with phenyl isocyanate
    • Mason DE & Liebler DC (2003) Quantitative analysis of modified proteins by LC-MS/MS of peptides labeled with phenyl isocyanate. J Proteome Res 2, 265-272
    • (2003) J Proteome Res , vol.2 , pp. 265-272
    • Mason, D.E.1    Liebler, D.C.2
  • 62
    • 0036523809 scopus 로고    scopus 로고
    • Minimizing resolution of isotopically coded peptides in comparative proteomics
    • Zhang R & Regnier FE (2002) Minimizing resolution of isotopically coded peptides in comparative proteomics. J Proteome Res 1, 139-147
    • (2002) J Proteome Res , vol.1 , pp. 139-147
    • Zhang, R.1    Regnier, F.E.2
  • 63
    • 0036682618 scopus 로고    scopus 로고
    • Controlling deuterium isotope effects in comparative proteomics
    • Zhang R, Sioma CS, Thompson RA, et al. (2002) Controlling deuterium isotope effects in comparative proteomics. Anal Chem 74, 3662-3669
    • (2002) Anal Chem , vol.74 , pp. 3662-3669
    • Zhang, R.1    Sioma, C.S.2    Thompson, R.A.3
  • 64
    • 0036665581 scopus 로고    scopus 로고
    • Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry
    • Chelius D & Bondarenko PV (2002) Quantitative profiling of proteins in complex mixtures using liquid chromatography and mass spectrometry. J Proteome Res 1, 317-323
    • (2002) J Proteome Res , vol.1 , pp. 317-323
    • Chelius, D.1    Bondarenko, P.V.2
  • 65
    • 35348965139 scopus 로고    scopus 로고
    • SuperHirn - A novel tool for high resolution LC-MS-based peptide/protein profiling
    • Mueller LN, Rinner O, Schmidt A, et al. (2007) SuperHirn - a novel tool for high resolution LC-MS-based peptide/protein profiling. Proteomics 7, 3470-3480
    • (2007) Proteomics , vol.7 , pp. 3470-3480
    • Mueller, L.N.1    Rinner, O.2    Schmidt, A.3
  • 66
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H, Sadygov RG & Yates JR, 3rd (2004) A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem 76, 4193-4201
    • (2004) Anal Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 67
    • 34748916981 scopus 로고    scopus 로고
    • Quantitative mass spectrometry in proteomics: A critical review
    • Bantscheff M, Schirle M, Sweetman G, et al. (2007) Quantitative mass spectrometry in proteomics: A critical review. Anal Bioanal Chem 389, 1017-1031
    • (2007) Anal Bioanal Chem , vol.389 , pp. 1017-1031
    • Bantscheff, M.1    Schirle, M.2    Sweetman, G.3
  • 68
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, et al. (2003) Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 100, 6940-6945
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3
  • 69
    • 34548427053 scopus 로고    scopus 로고
    • Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT
    • Rivers J, Simpson DM, Robertson DH, et al. (2007) Absolute multiplexed quantitative analysis of protein expression during muscle development using QconCAT. Mol Cell Proteomics 6, 1416-1427
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1416-1427
    • Rivers, J.1    Simpson, D.M.2    Robertson, D.H.3
  • 70
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange V, Picotti P, Domon B, et al. (2008) Selected reaction monitoring for quantitative proteomics: A tutorial. Mol Syst Biol 4, 222
    • (2008) Mol Syst Biol , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3
  • 71
    • 55849118087 scopus 로고    scopus 로고
    • Quantitative phosphoproteomics by mass spectrometry: Past, present, and future
    • Nita-Lazar A, Saito-Benz H & White FM (2008) Quantitative phosphoproteomics by mass spectrometry: Past, present, and future. Proteomics 8, 4433-4443
    • (2008) Proteomics , vol.8 , pp. 4433-4443
    • Nita-Lazar, A.1    Saito-Benz, H.2    White, F.M.3
  • 72
    • 0034690931 scopus 로고    scopus 로고
    • Use of mass spectrometry to study signaling pathways
    • Pandey A, Andersen JS & Mann M (2000) Use of mass spectrometry to study signaling pathways. Sci STKE 2000, pl1
    • (2000) Sci STKE
    • Pandey, A.1    Andersen, J.S.2    Mann, M.3
  • 73
    • 0022541790 scopus 로고
    • Isolation of phosphoproteins by immobilized metal (Fe3 + ) affinity chromatography
    • Andersson L & Porath J (1986) Isolation of phosphoproteins by immobilized metal (Fe3 + ) affinity chromatography. Anal Biochem 154, 250-254
    • (1986) Anal Biochem , vol.154 , pp. 250-254
    • Andersson, L.1    Porath, J.2
  • 74
    • 4344574540 scopus 로고    scopus 로고
    • Large-scale characterization of HeLa cell nuclear phosphoproteins
    • Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004) Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci USA 101, 12130-12135
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12130-12135
    • Beausoleil, S.A.1    Jedrychowski, M.2    Schwartz, D.3
  • 75
    • 0034133274 scopus 로고    scopus 로고
    • Electron capture dissociation for structural characterization of multiply charged protein cations
    • Zubarev RA, Horn DM, Fridriksson EK, et al. (2000) Electron capture dissociation for structural characterization of multiply charged protein cations. Anal Chem 72, 563-573
    • (2000) Anal Chem , vol.72 , pp. 563-573
    • Zubarev, R.A.1    Horn, D.M.2    Fridriksson, E.K.3
  • 76
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka JE, Coon JJ, Schroeder MJ, et al. (2004) Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci USA 101, 9528-9533
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3
  • 77
    • 55849104839 scopus 로고    scopus 로고
    • Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications
    • Wiesner J, Premsler T & Sickmann A (2008) Application of electron transfer dissociation (ETD) for the analysis of posttranslational modifications. Proteomics 8, 4466-4483
    • (2008) Proteomics , vol.8 , pp. 4466-4483
    • Wiesner, J.1    Premsler, T.2    Sickmann, A.3
  • 78
    • 58149186651 scopus 로고    scopus 로고
    • Glycobiology in the cytosol: The bitter side of a sweet world
    • Funakoshi Y & Suzuki T (2009) Glycobiology in the cytosol: The bitter side of a sweet world. Biochim Biophys Acta 1790, 81-94
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 81-94
    • Funakoshi, Y.1    Suzuki, T.2
  • 79
    • 0035937542 scopus 로고    scopus 로고
    • Glycoprotein structure determination by mass spectrometry
    • Dell A & Morris HR (2001) Glycoprotein structure determination by mass spectrometry. Science 291, 2351-2356
    • (2001) Science , vol.291 , pp. 2351-2356
    • Dell, A.1    Morris, H.R.2
  • 80
    • 67349272331 scopus 로고    scopus 로고
    • Glycoproteomics: Past, present and future
    • Tissot B, North SJ, Ceroni A, et al. (2009) Glycoproteomics: Past, present and future. FEBS Lett 583, 1728-1735
    • (2009) FEBS Lett , vol.583 , pp. 1728-1735
    • Tissot, B.1    North, S.J.2    Ceroni, A.3
  • 81
    • 5644244327 scopus 로고    scopus 로고
    • Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column
    • Yang Z & Hancock WS (2004) Approach to the comprehensive analysis of glycoproteins isolated from human serum using a multi-lectin affinity column. J Chromatogr A 1053, 79-88
    • (2004) J Chromatogr A , vol.1053 , pp. 79-88
    • Yang, Z.1    Hancock, W.S.2
  • 82
    • 78651162036 scopus 로고
    • Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis
    • Allfrey VG, Faulkner R & Mirsky AE (1964) Acetylation and methylation of histones and their possible role in the regulation of RNA synthesis. Proc Natl Acad Sci USA 51, 786-794
    • (1964) Proc Natl Acad Sci USA , vol.51 , pp. 786-794
    • Allfrey, V.G.1    Faulkner, R.2    Mirsky, A.E.3
  • 83
    • 0035032345 scopus 로고    scopus 로고
    • A tale of histone modifications
    • Grant PA (2001) A tale of histone modifications. Genome Biol 2, REVIEWS0003
    • (2001) Genome Biol , vol.2
    • Grant, P.A.1
  • 84
    • 35848961668 scopus 로고    scopus 로고
    • How chromatin- binding modules interpret histone modifications: Lessons from professional pocket pickers
    • Taverna SD, Li H, Ruthenburg AJ, et al. (2007) How chromatin- binding modules interpret histone modifications: Lessons from professional pocket pickers. Nat Struct Mol Biol 14, 1025-1040
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1025-1040
    • Taverna, S.D.1    Li, H.2    Ruthenburg, A.J.3
  • 85
    • 0032518442 scopus 로고    scopus 로고
    • Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase
    • Verreault A, Kaufman PD, Kobayashi R, et al. (1998) Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase. Curr Biol 8, 96-108
    • (1998) Curr Biol , vol.8 , pp. 96-108
    • Verreault, A.1    Kaufman, P.D.2    Kobayashi, R.3
  • 86
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD & Allis CD (2000) The language of covalent histone modifications. Nature 403, 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 87
    • 33645471026 scopus 로고    scopus 로고
    • Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry
    • Bonenfant D, Coulot M, Towbin H, et al. (2006) Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometry. Mol Cell Proteomics 5, 541-552
    • (2006) Mol Cell Proteomics , vol.5 , pp. 541-552
    • Bonenfant, D.1    Coulot, M.2    Towbin, H.3
  • 88
    • 34247869836 scopus 로고    scopus 로고
    • A newly discovered post-translational modification - The acetylation of serine and threonine residues
    • Mukherjee S, Hao YH & Orth K (2007) A newly discovered post-translational modification - the acetylation of serine and threonine residues. Trends Biochem Sci 32, 210-216
    • (2007) Trends Biochem Sci , vol.32 , pp. 210-216
    • Mukherjee, S.1    Hao, Y.H.2    Orth, K.3
  • 89
    • 35848970747 scopus 로고    scopus 로고
    • Mapping protein post-translational modifications with mass spectrometry
    • Witze ES, Old WM, Resing KA, et al. (2007) Mapping protein post-translational modifications with mass spectrometry. Nat Methods 4, 798-806
    • (2007) Nat Methods , vol.4 , pp. 798-806
    • Witze, E.S.1    Old, W.M.2    Resing, K.A.3
  • 90
    • 33746992118 scopus 로고    scopus 로고
    • Substrate and functional diversity of lysine acetylation revealed by a proteomics survey
    • Kim SC, Sprung R, Chen Y, et al. (2006) Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell 23, 607-618
    • (2006) Mol Cell , vol.23 , pp. 607-618
    • Kim, S.C.1    Sprung, R.2    Chen, Y.3
  • 91
    • 6344253356 scopus 로고    scopus 로고
    • Antiinflammatory properties of HDL
    • Barter PJ, Nicholls S, Rye KA, et al. (2004) Antiinflammatory properties of HDL. Circ Res 95, 764-772
    • (2004) Circ Res , vol.95 , pp. 764-772
    • Barter, P.J.1    Nicholls, S.2    Rye, K.A.3
  • 92
    • 17844392647 scopus 로고    scopus 로고
    • Atherosclerosis and innate immune signaling
    • Laberge MA, Moore KJ & Freeman MW (2005) Atherosclerosis and innate immune signaling. Ann Med 37, 130-140
    • (2005) Ann Med , vol.37 , pp. 130-140
    • Laberge, M.A.1    Moore, K.J.2    Freeman, M.W.3
  • 93
    • 25444468813 scopus 로고    scopus 로고
    • Human high density lipoproteins are platforms for the assembly of multicomponent innate immune complexes
    • Shiflett AM, Bishop JR, Pahwa A, et al. (2005) Human high density lipoproteins are platforms for the assembly of multicomponent innate immune complexes. J Biol Chem 280, 32578-32585
    • (2005) J Biol Chem , vol.280 , pp. 32578-32585
    • Shiflett, A.M.1    Bishop, J.R.2    Pahwa, A.3
  • 94
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • Havel RJ, Eder HA & Bragdon JH (1955) The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J Clin Invest 34, 1345-1353
    • (1955) J Clin Invest , vol.34 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.2    Bragdon, J.H.3
  • 95
    • 0020988593 scopus 로고
    • Apolipoproteins and lipoproteins of human plasma: Significance in health and in disease
    • Kostner GM (1983) Apolipoproteins and lipoproteins of human plasma: Significance in health and in disease. Adv Lipid Res 20, 1-43
    • (1983) Adv Lipid Res , vol.20 , pp. 1-43
    • Kostner, G.M.1
  • 96
    • 0028271643 scopus 로고
    • Identification of proteins associated with apolipoprotein A-I-containing lipoproteins purified by selected-affinity immunosorption
    • Kunitake ST, Carilli CT, Lau K, et al. (1994) Identification of proteins associated with apolipoprotein A-I-containing lipoproteins purified by selected-affinity immunosorption. Biochemistry 33, 1988-1993
    • (1994) Biochemistry , vol.33 , pp. 1988-1993
    • Kunitake, S.T.1    Carilli, C.T.2    Lau, K.3
  • 97
    • 0022455614 scopus 로고
    • Isolation of pure LpB from human serum
    • Zechner R, Moser R & Kostner GM (1986) Isolation of pure LpB from human serum. J Lipid Res 27, 681-686
    • (1986) J Lipid Res , vol.27 , pp. 681-686
    • Zechner, R.1    Moser, R.2    Kostner, G.M.3
  • 98
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipides from animal tissues
    • Folch J, Lees M & Sloane Stanley GH (1957) A simple method for the isolation and purification of total lipides from animal tissues. J Biol Chem 226, 497-509
    • (1957) J Biol Chem , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 99
    • 13844306306 scopus 로고    scopus 로고
    • Lipoproteomics I: Mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry
    • Karlsson H, Leanderson P, Tagesson C, et al. (2005) Lipoproteomics I: Mapping of proteins in low-density lipoprotein using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 5, 551-565
    • (2005) Proteomics , vol.5 , pp. 551-565
    • Karlsson, H.1    Leanderson, P.2    Tagesson, C.3
  • 100
    • 0042062361 scopus 로고    scopus 로고
    • Analysis of high-density lipoprotein apolipoproteins recovered from specific immobilized pH gradient gel pI domains by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Farwig ZN, Campbell AV & Macfarlane RD (2003) Analysis of high-density lipoprotein apolipoproteins recovered from specific immobilized pH gradient gel pI domains by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Anal Chem 75, 3823-3830
    • (2003) Anal Chem , vol.75 , pp. 3823-3830
    • Farwig, Z.N.1    Campbell, A.V.2    MacFarlane, R.D.3
  • 101
    • 4344581496 scopus 로고    scopus 로고
    • Virtual two-dimensional gel electrophoresis of high-density lipoproteins
    • Ogorzalek Loo RR, Yam L, Loo JA, et al. (2004) Virtual two-dimensional gel electrophoresis of high-density lipoproteins. Electrophoresis 25, 2384-2391
    • (2004) Electrophoresis , vol.25 , pp. 2384-2391
    • Ogorzalek Loo, R.R.1    Yam, L.2    Loo, J.A.3
  • 102
    • 32144455084 scopus 로고    scopus 로고
    • Proteomic analysis of high-density lipoprotein
    • Rezaee F, Casetta B, Levels JH, et al. (2006) Proteomic analysis of high-density lipoprotein. Proteomics 6, 721-730
    • (2006) Proteomics , vol.6 , pp. 721-730
    • Rezaee, F.1    Casetta, B.2    Levels, J.H.3
  • 103
    • 38949111042 scopus 로고    scopus 로고
    • Proteomics and lipids of lipoproteins isolated at low salt concentrations in D2O/sucrose or in KBr
    • Stahlman M, Davidsson P, Kanmert I, et al. (2008) Proteomics and lipids of lipoproteins isolated at low salt concentrations in D2O/sucrose or in KBr. J Lipid Res 49, 481-490
    • (2008) J Lipid Res , vol.49 , pp. 481-490
    • Stahlman, M.1    Davidsson, P.2    Kanmert, I.3
  • 104
    • 33846599241 scopus 로고    scopus 로고
    • Proteomic analysis of human very low-density lipoprotein by twodimensional gel electrophoresis and MALDI-TOF/TOF
    • Mancone C, Amicone L, Fimia GM, et al. (2007) Proteomic analysis of human very low-density lipoprotein by twodimensional gel electrophoresis and MALDI-TOF/TOF. Proteomics 7, 143-154
    • (2007) Proteomics , vol.7 , pp. 143-154
    • Mancone, C.1    Amicone, L.2    Fimia, G.M.3
  • 105
    • 33847368173 scopus 로고    scopus 로고
    • Shotgun proteomics implicates protease inhibition and complement activation in the anti-inflammatory properties of HDL
    • Vaisar T, Pennathur S, Green PS, et al. (2007) Shotgun proteomics implicates protease inhibition and complement activation in the anti-inflammatory properties of HDL. J Clin Invest 117, 746-756
    • (2007) J Clin Invest , vol.117 , pp. 746-756
    • Vaisar, T.1    Pennathur, S.2    Green, P.S.3
  • 106
    • 76149113930 scopus 로고    scopus 로고
    • Deconvolution of mixture spectra from ion-trap data- independentacquisition tandem mass spectrometry
    • Bern M, Finney G, Hoopmann MR, et al. (2010) Deconvolution of mixture spectra from ion-trap data-independentacquisition tandem mass spectrometry. Anal Chem 82, 833-841
    • (2010) Anal Chem , vol.82 , pp. 833-841
    • Bern, M.1    Finney, G.2    Hoopmann, M.R.3
  • 107
    • 0036747311 scopus 로고    scopus 로고
    • Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry
    • Chaurand P & Caprioli RM (2002) Direct profiling and imaging of peptides and proteins from mammalian cells and tissue sections by mass spectrometry. Electrophoresis 23, 3125-3135
    • (2002) Electrophoresis , vol.23 , pp. 3125-3135
    • Chaurand, P.1    Caprioli, R.M.2
  • 108
    • 57449106862 scopus 로고    scopus 로고
    • Molecular imaging of proteins in tissues by mass spectrometry
    • Seeley EH & Caprioli RM (2008) Molecular imaging of proteins in tissues by mass spectrometry. Proc Natl Acad Sci USA 105, 18126-18131
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 18126-18131
    • Seeley, E.H.1    Caprioli, R.M.2
  • 109
    • 0035048372 scopus 로고    scopus 로고
    • Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues
    • Stoeckli M, Chaurand P, Hallahan DE, et al. (2001) Imaging mass spectrometry: A new technology for the analysis of protein expression in mammalian tissues. Nat Med 7, 493-496
    • (2001) Nat Med , vol.7 , pp. 493-496
    • Stoeckli, M.1    Chaurand, P.2    Hallahan, D.E.3
  • 110
    • 71049165852 scopus 로고    scopus 로고
    • MALDI imaging mass spectrometry: State of the art technology in clinical proteomics
    • Franck J, Arafah K, Elayed M, et al. (2009) MALDI imaging mass spectrometry: State of the art technology in clinical proteomics. Mol Cell Proteomics 8, 2023-2033
    • (2009) Mol Cell Proteomics , vol.8 , pp. 2023-2033
    • Franck, J.1    Arafah, K.2    Elayed, M.3
  • 112
    • 35448978414 scopus 로고    scopus 로고
    • Identifying prostate carcinoma by MALDI-Imaging
    • Schwamborn K, Krieg RC, Reska M, et al. (2007) Identifying prostate carcinoma by MALDI-Imaging. Int J Mol Med 20, 155-159
    • (2007) Int J Mol Med , vol.20 , pp. 155-159
    • Schwamborn, K.1    Krieg, R.C.2    Reska, M.3
  • 113
    • 66849115115 scopus 로고    scopus 로고
    • Advanced proteomic technologies for cancer biomarker discovery
    • Wong SC, Chan CM, Ma BB, et al. (2009) Advanced proteomic technologies for cancer biomarker discovery. Expert Rev Proteomics 6, 123-134
    • (2009) Expert Rev Proteomics , vol.6 , pp. 123-134
    • Wong, S.C.1    Chan, C.M.2    Ma, B.B.3
  • 114
    • 33847018143 scopus 로고    scopus 로고
    • Identification of proteins directly from tissue: Situ tryptic digestions coupled with imaging mass spectrometry
    • Groseclose MR, Andersson M, Hardesty WM, et al. (2007) Identification of proteins directly from tissue: In situ tryptic digestions coupled with imaging mass spectrometry. J Mass Spectrom 42, 254-262
    • (2007) J Mass Spectrom , vol.42 , pp. 254-262
    • Groseclose, M.R.1    Andersson, M.2    Hardesty, W.M.3
  • 115
    • 34248230245 scopus 로고    scopus 로고
    • Direct analysis and MALDI imaging of formalin-fixed, paraffinembedded tissue sections
    • Lemaire R, Desmons A, Tabet JC, et al. (2007) Direct analysis and MALDI imaging of formalin-fixed, paraffinembedded tissue sections. J Proteome Res 6, 1295-1305
    • (2007) J Proteome Res , vol.6 , pp. 1295-1305
    • Lemaire, R.1    Desmons, A.2    Tabet, J.C.3
  • 116
    • 1442324454 scopus 로고    scopus 로고
    • Profiling and imaging proteins in tissue sections by MS
    • Chaurand P, Schwartz SA & Capriolo RM (2004) Profiling and imaging proteins in tissue sections by MS. Anal Chem 76, 87A-93A
    • (2004) Anal Chem , vol.76
    • Chaurand, P.1    Schwartz, S.A.2    Capriolo, R.M.3
  • 117
    • 13444304503 scopus 로고    scopus 로고
    • Imaging mass spectrometry: Principles and potentials
    • Chaurand P, Schwartz SA, Reyzer ML, et al. (2005) Imaging mass spectrometry: Principles and potentials. Toxicol Pathol 33, 92-101
    • (2005) Toxicol Pathol , vol.33 , pp. 92-101
    • Chaurand, P.1    Schwartz, S.A.2    Reyzer, M.L.3
  • 118
    • 67651202346 scopus 로고    scopus 로고
    • Towards single-molecule nanomechanical mass spectrometry
    • Naik AK, Hanay MS, Hiebert WK, et al. (2009) Towards single-molecule nanomechanical mass spectrometry. Nat Nanotechnol 4, 445-450
    • (2009) Nat Nanotechnol , vol.4 , pp. 445-450
    • Naik, A.K.1    Hanay, M.S.2    Hiebert, W.K.3
  • 119
    • 70350709997 scopus 로고    scopus 로고
    • Visual proteomics of the human pathogen Leptospira interrogans
    • Beck M, Malmstrom JA, Lange V, et al. (2009) Visual proteomics of the human pathogen Leptospira interrogans. Nat Methods 6, 817-823
    • (2009) Nat Methods , vol.6 , pp. 817-823
    • Beck, M.1    Malmstrom, J.A.2    Lange, V.3
  • 120
    • 79951518985 scopus 로고    scopus 로고
    • Mining the plasma proteome for disease applications across seven logs of protein abundance
    • Zhang Q, Faca V & Hanash S (2011) Mining the plasma proteome for disease applications across seven logs of protein abundance. J Proteome Res 10, 46-50
    • (2011) J Proteome Res , vol.10 , pp. 46-50
    • Zhang, Q.1    Faca, V.2    Hanash, S.3
  • 121
    • 77954523086 scopus 로고    scopus 로고
    • Options and considerations when selecting a quantitative proteomics strategy
    • Domon B & Aebersold R (2010) Options and considerations when selecting a quantitative proteomics strategy. Nat Biotechnol 28, 710-721
    • (2010) Nat Biotechnol , vol.28 , pp. 710-721
    • Domon, B.1    Aebersold, R.2
  • 123
    • 77957360551 scopus 로고    scopus 로고
    • Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives
    • Kussmann M, Panchaud A & Affolter M (2010) Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives. J Proteome Res 9, 4876-4887
    • (2010) J Proteome Res , vol.9 , pp. 4876-4887
    • Kussmann, M.1    Panchaud, A.2    Affolter, M.3
  • 124
    • 46649119060 scopus 로고    scopus 로고
    • Proteomics as a tool for the modelling of biological processes and biomarker development in nutrition research
    • de Roos B & McArdle HJ (2008) Proteomics as a tool for the modelling of biological processes and biomarker development in nutrition research. Br J Nutr 99 Suppl. 3, S66-S71
    • (2008) Br J Nutr , vol.99 , Issue.SUPPL. 3
    • De Roos, B.1    McArdle, H.J.2
  • 125
    • 26044473344 scopus 로고    scopus 로고
    • Proteomics in nutrition research: Principles, technologies and applications
    • Fuchs D, Winkelmann I, Johnson IT, et al. (2005) Proteomics in nutrition research: Principles, technologies and applications. Br J Nutr 94, 302-314
    • (2005) Br J Nutr , vol.94 , pp. 302-314
    • Fuchs, D.1    Winkelmann, I.2    Johnson, I.T.3
  • 126
    • 70349765534 scopus 로고    scopus 로고
    • Proteomics at the center of nutrigenomics: Comprehensive molecular understanding of dietary health effects
    • Kussmann M & Affolter M (2009) Proteomics at the center of nutrigenomics: Comprehensive molecular understanding of dietary health effects. Nutrition 25, 1085-1093
    • (2009) Nutrition , vol.25 , pp. 1085-1093
    • Kussmann, M.1    Affolter, M.2
  • 127
    • 34250845812 scopus 로고    scopus 로고
    • Nutritional proteomics: Methods and concepts for research in nutritional science
    • Schweigert FJ (2007) Nutritional proteomics: methods and concepts for research in nutritional science. Ann Nutr Metab 51, 99-107
    • (2007) Ann Nutr Metab , vol.51 , pp. 99-107
    • Schweigert, F.J.1
  • 128
    • 74049126605 scopus 로고    scopus 로고
    • Analysis of food proteins and peptides by mass spectrometry-based techniques
    • Mamone G, Picariello G, Caira S, et al. (2009) Analysis of food proteins and peptides by mass spectrometry-based techniques. J Chromatogr A 1216, 7130-7142
    • (2009) J Chromatogr A , vol.1216 , pp. 7130-7142
    • Mamone, G.1    Picariello, G.2    Caira, S.3
  • 129
    • 67650189497 scopus 로고    scopus 로고
    • Applications of proteomics in the study of inflammatory bowel diseases: Current status and future directions with available technologies
    • Alex P, Gucek M & Li X (2009) Applications of proteomics in the study of inflammatory bowel diseases: Current status and future directions with available technologies. Inflamm Bowel Dis 15, 616-629
    • (2009) Inflamm Bowel Dis , vol.15 , pp. 616-629
    • Alex, P.1    Gucek, M.2    Li, X.3
  • 130
    • 68949160878 scopus 로고    scopus 로고
    • Quantitative methods for food allergens: A review
    • Kirsch S, Fourdrilis S, Dobson R, et al. (2009) Quantitative methods for food allergens: A review. Anal Bioanal Chem 395, 57-67
    • (2009) Anal Bioanal Chem , vol.395 , pp. 57-67
    • Kirsch, S.1    Fourdrilis, S.2    Dobson, R.3
  • 132
    • 34250836975 scopus 로고    scopus 로고
    • Proteome analysis suggests that mitochondrial dysfunction in stressed endothelial cells is reversed by a soy extract and isolated isoflavones
    • Fuchs D, Dirscherl B, Schroot JH, et al. (2007) Proteome analysis suggests that mitochondrial dysfunction in stressed endothelial cells is reversed by a soy extract and isolated isoflavones. J Proteome Res 6, 2132-2142
    • (2007) J Proteome Res , vol.6 , pp. 2132-2142
    • Fuchs, D.1    Dirscherl, B.2    Schroot, J.H.3
  • 133
    • 69749123362 scopus 로고    scopus 로고
    • Ingestion of whey hydrolysate, casein, or soy protein isolate: Effects on mixed muscle protein synthesis at rest and following resistance exercise in young men
    • Tang JE, Moore DR, Kujbida GW, et al. (2009) Ingestion of whey hydrolysate, casein, or soy protein isolate: Effects on mixed muscle protein synthesis at rest and following resistance exercise in young men. J Appl Physiol 107, 987-992
    • (2009) J Appl Physiol , vol.107 , pp. 987-992
    • Tang, J.E.1    Moore, D.R.2    Kujbida, G.W.3
  • 134
    • 51049097278 scopus 로고    scopus 로고
    • The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease
    • Erdmann K, Cheung BW & Schroder H (2008) The possible roles of food-derived bioactive peptides in reducing the risk of cardiovascular disease. J Nutr Biochem 19, 643-654
    • (2008) J Nutr Biochem , vol.19 , pp. 643-654
    • Erdmann, K.1    Cheung, B.W.2    Schroder, H.3
  • 135
    • 49449094550 scopus 로고    scopus 로고
    • Human milk oligosaccharides: Evolution, structures and bioselectivity as substrates for intestinal bacteria
    • discussion 218-222
    • German JB, Freeman SL, Lebrilla CB, et al. (2008) Human milk oligosaccharides: Evolution, structures and bioselectivity as substrates for intestinal bacteria. Nestle Nutr Workshop Ser Pediatr Program 62, 205-218; discussion 218-222
    • (2008) Nestle Nutr Workshop ser Pediatr Program , vol.62 , pp. 205-218
    • German, J.B.1    Freeman, S.L.2    Lebrilla, C.B.3
  • 136
    • 70449705857 scopus 로고    scopus 로고
    • OMICSrooted studies of milk proteins, oligosaccharides and lipids
    • Casado B, Affolter M & Kussmann M (2009) OMICSrooted studies of milk proteins, oligosaccharides and lipids. J Proteomics 73, 196-208
    • (2009) J Proteomics , vol.73 , pp. 196-208
    • Casado, B.1    Affolter, M.2    Kussmann, M.3
  • 137
  • 138
    • 27144501029 scopus 로고    scopus 로고
    • Milk proteins: General and historical aspects
    • 3rd ed. [PF Fox & PLH McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • Fox PF (2003) Milk proteins: General and historical aspects. In Advanced Dairy Chemistry: Proteins, 3rd ed., pp. 1-48 [PF Fox & PLH McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • (2003) Advanced Dairy Chemistry: Proteins , pp. 1-48
    • Fox, P.F.1
  • 139
    • 70349512735 scopus 로고    scopus 로고
    • Molecular and biotechnological advances in milk proteins in relation to human health
    • Kanwar JR, Kanwar RK, Sun X, et al. (2009) Molecular and biotechnological advances in milk proteins in relation to human health. Curr Protein Pept Sci 10, 308-338
    • (2009) Curr Protein Pept Sci , vol.10 , pp. 308-338
    • Kanwar, J.R.1    Kanwar, R.K.2    Sun, X.3
  • 140
    • 56549116403 scopus 로고    scopus 로고
    • Comprehensive proteomic analysis of the human milk proteome: Contribution of protein fractionation
    • Mange A, Bellet V, Tuaillon E, et al. (2008) Comprehensive proteomic analysis of the human milk proteome: Contribution of protein fractionation. J Chromatogr B Analyt Technol Biomed Life Sci 876, 252-256
    • (2008) J Chromatogr B Analyt Technol Biomed Life Sci , vol.876 , pp. 252-256
    • Mange, A.1    Bellet, V.2    Tuaillon, E.3
  • 141
    • 36248966962 scopus 로고    scopus 로고
    • Quantitation of proteins in milk and milk products
    • 3rd ed. [PF Fox & PL McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • Tremblay L, Laporte M, Leonil J, et al. (2003) Quantitation of proteins in milk and milk products. In Advanced Dairy Chemistry: Proteins, 3rd ed., pp. 49-138 [PF Fox & PL McSweeney, editors]. New York: Kluwer Academic/Plenum Publishers
    • (2003) Advanced Dairy Chemistry: Proteins , pp. 49-138
    • Tremblay, L.1    Laporte, M.2    Leonil, J.3
  • 142
    • 36248998834 scopus 로고    scopus 로고
    • Fractionation of bovine whey proteins and characterisation by proteomic techniques
    • Fong YP, Norris CS & Palmano KP (2008) Fractionation of bovine whey proteins and characterisation by proteomic techniques. Int Dairy J 18, 23-46
    • (2008) Int Dairy J , vol.18 , pp. 23-46
    • Fong, Y.P.1    Norris, C.S.2    Palmano, K.P.3
  • 143
    • 60649112096 scopus 로고    scopus 로고
    • Comparison of electrospray and matrix-assisted laser desorption ionization on the same hybrid quadrupole time-of-flight tandem mass spectrometer: Application to bidimensional liquid chromatography of proteins from bovine milk fraction
    • Molle D, Jardin J, Piot M, et al. (2009) Comparison of electrospray and matrix-assisted laser desorption ionization on the same hybrid quadrupole time-of-flight tandem mass spectrometer: Application to bidimensional liquid chromatography of proteins from bovine milk fraction. J Chromatogr A 1216, 2424-2432
    • (2009) J Chromatogr A , vol.1216 , pp. 2424-2432
    • Molle, D.1    Jardin, J.2    Piot, M.3
  • 144
    • 77950517341 scopus 로고    scopus 로고
    • Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome
    • Affolter M, Grass L, Vanrobaeys F, et al. (2010) Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome. J Proteomics 73, 1079-1088
    • (2010) J Proteomics , vol.73 , pp. 1079-1088
    • Affolter, M.1    Grass, L.2    Vanrobaeys, F.3
  • 145
    • 64649104514 scopus 로고    scopus 로고
    • Identification and quantification of alphaS1, alphaS2, beta, and kappacaseins in water buffalo milk by reverse phase-high performance liquid chromatography and mass spectrometry
    • Feligini M, Bonizzi I, Buffoni JN, et al. (2009) Identification and quantification of alphaS1, alphaS2, beta, and kappacaseins in water buffalo milk by reverse phase-high performance liquid chromatography and mass spectrometry. J Agric Food Chem 57, 2988-2992
    • (2009) J Agric Food Chem , vol.57 , pp. 2988-2992
    • Feligini, M.1    Bonizzi, I.2    Buffoni, J.N.3
  • 146
    • 0012252007 scopus 로고    scopus 로고
    • Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage
    • Kjeldsen F, Haselmann KF, Budnik BA, et al. (2003) Complete characterization of posttranslational modification sites in the bovine milk protein PP3 by tandem mass spectrometry with electron capture dissociation as the last stage. Anal Chem 75, 2355-2361
    • (2003) Anal Chem , vol.75 , pp. 2355-2361
    • Kjeldsen, F.1    Haselmann, K.F.2    Budnik, B.A.3
  • 147
    • 67649221525 scopus 로고    scopus 로고
    • Twodimensional cartography of equine beta-casein variants achieved by isolation of phosphorylation isoforms and control of the deamidation phenomenon
    • Mateos A, Girardet JM, Molle D, et al. (2009) Twodimensional cartography of equine beta-casein variants achieved by isolation of phosphorylation isoforms and control of the deamidation phenomenon. J Dairy Sci 92, 2389-2399
    • (2009) J Dairy Sci , vol.92 , pp. 2389-2399
    • Mateos, A.1    Girardet, J.M.2    Molle, D.3
  • 148
    • 0035987501 scopus 로고    scopus 로고
    • Identification of caseins in goat milk
    • Roncada P, Gaviraghi A, Liberatori S, et al. (2002) Identification of caseins in goat milk. Proteomics 2, 723-726
    • (2002) Proteomics , vol.2 , pp. 723-726
    • Roncada, P.1    Gaviraghi, A.2    Liberatori, S.3
  • 149
    • 52649147543 scopus 로고    scopus 로고
    • A proteomic characterization of water buffalo milk fractions describing PTM of major species and the identification of minor components involved in nutrient delivery and defense against pathogens
    • DAmbrosio C, Arena S, Salzano AM, et al. (2008) A proteomic characterization of water buffalo milk fractions describing PTM of major species and the identification of minor components involved in nutrient delivery and defense against pathogens. Proteomics 8, 3657-3666
    • (2008) Proteomics , vol.8 , pp. 3657-3666
    • Dambrosio, C.1    Arena, S.2    Salzano, A.M.3
  • 150
    • 14344257501 scopus 로고    scopus 로고
    • Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry
    • Harvey DJ (2005) Proteomic analysis of glycosylation: Structural determination of N- and O-linked glycans by mass spectrometry. Expert Rev Proteomics 2, 87-101
    • (2005) Expert Rev Proteomics , vol.2 , pp. 87-101
    • Harvey, D.J.1
  • 151
    • 14744280296 scopus 로고    scopus 로고
    • Application of Fourier transform ion cyclotron resonance mass spectrometry to oligosaccharides
    • Park Y & Lebrilla CB (2005) Application of Fourier transform ion cyclotron resonance mass spectrometry to oligosaccharides. Mass Spectrom Rev 24, 232-264
    • (2005) Mass Spectrom Rev , vol.24 , pp. 232-264
    • Park, Y.1    Lebrilla, C.B.2
  • 152
    • 0031845193 scopus 로고    scopus 로고
    • Protective function of proteins and lipids in human milk
    • Hamosh M (1998) Protective function of proteins and lipids in human milk. Biol Neonate 74, 163-176
    • (1998) Biol Neonate , vol.74 , pp. 163-176
    • Hamosh, M.1
  • 153
    • 0032980624 scopus 로고    scopus 로고
    • Human milk glycoconjugates that inhibit pathogens
    • Newburg DS (1999) Human milk glycoconjugates that inhibit pathogens. Curr Med Chem 6, 117-127
    • (1999) Curr Med Chem , vol.6 , pp. 117-127
    • Newburg, D.S.1
  • 154
    • 33846953590 scopus 로고    scopus 로고
    • Protection of the neonate by the innate immune system of developing gut and of human milk
    • Newburg DS & Walker WA (2007) Protection of the neonate by the innate immune system of developing gut and of human milk. Pediatr Res 61, 2-8
    • (2007) Pediatr Res , vol.61 , pp. 2-8
    • Newburg, D.S.1    Walker, W.A.2
  • 155
    • 0033024052 scopus 로고    scopus 로고
    • Protective function of human milk: The milk fat globule
    • Hamosh M, Peterson JA, Henderson TR, et al. (1999) Protective function of human milk: The milk fat globule. Semin Perinatol 23, 242-249
    • (1999) Semin Perinatol , vol.23 , pp. 242-249
    • Hamosh, M.1    Peterson, J.A.2    Henderson, T.R.3
  • 156
    • 0031844095 scopus 로고    scopus 로고
    • Glycoproteins of the human milk fat globule in the protection of the breast-fed infant against infections
    • Peterson JA, Patton S & Hamosh M (1998) Glycoproteins of the human milk fat globule in the protection of the breast-fed infant against infections. Biol Neonate 74, 143-162
    • (1998) Biol Neonate , vol.74 , pp. 143-162
    • Peterson, J.A.1    Patton, S.2    Hamosh, M.3
  • 157
    • 0035701947 scopus 로고    scopus 로고
    • Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane
    • Peterson JA, Scallan CD, Ceriani RL, et al. (2001) Structural and functional aspects of three major glycoproteins of the human milk fat globule membrane. Adv Exp Med Biol 501, 179-187
    • (2001) Adv Exp Med Biol , vol.501 , pp. 179-187
    • Peterson, J.A.1    Scallan, C.D.2    Ceriani, R.L.3
  • 158
    • 53549093906 scopus 로고    scopus 로고
    • Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry
    • Picariello G, Ferranti P, Mamone G, et al. (2008) Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics 8, 3833-3847
    • (2008) Proteomics , vol.8 , pp. 3833-3847
    • Picariello, G.1    Ferranti, P.2    Mamone, G.3
  • 159
    • 0141918811 scopus 로고    scopus 로고
    • Lactoferrin - A multifunctional protein with antimicrobial properties
    • Farnaud S & Evans RW (2003) Lactoferrin - a multifunctional protein with antimicrobial properties. Mol Immunol 40, 395-405
    • (2003) Mol Immunol , vol.40 , pp. 395-405
    • Farnaud, S.1    Evans, R.W.2
  • 160
    • 0026716209 scopus 로고
    • Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin
    • Crouch SP, Slater KJ & Fletcher J (1992) Regulation of cytokine release from mononuclear cells by the iron-binding protein lactoferrin. Blood 80, 235-240
    • (1992) Blood , vol.80 , pp. 235-240
    • Crouch, S.P.1    Slater, K.J.2    Fletcher, J.3
  • 161
    • 0030469762 scopus 로고    scopus 로고
    • Antihypertensive peptides are present in aorta after oral administration of sour milk containing these peptides to spontaneously hypertensive rats
    • Masuda O, Nakamura Y & Takano T (1996) Antihypertensive peptides are present in aorta after oral administration of sour milk containing these peptides to spontaneously hypertensive rats. J Nutr 126, 3063-3068
    • (1996) J Nutr , vol.126 , pp. 3063-3068
    • Masuda, O.1    Nakamura, Y.2    Takano, T.3
  • 164
    • 18344387591 scopus 로고    scopus 로고
    • Probiotics that modify disease risk
    • Salminen SJ, Gueimonde M & Isolauri E (2005) Probiotics that modify disease risk. J Nutr 135, 1294-1298
    • (2005) J Nutr , vol.135 , pp. 1294-1298
    • Salminen, S.J.1    Gueimonde, M.2    Isolauri, E.3
  • 165
    • 67649095219 scopus 로고    scopus 로고
    • Coculture of Bifidobacterium longum and Bifidobacterium breve alters their protein expression profiles and enzymatic activities
    • Ruiz L, Sanchez B, de Los Reyes-Gavilan CG, et al. (2009) Coculture of Bifidobacterium longum and Bifidobacterium breve alters their protein expression profiles and enzymatic activities. Int J Food Microbiol 133, 148-153
    • (2009) Int J Food Microbiol , vol.133 , pp. 148-153
    • Ruiz, L.1    Sanchez, B.2    De Los Reyes-Gavilan, C.G.3
  • 166
    • 67650739490 scopus 로고    scopus 로고
    • Proteomic analysis of cell surface-associated proteins from probiotic Lactobacillus plantarum
    • Beck HC, Madsen SM, Glenting J, et al. (2009) Proteomic analysis of cell surface-associated proteins from probiotic Lactobacillus plantarum. FEMS Microbiol Lett 297, 61-66
    • (2009) FEMS Microbiol Lett , vol.297 , pp. 61-66
    • Beck, H.C.1    Madsen, S.M.2    Glenting, J.3
  • 167
    • 65949115304 scopus 로고    scopus 로고
    • 2-DE and MS analysis of key proteins in the adhesion of Lactobacillus plantarum, a first step toward early selection of probiotics based on bacterial biomarkers
    • Izquierdo E, Horvatovich P, Marchioni E, et al. (2009) 2-DE and MS analysis of key proteins in the adhesion of Lactobacillus plantarum, a first step toward early selection of probiotics based on bacterial biomarkers. Electrophoresis 30, 949-956
    • (2009) Electrophoresis , vol.30 , pp. 949-956
    • Izquierdo, E.1    Horvatovich, P.2    Marchioni, E.3
  • 169
    • 43049179748 scopus 로고    scopus 로고
    • Food allergies and hypersensitivity: A review of pharmacotherapy and therapeutic strategies
    • Burks W, Kulis M & Pons L (2008) Food allergies and hypersensitivity: A review of pharmacotherapy and therapeutic strategies. Expert Opin Pharmacother 9, 1145-1152
    • (2008) Expert Opin Pharmacother , vol.9 , pp. 1145-1152
    • Burks, W.1    Kulis, M.2    Pons, L.3
  • 170
    • 0037294555 scopus 로고    scopus 로고
    • Food allergy: An overview
    • Kagan RS (2003) Food allergy: An overview. Environ Health Perspect 111, 223-225
    • (2003) Environ Health Perspect , vol.111 , pp. 223-225
    • Kagan, R.S.1
  • 171
    • 0034969698 scopus 로고    scopus 로고
    • Introducing chemists to food allergy
    • Ortolani C, Ispano M, Scibilia J, et al. (2001) Introducing chemists to food allergy. Allergy 56, Suppl., 67, 5-8
    • (2001) Allergy , vol.56 , Issue.SUPPL. 67 , pp. 5-8
    • Ortolani, C.1    Ispano, M.2    Scibilia, J.3
  • 172
    • 1142287446 scopus 로고    scopus 로고
    • Methods for allergen analysis in food: A review
    • Poms RE, Klein CL & Anklam E (2004) Methods for allergen analysis in food: A review. Food Addit Contam 21, 1-31
    • (2004) Food Addit Contam , vol.21 , pp. 1-31
    • Poms, R.E.1    Klein, C.L.2    Anklam, E.3
  • 173
    • 67349171915 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics methods for analysis of food allergens
    • Monaci L & Visconti A (2009) Mass spectrometry-based proteomics methods for analysis of food allergens. Trends Anal. Chem. 28, 581-591
    • (2009) Trends Anal. Chem. , vol.28 , pp. 581-591
    • Monaci, L.1    Visconti, A.2
  • 174
    • 34548324638 scopus 로고    scopus 로고
    • Proteomic analysis of wheat flour allergens
    • Akagawa M, Handoyo T, Ishii T, et al. (2007) Proteomic analysis of wheat flour allergens. J Agric Food Chem 55, 6863-6870
    • (2007) J Agric Food Chem , vol.55 , pp. 6863-6870
    • Akagawa, M.1    Handoyo, T.2    Ishii, T.3
  • 175
    • 42549123065 scopus 로고    scopus 로고
    • Proteomic analysis of wheat proteins recognized by IgE antibodies of allergic patients
    • Sotkovsky P, Hubalek M, Hernychova L, et al. (2008) Proteomic analysis of wheat proteins recognized by IgE antibodies of allergic patients. Proteomics 8, 1677-1691
    • (2008) Proteomics , vol.8 , pp. 1677-1691
    • Sotkovsky, P.1    Hubalek, M.2    Hernychova, L.3
  • 176
    • 34250890007 scopus 로고    scopus 로고
    • Proteomic analysis of the major soluble components in Annurca apple flesh
    • Guarino C, Arena S, De Simone L, et al. (2007) Proteomic analysis of the major soluble components in Annurca apple flesh. Mol Nutr Food Res 51, 255-262
    • (2007) Mol Nutr Food Res , vol.51 , pp. 255-262
    • Guarino, C.1    Arena, S.2    De Simone, L.3
  • 177
    • 63349098136 scopus 로고    scopus 로고
    • Searching for allergens in maize kernels via proteomic tools
    • Fasoli E, Pastorello EA, Farioli L, et al. (2009) Searching for allergens in maize kernels via proteomic tools. J Proteomics 72, 501-510
    • (2009) J Proteomics , vol.72 , pp. 501-510
    • Fasoli, E.1    Pastorello, E.A.2    Farioli, L.3
  • 178
    • 0036968792 scopus 로고    scopus 로고
    • Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens
    • Beyer K, Bardina L, Grishina G, et al. (2002) Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: Seed storage proteins as common food allergens. J Allergy Clin Immunol 110, 154-159
    • (2002) J Allergy Clin Immunol , vol.110 , pp. 154-159
    • Beyer, K.1    Bardina, L.2    Grishina, G.3
  • 179
  • 180
    • 67651233459 scopus 로고    scopus 로고
    • 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents
    • Schmidt H, Gelhaus C, Latendorf T, et al. (2009) 2-D DIGE analysis of the proteome of extracts from peanut variants reveals striking differences in major allergen contents. Proteomics 9, 3507-3521
    • (2009) Proteomics , vol.9 , pp. 3507-3521
    • Schmidt, H.1    Gelhaus, C.2    Latendorf, T.3
  • 181
    • 63649131272 scopus 로고    scopus 로고
    • Validation of gel-free, label-free quantitative proteomics approaches: Applications for seed allergen profiling
    • Stevenson SE, Chu Y, Ozias-Akins P, et al. (2009) Validation of gel-free, label-free quantitative proteomics approaches: Applications for seed allergen profiling. J Proteomics 72, 555-566
    • (2009) J Proteomics , vol.72 , pp. 555-566
    • Stevenson, S.E.1    Chu, Y.2    Ozias-Akins, P.3
  • 182
    • 69549116025 scopus 로고    scopus 로고
    • Nutrition proteomics and biomarker discovery
    • De Roos B (2009) Nutrition proteomics and biomarker discovery. Expert Rev Proteomics 6, 349-351
    • (2009) Expert Rev Proteomics , vol.6 , pp. 349-351
    • De Roos, B.1
  • 183
    • 0037043658 scopus 로고    scopus 로고
    • Inflammatory bowel disease
    • Podolsky DK (2002) Inflammatory bowel disease. N Engl J Med 347, 417-429
    • (2002) N Engl J Med , vol.347 , pp. 417-429
    • Podolsky, D.K.1
  • 184
    • 33947603233 scopus 로고    scopus 로고
    • Differential protein expression profile in the intestinal epithelium from patients with inflammatory bowel disease
    • Shkoda A, Werner T, Daniel H, et al. (2007) Differential protein expression profile in the intestinal epithelium from patients with inflammatory bowel disease. J Proteome Res 6, 1114-1125
    • (2007) J Proteome Res , vol.6 , pp. 1114-1125
    • Shkoda, A.1    Werner, T.2    Daniel, H.3
  • 185
    • 1942423666 scopus 로고    scopus 로고
    • Paradoxical decrease of mitochondrial DNA deletions in epithelial cells of active ulcerative colitis patients
    • Fukushima K & Fiocchi C (2004) Paradoxical decrease of mitochondrial DNA deletions in epithelial cells of active ulcerative colitis patients. Am J Physiol Gastrointest Liver Physiol 286, G804-G813
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.286
    • Fukushima, K.1    Fiocchi, C.2
  • 186
    • 0018855591 scopus 로고
    • The colonic epithelium in ulcerative colitis: An energy-deficiency disease?
    • Roediger WE (1980) The colonic epithelium in ulcerative colitis: An energy-deficiency disease? Lancet 2, 712-715
    • (1980) Lancet , vol.2 , pp. 712-715
    • Roediger, W.E.1
  • 187
    • 33947505382 scopus 로고    scopus 로고
    • Biomarker discovery for inflammatory bowel disease, using proteomic serum profiling
    • Meuwis MA, Fillet M, Geurts P, et al. (2007) Biomarker discovery for inflammatory bowel disease, using proteomic serum profiling. Biochem Pharmacol 73, 1422-1433
    • (2007) Biochem Pharmacol , vol.73 , pp. 1422-1433
    • Meuwis, M.A.1    Fillet, M.2    Geurts, P.3
  • 188
    • 53149114839 scopus 로고    scopus 로고
    • Phagocytespecific S100 proteins are released from affected mucosa and promote immune responses during inflammatory bowel disease
    • Foell D, Wittkowski H, Ren Z, et al. (2008) Phagocytespecific S100 proteins are released from affected mucosa and promote immune responses during inflammatory bowel disease. J Pathol 216, 183-192
    • (2008) J Pathol , vol.216 , pp. 183-192
    • Foell, D.1    Wittkowski, H.2    Ren, Z.3
  • 189
    • 67651212322 scopus 로고    scopus 로고
    • Nutritional aspects in inflammatory bowel disease
    • Shamir R (2009) Nutritional aspects in inflammatory bowel disease. J Pediatr Gastroenterol Nutr 48, Suppl. 2, S86-S88
    • (2009) J Pediatr Gastroenterol Nutr , vol.48 , Issue.SUPPL. 2
    • Shamir, R.1
  • 190
    • 34347396040 scopus 로고    scopus 로고
    • Nutrition assessment of patients with inflammatory bowel disease
    • Vagianos K, Bector S, McConnell J, et al. (2007) Nutrition assessment of patients with inflammatory bowel disease. JPEN J Parenter Enteral Nutr 31, 311-319
    • (2007) JPEN J Parenter Enteral Nutr , vol.31 , pp. 311-319
    • Vagianos, K.1    Bector, S.2    McConnell, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.