메뉴 건너뛰기




Volumn 2, Issue 4, 2011, Pages 355-364

Proteomics and systems biology: Current and future applications in the nutritional sciences

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MODEL; BIOLOGY; FORECASTING; GENOMICS; HUMAN; METABOLOMICS; METHODOLOGY; NUTRITIONAL SCIENCE; PROTEOMICS; REVIEW; SYSTEM ANALYSIS; SYSTEMS BIOLOGY;

EID: 84861681913     PISSN: 21618313     EISSN: 21565376     Source Type: Journal    
DOI: 10.3945/an.111.000554     Document Type: Review
Times cited : (37)

References (97)
  • 1
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: a brief overview
    • Kitano H. Systems biology: a brief overview. Science. 2002;295:1662-4
    • (2002) Science. , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 3
    • 38449101948 scopus 로고    scopus 로고
    • Application of metabolic flux analysis to identify the mechanisms of free fatty acid toxicity to human hepatoma cell line
    • Srivastava S, Chan C. Application of metabolic flux analysis to identify the mechanisms of free fatty acid toxicity to human hepatoma cell line. Biotechnol Bioeng. 2008;99:399-410.
    • (2008) Biotechnol Bioeng. , vol.99 , pp. 399-410
    • Srivastava, S.1    Chan, C.2
  • 5
    • 33745805507 scopus 로고    scopus 로고
    • Computational model of in vivo human energy metabolism during semistarvation and refeeding
    • Hall KD. Computational model of in vivo human energy metabolism during semistarvation and refeeding. Am J Physiol Endocrinol Metab. 2006;291:E23-37.
    • (2006) Am J Physiol Endocrinol Metab. , vol.291
    • Hall, K.D.1
  • 6
    • 0003445619 scopus 로고
    • General system theory; foundations, development, applications
    • New York: G. Braziller
    • Bertalanffy LV. General system theory; foundations, development, applications. New York: G. Braziller; 1969.
    • (1969)
    • Bertalanffy, L.V.1
  • 7
    • 0004108421 scopus 로고
    • Cybernetics
    • New York: J. Wiley
    • Wiener N. Cybernetics. New York: J. Wiley; 1948.
    • (1948)
    • Wiener, N.1
  • 8
    • 0037079054 scopus 로고    scopus 로고
    • Computational systems biology
    • Kitano H. Computational systems biology. Nature. 2002;420:206-10.
    • (2002) Nature. , vol.420 , pp. 206-210
    • Kitano, H.1
  • 9
    • 7444253428 scopus 로고    scopus 로고
    • Systems biology and new technologies enable predictive and preventative medicine
    • Hood L, Heath JR, Phelps ME, Lin B. Systems biology and new technologies enable predictive and preventative medicine. Science. 2004;306:640-3.
    • (2004) Science. , vol.306 , pp. 640-643
    • Hood, L.1    Heath, J.R.2    Phelps, M.E.3    Lin, B.4
  • 10
    • 77949773550 scopus 로고    scopus 로고
    • Towards genome-scale signalling-network reconstructions
    • Hyduke DR, Palsson BO. Towards genome-scale signalling-network reconstructions. Nat Rev Genet. 2010;11:297-307.
    • (2010) Nat Rev Genet. , vol.11 , pp. 297-307
    • Hyduke, D.R.1    Palsson, B.O.2
  • 13
    • 58549110252 scopus 로고    scopus 로고
    • Stochastic modelling for quantitative description of heterogeneous biological systems
    • Wilkinson DJ. Stochastic modelling for quantitative description of heterogeneous biological systems. Nat Rev Genet. 2009;10:122-33.
    • (2009) Nat Rev Genet. , vol.10 , pp. 122-133
    • Wilkinson, D.J.1
  • 14
    • 40149110854 scopus 로고    scopus 로고
    • The signaling petri net-based simulator: a non-parametric strategy for characterizing the dynamics of cell-specific signaling networks
    • Ruths D, Muller M, Tseng JT, Nakhleh L, Ram PT. The signaling petri net-based simulator: a non-parametric strategy for characterizing the dynamics of cell-specific signaling networks. PLOS Comput Biol. 2008;4:e1000005.
    • (2008) PLOS Comput Biol. , vol.4
    • Ruths, D.1    Muller, M.2    Tseng, J.T.3    Nakhleh, L.4    Ram, P.T.5
  • 16
    • 78149296035 scopus 로고    scopus 로고
    • Patterns of human gene expression variance show strong associations with signaling network hierarchy
    • Komurov K, Ram PT. Patterns of human gene expression variance show strong associations with signaling network hierarchy. BMC Syst Biol. 2010;4:154.
    • (2010) BMC Syst Biol. , vol.4 , pp. 154
    • Komurov, K.1    Ram, P.T.2
  • 17
  • 18
    • 34347258175 scopus 로고    scopus 로고
    • Quantitative prediction of cellular metabolism with constraint-based models: the COBRA Toolbox
    • Becker SA, Feist AM, Mo ML, Hannum G, Palsson BO, Herrgard MJ. Quantitative prediction of cellular metabolism with constraint-based models: the COBRA Toolbox. Nat Protoc. 2007;2:727-38.
    • (2007) Nat Protoc. , vol.2 , pp. 727-738
    • Becker, S.A.1    Feist, A.M.2    Mo, M.L.3    Hannum, G.4    Palsson, B.O.5    Herrgard, M.J.6
  • 22
    • 77952674482 scopus 로고    scopus 로고
    • Metabolic network topology reveals transcriptional regulatory signatures of type 2 diabetes
    • Zelezniak A, Pers TH, Soares S, Patti ME, Patil KR. Metabolic network topology reveals transcriptional regulatory signatures of type 2 diabetes. PLOS Comput Biol. 2010;6:e1000729.
    • (2010) PLOS Comput Biol. , vol.6
    • Zelezniak, A.1    Pers, T.H.2    Soares, S.3    Patti, M.E.4    Patil, K.R.5
  • 23
    • 14544268137 scopus 로고    scopus 로고
    • Uncovering transcriptional regulation of metabolism by using metabolic network topology
    • Patil KR, Nielsen J. Uncovering transcriptional regulation of metabolism by using metabolic network topology. Proc Natl Acad Sci USA. 2005;102:2685-9.
    • (2005) Proc Natl Acad Sci USA. , vol.102 , pp. 2685-2689
    • Patil, K.R.1    Nielsen, J.2
  • 26
    • 77957745068 scopus 로고    scopus 로고
    • Gene regulatory network reveals oxidative stress as the underlying molecular mechanism of type 2 diabetes and hypertension
    • Jesmin J, Rashid MS, Jamil H, Hontecillas R, Bassaganya-Riera J. Gene regulatory network reveals oxidative stress as the underlying molecular mechanism of type 2 diabetes and hypertension. BMC Med Genomics. 2010;3:45.
    • (2010) BMC Med Genomics. , vol.3 , pp. 45
    • Jesmin, J.1    Rashid, M.S.2    Jamil, H.3    Hontecillas, R.4    Bassaganya-Riera, J.5
  • 27
    • 78649769648 scopus 로고    scopus 로고
    • Revealing the molecular relationship between type 2 diabetes and the metabolic changes induced by a very-low-carbohydrate low-fat ketogenic diet
    • Farres J, Pujol A, Coma M, Ruiz JL, Naval J, Mas JM, Molins A, Fondevila J, Aloy P. Revealing the molecular relationship between type 2 diabetes and the metabolic changes induced by a very-low-carbohydrate low-fat ketogenic diet. Nutr Metab (Lond). 2010;7:88.
    • (2010) Nutr Metab (Lond) , vol.7 , pp. 88
    • Farres, J.1    Pujol, A.2    Coma, M.3    Ruiz, J.L.4    Naval, J.5    Mas, J.M.6    Molins, A.7    Fondevila, J.8    Aloy, P.9
  • 30
    • 77957865001 scopus 로고    scopus 로고
    • Identifying molecular effects of diet through systems biology: influence of herring diet on sterol metabolism and protein turnover in mice
    • Nookaew I, Gabrielsson BG, Holmang A, Sandberg AS, Nielsen J. Identifying molecular effects of diet through systems biology: influence of herring diet on sterol metabolism and protein turnover in mice. PLoS ONE. 2010;5:e12361.
    • (2010) PLoS ONE , vol.5
    • Nookaew, I.1    Gabrielsson, B.G.2    Holmang, A.3    Sandberg, A.S.4    Nielsen, J.5
  • 31
    • 79551582182 scopus 로고    scopus 로고
    • SurreyFBA: a command line tool and graphics user interface for constraint-based modeling of genome-scale metabolic reaction networks
    • Gevorgyan A, Bushell ME, Avignone-Rossa C, Kierzek AM. SurreyFBA: a command line tool and graphics user interface for constraint-based modeling of genome-scale metabolic reaction networks. Bioinformatics. 2011;27:433-4.
    • (2011) Bioinformatics. , vol.27 , pp. 433-434
    • Gevorgyan, A.1    Bushell, M.E.2    Avignone-Rossa, C.3    Kierzek, A.M.4
  • 32
    • 61449134182 scopus 로고    scopus 로고
    • Identification of potential pathway mediation targets in Toll-like receptor signaling
    • Li F, Thiele I, Jamshidi N, Palsson BO. Identification of potential pathway mediation targets in Toll-like receptor signaling. PLOS Comput Biol. 2009;5:e1000292.
    • (2009) PLOS Comput Biol. , vol.5
    • Li, F.1    Thiele, I.2    Jamshidi, N.3    Palsson, B.O.4
  • 33
    • 4644335402 scopus 로고    scopus 로고
    • Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine
    • Weston AD, Hood L. Systems biology, proteomics, and the future of health care: toward predictive, preventative, and personalized medicine. J Proteome Res. 2004;3:179-96.
    • (2004) J Proteome Res. , vol.3 , pp. 179-196
    • Weston, A.D.1    Hood, L.2
  • 34
    • 84984042980 scopus 로고
    • Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry
    • Tanaka K, Waki H, Ido Y, Akita S, Yoshida Y, Yoshida T. Protein and polymer analyses up to m/z 100 000 by laser ionization time-of flight mass spectrometry. Rapid Commun Mass Spectrom. 1988;2:151-3.
    • (1988) Rapid Commun Mass Spectrom. , vol.2 , pp. 151-153
    • Tanaka, K.1    Waki, H.2    Ido, Y.3    Akita, S.4    Yoshida, Y.5    Yoshida, T.6
  • 35
    • 33748168091 scopus 로고
    • Electrospray ion source. Another variation on the free-jet theme
    • Yamashita M, Fenn JB. Electrospray ion source. Another variation on the free-jet theme. J Phys Chem. 1984;88:4451-9.
    • (1984) J Phys Chem. , vol.88 , pp. 4451-4459
    • Yamashita, M.1    Fenn, J.B.2
  • 36
    • 0032161546 scopus 로고    scopus 로고
    • Simplification of product ion spectra derived from multiply charged parent ions via ion/ion chemistry
    • Stephenson JL Jr, McLuckey SA. Simplification of product ion spectra derived from multiply charged parent ions via ion/ion chemistry. Anal Chem. 1998;70:3533-44.
    • (1998) Anal Chem. , vol.70 , pp. 3533-3544
    • Stephenson Jr., J.L.1    McLuckey, S.A.2
  • 37
    • 68949206409 scopus 로고    scopus 로고
    • Applying mass spectrometry-based proteomics to genetics, genomics and network biology
    • Gstaiger M, Aebersold R. Applying mass spectrometry-based proteomics to genetics, genomics and network biology. Nat Rev Genet. 2009;10:617-27.
    • (2009) Nat Rev Genet. , vol.10 , pp. 617-627
    • Gstaiger, M.1    Aebersold, R.2
  • 38
    • 78649438767 scopus 로고    scopus 로고
    • Top-down protein characterization facilitated by ion/ion reactions on a quadrupole/time of flight platform
    • Huang TY, McLuckey SA. Top-down protein characterization facilitated by ion/ion reactions on a quadrupole/time of flight platform. Proteomics. 2010;10:3577-88.
    • (2010) Proteomics. , vol.10 , pp. 3577-3588
    • Huang, T.Y.1    McLuckey, S.A.2
  • 39
    • 78649423856 scopus 로고    scopus 로고
    • High-efficiency nano-and micro-HPLC-high-resolution Orbitrap-MS platform for top-down proteomics
    • Mohr J, Swart R, Samonig M, Bohm G, Huber CG. High-efficiency nano-and micro-HPLC-high-resolution Orbitrap-MS platform for top-down proteomics. Proteomics. 2010;10:3598-609.
    • (2010) Proteomics. , vol.10 , pp. 3598-3609
    • Mohr, J.1    Swart, R.2    Samonig, M.3    Bohm, G.4    Huber, C.G.5
  • 40
    • 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;6:4688-703.
    • (2006) Proteomics. , vol.6 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 43
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R. Mass spectrometry and protein analysis. Science. 2006;312:212-7.
    • (2006) Science. , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 44
    • 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
  • 45
    • 0000944563 scopus 로고    scopus 로고
    • Electron capture dissociation of multiply charged protein cations. A nonergodic process
    • Zubarev RA, Kelleher NL, McLafferty FW. Electron capture dissociation of multiply charged protein cations. A nonergodic process. J Am Chem Soc. 1998;120:3265-6.
    • (1998) J Am Chem Soc. , vol.120 , pp. 3265-3266
    • Zubarev, R.A.1    Kelleher, N.L.2    McLafferty, F.W.3
  • 46
    • 34249022000 scopus 로고    scopus 로고
    • Implementation of electron-transfer dissociation on a hybrid linear ion traporbitrap mass spectrometer
    • McAlister GC, Phanstiel D, Good DM, Berggren WT, Coon JJ. Implementation of electron-transfer dissociation on a hybrid linear ion traporbitrap mass spectrometer. Anal Chem. 2007;79:3525-34.
    • (2007) Anal Chem. , vol.79 , pp. 3525-3534
    • McAlister, G.C.1    Phanstiel, D.2    Good, D.M.3    Berggren, W.T.4    Coon, J.J.5
  • 47
    • 0037398266 scopus 로고    scopus 로고
    • Interfacing the orbitrap mass analyzer to an electrospray ion source
    • Hardman M, Makarov AA. Interfacing the orbitrap mass analyzer to an electrospray ion source. Anal Chem. 2003;75:1699-705.
    • (2003) Anal Chem. , vol.75 , pp. 1699-1705
    • Hardman, M.1    Makarov, A.A.2
  • 49
    • 33646899550 scopus 로고    scopus 로고
    • Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer
    • Macek B, Waanders LF, Olsen JV, Mann M. Top-down protein sequencing and MS3 on a hybrid linear quadrupole ion trap-orbitrap mass spectrometer. Mol Cell Proteomics. 2006;5:949-58.
    • (2006) Mol Cell Proteomics. , vol.5 , pp. 949-958
    • Macek, B.1    Waanders, L.F.2    Olsen, J.V.3    Mann, M.4
  • 50
    • 58149477901 scopus 로고    scopus 로고
    • Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry
    • Thalassinos K, Grabenauer M, Slade SE, Hilton GR, Bowers MT, Scrivens JH. Characterization of phosphorylated peptides using traveling wave-based and drift cell ion mobility mass spectrometry. Anal Chem. 2009;81:248-54.
    • (2009) Anal Chem. , vol.81 , pp. 248-254
    • Thalassinos, K.1    Grabenauer, M.2    Slade, S.E.3    Hilton, G.R.4    Bowers, M.T.5    Scrivens, J.H.6
  • 51
    • 77957292542 scopus 로고    scopus 로고
    • Separation of peptide isomers with variant modified sites by high-resolution differential ion mobility spectrometry
    • Shvartsburg AA, Creese AJ, Smith RD, Cooper HJ. Separation of peptide isomers with variant modified sites by high-resolution differential ion mobility spectrometry. Anal Chem. 2010;82:8327-34.
    • (2010) Anal Chem. , vol.82 , pp. 8327-8334
    • Shvartsburg, A.A.1    Creese, A.J.2    Smith, R.D.3    Cooper, H.J.4
  • 53
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong SE, Mann M. Mass spectrometry-based proteomics turns quantitative. Nat Chem Biol. 2005;1:252-62.
    • (2005) Nat Chem Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 54
    • 45749144385 scopus 로고    scopus 로고
    • Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factor-dependent phosphotyrosineassociated signaling
    • Spellman DS, Deinhardt K, Darie CC, Chao MV, Neubert TA. Stable isotopic labeling by amino acids in cultured primary neurons: application to brain-derived neurotrophic factor-dependent phosphotyrosineassociated signaling. Mol Cell Proteomics. 2008;7:1067-76.
    • (2008) Mol Cell Proteomics. , vol.7 , pp. 1067-1076
    • Spellman, D.S.1    Deinhardt, K.2    Darie, C.C.3    Chao, M.V.4    Neubert, T.A.5
  • 56
    • 77958018495 scopus 로고    scopus 로고
    • The SILAC fly allows for accurate protein quantification in vivo
    • Sury MD, Chen JX, Selbach M. The SILAC fly allows for accurate protein quantification in vivo. Mol Cell Proteomics. 2010;9:2173-83.
    • (2010) Mol Cell Proteomics. , vol.9 , pp. 2173-2183
    • Sury, M.D.1    Chen, J.X.2    Selbach, M.3
  • 61
    • 34548228858 scopus 로고    scopus 로고
    • CILAT: a new reagent for quantitative proteomics
    • Li S, Zeng D. CILAT: a new reagent for quantitative proteomics. Chem Commun (Camb). 2007;2181-3.
    • (2007) Chem Commun (Camb) , pp. 2181-2183
    • Li, S.1    Zeng, D.2
  • 62
    • 34848862125 scopus 로고    scopus 로고
    • Label-free LCMS/MS quantitative proteomics for large-scale biomarker discovery in complex samples
    • Levin Y, Schwarz E, Wang L, Leweke FM, Bahn S. Label-free LCMS/MS quantitative proteomics for large-scale biomarker discovery in complex samples. J Sep Sci. 2007;30:2198-203.
    • (2007) J Sep Sci. , vol.30 , pp. 2198-2203
    • Levin, Y.1    Schwarz, E.2    Wang, L.3    Leweke, F.M.4    Bahn, S.5
  • 64
    • 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 III. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal Chem. 2004;76:4193-201.
    • (2004) Anal Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 65
    • 10744233766 scopus 로고    scopus 로고
    • Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards
    • Wang W, Zhou H, Lin H, Roy S, Shaler TA, Hill LR, Norton S, Kumar P, Anderle M, et al. Quantification of proteins and metabolites by mass spectrometry without isotopic labeling or spiked standards. Anal Chem. 2003;75:4818-26.
    • (2003) Anal Chem. , vol.75 , pp. 4818-4826
    • Wang, W.1    Zhou, H.2    Lin, H.3    Roy, S.4    Shaler, T.A.5    Hill, L.R.6    Norton, S.7    Kumar, P.8    Anderle, M.9
  • 66
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange V, Picotti P, Domon B, Aebersold R. Selected reaction monitoring for quantitative proteomics: a tutorial. Mol Syst Biol. 2008;4:222.
    • (2008) Mol Syst Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 67
    • 41349096900 scopus 로고    scopus 로고
    • Data analysis and bioinformatics tools for tandem mass spectrometry in proteomics
    • Deutsch EW, Lam H, Aebersold R. Data analysis and bioinformatics tools for tandem mass spectrometry in proteomics. Physiol Genomics. 2008;33:18-25.
    • (2008) Physiol Genomics. , vol.33 , pp. 18-25
    • Deutsch, E.W.1    Lam, H.2    Aebersold, R.3
  • 68
    • 79551483264 scopus 로고    scopus 로고
    • Discussion on common data analysis strategies used in MS-based proteomics
    • Matthiesen R, Azevedo L, Amorim A, Carvalho AS. Discussion on common data analysis strategies used in MS-based proteomics. Proteomics. 2011;11:604-19.
    • (2011) Proteomics. , vol.11 , pp. 604-619
    • Matthiesen, R.1    Azevedo, L.2    Amorim, A.3    Carvalho, A.S.4
  • 74
    • 77957360551 scopus 로고    scopus 로고
    • Proteomics in nutrition: status quo and outlook for biomarkers and bioactives
    • Kussmann M, Panchaud A, Affolter M. Proteomics in nutrition: status quo and outlook for biomarkers and bioactives. J Proteome Res. 2010;9:4876-87.
    • (2010) J Proteome Res. , vol.9 , pp. 4876-4887
    • Kussmann, M.1    Panchaud, A.2    Affolter, M.3
  • 77
    • 23944492134 scopus 로고    scopus 로고
    • Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database
    • Omenn GS, States DJ, Adamski M, Blackwell TW, Menon R, Hermjakob H, Apweiler R, Haab BB, Simpson RJ, et al. Overview of the HUPO Plasma Proteome Project: results from the pilot phase with 35 collaborating laboratories and multiple analytical groups, generating a core dataset of 3020 proteins and a publicly-available database. Proteomics. 2005;5:3226-45.
    • (2005) Proteomics. , vol.5 , pp. 3226-3245
    • Omenn, G.S.1    States, D.J.2    Adamski, M.3    Blackwell, T.W.4    Menon, R.5    Hermjakob, H.6    Apweiler, R.7    Haab, B.B.8    Simpson, R.J.9
  • 79
    • 46049084849 scopus 로고    scopus 로고
    • Towards standard protocols and guidelines for urine proteomics: a report on the Human Kidney and Urine Proteome Project (HKUPP) symposium and workshop, 6 October 2007, Seoul, Korea and 1 November 2007, San Francisco, CA, USA
    • Yamamoto T, Langham RG, Ronco P, Knepper MA, Thongboonkerd V. Towards standard protocols and guidelines for urine proteomics: a report on the Human Kidney and Urine Proteome Project (HKUPP) symposium and workshop, 6 October 2007, Seoul, Korea and 1 November 2007, San Francisco, CA, USA. Proteomics. 2008;8:2156-9.
    • (2008) Proteomics. , vol.8 , pp. 2156-2159
    • Yamamoto, T.1    Langham, R.G.2    Ronco, P.3    Knepper, M.A.4    Thongboonkerd, V.5
  • 80
    • 23944524368 scopus 로고    scopus 로고
    • Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma
    • Echan LA, Tang HY, Ali-Khan N, Lee K, Speicher DW. Depletion of multiple high-abundance proteins improves protein profiling capacities of human serum and plasma. Proteomics. 2005;5:3292-303.
    • (2005) Proteomics. , vol.5 , pp. 3292-3303
    • Echan, L.A.1    Tang, H.Y.2    Ali-Khan, N.3    Lee, K.4    Speicher, D.W.5
  • 81
    • 35649000519 scopus 로고    scopus 로고
    • Practical points in urinary proteomics
    • Thongboonkerd V. Practical points in urinary proteomics. J Proteome Res. 2007;6:3881-90.
    • (2007) J Proteome Res. , vol.6 , pp. 3881-3890
    • Thongboonkerd, V.1
  • 83
    • 69849106821 scopus 로고    scopus 로고
    • Capillary electrophoresis-mass spectrometry as a powerful tool in biomarker discovery and clinical diagnosis: an update of recent developments
    • Mischak H, Coon JJ, Novak J, Weissinger EM, Schanstra JP, Dominiczak AF. Capillary electrophoresis-mass spectrometry as a powerful tool in biomarker discovery and clinical diagnosis: an update of recent developments. Mass Spectrom Rev. 2009;28:703-24.
    • (2009) Mass Spectrom Rev. , vol.28 , pp. 703-724
    • Mischak, H.1    Coon, J.J.2    Novak, J.3    Weissinger, E.M.4    Schanstra, J.P.5    Dominiczak, A.F.6
  • 88
    • 65249190795 scopus 로고    scopus 로고
    • Proteomicsbased identification of differentially-expressed proteins including galectin-1 in the blood plasma of type 2 diabetic patients
    • Liu X, Feng Q, Chen Y, Zuo J, Gupta N, Chang Y, Fang F. Proteomicsbased identification of differentially-expressed proteins including galectin-1 in the blood plasma of type 2 diabetic patients. J Proteome Res. 2009;8:1255-62.
    • (2009) J Proteome Res. , vol.8 , pp. 1255-1262
    • Liu, X.1    Feng, Q.2    Chen, Y.3    Zuo, J.4    Gupta, N.5    Chang, Y.6    Fang, F.7
  • 89
    • 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, Gunckel M, Rogler G, Haller D. Differential protein expression profile in the intestinal epithelium from patients with inflammatory bowel disease. J Proteome Res. 2007;6:1114-25.
    • (2007) J Proteome Res. , vol.6 , pp. 1114-1125
    • Shkoda, A.1    Werner, T.2    Daniel, H.3    Gunckel, M.4    Rogler, G.5    Haller, D.6
  • 90
    • 52749091008 scopus 로고    scopus 로고
    • Increase in endoplasmic reticulum stress-related proteins and genes in adipose tissue of obese, insulin-resistant individuals
    • Boden G, Duan X, Homko C, Molina EJ, Song W, Perez O, Cheung P, Merali S. Increase in endoplasmic reticulum stress-related proteins and genes in adipose tissue of obese, insulin-resistant individuals. Diabetes. 2008;57:2438-44.
    • (2008) Diabetes. , vol.57 , pp. 2438-2444
    • Boden, G.1    Duan, X.2    Homko, C.3    Molina, E.J.4    Song, W.5    Perez, O.6    Cheung, P.7    Merali, S.8
  • 91
    • 71549126821 scopus 로고    scopus 로고
    • The physiologic effects of caloric restriction are reflected in the in vivo adipocyte-enriched proteome of overweight/obese subjects
    • Bouwman FG, Claessens M, van Baak MA, Noben JP, Wang P, Saris WH, Mariman EC. The physiologic effects of caloric restriction are reflected in the in vivo adipocyte-enriched proteome of overweight/obese subjects. J Proteome Res. 2009;8:5532-40.
    • (2009) J Proteome Res. , vol.8 , pp. 5532-5540
    • Bouwman, F.G.1    Claessens, M.2    Van Baak, M.A.3    Noben, J.P.4    Wang, P.5    Saris, W.H.6    Mariman, E.C.7
  • 93
    • 36248931106 scopus 로고    scopus 로고
    • Proteomic biomarkers of peripheral blood mononuclear cells obtained from postmenopausal women undergoing an intervention with soy isoflavones
    • Fuchs D, Vafeiadou K, Hall WL, Daniel H, Williams CM, Schroot JH, Wenzel U. Proteomic biomarkers of peripheral blood mononuclear cells obtained from postmenopausal women undergoing an intervention with soy isoflavones. Am J Clin Nutr. 2007;86:1369-75.
    • (2007) Am J Clin Nutr. , vol.86 , pp. 1369-1375
    • Fuchs, D.1    Vafeiadou, K.2    Hall, W.L.3    Daniel, H.4    Williams, C.M.5    Schroot, J.H.6    Wenzel, U.7
  • 94
    • 34948882909 scopus 로고    scopus 로고
    • The human peripheral bloodmononuclear cell proteome responds to a dietary flaxseed-intervention and proteins identified suggest a protective effect in atherosclerosis
    • Fuchs D, Piller R, Linseisen J, Daniel H, Wenzel U. The human peripheral bloodmononuclear cell proteome responds to a dietary flaxseed-intervention and proteins identified suggest a protective effect in atherosclerosis. Proteomics. 2007;7:3278-88
    • (2007) Proteomics. , vol.7 , pp. 3278-3288
    • Fuchs, D.1    Piller, R.2    Linseisen, J.3    Daniel, H.4    Wenzel, U.5
  • 95
    • 44649095227 scopus 로고    scopus 로고
    • Identification of potential serum biomarkers of inflammation and lipid modulation that are altered by fish oil supplementation in healthy volunteers
    • de Roos B, Geelen A, Ross K, Rucklidge G, Reid M, Duncan G, Caslake M, Horgan G, Brouwer IA. Identification of potential serum biomarkers of inflammation and lipid modulation that are altered by fish oil supplementation in healthy volunteers. Proteomics. 2008;8:1965-74.
    • (2008) Proteomics. , vol.8 , pp. 1965-1974
    • De Roos, B.1    Geelen, A.2    Ross, K.3    Rucklidge, G.4    Reid, M.5    Duncan, G.6    Caslake, M.7    Horgan, G.8    Brouwer, I.A.9
  • 96
    • 77950687099 scopus 로고    scopus 로고
    • Blood folate status and expression of proteins involved in immune function, inflammation, and coagulation: biochemical and proteomic changes in the plasma of humans in response to long-term synthetic folic acid supplementation
    • Duthie SJ, Horgan G, de Roos B, Rucklidge G, Reid M, Duncan G, Pirie L, Basten GP, Powers HJ. Blood folate status and expression of proteins involved in immune function, inflammation, and coagulation: biochemical and proteomic changes in the plasma of humans in response to long-term synthetic folic acid supplementation. J Proteome Res. 2010;9:1941-50.
    • (2010) J Proteome Res. , vol.9 , pp. 1941-1950
    • Duthie, S.J.1    Horgan, G.2    De Roos, B.3    Rucklidge, G.4    Reid, M.5    Duncan, G.6    Pirie, L.7    Basten, G.P.8    Powers, H.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.