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Volumn 75, Issue 14, 2012, Pages 4190-4206

Mass spectrometry and animal science: Protein identification strategies and particularities of farm animal species

Author keywords

Animal science; Mass spectrometry; Non model species; Protein identification

Indexed keywords

SERUM ALBUMIN;

EID: 84863856185     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2012.04.009     Document Type: Review
Times cited : (65)

References (132)
  • 1
    • 83755192039 scopus 로고    scopus 로고
    • Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques
    • Ohlendieck K. Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skeletal Muscle 2011, 1:6.
    • (2011) Skeletal Muscle , vol.1 , pp. 6
    • Ohlendieck, K.1
  • 3
    • 34250634816 scopus 로고    scopus 로고
    • Application of proteomics to understand the molecular mechanisms behind meat quality
    • Hollung K., Veiseth E., Jia X., Færgestad E.M., Hildrum K.I. Application of proteomics to understand the molecular mechanisms behind meat quality. Meat Sci 2007, 77:97-104.
    • (2007) Meat Sci , vol.77 , pp. 97-104
    • Hollung, K.1    Veiseth, E.2    Jia, X.3    Færgestad, E.M.4    Hildrum, K.I.5
  • 4
    • 83055169961 scopus 로고    scopus 로고
    • Identification by proteomic analysis of early post-mortem markers involved in the variability in fat loss during cooking of mule duck "foie gras"
    • Theron L., Fernandez X., Marty-Gasset N., Pichereaux C., Rossignol M., Chambon C., et al. Identification by proteomic analysis of early post-mortem markers involved in the variability in fat loss during cooking of mule duck "foie gras". J Agric Food Chem 2011, 59:12617-12628.
    • (2011) J Agric Food Chem , vol.59 , pp. 12617-12628
    • Theron, L.1    Fernandez, X.2    Marty-Gasset, N.3    Pichereaux, C.4    Rossignol, M.5    Chambon, C.6
  • 5
    • 61449163906 scopus 로고    scopus 로고
    • Invited review: proteomics of milk and bacteria used in fermented dairy products: from qualitative to quantitative advances
    • Gagnaire V., Jardin J., Jan G., Lortal S. Invited review: proteomics of milk and bacteria used in fermented dairy products: from qualitative to quantitative advances. J Dairy Sci 2009, 92:811-825.
    • (2009) J Dairy Sci , vol.92 , pp. 811-825
    • Gagnaire, V.1    Jardin, J.2    Jan, G.3    Lortal, S.4
  • 6
    • 78650404444 scopus 로고    scopus 로고
    • Proteomic analysis of egg white proteins during storage
    • Omana D.A., Liang Y., Kav N.N.V., Wu J. Proteomic analysis of egg white proteins during storage. Proteomics 2011, 11:144-153.
    • (2011) Proteomics , vol.11 , pp. 144-153
    • Omana, D.A.1    Liang, Y.2    Kav, N.N.V.3    Wu, J.4
  • 7
    • 77249107516 scopus 로고    scopus 로고
    • The egg white and yolk interactomes as gleaned from extensive proteomic data
    • D'Alessandro A., Righetti P.G., Fasoli E., Zolla L. The egg white and yolk interactomes as gleaned from extensive proteomic data. J Proteomics 2010, 73:1028-1042.
    • (2010) J Proteomics , vol.73 , pp. 1028-1042
    • D'Alessandro, A.1    Righetti, P.G.2    Fasoli, E.3    Zolla, L.4
  • 10
    • 32544432232 scopus 로고    scopus 로고
    • Use of a proteomics approach to identify favourable conditions for production of good quality lambskin leather
    • Choudhury S.D., Allsop T., Passman A., Norris G.E. Use of a proteomics approach to identify favourable conditions for production of good quality lambskin leather. Anal Bioanal Chem 2006, 384:723-735.
    • (2006) Anal Bioanal Chem , vol.384 , pp. 723-735
    • Choudhury, S.D.1    Allsop, T.2    Passman, A.3    Norris, G.E.4
  • 12
    • 77956181148 scopus 로고    scopus 로고
    • Enrichment of low-abundance proteins from bovine and porcine serum samples for proteomic studies
    • Marco-Ramell A., Bassols A. Enrichment of low-abundance proteins from bovine and porcine serum samples for proteomic studies. Res Vet Sci 2010, 89:340-343.
    • (2010) Res Vet Sci , vol.89 , pp. 340-343
    • Marco-Ramell, A.1    Bassols, A.2
  • 14
    • 82955203410 scopus 로고    scopus 로고
    • Comprehensive chromatographic separations in proteomics
    • Donato P., Cacciola F., Mondello L., Dugo P. Comprehensive chromatographic separations in proteomics. J Chromatogr A 2011, 1218:8777-8790.
    • (2011) J Chromatogr A , vol.1218 , pp. 8777-8790
    • Donato, P.1    Cacciola, F.2    Mondello, L.3    Dugo, P.4
  • 15
    • 78650492407 scopus 로고    scopus 로고
    • 2D electrophoresis-based expression proteomics: a microbiologist's perspective
    • Sá-Correia I., Teixeira M.C. 2D electrophoresis-based expression proteomics: a microbiologist's perspective. Expert Rev Proteomics 2010, 7:943-953.
    • (2010) Expert Rev Proteomics , vol.7 , pp. 943-953
    • Sá-Correia, I.1    Teixeira, M.C.2
  • 16
    • 0037338365 scopus 로고    scopus 로고
    • Proteomic analysis of post-translational modifications
    • Mann M., Jensen O.N. Proteomic analysis of post-translational modifications. Nat Biotechnol 2003, 21:255-261.
    • (2003) Nat Biotechnol , vol.21 , pp. 255-261
    • Mann, M.1    Jensen, O.N.2
  • 17
    • 79959465643 scopus 로고    scopus 로고
    • Mass spectrometry in the postgenomic era
    • Chait B.T. Mass spectrometry in the postgenomic era. Annu Rev Biochem 2011, 80:239-246.
    • (2011) Annu Rev Biochem , vol.80 , pp. 239-246
    • Chait, B.T.1
  • 18
  • 19
    • 71549114829 scopus 로고    scopus 로고
    • Advances in preparation of biological extracts for protein purification
    • Grabski A.C. Advances in preparation of biological extracts for protein purification. Methods Enzymol 2009, 463:285-303.
    • (2009) Methods Enzymol , vol.463 , pp. 285-303
    • Grabski, A.C.1
  • 20
    • 32344432397 scopus 로고    scopus 로고
    • Pre-extraction sample handling by automated frozen disruption significantly improves subsequent proteomic analyses
    • Butt R.H., Coorssen J.R. Pre-extraction sample handling by automated frozen disruption significantly improves subsequent proteomic analyses. J Proteome Res 2006, 5:437-448.
    • (2006) J Proteome Res , vol.5 , pp. 437-448
    • Butt, R.H.1    Coorssen, J.R.2
  • 22
    • 58949100303 scopus 로고    scopus 로고
    • Chicken egg yolk cytoplasmic proteome, mined via combinatorial peptide ligand libraries
    • Farinazzo A., Restuccia U., Bachi A., Guerrier L., Fortis F., Boschetti E., et al. Chicken egg yolk cytoplasmic proteome, mined via combinatorial peptide ligand libraries. J Chromatogr A 2009, 1216:1241-1252.
    • (2009) J Chromatogr A , vol.1216 , pp. 1241-1252
    • Farinazzo, A.1    Restuccia, U.2    Bachi, A.3    Guerrier, L.4    Fortis, F.5    Boschetti, E.6
  • 23
    • 35348963096 scopus 로고    scopus 로고
    • The chicken egg white proteome
    • Mann K. The chicken egg white proteome. Proteomics 2007, 7:3558-3568.
    • (2007) Proteomics , vol.7 , pp. 3558-3568
    • Mann, K.1
  • 24
    • 38149103492 scopus 로고    scopus 로고
    • The chicken egg yolk plasma and granule proteomes
    • Mann K., Mann M. The chicken egg yolk plasma and granule proteomes. Proteomics 2008, 8:178-191.
    • (2008) Proteomics , vol.8 , pp. 178-191
    • Mann, K.1    Mann, M.2
  • 25
    • 79551474552 scopus 로고    scopus 로고
    • Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome
    • Ly L., Wasinger V.C. Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome. Proteomics 2011, 11:513-534.
    • (2011) Proteomics , vol.11 , pp. 513-534
    • Ly, L.1    Wasinger, V.C.2
  • 26
    • 84555178070 scopus 로고    scopus 로고
    • Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis - an update covering the period 2008-2011
    • Selvaraju S., El Rassi Z. Liquid-phase-based separation systems for depletion, prefractionation and enrichment of proteins in biological fluids and matrices for in-depth proteomics analysis - an update covering the period 2008-2011. Electrophoresis 2012, 33:74-88.
    • (2012) Electrophoresis , vol.33 , pp. 74-88
    • Selvaraju, S.1    El Rassi, Z.2
  • 27
    • 79251635924 scopus 로고    scopus 로고
    • Quantitative proteomics: assessing the spectrum of in-gel protein detection methods
    • Gauci V.J., Wright E.P., Coorssen J.R. Quantitative proteomics: assessing the spectrum of in-gel protein detection methods. J Chem Biol 2011, 4:3-29.
    • (2011) J Chem Biol , vol.4 , pp. 3-29
    • Gauci, V.J.1    Wright, E.P.2    Coorssen, J.R.3
  • 29
    • 70350247861 scopus 로고    scopus 로고
    • Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques
    • Zhao Y., Jensen O.N. Modification-specific proteomics: strategies for characterization of post-translational modifications using enrichment techniques. Proteomics 2009, 9:4632-4641.
    • (2009) Proteomics , vol.9 , pp. 4632-4641
    • Zhao, Y.1    Jensen, O.N.2
  • 30
    • 84857656021 scopus 로고    scopus 로고
    • Finding the right balance - a personal journey from individual proteins to membrane embedded motors
    • Robinson C.V. Finding the right balance - a personal journey from individual proteins to membrane embedded motors. FEBS J 2012, 279:663-677.
    • (2012) FEBS J , vol.279 , pp. 663-677
    • Robinson, C.V.1
  • 31
    • 40549116289 scopus 로고    scopus 로고
    • Optimizing the difference gel electrophoresis (DIGE) technology
    • Friedman D.B., Lilley K.S. Optimizing the difference gel electrophoresis (DIGE) technology. Methods Mol Biol 2008, 428:93-124.
    • (2008) Methods Mol Biol , vol.428 , pp. 93-124
    • Friedman, D.B.1    Lilley, K.S.2
  • 32
    • 57649153125 scopus 로고    scopus 로고
    • Difference gel electrophoresis
    • Timms J.F., Cramer R. Difference gel electrophoresis. Proteomics 2008, 8:4886-4897.
    • (2008) Proteomics , vol.8 , pp. 4886-4897
    • Timms, J.F.1    Cramer, R.2
  • 34
    • 81955167399 scopus 로고    scopus 로고
    • DIGE and iTRAQ as biomarker discovery tools in aquatic toxicology
    • Martyniuk C.J., Alvarez S., Denslow N.D. DIGE and iTRAQ as biomarker discovery tools in aquatic toxicology. Ecotoxicol Environ Saf 2012, 76:3-10.
    • (2012) Ecotoxicol Environ Saf , vol.76 , pp. 3-10
    • Martyniuk, C.J.1    Alvarez, S.2    Denslow, N.D.3
  • 35
    • 79959241187 scopus 로고    scopus 로고
    • Proteomic analysis of pork meat in the production of cooked ham
    • Pioselli B., Paredi G., Mozzarelli A. Proteomic analysis of pork meat in the production of cooked ham. Mol Biosyst 2011, 7:2252-2260.
    • (2011) Mol Biosyst , vol.7 , pp. 2252-2260
    • Pioselli, B.1    Paredi, G.2    Mozzarelli, A.3
  • 37
    • 77952503261 scopus 로고    scopus 로고
    • MALDI-in source decay applied to mass spectrometry imaging: a new tool for protein identification
    • Debois D., Bertrand V., Quinton L., De Pauw-Gillet M.-C., De Pauw E. MALDI-in source decay applied to mass spectrometry imaging: a new tool for protein identification. Anal Chem 2010, 82:4036-4045.
    • (2010) Anal Chem , vol.82 , pp. 4036-4045
    • Debois, D.1    Bertrand, V.2    Quinton, L.3    De Pauw-Gillet, M.-C.4    De Pauw, E.5
  • 38
    • 79960431406 scopus 로고    scopus 로고
    • Imaging of intact tissue sections: moving beyond the microscope
    • Seeley E.H., Schwamborn K., Caprioli R.M. Imaging of intact tissue sections: moving beyond the microscope. J Biol Chem 2011, 286:25459-25466.
    • (2011) J Biol Chem , vol.286 , pp. 25459-25466
    • Seeley, E.H.1    Schwamborn, K.2    Caprioli, R.M.3
  • 39
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: approaches, advances, and applications
    • Yates J.R., Ruse C.I., Nakorchevsky A. Proteomics by mass spectrometry: approaches, advances, and applications. Annu Rev Biomed Eng 2009, 11:49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 41
    • 30644469415 scopus 로고    scopus 로고
    • Molecular weight determination of peptides and proteins by ESI and MALDI
    • Strupat K. Molecular weight determination of peptides and proteins by ESI and MALDI. Methods Enzymol 2005, 405:1-36.
    • (2005) Methods Enzymol , vol.405 , pp. 1-36
    • Strupat, K.1
  • 42
    • 0442276567 scopus 로고    scopus 로고
    • Under non-denaturing solvent conditions, the mean charge state of a multiply charged protein ion formed by electrospray is linearly correlated with the macromolecular surface
    • Hautreux M., Hue N., Du Fou de Kerdaniel A., Zahir A., Malec V., Laprévote O. Under non-denaturing solvent conditions, the mean charge state of a multiply charged protein ion formed by electrospray is linearly correlated with the macromolecular surface. Int J Mass Spectrom 2004, 231:131-137.
    • (2004) Int J Mass Spectrom , vol.231 , pp. 131-137
    • Hautreux, M.1    Hue, N.2    Du Fou de Kerdaniel, A.3    Zahir, A.4    Malec, V.5    Laprévote, O.6
  • 43
    • 0141669841 scopus 로고    scopus 로고
    • Mean charge state and charge state distribution of proteins as structural probes. An electrospray ionisation mass spectrometry study of lysozyme and ribonuclease A
    • Halgand F., Laprévote O. Mean charge state and charge state distribution of proteins as structural probes. An electrospray ionisation mass spectrometry study of lysozyme and ribonuclease A. Eur J Mass Spectrom 2001, 7:433.
    • (2001) Eur J Mass Spectrom , vol.7 , pp. 433
    • Halgand, F.1    Laprévote, O.2
  • 44
    • 0036302007 scopus 로고    scopus 로고
    • Peptide and protein analysis with mass spectrometry
    • Trauger S.A., Webb W., Siuzdak G. Peptide and protein analysis with mass spectrometry. Spectrosc Int J 2002, 16:15-28.
    • (2002) Spectrosc Int J , vol.16 , pp. 15-28
    • Trauger, S.A.1    Webb, W.2    Siuzdak, G.3
  • 47
    • 84990652333 scopus 로고
    • Metastable decay of peptides and proteins in matrix-assisted laser-desorption mass spectrometry
    • Spengler B., Kirsch D., Kaufmann R. Metastable decay of peptides and proteins in matrix-assisted laser-desorption mass spectrometry. Rapid Commun Mass Spectrom 1991, 5:198-202.
    • (1991) Rapid Commun Mass Spectrom , vol.5 , pp. 198-202
    • Spengler, B.1    Kirsch, D.2    Kaufmann, R.3
  • 48
    • 65649151144 scopus 로고    scopus 로고
    • Electrospray ionisation mass spectrometry: principles and clinical applications
    • Australian Association of Clinical Biochemists
    • Ho C.S., Lam C.W.K., Chan M.H.M., Cheung R.C.K., Law L.K., Lit L.C.W., et al. Electrospray ionisation mass spectrometry: principles and clinical applications. The Clinical Biochemist Reviews 2003, 24:3-12. Australian Association of Clinical Biochemists.
    • (2003) The Clinical Biochemist Reviews , vol.24 , pp. 3-12
    • Ho, C.S.1    Lam, C.W.K.2    Chan, M.H.M.3    Cheung, R.C.K.4    Law, L.K.5    Lit, L.C.W.6
  • 50
    • 1242351309 scopus 로고    scopus 로고
    • Electron-capture dissociation tandem mass spectrometry
    • Zubarev R.A. Electron-capture dissociation tandem mass spectrometry. Curr Opin Biotechnol 2004, 15:12-16.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 12-16
    • Zubarev, R.A.1
  • 52
    • 77958159767 scopus 로고    scopus 로고
    • New advances in the understanding of the in-source decay fragmentation of peptides in MALDI-TOF-MS
    • Demeure K., Gabelica V., De Pauw E.A. New advances in the understanding of the in-source decay fragmentation of peptides in MALDI-TOF-MS. J Am Soc Mass Spectrom 2010, 21:1906-1917.
    • (2010) J Am Soc Mass Spectrom , vol.21 , pp. 1906-1917
    • Demeure, K.1    Gabelica, V.2    De Pauw, E.A.3
  • 54
    • 79960258556 scopus 로고    scopus 로고
    • 100% protein sequence coverage: a modern form of surrealism in proteomics
    • Meyer B., Papasotiriou D.G., Karas M. 100% protein sequence coverage: a modern form of surrealism in proteomics. Amino Acids 2011, 41:291-310.
    • (2011) Amino Acids , vol.41 , pp. 291-310
    • Meyer, B.1    Papasotiriou, D.G.2    Karas, M.3
  • 55
    • 79961185259 scopus 로고    scopus 로고
    • Ion mobility mass spectrometry for peptide analysis
    • Harvey S.R., Macphee C.E., Barran P.E. Ion mobility mass spectrometry for peptide analysis. Methods 2011, 54:454-461.
    • (2011) Methods , vol.54 , pp. 454-461
    • Harvey, S.R.1    Macphee, C.E.2    Barran, P.E.3
  • 56
    • 28544450640 scopus 로고    scopus 로고
    • Farm animal genomics and informatics: an update
    • Fadiel A., Anidi I., Eichenbaum K.D. Farm animal genomics and informatics: an update. Nucleic Acids Res 2005, 33:6308-6318.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6308-6318
    • Fadiel, A.1    Anidi, I.2    Eichenbaum, K.D.3
  • 57
    • 75549089630 scopus 로고    scopus 로고
    • The 2010 nucleic acids research database issue and online database collection: a community of data resources
    • Cochrane G.R., Galperin M.Y. The 2010 nucleic acids research database issue and online database collection: a community of data resources. Nucleic Acids Res 2010, 38:D1-D4.
    • (2010) Nucleic Acids Res , vol.38
    • Cochrane, G.R.1    Galperin, M.Y.2
  • 58
    • 80052033624 scopus 로고    scopus 로고
    • Protein identification using MS/MS data
    • Cottrell J.S. Protein identification using MS/MS data. J Proteomics 2011, 74:1842-1851.
    • (2011) J Proteomics , vol.74 , pp. 1842-1851
    • Cottrell, J.S.1
  • 61
    • 78650309656 scopus 로고    scopus 로고
    • Utility, limitations, and promise of proteomics in animal science
    • Lippolis J.D., Reinhardt T.A. Utility, limitations, and promise of proteomics in animal science. Vet Immunol Immunopathol 2010, 138:241-251.
    • (2010) Vet Immunol Immunopathol , vol.138 , pp. 241-251
    • Lippolis, J.D.1    Reinhardt, T.A.2
  • 62
    • 40149108658 scopus 로고    scopus 로고
    • Computational methods for protein identification from mass spectrometry data
    • McHugh L., Arthur J.W. Computational methods for protein identification from mass spectrometry data. PLoS Comput Biol 2008, 4:e12.
    • (2008) PLoS Comput Biol , vol.4
    • McHugh, L.1    Arthur, J.W.2
  • 63
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 64
    • 80555146717 scopus 로고    scopus 로고
    • A face in the crowd: recognizing peptides through database search
    • [R111.009522]
    • Eng J.K., Searle B.C., Clauser K.R., Tabb D.L. A face in the crowd: recognizing peptides through database search. Mol Cell Proteomics 2011, 10. [R111.009522].
    • (2011) Mol Cell Proteomics , vol.10
    • Eng, J.K.1    Searle, B.C.2    Clauser, K.R.3    Tabb, D.L.4
  • 66
    • 77953155288 scopus 로고    scopus 로고
    • Template proteogenomics: sequencing whole proteins using an imperfect database
    • Castellana N.E., Pham V., Arnott D., Lill J.R., Bafna V. Template proteogenomics: sequencing whole proteins using an imperfect database. Mol Cell Proteomics 2010, 9:1260-1270.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 1260-1270
    • Castellana, N.E.1    Pham, V.2    Arnott, D.3    Lill, J.R.4    Bafna, V.5
  • 67
    • 79953054035 scopus 로고    scopus 로고
    • Exploring the proteome of an echinoderm nervous system: 2-DE of the sea star radial nerve cord and the synaptosomal membranes subproteome
    • Franco C.F., Santos R., Coelho A.V. Exploring the proteome of an echinoderm nervous system: 2-DE of the sea star radial nerve cord and the synaptosomal membranes subproteome. Proteomics 2011, 11:1359-1364.
    • (2011) Proteomics , vol.11 , pp. 1359-1364
    • Franco, C.F.1    Santos, R.2    Coelho, A.V.3
  • 68
    • 78649908934 scopus 로고    scopus 로고
    • Differential protein expression in two bivalve species; Mytilus galloprovincialis and Corbicula fluminea; exposed to Cylindrospermopsis raciborskii cells
    • Puerto M., Campos A., Prieto A., Cameán A., de Almeida A.M., Coelho A.V., et al. Differential protein expression in two bivalve species; Mytilus galloprovincialis and Corbicula fluminea; exposed to Cylindrospermopsis raciborskii cells. Aquat Toxicol 2011, 101:109-116.
    • (2011) Aquat Toxicol , vol.101 , pp. 109-116
    • Puerto, M.1    Campos, A.2    Prieto, A.3    Cameán, A.4    de Almeida, A.M.5    Coelho, A.V.6
  • 72
    • 34547153650 scopus 로고    scopus 로고
    • Sequence similarity-driven proteomics in organisms with unknown genomes by LC-MS/MS and automated de novo sequencing
    • Waridel P., Frank A., Thomas H., Surendranath V., Sunyaev S., Pevzner P., et al. Sequence similarity-driven proteomics in organisms with unknown genomes by LC-MS/MS and automated de novo sequencing. Proteomics 2007, 7:2318-2329.
    • (2007) Proteomics , vol.7 , pp. 2318-2329
    • Waridel, P.1    Frank, A.2    Thomas, H.3    Surendranath, V.4    Sunyaev, S.5    Pevzner, P.6
  • 73
    • 0001092477 scopus 로고    scopus 로고
    • Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes
    • Shevchenko A., Sunyaev S., Liska A., Bork P., Shevchenko A. Nanoelectrospray tandem mass spectrometry and sequence similarity searching for identification of proteins from organisms with unknown genomes. Methods Mol Biol 2003, 211:221-234.
    • (2003) Methods Mol Biol , vol.211 , pp. 221-234
    • Shevchenko, A.1    Sunyaev, S.2    Liska, A.3    Bork, P.4    Shevchenko, A.5
  • 74
    • 0037253223 scopus 로고    scopus 로고
    • Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications
    • Liska A.J., Shevchenko A. Expanding the organismal scope of proteomics: cross-species protein identification by mass spectrometry and its implications. Proteomics 2003, 3:19-28.
    • (2003) Proteomics , vol.3 , pp. 19-28
    • Liska, A.J.1    Shevchenko, A.2
  • 75
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates J.R., Eng J.K., McCormack A.L., Schieltz D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem 1995, 67:1426-1436.
    • (1995) Anal Chem , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 76
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with tandem mass spectra
    • Craig R., Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20:1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 78
    • 24044491542 scopus 로고    scopus 로고
    • Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and
    • Chalkley R.J., Baker P.R., Huang L., Hansen K.C., Allen N.P., Rexach M., et al. Comprehensive analysis of a multidimensional liquid chromatography mass spectrometry dataset acquired on a quadrupole selecting, quadrupole collision cell, time-of-flight mass spectrometer: II. New developments in Protein Prospector allow for reliable and. Mol Cell Proteomics 2005, 4:1194-1204.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1194-1204
    • Chalkley, R.J.1    Baker, P.R.2    Huang, L.3    Hansen, K.C.4    Allen, N.P.5    Rexach, M.6
  • 79
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J., Mann M. MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 2008, 26:1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 81
    • 78650147228 scopus 로고    scopus 로고
    • The generating function of CID, ETD, and CID/ETD pairs of tandem mass spectra: applications to database search
    • Kim S., Mischerikow N., Bandeira N., Navarro J.D., Wich L., Mohammed S., et al. The generating function of CID, ETD, and CID/ETD pairs of tandem mass spectra: applications to database search. Mol Cell Proteomics 2010, 9:2840-2852.
    • (2010) Mol Cell Proteomics , vol.9 , pp. 2840-2852
    • Kim, S.1    Mischerikow, N.2    Bandeira, N.3    Navarro, J.D.4    Wich, L.5    Mohammed, S.6
  • 82
    • 34848889259 scopus 로고    scopus 로고
    • The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • Shilov I.V., Seymour S.L., Patel A.A., Loboda A., Tang W.H., Keating S.P., et al. The Paragon Algorithm, a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 2007, 6:1638-1655.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 1638-1655
    • Shilov, I.V.1    Seymour, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6
  • 83
    • 0037725335 scopus 로고    scopus 로고
    • Combining mass spectrometry with database interrogation strategies in proteomics
    • Liska A.J., Shevchenko A. Combining mass spectrometry with database interrogation strategies in proteomics. TrAC, Trends Anal Chem 2003, 22:291-298.
    • (2003) TrAC, Trends Anal Chem , vol.22 , pp. 291-298
    • Liska, A.J.1    Shevchenko, A.2
  • 84
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • Mann M., Wilm M. Error-tolerant identification of peptides in sequence databases by peptide sequence tags. Anal Chem 1994, 66:4390-4399.
    • (1994) Anal Chem , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 85
    • 0030959279 scopus 로고    scopus 로고
    • Sequence database searches via de novo peptide sequencing by tandem mass spectrometry
    • Taylor J.A., Johnson R.S. Sequence database searches via de novo peptide sequencing by tandem mass spectrometry. Rapid Commun Mass Spectrom 1997, 11:1067-1075.
    • (1997) Rapid Commun Mass Spectrom , vol.11 , pp. 1067-1075
    • Taylor, J.A.1    Johnson, R.S.2
  • 86
    • 0035958869 scopus 로고    scopus 로고
    • Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches
    • Huang L., Jacob R.J., Pegg S.C., Baldwin M.A., Wang C.C., Burlingame A.L., et al. Functional assignment of the 20 S proteasome from Trypanosoma brucei using mass spectrometry and new bioinformatics approaches. J Biol Chem 2001, 276:28327-28339.
    • (2001) J Biol Chem , vol.276 , pp. 28327-28339
    • Huang, L.1    Jacob, R.J.2    Pegg, S.C.3    Baldwin, M.A.4    Wang, C.C.5    Burlingame, A.L.6
  • 87
    • 0035326344 scopus 로고    scopus 로고
    • Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching
    • Shevchenko A., Sunyaev S., Loboda A., Bork P., Ens W., Standing K.G. Charting the proteomes of organisms with unsequenced genomes by MALDI-quadrupole time-of-flight mass spectrometry and BLAST homology searching. Anal Chem 2001, 73:1917-1926.
    • (2001) Anal Chem , vol.73 , pp. 1917-1926
    • Shevchenko, A.1    Sunyaev, S.2    Loboda, A.3    Bork, P.4    Ens, W.5    Standing, K.G.6
  • 88
    • 0036463587 scopus 로고    scopus 로고
    • Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences
    • Mackey A.J., Haystead T.A.J., Pearson W.R. Getting more from less: algorithms for rapid protein identification with multiple short peptide sequences. Mol Cell Proteomics 2002, 1:139-147.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 139-147
    • Mackey, A.J.1    Haystead, T.A.J.2    Pearson, W.R.3
  • 89
    • 1942423061 scopus 로고    scopus 로고
    • High-throughput identification of proteins and unanticipated sequence modifications using a mass-based alignment algorithm for MS/MS de novo sequencing results
    • Searle B.C., Dasari S., Turner M., Reddy A.P., Choi D., Wilmarth P.A., et al. High-throughput identification of proteins and unanticipated sequence modifications using a mass-based alignment algorithm for MS/MS de novo sequencing results. Anal Chem 2004, 76:2220-2230.
    • (2004) Anal Chem , vol.76 , pp. 2220-2230
    • Searle, B.C.1    Dasari, S.2    Turner, M.3    Reddy, A.P.4    Choi, D.5    Wilmarth, P.A.6
  • 90
    • 37049006551 scopus 로고    scopus 로고
    • A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments
    • Grossmann J., Fischer B., Baerenfaller K., Owiti J., Buhmann J.M., Gruissem W., et al. A workflow to increase the detection rate of proteins from unsequenced organisms in high-throughput proteomics experiments. Proteomics 2007, 7:4245-4254.
    • (2007) Proteomics , vol.7 , pp. 4245-4254
    • Grossmann, J.1    Fischer, B.2    Baerenfaller, K.3    Owiti, J.4    Buhmann, J.M.5    Gruissem, W.6
  • 91
    • 2642523613 scopus 로고    scopus 로고
    • The power and the limitations of cross-species protein identification by mass spectrometry-driven sequence similarity searches
    • Habermann B., Oegema J., Sunyaev S., Shevchenko A. The power and the limitations of cross-species protein identification by mass spectrometry-driven sequence similarity searches. Mol Cell Proteomics 2004, 3:238-249.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 238-249
    • Habermann, B.1    Oegema, J.2    Sunyaev, S.3    Shevchenko, A.4
  • 92
  • 93
    • 13844319908 scopus 로고    scopus 로고
    • PepNovo: de novo peptide sequencing via probabilistic network modeling
    • Frank A., Pevzner P. PepNovo: de novo peptide sequencing via probabilistic network modeling. Anal Chem 2005, 77:964-973.
    • (2005) Anal Chem , vol.77 , pp. 964-973
    • Frank, A.1    Pevzner, P.2
  • 95
    • 70449517481 scopus 로고    scopus 로고
    • First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata)
    • Santos R., da Costa G., Franco C., Gomes-Alves P., Flammang P., Coelho A.V. First insights into the biochemistry of tube foot adhesive from the sea urchin Paracentrotus lividus (Echinoidea, Echinodermata). Mar Biotechnol (NY) 2009, 11:686-698.
    • (2009) Mar Biotechnol (NY) , vol.11 , pp. 686-698
    • Santos, R.1    da Costa, G.2    Franco, C.3    Gomes-Alves, P.4    Flammang, P.5    Coelho, A.V.6
  • 97
    • 0037387168 scopus 로고    scopus 로고
    • Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells
    • Talamo F., D'Ambrosio C., Arena S., Del Vecchio P., Ledda L., Zehender G., et al. Proteins from bovine tissues and biological fluids: defining a reference electrophoresis map for liver, kidney, muscle, plasma and red blood cells. Proteomics 2003, 3:440-460.
    • (2003) Proteomics , vol.3 , pp. 440-460
    • Talamo, F.1    D'Ambrosio, C.2    Arena, S.3    Del Vecchio, P.4    Ledda, L.5    Zehender, G.6
  • 98
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Bouley J., Chambon C., Picard B. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2004, 4:1811-1824.
    • (2004) Proteomics , vol.4 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 100
    • 67650429974 scopus 로고    scopus 로고
    • Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolagus cuniculus)
    • Almeida A.M., Campos A., van Harten S., Cardoso L.A., Coelho A.V. Establishment of a proteomic reference map for the gastrocnemius muscle in the rabbit (Oryctolagus cuniculus). Res Vet Sci 2009, 87:196-199.
    • (2009) Res Vet Sci , vol.87 , pp. 196-199
    • Almeida, A.M.1    Campos, A.2    van Harten, S.3    Cardoso, L.A.4    Coelho, A.V.5
  • 103
    • 77952053019 scopus 로고    scopus 로고
    • Proteomic investigation of the effects of weight loss in the gastrocnemius muscle of wild and NZW rabbits via 2D-electrophoresis and MALDI-TOF MS
    • Almeida A.M., Campos A., Francisco R., van Harten S., Cardoso L.A., Coelho A.V. Proteomic investigation of the effects of weight loss in the gastrocnemius muscle of wild and NZW rabbits via 2D-electrophoresis and MALDI-TOF MS. Anim Genet 2010, 41:260-272.
    • (2010) Anim Genet , vol.41 , pp. 260-272
    • Almeida, A.M.1    Campos, A.2    Francisco, R.3    van Harten, S.4    Cardoso, L.A.5    Coelho, A.V.6
  • 104
    • 84755161198 scopus 로고    scopus 로고
    • Differentially expressed proteins during fat accumulation in bovine skeletal muscle
    • Zhang Q., Lee H.-G., Han J.-A., Kim E.B., Kang S.K., Yin J., et al. Differentially expressed proteins during fat accumulation in bovine skeletal muscle. Meat Sci 2010, 86:814-820.
    • (2010) Meat Sci , vol.86 , pp. 814-820
    • Zhang, Q.1    Lee, H.-G.2    Han, J.-A.3    Kim, E.B.4    Kang, S.K.5    Yin, J.6
  • 105
    • 79958714052 scopus 로고    scopus 로고
    • Proteome changes in the insoluble protein fraction of bovine Longissimus dorsi muscle as a result of low-voltage electrical stimulation
    • Bjarnadóttir S.G., Hollung K., Høy M., Veiseth-Kent E. Proteome changes in the insoluble protein fraction of bovine Longissimus dorsi muscle as a result of low-voltage electrical stimulation. Meat Sci 2011, 89:143-149.
    • (2011) Meat Sci , vol.89 , pp. 143-149
    • Bjarnadóttir, S.G.1    Hollung, K.2    Høy, M.3    Veiseth-Kent, E.4
  • 106
    • 82355192275 scopus 로고    scopus 로고
    • Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: metabolomics and proteomics intertwined
    • D'Alessandro A., Marrocco C., Zolla V., D'Andrea M., Zolla L. Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: metabolomics and proteomics intertwined. J Proteomics 2011, 75:610-627.
    • (2011) J Proteomics , vol.75 , pp. 610-627
    • D'Alessandro, A.1    Marrocco, C.2    Zolla, V.3    D'Andrea, M.4    Zolla, L.5
  • 107
    • 2642568030 scopus 로고    scopus 로고
    • The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain
    • Doherty M.K., McLean L., Hayter J.R., Pratt J.M., Robertson D.H.L., El-Shafei A., et al. The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain. Proteomics 2004, 4:2082-2093.
    • (2004) Proteomics , vol.4 , pp. 2082-2093
    • Doherty, M.K.1    McLean, L.2    Hayter, J.R.3    Pratt, J.M.4    Robertson, D.H.L.5    El-Shafei, A.6
  • 108
    • 54449089070 scopus 로고    scopus 로고
    • Genetic diversity in native and commercial breeds of pigs in Portugal assessed by microsatellites
    • Vicente A.A., Carolino M.I., Sousa M.C.O., Ginja C., Silva F.S., Martinez A.M., et al. Genetic diversity in native and commercial breeds of pigs in Portugal assessed by microsatellites. J Anim Sci 2008, 86:2496-2507.
    • (2008) J Anim Sci , vol.86 , pp. 2496-2507
    • Vicente, A.A.1    Carolino, M.I.2    Sousa, M.C.O.3    Ginja, C.4    Silva, F.S.5    Martinez, A.M.6
  • 109
    • 79251508372 scopus 로고    scopus 로고
    • Proteome analysis of whole and water-soluble proteins in masseter and semitendinosus muscles of Holstein cows
    • Oe M., Ohnishi-Kameyama M., Nakajima I., Muroya S., Shibata M., Ojima K., et al. Proteome analysis of whole and water-soluble proteins in masseter and semitendinosus muscles of Holstein cows. Anim Sci J 2011, 82:181-186.
    • (2011) Anim Sci J , vol.82 , pp. 181-186
    • Oe, M.1    Ohnishi-Kameyama, M.2    Nakajima, I.3    Muroya, S.4    Shibata, M.5    Ojima, K.6
  • 110
    • 77951620846 scopus 로고    scopus 로고
    • Allergenicity study of EGFP-transgenic chicken meat by serological and 2D-DIGE analysis
    • Nakamura R., Nakamura R., Nakano M., Arisawa K., Ezaki R., Horiuchi H., et al. Allergenicity study of EGFP-transgenic chicken meat by serological and 2D-DIGE analysis. Food Chem Toxicol 2010, 48:1302-1310.
    • (2010) Food Chem Toxicol , vol.48 , pp. 1302-1310
    • Nakamura, R.1    Nakamura, R.2    Nakano, M.3    Arisawa, K.4    Ezaki, R.5    Horiuchi, H.6
  • 112
    • 60549106873 scopus 로고    scopus 로고
    • Transcriptomic and proteomic profiling of two porcine tissues using high-throughput technologies
    • Hornshøj H., Bendixen E., Conley L.N., Andersen P.K., Hedegaard J., Panitz F., et al. Transcriptomic and proteomic profiling of two porcine tissues using high-throughput technologies. BMC Genomics 2009, 10:30.
    • (2009) BMC Genomics , vol.10 , pp. 30
    • Hornshøj, H.1    Bendixen, E.2    Conley, L.N.3    Andersen, P.K.4    Hedegaard, J.5    Panitz, F.6
  • 113
    • 74849108510 scopus 로고    scopus 로고
    • Proteomic signature of muscle atrophy in rainbow trout
    • Salem M., Kenney P.B., Rexroad C.E., Yao J. Proteomic signature of muscle atrophy in rainbow trout. J Proteomics 2010, 73:778-789.
    • (2010) J Proteomics , vol.73 , pp. 778-789
    • Salem, M.1    Kenney, P.B.2    Rexroad, C.E.3    Yao, J.4
  • 115
    • 77953637963 scopus 로고    scopus 로고
    • Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: shifts in energy status and myofibrillar stability
    • Bjarnadóttir S.G., Hollung K., Faergestad E.M., Veiseth-Kent E. Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: shifts in energy status and myofibrillar stability. J Agric Food Chem 2010, 58:7408-7414.
    • (2010) J Agric Food Chem , vol.58 , pp. 7408-7414
    • Bjarnadóttir, S.G.1    Hollung, K.2    Faergestad, E.M.3    Veiseth-Kent, E.4
  • 116
    • 79951774411 scopus 로고    scopus 로고
    • Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity
    • Di Luca A., Mullen A.M., Elia G., Davey G., Hamill R.M. Centrifugal drip is an accessible source for protein indicators of pork ageing and water-holding capacity. Meat Sci 2011, 88:261-270.
    • (2011) Meat Sci , vol.88 , pp. 261-270
    • Di Luca, A.1    Mullen, A.M.2    Elia, G.3    Davey, G.4    Hamill, R.M.5
  • 119
    • 52649098420 scopus 로고    scopus 로고
    • Regional differences in porcine adipocytes isolated from skeletal muscle and adipose tissues as identified by a proteomic approach
    • Gondret F., Guitton N., Guillerm-Regost C., Louveau I. Regional differences in porcine adipocytes isolated from skeletal muscle and adipose tissues as identified by a proteomic approach. J Anim Sci 2008, 86:2115-2125.
    • (2008) J Anim Sci , vol.86 , pp. 2115-2125
    • Gondret, F.1    Guitton, N.2    Guillerm-Regost, C.3    Louveau, I.4
  • 120
    • 1242294371 scopus 로고    scopus 로고
    • Copper-associated liver disease: a proteomics study of copper challenge in a sheep model
    • Simpson D.M., Beynon R.J., Robertson D.H.L., Loughran M.J., Haywood S. Copper-associated liver disease: a proteomics study of copper challenge in a sheep model. Proteomics 2004, 4:524-536.
    • (2004) Proteomics , vol.4 , pp. 524-536
    • Simpson, D.M.1    Beynon, R.J.2    Robertson, D.H.L.3    Loughran, M.J.4    Haywood, S.5
  • 121
    • 79952318327 scopus 로고    scopus 로고
    • Proteomic analysis of swine serum following highly virulent classical swine fever virus infection
    • Sun J-fu, Shi Z-xue, Guo H-cheng, Li S., Tu C-chun Proteomic analysis of swine serum following highly virulent classical swine fever virus infection. Virol J 2011, 8:107.
    • (2011) Virol J , vol.8 , pp. 107
    • Sun, J.-F.1    Shi, Z.-X.2    Guo, H.-C.3    Li, S.4    Tu, C.-C.5
  • 122
    • 34748885730 scopus 로고    scopus 로고
    • Integrated analytical approach in veal calves administered the anabolic androgenic steroids boldenone and boldione: urine and plasma kinetic profile and changes in plasma protein expression
    • Draisci R., Montesissa C., Santamaria B., D'Ambrosio C., Ferretti G., Merlanti R., et al. Integrated analytical approach in veal calves administered the anabolic androgenic steroids boldenone and boldione: urine and plasma kinetic profile and changes in plasma protein expression. Proteomics 2007, 7:3184-3193.
    • (2007) Proteomics , vol.7 , pp. 3184-3193
    • Draisci, R.1    Montesissa, C.2    Santamaria, B.3    D'Ambrosio, C.4    Ferretti, G.5    Merlanti, R.6
  • 123
    • 0348147648 scopus 로고    scopus 로고
    • Characterization of a bovine pregnancy-associated protein using two-dimensional gel electrophoresis, N-terminal sequencing and mass spectrometry
    • Pyo J., Hwang S.-I., Oh J., Lee S.-J., Kang S.-C., Kim J.-S., et al. Characterization of a bovine pregnancy-associated protein using two-dimensional gel electrophoresis, N-terminal sequencing and mass spectrometry. Proteomics 2003, 3:2420-2427.
    • (2003) Proteomics , vol.3 , pp. 2420-2427
    • Pyo, J.1    Hwang, S.-I.2    Oh, J.3    Lee, S.-J.4    Kang, S.-C.5    Kim, J.-S.6
  • 124
    • 75949088794 scopus 로고    scopus 로고
    • Differential expression of liver proteins in Chianina and Holstein young bulls
    • Miarelli M., Signorelli F. Differential expression of liver proteins in Chianina and Holstein young bulls. J Anim Sci 2010, 88:593-598.
    • (2010) J Anim Sci , vol.88 , pp. 593-598
    • Miarelli, M.1    Signorelli, F.2
  • 125
    • 38649086403 scopus 로고    scopus 로고
    • Comparative proteomic analysis of livers from ketotic cows
    • Xu C., Wang Z. Comparative proteomic analysis of livers from ketotic cows. Vet Res Commun 2008, 32:263-273.
    • (2008) Vet Res Commun , vol.32 , pp. 263-273
    • Xu, C.1    Wang, Z.2
  • 126
    • 79955760759 scopus 로고    scopus 로고
    • Purification and identification of sperm surface proteins and changes during epididymal maturation
    • Belleannee C., Belghazi M., Labas V., Teixeira-Gomes A.-P., Gatti J.L., Dacheux J.-L., et al. Purification and identification of sperm surface proteins and changes during epididymal maturation. Proteomics 2011, 11:1952-1964.
    • (2011) Proteomics , vol.11 , pp. 1952-1964
    • Belleannee, C.1    Belghazi, M.2    Labas, V.3    Teixeira-Gomes, A.-P.4    Gatti, J.L.5    Dacheux, J.-L.6
  • 127
    • 84861341390 scopus 로고    scopus 로고
    • Proteomic characterization by 2-DE in bovine serum and whey from healthy and mastitis affected farm animals
    • In Press, available online December.
    • Alonso-Fauste I, Andrés M, Iturralde M, Lampreave F, Gallart J, Alava MA. Proteomic characterization by 2-DE in bovine serum and whey from healthy and mastitis affected farm animals. J Proteomics In Press, available online December 2011, http://dx.doi.org/10.1016/j.jprot.2011.11.035.
    • (2011) J Proteomics.
    • Alonso-Fauste, I.1    Andrés, M.2    Iturralde, M.3    Lampreave, F.4    Gallart, J.5    Alava, M.A.6
  • 128
    • 84862923501 scopus 로고    scopus 로고
    • Proteomics analysis of egg white proteins from different egg varieties
    • Wang J., Liang Y., Omana D.A., Kav N.N.V., Wu J. Proteomics analysis of egg white proteins from different egg varieties. J Agric Food Chem 2012, 60:272-282.
    • (2012) J Agric Food Chem , vol.60 , pp. 272-282
    • Wang, J.1    Liang, Y.2    Omana, D.A.3    Kav, N.N.V.4    Wu, J.5
  • 129
    • 34547872702 scopus 로고    scopus 로고
    • Global cooling: cold acclimation and the expression of soluble proteins in carp skeletal muscle
    • McLean L., Young I.S., Doherty M.K., Robertson D.H.L., Cossins A.R., Gracey A.Y., et al. Global cooling: cold acclimation and the expression of soluble proteins in carp skeletal muscle. Proteomics 2007, 7:2667-2681.
    • (2007) Proteomics , vol.7 , pp. 2667-2681
    • McLean, L.1    Young, I.S.2    Doherty, M.K.3    Robertson, D.H.L.4    Cossins, A.R.5    Gracey, A.Y.6
  • 131
    • 17644385255 scopus 로고    scopus 로고
    • Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax)
    • Monti G., De Napoli L., Mainolfi P., Barone R., Guida M., Marino G., et al. Monitoring food quality by microfluidic electrophoresis, gas chromatography, and mass spectrometry techniques: effects of aquaculture on the sea bass (Dicentrarchus labrax). Anal Chem 2005, 77:2587-2594.
    • (2005) Anal Chem , vol.77 , pp. 2587-2594
    • Monti, G.1    De Napoli, L.2    Mainolfi, P.3    Barone, R.4    Guida, M.5    Marino, G.6
  • 132
    • 84863673589 scopus 로고    scopus 로고
    • Analysis and comparison of proteomic profiles of tear fluid from human, cow, sheep, and camel eyes
    • Shamsi F.A., Chen Z., Liang J., Li K., Al-Rajhi A.A., Chaudhry I.A., et al. Analysis and comparison of proteomic profiles of tear fluid from human, cow, sheep, and camel eyes. Invest Ophthalmol Vis Sci 2011, 52:9156-9165.
    • (2011) Invest Ophthalmol Vis Sci , vol.52 , pp. 9156-9165
    • Shamsi, F.A.1    Chen, Z.2    Liang, J.3    Li, K.4    Al-Rajhi, A.A.5    Chaudhry, I.A.6


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