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Volumn 50, Issue 3, 2012, Pages 275-285

Food safety and quality control: Hints from proteomics

Author keywords

Food safety; Nutraceuticals; Proteomics; Quality control

Indexed keywords

EXPLORATORY ANALYSIS; FOOD QUALITY AND SAFETIES; GENETICALLY MODIFIED MAIZE; HEALTH ORGANIZATIONS; NUTRACEUTICALS; PROTEOMICS; QUANTITATIVE TRAIT LOCUS; TECHNICAL IMPROVEMENT;

EID: 84867432125     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (17)

References (81)
  • 1
    • 77955981327 scopus 로고    scopus 로고
    • Proteomics for quality-control processes in transfusion medicine
    • A. D'Alessandro, L. Zolla, Proteomics for quality-control processes in transfusion medicine, Anal. Bioanal. Chem. 398 (2010) 111-124.
    • (2010) Anal. Bioanal. Chem. , vol.398 , pp. 111-124
    • D'Alessandro, A.1    Zolla, L.2
  • 2
    • 78649732207 scopus 로고    scopus 로고
    • Application of proteomics in food technology and food biotechnology: Process development, quality control and product safety
    • D. Gašo-Sokač, S. Kovač, Dj. Josić, Application of proteomics in food technology and food biotechnology: Process development, quality control and product safety, Food Technol. Biotechnol. 48 (2010) 284-295.
    • (2010) Food Technol. Biotechnol. , vol.48 , pp. 284-295
    • Gašo-Sokač, D.1    Kovač, S.2    Josić, D.3
  • 3
    • 79952310105 scopus 로고    scopus 로고
    • Statistical issues in quality control of proteomic analyses: Good experimental design and planning
    • D.A. Cairns, Statistical issues in quality control of proteomic analyses: Good experimental design and planning, Proteomics, 11 (2011) 1037-1048.
    • (2011) Proteomics , vol.11 , pp. 1037-1048
    • Cairns, D.A.1
  • 4
    • 6344284935 scopus 로고    scopus 로고
    • The use of proteomics for the assessment of clinical samples in research
    • S. Aldred, M.M. Grant, H.R. Griffiths, The use of proteomics for the assessment of clinical samples in research, Clin. Biochem. 37 (2004) 943-952.
    • (2004) Clin. Biochem. , vol.37 , pp. 943-952
    • Aldred, S.1    Grant, M.M.2    Griffiths, H.R.3
  • 7
    • 34249745196 scopus 로고    scopus 로고
    • Proteomics of blood-based therapeutics: A promising tool for quality assurance in transfusion medicine
    • T. Thiele, L. Steil, U. Völker, A. Greinacher, Proteomics of blood-based therapeutics: A promising tool for quality assurance in transfusion medicine, BioDrugs, 21 (2007) 179-193.
    • (2007) BioDrugs , vol.21 , pp. 179-193
    • Thiele, T.1    Steil, L.2    Völker, U.3    Greinacher, A.4
  • 8
    • 78049379833 scopus 로고    scopus 로고
    • Comparison among plasma-derived clotting factor VIII by using monodimensional gel electrophoresis and mass spectrometry
    • A.M. Timperio, F. Gevi, G. Grazzini, S. Vaglio, L. Zolla, Comparison among plasma-derived clotting factor VIII by using monodimensional gel electrophoresis and mass spectrometry, Blood Transfusion, 8 (2010) 98-104.
    • (2010) Blood Transfusion , vol.8 , pp. 98-104
    • Timperio, A.M.1    Gevi, F.2    Grazzini, G.3    Vaglio, S.4    Zolla, L.5
  • 9
    • 70649093099 scopus 로고    scopus 로고
    • Proteomic characterization of plasma-derived clotting factor VIII - von Willebrand factor concentrates
    • J.G. Clifton, F. Huang, S. Kovac, X. Yang, D.C. Hixson, Dj. Josic, Proteomic characterization of plasma-derived clotting factor VIII - von Willebrand factor concentrates, Electrophoresis, 30 (2009) 3636-3646.
    • (2009) Electrophoresis , vol.30 , pp. 3636-3646
    • Clifton, J.G.1    Huang, F.2    Kovac, S.3    Yang, X.4    Hixson, D.C.5    Josic, Dj.6
  • 10
    • 73649136853 scopus 로고    scopus 로고
    • The red blood cell proteome and interactome: An update
    • A. D'Alessandro, P.G. Righetti, L. Zolla, The red blood cell proteome and interactome: An update, J. Proteome Res. 9 (2010) 144-163.
    • (2010) J. Proteome Res. , vol.9 , pp. 144-163
    • D'Alessandro, A.1    Righetti, P.G.2    Zolla, L.3
  • 11
    • 79960154426 scopus 로고    scopus 로고
    • Peroxiredoxin-2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions
    • S. Rinalducci, G.M. D'Amici, B. Blasi, S. Vaglio, G. Grazzini, L. Zolla, Peroxiredoxin-2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions, Transfusion, 51 (2011) 1439-1449.
    • (2011) Transfusion , vol.51 , pp. 1439-1449
    • Rinalducci, S.1    D'Amici, G.M.2    Blasi, B.3    Vaglio, S.4    Grazzini, G.5    Zolla, L.6
  • 12
    • 78649837277 scopus 로고    scopus 로고
    • Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds
    • L. Murgiano, A. D'Alessandro, M.G. Egidi, A. Crisà, G. Prosperini, A.M. Timperio et al., Proteomics and transcriptomics investigation on longissimus muscles in Large White and Casertana pig breeds, J. Proteome Res. 9 (2010) 6450- 6466.
    • (2010) J. Proteome Res. , vol.9 , pp. 6450-6466
    • Murgiano, L.1    D'Alessandro, A.2    Egidi, M.G.3    Crisà, A.4    Prosperini, G.5    Timperio, A.M.6
  • 13
    • 77954379514 scopus 로고    scopus 로고
    • Human milk proteins: An interactomics and updated functional overview
    • A. D'Alessandro, A. Scaloni, L. Zolla, Human milk proteins: An interactomics and updated functional overview, J. Proteome Res. 9 (2010) 3339-3373.
    • (2010) J. Proteome Res. , vol.9 , pp. 3339-3373
    • D'Alessandro, A.1    Scaloni, A.2    Zolla, L.3
  • 14
    • 77249107516 scopus 로고    scopus 로고
    • The egg white and yolk interactomes as gleaned from extensive proteomic data
    • A. D'Alessandro, P.G. Righetti, E. Fasoli, L. Zolla, The egg white and yolk interactomes as gleaned from extensive proteomic data, J. Proteomics, 73 (2010) 1028-1042.
    • (2010) J. Proteomics , vol.73 , pp. 1028-1042
    • D'Alessandro, A.1    Righetti, P.G.2    Fasoli, E.3    Zolla, L.4
  • 16
    • 70449519266 scopus 로고    scopus 로고
    • Comparative proteomics and transcriptomics analyses of livers from two different Bos taurus breeds: 'Chianina and Holstein Friesian'
    • A.M. Timperio, A. D'Alessandro, L. Pariset, G.M. D'Amici, A. Valentini, L. Zolla, Comparative proteomics and transcriptomics analyses of livers from two different Bos taurus breeds: 'Chianina and Holstein Friesian', J. Proteomics, 73 (2009) 309-322.
    • (2009) J. Proteomics , vol.73 , pp. 309-322
    • Timperio, A.M.1    D'Alessandro, A.2    Pariset, L.3    D'Amici, G.M.4    Valentini, A.5    Zolla, L.6
  • 18
    • 77954657745 scopus 로고    scopus 로고
    • Heard it through the grapevine: Proteomic perspective on grape and wine
    • M. Giribaldi, M.G. Giuffrida, Heard it through the grapevine: Proteomic perspective on grape and wine, J. Proteomics, 73 (2010) 1647-1655.
    • (2010) J. Proteomics , vol.73 , pp. 1647-1655
    • Giribaldi, M.1    Giuffrida, M.G.2
  • 19
    • 79951674235 scopus 로고    scopus 로고
    • Vulnerability of health to market forces
    • M. Brezis, W.H. Wiist, Vulnerability of health to market forces, Med. Care, 49 (2011) 232-239.
    • (2011) Med. Care , vol.49 , pp. 232-239
    • Brezis, M.1    Wiist, W.H.2
  • 20
    • 78049440083 scopus 로고    scopus 로고
    • Nature or nurture: Let food be your epigenetic medicine in chronic inflammatory disorders
    • K. Szarc vel Szic, M.N. Ndlovu, G. Haegeman, W. Vanden Berghe, Nature or nurture: Let food be your epigenetic medicine in chronic inflammatory disorders, Biochem. Pharmacol. 80 (2010) 1816-1832.
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1816-1832
    • Szarc vel Szic, K.1    Ndlovu, M.N.2    Haegeman, G.3    Vanden Berghe, W.4
  • 23
    • 77953927410 scopus 로고    scopus 로고
    • Advances in porcine genomics and proteomics - A toolbox for developing the pig as a model organism for molecular biomedical research
    • E. Bendixen, M. Danielsen, K. Larsen, C. Bendixen, Advances in porcine genomics and proteomics - A toolbox for developing the pig as a model organism for molecular biomedical research, Brief Funct. Genomics, 9 (2010) 208- 219.
    • (2010) Brief Funct. Genomics , vol.9 , pp. 208-219
    • Bendixen, E.1    Danielsen, M.2    Larsen, K.3    Bendixen, C.4
  • 25
    • 33644919384 scopus 로고    scopus 로고
    • Contribution of mass spectrometry to assess quality of milk-based products
    • P.A. Guy, F. Fenaille, Contribution of mass spectrometry to assess quality of milk-based products, Mass Spectrom. Rev. 25 (2006) 290-326.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 290-326
    • Guy, P.A.1    Fenaille, F.2
  • 26
    • 77953855865 scopus 로고    scopus 로고
    • Quantitative milk proteomics - Host responses to lipopolysaccharide-mediated inflammation of bovine mammary gland
    • M. Danielsen, M.C. Codrea, K.L. Ingvartsen, N.C. Friggens, E. Bendixen, C.M. Røntved, Quantitative milk proteomics - Host responses to lipopolysaccharide-mediated inflammation of bovine mammary gland, Proteomics, 10 (2010) 2240-2249.
    • (2010) Proteomics , vol.10 , pp. 2240-2249
    • Danielsen, M.1    Codrea, M.C.2    Ingvartsen, K.L.3    Friggens, N.C.4    Bendixen, E.5    Røntved, C.M.6
  • 28
    • 77953956761 scopus 로고    scopus 로고
    • Functional genomics and genetical genomics approaches towards elucidating networks of genes affecting meat performance in pigs
    • K. Wimmers, E. Murani, S. Ponsuksili, Functional genomics and genetical genomics approaches towards elucidating networks of genes affecting meat performance in pigs, Brief Funct. Genomics, 9 (2010) 251-258.
    • (2010) Brief Funct. Genomics , vol.9 , pp. 251-258
    • Wimmers, K.1    Murani, E.2    Ponsuksili, S.3
  • 29
    • 0034769635 scopus 로고    scopus 로고
    • Proteome analysis applied to meat science: Characterizing post mortem changes in porcine muscle
    • R. Lametsch, E. Bendixen, Proteome analysis applied to meat science: Characterizing post mortem changes in porcine muscle, J. Agric. Food Chem. 49 (2001) 4531-4537.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4531-4537
    • Lametsch, R.1    Bendixen, E.2
  • 30
    • 77954387385 scopus 로고    scopus 로고
    • Biochemistry of postmortem muscle - Lessons on mechanisms of meat tenderization
    • E. Huff Lonergan, W. Zhang, S.M. Lonergan, Biochemistry of postmortem muscle - Lessons on mechanisms of meat tenderization, Meat Sci. 86 (2010) 184-195.
    • (2010) Meat Sci , vol.86 , pp. 184-195
    • Huff Lonergan, E.1    Zhang, W.2    Lonergan, S.M.3
  • 31
    • 82355192275 scopus 로고    scopus 로고
    • Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: Metabolomics and proteomics intertwined
    • A. D'Alessandro, C. Marrocco, V. Zolla, M. D'Andrea, L. Zolla, Meat quality of the longissimus lumborum muscle of Casertana and Large White pigs: Metabolomics and proteomics intertwined, J. Proteomics, 75 (2011) 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
  • 32
    • 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
    • S.G. Bjarnadóttir, K. Hollung, M. Høy, E. Veiseth-Kent, Proteome changes in the insoluble protein fraction of bovine Longissimus dorsi muscle as a result of low-voltage electrical stimulation, Meat Sci. 89 (2011) 143-149.
    • (2011) Meat Sci , vol.89 , pp. 143-149
    • Bjarnadóttir, S.G.1    Hollung, K.2    Høy, M.3    Veiseth-Kent, E.4
  • 33
    • 84755161198 scopus 로고    scopus 로고
    • Differentially expressed proteins during fat accumulation in bovine skeletal muscle
    • Q. Zhang, H.G. Lee, J.A. Han, E.B. Kim, S.K. Kang, J. Yin et al., Differentially expressed proteins during fat accumulation in bovine skeletal muscle, Meat Sci. 86 (2010) 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
  • 34
    • 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
    • S.G. Bjarnadóttir, K. Hollung, E.M. Færgestad, E. Veiseth--Kent, Proteome changes in bovine longissimus thoracis muscle during the first 48 h postmortem: Shifts in energy status and myofibrillar stability, J. Agric. Food Chem. 58 (2010) 7408-7414.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 7408-7414
    • Bjarnadóttir, S.G.1    Hollung, K.2    Færgestad, E.M.3    Veiseth--Kent, E.4
  • 35
    • 79955018206 scopus 로고    scopus 로고
    • Intense degradation of myosin light chain isoforms in Spanish dry-cured ham
    • L. Mora, M.A. Sentandreu, F. Toldrá, Intense degradation of myosin light chain isoforms in Spanish dry-cured ham, J. Agric. Food Chem. 59 (2011) 3884-3892.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 3884-3892
    • Mora, L.1    Sentandreu, M.A.2    Toldrá, F.3
  • 39
    • 0022451471 scopus 로고
    • Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis
    • S.P. Wolff, R.T. Dean, Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis, Biochem. J. 234 (1986) 399-403.
    • (1986) Biochem. J. , vol.234 , pp. 399-403
    • Wolff, S.P.1    Dean, R.T.2
  • 40
    • 0023655449 scopus 로고
    • Protein damage and degradation by oxygen radicals: IV. Degradation of denatured protein
    • K.J.A. Davies, S.W. Lin, R.E. Pacifici, Protein damage and degradation by oxygen radicals: IV. Degradation of denatured protein, J. Biol. Chem. 262 (1987) 9914-9920.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9914-9920
    • Davies, K.J.A.1    Lin, S.W.2    Pacifici, R.E.3
  • 41
    • 33646525423 scopus 로고    scopus 로고
    • Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins
    • M. Morzel, S. Gatellier, T. Sayd, M. Renerre, E. Laville, Chemical oxidation decreases proteolytic susceptibility of skeletal muscle myofibrillar proteins, Meat Sci. 73 (2006) 536-543.
    • (2006) Meat Sci , vol.73 , pp. 536-543
    • Morzel, M.1    Gatellier, S.2    Sayd, T.3    Renerre, M.4    Laville, E.5
  • 42
    • 77957298699 scopus 로고    scopus 로고
    • Control of beef tenderness: Identification of biological markers, INRA Prod
    • N. Guillemin, I. Cassar-Malek, J.F. Hocquette, C. Jurie, D. Micol, A. Listrat et al., Control of beef tenderness: Identification of biological markers, INRA Prod. Anim. 22 (2009) 331-344.
    • (2009) Anim , vol.22 , pp. 331-344
    • Guillemin, N.1    Cassar-Malek, I.2    Hocquette, J.F.3    Jurie, C.4    Micol, D.5    Listrat, A.6
  • 43
    • 79958807293 scopus 로고    scopus 로고
    • Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type
    • N. Guillemin, C. Jurie, I. Cassar-Malek, J.F. Hocquette, G. Renand, B. Picard, Variations in the abundance of 24 protein biomarkers of beef tenderness according to muscle and animal type, Animal, 5 (2011) 885-894.
    • (2011) Animal , vol.5 , pp. 885-894
    • Guillemin, N.1    Jurie, C.2    Cassar-Malek, I.3    Hocquette, J.F.4    Renand, G.5    Picard, B.6
  • 44
    • 0038463515 scopus 로고    scopus 로고
    • Proteome analysis applied to the study of muscle development and sensorial qualities of bovine meat
    • J. Bouley, C. Chambon, B. Picard, Proteome analysis applied to the study of muscle development and sensorial qualities of bovine meat, Sci. Aliment. 23 (2003) 75-78.
    • (2003) Sci. Aliment. , vol.23 , pp. 75-78
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 45
    • 72449156073 scopus 로고    scopus 로고
    • Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization
    • E. Laville, T. Sayd, M. Morzel, S. Blinet, C. Chambon, J. Lepetit et al., Proteome changes during meat aging in tough and tender beef suggest the importance of apoptosis and protein solubility for beef aging and tenderization, J. Agric. Food Chem. 57 (2009) 10755-10764.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 10755-10764
    • Laville, E.1    Sayd, T.2    Morzel, M.3    Blinet, S.4    Chambon, C.5    Lepetit, J.6
  • 46
    • 36749014526 scopus 로고    scopus 로고
    • Muscle proteome and meat eating qualities of Longissimus thoracis of 'Blonde d'Aquitaine' young bulls: A central role of HSP27 isoforms
    • M. Morzel, C. Terlouw, C. Chambon, D. Micol, B. Picard, Muscle proteome and meat eating qualities of Longissimus thoracis of 'Blonde d'Aquitaine' young bulls: A central role of HSP27 isoforms, Meat Sci. 78 (2008) 297-304.
    • (2008) Meat Sci , vol.78 , pp. 297-304
    • Morzel, M.1    Terlouw, C.2    Chambon, C.3    Micol, D.4    Picard, B.5
  • 47
    • 0032858218 scopus 로고    scopus 로고
    • HSP27 in signal transduction and association with contractile proteins in smooth muscle cells
    • A.I. Ibitayo, J. Sladick, S. Tuteja, O. Louis-Jacques, H. Yamada, G. Groblewski et al., HSP27 in signal transduction and association with contractile proteins in smooth muscle cells, Am. J. Physiol. 277 (1999) 445-454.
    • (1999) Am. J. Physiol. , vol.277 , pp. 445-454
    • Ibitayo, A.I.1    Sladick, J.2    Tuteja, S.3    Louis-Jacques, O.4    Yamada, H.5    Groblewski, G.6
  • 48
    • 52249101738 scopus 로고    scopus 로고
    • Pig Longissimus lumborum proteome: Part I. Effects of genetic background, rearing environment and gender
    • A. Kwasiborski, T. Sayd, C. Chambon, V. Santé-Lhoutellier, D. Rocha, C. Terlouw, Pig Longissimus lumborum proteome: Part I. Effects of genetic background, rearing environment and gender, Meat Sci. 80 (2008) 968-981.
    • (2008) Meat Sci , vol.80 , pp. 968-981
    • Kwasiborski, A.1    Sayd, T.2    Chambon, C.3    Santé-Lhoutellier, V.4    Rocha, D.5    Terlouw, C.6
  • 49
    • 52249120543 scopus 로고    scopus 로고
    • Pig Longissimus lumborum proteome: Part II: Relationships between protein content and meat quality
    • A. Kwasiborski, T. Sayd, C. Chambon, V. Santé-Lhoutellier, D. Rocha, C. Terlouw, Pig Longissimus lumborum proteome: Part II: Relationships between protein content and meat quality, Meat Sci. 80 (2008) 982-996.
    • (2008) Meat Sci , vol.80 , pp. 982-996
    • Kwasiborski, A.1    Sayd, T.2    Chambon, C.3    Santé-Lhoutellier, V.4    Rocha, D.5    Terlouw, C.6
  • 50
  • 52
    • 79960472212 scopus 로고    scopus 로고
    • Peptide biomarkers as a way to determine meat authenticity
    • M.A. Sentandreu, E. Sentandreu, Peptide biomarkers as a way to determine meat authenticity, Meat Sci. 89 (2011) 280-285.
    • (2011) Meat Sci , vol.89 , pp. 280-285
    • Sentandreu, M.A.1    Sentandreu, E.2
  • 53
    • 1842478237 scopus 로고    scopus 로고
    • Understanding milk's bioactive components: A goal for the genomics toolbox
    • R.E. Ward, J.B. German, Understanding milk's bioactive components: A goal for the genomics toolbox, J. Nutr. (Suppl.), 134 (2004) 962-967.
    • (2004) J. Nutr , Issue.SUPPL , pp. 962-967
    • Ward, R.E.1    German, J.B.2
  • 54
    • 70449705857 scopus 로고    scopus 로고
    • OMICS-rooted studies of milk proteins, oligosaccharides and lipids
    • B. Casado, M. Affolter, M. Kussmann, OMICS-rooted studies of milk proteins, oligosaccharides and lipids, J. Proteomics, 73 (2009) 196-208.
    • (2009) J. Proteomics , vol.73 , pp. 196-208
    • Casado, B.1    Affolter, M.2    Kussmann, M.3
  • 56
    • 38749131273 scopus 로고    scopus 로고
    • Independent introduction of two lactase-persistence alleles into human populations reflects different history of adaptation to milk culture
    • N.S. Enattah, T.G. Jensen, M. Nielsen, R. Lewinski, M. Kuokkanen, H. Rasinpera et al., Independent introduction of two lactase-persistence alleles into human populations reflects different history of adaptation to milk culture, Am. J. Hum. Genet. 82 (2008) 57-72.
    • (2008) Am. J. Hum. Genet. , vol.82 , pp. 57-72
    • Enattah, N.S.1    Jensen, T.G.2    Nielsen, M.3    Lewinski, R.4    Kuokkanen, M.5    Rasinpera, H.6
  • 57
    • 33845972952 scopus 로고    scopus 로고
    • Protein and lipid composition of bovine milk-fat-globule membrane
    • B.Y. Fong, C.S. Norris, A.K.H. McGibbon, Protein and lipid composition of bovine milk-fat-globule membrane, Int. Dairy J. 17 (2007) 275-288.
    • (2007) Int. Dairy J. , vol.17 , pp. 275-288
    • Fong, B.Y.1    Norris, C.S.2    McGibbon, A.K.H.3
  • 58
    • 44949253954 scopus 로고    scopus 로고
    • Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk
    • T.A. Reinhardt, J.D. Lippolis, Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk, J. Dairy Sci. 91 (2008) 2307-2318.
    • (2008) J. Dairy Sci. , vol.91 , pp. 2307-2318
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 60
    • 55249117743 scopus 로고    scopus 로고
    • Glycoproteomics of milk: Differences in sugar epitopes on human and bovine milk fat globule membranes
    • N.L. Wilson, L.J. Robinson, A. Donnet, L. Bovetto, N.H. Packer, N.G. Karlsson, Glycoproteomics of milk: Differences in sugar epitopes on human and bovine milk fat globule membranes, J. Proteome Res. 7 (2008) 3687-3696.
    • (2008) J. Proteome Res. , vol.7 , pp. 3687-3696
    • Wilson, N.L.1    Robinson, L.J.2    Donnet, A.3    Bovetto, L.4    Packer, N.H.5    Karlsson, N.G.6
  • 61
    • 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
    • C. D'Ambrosio, S. Arena, A.M. Salzano, G. Renzone, L. Ledda, A. Scaloni, 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 (2008) 3657-3666.
    • (2008) Proteomics , vol.8 , pp. 3657-3666
    • D'Ambrosio, C.1    Arena, S.2    Salzano, A.M.3    Renzone, G.4    Ledda, L.5    Scaloni, A.6
  • 62
    • 3042854907 scopus 로고    scopus 로고
    • Differential protein composition of bovine whey: A comparison of whey from healthy animals and from those with clinical mastitis
    • C.J. Hogarth, J.L. Fitzpatrick, A.M. Nolan, F.J. Young, A. Pitt, P.D. Eckersall, Differential protein composition of bovine whey: A comparison of whey from healthy animals and from those with clinical mastitis, Proteomics, 4 (2004) 2094-2100.
    • (2004) Proteomics , vol.4 , pp. 2094-2100
    • Hogarth, C.J.1    Fitzpatrick, J.L.2    Nolan, A.M.3    Young, F.J.4    Pitt, A.5    Eckersall, P.D.6
  • 63
    • 77957192354 scopus 로고    scopus 로고
    • Modern proteomic methodologies for the characterization of lactosylation protein targets in milk
    • S. Arena, G. Renzone, G. Novi, A. Paffetti, G. Bernardini, A. Santucci, A. Scaloni, Modern proteomic methodologies for the characterization of lactosylation protein targets in milk, Proteomics, 10 (2010) 3414-3434.
    • (2010) Proteomics , vol.10 , pp. 3414-3434
    • Arena, S.1    Renzone, G.2    Novi, G.3    Paffetti, A.4    Bernardini, G.5    Santucci, A.6    Scaloni, A.7
  • 64
    • 33646192548 scopus 로고    scopus 로고
    • Major technological advances and trends in cheese
    • M.E. Johnson, J.A. Lucey, Major technological advances and trends in cheese, J. Dairy Sci. 89 (2006) 1174-1178.
    • (2006) J. Dairy Sci. , vol.89 , pp. 1174-1178
    • Johnson, M.E.1    Lucey, J.A.2
  • 65
    • 31544454202 scopus 로고    scopus 로고
    • Proteomic evaluation of milk from different mammalian species as a substitute for breast milk
    • E. D'Auria, C. Agostoni, M. Giovannini, E. Riva, R. Zetterström, R. Fortin et al., Proteomic evaluation of milk from different mammalian species as a substitute for breast milk, Acta Paediatr. 94 (2005) 1708-1713.
    • (2005) Acta Paediatr , vol.94 , pp. 1708-1713
    • D'Auria, E.1    Agostoni, C.2    Giovannini, M.3    Riva, E.4    Zetterström, R.5    Fortin, R.6
  • 66
    • 0346059361 scopus 로고    scopus 로고
    • The French paradox: Lessons for other countries
    • J. Ferrières, The French paradox: Lessons for other countries, Heart, 90 (2004) 107-111.
    • (2004) Heart , vol.90 , pp. 107-111
    • Ferrières, J.1
  • 68
    • 33745575079 scopus 로고    scopus 로고
    • Mass spectrometry in the analysis of grape and wine proteins
    • R. Flamini, M. De Rosso, Mass spectrometry in the analysis of grape and wine proteins, Exp. Rev. Proteomics, 3 (2006) 321-331.
    • (2006) Exp. Rev. Proteomics , vol.3 , pp. 321-331
    • Flamini, R.1    De Rosso, M.2
  • 70
    • 33847220001 scopus 로고    scopus 로고
    • Influence of Botrytis cinerea infection on Champagne wine proteins (characterized by two-dimensional electrophoresis/ immunodetection) and wine foaming properties
    • C. Cilindre, A.J. Castro, C. Clément, P. Jeandet, R. Marchal, Influence of Botrytis cinerea infection on Champagne wine proteins (characterized by two-dimensional electrophoresis/ immunodetection) and wine foaming properties, Food Chem. 103 (2007) 139-149.
    • (2007) Food Chem , vol.103 , pp. 139-149
    • Cilindre, C.1    Castro, A.J.2    Clément, C.3    Jeandet, P.4    Marchal, R.5
  • 71
    • 69349099800 scopus 로고    scopus 로고
    • Construction of a novel beer proteome map and its use in beer quality control
    • T. Iimure, N. Nankaku, N. Hirota, Z. Tiansu, T. Hoki, M. Kihara et al., Construction of a novel beer proteome map and its use in beer quality control, Food Chem. 118 (2010) 566-574.
    • (2010) Food Chem , vol.118 , pp. 566-574
    • Iimure, T.1    Nankaku, N.2    Hirota, N.3    Tiansu, Z.4    Hoki, T.5    Kihara, M.6
  • 73
    • 33645777854 scopus 로고    scopus 로고
    • Application of two-dimensional gel electrophoresis to interrogate alterations in the proteome of genetically modified crops. 3. Assessing unintended effects
    • M.C. Ruebelt, M. Lipp, T.L. Reynolds, J.J. Schmuke, J.D. Astwood, D. DellaPenna et al., Application of two-dimensional gel electrophoresis to interrogate alterations in the proteome of genetically modified crops. 3. Assessing unintended effects, J. Agric. Food Chem. 54 (2006) 2169-2177.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 2169-2177
    • Ruebelt, M.C.1    Lipp, M.2    Reynolds, T.L.3    Schmuke, J.J.4    Astwood, J.D.5    DellaPenna, D.6
  • 74
    • 52049102730 scopus 로고    scopus 로고
    • Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modifications
    • L. Zolla, S. Rinalducci, P. Antonioli, P.G. Righetti, Proteomics as a complementary tool for identifying unintended side effects occurring in transgenic maize seeds as a result of genetic modifications, J. Proteome Res. 7 (2008) 1850- 1861.
    • (2008) J. Proteome Res. , vol.7 , pp. 1850-1861
    • Zolla, L.1    Rinalducci, S.2    Antonioli, P.3    Righetti, P.G.4
  • 76
    • 67650925450 scopus 로고    scopus 로고
    • NMR metabolic profiling of transgenic maize with the Cry1Ab gene
    • F. Piccioni, D. Capitani, L. Zolla, L. Mannina, NMR metabolic profiling of transgenic maize with the Cry1Ab gene, J. Agric. Food Chem. 57 (2009) 6041-6049.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 6041-6049
    • Piccioni, F.1    Capitani, D.2    Zolla, L.3    Mannina, L.4
  • 77
    • 84855553803 scopus 로고    scopus 로고
    • We are what we eat: Food safety and proteomics
    • A. D'Alessandro, L. Zolla, We are what we eat: Food safety and proteomics, J. Proteome Res. 11 (2012) 26-36.
    • (2012) J. Proteome Res. , vol.11 , pp. 26-36
    • D'Alessandro, A.1    Zolla, L.2
  • 78
    • 34548630583 scopus 로고    scopus 로고
    • Screening method for the addition of bovine blood-based binding agents to food using liquid chromatography triple quadrupole mass spectrometry
    • H.H. Grundy, P. Reece, M.D. Sykes, J.A. Clough, N. Audsley, R. Stones, Screening method for the addition of bovine blood-based binding agents to food using liquid chromatography triple quadrupole mass spectrometry, Rapid Commun. Mass Spectrom. 21 (2007) 2919-2925.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 2919-2925
    • Grundy, H.H.1    Reece, P.2    Sykes, M.D.3    Clough, J.A.4    Audsley, N.5    Stones, R.6
  • 79
    • 73449101111 scopus 로고    scopus 로고
    • A food safety control low mass--range proteomics platform for the detection of illicit treatments in veal calves by MALDI-TOF-MS serum profiling
    • L. Della Donna, M. Ronci, P. Sacchetta, C. Di Ilio, B. Biolatti, G. Federici et al., A food safety control low mass--range proteomics platform for the detection of illicit treatments in veal calves by MALDI-TOF-MS serum profiling, Biotechnol. J. 4 (2009) 1596-1609.
    • (2009) Biotechnol. J. , vol.4 , pp. 1596-1609
    • Della Donna, L.1    Ronci, M.2    Sacchetta, P.3    Di Ilio, C.4    Biolatti, B.5    Federici, G.6
  • 80
    • 67651108596 scopus 로고    scopus 로고
    • Ongoing revolution in bacteriology: Routine identification of bacteria by matrix-assisted laser desorption ionization time-of-flight mass spectrometry
    • P. Seng, M. Drancourt, F. Gouriet, B. La Scola, P.E. Fournier, J.M. Rolain, D. Raoult, Ongoing revolution in bacteriology: Routine identification of bacteria by matrix-assisted laser desorption ionization time-of-flight mass spectrometry, Clin. Infect. Dis. 49 (2009) 543-551.
    • (2009) Clin. Infect. Dis. , vol.49 , pp. 543-551
    • Seng, P.1    Drancourt, M.2    Gouriet, F.3    La Scola, B.4    Fournier, P.E.5    Rolain, J.M.6    Raoult, D.7
  • 81
    • 78649629973 scopus 로고    scopus 로고
    • Pharmacoproteomics: A chess game on a protein field
    • A. D'Alessandro, L. Zolla, Pharmacoproteomics: A chess game on a protein field, Drug Discov. Today, 15 (2010) 1015-1023.
    • (2010) Drug Discov. Today , vol.15 , pp. 1015-1023
    • D'Alessandro, A.1    Zolla, L.2


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