메뉴 건너뛰기




Volumn 50, Issue 3, 2012, Pages 286-305

Novel mass spectrometry-based applications of the 'omic': Sciences in food technology and biotechnology

Author keywords

Food proteins and peptides; Food quality; Food safety; Food technology; Interactomics; Mass spectrometry; Metabolomics; Peptidomics; Proteomics

Indexed keywords

FOOD PROTEINS; FOOD QUALITY; INTERACTOMICS; METABOLOMICS; PEPTIDOMICS; PROTEOMICS;

EID: 84867450906     PISSN: 13309862     EISSN: 13342606     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (42)

References (225)
  • 1
    • 77957360551 scopus 로고    scopus 로고
    • Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives
    • M. Kussmann, A. Panchaud, M. Affolter, Proteomics in nutrition: Status quo and outlook for biomarkers and bioactives, J. Proteome Res. 10 (2010) 4876-4887.
    • (2010) J. Proteome Res. , vol.10 , pp. 4876-4887
    • Kussmann, M.1    Panchaud, A.2    Affolter, M.3
  • 2
    • 84867475032 scopus 로고    scopus 로고
    • Guidance Document of the Scientific Panel on Genetically Modified Organisms for the Risk Assessment of Genetically Modified Plants and Derived Food and Feed, Parma, Italy
    • Guidance Document of the Scientific Panel on Genetically Modified Organisms for the Risk Assessment of Genetically Modified Plants and Derived Food and Feed, European Food Safety Agency (EFSA), Parma, Italy (2006)
    • (2006) European Food Safety Agency (EFSA)
  • 5
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • B. Domon, R. Aebersold, Mass spectrometry and protein analysis, Science, 312 (2006) 212-217.
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 6
    • 80053063559 scopus 로고    scopus 로고
    • Mass spectrometry in systems biology: An introduction
    • W.B. Dunn, Mass spectrometry in systems biology: An introduction, Methods Enzymol. 500 (2011) 15-35.
    • (2011) Methods Enzymol , vol.500 , pp. 15-35
    • Dunn, W.B.1
  • 7
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold, M. Mann, Mass spectrometry-based proteomics, Nature, 422 (2003) 198-207.
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 8
    • 0024438708 scopus 로고
    • Electrospray ionization for the mass spectrometry of large biomolecules
    • J.B. Fenn, M. Mann, C.K. Meng, S.F. Wong, C.M. Whitehouse, Electrospray ionization for the mass spectrometry of large biomolecules, Science, 246 (1989) 64-71.
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 9
    • 0024289037 scopus 로고
    • Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons
    • M. Karas, F. Hillenkamp, Laser desorption ionization of proteins with molecular masses exceeding 10000 daltons, Anal. Chem. 60 (1989) 2299-2301.
    • (1989) Anal. Chem. , vol.60 , pp. 2299-2301
    • Karas, M.1    Hillenkamp, F.2
  • 10
    • 0031962612 scopus 로고    scopus 로고
    • Mass spectrometry and the age of the proteome
    • J.R Yates III, Mass spectrometry and the age of the proteome, J. Mass Spectrom. 33 (1998) 1-19.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 1-19
    • Yates III, J.R.1
  • 11
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrometry: Approaches, advances, and applications
    • J.R. Yates III, C.I. Ruse, A. Nakorchevsky, Proteomics by mass spectrometry: Approaches, advances, and applications, Annu. Rev. Biomed. Eng. 11 (2009) 49-79.
    • (2009) Annu. Rev. Biomed. Eng. , vol.11 , pp. 49-79
    • Yates III, J.R.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 12
    • 13844312665 scopus 로고    scopus 로고
    • Differential proteomics: An overview of gel and non-gel based approaches
    • L. Monteoliva, J.P. Albar, Differential proteomics: An overview of gel and non-gel based approaches, Brief. Funct. Genomic. Proteomic. 3 (2004) 220-239.
    • (2004) Brief. Funct. Genomic. Proteomic. , vol.3 , pp. 220-239
    • Monteoliva, L.1    Albar, J.P.2
  • 13
    • 36448962323 scopus 로고    scopus 로고
    • MudPIT: Multidimensional protein identification technology
    • C.M. Delahunty, J.R. Yates III, MudPIT: Multidimensional protein identification technology, Biotechniques, 43 (2007) 565-567.
    • (2007) Biotechniques , vol.43 , pp. 565-567
    • Delahunty, C.M.1    Yates III, J.R.2
  • 14
    • 51949083217 scopus 로고    scopus 로고
    • Practical implementation of 2D HPLC scheme with accurate peptide retention prediction in both dimensions for high-throughput bottom-up proteomics
    • R.C. Dwivedi, V. Spicer, M. Harder, M. Antonovici, W. Ens, K.G. Standing et al., Practical implementation of 2D HPLC scheme with accurate peptide retention prediction in both dimensions for high-throughput bottom-up proteomics, Anal. Chem. 80 (2008) 7036-7042.
    • (2008) Anal. Chem. , vol.80 , pp. 7036-7042
    • Dwivedi, R.C.1    Spicer, V.2    Harder, M.3    Antonovici, M.4    Ens, W.5    Standing, K.G.6
  • 15
    • 0035582244 scopus 로고    scopus 로고
    • An automated multidimensional protein identification technology for shotgun proteomics
    • D.A. Wolters, M.P. Washburn, J.R. Yates III, An automated multidimensional protein identification technology for shotgun proteomics, Anal. Chem. 73 (2001) 5683-5690.
    • (2001) Anal. Chem. , vol.73 , pp. 5683-5690
    • Wolters, D.A.1    Washburn, M.P.2    Yates III, J.R.3
  • 16
    • 0000178042 scopus 로고
    • Micro-electrospray mass spectrometry: Ultra-high-sensitivity analysis of peptides and proteins
    • R. Emmett, R.M. Caprioli, Micro-electrospray mass spectrometry: Ultra-high-sensitivity analysis of peptides and proteins, J. Am. Soc. Mass Spectrom. 5 (1994) 605-613.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 605-613
    • Emmett, R.1    Caprioli, R.M.2
  • 18
    • 78649406605 scopus 로고    scopus 로고
    • Achievements and perspectives of top-down proteomics
    • A. Armirotti, G. Damonte, Achievements and perspectives of top-down proteomics, Proteomics, 10 (2010) 3566-3576.
    • (2010) Proteomics , vol.10 , pp. 3566-3576
    • Armirotti, A.1    Damonte, G.2
  • 19
    • 74249106136 scopus 로고    scopus 로고
    • What does the future hold for top down mass spectrometry?
    • B.A. Garcia, What does the future hold for top down mass spectrometry?, J. Am. Soc. Mass Spectrom. 21 (2010) 193- 202.
    • (2010) J. Am. Soc. Mass Spectrom. , vol.21 , pp. 193-202
    • Garcia, B.A.1
  • 21
    • 80052530606 scopus 로고    scopus 로고
    • Top-down mass spectrometry: Recent developments, applications and perspectives
    • W. Cui, H.W. Rohrs, M.L. Gross, Top-down mass spectrometry: Recent developments, applications and perspectives, Analyst, 139 (2011) 3854-3864.
    • (2011) Analyst , vol.139 , pp. 3854-3864
    • Cui, W.1    Rohrs, H.W.2    Gross, M.L.3
  • 22
    • 80051682403 scopus 로고    scopus 로고
    • Advances in metabolite identification
    • D.S. Wishart, Advances in metabolite identification, Bioanalysis, 3 (2011) 1769-1782.
    • (2011) Bioanalysis , vol.3 , pp. 1769-1782
    • Wishart, D.S.1
  • 23
    • 77951031841 scopus 로고    scopus 로고
    • Challenges in mass spectrometry based targeted metabolomics
    • T. Koal, H.P. Deigner, Challenges in mass spectrometry based targeted metabolomics, Curr. Mol. Med. 10 (2010) 216-226.
    • (2010) Curr. Mol. Med. , vol.10 , pp. 216-226
    • Koal, T.1    Deigner, H.P.2
  • 25
    • 0000728041 scopus 로고
    • Technological properties of milk as influenced by genetic polymorphism of milk proteins -A review
    • E. Jakob, Z. Puhan, Technological properties of milk as influenced by genetic polymorphism of milk proteins - A review, Int. Dairy J. 2 (1992) 157-178.
    • (1992) Int. Dairy J. , vol.2 , pp. 157-178
    • Jakob, E.1    Puhan, Z.2
  • 26
    • 0029298872 scopus 로고
    • Primary structure of ovine as1-caseins: Localization of phosphorylation sites and characterization of genetic variants A, C and D
    • P. Ferranti, A. Malorni, G. Nitti, P. Laezza, R. Pizzano, L. Chianese, F. Addeo, Primary structure of ovine as1-caseins: Localization of phosphorylation sites and characterization of genetic variants A, C and D, J. Dairy Res. 62 (1995) 281-296.
    • (1995) J. Dairy Res. , vol.62 , pp. 281-296
    • Ferranti, P.1    Malorni, A.2    Nitti, G.3    Laezza, P.4    Pizzano, R.5    Chianese, L.6    Addeo, F.7
  • 27
    • 0033178923 scopus 로고    scopus 로고
    • Effects of sheep as1-casein CC, CD and DD genotypes on milk composition and cheesemaking properties
    • A. Pirisi, G. Piredda, C.M. Papoff, R. Di Salvo, S. Pintus, G. Garro et al., Effects of sheep as1-casein CC, CD and DD genotypes on milk composition and cheesemaking properties, J. Dairy Res. 66 (1999) 409-419.
    • (1999) J. Dairy Res. , vol.66 , pp. 409-419
    • Pirisi, A.1    Piredda, G.2    Papoff, C.M.3    Di Salvo, R.4    Pintus, S.5    Garro, G.6
  • 29
    • 0001104174 scopus 로고    scopus 로고
    • The co-presence of deleted protein species generates the structural heterogeneity of ovine as1-casein
    • P. Ferranti, L. Chianese, A. Malorni, F. Migliaccio, V. Stingo, F. Addeo, The co-presence of deleted protein species generates the structural heterogeneity of ovine as1-casein, J. Agric. Food Chem. 46 (1998) 411-416.
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 411-416
    • Ferranti, P.1    Chianese, L.2    Malorni, A.3    Migliaccio, F.4    Stingo, V.5    Addeo, F.6
  • 30
    • 0030873812 scopus 로고    scopus 로고
    • Differential splicing of pre-messenger RNA produces multipe forms of caprine as1-casein
    • P. Ferranti, F. Addeo, L. Chianese, A. Malorni, C. Leroux, P. Martin, Differential splicing of pre-messenger RNA produces multipe forms of caprine as1-casein, Eur. J. Biochem. 249 (1997) 1-7.
    • (1997) Eur. J. Biochem. , vol.249 , pp. 1-7
    • Ferranti, P.1    Addeo, F.2    Chianese, L.3    Malorni, A.4    Leroux, C.5    Martin, P.6
  • 31
    • 54749091999 scopus 로고    scopus 로고
    • The primary structure of the water buffalo as1-and b-casein: Identification of phosphorylation sites and characterization of a novel b-casein variant
    • P. Ferranti, A. Scaloni, S. Caira, L. Chianese, A. Malorni, F. Addeo, The primary structure of the water buffalo as1- and b-casein: Identification of phosphorylation sites and characterization of a novel b-casein variant, J. Prot. Chem. 17 (1998) 835-844.
    • (1998) J. Prot. Chem. , vol.17 , pp. 835-844
    • Ferranti, P.1    Scaloni, A.2    Caira, S.3    Chianese, L.4    Malorni, A.5    Addeo, F.6
  • 32
    • 79953697144 scopus 로고    scopus 로고
    • Proteomic characterization of human milk whey proteins during a twelve-month lactation period
    • Y. Liao, R. Alvarado, B. Phinney, B. Lönnerdal, Proteomic characterization of human milk whey proteins during a twelve-month lactation period, J. Proteome Res. 10 (2011) 1746-1754.
    • (2011) J. Proteome Res. , vol.10 , pp. 1746-1754
    • Liao, Y.1    Alvarado, R.2    Phinney, B.3    Lönnerdal, B.4
  • 33
    • 3543112680 scopus 로고    scopus 로고
    • Proteomic tools to characterize the protein fraction of Equidae milk
    • G. Miranda, M.F. Mahé, C. Leroux, P. Martin, Proteomic tools to characterize the protein fraction of Equidae milk, Proteomics, 4 (2004) 2496-509.
    • (2004) Proteomics , vol.4 , pp. 2496-2509
    • Miranda, G.1    Mahé, M.F.2    Leroux, C.3    Martin, P.4
  • 36
    • 0347134597 scopus 로고    scopus 로고
    • Casein phosphoproteome: Identification of phosphoproteins by combined mass spectrometry and two--dimensional gel electrophoresis
    • G. Mamone, S. Caira, G. Garro, A. Nicolai, P. Ferranti, G. Picariello et al., Casein phosphoproteome: Identification of phosphoproteins by combined mass spectrometry and two--dimensional gel electrophoresis, Electrophoresis, 24 (2003) 2824-2837.
    • (2003) Electrophoresis , vol.24 , pp. 2824-2837
    • Mamone, G.1    Caira, S.2    Garro, G.3    Nicolai, A.4    Ferranti, P.5    Picariello, G.6
  • 37
    • 76649129012 scopus 로고    scopus 로고
    • Hydroxyapatite affinity chromatography for the highly selective enrichment of mono-and multi-phosphorylated peptides in phosphoproteome analysis
    • G. Mamone, G. Picariello, P. Ferranti, F. Addeo, Hydroxyapatite affinity chromatography for the highly selective enrichment of mono- and multi-phosphorylated peptides in phosphoproteome analysis, Proteomics, 10 (2010) 380-393.
    • (2010) Proteomics , vol.10 , pp. 380-393
    • Mamone, G.1    Picariello, G.2    Ferranti, P.3    Addeo, F.4
  • 39
    • 64149099586 scopus 로고    scopus 로고
    • Fast screening and quantitative evaluation of internally deleted goat as1-casein variants by mass spectrometric detection of the signature peptides
    • G. Picariello, P. Ferranti, S. Caira, O. Fierro, L. Chianese, F. Addeo, Fast screening and quantitative evaluation of internally deleted goat as1-casein variants by mass spectrometric detection of the signature peptides, Rapid Commun. Mass Spectrom. 23 (2009) 775-787.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 775-787
    • Picariello, G.1    Ferranti, P.2    Caira, S.3    Fierro, O.4    Chianese, L.5    Addeo, F.6
  • 40
    • 0042404510 scopus 로고
    • Structural Differences in Allelic Glutenin Subunits of High and Low Mr and Their Relationships with Flour Technological Properties
    • J.P. Schofield (Ed.), The Royal Society of Chemistry, Cambridge UK
    • D. Lafiandra, S. Masci, R. D'Ovidio, T. Turchetta, B. Margiotta, F. Mac Ritchie: Structural Differences in Allelic Glutenin Subunits of High and Low Mr and Their Relationships with Flour Technological Properties. In: Wheat Structure: Biochemistry and Functionality, J.P. Schofield (Ed.), The Royal Society of Chemistry, Cambridge, UK (1995) pp. 117-127.
    • (1995) Wheat Structure: Biochemistry and Functionality , pp. 117-127
    • Lafiandra, D.1    Masci, S.2    D'Ovidio, R.3    Turchetta, T.4    Margiotta, B.5    Mac Ritchie, F.6
  • 42
    • 0034129841 scopus 로고    scopus 로고
    • Qualitative and quantitative analysis of wheat gluten proteins by liquid chromatography and electrospray mass spectrometry
    • G. Mamone, P. Ferranti, L. Chianese, L. Scafuri, F. Addeo, Qualitative and quantitative analysis of wheat gluten proteins by liquid chromatography and electrospray mass spectrometry, Rapid Commun. Mass Spectrom. 14 (2000) 897-904.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 897-904
    • Mamone, G.1    Ferranti, P.2    Chianese, L.3    Scafuri, L.4    Addeo, F.5
  • 43
    • 34548164835 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization time-of--flight based wheat gliadin protein peaks are useful molecular markers for wheat genetic study
    • J. Chen, P. Lan, A. Tarr, Y.M. Yan, M. Francki, R. Appels, W. Ma, Matrix-assisted laser desorption/ionization time-of--flight based wheat gliadin protein peaks are useful molecular markers for wheat genetic study, Rapid Commun. Mass Spectrom. 21 (2007) 2913-2917.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 2913-2917
    • Chen, J.1    Lan, P.2    Tarr, A.3    Yan, Y.M.4    Francki, M.5    Appels, R.6    Ma, W.7
  • 44
    • 53149140998 scopus 로고    scopus 로고
    • Characterization of wheat gluten proteins by HPLC and MALDI TOF mass spectrometry
    • Y. Qian, K. Preston, O. Krokhin, J. Mellish, W. Ens, Characterization of wheat gluten proteins by HPLC and MALDI TOF mass spectrometry, J. Am. Soc. Mass Spectrom. 19 (2008) 1542-1550.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1542-1550
    • Qian, Y.1    Preston, K.2    Krokhin, O.3    Mellish, J.4    Ens, W.5
  • 45
    • 23044444710 scopus 로고    scopus 로고
    • Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry
    • G. Mamone, F. Addeo, L. Chianese, A. Di Luccia, A. De Martino, A. Nappo et al., Characterization of wheat gliadin proteins by combined two-dimensional gel electrophoresis and tandem mass spectrometry, Proteomics, 5 (2005) 2859-2865.
    • (2005) Proteomics , vol.5 , pp. 2859-2865
    • Mamone, G.1    Addeo, F.2    Chianese, L.3    Di Luccia, A.4    De Martino, A.5    Nappo, A.6
  • 46
    • 33645467513 scopus 로고    scopus 로고
    • A proteomic approach to verify in vivo expression of a novel g-gliadin containing an extra cysteine residue
    • P. Ferrante, S. Masci, R. D'Ovidio, D. Lafiandra, C. Volpi, B. Mattei, A proteomic approach to verify in vivo expression of a novel g-gliadin containing an extra cysteine residue, Proteomics, 6 (2006) 1908-1914.
    • (2006) Proteomics , vol.6 , pp. 1908-1914
    • Ferrante, P.1    Masci, S.2    D'Ovidio, R.3    Lafiandra, D.4    Volpi, C.5    Mattei, B.6
  • 47
    • 79751524014 scopus 로고    scopus 로고
    • Deciphering the complexities of the wheat flour proteome using quantitative two-dimensional electrophoresis, three proteases and tandem mass spectrometry
    • F.M. Dupont, W.H. Vensel, C.K. Tanaka, W.J. Hurkman, S.B. Altenbach, Deciphering the complexities of the wheat flour proteome using quantitative two-dimensional electrophoresis, three proteases and tandem mass spectrometry, Proteome Sci. 11 (2011) 9-10.
    • (2011) Proteome Sci , vol.11 , pp. 9-10
    • Dupont, F.M.1    Vensel, W.H.2    Tanaka, C.K.3    Hurkman, W.J.4    Altenbach, S.B.5
  • 48
    • 72449201048 scopus 로고    scopus 로고
    • Proteomic-based analytical approach for the characterization of glutenin subunits in durum wheat
    • G. Mamone, S. De Caro, A. Di Luccia, F. Addeo, P. Ferranti, Proteomic-based analytical approach for the characterization of glutenin subunits in durum wheat, J. Mass Spectrom. 44 (2009) 1709-1723.
    • (2009) J. Mass Spectrom. , vol.44 , pp. 1709-1723
    • Mamone, G.1    De Caro, S.2    Di Luccia, A.3    Addeo, F.4    Ferranti, P.5
  • 49
    • 0030832023 scopus 로고    scopus 로고
    • Detection of O-glycosidically linked mannose within the structure of a highly purified glutenin subunit isolated from chinese spring wheat
    • K.A. Tilley, Detection of O-glycosidically linked mannose within the structure of a highly purified glutenin subunit isolated from chinese spring wheat, Cereal Chem. 74 (1997) 371-374.
    • (1997) Cereal Chem , vol.74 , pp. 371-374
    • Tilley, K.A.1
  • 51
    • 78649631738 scopus 로고    scopus 로고
    • Isolation and characterization of avenin-like protein type-B from durum wheat
    • S. De Caro, P. Ferranti, F. Addeo, G. Mamone, Isolation and characterization of avenin-like protein type-B from durum wheat, J. Cereal Sci. 52 (2010) 426-431.
    • (2010) J. Cereal Sci. , vol.52 , pp. 426-431
    • De Caro, S.1    Ferranti, P.2    Addeo, F.3    Mamone, G.4
  • 52
    • 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
  • 53
    • 0031808711 scopus 로고    scopus 로고
    • The potential of matrix-assisted laser desorption/ionization mass spectrometry in the quality control of water buffalo mozzarella cheese
    • R. Angeletti, A.M. Gioacchini, R. Seraglia, R. Piro, P. Traldi, The potential of matrix-assisted laser desorption/ionization mass spectrometry in the quality control of water buffalo mozzarella cheese, J. Mass Spectrom. 33 (1998) 525- 531.
    • (1998) J. Mass Spectrom. , vol.33 , pp. 525-531
    • Angeletti, R.1    Gioacchini, A.M.2    Seraglia, R.3    Piro, R.4    Traldi, P.5
  • 54
    • 0034784852 scopus 로고    scopus 로고
    • Identification of adulteration in milk by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • R. Cozzolino, S. Passalacqua, S. Salemi, P. Malvagna, E. Spina, D. Garozzo, Identification of adulteration in milk by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, J. Mass Spectrom. 36 (2002) 1031-1037.
    • (2002) J. Mass Spectrom. , vol.36 , pp. 1031-1037
    • Cozzolino, R.1    Passalacqua, S.2    Salemi, S.3    Malvagna, P.4    Spina, E.5    Garozzo, D.6
  • 56
    • 0020998272 scopus 로고
    • Food processing and storage as a determinant of protein and amino acid availability
    • R.F. Hurrell, P.A. Finot, Food processing and storage as a determinant of protein and amino acid availability, Experientia (Suppl.), 44 (1983) 135-156.
    • (1983) Experientia (Suppl. ) , vol.44 , pp. 135-156
    • Hurrell, R.F.1    Finot, P.A.2
  • 58
    • 68949145941 scopus 로고    scopus 로고
    • Emerging analytical methods to determine gluten markers in processed foods -Method development in support of standard setting
    • D. Weber, C. Cleroux, S.B. Godenfroy, Emerging analytical methods to determine gluten markers in processed foods - Method development in support of standard setting, Anal. Biochem. Chem. 395 (2009) 111-117.
    • (2009) Anal. Biochem. Chem. , vol.395 , pp. 111-117
    • Weber, D.1    Cleroux, C.2    Godenfroy, S.B.3
  • 60
    • 0042856251 scopus 로고    scopus 로고
    • New strategy for the determination of gliadins in maize-or rice-based foods matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: Fractionation of gliadins from maize or rice prolamins by acidic treatment
    • A. Hernando, I. Valdes, E. Mendez, New strategy for the determination of gliadins in maize- or rice-based foods matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: Fractionation of gliadins from maize or rice prolamins by acidic treatment, J. Mass Spectrom. 38 (2003) 862-871.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 862-871
    • Hernando, A.1    Valdes, I.2    Mendez, E.3
  • 61
    • 0037228383 scopus 로고    scopus 로고
    • Isolation and identification of indigestible pyroglutamyl peptides in an enzymatic hydrolysate of wheat gluten prepared on an industrial scale
    • N. Higaki-Sato, K. Sato, Y. Esumi, T. Okumura, H. Yoshikawa, C. Tanaka-Kuwajima et al., Isolation and identification of indigestible pyroglutamyl peptides in an enzymatic hydrolysate of wheat gluten prepared on an industrial scale, J. Agric. Food Chem. 51 (2003) 8-13.
    • (2003) J. Agric. Food Chem. , vol.51 , pp. 8-13
    • Higaki-Sato, N.1    Sato, K.2    Esumi, Y.3    Okumura, T.4    Yoshikawa, H.5    Tanaka-Kuwajima, C.6
  • 63
    • 67349112777 scopus 로고    scopus 로고
    • Quantitation of lysinoalanine in dairy products by liquid chromatography-mass spectrometry with selective ion monitoring
    • M.G. Calabrese, G. Mamone, S. Caira, P. Ferranti, F. Addeo, Quantitation of lysinoalanine in dairy products by liquid chromatography-mass spectrometry with selective ion monitoring, Food Chem. 116 (2009) 799-805.
    • (2009) Food Chem , vol.116 , pp. 799-805
    • Calabrese, M.G.1    Mamone, G.2    Caira, S.3    Ferranti, P.4    Addeo, F.5
  • 64
    • 0030130380 scopus 로고    scopus 로고
    • Prevalence, biological activity and genetic manipulation of lectins in foods
    • W.J. Peumans, E.J.M. Van Damme, Prevalence, biological activity and genetic manipulation of lectins in foods, Trends Food Sci. Technol. 7 (1996) 132-138.
    • (1996) Trends Food Sci. Technol. , vol.7 , pp. 132-138
    • Peumans, W.J.1    Van Damme, E.J.M.2
  • 65
    • 0033577557 scopus 로고    scopus 로고
    • Do dietary lectins cause disease?
    • D.L. Freed, Do dietary lectins cause disease?, Br. Med. J. 318 (1999) 1023-1025.
    • (1999) Br. Med. J. , vol.318 , pp. 1023-1025
    • Freed, D.L.1
  • 67
    • 77649154861 scopus 로고    scopus 로고
    • Changes in the proteome of Salmonella enterica serovar Thompson as stress adaptation to sublethal concentrations of thymol
    • R. Di Pasqua, G. Mamone, P. Ferranti, D. Ercolini, G. Mauriello, Changes in the proteome of Salmonella enterica serovar Thompson as stress adaptation to sublethal concentrations of thymol, Proteomics, 10 (2010) 1040-1049.
    • (2010) Proteomics , vol.10 , pp. 1040-1049
    • Di Pasqua, R.1    Mamone, G.2    Ferranti, P.3    Ercolini, D.4    Mauriello, G.5
  • 68
    • 48249147379 scopus 로고    scopus 로고
    • Proteomic analysis of exoproteins expressed by enterotoxigenic Staphylococcus aureus strains
    • G. Pocsfàlvi, G. Cacace, M. Cuccurullo, G. Serluca, A. Sorrentino, G. Schlosser et al., Proteomic analysis of exoproteins expressed by enterotoxigenic Staphylococcus aureus strains, Proteomics, 8 (2008) 2462-2476.
    • (2008) Proteomics , vol.8 , pp. 2462-2476
    • Pocsfàlvi, G.1    Cacace, G.2    Cuccurullo, M.3    Serluca, G.4    Sorrentino, A.5    Schlosser, G.6
  • 69
    • 80052528088 scopus 로고    scopus 로고
    • G. Pocsfalvi, G. Schlosser, Detection of bacterial protein toxins by solid phase magnetic immunocapture and mass spectrometry, Methods Mol. Biol. 739 (2011) 3-12.
    • (2011) Methods Mol. Biol. , vol.739 , pp. 3-12
    • Pocsfalvi, G.1    Schlosser, G.2
  • 70
    • 0028487702 scopus 로고
    • Characterization of the oligopeptides of Parmigiano-Reggiano cheese soluble in 120 g trichloroacetic acid/l
    • F. Addeo, L. Chianese, R. Sacchi, S. Spagna-Musso, P. Ferranti, A. Malorni, Characterization of the oligopeptides of Parmigiano-Reggiano cheese soluble in 120 g trichloroacetic acid/l, J. Dairy Res. 61 (1994) 365-374.
    • (1994) J. Dairy Res. , vol.61 , pp. 365-374
    • Addeo, F.1    Chianese, L.2    Sacchi, R.3    Spagna-Musso, S.4    Ferranti, P.5    Malorni, A.6
  • 71
    • 84974067240 scopus 로고
    • Characterization of the 12% trichloroacetic acid-insoluble oligopeptides of Parmigiano-Reggiano cheese
    • F. Addeo, L. Chianese, A. Salzano, R. Sacchi, U. Cappuccio, P. Ferranti et al., Characterization of the 12% trichloroacetic acid-insoluble oligopeptides of Parmigiano-Reggiano cheese, J. Dairy Res. 59 (1992) 401-411.
    • (1992) J. Dairy Res. , vol.59 , pp. 401-411
    • Addeo, F.1    Chianese, L.2    Salzano, A.3    Sacchi, R.4    Cappuccio, U.5    Ferranti, P.6
  • 72
    • 0034832894 scopus 로고    scopus 로고
    • Peptides identified during Emmental cheese ripening: Origin and proteolytic systems involved
    • V. Gagnaire, D. Mollé, M. Herrouin, J. Léonil, Peptides identified during Emmental cheese ripening: Origin and proteolytic systems involved, J. Agric. Food Chem. 49 (2001) 4402-4413.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 4402-4413
    • Gagnaire, V.1    Mollé, D.2    Herrouin, M.3    Léonil, J.4
  • 73
    • 0030210080 scopus 로고    scopus 로고
    • Application of a mass spectrometry sequencing technique for identifying peptides present in Cheddar cheese
    • A.M. Gouldsworthy, J. Leaver, J.M. Banks, Application of a mass spectrometry sequencing technique for identifying peptides present in Cheddar cheese, Int. Dairy J. 6 (1996) 781-790.
    • (1996) Int. Dairy J. , vol.6 , pp. 781-790
    • Gouldsworthy, A.M.1    Leaver, J.2    Banks, J.M.3
  • 74
    • 33751235300 scopus 로고    scopus 로고
    • Relationship between the enzymatic composition of lamb rennet paste and proteolytic, lipolytic pattern and texture of PDO Fiore Sardo ovine cheese
    • A. Pirisi, G. Pinna, M. Addis, G. Piredda, R. Mauriello, S. De Pascale, Relationship between the enzymatic composition of lamb rennet paste and proteolytic, lipolytic pattern and texture of PDO Fiore Sardo ovine cheese, Int. Dairy J. 17 (2007) 143-156.
    • (2007) Int. Dairy J. , vol.17 , pp. 143-156
    • Pirisi, A.1    Pinna, G.2    Addis, M.3    Piredda, G.4    Mauriello, R.5    De Pascale, S.6
  • 76
    • 1642301670 scopus 로고    scopus 로고
    • Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides
    • P. Ferranti, M.V. Traisci, G. Picariello, A. Nasi, V. Boschi, M. Siervo et al., Casein proteolysis in human milk: Tracing the pattern of casein breakdown and the formation of potential bioactive peptides, J. Dairy Res. 71 (2004) 74-87.
    • (2004) J. Dairy Res. , vol.71 , pp. 74-87
    • Ferranti, P.1    Traisci, M.V.2    Picariello, G.3    Nasi, A.4    Boschi, V.5    Siervo, M.6
  • 78
    • 31644441857 scopus 로고    scopus 로고
    • Enzymatic debittering of food protein hydrolysates
    • R.J. FitzGerald, G. O'Cuinn, Enzymatic debittering of food protein hydrolysates, Biotechnol. Adv. 24 (2006) 234-237.
    • (2006) Biotechnol. Adv. , vol.24 , pp. 234-237
    • FitzGerald, R.J.1    O'Cuinn, G.2
  • 79
    • 43049168777 scopus 로고    scopus 로고
    • Peptidomic approach based on combined capillary isoelectric focusing and mass spectrometry for the characterization of the plasmin primary products from bovine and water buffalo b-casein
    • A. Somma, P. Ferranti, F. Addeo, R. Mauriello, L. Chianese, Peptidomic approach based on combined capillary isoelectric focusing and mass spectrometry for the characterization of the plasmin primary products from bovine and water buffalo b-casein, J. Chromatogr. A, 1192 (2008) 294-300.
    • (2008) J. Chromatogr. A , vol.1192 , pp. 294-300
    • Somma, A.1    Ferranti, P.2    Addeo, F.3    Mauriello, R.4    Chianese, L.5
  • 80
    • 65249094756 scopus 로고    scopus 로고
    • Occurrence of b-casein fragments in cold-stored and curdled river buffalo (Bubalus bubalis L.) milk
    • A. Di Luccia, G. Picariello, A. Trani, G. Alviti, P. Loizzo, M. Faccia, F. Addeo, Occurrence of b-casein fragments in cold-stored and curdled river buffalo (Bubalus bubalis L.) milk, J. Dairy Sci. 92 (2004) 1319-1329.
    • (2004) J. Dairy Sci. , vol.92 , pp. 1319-1329
    • Di Luccia, A.1    Picariello, G.2    Trani, A.3    Alviti, G.4    Loizzo, P.5    Faccia, M.6    Addeo, F.7
  • 81
    • 33746522377 scopus 로고    scopus 로고
    • Peptides in rainbow trout (Oncorhynchus mykiss) muscle subjected to ice storage and cooking
    • C. Bauchart, C. Chambon, P.P. Mirand, I. Savary-Auzeloux, D. Remond, M. Morzel, Peptides in rainbow trout (Oncorhynchus mykiss) muscle subjected to ice storage and cooking, Food Chem. 100 (2007) 1566-1572.
    • (2007) Food Chem , vol.100 , pp. 1566-1572
    • Bauchart, C.1    Chambon, C.2    Mirand, P.P.3    Savary-Auzeloux, I.4    Remond, D.5    Morzel, M.6
  • 82
  • 83
    • 70349898584 scopus 로고    scopus 로고
    • Oligopeptides arising from the degradation of creatine kinase in Spanish dry-cured ham
    • L. Mora, M.A. Sentandreu, P.D. Fraser, F. Toldrá, P.M. Bramley, Oligopeptides arising from the degradation of creatine kinase in Spanish dry-cured ham, J. Agric. Food Chem. 57 (2009) 8982-8988.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 8982-8988
    • Mora, L.1    Sentandreu, M.A.2    Fraser, P.D.3    Toldrá, F.4    Bramley, P.M.5
  • 84
    • 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
  • 85
    • 11444259281 scopus 로고    scopus 로고
    • Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams
    • A.D. Luccia, G. Picariello, G. Cacace, A. Scaloni, M. Faccia, V. Liuzzi et al., Proteomic analysis of water soluble and myofibrillar protein changes occurring in dry-cured hams, Meat Sci. 69 (2005) 479-491.
    • (2005) Meat Sci , vol.69 , pp. 479-491
    • Luccia, A.D.1    Picariello, G.2    Cacace, G.3    Scaloni, A.4    Faccia, M.5    Liuzzi, V.6
  • 87
    • 33644914704 scopus 로고    scopus 로고
    • Proteomic study of muscle sarcoplasmic proteins using AUT-PAGE/SDS-PAGE as two-dimensional gel electrophoresis
    • G. Picariello, A. De Martino, G. Mamone, P. Ferranti, F. Addeo, M. Faccia et al., Proteomic study of muscle sarcoplasmic proteins using AUT-PAGE/SDS-PAGE as two-dimensional gel electrophoresis, J. Chromatogr. B, 833 (2006) 101-108.
    • (2006) J. Chromatogr. B , vol.833 , pp. 101-108
    • Picariello, G.1    De Martino, A.2    Mamone, G.3    Ferranti, P.4    Addeo, F.5    Faccia, M.6
  • 88
    • 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
  • 89
    • 85056684142 scopus 로고    scopus 로고
    • Functional Properties of Bioactive Peptides Derived from Meat Proteins
    • L.M.L. Nollet, F. Toldrà (Eds.), CRC Press, Boca Raton, FL USA
    • K. Arihara: Functional Properties of Bioactive Peptides Derived from Meat Proteins. In: Advanced Technologies for Meat Processing, L.M.L. Nollet, F. Toldrà (Eds.), CRC Press, Boca Raton, FL, USA (2006) pp. 245-273.
    • (2006) Advanced Technologies for Meat Processing , pp. 245-273
    • Arihara, K.1
  • 90
    • 68849084346 scopus 로고    scopus 로고
    • Degradation of milk-based bioactive peptides by yogurt fermentation bacteria
    • M. Paul, G.A. Somkuti, Degradation of milk-based bioactive peptides by yogurt fermentation bacteria, Lett. Appl. Microbiol. 49 (2009) 345-350.
    • (2009) Lett. Appl. Microbiol. , vol.49 , pp. 345-350
    • Paul, M.1    Somkuti, G.A.2
  • 91
    • 51049122580 scopus 로고    scopus 로고
    • Bioactive peptides
    • F. Shahidi, Y. Zhong, Bioactive peptides, J. AOAC, 91 (2008) 914-931.
    • (2008) J. AOAC , vol.91 , pp. 914-931
    • Shahidi, F.1    Zhong, Y.2
  • 92
    • 78649334104 scopus 로고    scopus 로고
    • Identification of bioactive peptides in hypoallergenic infant milk formulas by capillary electrophoresis--mass spectrometry
    • S. Català-Clariana, F. Benavente, E. Giménez, J. Barbosa, V. Sanz-Nebot, Identification of bioactive peptides in hypoallergenic infant milk formulas by capillary electrophoresis--mass spectrometry, Anal. Chim. Acta, 68 (2010) 119-125.
    • (2010) Anal. Chim. Acta , vol.68 , pp. 119-125
    • Català-Clariana, S.1    Benavente, F.2    Giménez, E.3    Barbosa, J.4    Sanz-Nebot, V.5
  • 93
    • 74049126072 scopus 로고    scopus 로고
    • Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications
    • G. Picariello, P. Ferranti, O. Fierro, G. Mamone, S. Caira, A. Di Luccia et al., Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications, J. Chromatogr. B, 878 (2010) 295-308.
    • (2010) J. Chromatogr. B , vol.878 , pp. 295-308
    • Picariello, G.1    Ferranti, P.2    Fierro, O.3    Mamone, G.4    Caira, S.5    Di Luccia, A.6
  • 94
    • 19944369777 scopus 로고    scopus 로고
    • Identification of casein phosphopeptides released after simulated digestion of milk-based infant formulas
    • E. Miquel, J.A. Gómez, A. Alegría, R. Barberá, R. Farré, I. Recio, Identification of casein phosphopeptides released after simulated digestion of milk-based infant formulas, J. Agric. Food Chem. 53 (2005) 3426-3433.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 3426-3433
    • Miquel, E.1    Gómez, J.A.2    Alegría, A.3    Barberá, R.4    Farré, R.5    Recio, I.6
  • 95
    • 33646529864 scopus 로고    scopus 로고
    • Casein phosphopeptides released by simulated gastrointestinal digestion of infant formulas and their potential role in mineral binding
    • E. Miquel, A. Alegría, R. Barberá, R. Farré, Casein phosphopeptides released by simulated gastrointestinal digestion of infant formulas and their potential role in mineral binding, Int. Dairy J. 16 (2006) 992-1000.
    • (2006) Int. Dairy J. , vol.16 , pp. 992-1000
    • Miquel, E.1    Alegría, A.2    Barberá, R.3    Farré, R.4
  • 96
    • 34547692864 scopus 로고    scopus 로고
    • Identification of a peptide from a-gliadin resistant to digestive enzymes: Implications for celiac disease
    • G. Mamone, P. Ferranti, M. Rossi, P. Roepstorff, O. Fierro, A. Malorni, F. Addeo, Identification of a peptide from a-gliadin resistant to digestive enzymes: Implications for celiac disease, J. Chromatogr. B, 855 (2007) 236-241.
    • (2007) J. Chromatogr. B , vol.855 , pp. 236-241
    • Mamone, G.1    Ferranti, P.2    Rossi, M.3    Roepstorff, P.4    Fierro, O.5    Malorni, A.6    Addeo, F.7
  • 97
    • 80053304692 scopus 로고    scopus 로고
    • The frontiers of mass spectrometry-based techniques in food allergenomics
    • G. Picariello, G. Mamone, F. Addeo, P. Ferranti, The frontiers of mass spectrometry-based techniques in food allergenomics, J. Chromatogr. A, 1218 (2011) 7386-7398.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 7386-7398
    • Picariello, G.1    Mamone, G.2    Addeo, F.3    Ferranti, P.4
  • 100
    • 77957020789 scopus 로고    scopus 로고
    • Proteomic and peptidomic characterisation of beer: Immunological and technological implications
    • G. Picariello, F. Bonomi, S. Iametti, P. Rasmussen, C. Pepe, S. Lilla, P. Ferranti, Proteomic and peptidomic characterisation of beer: Immunological and technological implications, Food Chem. 124 (2011) 1718-1726.
    • (2011) Food Chem , vol.124 , pp. 1718-1726
    • Picariello, G.1    Bonomi, F.2    Iametti, S.3    Rasmussen, P.4    Pepe, C.5    Lilla, S.6    Ferranti, P.7
  • 101
    • 83455209014 scopus 로고    scopus 로고
    • What is in a beer? Proteomic characterization and relative quantification of hordein (gluten) in beer
    • M.L. Colgrave, H. Goswami, C.A. Howitt, G.J. Tanner, What is in a beer? Proteomic characterization and relative quantification of hordein (gluten) in beer, J. Proteome Res. 11 (2012) 386-396.
    • (2012) J. Proteome Res. , vol.11 , pp. 386-396
    • Colgrave, M.L.1    Goswami, H.2    Howitt, C.A.3    Tanner, G.J.4
  • 104
    • 19444380734 scopus 로고    scopus 로고
    • Sphingolipidomics: High-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry
    • A.H. Merrill Jr., M.C. Sullards, J.C. Allegood, S. Kelly, E. Wang, Sphingolipidomics: High-throughput, structure-specific, and quantitative analysis of sphingolipids by liquid chromatography tandem mass spectrometry, Methods, 36 (2005) 207-224.
    • (2005) Methods , vol.36 , pp. 207-224
    • Merrill Jr., A.H.1    Sullards, M.C.2    Allegood, J.C.3    Kelly, S.4    Wang, E.5
  • 105
    • 80054079107 scopus 로고    scopus 로고
    • Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics
    • A.H. Merrill Jr., Sphingolipid and glycosphingolipid metabolic pathways in the era of sphingolipidomics, Chem. Rev. 111 (2011) 6387-6422.
    • (2011) Chem. Rev. , vol.111 , pp. 6387-6422
    • Merrill Jr., A.H.1
  • 106
    • 67849111947 scopus 로고    scopus 로고
    • Sphingolipidomics: Methods for the comprehensive analysis of sphingolipids
    • C.A. Haynes, J.C. Allegood, H. Park, M.C. Sullards, Sphingolipidomics: Methods for the comprehensive analysis of sphingolipids, J. Chromatogr. B, 877 (2009) 2696-2708.
    • (2009) J. Chromatogr. B , vol.877 , pp. 2696-2708
    • Haynes, C.A.1    Allegood, J.C.2    Park, H.3    Sullards, M.C.4
  • 107
    • 64549148453 scopus 로고    scopus 로고
    • The importance of steroidomics in the study of neurodegenerative disease and ageing
    • W.J. Griffiths, Y. Wang, The importance of steroidomics in the study of neurodegenerative disease and ageing, Comb. Chem. High Throughput Screen. 12 (2009) 212-228.
    • (2009) Comb. Chem. High Throughput Screen. , vol.12 , pp. 212-228
    • Griffiths, W.J.1    Wang, Y.2
  • 108
    • 58949089940 scopus 로고    scopus 로고
    • Lipidomic methodologies applicable to the study of endocannabinoids and related compounds: Endocannabinoidomics
    • T. Bisogno, F. Piscitelli, V. Di Marzo, Lipidomic methodologies applicable to the study of endocannabinoids and related compounds: Endocannabinoidomics, Eur. J. Lipid Sci. Technol. 111 (2009) 53-63.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 53-63
    • Bisogno, T.1    Piscitelli, F.2    Di Marzo, V.3
  • 109
    • 0035041484 scopus 로고    scopus 로고
    • Atmospheric pressure chemical ionization mass spectrometry for analysis of lipids
    • W.C. Byrdwell, Atmospheric pressure chemical ionization mass spectrometry for analysis of lipids, Lipids, 36 (2001) 327-346.
    • (2001) Lipids , vol.36 , pp. 327-346
    • Byrdwell, W.C.1
  • 110
    • 0141974064 scopus 로고    scopus 로고
    • Electrospray mass spectrometry of phospholipids
    • M. Pulfer, R.C. Murphy, Electrospray mass spectrometry of phospholipids, Mass Spectrom. Rev. 22 (2003) 332-364.
    • (2003) Mass Spectrom. Rev. , vol.22 , pp. 332-364
    • Pulfer, M.1    Murphy, R.C.2
  • 111
    • 0026213291 scopus 로고
    • Electrospray and tandem mass spectrometric characterization of acylglycerol mixtures that are dissolved in nonpolar solvents
    • K.L. Duffin, J.D. Henion, J.J. Shieh, Electrospray and tandem mass spectrometric characterization of acylglycerol mixtures that are dissolved in nonpolar solvents, Anal. Chem. 63 (1991) 1781-1788.
    • (1991) Anal. Chem. , vol.63 , pp. 1781-1788
    • Duffin, K.L.1    Henion, J.D.2    Shieh, J.J.3
  • 112
    • 78049355456 scopus 로고    scopus 로고
    • Advances in mass spectrometry for lipidomics
    • S.J. Blanksby, T.W. Mitchell, Advances in mass spectrometry for lipidomics, Annu. Rev. Anal. Chem. 3 (2010) 433-465.
    • (2010) Annu. Rev. Anal. Chem. , vol.3 , pp. 433-465
    • Blanksby, S.J.1    Mitchell, T.W.2
  • 113
    • 79958808983 scopus 로고    scopus 로고
    • Mass spectrometric analysis of long-chain lipids
    • R.C. Murphy, P.H. Axelesen, Mass spectrometric analysis of long-chain lipids, Mass Spectrom. Rev. 30 (2011) 579-599.
    • (2011) Mass Spectrom. Rev. , vol.30 , pp. 579-599
    • Murphy, R.C.1    Axelesen, P.H.2
  • 115
    • 0742271072 scopus 로고    scopus 로고
    • Quantitative analysis of triacylglycerol regioisomers in fats and oils using reversed-phase high-performance liquid chromatography and atmospheric pressure chemical ionization mass spectrometry
    • L. Fauconnot, J. Hau, J.M. Aeschlimann, L.B. Fay, F. Dionisi, Quantitative analysis of triacylglycerol regioisomers in fats and oils using reversed-phase high-performance liquid chromatography and atmospheric pressure chemical ionization mass spectrometry, Rapid Commun. Mass Spectrom. 18 (2004) 218-224.
    • (2004) Rapid Commun. Mass Spectrom. , vol.18 , pp. 218-224
    • Fauconnot, L.1    Hau, J.2    Aeschlimann, J.M.3    Fay, L.B.4    Dionisi, F.5
  • 116
    • 4143107026 scopus 로고    scopus 로고
    • Characterization of vegetable oils: Detailed compositional fingerprints derived from electrospray ionization fourier transform ion cyclotron resonance mass spectrometry
    • Z. Wu, R.P. Rodgers, A.G. Marshall, Characterization of vegetable oils: Detailed compositional fingerprints derived from electrospray ionization fourier transform ion cyclotron resonance mass spectrometry, J. Agric. Food Chem. 52 (2004) 5322-5328.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 5322-5328
    • Wu, Z.1    Rodgers, R.P.2    Marshall, A.G.3
  • 117
    • 27944473997 scopus 로고    scopus 로고
    • Characterization of vegetable oils by electrospray ionization mass spectrometry fingerprinting: classification, quality, adulteration, and aging
    • R.R. Catharino, R. Haddad, L.G. Cabrini, I.B. Cunha, A.C. Sawaya, M.N. Eberlin, Characterization of vegetable oils by electrospray ionization mass spectrometry fingerprinting: classification, quality, adulteration, and aging, Anal. Chem. 77 (2005) 7429-7433.
    • (2005) Anal. Chem. , vol.77 , pp. 7429-7433
    • Catharino, R.R.1    Haddad, R.2    Cabrini, L.G.3    Cunha, I.B.4    Sawaya, A.C.5    Eberlin, M.N.6
  • 118
    • 77949339572 scopus 로고    scopus 로고
    • Optimization and application of methods of triacylglycerol evaluation for characterization of olive oil adulteration by soybean oil with HPLC-APCI-MS-MS
    • M. Fasciotti, A.D. Pereira Netto, Optimization and application of methods of triacylglycerol evaluation for characterization of olive oil adulteration by soybean oil with HPLC-APCI-MS-MS, Talanta, 81 (2010) 1116-1125.
    • (2010) Talanta , vol.81 , pp. 1116-1125
    • Fasciotti, M.1    Pereira Netto, A.D.2
  • 119
    • 34547235048 scopus 로고    scopus 로고
    • Quantification of triacylglycerol regioisomers in oils and fat using different mass spectrometric and liquid chromatographic methods
    • H. Leskinen, J.P. Suomela, H.Kallio, Quantification of triacylglycerol regioisomers in oils and fat using different mass spectrometric and liquid chromatographic methods, Rapid Commun. Mass Spectrom. 21 (2007) 2361-2373.
    • (2007) Rapid Commun. Mass Spectrom. , vol.21 , pp. 2361-2373
    • Leskinen, H.1    Suomela, J.P.2    Kallio, H.3
  • 120
    • 73249145464 scopus 로고    scopus 로고
    • Quantification of triacylglycerol regioisomers by ultra-high-performance liquid chromatography and ammonia negative ion atmospheric pressure chemical ionization tandem mass spectrometry
    • H.M. Leskinen, J.P. Suomela, H.P. Kallio, Quantification of triacylglycerol regioisomers by ultra-high-performance liquid chromatography and ammonia negative ion atmospheric pressure chemical ionization tandem mass spectrometry, Rapid Commun. Mass Spectrom. 24 (2010) 1-5.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 1-5
    • Leskinen, H.M.1    Suomela, J.P.2    Kallio, H.P.3
  • 121
    • 17344381218 scopus 로고    scopus 로고
    • Characterisation of castor oil by on-line and off-line non-aqueous reverse-phase high-performance liquid chromatography-mass spectrometry (APCI and UV/MALDI)
    • G. Stübiger, E. Pittenauer, G. Allmaier, Characterisation of castor oil by on-line and off-line non-aqueous reverse-phase high-performance liquid chromatography-mass spectrometry (APCI and UV/MALDI), Phytochem. Anal. 14 (2003) 337-346.
    • (2003) Phytochem. Anal. , vol.14 , pp. 337-346
    • Stübiger, G.1    Pittenauer, E.2    Allmaier, G.3
  • 122
    • 71949101026 scopus 로고    scopus 로고
    • Contribution of two approaches using electrospray ionization with multi-stage mass spectrometry for the characterization of linseed oil
    • C. Loutelier-Bourhis, O. Zovi, L. Lecamp, C. Bunel, C.M. Lange, Contribution of two approaches using electrospray ionization with multi-stage mass spectrometry for the characterization of linseed oil, Rapid Commun. Mass Spectrom. 23 (2009) 3743-3752.
    • (2009) Rapid Commun. Mass Spectrom. , vol.23 , pp. 3743-3752
    • Loutelier-Bourhis, C.1    Zovi, O.2    Lecamp, L.3    Bunel, C.4    Lange, C.M.5
  • 123
    • 77956189023 scopus 로고    scopus 로고
    • Elucidation of triacylglycerols in cod liver oil by liquid chromatography electrospray tandem ion-trap mass spectrometry
    • Y. Zeng, P. Araujo, Z.Y. Du, T.T. Nguyen, L. Frøyland, B. Grung, Elucidation of triacylglycerols in cod liver oil by liquid chromatography electrospray tandem ion-trap mass spectrometry, Talanta, 82 (2010) 1261-1270.
    • (2010) Talanta , vol.82 , pp. 1261-1270
    • Zeng, Y.1    Araujo, P.2    Du, Z.Y.3    Nguyen, T.T.4    Frøyland, L.5    Grung, B.6
  • 124
    • 79952605397 scopus 로고    scopus 로고
    • Evaluation of different fingerprinting strategies for differentiating marine oils by liquid chromatography ion-trap mass spectrometry and chemometrics
    • Y.X. Zeng, P. Araujo, B. Grung, L. Zhang, Evaluation of different fingerprinting strategies for differentiating marine oils by liquid chromatography ion-trap mass spectrometry and chemometrics, Analyst, 136 (2011) 1507-1514.
    • (2011) Analyst , vol.136 , pp. 1507-1514
    • Zeng, Y.X.1    Araujo, P.2    Grung, B.3    Zhang, L.4
  • 125
    • 33845938874 scopus 로고    scopus 로고
    • Analysis of sphingolipids in potatoes (Solanum tuberosum L.) and sweet potatoes (Ipomoea batatas (L.) Lam.) by reversed phase high-performance liquid chromatography electrospray ionization tandem mass spectrometry (HPLC-ESI-MS/MS)
    • N. Bartke, A. Fischbeck, H.U. Humpf, Analysis of sphingolipids in potatoes (Solanum tuberosum L.) and sweet potatoes (Ipomoea batatas (L.) Lam.) by reversed phase high-performance liquid chromatography electrospray ionization tandem mass spectrometry (HPLC-ESI-MS/MS), Mol. Nutr. Food Res. 50 (2006) 1201-1211.
    • (2006) Mol. Nutr. Food Res. , vol.50 , pp. 1201-1211
    • Bartke, N.1    Fischbeck, A.2    Humpf, H.U.3
  • 126
    • 70350290230 scopus 로고    scopus 로고
    • Analysis of sphingomyelin in meat based on hydrophilic interaction liquid chromatography coupled to electrospray ionization--tandem mass spectrometry (HILIC-HPLC-ESI-MS/MS)
    • A. Fischbeck, M. Krüger, N. Blaas, H.U. Humpf, Analysis of sphingomyelin in meat based on hydrophilic interaction liquid chromatography coupled to electrospray ionization--tandem mass spectrometry (HILIC-HPLC-ESI-MS/MS), J. Agric. Food Chem. 57 (2009) 9469-9474.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 9469-9474
    • Fischbeck, A.1    Krüger, M.2    Blaas, N.3    Humpf, H.U.4
  • 127
    • 79957993445 scopus 로고    scopus 로고
    • Structural profiling and quantification of sphingomyelin in human breast milk by HPLC-MS/MS
    • N. Blaas, C. Schüürmann, N. Bartke, B. Stahl, H.U. Humpf, Structural profiling and quantification of sphingomyelin in human breast milk by HPLC-MS/MS, J. Agric. Food Chem. 59 (2011) 6018-6024.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 6018-6024
    • Blaas, N.1    Schüürmann, C.2    Bartke, N.3    Stahl, B.4    Humpf, H.U.5
  • 128
    • 0033784938 scopus 로고    scopus 로고
    • Analysis of sphingomyelin, glucosylceramide, ceramide, sphingosine, and sphingosine 1-phosphate by tandem mass spectrometry
    • M.C. Sullards, Analysis of sphingomyelin, glucosylceramide, ceramide, sphingosine, and sphingosine 1-phosphate by tandem mass spectrometry, Methods Enzymol. 312 (2000) 32- 45.
    • (2000) Methods Enzymol , vol.312 , pp. 32-45
    • Sullards, M.C.1
  • 129
    • 58949086124 scopus 로고    scopus 로고
    • Application of MALDI-TOF mass spectrometry in lipidomics
    • B. Fuchs, J. Schiller, Application of MALDI-TOF mass spectrometry in lipidomics, Eur. J. Lipid Sci. Technol. 111 (2009) 83-98.
    • (2009) Eur. J. Lipid Sci. Technol. , vol.111 , pp. 83-98
    • Fuchs, B.1    Schiller, J.2
  • 130
    • 77954219046 scopus 로고    scopus 로고
    • Significant sensitivity improvements by matrix optimization: A MALDI-TOF mass spectrometric study of lipids from hen egg yolk
    • K. Teuber, J. Schiller, B. Fuchs, M. Karas, T.W. Jaskolla, Significant sensitivity improvements by matrix optimization: A MALDI-TOF mass spectrometric study of lipids from hen egg yolk, Chem. Phys. Lipids, 163 (2010) 552-560.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 552-560
    • Teuber, K.1    Schiller, J.2    Fuchs, B.3    Karas, M.4    Jaskolla, T.W.5
  • 131
    • 34249878763 scopus 로고    scopus 로고
    • One-step characterization of triacylglycerols from animal fat by MALDI-TOF MS
    • G. Picariello, R. Sacchi, F. Addeo, One-step characterization of triacylglycerols from animal fat by MALDI-TOF MS, Eur. J. Lipid Sci. Technol. 109 (2007) 511-524.
    • (2007) Eur. J. Lipid Sci. Technol. , vol.109 , pp. 511-524
    • Picariello, G.1    Sacchi, R.2    Addeo, F.3
  • 132
    • 33645234035 scopus 로고    scopus 로고
    • Rapid characterization of edible oils by direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis using triacylglycerols
    • J.O. Lay Jr., R. Liyanage, B. Durham, J. Brooks, Rapid characterization of edible oils by direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometry analysis using triacylglycerols, Rapid Commun. Mass Spectrom. 20 (2006) 952-958.
    • (2006) Rapid Commun. Mass Spectrom. , vol.20 , pp. 952-958
    • Lay Jr., J.O.1    Liyanage, R.2    Durham, B.3    Brooks, J.4
  • 133
    • 64549160245 scopus 로고    scopus 로고
    • MALDI-TOF/MS fingerprinting of triacylglycerols (TAGs) in olive oils produced in the Israeli Negev desert
    • B.P. Chapagain, Z. Wiesman, MALDI-TOF/MS fingerprinting of triacylglycerols (TAGs) in olive oils produced in the Israeli Negev desert, J. Agric. Food Chem. 57 (2009) 1135- 1142.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 1135-1142
    • Chapagain, B.P.1    Wiesman, Z.2
  • 134
    • 67649322213 scopus 로고    scopus 로고
    • MALDI--TOF mass spectrometry profiling of polar and nonpolar fractions in heated vegetable oils
    • G. Picariello, A. Paduano, R. Sacchi, F. Addeo, MALDI--TOF mass spectrometry profiling of polar and nonpolar fractions in heated vegetable oils, J. Agric. Food Chem. 57 (2009) 5391-400.
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 5391-5400
    • Picariello, G.1    Paduano, A.2    Sacchi, R.3    Addeo, F.4
  • 135
    • 65549128165 scopus 로고    scopus 로고
    • The renaissance of high-energy CID for structural elucidation of complex lipids: MALDI--TOF/RTOF-MS of alkali cationized triacylglycerols
    • E. Pittenauer, G. Allmaier, The renaissance of high-energy CID for structural elucidation of complex lipids: MALDI--TOF/RTOF-MS of alkali cationized triacylglycerols, J. Am. Soc. Mass Spectrom. 20 (2009) 1037-1047.
    • (2009) J. Am. Soc. Mass Spectrom. , vol.20 , pp. 1037-1047
    • Pittenauer, E.1    Allmaier, G.2
  • 136
    • 1942445171 scopus 로고    scopus 로고
    • Electrospray ionization MS of high M.W. TAG oligomers
    • W.C. Byrdwell, W.E. Neff, Electrospray ionization MS of high M.W. TAG oligomers, J. Am. Oil Chem. Soc. 81 (2004) 13-26.
    • (2004) J. Am. Oil Chem. Soc. , vol.81 , pp. 13-26
    • Byrdwell, W.C.1    Neff, W.E.2
  • 137
    • 0036007549 scopus 로고    scopus 로고
    • Dual parallel electrospray ionization and atmospheric pressure chemical ionization mass spectrometry (MS), MS/MS and MS/MS/MS for the analysis of triacylglycerols and triacylglycerol oxidation products
    • W.C. Byrdwell, W.E. Neff, Dual parallel electrospray ionization and atmospheric pressure chemical ionization mass spectrometry (MS), MS/MS and MS/MS/MS for the analysis of triacylglycerols and triacylglycerol oxidation products, Rapid Commun. Mass Spectrom. 16 (2002) 300-319.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 300-319
    • Byrdwell, W.C.1    Neff, W.E.2
  • 138
    • 0141920569 scopus 로고    scopus 로고
    • Comparative study of matrix-assisted laser desorption/ ionization and gas chromatography for quantitative determination of cocoa butter and cocoa butter equivalent triacylglycerol composition
    • F. Guyon, Ch. Absalon, A. Eloy, M.H. Salagoity, M. Esclapez, B. Medina, Comparative study of matrix-assisted laser desorption/ ionization and gas chromatography for quantitative determination of cocoa butter and cocoa butter equivalent triacylglycerol composition, Rapid Commun. Mass Spectrom. 17 (2003) 2317-2322.
    • (2003) Rapid Commun. Mass Spectrom. , vol.17 , pp. 2317-2322
    • Guyon, F.1    Absalon, C.2    Eloy, A.3    Salagoity, M.H.4    Esclapez, M.5    Medina, B.6
  • 139
    • 77954206597 scopus 로고    scopus 로고
    • Nitrocellulose film substrate minimizes fragmentation in matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of triacylglycerols
    • G. Picariello, R. Romano, F. Addeo, Nitrocellulose film substrate minimizes fragmentation in matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of triacylglycerols, Anal. Chem. 82 (2010) 5783-5791.
    • (2010) Anal. Chem. , vol.82 , pp. 5783-5791
    • Picariello, G.1    Romano, R.2    Addeo, F.3
  • 140
    • 0034107329 scopus 로고    scopus 로고
    • Determination of the fatty acid composition of saponified vegetable oils using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • F.O. Ayorinde, K. Garvin, K. Saeed, Determination of the fatty acid composition of saponified vegetable oils using matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, Rapid Commun. Mass Spectrom. 14 (2000) 608-615.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 608-615
    • Ayorinde, F.O.1    Garvin, K.2    Saeed, K.3
  • 142
    • 77956394487 scopus 로고    scopus 로고
    • An update of MALDI-TOF mass spectrometry in lipid research
    • B. Fuchs, R. Süss, J. Schiller, An update of MALDI-TOF mass spectrometry in lipid research, Progr. Lipid Res. 49 (2010) 450-475.
    • (2010) Progr. Lipid Res. , vol.49 , pp. 450-475
    • Fuchs, B.1    Süss, R.2    Schiller, J.3
  • 143
    • 74949103391 scopus 로고    scopus 로고
    • On line ozonolysis methods for the determination of double bond position in unsaturated lipids
    • M.C. Thomas, T.W. Mitchell, S.J. Blanksby, On line ozonolysis methods for the determination of double bond position in unsaturated lipids, Methods Mol. Biol. 579 (2009) 413-441.
    • (2009) Methods Mol. Biol. , vol.579 , pp. 413-441
    • Thomas, M.C.1    Mitchell, T.W.2    Blanksby, S.J.3
  • 145
    • 77955860240 scopus 로고    scopus 로고
    • Quantitative analysis of positional isomers of triacylglycerols via electrospray ionization tandem mass spectrometry of sodiated adducts
    • L.C. Herrera, M.A. Potvin, J.E. Melanson, Quantitative analysis of positional isomers of triacylglycerols via electrospray ionization tandem mass spectrometry of sodiated adducts, Rapid Commun. Mass Spectrom. 24 (2010) 2745-2752.
    • (2010) Rapid Commun. Mass Spectrom. , vol.24 , pp. 2745-2752
    • Herrera, L.C.1    Potvin, M.A.2    Melanson, J.E.3
  • 146
    • 0013652874 scopus 로고
    • Quantitative high-resolution C-13 NMR analysis of lipids extracted from the white muscle of Atlantic tuna (Thunnus alalunga)
    • R. Sacchi, I. Medina, S.P. Aubourg, I. Giudicianni, L. Paolillo, F. Addeo, Quantitative high-resolution C-13 NMR analysis of lipids extracted from the white muscle of Atlantic tuna (Thunnus alalunga), J. Agric. Food Chem. 41 (1993) 1247-1253.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1247-1253
    • Sacchi, R.1    Medina, I.2    Aubourg, S.P.3    Giudicianni, I.4    Paolillo, L.5    Addeo, F.6
  • 147
    • 0036473985 scopus 로고    scopus 로고
    • 13C--NMR spectra of TAG: An easy way to distinguish milks from different animal species
    • G. Andreotti, R. Lamanna, E. Trivellone, A. Motta, 13C--NMR spectra of TAG: An easy way to distinguish milks from different animal species, J. Am. Oil Chem. Soc. 79 (2002) 123-127.
    • (2002) J. Am. Oil Chem. Soc. , vol.79 , pp. 123-127
    • Andreotti, G.1    Lamanna, R.2    Trivellone, E.3    Motta, A.4
  • 148
    • 0028786772 scopus 로고
    • Electrospray liquid chromatography mass spectrometry of carotenoids
    • R.B. Van Breemen, Electrospray liquid chromatography mass spectrometry of carotenoids, Anal. Chem. 67 (1995) 2004-2009.
    • (1995) Anal. Chem. , vol.67 , pp. 2004-2009
    • Van Breemen, R.B.1
  • 149
    • 84858701312 scopus 로고    scopus 로고
    • Rapid determination of lycopene and b-carotene in tomato by liquid chromatography/electrospray tandem mass spectrometry
    • L. Lucin, M. Pellizzoni, C. Baffi, G.P. Molinari, Rapid determination of lycopene and b-carotene in tomato by liquid chromatography/electrospray tandem mass spectrometry, J. Sci. Food Agric. 92 (2011) 1297-1303.
    • (2011) J. Sci. Food Agric. , vol.92 , pp. 1297-1303
    • Lucin, L.1    Pellizzoni, M.2    Baffi, C.3    Molinari, G.P.4
  • 150
    • 77956863350 scopus 로고    scopus 로고
    • (ESI+) determination of structural and geometrical isomers of carotenoids in mature grapes
    • P. Crupi, R.A. Milella, D. Antonacci, Simultaneous HPLC--DAD-MS (ESI+) determination of structural and geometrical isomers of carotenoids in mature grapes, J. Mass Spectrom. 45 (2010) 971-980.
    • (2010) J. Mass Spectrom. , vol.45 , pp. 971-980
    • Crupi, P.1    Milella, R.A.2    Antonacci, D.3    Simultaneous, H.-D.-M.4
  • 151
    • 79960082011 scopus 로고    scopus 로고
    • Ultra-high performance liquid chromatography-tandem mass spectrometry in high-throughput confirmation and quantification of 34 anabolic steroids in bovine muscle
    • L. Vanhaecke, J. Vanden Bussche, K. Wille, K. Bekaert, H.F. De Brabander, Ultra-high performance liquid chromatography-tandem mass spectrometry in high-throughput confirmation and quantification of 34 anabolic steroids in bovine muscle, Anal. Chim. Acta, 700 (2011) 70-77.
    • (2011) Anal. Chim. Acta , vol.700 , pp. 70-77
    • Vanhaecke, L.1    Vanden Bussche, J.2    Wille, K.3    Bekaert, K.4    De Brabander, H.F.5
  • 153
    • 64549097631 scopus 로고    scopus 로고
    • Comparison of analysis of vitamin D3 in foods using ultraviolet and mass spectrometric detection
    • W.C. Byrdwell, Comparison of analysis of vitamin D3 in foods using ultraviolet and mass spectrometric detection, J. Agric. Food Chem. 25 (2009) 2135-2146.
    • (2009) J. Agric. Food Chem. , vol.25 , pp. 2135-2146
    • Byrdwell, W.C.1
  • 154
    • 38049077423 scopus 로고    scopus 로고
    • Pomegranate oil analysis with emphasis on MALDI-TOF/MS triacylglycerol fingerprinting
    • M. Kaufman, Z. Wiesman, Pomegranate oil analysis with emphasis on MALDI-TOF/MS triacylglycerol fingerprinting, J. Agric. Food Chem. 55 (2007) 10405-10413.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 10405-10413
    • Kaufman, M.1    Wiesman, Z.2
  • 156
    • 0035735890 scopus 로고    scopus 로고
    • N-and O-linked oligosaccharides of allergenic glycoproteins
    • K. Fötisch, S. Vieths, N- and O-linked oligosaccharides of allergenic glycoproteins, Glycoconj. J. 18 (2001) 373-383.
    • (2001) Glycoconj. J. , vol.18 , pp. 373-383
    • Fötisch, K.1    Vieths, S.2
  • 157
  • 158
    • 0038581900 scopus 로고    scopus 로고
    • Immunoreactivity in mammals of two typical plant glyco-epitopes, core a(1,3)-fucose and core xylose
    • M. Bardor, C. Faveeuw, A.C. Fitchette, D. Gilbert, L. Galas, F. Trottein et al., Immunoreactivity in mammals of two typical plant glyco-epitopes, core a(1,3)-fucose and core xylose, Glycobiology, 13 (2003) 427-434.
    • (2003) Glycobiology , vol.13 , pp. 427-434
    • Bardor, M.1    Faveeuw, C.2    Fitchette, A.C.3    Gilbert, D.4    Galas, L.5    Trottein, F.6
  • 159
    • 0034120710 scopus 로고    scopus 로고
    • Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation
    • S.J. Maleki, R.A. Kopper, D.S. Shin, C.W. Park, C.M. Compadre, H. Sampson et al., Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation, J. Immunol. 164 (2000) 5844-5849.
    • (2000) J. Immunol. , vol.164 , pp. 5844-5849
    • Maleki, S.J.1    Kopper, R.A.2    Shin, D.S.3    Park, C.W.4    Compadre, C.M.5    Sampson, H.6
  • 160
    • 0033582479 scopus 로고    scopus 로고
    • Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
    • S.J. Koppelman, C.A. Bruijnzeel-Koomen, M. Hessing, H.H. de Jongh, Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties, J. Biol. Chem. 274 (1999) 4770-4777.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4770-4777
    • Koppelman, S.J.1    Bruijnzeel-Koomen, C.A.2    Hessing, M.3    De Jongh, H.H.4
  • 161
    • 34047164035 scopus 로고    scopus 로고
    • Glycoproteomics based on tandem mass spectrometry of glycopeptides
    • M. Wuhrer, M.I. Catalina, A.M. Deelder, C.H. Hokke, Glycoproteomics based on tandem mass spectrometry of glycopeptides, J. Chromatogr. B, 849 (2007) 115-128.
    • (2007) J. Chromatogr. B , vol.849 , pp. 115-128
    • Wuhrer, M.1    Catalina, M.I.2    Deelder, A.M.3    Hokke, C.H.4
  • 162
    • 0034083133 scopus 로고    scopus 로고
    • Human milk oligosaccharides are resistant to enzymatic hydrolysis in the upper gastrointestinal tract
    • M.B. Engfer, B. Stahl, B. Finke, G. Sawatzki, H. Daniel, Human milk oligosaccharides are resistant to enzymatic hydrolysis in the upper gastrointestinal tract, Am. J. Clin. Nutr. 71 (2000) 1589-1596.
    • (2000) Am. J. Clin. Nutr. , vol.71 , pp. 1589-1596
    • Engfer, M.B.1    Stahl, B.2    Finke, B.3    Sawatzki, G.4    Daniel, H.5
  • 163
    • 69749125001 scopus 로고    scopus 로고
    • Gastrointestinal microflora, food components and colon cancer prevention
    • C.D. Davis, J.A. Milner, Gastrointestinal microflora, food components and colon cancer prevention, J. Nutr. Biochem. 20 (2009) 743-752.
    • (2009) J. Nutr. Biochem. , vol.20 , pp. 743-752
    • Davis, C.D.1    Milner, J.A.2
  • 164
    • 79955124747 scopus 로고    scopus 로고
    • Functional oligosaccharides: Production, properties and applications
    • S. Patel, A. Goyal, Functional oligosaccharides: Production, properties and applications, World J. Microbiol. Biotechnol. 27 (2011) 1119-1128.
    • (2011) World J. Microbiol. Biotechnol. , vol.27 , pp. 1119-1128
    • Patel, S.1    Goyal, A.2
  • 166
    • 0031569338 scopus 로고    scopus 로고
    • Analysis of fructans from higher plants by matrix-assisted laser desorption/ionization mass spectrometry
    • B. Stahl, A. Linos, M. Karas, F. Hillenkamp, M. Steup, Analysis of fructans from higher plants by matrix-assisted laser desorption/ionization mass spectrometry, Anal. Biochem. 246 (1997) 195-204.
    • (1997) Anal. Biochem. , vol.246 , pp. 195-204
    • Stahl, B.1    Linos, A.2    Karas, M.3    Hillenkamp, F.4    Steup, M.5
  • 167
    • 0141672821 scopus 로고    scopus 로고
    • Molecular size of garlic fructooligosaccharides and fructopolysaccharides by matrix-assisted laser desorption ionization mass spectrometry
    • J.N. Losso, S. Nakai, Molecular size of garlic fructooligosaccharides
    • (1997) J. Agric. Food Chem. , vol.45 , pp. 4342-4346
    • Losso, J.N.1    Nakai, S.2
  • 168
    • 33746556603 scopus 로고    scopus 로고
    • Simple and fast method for recognition of reducing and nonreducing neutral carbohydrates by matrix-assisted laser desorption/ionization time--of-flight mass spectrometry
    • M. Laštovicková, J. Chmelík, Simple and fast method for recognition of reducing and nonreducing neutral carbohydrates by matrix-assisted laser desorption/ionization time--of-flight mass spectrometry, J. Agric. Food Chem. 54 (2006) 5092-5097.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 5092-5097
    • Laštovicková, M.1    Chmelík, J.2
  • 169
    • 4143124420 scopus 로고    scopus 로고
    • Determination of neutral oligosaccharides in vegetables by matrix-assisted laser desorption/ ionization mass spectrometry
    • M. Tikarovská, J. Chmelík, Determination of neutral oligosaccharides in vegetables by matrix-assisted laser desorption/ ionization mass spectrometry, Anal. Chim. Acta, 520 (2004) 47-55.
    • (2004) Anal. Chim. Acta , vol.520 , pp. 47-55
    • Tikarovská, M.1    Chmelík, J.2
  • 170
    • 41149086364 scopus 로고    scopus 로고
    • Analysis and quantitation of fructooligosaccharides using matrix-assisted laser desorption/ ionization Fourier transform ion cyclotron resonance mass spectrometry
    • R.R. Seipert, M. Barboza, M.R. Niñonuevo, R.G. LoCascio D.A. Mills, S.L. Freeman et al., Analysis and quantitation of fructooligosaccharides using matrix-assisted laser desorption/ ionization Fourier transform ion cyclotron resonance mass spectrometry, Anal. Chem. 80 (2008) 159-165.
    • (2008) Anal. Chem. , vol.80 , pp. 159-165
    • Seipert, R.R.1    Barboza, M.2    Niñonuevo, M.R.3    LoCascio, R.G.4    Mills, D.A.5    Freeman, S.L.6
  • 171
    • 0031734879 scopus 로고    scopus 로고
    • A general approach to desalting oligosaccharides released from glycoproteins
    • N.H. Packer, M.A. Lawson, D.R. Jardine, J.W. Redmond, A general approach to desalting oligosaccharides released from glycoproteins, Glycoconj. J. 15 (1998) 737-747.
    • (1998) Glycoconj. J. , vol.15 , pp. 737-747
    • Packer, N.H.1    Lawson, M.A.2    Jardine, D.R.3    Redmond, J.W.4
  • 173
    • 66149129573 scopus 로고    scopus 로고
    • Method for investigation of oligosaccharides using phenylhydrazine derivatization
    • E. Lattová, H. Perreault, Method for investigation of oligosaccharides using phenylhydrazine derivatization, Methods Mol. Biol. 534 (2009) 65-77.
    • (2009) Methods Mol. Biol. , vol.534 , pp. 65-77
    • Lattová, E.1    Perreault, H.2
  • 174
    • 0036009362 scopus 로고    scopus 로고
    • Analysis of saccharides in beer samples by flow injection with electrospray mass spectrometry
    • P. Mauri, M. Minoggio, P. Somonetti, C. Gardana, P. Pietta, Analysis of saccharides in beer samples by flow injection with electrospray mass spectrometry, Rapid Commun. Mass Spectrom. 16 (2002) 743-748.
    • (2002) Rapid Commun. Mass Spectrom. , vol.16 , pp. 743-748
    • Mauri, P.1    Minoggio, M.2    Somonetti, P.3    Gardana, C.4    Pietta, P.5
  • 175
    • 0037649054 scopus 로고    scopus 로고
    • Characterization of plant oligosaccharides by matrix-assisted laser desorption/ionization and electrospray mass spectrometry
    • L.E. Matamoros Fernández, N. Obel, H.V. Scheller, P. Roepstorff, Characterization of plant oligosaccharides by matrix-assisted laser desorption/ionization and electrospray mass spectrometry, J. Mass Spectrom. 38 (2003) 427-437.
    • (2003) J. Mass Spectrom. , vol.38 , pp. 427-437
    • Matamoros Fernández, L.E.1    Obel, N.2    Scheller, H.V.3    Roepstorff, P.4
  • 176
  • 177
    • 51649085326 scopus 로고    scopus 로고
    • Mass spectrometry and the emerging field of glycomics
    • J. Zaia, Mass spectrometry and the emerging field of glycomics, Chem. Biol. 15 (2008) 881-892.
    • (2008) Chem. Biol. , vol.15 , pp. 881-892
    • Zaia, J.1
  • 178
    • 34548700809 scopus 로고    scopus 로고
    • Discrimination of 16 structural isomers of fucosyl galactoside based on energy-resolved mass spectrometry
    • S. Daikoku, T. Ako, R. Kato, I. Ohtsuka, O. Kanie, Discrimination of 16 structural isomers of fucosyl galactoside based on energy-resolved mass spectrometry, J. Am. Soc. Mass Spectrom. 18 (2007) 1873-1879.
    • (2007) J. Am. Soc. Mass Spectrom. , vol.18 , pp. 1873-1879
    • Daikoku, S.1    Ako, T.2    Kato, R.3    Ohtsuka, I.4    Kanie, O.5
  • 179
    • 0038148603 scopus 로고    scopus 로고
    • Lipid and oxylipin profiles during aging and sprout development in potato tubers (Solanum tuberosum L.)
    • M.L. Fauconnier, R. Welti, E. Blée, M. Marlier, Lipid and oxylipin profiles during aging and sprout development in potato tubers (Solanum tuberosum L.), Biochim. Biophys. Acta, 1633 (2003) 118-126.
    • (2003) Biochim. Biophys. Acta , vol.1633 , pp. 118-126
    • Fauconnier, M.L.1    Welti, R.2    Blée, E.3    Marlier, M.4
  • 180
    • 38049028642 scopus 로고    scopus 로고
    • Novel galactolipids from the leaves of Ipomoea batatas L.: Characterization by liquid chromatography coupled with electrospray ionization-quadrupole time-of-flight tandem mass spectrometry
    • A. Napolitano, V. Carbone, P. Saggese, K. Takagaki, C. Pizza, Novel galactolipids from the leaves of Ipomoea batatas L.: Characterization by liquid chromatography coupled with electrospray ionization-quadrupole time-of-flight tandem mass spectrometry, J. Agric. Food Chem. 55 (2007) 10289- 10297.
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 10289-10297
    • Napolitano, A.1    Carbone, V.2    Saggese, P.3    Takagaki, K.4    Pizza, C.5
  • 181
    • 0035114313 scopus 로고    scopus 로고
    • Analysis of molecular species of glycolipids in fruit pastes of red bell pepper (Capsicum annuum L.) by high-performance liquid chromatography-mass spectrometry
    • R. Yamauchi, K. Aizawa, T. Inakuma, K. Kato, Analysis of molecular species of glycolipids in fruit pastes of red bell pepper (Capsicum annuum L.) by high-performance liquid chromatography-mass spectrometry, J. Agric. Food Chem. 49 (2001) 622-627.
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 622-627
    • Yamauchi, R.1    Aizawa, K.2    Inakuma, T.3    Kato, K.4
  • 182
    • 49349114712 scopus 로고    scopus 로고
    • The identification of mono-, di-, tri-, and tetragalactosyl-diacylglycerols and their natural estolides in oat kernels
    • R.A. Moreau, D.C. Doehlert, R. Welti, G. Isaac, M. Roth, P. Tamura, A. Nuñez, The identification of mono-, di-, tri-, and tetragalactosyl-diacylglycerols and their natural estolides in oat kernels, Lipids, 43 (2008) 533-548.
    • (2008) Lipids , vol.43 , pp. 533-548
    • Moreau, R.A.1    Doehlert, D.C.2    Welti, R.3    Isaac, G.4    Roth, M.5    Tamura, P.6    Nuñez, A.7
  • 183
    • 79955770452 scopus 로고    scopus 로고
    • Structural characterization of neutral oligosaccharides by laser-enhanced in-source decay of MALDI-FTICR MS
    • H. Yang, Y. Yu, F. Song, S. Liu, Structural characterization of neutral oligosaccharides by laser-enhanced in-source decay of MALDI-FTICR MS, J. Am. Soc. Mass Spectrom. 22 (2011) 845-855.
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 845-855
    • Yang, H.1    Yu, Y.2    Song, F.3    Liu, S.4
  • 184
    • 77949710577 scopus 로고    scopus 로고
    • Mass spectrometric methods for analysis of oligosaccharides in human milk
    • M.R. Niñonuevo, C.B. Lebrilla, Mass spectrometric methods for analysis of oligosaccharides in human milk, Nutr. Rev. 67 (2009) 216-226.
    • (2009) Nutr. Rev. , vol.67 , pp. 216-226
    • Niñonuevo, M.R.1    Lebrilla, C.B.2
  • 185
    • 79953709953 scopus 로고    scopus 로고
    • Annotation and structural analysis of sialylated human milk oligosaccharides
    • S. Wu, R. Grimm, J.B. German, C.B. Lebrilla, Annotation and structural analysis of sialylated human milk oligosaccharides, J. Proteome Res. 10 (2011) 856-868.
    • (2011) J. Proteome Res. , vol.10 , pp. 856-868
    • Wu, S.1    Grimm, R.2    German, J.B.3    Lebrilla, C.B.4
  • 186
    • 68149089456 scopus 로고    scopus 로고
    • Variations in bovine milk oligosaccharides during early and middle lactation stages analyzed by high-performance liquid chromatography-chip/mass spectrometry
    • N. Tao, E.J. DePeters, J.B German, R. Grimm, C.B. Lebrilla, Variations in bovine milk oligosaccharides during early and middle lactation stages analyzed by high-performance liquid chromatography-chip/mass spectrometry, J. Dairy Sci. 92 (2009) 2991-3001.
    • (2009) J. Dairy Sci. , vol.92 , pp. 2991-3001
    • Tao, N.1    DePeters, E.J.2    German, J.B.3    Grimm, R.4    Lebrilla, C.B.5
  • 188
    • 79953727599 scopus 로고    scopus 로고
    • Evolutionary glycomics: Characterization of milk oligosaccharides in primates
    • N. Tao, S. Wu, J. Kim, H.J. An, K. Hinde, M.L. Power et al., Evolutionary glycomics: Characterization of milk oligosaccharides in primates, J. Proteome Res. 10 (2011) 1548- 1557.
    • (2011) J. Proteome Res. , vol.10 , pp. 1548-1557
    • Tao, N.1    Wu, S.2    Kim, J.3    An, H.J.4    Hinde, K.5    Power, M.L.6
  • 190
    • 72949102869 scopus 로고    scopus 로고
    • Glycoprofiling bifidobacterial consumption of galacto-oligosaccharides by mass spectrometry reveals strain-specific, preferential consumption of glycans
    • M. Barboza, D.A. Sela, C. Pirim, R.G. Locascio, S.L. Freeman, J.B. German et al., Glycoprofiling bifidobacterial consumption of galacto-oligosaccharides by mass spectrometry reveals strain-specific, preferential consumption of glycans, Appl. Environ. Microbiol. 75 (2009) 7319-7325.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7319-7325
    • Barboza, M.1    Sela, D.A.2    Pirim, C.3    Locascio, R.G.4    Freeman, S.L.5    German, J.B.6
  • 191
    • 67349260397 scopus 로고    scopus 로고
    • Permeate from cheese whey ultrafiltration is a source of milk oligosaccharides
    • D. Barile, N. Tao, C.B. Lebrilla, J.D. Coisson, M. Arlorio, Permeate from cheese whey ultrafiltration is a source of milk oligosaccharides, Int. Dairy J. 19 (2009) 524-530.
    • (2009) Int. Dairy J. , vol.19 , pp. 524-530
    • Barile, D.1    Tao, N.2    Lebrilla, C.B.3    Coisson, J.D.4    Arlorio, M.5
  • 192
    • 28544444249 scopus 로고    scopus 로고
    • Glycomics: An integrated systems approach to structure-function relationships of glycans
    • R. Raman, S. Raguram, G. Venkataraman, J.C. Paulson, R. Sasisekharan, Glycomics: An integrated systems approach to structure-function relationships of glycans, Nat. Methods, 2 (2005) 817-824.
    • (2005) Nat. Methods , vol.2 , pp. 817-824
    • Raman, R.1    Raguram, S.2    Venkataraman, G.3    Paulson, J.C.4    Sasisekharan, R.5
  • 193
    • 33947307759 scopus 로고    scopus 로고
    • Plant metabolomics: Towards biological function and mechanism
    • N. Schauer, A.R. Fernie, Plant metabolomics: Towards biological function and mechanism, Trends Plant Sci. 11 (2006) 508-516.
    • (2006) Trends Plant Sci , vol.11 , pp. 508-516
    • Schauer, N.1    Fernie, A.R.2
  • 194
    • 38149013060 scopus 로고    scopus 로고
    • Plant metabolomics and its potential application for human nutrition
    • R.D. Hall, I.D. Brouwer, M.A. Fitzgerald, Plant metabolomics and its potential application for human nutrition, Physiol. Plant. 132 (2008) 162-175.
    • (2008) Physiol. Plant. , vol.132 , pp. 162-175
    • Hall, R.D.1    Brouwer, I.D.2    Fitzgerald, M.A.3
  • 195
    • 33747326809 scopus 로고    scopus 로고
    • Anthocyanins profile as fingerprint of wines using atmospheric pressure photoionisation coupled to quadrupole time-of-flight mass spectrometry
    • J.L. Gómez-Arisa, T. García-Barrera, F. Lorenzo, Anthocyanins profile as fingerprint of wines using atmospheric pressure photoionisation coupled to quadrupole time-of-flight mass spectrometry, Anal. Chim. Acta, 570 (2006) 101-108.
    • (2006) Anal. Chim. Acta , vol.570 , pp. 101-108
    • Gómez-Arisa, J.L.1    García-Barrera, T.2    Lorenzo, F.3
  • 197
    • 48949118698 scopus 로고    scopus 로고
    • Metabolomics: Applications to food science and nutrition research
    • S.D. Wishar, Metabolomics: Applications to food science and nutrition research, Trends Food Sci. Technol. 19 (2008) 482-493.
    • (2008) Trends Food Sci. Technol. , vol.19 , pp. 482-493
    • Wishar, S.D.1
  • 198
    • 63849182878 scopus 로고    scopus 로고
    • Mesophilic and psychrotrophic bacteria from meat and their spoilage potential in vitro and in beef
    • D. Ercolini, F. Russo, A. Nasi, P. Ferranti, F. Villani, Mesophilic and psychrotrophic bacteria from meat and their spoilage potential in vitro and in beef, Appl. Environ. Microbiol. 75 (2009) 1990-2001.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1990-2001
    • Ercolini, D.1    Russo, F.2    Nasi, A.3    Ferranti, P.4    Villani, F.5
  • 199
  • 200
    • 0034096182 scopus 로고    scopus 로고
    • Characterisation of bacteria by matrix--assisted laser desorption/ionisation and electrospray mass spectrometry
    • B.L.M. Van Baar, Characterisation of bacteria by matrix--assisted laser desorption/ionisation and electrospray mass spectrometry, FEMS Microbiol. Rev. 24 (2000) 193-219.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 193-219
    • Van Baar, B.L.M.1
  • 201
    • 0034255691 scopus 로고    scopus 로고
    • Rapid isolation and identification of staphylococcal exoproteins by reverse phase capillary high performance liquid chromatography-electrospray ionization mass spectrometry
    • Y. Kawano, Y. Ito, Y. Yamakawa, T. Yamashimo, T. Horii, T. Hasegawa, M. Ohta, Rapid isolation and identification of staphylococcal exoproteins by reverse phase capillary high performance liquid chromatography-electrospray ionization mass spectrometry, FEMS Microbiol. 189 (2000) 103- 108.
    • (2000) FEMS Microbiol , vol.189 , pp. 103-108
    • Kawano, Y.1    Ito, Y.2    Yamakawa, Y.3    Yamashimo, T.4    Horii, T.5    Hasegawa, T.6    Ohta, M.7
  • 202
    • 79957976289 scopus 로고    scopus 로고
    • Simultaneous quantification of eight biogenic amine compounds in tuna by matrix solid-phase dispersion followed by HPLC-Orbitrap mass spectrometry
    • R.L. Self, W.H. Wu, H.S. Marks, Simultaneous quantification of eight biogenic amine compounds in tuna by matrix solid-phase dispersion followed by HPLC-Orbitrap mass spectrometry, J. Agric. Food Chem. 59 (2011) 5906-5913.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 5906-5913
    • Self, R.L.1    Wu, W.H.2    Marks, H.S.3
  • 203
    • 20844453276 scopus 로고    scopus 로고
    • Rapid assay for analyzing biogenic amines in cheese: Matrix solid-phase dispersion followed by liquid chromatography-electrospray-tandem mass spectrometry
    • F. Calbiani, M. Careri, L. Elviri, A. Mangia, L. Pistarà, I. Zagnoni, Rapid assay for analyzing biogenic amines in cheese: Matrix solid-phase dispersion followed by liquid chromatography-electrospray-tandem mass spectrometry, J. Agric. Food Chem. 53 (2005) 3779-3783.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 3779-3783
    • Calbiani, F.1    Careri, M.2    Elviri, L.3    Mangia, A.4    Pistarà, L.5    Zagnoni, I.6
  • 204
    • 43649086418 scopus 로고    scopus 로고
    • Sensomics mapping and identification of the key bitter metabolites in Gouda cheese
    • S. Toelstede, T. Hofmann, Sensomics mapping and identification of the key bitter metabolites in Gouda cheese, J. Agric. Food Chem. 56 (2008) 2795-2804.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 2795-2804
    • Toelstede, S.1    Hofmann, T.2
  • 205
    • 43049120224 scopus 로고    scopus 로고
    • Identification of free and bound volatile compounds as typicalness and authenticity markers of non-aromatic grapes and wines through a combined use of mass spectrometric techniques
    • A. Nasi, P. Ferranti, S. Amato, L. Chianese, Identification of free and bound volatile compounds as typicalness and authenticity markers of non-aromatic grapes and wines through a combined use of mass spectrometric techniques, Food Chem. 110 (2008) 762-768.
    • (2008) Food Chem , vol.110 , pp. 762-768
    • Nasi, A.1    Ferranti, P.2    Amato, S.3    Chianese, L.4
  • 206
    • 77950685615 scopus 로고    scopus 로고
    • Evolution of S-cysteinylated and S-glutathionylated thiol precursors during oxidation of Melon B. and Sauvignon blanc musts
    • A. Roland, J. Vialaret, A. Razungles, P. Rigou, R. Schneider, Evolution of S-cysteinylated and S-glutathionylated thiol precursors during oxidation of Melon B. and Sauvignon blanc musts, J. Agric. Food Chem. 58 (2010) 4406- 4413.
    • (2010) J. Agric. Food Chem. , vol.58 , pp. 4406-4413
    • Roland, A.1    Vialaret, J.2    Razungles, A.3    Rigou, P.4    Schneider, R.5
  • 207
    • 67649382947 scopus 로고    scopus 로고
    • Improved method to quantitatively determine powerful odorant volatile thiols in wine by headspace solid--phase microextraction after derivatization
    • J.J. Rodríguez-Bencomo, R. Schneider, J.P. Lepoutre, P. Rigou, Improved method to quantitatively determine powerful odorant volatile thiols in wine by headspace solid--phase microextraction after derivatization, J. Chromatogr. A, 1216 (2009) 5640-5646.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5640-5646
    • Rodríguez-Bencomo, J.J.1    Schneider, R.2    Lepoutre, J.P.3    Rigou, P.4
  • 208
    • 34548863332 scopus 로고    scopus 로고
    • Comparative interactomics: Comparing apples and pears?
    • L. Kiemer, G. Cesareni, Comparative interactomics: Comparing apples and pears?, Trends Biochem. 25 (2007) 448- 454.
    • (2007) Trends Biochem , vol.25 , pp. 448-454
    • Kiemer, L.1    Cesareni, G.2
  • 209
    • 33645453254 scopus 로고    scopus 로고
    • Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
    • N.J. Krogan, G. Cagney, H. Yu, G. Zhong, X. Guo, A. Ignatchenko, Global landscape of protein complexes in the yeast Saccharomyces cerevisiae, Nature, 440 (2006) 637-643.
    • (2006) Nature , vol.440 , pp. 637-643
    • Krogan, N.J.1    Cagney, G.2    Yu, H.3    Zhong, G.4    Guo, X.5    Ignatchenko, A.6
  • 211
    • 78149495201 scopus 로고    scopus 로고
    • Identification of Lactobacillus plantarum genes modulating the cytokine response of human peripheral blood mononuclear cells
    • S. van Hemert, M. Meijerink, D. Molenaar, P.A. Bron, P. de Vos, M. Kleerebezem et al., Identification of Lactobacillus plantarum genes modulating the cytokine response of human peripheral blood mononuclear cells, BMC Microbiol. 16 (2010) 293-305.
    • (2010) BMC Microbiol , vol.16 , pp. 293-305
    • Van Hemert, S.1    Meijerink, M.2    Molenaar, D.3    Bron, P.A.4    De Vos, P.5    Kleerebezem, M.6
  • 212
    • 58149107941 scopus 로고    scopus 로고
    • Interactomics in the human intestine: Lactobacilli and Bifidobacteria make a difference
    • R.J. Boesten, W.M. de Vos, Interactomics in the human intestine: Lactobacilli and Bifidobacteria make a difference, J. Clin. Gastroenterol. 42 (2008) 163-167.
    • (2008) J. Clin. Gastroenterol. , vol.42 , pp. 163-167
    • Boesten, R.J.1    De Vos, W.M.2
  • 214
    • 17144368764 scopus 로고    scopus 로고
    • Identification and quantification of e-(g-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS)
    • C. Schafer, M. Schott, F. Brandl, S. Neidhart, R. Carle, Identification and quantification of e-(g-glutamyl)lysine in digests of enzymatically cross-linked leguminous proteins by high-performance liquid chromatography-electrospray ionization mass spectrometry (HPLC-ESI-MS), J. Agric. Food Chem. 53 (2005) 2830-2837.
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2830-2837
    • Schafer, C.1    Schott, M.2    Brandl, F.3    Neidhart, S.4    Carle, R.5
  • 215
    • 13844272546 scopus 로고    scopus 로고
    • Polyphenols in foods are more complex than often thought
    • V. Cheynier, Polyphenols in foods are more complex than often thought, Am. J. Clin. Nutr. 81 (2005) 223S-229S.
    • (2005) Am. J. Clin. Nutr. , vol.81
    • Cheynier, V.1
  • 218
    • 23044462504 scopus 로고    scopus 로고
    • Probing heat-stable water-soluble proteins from barley to malt and beer
    • L. Perrocheau, H. Rogniaux, P. Boivin, D. Marion, Probing heat-stable water-soluble proteins from barley to malt and beer, Proteomics, 5 (2005) 2849-2858.
    • (2005) Proteomics , vol.5 , pp. 2849-2858
    • Perrocheau, L.1    Rogniaux, H.2    Boivin, P.3    Marion, D.4
  • 219
    • 53649109386 scopus 로고    scopus 로고
    • Novel prediction method of beer foam stability using protein Z, barley dimeric a-amylase inhibitor-1 (BDAI-1) and yeast thioredoxin
    • T. Iimure, K. Takoi, T. Kaneko, M. Kihara, K. Hayashi, K. Ito et al., Novel prediction method of beer foam stability using protein Z, barley dimeric a-amylase inhibitor-1 (BDAI-1) and yeast thioredoxin, J. Agric. Food Chem. 56 (2008) 8664-8671.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 8664-8671
    • Iimure, T.1    Takoi, K.2    Kaneko, T.3    Kihara, M.4    Hayashi, K.5    Ito, K.6
  • 220
    • 40549116282 scopus 로고    scopus 로고
    • The influence of barley malt protein modification on beer foam stability and their relationship to the barley dimeric a-amylase inhibitor-I (BDAI-I) as a possible foam-promoting protein
    • Y. Okada, T. Iimure, K. Takoi, T. Kaneko, M. Kihara, K. Hayashi et al., The influence of barley malt protein modification on beer foam stability and their relationship to the barley dimeric a-amylase inhibitor-I (BDAI-I) as a possible foam-promoting protein, J. Agric. Food Chem. 56 (2008) 1458-1464.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 1458-1464
    • Okada, Y.1    Iimure, T.2    Takoi, K.3    Kaneko, T.4    Kihara, M.5    Hayashi, K.6
  • 221
    • 0023070919 scopus 로고
    • Dietary tannins and salivary proline-rich proteins: Interactions, induction, and defense mechanisms
    • H. Mehansho, L.G. Butler, D.M. Carlson, Dietary tannins and salivary proline-rich proteins: Interactions, induction, and defense mechanisms, Ann. Rev. Nutr. 7 (1987) 423-440.
    • (1987) Ann. Rev. Nutr. , vol.7 , pp. 423-440
    • Mehansho, H.1    Butler, L.G.2    Carlson, D.M.3
  • 222
    • 70349876855 scopus 로고    scopus 로고
    • Mass spectrometry of large complexes
    • C. Bich, R. Zenobi, Mass spectrometry of large complexes, Curr. Opin. Struct. Biol. 19 (2009) 632-639.
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 632-639
    • Bich, C.1    Zenobi, R.2
  • 223
    • 79957931676 scopus 로고    scopus 로고
    • Bound fatty acids modulate the sensitivity of bovine b-lactoglobulin to chemical and physical denaturation
    • A. Barbiroli, F. Bonomi, P. Ferranti, D. Fessas, A. Nasi, P. Rasmussen, S. Iametti, Bound fatty acids modulate the sensitivity of bovine b-lactoglobulin to chemical and physical denaturation, J. Agric. Food Chem. 59 (2011) 5729-5737.
    • (2011) J. Agric. Food Chem. , vol.59 , pp. 5729-5737
    • Barbiroli, A.1    Bonomi, F.2    Ferranti, P.3    Fessas, D.4    Nasi, A.5    Rasmussen, P.6    Iametti, S.7
  • 224
    • 55549109075 scopus 로고    scopus 로고
    • Polyphenol-b-casein complexes at the air/water interface and in solution: Effects of polyphenol structure
    • V. Aguié-Béghin, P. Sausse, E. Meudec, V. Cheynier, R. Douillard, Polyphenol-b-casein complexes at the air/water interface and in solution: Effects of polyphenol structure, J. Agric. Food Chem. 56 (2008) 9600-9611.
    • (2008) J. Agric. Food Chem. , vol.56 , pp. 9600-9611
    • Aguié-Béghin, V.1    Sausse, P.2    Meudec, E.3    Cheynier, V.4    Douillard, R.5
  • 225
    • 0041524991 scopus 로고    scopus 로고
    • Model studies on reactions of plant phenols with whey proteins
    • H.M. Rawel, J. Kroll, U.C. Hohl, Model studies on reactions of plant phenols with whey proteins, Nahrung/Food, 45 (2001) 72-81.
    • (2001) Nahrung/Food , vol.45 , pp. 72-81
    • Rawel, H.M.1    Kroll, J.2    Hohl, U.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.