메뉴 건너뛰기




Volumn 75, Issue 12, 2012, Pages 3546-3559

Mass spectrometry for nutritional peptidomics: How to analyze food bioactives and their health effects

Author keywords

Bioactive; Bioavailability; Mass spectrometry; Nutrition; Peptide; Peptidomics

Indexed keywords

BIOLOGICAL MARKER; PROTEINASE;

EID: 84862189137     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2011.12.022     Document Type: Review
Times cited : (132)

References (105)
  • 1
    • 77957360551 scopus 로고    scopus 로고
    • Proteomics in nutrition: status quo and outlook for biomarkers and bioactives
    • Kussmann M., Panchaud A., Affolter M. Proteomics in nutrition: status quo and outlook for biomarkers and bioactives. J Proteome Res 2010, 9:4876-4887.
    • (2010) J Proteome Res , vol.9 , pp. 4876-4887
    • Kussmann, M.1    Panchaud, A.2    Affolter, M.3
  • 2
    • 44049105535 scopus 로고    scopus 로고
    • Experimental and computational approaches to quantitative proteomics: status quo and outlook
    • Panchaud A., Affolter M., Moreillon P., Kussmann M. Experimental and computational approaches to quantitative proteomics: status quo and outlook. J Proteomics 2008, 71:19-33.
    • (2008) J Proteomics , vol.71 , pp. 19-33
    • Panchaud, A.1    Affolter, M.2    Moreillon, P.3    Kussmann, M.4
  • 3
    • 42449157075 scopus 로고    scopus 로고
    • Profiling techniques in nutrition and health research
    • Kussmann M., Rezzi S., Daniel H. Profiling techniques in nutrition and health research. Curr Opin Biotechnol 2008, 19:83-99.
    • (2008) Curr Opin Biotechnol , vol.19 , pp. 83-99
    • Kussmann, M.1    Rezzi, S.2    Daniel, H.3
  • 4
    • 33746211196 scopus 로고    scopus 로고
    • OMICS-driven biomarker discovery in nutrition and health
    • Kussmann M., Raymond F., Affolter M. OMICS-driven biomarker discovery in nutrition and health. J Biotechnol 2006, 124:758-787.
    • (2006) J Biotechnol , vol.124 , pp. 758-787
    • Kussmann, M.1    Raymond, F.2    Affolter, M.3
  • 5
    • 56149117157 scopus 로고    scopus 로고
    • Nutrigenomics and personalized nutrition: science and concept
    • Kussmann M., Fay L.B. Nutrigenomics and personalized nutrition: science and concept. Pers Med 2008, 5:447-455.
    • (2008) Pers Med , vol.5 , pp. 447-455
    • Kussmann, M.1    Fay, L.B.2
  • 6
    • 84862172768 scopus 로고    scopus 로고
    • The externded nutrigenomics - understanding the interplay between the genomes of food, gut microbes, and human host
    • Kussmann M., Van Bladeren P.J. The externded nutrigenomics - understanding the interplay between the genomes of food, gut microbes, and human host. Front Genet 2011, 2:1-13.
    • (2011) Front Genet , vol.2 , pp. 1-13
    • Kussmann, M.1    Van Bladeren, P.J.2
  • 8
    • 1242272750 scopus 로고    scopus 로고
    • The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology
    • Daniel H., Kottra G. The proton oligopeptide cotransporter family SLC15 in physiology and pharmacology. Pflugers Arch 2004, 447:610-618.
    • (2004) Pflugers Arch , vol.447 , pp. 610-618
    • Daniel, H.1    Kottra, G.2
  • 9
    • 0026537542 scopus 로고
    • Physiology and pathophysiology of intestinal absorption
    • Caspary W.F. Physiology and pathophysiology of intestinal absorption. Am J Clin Nutr 1992, 55:299S-308S.
    • (1992) Am J Clin Nutr , vol.55
    • Caspary, W.F.1
  • 10
    • 0024147740 scopus 로고
    • Gastrointestinal absorption of intact proteins
    • Gardner M.L. Gastrointestinal absorption of intact proteins. Annu Rev Nutr 1988, 8:329-350.
    • (1988) Annu Rev Nutr , vol.8 , pp. 329-350
    • Gardner, M.L.1
  • 11
    • 0017895531 scopus 로고
    • Transport of large breakdown products of dietary protein through the gut wall
    • Hemmings W.A., Williams E.W. Transport of large breakdown products of dietary protein through the gut wall. Gut 1978, 19:715-723.
    • (1978) Gut , vol.19 , pp. 715-723
    • Hemmings, W.A.1    Williams, E.W.2
  • 12
    • 33846133955 scopus 로고    scopus 로고
    • Computational prediction of proteotypic peptides for quantitative proteomics
    • Mallick P., Schirle M., Chen S.S., Flory M.R., Lee H., Martin D., et al. Computational prediction of proteotypic peptides for quantitative proteomics. Nat Biotechnol 2007, 25:125-131.
    • (2007) Nat Biotechnol , vol.25 , pp. 125-131
    • Mallick, P.1    Schirle, M.2    Chen, S.S.3    Flory, M.R.4    Lee, H.5    Martin, D.6
  • 13
    • 77954523086 scopus 로고    scopus 로고
    • Options and considerations when selecting a quantitative proteomics strategy
    • Domon B., Aebersold R. Options and considerations when selecting a quantitative proteomics strategy. Nat Biotechnol 2010, 28:710-721.
    • (2010) Nat Biotechnol , vol.28 , pp. 710-721
    • Domon, B.1    Aebersold, R.2
  • 15
    • 0029286291 scopus 로고
    • Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk
    • Nakamura Y., Yamamoto N., Sakai K., Okubo A., Yamazaki S., Takano T. Purification and characterization of angiotensin I-converting enzyme inhibitors from sour milk. J Dairy Sci 1995, 78:777-783.
    • (1995) J Dairy Sci , vol.78 , pp. 777-783
    • Nakamura, Y.1    Yamamoto, N.2    Sakai, K.3    Okubo, A.4    Yamazaki, S.5    Takano, T.6
  • 16
    • 70449556123 scopus 로고    scopus 로고
    • Angiotensin converting enzyme (ACE) inhibitory peptides: production and implementation of functional food
    • De Leo F., Panarese S., Gallerani R., Ceci L.R. Angiotensin converting enzyme (ACE) inhibitory peptides: production and implementation of functional food. Curr Pharm Des 2009, 15:3622-3643.
    • (2009) Curr Pharm Des , vol.15 , pp. 3622-3643
    • De Leo, F.1    Panarese, S.2    Gallerani, R.3    Ceci, L.R.4
  • 19
    • 0028838436 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS)
    • Stults J.T. Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Curr Opin Struct Biol 1995, 5:691-698.
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 691-698
    • Stults, J.T.1
  • 20
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn J.B., Mann M., Meng C.K., Wong S.F., Whitehouse C.M. Electrospray ionization for mass spectrometry of large biomolecules. Science 1989, 246:64-71.
    • (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
  • 21
    • 30144438909 scopus 로고    scopus 로고
    • Collision-induced dissociation (CID) of peptides and proteins
    • Wells J.M., McLuckey S.A. Collision-induced dissociation (CID) of peptides and proteins. Methods Enzymol 2005, 402:148-185.
    • (2005) Methods Enzymol , vol.402 , pp. 148-185
    • Wells, J.M.1    McLuckey, S.A.2
  • 23
    • 3042789073 scopus 로고    scopus 로고
    • Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry
    • Syka J.E., Coon J.J., Schroeder M.J., Shabanowitz J., Hunt D.F. Peptide and protein sequence analysis by electron transfer dissociation mass spectrometry. Proc Natl Acad Sci U S A 2004, 101:9528-9533.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9528-9533
    • Syka, J.E.1    Coon, J.J.2    Schroeder, M.J.3    Shabanowitz, J.4    Hunt, D.F.5
  • 24
    • 0034133274 scopus 로고    scopus 로고
    • Electron capture dissociation for structural characterization of multiply charged protein cations
    • Zubarev R.A., Horn D.M., Fridriksson E.K., Kelleher N.L., Kruger N.A., Lewis M.A., et al. Electron capture dissociation for structural characterization of multiply charged protein cations. Anal Chem 2000, 72:563-573.
    • (2000) Anal Chem , vol.72 , pp. 563-573
    • Zubarev, R.A.1    Horn, D.M.2    Fridriksson, E.K.3    Kelleher, N.L.4    Kruger, N.A.5    Lewis, M.A.6
  • 25
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little D.P., Speir J.P., Senko M.W., O'Connor P.B., McLafferty F.W. Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing. Anal Chem 1994, 66:2809-2815.
    • (1994) Anal Chem , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 26
    • 0029644596 scopus 로고
    • Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database
    • Yates J.R., Eng J.K., McCormack A.L., Schieltz D. Method to correlate tandem mass spectra of modified peptides to amino acid sequences in the protein database. Anal Chem 1995, 67:1426-1436.
    • (1995) Anal Chem , vol.67 , pp. 1426-1436
    • Yates, J.R.1    Eng, J.K.2    McCormack, A.L.3    Schieltz, D.4
  • 27
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 29
    • 3142702204 scopus 로고    scopus 로고
    • TANDEM: matching proteins with tandem mass spectra
    • Craig R., Beavis R.C. TANDEM: matching proteins with tandem mass spectra. Bioinformatics 2004, 20:1466-1467.
    • (2004) Bioinformatics , vol.20 , pp. 1466-1467
    • Craig, R.1    Beavis, R.C.2
  • 30
    • 35848929694 scopus 로고    scopus 로고
    • Analysis and validation of proteomic data generated by tandem mass spectrometry
    • Nesvizhskii A.I., Vitek O., Aebersold R. Analysis and validation of proteomic data generated by tandem mass spectrometry. Nat Methods 2007, 4:787-797.
    • (2007) Nat Methods , vol.4 , pp. 787-797
    • Nesvizhskii, A.I.1    Vitek, O.2    Aebersold, R.3
  • 31
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A., Nesvizhskii A.I., Kolker E., Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002, 74:5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 32
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • Elias J.E., Gygi S.P. Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 2007, 4:207-214.
    • (2007) Nat Methods , vol.4 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 33
    • 35748972060 scopus 로고    scopus 로고
    • Semi-supervised learning for peptide identification from shotgun proteomics datasets
    • Kall L., Canterbury J.D., Weston J., Noble W.S., MacCoss M.J. Semi-supervised learning for peptide identification from shotgun proteomics datasets. Nat Methods 2007, 4:923-925.
    • (2007) Nat Methods , vol.4 , pp. 923-925
    • Kall, L.1    Canterbury, J.D.2    Weston, J.3    Noble, W.S.4    MacCoss, M.J.5
  • 34
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: a tutorial
    • Lange V., Picotti P., Domon B., Aebersold R. Selected reaction monitoring for quantitative proteomics: a tutorial. Mol Syst Biol 2008, 4:222.
    • (2008) Mol Syst Biol , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 36
    • 0344737959 scopus 로고    scopus 로고
    • Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry
    • Li X.J., Zhang H., Ranish J.A., Aebersold R. Automated statistical analysis of protein abundance ratios from data generated by stable-isotope dilution and tandem mass spectrometry. Anal Chem 2003, 75:6648-6657.
    • (2003) Anal Chem , vol.75 , pp. 6648-6657
    • Li, X.J.1    Zhang, H.2    Ranish, J.A.3    Aebersold, R.4
  • 37
    • 0034789979 scopus 로고    scopus 로고
    • Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry
    • Han D.K., Eng J., Zhou H., Aebersold R. Quantitative profiling of differentiation-induced microsomal proteins using isotope-coded affinity tags and mass spectrometry. Nat Biotechnol 2001, 19:946-951.
    • (2001) Nat Biotechnol , vol.19 , pp. 946-951
    • Han, D.K.1    Eng, J.2    Zhou, H.3    Aebersold, R.4
  • 38
    • 59149084542 scopus 로고    scopus 로고
    • Targeted proteomic strategy for clinical biomarker discovery
    • Schiess R., Wollscheid B., Aebersold R. Targeted proteomic strategy for clinical biomarker discovery. Mol Oncol 2009, 3:33-44.
    • (2009) Mol Oncol , vol.3 , pp. 33-44
    • Schiess, R.1    Wollscheid, B.2    Aebersold, R.3
  • 39
    • 77954464041 scopus 로고    scopus 로고
    • Proteomics: a pragmatic perspective
    • Mallick P., Kuster B. Proteomics: a pragmatic perspective. Nat Biotechnol 2010, 28:695-709.
    • (2010) Nat Biotechnol , vol.28 , pp. 695-709
    • Mallick, P.1    Kuster, B.2
  • 40
    • 78649410782 scopus 로고    scopus 로고
    • Intact mass detection, interpretation, and visualization to automate Top-Down proteomics on a large scale
    • Durbin K.R., Tran J.C., Zamdborg L., Sweet S.M., Catherman A.D., Lee J.E., et al. Intact mass detection, interpretation, and visualization to automate Top-Down proteomics on a large scale. Proteomics 2010, 10:3589-3597.
    • (2010) Proteomics , vol.10 , pp. 3589-3597
    • Durbin, K.R.1    Tran, J.C.2    Zamdborg, L.3    Sweet, S.M.4    Catherman, A.D.5    Lee, J.E.6
  • 41
    • 82955163228 scopus 로고    scopus 로고
    • Intact protein separation by chromatographic and/or electrophoretic techniques for top-down proteomics
    • Capriotti A.L., Cavaliere C., Foglia P., Samperi R., Lagana A. Intact protein separation by chromatographic and/or electrophoretic techniques for top-down proteomics. J Chromatogr A 2011, 1218:8760-8776.
    • (2011) J Chromatogr A , vol.1218 , pp. 8760-8776
    • Capriotti, A.L.1    Cavaliere, C.2    Foglia, P.3    Samperi, R.4    Lagana, A.5
  • 42
    • 70449472505 scopus 로고    scopus 로고
    • A robust two-dimensional separation for top-down tandem mass spectrometry of the low-mass proteome
    • Lee J.E., Kellie J.F., Tran J.C., Tipton J.D., Catherman A.D., Thomas H.M., et al. A robust two-dimensional separation for top-down tandem mass spectrometry of the low-mass proteome. J Am Soc Mass Spectrom 2009, 20:2183-2191.
    • (2009) J Am Soc Mass Spectrom , vol.20 , pp. 2183-2191
    • Lee, J.E.1    Kellie, J.F.2    Tran, J.C.3    Tipton, J.D.4    Catherman, A.D.5    Thomas, H.M.6
  • 45
    • 45549099717 scopus 로고    scopus 로고
    • Rapid and effective focusing in a carrier ampholyte solution isoelectric focusing system: a proteome prefractionation tool
    • Tran J.C., Doucette A.A. Rapid and effective focusing in a carrier ampholyte solution isoelectric focusing system: a proteome prefractionation tool. J Proteome Res 2008, 7:1761-1766.
    • (2008) J Proteome Res , vol.7 , pp. 1761-1766
    • Tran, J.C.1    Doucette, A.A.2
  • 46
    • 41149161152 scopus 로고    scopus 로고
    • Gel-eluted liquid fraction entrapment electrophoresis: an electrophoretic method for broad molecular weight range proteome separation
    • Tran J.C., Doucette A.A. Gel-eluted liquid fraction entrapment electrophoresis: an electrophoretic method for broad molecular weight range proteome separation. Anal Chem 2008, 80:1568-1573.
    • (2008) Anal Chem , vol.80 , pp. 1568-1573
    • Tran, J.C.1    Doucette, A.A.2
  • 47
    • 76849109997 scopus 로고    scopus 로고
    • Size-sorting combined with improved nanocapillary liquid chromatography-mass spectrometry for identification of intact proteins up to 80 kDa
    • Vellaichamy A., Tran J.C., Catherman A.D., Lee J.E., Kellie J.F., Sweet S.M., et al. Size-sorting combined with improved nanocapillary liquid chromatography-mass spectrometry for identification of intact proteins up to 80 kDa. Anal Chem 2010, 82:1234-1244.
    • (2010) Anal Chem , vol.82 , pp. 1234-1244
    • Vellaichamy, A.1    Tran, J.C.2    Catherman, A.D.3    Lee, J.E.4    Kellie, J.F.5    Sweet, S.M.6
  • 49
    • 0034582319 scopus 로고    scopus 로고
    • Automated reduction and interpretation of high resolution electrospray mass spectra of large molecules
    • Horn D.M., Zubarev R.A., McLafferty F.W. Automated reduction and interpretation of high resolution electrospray mass spectra of large molecules. J Am Soc Mass Spectrom 2000, 11:320-332.
    • (2000) J Am Soc Mass Spectrom , vol.11 , pp. 320-332
    • Horn, D.M.1    Zubarev, R.A.2    McLafferty, F.W.3
  • 50
    • 11844293425 scopus 로고    scopus 로고
    • Analysis of Amadori compounds by high-performance cation exchange chromatography coupled to tandem mass spectrometry
    • Davidek T., Kraehenbuehl K., Devaud S., Robert F., Blank I. Analysis of Amadori compounds by high-performance cation exchange chromatography coupled to tandem mass spectrometry. Anal Chem 2005, 77:140-147.
    • (2005) Anal Chem , vol.77 , pp. 140-147
    • Davidek, T.1    Kraehenbuehl, K.2    Devaud, S.3    Robert, F.4    Blank, I.5
  • 51
    • 40649121726 scopus 로고    scopus 로고
    • Venomics: unravelling the complexity of animal venoms with mass spectrometry
    • Escoubas P., Quinton L., Nicholson G.M. Venomics: unravelling the complexity of animal venoms with mass spectrometry. J Mass Spectrom 2008, 43:279-295.
    • (2008) J Mass Spectrom , vol.43 , pp. 279-295
    • Escoubas, P.1    Quinton, L.2    Nicholson, G.M.3
  • 52
    • 0033007311 scopus 로고    scopus 로고
    • Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract
    • Roberts P.R., Burney J.D., Black K.W., Zaloga G.P. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion 1999, 60:332-337.
    • (1999) Digestion , vol.60 , pp. 332-337
    • Roberts, P.R.1    Burney, J.D.2    Black, K.W.3    Zaloga, G.P.4
  • 53
    • 21844457685 scopus 로고    scopus 로고
    • Fragmentation pathways of protonated peptides
    • Paizs B., Suhai S. Fragmentation pathways of protonated peptides. Mass Spectrom Rev 2005, 24:508-548.
    • (2005) Mass Spectrom Rev , vol.24 , pp. 508-548
    • Paizs, B.1    Suhai, S.2
  • 54
    • 66849115217 scopus 로고    scopus 로고
    • Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles
    • Morifuji M., Koga J., Kawanaka K., Higuchi M. Branched-chain amino acid-containing dipeptides, identified from whey protein hydrolysates, stimulate glucose uptake rate in L6 myotubes and isolated skeletal muscles. J Nutr Sci Vitaminol (Tokyo) 2009, 55:81-86.
    • (2009) J Nutr Sci Vitaminol (Tokyo) , vol.55 , pp. 81-86
    • Morifuji, M.1    Koga, J.2    Kawanaka, K.3    Higuchi, M.4
  • 57
  • 58
    • 79955417151 scopus 로고    scopus 로고
    • Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides
    • Tran B.Q., Hernandez C., Waridel P., Potts A., Barblan J., Lisacek F., et al. Addressing trypsin bias in large scale (phospho)proteome analysis by size exclusion chromatography and secondary digestion of large post-trypsin peptides. J Proteome Res 2011, 10:800-811.
    • (2011) J Proteome Res , vol.10 , pp. 800-811
    • Tran, B.Q.1    Hernandez, C.2    Waridel, P.3    Potts, A.4    Barblan, J.5    Lisacek, F.6
  • 59
    • 78149408051 scopus 로고    scopus 로고
    • Characterisation of peptide molecular mass distribution in commercial hydrolysates and hydrolysate-based nutritional products
    • Johns P.W., Jacobs W.A., Phillips R.R., McKenna R.J., O'Kane K.A., McEwen J.W. Characterisation of peptide molecular mass distribution in commercial hydrolysates and hydrolysate-based nutritional products. Food Chem 2011, 125:1041-1050.
    • (2011) Food Chem , vol.125 , pp. 1041-1050
    • Johns, P.W.1    Jacobs, W.A.2    Phillips, R.R.3    McKenna, R.J.4    O'Kane, K.A.5    McEwen, J.W.6
  • 60
    • 55249096894 scopus 로고    scopus 로고
    • Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast
    • de Godoy L.M., Olsen J.V., Cox J., Nielsen M.L., Hubner N.C., Frohlich F., et al. Comprehensive mass-spectrometry-based proteome quantification of haploid versus diploid yeast. Nature 2008, 455:1251-1254.
    • (2008) Nature , vol.455 , pp. 1251-1254
    • de Godoy, L.M.1    Olsen, J.V.2    Cox, J.3    Nielsen, M.L.4    Hubner, N.C.5    Frohlich, F.6
  • 61
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 62
    • 33746233271 scopus 로고    scopus 로고
    • The BIOPEP database - a tool for the in silico method of classification of food proteins as the source of peptides with antihypertensive activity
    • Iwaniak A., Dziuba J., Niklewicz M. The BIOPEP database - a tool for the in silico method of classification of food proteins as the source of peptides with antihypertensive activity. Acta Aliment 2005, 34:417-425.
    • (2005) Acta Aliment , vol.34 , pp. 417-425
    • Iwaniak, A.1    Dziuba, J.2    Niklewicz, M.3
  • 63
    • 34548658287 scopus 로고    scopus 로고
    • PepBank-a database of peptides based on sequence text mining and public peptide data sources
    • Shtatland T., Guettler D., Kossodo M., Pivovarov M., Weissleder R. PepBank-a database of peptides based on sequence text mining and public peptide data sources. BMC Bioinformatics 2007, 8:280.
    • (2007) BMC Bioinformatics , vol.8 , pp. 280
    • Shtatland, T.1    Guettler, D.2    Kossodo, M.3    Pivovarov, M.4    Weissleder, R.5
  • 64
    • 70449719005 scopus 로고    scopus 로고
    • Enhancing navigation in biomedical databases by community voting and database-driven text classification
    • Duchrow T., Shtatland T., Guettler D., Pivovarov M., Kramer S., Weissleder R. Enhancing navigation in biomedical databases by community voting and database-driven text classification. BMC Bioinformatics 2009, 10:317.
    • (2009) BMC Bioinformatics , vol.10 , pp. 317
    • Duchrow, T.1    Shtatland, T.2    Guettler, D.3    Pivovarov, M.4    Kramer, S.5    Weissleder, R.6
  • 65
    • 0026195181 scopus 로고
    • EROP-Moscow: specialized data bank for endogenous regulatory oligopeptides
    • Zamyatnin A.A. EROP-Moscow: specialized data bank for endogenous regulatory oligopeptides. Protein Seq Data Anal 1991, 4:49-52.
    • (1991) Protein Seq Data Anal , vol.4 , pp. 49-52
    • Zamyatnin, A.A.1
  • 67
    • 0347755460 scopus 로고    scopus 로고
    • APD: the antimicrobial peptide database
    • Wang Z., Wang G. APD: the antimicrobial peptide database. Nucleic Acids Res 2004, 32:D590-D592.
    • (2004) Nucleic Acids Res , vol.32
    • Wang, Z.1    Wang, G.2
  • 68
    • 45849147682 scopus 로고    scopus 로고
    • Bioactive peptides and proteins from foods: indication for health effects
    • Moller N.P., Scholz-Ahrens K.E., Roos N., Schrezenmeir J. Bioactive peptides and proteins from foods: indication for health effects. Eur J Nutr 2008, 47:171-182.
    • (2008) Eur J Nutr , vol.47 , pp. 171-182
    • Moller, N.P.1    Scholz-Ahrens, K.E.2    Roos, N.3    Schrezenmeir, J.4
  • 69
    • 74049126605 scopus 로고    scopus 로고
    • Analysis of food proteins and peptides by mass spectrometry-based techniques
    • Mamone G., Picariello G., Caira S., Addeo F., Ferranti P. Analysis of food proteins and peptides by mass spectrometry-based techniques. J Chromatogr A 2009, 1216:7130-7142.
    • (2009) J Chromatogr A , vol.1216 , pp. 7130-7142
    • Mamone, G.1    Picariello, G.2    Caira, S.3    Addeo, F.4    Ferranti, P.5
  • 70
    • 33747503962 scopus 로고    scopus 로고
    • Bioactive peptides: production and functionality
    • Korhonen H., Pihlanto A. Bioactive peptides: production and functionality. Int Dairy J 2006, 16:945-960.
    • (2006) Int Dairy J , vol.16 , pp. 945-960
    • Korhonen, H.1    Pihlanto, A.2
  • 71
    • 34248366062 scopus 로고    scopus 로고
    • Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview
    • Hayes M., Ross R.P., Fitzgerald G.F., Stanton C. Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part I: overview. Biotechnol J 2007, 2:426-434.
    • (2007) Biotechnol J , vol.2 , pp. 426-434
    • Hayes, M.1    Ross, R.P.2    Fitzgerald, G.F.3    Stanton, C.4
  • 72
    • 34248585146 scopus 로고    scopus 로고
    • Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part II: bioactive peptide functions
    • Hayes M., Stanton C., Fitzgerald G.F., Ross R.P. Putting microbes to work: dairy fermentation, cell factories and bioactive peptides. Part II: bioactive peptide functions. Biotechnol J 2007, 2:435-449.
    • (2007) Biotechnol J , vol.2 , pp. 435-449
    • Hayes, M.1    Stanton, C.2    Fitzgerald, G.F.3    Ross, R.P.4
  • 73
    • 59849112823 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs
    • Majumder K., Wu J. Angiotensin I converting enzyme inhibitory peptides from simulated in vitro gastrointestinal digestion of cooked eggs. J Agric Food Chem 2009, 57:471-477.
    • (2009) J Agric Food Chem , vol.57 , pp. 471-477
    • Majumder, K.1    Wu, J.2
  • 74
    • 36749057853 scopus 로고    scopus 로고
    • Peptides reproducibly released by in vivo digestion of beef meat and trout flesh in pigs
    • Bauchart C., Morzel M., Chambon C., Mirand P.P., Reynès C., Buffière C., et al. Peptides reproducibly released by in vivo digestion of beef meat and trout flesh in pigs. Br J Nutr 2007, 98:1187-1195.
    • (2007) Br J Nutr , vol.98 , pp. 1187-1195
    • Bauchart, C.1    Morzel, M.2    Chambon, C.3    Mirand, P.P.4    Reynès, C.5    Buffière, C.6
  • 76
    • 50649104560 scopus 로고    scopus 로고
    • Application of mass spectrometry to the characterization and quantification of food-derived bioactive peptides
    • Contreras M.M., Lopez-Exposito I., Hernandez-Ledesma B., Ramos M., Recio I. Application of mass spectrometry to the characterization and quantification of food-derived bioactive peptides. J AOAC Int 2008, 91:981-994.
    • (2008) J AOAC Int , vol.91 , pp. 981-994
    • Contreras, M.M.1    Lopez-Exposito, I.2    Hernandez-Ledesma, B.3    Ramos, M.4    Recio, I.5
  • 80
    • 0037107887 scopus 로고    scopus 로고
    • Structure-based virtual screening: an overview
    • Lyne P.D. Structure-based virtual screening: an overview. Drug Discov Today 2002, 7:1047-1055.
    • (2002) Drug Discov Today , vol.7 , pp. 1047-1055
    • Lyne, P.D.1
  • 84
    • 77951621301 scopus 로고    scopus 로고
    • The genome sequence of taurine cattle: a window to ruminant biology and evolution
    • Elsik C.G., Tellam R.L., Worley K.C., Gibbs R.A., Muzny D.M., Weinstock G.M., et al. The genome sequence of taurine cattle: a window to ruminant biology and evolution. Science 2009, 324:522-528.
    • (2009) Science , vol.324 , pp. 522-528
    • Elsik, C.G.1    Tellam, R.L.2    Worley, K.C.3    Gibbs, R.A.4    Muzny, D.M.5    Weinstock, G.M.6
  • 86
    • 0037195083 scopus 로고    scopus 로고
    • The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract
    • Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., et al. The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract. Proc Natl Acad Sci U S A 2002, 99:14422-14427.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 14422-14427
    • Schell, M.A.1    Karmirantzou, M.2    Snel, B.3    Vilanova, D.4    Berger, B.5    Pessi, G.6
  • 87
    • 27444437848 scopus 로고    scopus 로고
    • Quantitative structure activity relationship modelling of peptides and proteins as a tool in food science
    • Pripp A.H., Isaksson T., Stepaniak L., Sorhaug T., Ardoe Y. Quantitative structure activity relationship modelling of peptides and proteins as a tool in food science. Trends Food Sci Technol 2005, 16:484-494.
    • (2005) Trends Food Sci Technol , vol.16 , pp. 484-494
    • Pripp, A.H.1    Isaksson, T.2    Stepaniak, L.3    Sorhaug, T.4    Ardoe, Y.5
  • 88
    • 0037467117 scopus 로고    scopus 로고
    • Homology similarity analysis of sequences of lactoferricin and its derivatives
    • Nakai S., Chan J.C., Li-Chan E.C., Dou J., Ogawa M. Homology similarity analysis of sequences of lactoferricin and its derivatives. J Agric Food Chem 2003, 51:1215-1223.
    • (2003) J Agric Food Chem , vol.51 , pp. 1215-1223
    • Nakai, S.1    Chan, J.C.2    Li-Chan, E.C.3    Dou, J.4    Ogawa, M.5
  • 89
    • 10444265979 scopus 로고    scopus 로고
    • Quantitative structure-activity relationship modelling of ACE-inhibitory peptides derived from milk proteins
    • Pripp A.H., Isaksson T., Stepaniak L., Sorhaug T. Quantitative structure-activity relationship modelling of ACE-inhibitory peptides derived from milk proteins. Eur Food Res Technol 2004, 219:579-583.
    • (2004) Eur Food Res Technol , vol.219 , pp. 579-583
    • Pripp, A.H.1    Isaksson, T.2    Stepaniak, L.3    Sorhaug, T.4
  • 90
    • 0023428914 scopus 로고
    • Quantitative structure-activity relationships of the bitter thresholds of amino acids, peptides, and their derivatives
    • Asao M., Iwamura H., Akamatsu M., Fujita T. Quantitative structure-activity relationships of the bitter thresholds of amino acids, peptides, and their derivatives. J Med Chem 1987, 30:1873-1879.
    • (1987) J Med Chem , vol.30 , pp. 1873-1879
    • Asao, M.1    Iwamura, H.2    Akamatsu, M.3    Fujita, T.4
  • 92
    • 50649101652 scopus 로고    scopus 로고
    • BIOPEP database and other programs for processing bioactive peptide sequences
    • Minkiewicz P., Dziuba J., Iwaniak A., Dziuba M., Darewicz M. BIOPEP database and other programs for processing bioactive peptide sequences. J AOAC Int 2008, 91:965-980.
    • (2008) J AOAC Int , vol.91 , pp. 965-980
    • Minkiewicz, P.1    Dziuba, J.2    Iwaniak, A.3    Dziuba, M.4    Darewicz, M.5
  • 93
    • 0022340599 scopus 로고
    • Demonstration of beta-casomorphin immunoreactive materials in in vitro digests of bovine milk and in small intestine contents after bovine milk ingestion in adult humans
    • Svedberg J., de H.J., Leimenstoll G., Paul F., Teschemacher H. Demonstration of beta-casomorphin immunoreactive materials in in vitro digests of bovine milk and in small intestine contents after bovine milk ingestion in adult humans. Peptides 1985, 6:825-830.
    • (1985) Peptides , vol.6 , pp. 825-830
    • Svedberg, J.1    de, H.J.2    Leimenstoll, G.3    Paul, F.4    Teschemacher, H.5
  • 94
    • 0031716772 scopus 로고    scopus 로고
    • Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry
    • Kuwata H., Yip T.T., Yip C.L., Tomita M., Hutchens T.W. Direct detection and quantitative determination of bovine lactoferricin and lactoferrin fragments in human gastric contents by affinity mass spectrometry. Adv Exp Med Biol 1998, 443:23-32.
    • (1998) Adv Exp Med Biol , vol.443 , pp. 23-32
    • Kuwata, H.1    Yip, T.T.2    Yip, C.L.3    Tomita, M.4    Hutchens, T.W.5
  • 95
    • 50649107220 scopus 로고    scopus 로고
    • Identification of food-derived bioactive peptides in blood and other biological samples
    • Sato K., Iwai K., Aito-Inoue M. Identification of food-derived bioactive peptides in blood and other biological samples. J AOAC Int 2008, 91:995-1001.
    • (2008) J AOAC Int , vol.91 , pp. 995-1001
    • Sato, K.1    Iwai, K.2    Aito-Inoue, M.3
  • 96
    • 0028657017 scopus 로고
    • Enzymatic barriers for GI peptide and protein delivery
    • Woodley J.F. Enzymatic barriers for GI peptide and protein delivery. Crit Rev Ther Drug Carrier Syst 1994, 11:61-95.
    • (1994) Crit Rev Ther Drug Carrier Syst , vol.11 , pp. 61-95
    • Woodley, J.F.1
  • 97
    • 0029044529 scopus 로고
    • Proline motifs in peptides and their biological processing
    • Vanhoof G., Goossens F., De M.I., Hendriks D., Scharpe S. Proline motifs in peptides and their biological processing. FASEB J 1995, 9:736-744.
    • (1995) FASEB J , vol.9 , pp. 736-744
    • Vanhoof, G.1    Goossens, F.2    De, M.I.3    Hendriks, D.4    Scharpe, S.5
  • 98
    • 0025482614 scopus 로고
    • Intestinal absorption of protein hydrolysis products: a review
    • Webb K.E. Intestinal absorption of protein hydrolysis products: a review. J Anim Sci 1990, 68:3011-3022.
    • (1990) J Anim Sci , vol.68 , pp. 3011-3022
    • Webb, K.E.1
  • 99
    • 61449455434 scopus 로고    scopus 로고
    • Review. The mammalian proton-coupled peptide cotransporter PepT1: sitting on the transporter-channel fence?
    • Meredith D. Review. The mammalian proton-coupled peptide cotransporter PepT1: sitting on the transporter-channel fence?. Philos Trans R Soc Lond B Biol Sci 2009, 364:203-207.
    • (2009) Philos Trans R Soc Lond B Biol Sci , vol.364 , pp. 203-207
    • Meredith, D.1
  • 100
    • 0034657529 scopus 로고    scopus 로고
    • Intestinal absorption of peptides through the enterocytes
    • Ziv E., Bendayan M. Intestinal absorption of peptides through the enterocytes. Microsc Res Tech 2000, 49:346-352.
    • (2000) Microsc Res Tech , vol.49 , pp. 346-352
    • Ziv, E.1    Bendayan, M.2
  • 102
    • 0022000677 scopus 로고
    • Absorption of protein and protein fragments in the developing intestine: role in immunologic/allergic reactions
    • Walker W.A. Absorption of protein and protein fragments in the developing intestine: role in immunologic/allergic reactions. Pediatrics 1985, 75:167-171.
    • (1985) Pediatrics , vol.75 , pp. 167-171
    • Walker, W.A.1
  • 103
    • 0035491061 scopus 로고    scopus 로고
    • Soluble CD14 in human breast milk and its role in innate immune responses
    • Vidal K., Labeta M.O., Schiffrin E.J., Donnet-Hughes A. Soluble CD14 in human breast milk and its role in innate immune responses. Acta Odontol Scand 2001, 59:330-334.
    • (2001) Acta Odontol Scand , vol.59 , pp. 330-334
    • Vidal, K.1    Labeta, M.O.2    Schiffrin, E.J.3    Donnet-Hughes, A.4
  • 104
    • 0033953592 scopus 로고    scopus 로고
    • Bioactive molecules in milk and their role in health and disease: the role of transforming growth factor-beta
    • Donnet-Hughes A., Duc N., Serrant P., Vidal K., Schiffrin E.J. Bioactive molecules in milk and their role in health and disease: the role of transforming growth factor-beta. Immunol Cell Biol 2000, 78:74-79.
    • (2000) Immunol Cell Biol , vol.78 , pp. 74-79
    • Donnet-Hughes, A.1    Duc, N.2    Serrant, P.3    Vidal, K.4    Schiffrin, E.J.5
  • 105
    • 6944221879 scopus 로고    scopus 로고
    • Bioavailability of angiotensin I converting enzyme inhibitory peptides
    • Vermeirssen V., Van C.J., Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. Br J Nutr 2004, 92:357-366.
    • (2004) Br J Nutr , vol.92 , pp. 357-366
    • Vermeirssen, V.1    Van, C.J.2    Verstraete, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.