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Volumn , Issue , 2013, Pages 3-19

Understanding the proteome

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EID: 84927575402     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-4614-5626-1_1     Document Type: Chapter
Times cited : (11)

References (56)
  • 4
    • 66749092934 scopus 로고    scopus 로고
    • Systematic LC-MS analysis of labile post-translational modifications in complex mixtures
    • Carapito C, Klemm C, Aebersold R, Domon B (2009) Systematic LC-MS analysis of labile post-translational modifications in complex mixtures. J Proteome Res 8:2608-2614
    • (2009) J Proteome Res , vol.8 , pp. 2608-2614
    • Carapito, C.1    Klemm, C.2    Aebersold, R.3    Domon, B.4
  • 6
    • 77952314934 scopus 로고    scopus 로고
    • Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach
    • Chiou SH, Huang CH, Lee IL, Wang YT, Liu NY, Tsay YG, Chen YJ (2010) Identification of in vivo phosphorylation sites of lens proteins from porcine eye lenses by a gel-free phosphoproteomics approach. Mol Vis 16:294-302
    • (2010) Mol Vis , vol.16 , pp. 294-302
    • Chiou, S.H.1    Huang, C.H.2    Lee, I.L.3    Wang, Y.T.4    Liu, N.Y.5    Tsay, Y.G.6    Chen, Y.J.7
  • 7
    • 80054753537 scopus 로고    scopus 로고
    • Review: applications of mass spectrometry techniques in the investigation of milk proteome
    • Cunsolo V, Muccilli V, Saletti R, Foti S (2011) Review: applications of mass spectrometry techniques in the investigation of milk proteome. Eur J Mass Spectrom (Chichester, Eng) 17:305-320
    • (2011) Eur J Mass Spectrom (Chichester, Eng) , vol.17 , pp. 305-320
    • Cunsolo, V.1    Muccilli, V.2    Saletti, R.3    Foti, S.4
  • 8
    • 84855553803 scopus 로고    scopus 로고
    • We are what we eat: food safety and proteomics
    • D'Alessandro A, Zolla L (2012) We are what we eat: food safety and proteomics. J Proteome Res 11:26-36
    • (2012) J Proteome Res , vol.11 , pp. 26-36
    • D'Alessandro, A.1    Zolla, L.2
  • 9
    • 52649147543 scopus 로고    scopus 로고
    • A proteomic characterization of water buffalo milk fractions describing PTM of major species and the identification of minor components involved in nutrient delivery and defense against pathogens
    • D'Ambrosio C, Arena S, Salzano AM, Renzone G, Ledda L, Scaloni A (2008) A proteomic characterization of water buffalo milk fractions describing PTM of major species and the identification of minor components involved in nutrient delivery and defense against pathogens. Proteomics 8:3657-3666
    • (2008) Proteomics , vol.8 , pp. 3657-3666
    • D'Ambrosio, C.1    Arena, S.2    Salzano, A.M.3    Renzone, G.4    Ledda, L.5    Scaloni, A.6
  • 10
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R (2006) Mass spectrometry and protein analysis. Science 312:212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 12
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel lecture)
    • Fenn JB (2003) Electrospray wings for molecular elephants (Nobel lecture). Angew Chem Int Ed Engl 42:3871-3894
    • (2003) Angew Chem Int Ed Engl , vol.42 , pp. 3871-3894
    • Fenn, J.B.1
  • 13
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 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
  • 14
    • 0030873812 scopus 로고    scopus 로고
    • Differential splicing of pre-messenger RNA produces multiple forms of mature caprine alpha(s1)-casein
    • Ferranti P, Addeo F, Malorni A, Chianese L, Leroux C, Martin P (1997) Differential splicing of pre-messenger RNA produces multiple forms of mature caprine alpha(s1)-casein. Eur J Biochem 249:1-7
    • (1997) Eur J Biochem , vol.249 , pp. 1-7
    • Ferranti, P.1    Addeo, F.2    Malorni, A.3    Chianese, L.4    Leroux, C.5    Martin, P.6
  • 15
    • 84861860481 scopus 로고    scopus 로고
    • Targeted data extraction of the MS/MS spectra generated by data independent acquisition: a new concept for consistent and accurate proteome analysis
    • Gillet LC, Navarro P, Tate S, Roest H, Selevsek N, Reiter L, Bonner R, Aebersold R (2012) Targeted data extraction of the MS/MS spectra generated by data independent acquisition: a new concept for consistent and accurate proteome analysis. Mol Cell Proteomics 6:1-17
    • (2012) Mol Cell Proteomics , vol.6 , pp. 1-17
    • Gillet, L.C.1    Navarro, P.2    Tate, S.3    Roest, H.4    Selevsek, N.5    Reiter, L.6    Bonner, R.7    Aebersold, R.8
  • 18
    • 2142856295 scopus 로고    scopus 로고
    • Proteome profiling-pitfalls and progress
    • Haynes PA, Yates JR (2000) Proteome profiling-pitfalls and progress. Yeast 17:81-87
    • (2000) Yeast , vol.17 , pp. 81-87
    • Haynes, P.A.1    Yates, J.R.2
  • 19
    • 78649434468 scopus 로고    scopus 로고
    • Development of a new method using HILIC-tandem mass spectrometry for the characterization of O-sialoglycopeptides from proteolytically digested caseinomacropeptide
    • Hernandez-Hernandez O, Lebron-Aguilar R, Quintanilla-Lopez JE, Sanz ML, Moreno FJ (2010) Development of a new method using HILIC-tandem mass spectrometry for the characterization of O-sialoglycopeptides from proteolytically digested caseinomacropeptide. Proteomics 10:3699-3711
    • (2010) Proteomics , vol.10 , pp. 3699-3711
    • Hernandez-Hernandez, O.1    Lebron-Aguilar, R.2    Quintanilla-Lopez, J.E.3    Sanz, M.L.4    Moreno, F.J.5
  • 20
    • 84875463071 scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers
    • Hillenkamp F, Karas M, Beavis RC, Chait BT (1991) Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers. Anal Chem 63:1193A-1203A
    • (1991) Anal Chem , vol.63 , pp. 1193A-1203A
    • Hillenkamp, F.1    Karas, M.2    Beavis, R.C.3    Chait, B.T.4
  • 21
    • 80053996537 scopus 로고    scopus 로고
    • Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences
    • Huang H, Larsen MR, Karlsson AH, Pomponio L, Costa LN, Lametsch R (2011) Gel-based phosphoproteomics analysis of sarcoplasmic proteins in postmortem porcine muscle with pH decline rate and time differences. Proteomics 11:4063-4076
    • (2011) Proteomics , vol.11 , pp. 4063-4076
    • Huang, H.1    Larsen, M.R.2    Karlsson, A.H.3    Pomponio, L.4    Costa, L.N.5    Lametsch, R.6
  • 22
    • 70549113220 scopus 로고    scopus 로고
    • Perspectives of targeted mass spectrometry for protein biomarker verification
    • Huttenhain R, Malmstrom J, Picotti P, Aebersold R (2009) Perspectives of targeted mass spectrometry for protein biomarker verification. Curr Opin Chem Biol 13:518-525
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 518-525
    • Huttenhain, R.1    Malmstrom, J.2    Picotti, P.3    Aebersold, R.4
  • 23
    • 84857913661 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of bacterial enzymes released in cheese during ripening
    • Jardin J, Molle D, Piot M, Lortal S, Gagnaire V (2012) Quantitative proteomic analysis of bacterial enzymes released in cheese during ripening. Int J Food Microbiol 155:19-28
    • (2012) Int J Food Microbiol , vol.155 , pp. 19-28
    • Jardin, J.1    Molle, D.2    Piot, M.3    Lortal, S.4    Gagnaire, V.5
  • 24
    • 0032253972 scopus 로고    scopus 로고
    • Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: strategies and applications
    • Jensen ON, Larsen MR, Roepstorff P (1998) Mass spectrometric identification and microcharacterization of proteins from electrophoretic gels: strategies and applications. Proteins 2:74-89
    • (1998) Proteins , vol.2 , pp. 74-89
    • Jensen, O.N.1    Larsen, M.R.2    Roepstorff, P.3
  • 25
    • 0034875816 scopus 로고    scopus 로고
    • Improvement of in-gel digestion protocol for peptide mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry
    • Katayama H, Nagasu T, Oda Y (2001) Improvement of in-gel digestion protocol for peptide mass fingerprinting by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 15:1416-1421
    • (2001) Rapid Commun Mass Spectrom , vol.15 , pp. 1416-1421
    • Katayama, H.1    Nagasu, T.2    Oda, Y.3
  • 26
    • 84910679144 scopus 로고    scopus 로고
    • Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database
    • srep00090
    • Khoury GA, Baliban RC, Floudas CA (2011) Proteome-wide post-translational modification statistics: frequency analysis and curation of the swiss-prot database. Sci Rep 1:srep00090
    • (2011) Sci Rep , vol.1
    • Khoury, G.A.1    Baliban, R.C.2    Floudas, C.A.3
  • 27
    • 67349207877 scopus 로고    scopus 로고
    • The effect of glycosylation on the interfacial properties of bovine caseinomacropeptide
    • Kreuss M, Strixner T, Kulozik U (2009) The effect of glycosylation on the interfacial properties of bovine caseinomacropeptide. Food Hydrocoll 23:1818-1826
    • (2009) Food Hydrocoll , vol.23 , pp. 1818-1826
    • Kreuss, M.1    Strixner, T.2    Kulozik, U.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 24944519450 scopus 로고    scopus 로고
    • Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns
    • Larsen MR, Thingholm TE, Jensen ON, Roepstorff P, Jorgensen TJ (2005) Highly selective enrichment of phosphorylated peptides from peptide mixtures using titanium dioxide microcolumns. Mol Cell Proteomics 4:873-886
    • (2005) Mol Cell Proteomics , vol.4 , pp. 873-886
    • Larsen, M.R.1    Thingholm, T.E.2    Jensen, O.N.3    Roepstorff, P.4    Jorgensen, T.J.5
  • 32
    • 33746570234 scopus 로고    scopus 로고
    • Analysis of posttranslational modifications of proteins by tandem mass spectrometry
    • Larsen MR, Trelle MB, Thingholm TE, Jensen ON (2006) Analysis of posttranslational modifications of proteins by tandem mass spectrometry. Biotechniques 40:790-798
    • (2006) Biotechniques , vol.40 , pp. 790-798
    • Larsen, M.R.1    Trelle, M.B.2    Thingholm, T.E.3    Jensen, O.N.4
  • 33
    • 13944255538 scopus 로고    scopus 로고
    • Protein composition, plasmin activity and cheesemaking properties of cows' milk produced at two altitudes from hay of lowland and high-alpine origins
    • Leiber F, Nigg D, Kunz C, Scheeder MRL, Wettstein HR, Kreuzer M (2005) Protein composition, plasmin activity and cheesemaking properties of cows' milk produced at two altitudes from hay of lowland and high-alpine origins. J Dairy Res 72:65-74
    • (2005) J Dairy Res , vol.72 , pp. 65-74
    • Leiber, F.1    Nigg, D.2    Kunz, C.3    Scheeder, M.R.L.4    Wettstein, H.R.5    Kreuzer, M.6
  • 34
    • 34548522775 scopus 로고    scopus 로고
    • Advances in proteomic workflows for systems biology
    • Malmstrom J, Lee H, Aebersold R (2007) Advances in proteomic workflows for systems biology. Curr Opin Biotechnol 18:378-384
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 378-384
    • Malmstrom, J.1    Lee, H.2    Aebersold, R.3
  • 35
    • 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 (2009) Analysis of food proteins and peptides by mass spectrometry-based techniques. J Chromatogr A 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
  • 36
    • 79960258556 scopus 로고    scopus 로고
    • 100 % protein sequence coverage: a modern form of surrealism in proteomics
    • Meyer B, Papasotiriou DG, Karas M (2011) 100 % protein sequence coverage: a modern form of surrealism in proteomics. Amino Acids 41:291-310
    • (2011) Amino Acids , vol.41 , pp. 291-310
    • Meyer, B.1    Papasotiriou, D.G.2    Karas, M.3
  • 37
    • 81255128917 scopus 로고    scopus 로고
    • High molecular weight glutenin subunits in some durum wheat cultivars investigated by means of mass spectrometric techniques
    • Muccilli V, Lo BM, Cunsolo V, Saletti R, Gallo G, Foti S (2011) High molecular weight glutenin subunits in some durum wheat cultivars investigated by means of mass spectrometric techniques. J Agric Food Chem 59:12226-12237
    • (2011) J Agric Food Chem , vol.59 , pp. 12226-12237
    • Muccilli, V.1    Lo, B.M.2    Cunsolo, V.3    Saletti, R.4    Gallo, G.5    Foti, S.6
  • 38
    • 84855549488 scopus 로고    scopus 로고
    • System-wide Perturbation Analysis with Nearly Complete Coverage of the Yeast Proteome by Single-shot Ultra HPLC Runs on a Bench Top Orbitrap
    • Nagaraj N, Alexander KN, Cox J, Neuhauser N, Mayr K, Hoerning O, Vorm O, Mann M (2012) System-wide Perturbation Analysis with Nearly Complete Coverage of the Yeast Proteome by Single-shot Ultra HPLC Runs on a Bench Top Orbitrap. Mol Cell Proteomics 11:M111
    • (2012) Mol Cell Proteomics , vol.11 , pp. M111
    • Nagaraj, N.1    Alexander, K.N.2    Cox, J.3    Neuhauser, N.4    Mayr, K.5    Hoerning, O.6    Vorm, O.7    Mann, M.8
  • 39
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii AI, Keller A, Kolker E, Aebersold R (2003) A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 75:4646-4658
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 42
    • 84862189137 scopus 로고    scopus 로고
    • Mass spectrometry for nutritional peptidomics: how to analyze food bioactives and their health effects
    • Panchaud A, Affolter M, Kussmann M (2012) Mass spectrometry for nutritional peptidomics: how to analyze food bioactives and their health effects. J Proteomics 12:3546-3559
    • (2012) J Proteomics , vol.12 , pp. 3546-3559
    • Panchaud, A.1    Affolter, M.2    Kussmann, M.3
  • 44
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti P, Bodenmiller B, Mueller LN, Domon B, Aebersold R (2009) Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138:795-806
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5
  • 46
    • 77957326091 scopus 로고    scopus 로고
    • Quantitative analysis of protein complex constituents and their phosphorylation states on a LTQ-Orbitrap instrument
    • Przybylski C, Junger MA, Aubertin J, Radvanyi F, Aebersold R, Pflieger D (2010) Quantitative analysis of protein complex constituents and their phosphorylation states on a LTQ-Orbitrap instrument. J Proteome Res 9:5118-5132
    • (2010) J Proteome Res , vol.9 , pp. 5118-5132
    • Przybylski, C.1    Junger, M.A.2    Aubertin, J.3    Radvanyi, F.4    Aebersold, R.5    Pflieger, D.6
  • 47
    • 79957452008 scopus 로고    scopus 로고
    • Advances in research on the prenatal development of skeletal muscle in animals in relation to the quality of muscle-based food. II-genetic factors related to animal performance and advances in methodology
    • Rehfeldt C, Te Pas MF, Wimmers K, Brameld JM, Nissen PM, Berri C, Valente LM, Power DM, Picard B, Stickland NC, Oksbjerg N (2011) Advances in research on the prenatal development of skeletal muscle in animals in relation to the quality of muscle-based food. II-genetic factors related to animal performance and advances in methodology. Animal 5:718-730
    • (2011) Animal , vol.5 , pp. 718-730
    • Rehfeldt, C.1    Te Pas, M.F.2    Wimmers, K.3    Brameld, J.M.4    Nissen, P.M.5    Berri, C.6    Valente, L.M.7    Power, D.M.8    Picard, B.9    Stickland, N.C.10    Oksbjerg, N.11
  • 48
    • 38249006079 scopus 로고
    • Effect of kappa-casein glycosylation on cheese yielding capacity and coagulating properties of milk
    • Robitaille G, Ngkwaihang KF, Monardes HG (1993) Effect of kappa-casein glycosylation on cheese yielding capacity and coagulating properties of milk. Food Res Int 26:365-369
    • (1993) Food Res Int , vol.26 , pp. 365-369
    • Robitaille, G.1    Ngkwaihang, K.F.2    Monardes, H.G.3
  • 49
    • 80054881621 scopus 로고    scopus 로고
    • Nutriproteomics: technologies and applications for identification and quantification of biomarkers and ingredients
    • Senechal S, Kussmann M (2011) Nutriproteomics: technologies and applications for identification and quantification of biomarkers and ingredients. Proc Nutr Soc 70:351-364
    • (2011) Proc Nutr Soc , vol.70 , pp. 351-364
    • Senechal, S.1    Kussmann, M.2
  • 50
    • 79960472212 scopus 로고    scopus 로고
    • Peptide biomarkers as a way to determine meat authenticity
    • Sentandreu MA, Sentandreu E (2011) Peptide biomarkers as a way to determine meat authenticity. Meat Sci 89:280-285
    • (2011) Meat Sci , vol.89 , pp. 280-285
    • Sentandreu, M.A.1    Sentandreu, E.2
  • 51
    • 0036019907 scopus 로고    scopus 로고
    • Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds
    • Spiro RG (2002) Protein glycosylation: nature, distribution, enzymatic formation, and disease implications of glycopeptide bonds. Glycobiology 12:43R-456R
    • (2002) Glycobiology , vol.12 , pp. 43R-456R
    • Spiro, R.G.1
  • 52
    • 27844516621 scopus 로고    scopus 로고
    • Therapeutic potentials of bovine colostrums
    • Thapa BR (2005) Therapeutic potentials of bovine colostrums. Indian J Pediatr 72:849-852
    • (2005) Indian J Pediatr , vol.72 , pp. 849-852
    • Thapa, B.R.1
  • 54
    • 83455210605 scopus 로고    scopus 로고
    • Molecular and functional characterization of glycogen synthase in the porcine satellite cells under insulin treatment
    • Wang L, Xiong Y, Zuo B, Lei M, Ren Z, Xu D (2012) Molecular and functional characterization of glycogen synthase in the porcine satellite cells under insulin treatment. Mol Cell Biochem 360:169-180
    • (2012) Mol Cell Biochem , vol.360 , pp. 169-180
    • Wang, L.1    Xiong, Y.2    Zuo, B.3    Lei, M.4    Ren, Z.5    Xu, D.6
  • 55
    • 76649109590 scopus 로고    scopus 로고
    • An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers
    • Whiteaker JR, Zhao L, Anderson L, Paulovich AG (2010) An automated and multiplexed method for high throughput peptide immunoaffinity enrichment and multiple reaction monitoring mass spectrometry-based quantification of protein biomarkers. Mol Cell Proteomics 9:184-196
    • (2010) Mol Cell Proteomics , vol.9 , pp. 184-196
    • Whiteaker, J.R.1    Zhao, L.2    Anderson, L.3    Paulovich, A.G.4


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