메뉴 건너뛰기




Volumn 93, Issue 2, 2010, Pages 593-603

Proteomic analysis of the temporal expression of bovine milk proteins during coliform mastitis and label-free relative quantification

Author keywords

Bovine milk proteome; Coliform mastitis; Label free quantification; Liquid chromatography tandem mass spectrometry

Indexed keywords

MILK PROTEIN;

EID: 77949288153     PISSN: 00220302     EISSN: 15253198     Source Type: Journal    
DOI: 10.3168/jds.2009-2526     Document Type: Article
Times cited : (52)

References (34)
  • 1
    • 65449184912 scopus 로고    scopus 로고
    • Pathogen-dependent induction of cytokines and other soluble inflammatory mediators during intramammary infection of dairy cows
    • Bannerman D.D. Pathogen-dependent induction of cytokines and other soluble inflammatory mediators during intramammary infection of dairy cows. J. Anim. Sci. 2009, 87:10-25.
    • (2009) J. Anim. Sci. , vol.87 , pp. 10-25
    • Bannerman, D.D.1
  • 2
    • 0642281205 scopus 로고    scopus 로고
    • Increased levels of LPS-binding protein in bovine blood and milk following bacterial lipopolysaccharide challenge
    • Bannerman D.D., Paape M.J., Hare W.R., Sohn E.J. Increased levels of LPS-binding protein in bovine blood and milk following bacterial lipopolysaccharide challenge. J. Dairy Sci. 2003, 86:3128-3137.
    • (2003) J. Dairy Sci. , vol.86 , pp. 3128-3137
    • Bannerman, D.D.1    Paape, M.J.2    Hare, W.R.3    Sohn, E.J.4
  • 3
    • 2442675425 scopus 로고    scopus 로고
    • Escherichia coli and Staphylococcus aureus elicit differential innate immune responses following intramammary infection
    • Bannerman D.D., Paape M.J., Lee J.-W., Zhao X., Hope J.C., Rainard P. Escherichia coli and Staphylococcus aureus elicit differential innate immune responses following intramammary infection. Clin. Diagn. Lab. Immunol. 2004, 11:463-472.
    • (2004) Clin. Diagn. Lab. Immunol. , vol.11 , pp. 463-472
    • Bannerman, D.D.1    Paape, M.J.2    Lee, J.-W.3    Zhao, X.4    Hope, J.C.5    Rainard, P.6
  • 4
    • 55849093290 scopus 로고    scopus 로고
    • Proteomic analysis of differentially expressed proteins in bovine milk during experimentally induced Escherichia coli mastitis
    • Boehmer J.L., Bannerman D.D., Shefcheck K.J., Ward J.L. Proteomic analysis of differentially expressed proteins in bovine milk during experimentally induced Escherichia coli mastitis. J. Dairy Sci. 2008, 91:4206-4218.
    • (2008) J. Dairy Sci. , vol.91 , pp. 4206-4218
    • Boehmer, J.L.1    Bannerman, D.D.2    Shefcheck, K.J.3    Ward, J.L.4
  • 5
    • 0037106398 scopus 로고    scopus 로고
    • Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry
    • Bondarenko P.V., Chelius D., Shaler T.A. Identification and relative quantitation of protein mixtures by enzymatic digestion followed by capillary reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Chem. 2002, 74:4741-4749.
    • (2002) Anal. Chem. , vol.74 , pp. 4741-4749
    • Bondarenko, P.V.1    Chelius, D.2    Shaler, T.A.3
  • 6
    • 0348048803 scopus 로고    scopus 로고
    • Peptidoglycan recognition proteins (PGRPs)
    • Dziarski R. Peptidoglycan recognition proteins (PGRPs). Mol. Immunol. 2003, 40:877-886.
    • (2003) Mol. Immunol. , vol.40 , pp. 877-886
    • Dziarski, R.1
  • 7
    • 36248998834 scopus 로고    scopus 로고
    • Fractionation of bovine whey proteins and characterization by proteomic techniques
    • Fong B.Y., Norris S.C., Palmano K.P. Fractionation of bovine whey proteins and characterization by proteomic techniques. Int. Dairy J. 2008, 18:23-46.
    • (2008) Int. Dairy J. , vol.18 , pp. 23-46
    • Fong, B.Y.1    Norris, S.C.2    Palmano, K.P.3
  • 8
    • 61449163906 scopus 로고    scopus 로고
    • Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances
    • Gagnaire V., Jardin J., Jan G., Lortal S. Invited review: Proteomics of milk and bacteria used in fermented dairy products: From qualitative to quantitative advances. J. Dairy Sci. 2009, 92:811-825.
    • (2009) J. Dairy Sci. , vol.92 , pp. 811-825
    • Gagnaire, V.1    Jardin, J.2    Jan, G.3    Lortal, S.4
  • 10
  • 11
    • 3042854907 scopus 로고    scopus 로고
    • Differential protein composition of bovine whey: A comparison of whey from healthy animals and from those with clinical mastitis
    • Hogarth C.J., Fitzpatrick J.L., Nolan A.M., Young F.J., Pitt A., Eckersall P.D. Differential protein composition of bovine whey: A comparison of whey from healthy animals and from those with clinical mastitis. Proteomics 2004, 4:2094-2100.
    • (2004) Proteomics , vol.4 , pp. 2094-2100
    • Hogarth, C.J.1    Fitzpatrick, J.L.2    Nolan, A.M.3    Young, F.J.4    Pitt, A.5    Eckersall, P.D.6
  • 14
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu H., Sadygov R.G., Yates J.R. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 2004, 76:4193-4201.
    • (2004) Anal. Chem. , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates, J.R.3
  • 15
    • 27744461612 scopus 로고    scopus 로고
    • Cytokine response of bovine mammary gland epithelial cells to Escherichia coli, coliform culture filtrate, or lipopolysaccharide
    • McClenahan D.J., Sotos J.P., Czuprynski C.J. Cytokine response of bovine mammary gland epithelial cells to Escherichia coli, coliform culture filtrate, or lipopolysaccharide. Am. J. Vet. Res. 2005, 66:1590-1596.
    • (2005) Am. J. Vet. Res. , vol.66 , pp. 1590-1596
    • McClenahan, D.J.1    Sotos, J.P.2    Czuprynski, C.J.3
  • 16
    • 57049151865 scopus 로고    scopus 로고
    • Proteomics analysis identifies phosphorylation-dependent α-synuclein protein interactions
    • McFarland M.A., Ellis C.E., Markey S.P., Nussbaum R.L. Proteomics analysis identifies phosphorylation-dependent α-synuclein protein interactions. Mol. Cell Proteomics 2008, 7:2123-2137.
    • (2008) Mol. Cell Proteomics , vol.7 , pp. 2123-2137
    • McFarland, M.A.1    Ellis, C.E.2    Markey, S.P.3    Nussbaum, R.L.4
  • 17
    • 60649087511 scopus 로고    scopus 로고
    • A label free quantitative proteomic analysis of the Saccharomyces cerevisiae nucleus
    • Mosley A.L., Florens L., Wen Z., Washburn M.P. A label free quantitative proteomic analysis of the Saccharomyces cerevisiae nucleus. J. Proteomics 2009, 72:110-120.
    • (2009) J. Proteomics , vol.72 , pp. 110-120
    • Mosley, A.L.1    Florens, L.2    Wen, Z.3    Washburn, M.P.4
  • 18
    • 38649095599 scopus 로고    scopus 로고
    • An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data
    • Mueller L.N., Brusniak M.-Y., Mani D.R., Aebersold R. An assessment of software solutions for the analysis of mass spectrometry based quantitative proteomics data. J. Proteome Res. 2008, 7:51-61.
    • (2008) J. Proteome Res. , vol.7 , pp. 51-61
    • Mueller, L.N.1    Brusniak, M.-Y.2    Mani, D.R.3    Aebersold, R.4
  • 23
    • 33750362923 scopus 로고    scopus 로고
    • Bovine milk fat globule membrane proteome
    • Reinhardt T.A., Lippolis J.D. Bovine milk fat globule membrane proteome. J. Dairy Res. 2006, 73:406-416.
    • (2006) J. Dairy Res. , vol.73 , pp. 406-416
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 24
    • 44949253954 scopus 로고    scopus 로고
    • Developmental changes in the milk fat globule membrane proteome during the transition from colostrums to milk
    • Reinhardt T.A., Lippolis J.D. Developmental changes in the milk fat globule membrane proteome during the transition from colostrums to milk. J. Dairy Sci. 2008, 91:2307-2318.
    • (2008) J. Dairy Sci. , vol.91 , pp. 2307-2318
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 25
    • 0030728214 scopus 로고    scopus 로고
    • Structural organization of the bovine cathelicidin gene family and identification of a novel member
    • Scocchi M., Wang S., Zanettia M. Structural organization of the bovine cathelicidin gene family and identification of a novel member. FEBS Lett. 1997, 417:311-315.
    • (1997) FEBS Lett. , vol.417 , pp. 311-315
    • Scocchi, M.1    Wang, S.2    Zanettia, M.3
  • 26
    • 64149101160 scopus 로고    scopus 로고
    • Quantitative mass spectrometry-based techniques for clinical use: Biomarker identification and quantification
    • Simpson K.L., Whetton A.D., Dive C. Quantitative mass spectrometry-based techniques for clinical use: Biomarker identification and quantification. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2009, 877:1240-1249.
    • (2009) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.877 , pp. 1240-1249
    • Simpson, K.L.1    Whetton, A.D.2    Dive, C.3
  • 30
    • 30744475689 scopus 로고    scopus 로고
    • Bovine peptidoglycan recognition protein-S: Antimicrobial activityl localization, secretion, and binding properties
    • Tydell C.C., Yuan J., Tran P., Selsted M.E. Bovine peptidoglycan recognition protein-S: Antimicrobial activityl localization, secretion, and binding properties. J. Immunol. 2006, 176:1154-1162.
    • (2006) J. Immunol. , vol.176 , pp. 1154-1162
    • Tydell, C.C.1    Yuan, J.2    Tran, P.3    Selsted, M.E.4
  • 33
    • 68049085754 scopus 로고    scopus 로고
    • Effect of dynamic exclusion duration on spectral count based quantitative proteomics
    • Zhang Y., Wen Z., Washburn M.P., Florens L. Effect of dynamic exclusion duration on spectral count based quantitative proteomics. Anal. Chem. 2009, 81:6317-6326.
    • (2009) Anal. Chem. , vol.81 , pp. 6317-6326
    • Zhang, Y.1    Wen, Z.2    Washburn, M.P.3    Florens, L.4
  • 34
    • 26444506068 scopus 로고    scopus 로고
    • Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling
    • Zybailov B., Coleman M.K., Florens L., Washburn M.P. Correlation of relative abundance ratios derived from peptide ion chromatograms and spectrum counting for quantitative proteomic analysis using stable isotope labeling. Anal. Chem. 2005, 77:6218-6224.
    • (2005) Anal. Chem. , vol.77 , pp. 6218-6224
    • Zybailov, B.1    Coleman, M.K.2    Florens, L.3    Washburn, M.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.