메뉴 건너뛰기




Volumn 117, Issue 1-4, 2007, Pages 358-369

Avian proteomics: Advances, challenges and new technologies

Author keywords

[No Author keywords available]

Indexed keywords

BIOTECHNOLOGY; BONE GROWTH; BRAIN DEVELOPMENT; CELL DEATH; CEREBROSPINAL FLUID; EMBRYO DEVELOPMENT; FOWL; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NECROTIZING ENTERITIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEOMICS; REVIEW; SKELETAL MUSCLE;

EID: 34547622842     PISSN: 14248581     EISSN: None     Source Type: Journal    
DOI: 10.1159/000103199     Document Type: Review
Times cited : (14)

References (67)
  • 2
    • 17044410168 scopus 로고    scopus 로고
    • Normalization and analysis of residual variation in two-dimensional gel electrophoresis for quantitative differential proteomics
    • Almeida JS, Stanislaus R, Krug E, Arthur JM: Normalization and analysis of residual variation in two-dimensional gel electrophoresis for quantitative differential proteomics. Proteomics 5:1242-1249 (2005).
    • (2005) Proteomics , vol.5 , pp. 1242-1249
    • Almeida, J.S.1    Stanislaus, R.2    Krug, E.3    Arthur, J.M.4
  • 3
    • 0031824886 scopus 로고    scopus 로고
    • Effects of body mass and genotype on avian degenerative joint disease pathology and articular cartilage proteoglycan distribution
    • Anderson-MacKenzie JM, Hulmes DJ, Thorp BH: Effects of body mass and genotype on avian degenerative joint disease pathology and articular cartilage proteoglycan distribution. Clin Exp Rheumatol 16:403-408 (1998).
    • (1998) Clin Exp Rheumatol , vol.16 , pp. 403-408
    • Anderson-MacKenzie, J.M.1    Hulmes, D.J.2    Thorp, B.H.3
  • 4
    • 33745160404 scopus 로고    scopus 로고
    • Large-scale identification of protein-protein interaction of Escherichia coli K-12
    • Arifuzzaman M, Maeda M, et al: Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16:686-691 (2006).
    • (2006) Genome Res , vol.16 , pp. 686-691
    • Arifuzzaman, M.1    Maeda, M.2
  • 5
    • 22144489165 scopus 로고    scopus 로고
    • The use of proteomics in meat science
    • Bendixen E: The use of proteomics in meat science. Meat Science 71:138-149 (2005).
    • (2005) Meat Science , vol.71 , pp. 138-149
    • Bendixen, E.1
  • 6
    • 16344389629 scopus 로고    scopus 로고
    • Metabolic labeling of proteins for proteomics
    • Beynon RJ, Pratt JM: Metabolic labeling of proteins for proteomics. Mol Cell Proteomics 4:857-872 (2005).
    • (2005) Mol Cell Proteomics , vol.4 , pp. 857-872
    • Beynon, R.J.1    Pratt, J.M.2
  • 7
    • 33749072902 scopus 로고    scopus 로고
    • Strategies for measuring dynamics: The temporal component of proteomics
    • Beynon RJ, Pratt JM: Strategies for measuring dynamics: the temporal component of proteomics. Methods Biochem Anal 49:15-25 (2006).
    • (2006) Methods Biochem Anal , vol.49 , pp. 15-25
    • Beynon, R.J.1    Pratt, J.M.2
  • 8
    • 23144442824 scopus 로고    scopus 로고
    • Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides
    • Beynon RJ, Doherty MK, Pratt JM, Gaskell SJ: Multiplexed absolute quantification in proteomics using artificial QCAT proteins of concatenated signature peptides. Nat Methods 2:587-589 (2005).
    • (2005) Nat Methods , vol.2 , pp. 587-589
    • Beynon, R.J.1    Doherty, M.K.2    Pratt, J.M.3    Gaskell, S.J.4
  • 9
    • 0037093117 scopus 로고    scopus 로고
    • Low-energy collision-induced dissociation fragmentation analysis of cysteinyl-modified peptides
    • Borisov OV, Goshe MB, Conrads TP, Rakov VS, Veenstra TD, Smith RD: Low-energy collision-induced dissociation fragmentation analysis of cysteinyl-modified peptides. Anal Chem 74:2284-2292 (2002).
    • (2002) Anal Chem , vol.74 , pp. 2284-2292
    • Borisov, O.V.1    Goshe, M.B.2    Conrads, T.P.3    Rakov, V.S.4    Veenstra, T.D.5    Smith, R.D.6
  • 10
    • 33745090847 scopus 로고    scopus 로고
    • Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column
    • Brand J, Haslberger TH, Zolg W, Pestlin G, Palme S:Depletion efficiency and recovery of trace markers from a multiparameter immunodepletion column. Proteomics 6:3236-3242 (2006).
    • (2006) Proteomics , vol.6 , pp. 3236-3242
    • Brand, J.1    Haslberger, T.H.2    Zolg, W.3    Pestlin, G.4    Palme, S.5
  • 11
    • 0037306116 scopus 로고    scopus 로고
    • The chicken as a model for large-scale analysis of vertebrate gene function
    • Brown WRA, Hubbard SJ, Tickle C, Wilson SA: The chicken as a model for large-scale analysis of vertebrate gene function. Nat Rev Genet 4:87-98 (2003).
    • (2003) Nat Rev Genet , vol.4 , pp. 87-98
    • Brown, W.R.A.1    Hubbard, S.J.2    Tickle, C.3    Wilson, S.A.4
  • 12
    • 4043083306 scopus 로고    scopus 로고
    • Proteomics in the chicken: Tools for understanding immune responses to avian diseases
    • Burgess SC: Proteomics in the chicken: tools for understanding immune responses to avian diseases. Poult Sci 83:552-573 (2004).
    • (2004) Poult Sci , vol.83 , pp. 552-573
    • Burgess, S.C.1
  • 13
    • 4644308446 scopus 로고    scopus 로고
    • Marek's disease is a natural model for lymphomas overexpressing Hodgkin's disease antigen (CD30)
    • Burgess SC, Young JR, Baaten BJ, Hunt L, Ross LN, et al: Marek's disease is a natural model for lymphomas overexpressing Hodgkin's disease antigen (CD30). Proc Natl Acad Sci USA 101:13879-13884 (2004).
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13879-13884
    • Burgess, S.C.1    Young, J.R.2    Baaten, B.J.3    Hunt, L.4    Ross, L.N.5
  • 14
    • 28844443822 scopus 로고    scopus 로고
    • Chicken genome: Current status and future opportunities
    • Burt DW: Chicken genome: current status and future opportunities. Genome Res 15:1692-1698 (2005).
    • (2005) Genome Res , vol.15 , pp. 1692-1698
    • Burt, D.W.1
  • 15
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol E, Piulats E, Echave P, Herrero E, Ros J: Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J Biol Chem 275:27393-27398 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 16
    • 0036733145 scopus 로고    scopus 로고
    • Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: Dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71
    • Castegna A, Aksenov M, Thongboonkerd V, Klein JB, Pierce WM, et al: Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, alpha-enolase and heat shock cognate 71. J Neurochem 82:1524-1532 (2002).
    • (2002) J Neurochem , vol.82 , pp. 1524-1532
    • Castegna, A.1    Aksenov, M.2    Thongboonkerd, V.3    Klein, J.B.4    Pierce, W.M.5
  • 18
    • 0033180434 scopus 로고    scopus 로고
    • Ascites in poultry: Recent investigations
    • Currie RJ: Ascites in poultry: recent investigations. Avian Pathol 28:313-326 (1999).
    • (1999) Avian Pathol , vol.28 , pp. 313-326
    • Currie, R.J.1
  • 19
    • 2642568030 scopus 로고    scopus 로고
    • The proteome of chicken skeletal muscle: Changes in soluble protein expression during growth in a layer strain
    • Doherty MK, McLean L, Hayter JR, Pratt JM, Robertson DH, et al: The proteome of chicken skeletal muscle: changes in soluble protein expression during growth in a layer strain. Proteomics 4:2082-2093 (2004).
    • (2004) Proteomics , vol.4 , pp. 2082-2093
    • Doherty, M.K.1    McLean, L.2    Hayter, J.R.3    Pratt, J.M.4    Robertson, D.H.5
  • 20
    • 13844317869 scopus 로고    scopus 로고
    • Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates
    • Doherty MK, Whitehead C, McCormack H, Gaskell SJ, Beynon RJ: Proteome dynamics in complex organisms: Using stable isotopes to monitor individual protein turnover rates. Proteomics 5:522-533 (2005).
    • (2005) Proteomics , vol.5 , pp. 522-533
    • Doherty, M.K.1    Whitehead, C.2    McCormack, H.3    Gaskell, S.J.4    Beynon, R.J.5
  • 21
    • 0021750803 scopus 로고
    • Interrelationships between the hypothalamus, pituitary gland, ovary, adrenal gland, and the open period for LH release in the hen (Gallus domesticus)
    • Etches RJ, Petitte JN, Anderson-Langmuir CE: Interrelationships between the hypothalamus, pituitary gland, ovary, adrenal gland, and the open period for LH release in the hen (Gallus domesticus). J Exp Zool 232:501-511 (1984).
    • (1984) J Exp Zool , vol.232 , pp. 501-511
    • Etches, R.J.1    Petitte, J.N.2    Anderson-Langmuir, C.E.3
  • 22
    • 0025075708 scopus 로고
    • Prostaglandin production by the largest preovulatory follicles in the domestic hen (Gallus domesticus)
    • Etches R, Kelly J, Anderson-Langmuir CE, Olson DM: Prostaglandin production by the largest preovulatory follicles in the domestic hen (Gallus domesticus). Biol Reprod 43:378-384 (1990).
    • (1990) Biol Reprod , vol.43 , pp. 378-384
    • Etches, R.1    Kelly, J.2    Anderson-Langmuir, C.E.3    Olson, D.M.4
  • 23
    • 0037795741 scopus 로고    scopus 로고
    • Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
    • Gerber SA, Rush J, Stemman O, Kirschner MW, Gygi SP: Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS. Proc Natl Acad Sci USA 100:6940-6945 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6940-6945
    • Gerber, S.A.1    Rush, J.2    Stemman, O.3    Kirschner, M.W.4    Gygi, S.P.5
  • 24
    • 0038333588 scopus 로고    scopus 로고
    • Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides
    • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, et al: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol 21:566-569 (2003).
    • (2003) Nat Biotechnol , vol.21 , pp. 566-569
    • Gevaert, K.1    Goethals, M.2    Martens, L.3    Van Damme, J.4    Staes, A.5
  • 25
    • 24144468009 scopus 로고    scopus 로고
    • Diagonal reverse-phase chromatography applications in peptide-centric proteomics: Ahead of catalogue-omics?
    • Gevaert K, Van Damme P, Martens L, Vandekerckhove J: Diagonal reverse-phase chromatography applications in peptide-centric proteomics: ahead of catalogue-omics? Anal Biochem 345:18-29 (2005).
    • (2005) Anal Biochem , vol.345 , pp. 18-29
    • Gevaert, K.1    Van Damme, P.2    Martens, L.3    Vandekerckhove, J.4
  • 26
    • 33845413316 scopus 로고    scopus 로고
    • Protein processing and other modifications analyzed by diagonal peptide chromatography
    • Gevaert K, Van Damme P, Ghesquiere B, Vandekerckhove J: Protein processing and other modifications analyzed by diagonal peptide chromatography. Biochim Biophys Acta 1764:1801-1810 (2006).
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1801-1810
    • Gevaert, K.1    Van Damme, P.2    Ghesquiere, B.3    Vandekerckhove, J.4
  • 27
    • 14844314804 scopus 로고    scopus 로고
    • Advances in protein complex analysis using mass spectrometry
    • Gingras A-C, Aebersold R, Raught B: Advances in protein complex analysis using mass spectrometry. J Physiol (Lond) 563:11-21 (2005).
    • (2005) J Physiol (Lond) , vol.563 , pp. 11-21
    • Gingras, A.-C.1    Aebersold, R.2    Raught, B.3
  • 28
    • 29544441467 scopus 로고    scopus 로고
    • Albumin depletion of human plasma also removes low abundance proteins including the cytokines
    • Granger J, Siddiqui J, Copeland S, Remick D: Albumin depletion of human plasma also removes low abundance proteins including the cytokines. Proteomics 5:4713-4718 (2005).
    • (2005) Proteomics , vol.5 , pp. 4713-4718
    • Granger, J.1    Siddiqui, J.2    Copeland, S.3    Remick, D.4
  • 31
    • 27144466714 scopus 로고    scopus 로고
    • Proteome analysis of chicken embryonic gonads: Identification of major proteins from cultured gonadal primordial germ cells
    • Han BK, Kim JN, Shin JH, Kim JK, Jo DH, et al: Proteome analysis of chicken embryonic gonads: identification of major proteins from cultured gonadal primordial germ cells. Mol Reprod Dev 72:521-529 (2005).
    • (2005) Mol Reprod Dev , vol.72 , pp. 521-529
    • Han, B.K.1    Kim, J.N.2    Shin, J.H.3    Kim, J.K.4    Jo, D.H.5
  • 34
    • 0026448766 scopus 로고
    • Mass isotopomer distribution analysis: A technique for measuring biosynthesis and turnover of polymers
    • Hellerstein MK, Neese RA: Mass isotopomer distribution analysis: a technique for measuring biosynthesis and turnover of polymers. Am J Physiol 263:E988-1001 (1992).
    • (1992) Am J Physiol , vol.263
    • Hellerstein, M.K.1    Neese, R.A.2
  • 35
    • 0033038503 scopus 로고    scopus 로고
    • Mass isotopomer distribution analysis at eight years: Theoretical, analytic, and experimental considerations
    • Hellerstein MK, Neese RA: Mass isotopomer distribution analysis at eight years: theoretical, analytic, and experimental considerations. Am J Physiol 276:E1146-1170 (1999).
    • (1999) Am J Physiol , vol.276
    • Hellerstein, M.K.1    Neese, R.A.2
  • 36
    • 10644283823 scopus 로고    scopus 로고
    • Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution
    • Hillier LW, Miller W, et al: Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution. Nature 432:695-716 (2004).
    • (2004) Nature , vol.432 , pp. 695-716
    • Hillier, L.W.1    Miller, W.2
  • 37
    • 0029688459 scopus 로고    scopus 로고
    • Comparative development of the antitrochanter in three strains of domestic fowl
    • Hocking PM, Thorp BH, Bernard R, Dick L: Comparative development of the antitrochanter in three strains of domestic fowl. Res Vet Sci 60:37-43 (1996).
    • (1996) Res Vet Sci , vol.60 , pp. 37-43
    • Hocking, P.M.1    Thorp, B.H.2    Bernard, R.3    Dick, L.4
  • 38
    • 33645678466 scopus 로고    scopus 로고
    • Analysis of chicken serum proteome and differential protein expression during development in single-comb White Leghorn hens
    • Huang SY, Lin JH, Chen YH, Chuang CK, Chiu YF, et al: Analysis of chicken serum proteome and differential protein expression during development in single-comb White Leghorn hens. Proteomics 6:2217-2224(2006).
    • (2006) Proteomics , vol.6 , pp. 2217-2224
    • Huang, S.Y.1    Lin, J.H.2    Chen, Y.H.3    Chuang, C.K.4    Chiu, Y.F.5
  • 39
    • 13444260275 scopus 로고    scopus 로고
    • The absolute quantification strategy: A general procedure for the quantification of proteins and post-translational modifications
    • Kirkpatrick DS, Gerber SA, Gygi SP: The absolute quantification strategy: a general procedure for the quantification of proteins and post-translational modifications. Methods 35:265-273 (2005).
    • (2005) Methods , vol.35 , pp. 265-273
    • Kirkpatrick, D.S.1    Gerber, S.A.2    Gygi, S.P.3
  • 40
    • 25144497603 scopus 로고    scopus 로고
    • Proteomic analysis of hypothalamic proteins of high and low egg production strains of chickens
    • Kuo YM, Shiue YL, Chen CF, Tang PC, Lee YP: Proteomic analysis of hypothalamic proteins of high and low egg production strains of chickens. Theriogenology 64:1490-1502 (2005).
    • (2005) Theriogenology , vol.64 , pp. 1490-1502
    • Kuo, Y.M.1    Shiue, Y.L.2    Chen, C.F.3    Tang, P.C.4    Lee, Y.P.5
  • 41
    • 33645779008 scopus 로고    scopus 로고
    • A chick retinal proteome database and differential retinal protein expressions during early ocular development
    • Lam TC, Li KK, Lo SC, Guggenheim JA, To CH: A chick retinal proteome database and differential retinal protein expressions during early ocular development. J Proteome Res 5:771-784 (2006).
    • (2006) J Proteome Res , vol.5 , pp. 771-784
    • Lam, T.C.1    Li, K.K.2    Lo, S.C.3    Guggenheim, J.A.4    To, C.H.5
  • 42
    • 0040782137 scopus 로고    scopus 로고
    • Avian mycoplasmosis (Mycoplasma gallisepticum)
    • Levisohn S, Kleven SH: Avian mycoplasmosis (Mycoplasma gallisepticum). Rev Sci Tech 19:425-442 (2000).
    • (2000) Rev Sci Tech , vol.19 , pp. 425-442
    • Levisohn, S.1    Kleven, S.H.2
  • 43
    • 33646557327 scopus 로고    scopus 로고
    • A mass spectrometry-based proteomic approach to study Marek's disease virus gene expression
    • Liu HC, Soderblom EJ, Goshe MB: A mass spectrometry-based proteomic approach to study Marek's disease virus gene expression. J Virol Methods 135:66-75 (2006).
    • (2006) J Virol Methods , vol.135 , pp. 66-75
    • Liu, H.C.1    Soderblom, E.J.2    Goshe, M.B.3
  • 44
    • 0016260916 scopus 로고
    • Necrotic enteritis in broiler chickens. II. Pathology and proposed pathogenesis
    • Long JR, Pettit JR, Barnum DA: Necrotic enteritis in broiler chickens. II. Pathology and proposed pathogenesis. Can J Comp Med 38:467-474 (1974).
    • (1974) Can J Comp Med , vol.38 , pp. 467-474
    • Long, J.R.1    Pettit, J.R.2    Barnum, D.A.3
  • 45
    • 22044439420 scopus 로고    scopus 로고
    • Proteomic profiling of facial development in chick embryos
    • Mangum JE, Farlie PG, Hubbard MJ: Proteomic profiling of facial development in chick embryos. Proteomics 5:2542-2550 (2005).
    • (2005) Proteomics , vol.5 , pp. 2542-2550
    • Mangum, J.E.1    Farlie, P.G.2    Hubbard, M.J.3
  • 46
    • 11144358205 scopus 로고    scopus 로고
    • Molecular cytogenetic definition of the chicken genome: The first complete avian karyotype
    • Masabanda JS, Burt DW, O'Brien PC, Vignal A, Fillon V, et al: Molecular cytogenetic definition of the chicken genome: the first complete avian karyotype. Genetics 166:1367-1373 (2004).
    • (2004) Genetics , vol.166 , pp. 1367-1373
    • Masabanda, J.S.1    Burt, D.W.2    O'Brien, P.C.3    Vignal, A.4    Fillon, V.5
  • 48
    • 34248637584 scopus 로고    scopus 로고
    • Positional proteomics: Preparation of amino-terminal peptides as a strategy for proteome simplification and characterization
    • McDonald L, Beynon RJ: Positional proteomics: preparation of amino-terminal peptides as a strategy for proteome simplification and characterization. Nat Protocols 1:1790-1798 (2006).
    • (2006) Nat Protocols , vol.1 , pp. 1790-1798
    • McDonald, L.1    Beynon, R.J.2
  • 49
    • 30944438540 scopus 로고    scopus 로고
    • Positional proteomics: Selective recovery and analysis of N-terminal proteolytic peptides
    • McDonald L, Robertson DH, Hurst JL, Beynon RJ: Positional proteomics: selective recovery and analysis of N-terminal proteolytic peptides. Nat Methods 2:955-957 (2005).
    • (2005) Nat Methods , vol.2 , pp. 955-957
    • McDonald, L.1    Robertson, D.H.2    Hurst, J.L.3    Beynon, R.J.4
  • 53
    • 29144462019 scopus 로고    scopus 로고
    • Mammalian embryonic cerebrospinal fluid proteome has greater apolipoprotein and enzyme pattern complexity than the avian proteome
    • Parada C, Gato A, Bueno D: Mammalian embryonic cerebrospinal fluid proteome has greater apolipoprotein and enzyme pattern complexity than the avian proteome. J Proteome Res 4:2420-2428 (2005).
    • (2005) J Proteome Res , vol.4 , pp. 2420-2428
    • Parada, C.1    Gato, A.2    Bueno, D.3
  • 56
    • 33750342104 scopus 로고    scopus 로고
    • Development and evaluation of a diagnostic PCR for Mycoplasma synoviae using primers located in the intergenic spacer region and the 23S rRNA gene
    • Ramirez AS, Naylor CJ, Hammond PP, Bradbury JM: Development and evaluation of a diagnostic PCR for Mycoplasma synoviae using primers located in the intergenic spacer region and the 23S rRNA gene. Vet Microbiol 118:76-82 (2006).
    • (2006) Vet Microbiol , vol.118 , pp. 76-82
    • Ramirez, A.S.1    Naylor, C.J.2    Hammond, P.P.3    Bradbury, J.M.4
  • 57
    • 33750112796 scopus 로고    scopus 로고
    • Protein equalizer technology: The quest for a democratic proteome
    • Righetti PG, Boschetti E, Lomas L, Citterio A: Protein equalizer technology: the quest for a democratic proteome. Proteomics 6:3980-3992 (2006).
    • (2006) Proteomics , vol.6 , pp. 3980-3992
    • Righetti, P.G.1    Boschetti, E.2    Lomas, L.3    Citterio, A.4
  • 59
    • 2942586687 scopus 로고    scopus 로고
    • Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach
    • Stagsted J, Bendixen E, Andersen HJ: Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach. J Agric Food Chem 52:3967-3974 (2004).
    • (2004) J Agric Food Chem , vol.52 , pp. 3967-3974
    • Stagsted, J.1    Bendixen, E.2    Andersen, H.J.3
  • 60
    • 11244302359 scopus 로고    scopus 로고
    • The chick: A great model system becomes even greater
    • Stern CD: The chick: a great model system becomes even greater. Develop Cell 8:9-17 (2005).
    • (2005) Develop Cell , vol.8 , pp. 9-17
    • Stern, C.D.1
  • 61
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J, Cabiscol E, Ros J: Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem 273:3027-3032 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 62
    • 0022369652 scopus 로고
    • Purification, characterization, and distribution of enolase isozymes in chicken
    • Tanaka M, Sugisaki K, Nakashima K: Purification, characterization, and distribution of enolase isozymes in chicken. J Biochem (Tokyo) 98:1527-1534 (1985).
    • (1985) J Biochem (Tokyo) , vol.98 , pp. 1527-1534
    • Tanaka, M.1    Sugisaki, K.2    Nakashima, K.3
  • 63
    • 0028988402 scopus 로고
    • Chicken alphaenolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: CDNA cloning and nucleotide sequence analysis
    • Tanaka M, Maeda K, Nakashima K: Chicken alphaenolase but not beta-enolase has a Src-dependent tyrosine-phosphorylation site: cDNA cloning and nucleotide sequence analysis. J Biochem (Tokyo) 117:554-559 (1995).
    • (1995) J Biochem (Tokyo) , vol.117 , pp. 554-559
    • Tanaka, M.1    Maeda, K.2    Nakashima, K.3
  • 64
    • 0026742226 scopus 로고
    • Detection and differentiation of chicken anemia virus isolates by using the polymerase chain reaction
    • Todd D, Mawhinney KA, McNulty MS: Detection and differentiation of chicken anemia virus isolates by using the polymerase chain reaction. J Clin Microbiol 30:1661-1666 (1992).
    • (1992) J Clin Microbiol , vol.30 , pp. 1661-1666
    • Todd, D.1    Mawhinney, K.A.2    McNulty, M.S.3
  • 65
    • 3242888358 scopus 로고    scopus 로고
    • Proteomic and sequence analysis of chicken lens crystallins reveals alternate splicing and translational forms of beta B2 and beta A2 crystallins
    • Wilmarth PA, Taube JR, Riviere MA, Duncan MK, David LL: Proteomic and sequence analysis of chicken lens crystallins reveals alternate splicing and translational forms of beta B2 and beta A2 crystallins. Invest Ophthalmol Vis Sci 45:2705-2715 (2004).
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 2705-2715
    • Wilmarth, P.A.1    Taube, J.R.2    Riviere, M.A.3    Duncan, M.K.4    David, L.L.5
  • 66
    • 22144442469 scopus 로고    scopus 로고
    • Quantitative detection of Clostridium perfringens in the broiler fowl gastrointestinal tract by real-time PCR
    • Wise MG, Siragusa GR: Quantitative detection of Clostridium perfringens in the broiler fowl gastrointestinal tract by real-time PCR. Appl Environ Microbiol 71:3911-3916 (2005).
    • (2005) Appl Environ Microbiol , vol.71 , pp. 3911-3916
    • Wise, M.G.1    Siragusa, G.R.2
  • 67
    • 23044464125 scopus 로고    scopus 로고
    • A quantitative investigation into the losses of proteins at different stages of a two-dimensional gel electrophoresis procedure
    • Zhou S, Bailey MJ, Dunn MJ, Preedy VR, Emery PW: A quantitative investigation into the losses of proteins at different stages of a two-dimensional gel electrophoresis procedure. Proteomics 5:2739-2747 (2005).
    • (2005) Proteomics , vol.5 , pp. 2739-2747
    • Zhou, S.1    Bailey, M.J.2    Dunn, M.J.3    Preedy, V.R.4    Emery, P.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.