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Volumn 9, Issue 16, 2009, Pages 4000-4016

Application of iTRAQ to catalogue the skeletal muscle proteome in pigs and assessment of effects of gender and diet dephytinization

Author keywords

Animal proteomics; Gender; iTRAQ; Muscle; Phytate; Pig

Indexed keywords

ADENOSINE MONOPHOSPHATE DEAMINASE; ALPHA TROPOMYOSIN; COLLAGEN TYPE 1; COLLAGEN TYPE 5; CYTOCHROME C OXIDASE; DIAZEPAM BINDING INHIBITOR; DIHYDROLIPOAMIDE DEHYDROGENASE; DJ 1 PROTEIN; FILAMIN A; FRUCTOSE BISPHOSPHATE ALDOLASE; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; HEAT SHOCK PROTEIN 10; HISTONE H2A; IMMUNOGLOBULIN LAMBDA CHAIN; LIM KINASE; MACROPHAGE MIGRATION INHIBITION FACTOR; MUSCLE PROTEIN; MYOGLOBIN; MYOSIN HEAVY CHAIN; MYOSIN HEAVY CHAIN BETA; NEBULIN; PHOSPHOGLUCOMUTASE; PHYTATE; PROTEOME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); TRANSFERRIN; TROPOMODULIN; TRYPSIN; TYROSINE 3 MONOOXYGENASE;

EID: 69449097755     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.200900049     Document Type: Article
Times cited : (50)

References (128)
  • 1
    • 2542596176 scopus 로고    scopus 로고
    • HUPO initiatives relevant to clinical proteomics
    • DOI 10.1074/mcp.R400004-MCP200, Cancer Proteomics
    • Hanash, S., HUPO initiatives relevant to clinical proteomics. Mol. Cell. Proteomics 2004, 3, 298-301. (Pubitemid 38702084)
    • (2004) Molecular and Cellular Proteomics , vol.3 , Issue.4 , pp. 298-301
    • Hanash, S.1
  • 2
    • 27844583947 scopus 로고    scopus 로고
    • Swine in biomedical research: Creating the building blocks of animal models
    • Schook, L., Beattie, C., Beever, J., Donovan, S. et al., Swine in biomedical research: creating the building blocks of animal models. Anim. Biotechnol. 2005, 16, 183-190.
    • (2005) Anim. Biotechnol. , vol.16 , pp. 183-190
    • Schook, L.1    Beattie, C.2    Beever, J.3    Donovan, S.4
  • 3
    • 33847068799 scopus 로고    scopus 로고
    • Advances in swine biomedical model genomics
    • Lunney, J. K., Advances in swine biomedical model genomics. Int. J. Biol. Sci. 2007, 3, 179-184.
    • (2007) Int. J. Biol. Sci. , vol.3 , pp. 179-184
    • Lunney, J.K.1
  • 4
    • 46449118663 scopus 로고    scopus 로고
    • The pig as an experimental model for elucidating the mechanisms governing dietary influence on mineral absorption
    • Maywood
    • Patterson, J. K., Lei, X. G., Miller, D. D., The pig as an experimental model for elucidating the mechanisms governing dietary influence on mineral absorption. Exp. Biol. Med. (Maywood) 2008, 233, 651-664.
    • (2008) Exp. Biol. Med. , vol.233 , pp. 651-664
    • Patterson, J.K.1    Lei, X.G.2    Miller, D.D.3
  • 5
    • 33750095969 scopus 로고    scopus 로고
    • Selected physiologic compatibilities and incompatibilities between human and porcine organ systems
    • DOI 10.1111/j.1399-3089.2006.00346.x
    • Ibrahim, Z., Busch, J., Awwad, M., Wagner, R. et al., Selected physiologic compatibilities and incompatibilities between human and porcine organ systems. Xenotransplantation 2006, 13, 488-499. (Pubitemid 44592548)
    • (2006) Xenotransplantation , vol.13 , Issue.6 , pp. 488-499
    • Ibrahim, Z.1    Busch, J.2    Awwad, M.3    Wagner, R.4    Wells, K.5    Cooper, D.K.C.6
  • 7
    • 33847034000 scopus 로고    scopus 로고
    • Gene expression profiling: Insights into skeletal muscle growth and development
    • Reecy, J. M., Spurlock, D. M., Stahl, C. H., Gene expression profiling: insights into skeletal muscle growth and development. J. Anim. Sci. 2006, 84, E150-E154.
    • (2006) J. Anim. Sci. , vol.84
    • Reecy, J.M.1    Spurlock, D.M.2    Stahl, C.H.3
  • 9
    • 52249101738 scopus 로고    scopus 로고
    • Pig Longissimus lumborum proteome: Part I. Effects of genetic background, rearing environment and gender
    • Kwasiborski, A., Sayd, T., Chambon, C., Sante-Lhoutellier, V. et al., Pig Longissimus lumborum proteome: part I. Effects of genetic background, rearing environment and gender. Meat Sci. 2008, 80, 968-981.
    • (2008) Meat Sci. , vol.80 , pp. 968-981
    • Kwasiborski, A.1    Sayd, T.2    Chambon, C.3    Sante-Lhoutellier, V.4
  • 10
    • 57149142755 scopus 로고    scopus 로고
    • Comparison of muscle proteome profiles in pure breeds of Norwegian Landrace and Duroc at three different ages
    • Hollung, K., Grove, H., Faergestad, E. M., Sidhu, M. S., Berg, P., Comparison of muscle proteome profiles in pure breeds of Norwegian Landrace and Duroc at three different ages. Meat Sci. 2009, 81, 487-492.
    • (2009) Meat Sci. , vol.81 , pp. 487-492
    • Hollung, K.1    Grove, H.2    Faergestad, E.M.3    Sidhu, M.S.4    Berg, P.5
  • 11
    • 1842584567 scopus 로고    scopus 로고
    • Proteome changes during pork meat ageing following use of two different pre-slaughter handling procedures
    • DOI 10.1016/j.meatsci.2004.01.008, PII S0309174004000269
    • Morzel, M., Chambon, C., Hamelin, M., Sante-Lhoutellier, V. et al., Proteome changes during porkmeat ageing following use of two different pre-slaughter handling procedures. Meat Sci. 2004, 67, 689-696. (Pubitemid 38416892)
    • (2004) Meat Science , vol.67 , Issue.4 , pp. 689-696
    • Morzel, M.1    Chambon, C.2    Hamelin, M.3    Sante-Lhoutellier, V.4    Sayd, T.5    Monin, G.6
  • 12
    • 33645976443 scopus 로고    scopus 로고
    • Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: Implications on meat color development
    • Sayd, T., Morzel, M., Chambon, C., Franck, M. et al., Proteome analysis of the sarcoplasmic fraction of pig semimembranosus muscle: implications on meat color development. J. Agric. Food Chem. 2006, 54, 2732-2737.
    • (2006) J. Agric. Food Chem. , vol.54 , pp. 2732-2737
    • Sayd, T.1    Morzel, M.2    Chambon, C.3    Franck, M.4
  • 15
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • DOI 10.1002/pmic.200300688
    • Bouley, J., Chambon, C., Picard, B., Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2004, 4, 1811-1824. (Pubitemid 38738335)
    • (2004) Proteomics , vol.4 , Issue.6 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 16
    • 0037269496 scopus 로고    scopus 로고
    • Two-dimensional protein map of human vastus lateralis muscle
    • Gelfi, C., De Palma, S., Cerretelli, P., Begum, S., Wait, R., Two-dimensional protein map of human Vastus lateralis muscle. Electrophoresis 2003, 24, 286-295. (Pubitemid 36175878)
    • (2003) Electrophoresis , vol.24 , Issue.1-2 , pp. 286-295
    • Gelfi, C.1    De Palma, S.2    Cerretelli, P.3    Begum, S.4    Wait, R.5
  • 20
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 21
    • 21644483165 scopus 로고    scopus 로고
    • A comparison of the consistency of proteome quantitation using two-dimensional electrophoresis and shotgun isobaric tagging in Escherichia coli cells
    • DOI 10.1002/elps.200410336
    • Choe, L. H., Aggarwal, K., Franck, Z., Lee, K. H., A comparison of the consistency of proteome quantitation using two-dimensional electrophoresis and shotgun isobaric tagging in Escherichia coli cells. Electrophoresis 2005, 26, 2437-2449. (Pubitemid 40932751)
    • (2005) Electrophoresis , vol.26 , Issue.12 , pp. 2437-2449
    • Choe, L.H.1    Aggarwal, K.2    Franck, Z.3    Lee, K.H.4
  • 22
    • 35648942133 scopus 로고    scopus 로고
    • 8-Plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease
    • DOI 10.1002/pmic.200700316
    • Choe, L., D'Ascenzo, M., Relkin, N. R., Pappin, D. et al., 8-Plex quantitation of changes in cerebrospinal fluid protein expression in subjects undergoing intravenous immunoglobulin treatment for Alzheimer's disease. Proteomics 2007, 7, 3651-3660. (Pubitemid 350022271)
    • (2007) Proteomics , vol.7 , Issue.20 , pp. 3651-3660
    • Choe, L.1    D'Ascenzo, M.2    Relkin, N.R.3    Pappin, D.4    Ross, P.5    Williamson, B.6    Guertin, S.7    Pribil, P.8    Lee, K.H.9
  • 23
    • 27744450286 scopus 로고    scopus 로고
    • I-Tracker: For quantitative proteomics using iTRAQ
    • DOI 10.1186/1471-2164-6-145
    • Shadforth, I. P., Dunkley, T. P., Lilley, K. S., Bessant, C., i-Tracker: for quantitative proteomics using iTRAQ. BMC Genomics 2005, 6, 145. (Pubitemid 41631205)
    • (2005) BMC Genomics , vol.6 , pp. 145
    • Shadforth, I.P.1    Dunkley, T.P.J.2    Lilley, K.S.3    Bessant, C.4
  • 24
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S. K., Venable, J. D., Xu, T., Yates, J. R., III, A quantitative analysis software tool for mass spectrometry-based proteomics. Nat. Methods 2008, 5, 319-322.
    • (2008) Nat. Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates III, J.R.4
  • 25
    • 41349092313 scopus 로고    scopus 로고
    • Phytate: Impact on environment and human nutrition. A challenge for molecular breeding
    • Bohn, L., Meyer, A. S., Rasmussen, S. K., Phytate: impact on environment and human nutrition. A challenge for molecular breeding. J. Zhejiang Univ. Sci. B 2008, 9, 165-191.
    • (2008) J. Zhejiang Univ. Sci. B , vol.9 , pp. 165-191
    • Bohn, L.1    Meyer, A.S.2    Rasmussen, S.K.3
  • 26
    • 13444265893 scopus 로고    scopus 로고
    • Phytic acid degradation as a means of improving iron absorption
    • Hurrell, R. F., Phytic acid degradation as a means of improving iron absorption. Int. J. Vitam. Nutr. Res. 2004, 74, 445-452.
    • (2004) Int. J. Vitam. Nutr. Res. , vol.74 , pp. 445-452
    • Hurrell, R.F.1
  • 27
    • 33750846875 scopus 로고    scopus 로고
    • 6 and inositol
    • DOI 10.1207/s15327914nc5502-1
    • Vucenik, I., Shamsuddin, A. M., Protection against cancer by dietary IP6 and inositol. Nutr. Cancer 2006, 55, 109-125. (Pubitemid 44719624)
    • (2006) Nutrition and Cancer , vol.55 , Issue.2 , pp. 109-125
    • Vucenik, I.1    Shamsuddin, A.M.2
  • 29
    • 47849089236 scopus 로고    scopus 로고
    • Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines
    • Golovan, S. P., Hakimov, H. A., Verschoor, C. P., Walters, S. et al., Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines. Comp. Biochem. Physiol. D-Genomics Proteomics 2008, 3, 234-242.
    • (2008) Comp. Biochem. Physiol. D-Genomics Proteomics , vol.3 , pp. 234-242
    • Golovan, S.P.1    Hakimov, H.A.2    Verschoor, C.P.3    Walters, S.4
  • 30
    • 34250318625 scopus 로고    scopus 로고
    • From selenium to selenoproteins: Synthesis, identity, and their role in human health
    • DOI 10.1089/ars.2007.1528
    • Papp, L. V., Lu, J., Holmgren, A., Khanna, K. K., From selenium to selenoproteins: synthesis, identity, and their role in human health. Antioxid. Redox Signal 2007, 9, 775-806. (Pubitemid 46919583)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.7 , pp. 775-806
    • Papp, L.V.1    Lu, J.2    Holmgren, A.3    Khanna, K.K.4
  • 32
    • 40549141833 scopus 로고    scopus 로고
    • Design and analysis issues in quantitative proteomics studies
    • DOI 10.1002/pmic.200700683
    • Karp, N. A., Lilley, K. S., Design and analysis issues in quantitative proteomics studies. Proteomics 2007, 7, 42-50. (Pubitemid 351547769)
    • (2007) Proteomics - Practical Proteomics , vol.2 , Issue.1 , pp. 42-50
    • Karp, N.A.1    Lilley, K.S.2
  • 33
    • 47849089236 scopus 로고    scopus 로고
    • Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines
    • Golovan, S. P., Hakimov, H. A., Verschoor, C. P., Walters, S. et al., Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines. Comp. Biochem. Physiol. D-Genomics Proteomics 2008, 3, 234-242.
    • (2008) Comp. Biochem. Physiol. D-Genomics Proteomics , vol.3 , pp. 234-242
    • Golovan, S.P.1    Hakimov, H.A.2    Verschoor, C.P.3    Walters, S.4
  • 34
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • DOI 10.1074/mcp.T600050-MCP200
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A. et al., The Paragon Algorithm: a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol. Cell. Proteomics 2007, 6, 1638-1655. (Pubitemid 47506173)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymourt, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 36
    • 33749630783 scopus 로고    scopus 로고
    • An integrated approach to mapping the proteome of the human bone marrow stromal cell
    • DOI 10.1002/pmic.200600209
    • Seshi, B., An integrated approach to mapping the proteome of the human bone marrow stromal cell. Proteomics 2006, 6, 5169-5182. (Pubitemid 44547158)
    • (2006) Proteomics , vol.6 , Issue.19 , pp. 5169-5182
    • Seshi, B.1
  • 37
    • 0001677717 scopus 로고
    • Controlling the false discovery rate - A practical and powerful approach to multiple testing
    • Benjamini, Y., Hochberg, Y., Controlling the false discovery rate - a practical and powerful approach to multiple testing. J. Roy. Stat. Soc. B Met. 1995, 57, 289-300.
    • (1995) J. Roy. Stat. Soc. B Met. , vol.57 , pp. 289-300
    • Benjamini, Y.1    Hochberg, Y.2
  • 39
    • 58149191270 scopus 로고    scopus 로고
    • The Universal Protein Resource (UniProt)
    • UniProt Consortium
    • UniProt Consortium. The Universal Protein Resource (UniProt). Nucleic Acids Res. 2009, 37, D169-D174.
    • (2009) Nucleic Acids Res. , vol.37
  • 40
    • 0038005018 scopus 로고    scopus 로고
    • DAVID: Database for annotation, visualization, and integrated discovery
    • Dennis, G., jr., Sherman, B. T., Hosack, D. A., Yang, J. et al., DAVID: database for annotation, visualization, and integrated discovery. Genome Biol. 2003, 4, 3.
    • (2003) Genome Biol. , vol.4 , pp. 3
    • Dennis Jr., G.1    Sherman, B.T.2    Hosack, D.A.3    Yang, J.4
  • 43
    • 34848889259 scopus 로고    scopus 로고
    • The paragon algorithm, a next generation search engine that uses sequence temperature values sequence temperature values and feature probabilities to identify peptides from tandem mass spectra
    • DOI 10.1074/mcp.T600050-MCP200
    • Shilov, I. V., Seymour, S. L., Patel, A. A., Loboda, A. et al., The Paragon Algorithm: a next generation search engine that uses sequence temperature values and feature probabilities to identify peptides from tandem mass spectra. Mol Cell Proteomics 2007, 6, 1638-1655. (Pubitemid 47506173)
    • (2007) Molecular and Cellular Proteomics , vol.6 , Issue.9 , pp. 1638-1655
    • Shilov, I.V.1    Seymourt, S.L.2    Patel, A.A.3    Loboda, A.4    Tang, W.H.5    Keating, S.P.6    Hunter, C.L.7    Nuwaysir, L.M.8    Schaeffer, D.A.9
  • 44
    • 34249062964 scopus 로고    scopus 로고
    • The minimum information about a proteomics experiment (MIAPE)
    • Taylor, C. F., Paton, N. W., Lilley, K. S., Binz, P. A. et al., The minimum information about a proteomics experiment (MIAPE). Nat. Biotechnol. 2007, 25, 887-893.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 887-893
    • Taylor, C.F.1    Paton, N.W.2    Lilley, K.S.3    Binz, P.A.4
  • 45
    • 23944526367 scopus 로고    scopus 로고
    • PRIDE: The proteomics identifications database
    • Martens, L., Hermjakob, H., Jones, P., Adamski, M. et al., PRIDE: the proteomics identifications database. Proteomics 2005, 5, 3537-3545.
    • (2005) Proteomics , vol.5 , pp. 3537-3545
    • Martens, L.1    Hermjakob, H.2    Jones, P.3    Adamski, M.4
  • 48
    • 0346364695 scopus 로고    scopus 로고
    • Characterization of the low molecular weight human serum proteome
    • Tirumalai, R. S., Chan, K. C., Prieto, D. A., Issaq, H. J. et al., Characterization of the low molecular weight human serum proteome. Mol. Cell. Proteomics 2003, 2, 1096-1103.
    • (2003) Mol. Cell. Proteomics , vol.2 , pp. 1096-1103
    • Tirumalai, R.S.1    Chan, K.C.2    Prieto, D.A.3    Issaq, H.J.4
  • 49
    • 24944440037 scopus 로고    scopus 로고
    • Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells
    • DOI 10.1074/mcp.M400193-MCP200
    • Unwin, R. D., Pierce, A., Watson, R. B., Sternberg, D. W., Whetton, A. D., Quantitative proteomic analysis using isobaric protein tags enables rapid comparison of changes in transcript and protein levels in transformed cells. Mol. Cell. Proteomics 2005, 4, 924-935. (Pubitemid 41309150)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.7 , pp. 924-935
    • Unwin, R.D.1    Pierce, A.2    Watson, R.B.3    Sternberg, D.W.4    Whetton, A.D.5
  • 50
    • 0037276175 scopus 로고    scopus 로고
    • Statistical tests for differential expression in cDNA microarray experiments
    • Cui, X. Q., Churchill, G. A., Statistical tests for differential expression in cDNA microarray experiments. Genome Biol. 2003, 4, 210.
    • (2003) Genome Biol. , vol.4 , pp. 210
    • Cui, X.Q.1    Churchill, G.A.2
  • 53
    • 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
  • 54
    • 33646570847 scopus 로고    scopus 로고
    • Isobaric tags for relative and absolute quantitation (iTRAQ) reproducibility: Implication of multiple injections
    • Chong, P. K., Gan, C. S., Pham, T. K., Wright, P. C., Isobaric tags for relative and absolute quantitation (iTRAQ) reproducibility: implication of multiple injections. J. Proteome Res. 2006, 5, 1232-1240.
    • (2006) J. Proteome Res. , vol.5 , pp. 1232-1240
    • Chong, P.K.1    Gan, C.S.2    Pham, T.K.3    Wright, P.C.4
  • 56
    • 42149195071 scopus 로고    scopus 로고
    • Heart protein expression related to age and sex in mice and humans
    • Diedrich, M., Tadic, J., Mao, L., Wacker, M. A. et al., Heart protein expression related to age and sex in mice and humans. Int. J. Mol. Med. 2007, 20, 865-874.
    • (2007) Int. J. Mol. Med. , vol.20 , pp. 865-874
    • Diedrich, M.1    Tadic, J.2    Mao, L.3    Wacker, M.A.4
  • 57
    • 60549106873 scopus 로고    scopus 로고
    • Transcriptomic and proteomic profiling of two porcine tissues using high-throughput technologies
    • Hornshoj, H., Bendixen, E., Conley, L. N., Andersen, P. K. et al., Transcriptomic and proteomic profiling of two porcine tissues using high-throughput technologies. BMC Genomics 2009, 10, 30.
    • (2009) BMC Genomics , vol.10 , pp. 30
    • Hornshoj, H.1    Bendixen, E.2    Conley, L.N.3    Andersen, P.K.4
  • 58
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino, S., Reggiani, C., Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 1996, 76, 371-423. (Pubitemid 26163713)
    • (1996) Physiological Reviews , vol.76 , Issue.2 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 59
    • 0015253408 scopus 로고
    • Postnatal-development of muscle fiber types in domestic-animals
    • Ashmore, C. R., Tompkins, G., Doerr, L., Postnatal-development of muscle fiber types in domestic-animals. J. Anim. Sci. 1972, 34, 37-41.
    • (1972) J. Anim. Sci. , vol.34 , pp. 37-41
    • Ashmore, C.R.1    Tompkins, G.2    Doerr, L.3
  • 61
    • 1242287698 scopus 로고    scopus 로고
    • Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties
    • DOI 10.1016/j.meatsci.2003.12.008, PII S0309174004000038
    • Ruusunen, M., Puolanne, E., Histochemical properties of fibre types in muscles of wild and domestic pigs and the effect of growth rate on muscle fibre properties. Meat Sci. 2004, 67, 533-539. (Pubitemid 38232334)
    • (2004) Meat Science , vol.67 , Issue.3 , pp. 533-539
    • Ruusunen, M.1    Puolanne, E.2
  • 62
    • 42149093908 scopus 로고    scopus 로고
    • Relationship between myosin heavy chain isoform expression and muscling in several diverse pig breeds
    • Wimmers, K., Ngu, N. T., Jennen, D. G. J., Tesfaye, D. et al., Relationship between myosin heavy chain isoform expression and muscling in several diverse pig breeds. J. Anim. Sci. 2008, 86, 795-803.
    • (2008) J. Anim. Sci. , vol.86 , pp. 795-803
    • Wimmers, K.1    Ngu, N.T.2    Jennen, D.G.J.3    Tesfaye, D.4
  • 67
    • 33644845960 scopus 로고    scopus 로고
    • Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2-D gel or LC-MALDI TOF/TOF
    • Wu, W. W., Wang, G. H., Baek, S. J., Shen, R. F., Comparative study of three proteomic quantitative methods, DIGE, cICAT, and iTRAQ, using 2-D gel or LC-MALDI TOF/TOF. J. Proteome Res. 2006, 5, 651-658.
    • (2006) J. Proteome Res. , vol.5 , pp. 651-658
    • Wu, W.W.1    Wang, G.H.2    Baek, S.J.3    Shen, R.F.4
  • 69
    • 38649090064 scopus 로고    scopus 로고
    • False discovery rates and related statistical concepts in mass spectrometry-based proteomics
    • DOI 10.1021/pr700747q
    • Choi, H., Nesvizhskii, A. I., False discovery rates and related statistical concepts in mass spectrometry-based proteomics. J. Proteome Res. 2008, 7, 47-50. (Pubitemid 351171114)
    • (2008) Journal of Proteome Research , vol.7 , Issue.1 , pp. 47-50
    • Choi, H.1    Nesvizhskii, A.I.2
  • 71
    • 34547572949 scopus 로고    scopus 로고
    • Is Proteomics the New Genomics?
    • DOI 10.1016/j.cell.2007.07.032, PII S0092867407009701
    • Cox, J., Mann, M., Is proteomics the new genomics? Cell 2007, 130, 395-398. (Pubitemid 47198310)
    • (2007) Cell , vol.130 , Issue.3 , pp. 395-398
    • Cox, J.1    Mann, M.2
  • 72
    • 69849103563 scopus 로고    scopus 로고
    • Power and limitations of electrophoretic separations in proteomics strategies
    • DOI: 10.1002/mas.20204
    • Rabilloud, T., Vaezzadeh, A. R., Potier, N., Lelong, C. et al., Power and limitations of electrophoretic separations in proteomics strategies. Mass Spectrom. Rev. 2008. DOI: 10.1002/mas.20204
    • (2008) Mass Spectrom. Rev.
    • Rabilloud, T.1    Vaezzadeh, A.R.2    Potier, N.3    Lelong, C.4
  • 74
    • 34249053821 scopus 로고    scopus 로고
    • Tissue subcellular fractionation and protein extraction for use in mass-spectrometry-based proteomics
    • DOI 10.1038/nprot.2006.273, PII NPROT.2006.273
    • Cox, B., Emili, A., Tissue subcellular fractionation and protein extraction for use in mass-spectrometry-based proteomics. Nat. Protoc. 2006, 1, 1872-1878. (Pubitemid 46778056)
    • (2006) Nature Protocols , vol.1 , Issue.4 , pp. 1872-1878
    • Cox, B.1    Emili, A.2
  • 75
    • 34548409217 scopus 로고    scopus 로고
    • Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential ingel electrophoresis
    • Karp, N. A., McCormick, P. S., Russell, M. R., Lilley, K. S., Experimental and statistical considerations to avoid false conclusions in proteomics studies using differential ingel electrophoresis. Mol. Cell. Proteomics 2007, 6, 1354-1364.
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1354-1364
    • Karp, N.A.1    McCormick, P.S.2    Russell, M.R.3    Lilley, K.S.4
  • 76
    • 29244448340 scopus 로고    scopus 로고
    • Microarray data analysis: From disarray to consolidation and consensus
    • DOI 10.1038/nrg1749
    • Allison, D. B., Cui, X. Q., Page, G. P., Sabripour, M., Microarray data analysis: from disarray to consolidation and consensus. Nat. Rev. Genetics 2006, 7, 55-65. (Pubitemid 41828948)
    • (2006) Nature Reviews Genetics , vol.7 , Issue.1 , pp. 55-65
    • Allison, D.B.1    Cui, X.2    Page, G.P.3    Sabripour, M.4
  • 77
    • 33750362838 scopus 로고    scopus 로고
    • Statistics for proteomics: A review of tools for analyzing experimental data
    • DOI 10.1002/pmic.200600554
    • Urfer, W., Grzegorczyk, M., Jung, K., Statistics for proteomics: a review of tools for analyzing experimental data. Proteomics 2006, 6, 48-55. (Pubitemid 44625769)
    • (2006) Proteomics , vol.1 , Issue.1-2 SUPPL. , pp. 48-55
    • Urfer, W.1    Grzegorczyk, M.2    Jung, K.3
  • 78
    • 0142151385 scopus 로고    scopus 로고
    • Overcoming technical variation and biological variation in quantitative proteomics
    • DOI 10.1002/pmic.200300534
    • Molloy, M. P., Brzezinski, E. E., Hang, J., McDowell, M. T., VanBogelen, R. A., Overcoming technical variation and biological variation in quantitative proteomics. Proteomics 2003, 3, 1912-1919. (Pubitemid 37305885)
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1912-1919
    • Molloy, M.P.1    Brzezinski, E.E.2    Hang, J.3    McDowell, M.T.4    Vanbogelen, R.A.5
  • 79
    • 19944432197 scopus 로고    scopus 로고
    • Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents
    • Ross, P. L., Huang, Y. N., Marchese, J. N., Williamson, B. et al., Multiplexed protein quantitation in Saccharomyces cerevisiae using amine-reactive isobaric tagging reagents. Mol. Cell. Proteomics 2004, 3, 1154-1169.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 1154-1169
    • Ross, P.L.1    Huang, Y.N.2    Marchese, J.N.3    Williamson, B.4
  • 80
    • 33847340190 scopus 로고    scopus 로고
    • Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ)
    • Gan, C. S., Chong, P. K., Pham, T. K., Wright, P. C., Technical, experimental, and biological variations in isobaric tags for relative and absolute quantitation (iTRAQ). J. Proteome Res. 2007, 6, 821-827.
    • (2007) J. Proteome Res. , vol.6 , pp. 821-827
    • Gan, C.S.1    Chong, P.K.2    Pham, T.K.3    Wright, P.C.4
  • 83
    • 38249041480 scopus 로고
    • The effects of sex condition, genotype and diet on bovine muscle-fiber characteristics
    • Seideman, S. C., Crouse, J. D., The effects of sex condition, genotype and diet on bovine muscle-fiber characteristics. Meat Sci. 1986, 17, 55-72.
    • (1986) Meat Sci. , vol.17 , pp. 55-72
    • Seideman, S.C.1    Crouse, J.D.2
  • 84
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DOI 10.1016/j.tcb.2005.05.001, PII S0962892405001273
    • DerMardirossian, C., Bokoch, G. M., GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol. 2005, 15, 356-363. (Pubitemid 40943524)
    • (2005) Trends in Cell Biology , vol.15 , Issue.7 , pp. 356-363
    • Dermardirossian, C.1    Bokoch, G.M.2
  • 88
    • 0242694008 scopus 로고    scopus 로고
    • Subtractive Hybridisation Screen Identifies Sexually Dimorphic Gene Expression in the Embryonic Mouse Gonad
    • DOI 10.1002/gene.10231
    • McClive, P. J., Hurley, T. M., Sarraj, M. A., van den Bergen, J. A., Sinclair, A. H., Subtractive hybridisation screen identifies sexually dimorphic gene expression in the embryonic mouse gonad. Genesis 2003, 37, 84-90. (Pubitemid 37413694)
    • (2003) Genesis , vol.37 , Issue.2 , pp. 84-90
    • McClive, P.J.1    Hurley, T.M.2    Sarraj, M.A.3    Van Den Bergen, J.A.4    Sinclair, A.H.5
  • 91
    • 38149016903 scopus 로고    scopus 로고
    • Sexually dimorphic gene expression in the heart of mice and men
    • Isensee, J., Witt, H., Pregla, R., Hetzer, R. et al., Sexually dimorphic gene expression in the heart of mice and men. J. Mol. Med. 2008, 86, 61-74.
    • (2008) J. Mol. Med. , vol.86 , pp. 61-74
    • Isensee, J.1    Witt, H.2    Pregla, R.3    Hetzer, R.4
  • 92
    • 0025034650 scopus 로고
    • Effects of gender and sex steroids on the immune response
    • Schuurs, A. H., Verheul, H. A., Effects of gender and sex steroids on the immune response. J. Steroid. Biochem. 1990, 35, 157-172. (Pubitemid 20067758)
    • (1990) Journal of Steroid Biochemistry , vol.35 , Issue.2 , pp. 157-172
    • Schuurs, A.H.W.M.1    Verheul, H.A.M.2
  • 93
    • 33746880282 scopus 로고    scopus 로고
    • Sexual dimorphism in innate immune responses to infectious organisms
    • DOI 10.1385/IR:34:3:177, PII IR343177
    • Marriott, I., Huet-Hudson, Y. M., Sexual dimorphism in innate immune responses to infectious organisms. Immunol. Res. 2006, 34, 177-192. (Pubitemid 44195935)
    • (2006) Immunologic Research , vol.34 , Issue.3 , pp. 177-192
    • Marriott, I.1    Huet-Hudson, Y.M.2
  • 94
    • 0034654329 scopus 로고    scopus 로고
    • Estrogen influences the differentiation, proliferation, and survival of early B-lineage precursors
    • Medina, K. L., Strasser, A., Kincade, P. W., Estrogen influences the differentiation, proliferation, and survival of early B-lineage precursors. Blood 2000, 95, 2059-2067. (Pubitemid 30151646)
    • (2000) Blood , vol.95 , Issue.6 , pp. 2059-2067
    • Medina, K.L.1    Strasser, A.2    Kincade, P.W.3
  • 95
    • 34247536306 scopus 로고    scopus 로고
    • Quantitative cellular and molecular analysis of the effect of progesterone withdrawal in a murine model of decidualization
    • DOI 10.1095/biolreprod.106.057950
    • Cheng, C. W., Bielby, H., Licence, D., Smith, S. K. et al., Quantitative cellular and molecular analysis of the effect of progesterone withdrawal in a murine model of decidualization. Biol. Reprod. 2007, 76, 871-883. (Pubitemid 46651228)
    • (2007) Biology of Reproduction , vol.76 , Issue.5 , pp. 871-883
    • Cheng, C.-W.1    Bielby, H.2    Licence, D.3    Smith, S.K.4    Print, C.G.5    Charnock-Jones, D.S.6
  • 96
    • 54349128377 scopus 로고    scopus 로고
    • Sex dimorphism in wound healing: The roles of sex steroids and macrophage migration inhibitory factor
    • Gilliver, S. C., Ruckshanthi, J. P., Hardman, M. J., Nakayama, T., Ashcroft, G. S., Sex dimorphism in wound healing: the roles of sex steroids and macrophage migration inhibitory factor. Endocrinology 2008, 149, 5747-5757.
    • (2008) Endocrinology , vol.149 , pp. 5747-5757
    • Gilliver, S.C.1    Ruckshanthi, J.P.2    Hardman, M.J.3    Nakayama, T.4    Ashcroft, G.S.5
  • 98
    • 0032928198 scopus 로고    scopus 로고
    • Estradiol suppresses type I collagen synthesis in mesangial cells via activation of activator protein-1
    • DOI 10.1046/j.1523-1755.1999.00376.x
    • Silbiger, S., Lei, J., Neugarten, J., Estradiol suppresses type I collagen synthesis in mesangial cells via activation of activator protein-1. Kidney Int. 1999, 55, 1268-1276. (Pubitemid 29157124)
    • (1999) Kidney International , vol.55 , Issue.4 , pp. 1268-1276
    • Silbiger, S.1    Lei, J.2    Neugarten, J.3
  • 99
    • 41449083289 scopus 로고    scopus 로고
    • Gender and human chronic renal disease
    • Silbiger, S., Neugarten, J., Gender and human chronic renal disease. Gend. Med. 2008, 5, S3-S10.
    • (2008) Gend. Med. , vol.5
    • Silbiger, S.1    Neugarten, J.2
  • 100
    • 19444383695 scopus 로고    scopus 로고
    • Effects of estradiol-17beta, testosterone and a black cohosh preparation on bone and prostate in orchidectomized rats
    • DOI 10.1016/j.maturitas.2004.07.007, PII S037851220400249X
    • Seidlova-Wuttke, D., Jarry, H., Pitzel, L., Wuttke, W., Effects of estradiol-17beta, testosterone and a black cohosh preparation on bone and prostate in orchidectomized rats. Maturitas 2005, 51, 177-186. (Pubitemid 40726117)
    • (2005) Maturitas , vol.51 , Issue.2 , pp. 177-186
    • Seidlova-Wuttke, D.1    Jarry, H.2    Pitzel, L.3    Wuttke, W.4
  • 101
    • 34848848209 scopus 로고    scopus 로고
    • Dihydrotestosterone stimulates proliferation and differentiation of fetal calvarial osteoblasts and dural cells and induces cranial suture fusion
    • DOI 10.1097/01.prs.0000279527.99734.bf, PII 0000653420071000000007
    • Lin, I. C., Slemp, A. E., Hwang, C., Sena-Esteves, M. et al., Dihydrotestosterone stimulates proliferation and differentiation of fetal calvarial osteoblasts and dural cells and induces cranial suture fusion. Plast. Reconstr. Surg. 2007, 120, 1137-1147. (Pubitemid 47493937)
    • (2007) Plastic and Reconstructive Surgery , vol.120 , Issue.5 , pp. 1137-1147
    • Lin, I.C.1    Slemp, A.E.2    Hwang, C.3    Sena-Esteves, M.4    Nah, H.-D.5    Kirschner, R.E.6
  • 103
    • 34247873129 scopus 로고    scopus 로고
    • 2 production and oxidative damage
    • DOI 10.1016/j.cardiores.2007.02.001, PII S0008636307000570
    • Colom, B., Oliver, J., Roca, P., Garcia-Palmer, F. J., Caloric restriction and gender modulate cardiac muscle mitochondrial H2O2 production and oxidative damage. Cardiovasc. Res. 2007, 74, 456-465. (Pubitemid 46693701)
    • (2007) Cardiovascular Research , vol.74 , Issue.3 , pp. 456-465
    • Colom, B.1    Oliver, J.2    Roca, P.3    Garcia-Palmer, F.J.4
  • 104
    • 53849088227 scopus 로고    scopus 로고
    • Transcriptional control of energy homeostasis by the estrogen-related receptors
    • Giguere, V., Transcriptional control of energy homeostasis by the estrogen-related receptors. Endocr. Rev. 2008, 29, 677-696.
    • (2008) Endocr. Rev. , vol.29 , pp. 677-696
    • Giguere, V.1
  • 106
    • 61749090415 scopus 로고    scopus 로고
    • Transcriptional analysis of estrogen effects in human embryonic neurons and glial cells
    • Csoregh, L., Andersson, E., Fried, G., Transcriptional analysis of estrogen effects in human embryonic neurons and glial cells. Neuroendocrinology 2009, 89, 171-186.
    • (2009) Neuroendocrinology , vol.89 , pp. 171-186
    • Csoregh, L.1    Andersson, E.2    Fried, G.3
  • 108
    • 38149075215 scopus 로고    scopus 로고
    • BMDExpress: A software tool for the benchmark dose analyses of genomic data
    • Yang, L., Allen, B. C., Thomas, R. S., BMDExpress: a software tool for the benchmark dose analyses of genomic data. BMC Genomics 2007, 8, 387.
    • (2007) BMC Genomics , vol.8 , pp. 387
    • Yang, L.1    Allen, B.C.2    Thomas, R.S.3
  • 110
    • 0037389501 scopus 로고    scopus 로고
    • Gene expression profile induced by 17 alpha-ethynyl estradiol in the prepubertal female reproductive system of the rat
    • Naciff, J. M., Overmann, G. J., Torontali, S. M., Carr, G. J. et al., Gene expression profile induced by 17 alpha-ethynyl estradiol in the prepubertal female reproductive system of the rat. Toxicol. Sci. 2003, 72, 314-330.
    • (2003) Toxicol. Sci. , vol.72 , pp. 314-330
    • Naciff, J.M.1    Overmann, G.J.2    Torontali, S.M.3    Carr, G.J.4
  • 113
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • DOI 10.1038/31275
    • Costanzi, C., Pehrson, J. R., Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 1998, 393, 599-601. (Pubitemid 28319252)
    • (1998) Nature , vol.393 , Issue.6685 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 114
    • 0348000613 scopus 로고    scopus 로고
    • Influence of age, sex, and strength training on human muscle gene expression determined by microarray
    • Roth, S. M., Ferrell, R. E., Peters, D. G., Metter, E. J. et al., Influence of age, sex, and strength training on human muscle gene expression determined by microarray. Physiol. Genomics 2002, 10, 181-190.
    • (2002) Physiol. Genomics , vol.10 , pp. 181-190
    • Roth, S.M.1    Ferrell, R.E.2    Peters, D.G.3    Metter, E.J.4
  • 115
    • 34548301709 scopus 로고    scopus 로고
    • Gender difference of androgen actions on skeletal muscle transcriptone
    • DOI 10.1677/JME-07-0027
    • Yoshioka, M., Boivin, A., Bolduc, C., St-Amand, J., Gender difference of androgen actions on skeletal muscle transcriptome. J. Mol. Endocrinol. 2007, 39, 119-133. (Pubitemid 47337871)
    • (2007) Journal of Molecular Endocrinology , vol.39 , Issue.1-2 , pp. 119-133
    • Yoshioka, M.1    Boivin, A.2    Bolduc, C.3    St-Amand, J.4
  • 116
    • 38949173060 scopus 로고    scopus 로고
    • Sex-related differences in gene expression in human skeletal muscle
    • DOI 10.1371/journal.pone.0001385
    • Welle, S., Tawil, R., Thornton, C. A., Sex-related differences in gene expression in human skeletal muscle. PLoS ONE 2008, 3, e1385. (Pubitemid 351223133)
    • (2008) PLoS ONE , vol.3 , Issue.1
    • Welle, S.1    Tawil, R.2    Thornton, C.A.3
  • 117
    • 47849089236 scopus 로고    scopus 로고
    • Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines
    • Golovan, S. P., Hakimov, H. A., Verschoor, C. P., Walters, S. et al., Analysis of Sus scrofa liver proteome and identification of proteins differentially expressed between genders, and conventional and genetically enhanced lines. Comp. Biochem. Physiol. D Genomics Proteomics 2008, 3, 234-242.
    • (2008) Comp. Biochem. Physiol. D Genomics Proteomics , vol.3 , pp. 234-242
    • Golovan, S.P.1    Hakimov, H.A.2    Verschoor, C.P.3    Walters, S.4
  • 118
    • 1542286872 scopus 로고    scopus 로고
    • Pharmacological zinc and phytase supplementation enhance metallothionein mRNA abundance and protein concentration in newly weaned pigs
    • Martinez, M. M., Hill, G. M., Link, J. E., Raney, N. E. et al., Pharmacological zinc and phytase supplementation enhance metallothionein mRNA abundance and protein concentration in newly weaned pigs. J. Nutr. 2004, 134, 538-544.
    • (2004) J. Nutr. , vol.134 , pp. 538-544
    • Martinez, M.M.1    Hill, G.M.2    Link, J.E.3    Raney, N.E.4
  • 119
    • 53749101270 scopus 로고    scopus 로고
    • Gene expression profiling in hepatic tissue of newly weaned pigs fed pharmacological zinc and phytase supplemented diets
    • Martinez-Montemayor, M. M., Hill, G. M., Raney, N. E., Rilington, V. D. et al., Gene expression profiling in hepatic tissue of newly weaned pigs fed pharmacological zinc and phytase supplemented diets. BMC Genomics 2008, 9, 421.
    • (2008) BMC Genomics , vol.9 , pp. 421
    • Martinez-Montemayor, M.M.1    Hill, G.M.2    Raney, N.E.3    Rilington, V.D.4
  • 121
    • 50049095281 scopus 로고    scopus 로고
    • Molecular characterization and expression patterns of AMP deaminase1 (AMPD1) in porcine skeletal muscle
    • Wang, L., Mo, X., Xu, Y., Zuo, B. et al., Molecular characterization and expression patterns of AMP deaminase1 (AMPD1) in porcine skeletal muscle. Comp. Biochem. Physiol. B Biochem. Mol. Biol. 2008, 151, 159-166.
    • (2008) Comp. Biochem. Physiol. B Biochem. Mol. Biol. , vol.151 , pp. 159-166
    • Wang, L.1    Mo, X.2    Xu, Y.3    Zuo, B.4
  • 123
    • 0036063842 scopus 로고    scopus 로고
    • Acyl-CoA binding protein expression is fiber type-specific and elevated in muscles from the obese insulin-resistant Zucker rat
    • Franch, J., Knudsen, J., Ellis, B. A., Pedersen, P. K. et al., Acyl-CoA-binding protein expression is fiber type- specific and elevated in muscles from the obese insulin-resistant Zucker rat. Diabetes 2002, 51, 449-454. (Pubitemid 34764802)
    • (2002) Diabetes , vol.51 , Issue.2 , pp. 449-454
    • Franch, J.1    Knudsen, J.2    Ellis, B.A.3    Pedersen, P.K.4    Cooney, G.J.5    Jensen, J.6
  • 124
    • 8744309971 scopus 로고    scopus 로고
    • Differential expression profiling of the proteomes and their mRNAs in porcine white and red skeletal muscles
    • Kim, N. K., Joh, J. H., Park, H. R., Kim, O. H. et al., Differential expression profiling of the proteomes and their mRNAs in porcine white and red skeletal muscles. Proteomics 2004, 4, 3422-3428.
    • (2004) Proteomics , vol.4 , pp. 3422-3428
    • Kim, N.K.1    Joh, J.H.2    Park, H.R.3    Kim, O.H.4
  • 127
    • 0030041946 scopus 로고    scopus 로고
    • Dietary Aspergillus niger phytase increases iron absorption in humans
    • Sandberg, A. S., Hulthen, L. R., Turk, M., Dietary Aspergillus niger phytase increases iron absorption in humans. J. Nutr. 1996, 126, 476-480. (Pubitemid 26055778)
    • (1996) Journal of Nutrition , vol.126 , Issue.2 , pp. 476-480
    • Sandberg, A.-S.1    Hulthen, L.R.2    Turk, M.3
  • 128
    • 0033176394 scopus 로고    scopus 로고
    • Phytase improves iron bioavailability for hemoglobin synthesis in young pigs
    • Stahl, C. H., Han, Y. M., Roneker, K. R., House, W. A., Lei, X. G., Phytase improves iron bioavailability for hemoglobin synthesis in young pigs. J. Anim. Sci. 1999, 77, 2135-2142.
    • (1999) J. Anim. Sci. , vol.77 , pp. 2135-2142
    • Stahl, C.H.1    Han, Y.M.2    Roneker, K.R.3    House, W.A.4    Lei, X.G.5


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