메뉴 건너뛰기




Volumn 54, Issue 1, 2013, Pages 1280-1286

Comparison of Milk Fat Globule Membrane (MFGM) proteins in milk samples of Chianina and Holstein cattle breeds across three lactation phases through 2D IEF SDS PAGE - A preliminary study

Author keywords

Cattle; IEF SDS PAGE; Lactation; MFGM; Milk proteomics

Indexed keywords

CATTLE; IEF-SDS PAGE; LACTATION; MFGM; PROTEOMICS;

EID: 84886283249     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2012.10.035     Document Type: Article
Times cited : (8)

References (71)
  • 1
    • 77950517341 scopus 로고    scopus 로고
    • Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome
    • Affolter M., Grass L., Vanrobaeys F., Casado B., Kussmann M. Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome. Journal of Proteomics 2010, 73:1079-1088.
    • (2010) Journal of Proteomics , vol.73 , pp. 1079-1088
    • Affolter, M.1    Grass, L.2    Vanrobaeys, F.3    Casado, B.4    Kussmann, M.5
  • 3
    • 0346037294 scopus 로고    scopus 로고
    • A proteome study of secreted prostatic factors affecting osteoblastic activity: Identification and characterisation of cyclophilin A
    • Andersen H., Jensen O.N., Eriksen E.F. A proteome study of secreted prostatic factors affecting osteoblastic activity: Identification and characterisation of cyclophilin A. European Journal of Cancer 2003, 39:989-995.
    • (2003) European Journal of Cancer , vol.39 , pp. 989-995
    • Andersen, H.1    Jensen, O.N.2    Eriksen, E.F.3
  • 4
    • 33748990292 scopus 로고    scopus 로고
    • Regulation and functional relevance of milk fat globules and their components in the mammary gland
    • Aoki N. Regulation and functional relevance of milk fat globules and their components in the mammary gland. Bioscience, Biotechnology, and Biochemistry 2006, 70:2019-2027.
    • (2006) Bioscience, Biotechnology, and Biochemistry , vol.70 , pp. 2019-2027
    • Aoki, N.1
  • 5
    • 67349259050 scopus 로고    scopus 로고
    • Regulation of costimulation in the era of butyrophilins
    • Arnett H.A., Escobara S.S., Viney S.L. Regulation of costimulation in the era of butyrophilins. Cytokine 2009, 46:370-375.
    • (2009) Cytokine , vol.46 , pp. 370-375
    • Arnett, H.A.1    Escobara, S.S.2    Viney, S.L.3
  • 6
    • 0026344545 scopus 로고
    • The cyclophilin multigene family of peptidylprolyl isomerases. Characterization of three separate human isoforms
    • Bergsma D.J., Eder C., Gross M., Kersten H., Sylvester D., Appelbaum E., et al. The cyclophilin multigene family of peptidylprolyl isomerases. Characterization of three separate human isoforms. Journal of Biological Chemistry 1991, 266:23204.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 23204
    • Bergsma, D.J.1    Eder, C.2    Gross, M.3    Kersten, H.4    Sylvester, D.5    Appelbaum, E.6
  • 8
    • 44449113267 scopus 로고    scopus 로고
    • ACSL1, AGPAT6, FABP3, LPIN1, and SLC27A6 are the most abundant isoforms in bovine mammary tissue and their expression is affected by stage of lactation 1-3
    • Bionaz M., Loor J.J. ACSL1, AGPAT6, FABP3, LPIN1, and SLC27A6 are the most abundant isoforms in bovine mammary tissue and their expression is affected by stage of lactation 1-3. Journal of Nutrition 2008, 138:1019-1024.
    • (2008) Journal of Nutrition , vol.138 , pp. 1019-1024
    • Bionaz, M.1    Loor, J.J.2
  • 9
    • 52249089184 scopus 로고    scopus 로고
    • Gene networks driving bovine milk fat synthesis during the lactation cycle
    • Bionaz M., Loor J.J. Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics 2008, 9:366.
    • (2008) BMC Genomics , vol.9 , pp. 366
    • Bionaz, M.1    Loor, J.J.2
  • 10
    • 0020071441 scopus 로고
    • Characteristics of membrane-bound and soluble forms of xanthine oxidase from milk and endothelial cells of capillaries
    • Bruder G., Heid H., Jarasch E.D., Keenan T.W., Mather I.H. Characteristics of membrane-bound and soluble forms of xanthine oxidase from milk and endothelial cells of capillaries. Biochimica et Biophysica Acta 1982, 701:357-369.
    • (1982) Biochimica et Biophysica Acta , vol.701 , pp. 357-369
    • Bruder, G.1    Heid, H.2    Jarasch, E.D.3    Keenan, T.W.4    Mather, I.H.5
  • 11
    • 0035487930 scopus 로고    scopus 로고
    • Mammary cell number, proliferation, and apoptosis during a bovine lactation: Relation to milk production and effect of bST
    • Capuco A.V., Wood D.L., Baldwin R., Mcleod K., Paape M.J. Mammary cell number, proliferation, and apoptosis during a bovine lactation: Relation to milk production and effect of bST. Journal of Dairy Science 2001, 84(10):2177-2187.
    • (2001) Journal of Dairy Science , vol.84 , Issue.10 , pp. 2177-2187
    • Capuco, A.V.1    Wood, D.L.2    Baldwin, R.3    Mcleod, K.4    Paape, M.J.5
  • 13
    • 0034668791 scopus 로고    scopus 로고
    • Mitochondrial intermembrane junctional complexes and their role in cell death
    • Crompton M. Mitochondrial intermembrane junctional complexes and their role in cell death. The Journal of Physiology 2000, 529:11.
    • (2000) The Journal of Physiology , vol.529 , pp. 11
    • Crompton, M.1
  • 16
    • 77954379514 scopus 로고    scopus 로고
    • Human milk proteins: an interactomics and updated functional overview
    • D'Alessandro A., Scaloni A., Zolla L. Human milk proteins: an interactomics and updated functional overview. Journal of Proteome Research 2010, 9:3339-3373.
    • (2010) Journal of Proteome Research , vol.9 , pp. 3339-3373
    • D'Alessandro, A.1    Scaloni, A.2    Zolla, L.3
  • 17
    • 79951640840 scopus 로고    scopus 로고
    • The bovine milk proteome: cherishing, nourishing and fostering molecular complexity. An interactomics and functional overview
    • D'Alessandro A., Zolla L., Scaloni A. The bovine milk proteome: cherishing, nourishing and fostering molecular complexity. An interactomics and functional overview. Molecular Biosystems 2010, 7:579-597.
    • (2010) Molecular Biosystems , vol.7 , pp. 579-597
    • D'Alessandro, A.1    Zolla, L.2    Scaloni, A.3
  • 18
    • 33751089054 scopus 로고    scopus 로고
    • Proteomic analysis of the mouse mammary gland is a powerful tool to identify novel proteins that are differentially expressed during mammary development
    • Davies C.R., Morris V., Griffiths V., Page V., Pitt A., Stein T., et al. Proteomic analysis of the mouse mammary gland is a powerful tool to identify novel proteins that are differentially expressed during mammary development. Proteomics 2006, 6:5694-5704.
    • (2006) Proteomics , vol.6 , pp. 5694-5704
    • Davies, C.R.1    Morris, V.2    Griffiths, V.3    Page, V.4    Pitt, A.5    Stein, T.6
  • 19
    • 0033117463 scopus 로고    scopus 로고
    • Over-expression of the murine polymeric immunoglobulin receptor gene in the mammary gland of transgenic mice
    • De Groot N., Van Kuik-Romeijn P., Lee S.H., de Boer A.H. Over-expression of the murine polymeric immunoglobulin receptor gene in the mammary gland of transgenic mice. Transgenic Research 1999, 8:125-135.
    • (1999) Transgenic Research , vol.8 , pp. 125-135
    • De Groot, N.1    Van Kuik-Romeijn, P.2    Lee, S.H.3    de Boer, A.H.4
  • 20
    • 70350354688 scopus 로고    scopus 로고
    • Phosphorylation of perilipin is associated with indicators of lipolysis in Holstein cows
    • Elkins D.A., Spurlock D.M. Phosphorylation of perilipin is associated with indicators of lipolysis in Holstein cows. Hormone and Metabolism Research 2009, 41:736-740.
    • (2009) Hormone and Metabolism Research , vol.41 , pp. 736-740
    • Elkins, D.A.1    Spurlock, D.M.2
  • 21
    • 79952201523 scopus 로고    scopus 로고
    • Dimensional analysis of milk fat globules in sowmilk: Effects of the lactation stage and fat content and comparison with vaccine milk
    • Faustini M., Colombani C., Vigo D., Communod R., Russo V., Chlapanidas T. Dimensional analysis of milk fat globules in sowmilk: Effects of the lactation stage and fat content and comparison with vaccine milk. Veterinary Research Community 2010, 34(1):29-32.
    • (2010) Veterinary Research Community , vol.34 , Issue.1 , pp. 29-32
    • Faustini, M.1    Colombani, C.2    Vigo, D.3    Communod, R.4    Russo, V.5    Chlapanidas, T.6
  • 22
    • 67650909307 scopus 로고    scopus 로고
    • Quantification of milk fat globule membrane proteins using selected reaction monitoring mass spectrometry
    • Fong B.Y., Norris C.S. Quantification of milk fat globule membrane proteins using selected reaction monitoring mass spectrometry. Journal of Agriculture and Food Chemistry 2009, 57:6021-6028.
    • (2009) Journal of Agriculture and Food Chemistry , vol.57 , pp. 6021-6028
    • Fong, B.Y.1    Norris, C.S.2
  • 23
    • 0028276439 scopus 로고
    • Immunophilins in protein folding and immunosuppression
    • Fruman D.A., Burakoff S.J., Bierer B.E. Immunophilins in protein folding and immunosuppression. The FASEB Journal 1994, 8:391-400.
    • (1994) The FASEB Journal , vol.8 , pp. 391-400
    • Fruman, D.A.1    Burakoff, S.J.2    Bierer, B.E.3
  • 24
    • 0027363385 scopus 로고
    • Peptidylproline cis-trans-isomerases: Immunophilins
    • Galat A. Peptidylproline cis-trans-isomerases: Immunophilins. European Journal of Biochemistry 1993, 216:689.
    • (1993) European Journal of Biochemistry , vol.216 , pp. 689
    • Galat, A.1
  • 27
    • 28044440907 scopus 로고    scopus 로고
    • Impaired involution of mammary glands in the absence of milk fat globule EGF factor 8
    • Hanayam R., Nagata S. Impaired involution of mammary glands in the absence of milk fat globule EGF factor 8. Proceedings of the National Academy of Sciences 2005, 102:16886-16891.
    • (2005) Proceedings of the National Academy of Sciences , vol.102 , pp. 16886-16891
    • Hanayam, R.1    Nagata, S.2
  • 29
    • 2442665179 scopus 로고    scopus 로고
    • Autoimmune disease and impaired uptake of apoptotic cells in MFGE8-deficient mice
    • Hanayama R., Tanaka M., Miyasaka K., Aozasa K., Koike M., Uchiyama Y., et al. Autoimmune disease and impaired uptake of apoptotic cells in MFGE8-deficient mice. Science 2004, 304:1147-1150.
    • (2004) Science , vol.304 , pp. 1147-1150
    • Hanayama, R.1    Tanaka, M.2    Miyasaka, K.3    Aozasa, K.4    Koike, M.5    Uchiyama, Y.6
  • 30
    • 0030469694 scopus 로고    scopus 로고
    • Adipocyte differentiation-related protein is secreted into milk as a constituent of milk lipid globule membrane
    • Heid H.W., Schnolzer H.M., Keenan T.W. Adipocyte differentiation-related protein is secreted into milk as a constituent of milk lipid globule membrane. Biochemical Journal 1996, 320:1025-1030.
    • (1996) Biochemical Journal , vol.320 , pp. 1025-1030
    • Heid, H.W.1    Schnolzer, H.M.2    Keenan, T.W.3
  • 31
    • 84886277051 scopus 로고    scopus 로고
    • FAO
    • Last accessed on April 14, 2012)
    • Henriksen J. FAO. Milk for health and wealth 2009, (ftp://ftp.fao.org/docrep/fao/011/i0521e/i0521e00.pdf Last accessed on April 14, 2012).
    • (2009) Milk for health and wealth
    • Henriksen, J.1
  • 32
    • 0021986254 scopus 로고
    • Cell antigen receptors and the immunoglobulin gene family
    • Hood L., Kronemberg M., Hunkapiller T.T. Cell antigen receptors and the immunoglobulin gene family. Cell 1985, 40:225-229.
    • (1985) Cell , vol.40 , pp. 225-229
    • Hood, L.1    Kronemberg, M.2    Hunkapiller, T.T.3
  • 33
    • 0024675579 scopus 로고
    • Mammary gland function during involution
    • Hurley W.L. Mammary gland function during involution. Journal of Dairy Science 1989, 72:1637-1646.
    • (1989) Journal of Dairy Science , vol.72 , pp. 1637-1646
    • Hurley, W.L.1
  • 34
    • 77955712890 scopus 로고    scopus 로고
    • Alterations in coagulation parameters in dairy cows affected with acute mastitis caused by E. coli and S. aureus pathogens
    • Ismail Z.A., Dickinson C. Alterations in coagulation parameters in dairy cows affected with acute mastitis caused by E. coli and S. aureus pathogens. Veterinary Research Community 2010, 34:533-539.
    • (2010) Veterinary Research Community , vol.34 , pp. 533-539
    • Ismail, Z.A.1    Dickinson, C.2
  • 35
    • 0025102648 scopus 로고
    • Cloning and analysis of cDNA encoding bovine butyrophilin, an apical glycoprotein expressed in mammary tissue and secreted in association with the milk-fat globule membrane during lactation
    • Jack L.J., Mather I.H. Cloning and analysis of cDNA encoding bovine butyrophilin, an apical glycoprotein expressed in mammary tissue and secreted in association with the milk-fat globule membrane during lactation. Journal of Biological Chemistry 1990, 265:14481-14486.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 14481-14486
    • Jack, L.J.1    Mather, I.H.2
  • 36
    • 0034721931 scopus 로고    scopus 로고
    • Cyclophilin A is a secreted growth factor induced by oxidative stress
    • Jin Z.G., Melaragno M.G., Liao D.F. Cyclophilin A is a secreted growth factor induced by oxidative stress. Circulation Research 2000, 87:789-796.
    • (2000) Circulation Research , vol.87 , pp. 789-796
    • Jin, Z.G.1    Melaragno, M.G.2    Liao, D.F.3
  • 37
    • 0027658739 scopus 로고
    • Functional characteristics of dairy proteins
    • Jost R. Functional characteristics of dairy proteins. Trends in Food Science and Technology 1993, 4:283-288.
    • (1993) Trends in Food Science and Technology , vol.4 , pp. 283-288
    • Jost, R.1
  • 38
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • Khofron J.L., Kuzmic P., Kishore V., Colon-Bonilla E., Rich D.H. Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 1991, 30:6127.
    • (1991) Biochemistry , vol.30 , pp. 6127
    • Khofron, J.L.1    Kuzmic, P.2    Kishore, V.3    Colon-Bonilla, E.4    Rich, D.H.5
  • 39
    • 0026469077 scopus 로고
    • Molecular and cellular basis of immune protection of mucosal surfaces
    • Kraehenbuhl J.P., Neutra M.R. Molecular and cellular basis of immune protection of mucosal surfaces. Physiological Reviews 1992, 72:853-879.
    • (1992) Physiological Reviews , vol.72 , pp. 853-879
    • Kraehenbuhl, J.P.1    Neutra, M.R.2
  • 40
    • 0034633725 scopus 로고    scopus 로고
    • Interaction of β-lactoglobulin with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy
    • Lefevre T., Subirade M. Interaction of β-lactoglobulin with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy. International Journal of Biology and Macromolecules 2000, 28:59-67.
    • (2000) International Journal of Biology and Macromolecules , vol.28 , pp. 59-67
    • Lefevre, T.1    Subirade, M.2
  • 42
    • 0027245483 scopus 로고
    • FK506 and cyclosporin, molecular probes for studying intracellular signal transduction
    • Liu J. FK506 and cyclosporin, molecular probes for studying intracellular signal transduction. Immunology Today 1993, 14:290-295.
    • (1993) Immunology Today , vol.14 , pp. 290-295
    • Liu, J.1
  • 44
    • 0029916122 scopus 로고    scopus 로고
    • A human peptidyl-prolyl isomerase essential for regulation of mitosis
    • Lu K.P., Hanes S.D., Hunter T. A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 1996, 380:544-547.
    • (1996) Nature , vol.380 , pp. 544-547
    • Lu, K.P.1    Hanes, S.D.2    Hunter, T.3
  • 45
    • 1542329604 scopus 로고    scopus 로고
    • Tolerance induction by molecular mimicry: Prevention and suppression of experimental autoimmune encephalomyelitis with the milk protein butyrophilin
    • Mana P., Goodyear M., Bernard C., Tomioka R., Freire-Garabal M., Linares D. Tolerance induction by molecular mimicry: Prevention and suppression of experimental autoimmune encephalomyelitis with the milk protein butyrophilin. International Immunology 2004, 16:489-499.
    • (2004) International Immunology , vol.16 , pp. 489-499
    • Mana, P.1    Goodyear, M.2    Bernard, C.3    Tomioka, R.4    Freire-Garabal, M.5    Linares, D.6
  • 46
    • 75949088794 scopus 로고    scopus 로고
    • Differential expression of liver proteins in Chianina and Holstein young bulls
    • Miarelli M., Signorelli F. Differential expression of liver proteins in Chianina and Holstein young bulls. Journal of Animal Science 2010, 88:593-598.
    • (2010) Journal of Animal Science , vol.88 , pp. 593-598
    • Miarelli, M.1    Signorelli, F.2
  • 47
    • 0028202474 scopus 로고
    • Transepithelial transport of immunoglobulins
    • Mostov K.E. Transepithelial transport of immunoglobulins. Annual Review of Immunology 1994, 12:63-84.
    • (1994) Annual Review of Immunology , vol.12 , pp. 63-84
    • Mostov, K.E.1
  • 48
    • 84859645899 scopus 로고    scopus 로고
    • Comparison of milk fat globule membrane (MFGM) proteins of Chianina and Holstein cattle breed milk samples through proteomics methods
    • Murgiano L., Timperio A.M., Zolla L., Bongiorni S., Valentini A., Pariset L. Comparison of milk fat globule membrane (MFGM) proteins of Chianina and Holstein cattle breed milk samples through proteomics methods. Nutrients 2009, 1(2):302-315.
    • (2009) Nutrients , vol.1 , Issue.2 , pp. 302-315
    • Murgiano, L.1    Timperio, A.M.2    Zolla, L.3    Bongiorni, S.4    Valentini, A.5    Pariset, L.6
  • 49
    • 33645581647 scopus 로고    scopus 로고
    • Weaning-induced expression of a milk-fat globule protein, MFG-E8, in mouse mammary glands as demonstrated by the analyses of its mRNA, protein and phosphatidylserine-binding activity
    • Nakatani H., Aoki N., Nakagawa Y., Jin-No S., Aoyama K., Oshima K., et al. Weaning-induced expression of a milk-fat globule protein, MFG-E8, in mouse mammary glands as demonstrated by the analyses of its mRNA, protein and phosphatidylserine-binding activity. Biochemical Journal 2006, 395:21-30.
    • (2006) Biochemical Journal , vol.395 , pp. 21-30
    • Nakatani, H.1    Aoki, N.2    Nakagawa, Y.3    Jin-No, S.4    Aoyama, K.5    Oshima, K.6
  • 50
    • 18344374733 scopus 로고    scopus 로고
    • Innate immunity and human milk
    • Newburg D.S. Innate immunity and human milk. Journal of Nutrition 2005, 135(5):1308-1312.
    • (2005) Journal of Nutrition , vol.135 , Issue.5 , pp. 1308-1312
    • Newburg, D.S.1
  • 53
    • 64149114905 scopus 로고    scopus 로고
    • Secreted cyclophilin A, a peptidylprolyl cis-trans isomerase, mediates matrix assembly of hensin, a protein implicated in epithelial differentiation
    • Peng H., Vijayakumar S., Schiene-Fischer C. Secreted cyclophilin A, a peptidylprolyl cis-trans isomerase, mediates matrix assembly of hensin, a protein implicated in epithelial differentiation. Journal of Biological Chemistry 2009, 284:6465-6475.
    • (2009) Journal of Biological Chemistry , vol.284 , pp. 6465-6475
    • Peng, H.1    Vijayakumar, S.2    Schiene-Fischer, C.3
  • 54
    • 0031697191 scopus 로고    scopus 로고
    • Milk fat globule glycoproteins in human milk and in gastric aspirates of mother's milk-fed preterm infants
    • Peterson J.A., Hamosh M., Scallan C.D., Ceriani R.L., Henderson T.R., Mehta N., et al. Milk fat globule glycoproteins in human milk and in gastric aspirates of mother's milk-fed preterm infants. Pediatric Research 1998, 44:499-506.
    • (1998) Pediatric Research , vol.44 , pp. 499-506
    • Peterson, J.A.1    Hamosh, M.2    Scallan, C.D.3    Ceriani, R.L.4    Henderson, T.R.5    Mehta, N.6
  • 56
    • 70449637041 scopus 로고    scopus 로고
    • Human proteome enhancement: High-recovery method and improved two-dimensional map of colostral fat globule membrane proteins
    • Quaranta S., Giuffrida M.G., Cavaletto M., Giunta C., Godovac- Zimmermann J., Canas B., et al. Human proteome enhancement: High-recovery method and improved two-dimensional map of colostral fat globule membrane proteins. Electrophoresis 2001, 22:1810-1818.
    • (2001) Electrophoresis , vol.22 , pp. 1810-1818
    • Quaranta, S.1    Giuffrida, M.G.2    Cavaletto, M.3    Giunta, C.4    Godovac-Zimmermann, J.5    Canas, B.6
  • 58
    • 44949253954 scopus 로고    scopus 로고
    • Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk
    • Reinhardt T.A., Lippolis J.D. Developmental changes in the milk fat globule membrane proteome during the transition from colostrum to milk. Journal of Dairy Science 2008, 91:2307-2318.
    • (2008) Journal of Dairy Science , vol.91 , pp. 2307-2318
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 59
    • 1042272548 scopus 로고    scopus 로고
    • The housekeeping genes GAPDH and cyclophilin are regulated by metabolic state in the liver of dairy cows
    • Rhoads R.P. The housekeeping genes GAPDH and cyclophilin are regulated by metabolic state in the liver of dairy cows. Journal of Dairy Science 2003, 86:3423-3429.
    • (2003) Journal of Dairy Science , vol.86 , pp. 3423-3429
    • Rhoads, R.P.1
  • 62
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Analytical Chemistry 1996, 68:850-858.
    • (1996) Analytical Chemistry , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 63
    • 44949123534 scopus 로고    scopus 로고
    • CDNA microarray analysis reveals that antioxidant and immune genes are upregulated during involution of the bovine mammary gland
    • Singh K., Davis S.R., Dobson J.M., Molenaar A.M., Wheeler T.T., Prosser C.G., et al. cDNA microarray analysis reveals that antioxidant and immune genes are upregulated during involution of the bovine mammary gland. Journal of Dairy Science 2008, 91:2236-2246.
    • (2008) Journal of Dairy Science , vol.91 , pp. 2236-2246
    • Singh, K.1    Davis, S.R.2    Dobson, J.M.3    Molenaar, A.M.4    Wheeler, T.T.5    Prosser, C.G.6
  • 64
    • 77951633576 scopus 로고    scopus 로고
    • BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of T cell activation
    • Smith I.A., Knezevic B.R., Ammann J.U., Rhodes D.A., Aw D., Palmer D.B., et al. BTN1A1, the mammary gland butyrophilin, and BTN2A2 are both inhibitors of T cell activation. Journal of Immunology 2010, 184(7):3514-3525.
    • (2010) Journal of Immunology , vol.184 , Issue.7 , pp. 3514-3525
    • Smith, I.A.1    Knezevic, B.R.2    Ammann, J.U.3    Rhodes, D.A.4    Aw, D.5    Palmer, D.B.6
  • 65
    • 70449519266 scopus 로고    scopus 로고
    • Comparative proteomics and transcriptomics analyses of livers from two different Bos taurus breeds: "Chianina and Holstein Friesian"
    • Timperio A.M., D'Alessandro A., Pariset L., D'Amici G.M., Valentini A., Zolla L. Comparative proteomics and transcriptomics analyses of livers from two different Bos taurus breeds: "Chianina and Holstein Friesian". Journal of Proteomics 2009, 73:309-322.
    • (2009) Journal of Proteomics , vol.73 , pp. 309-322
    • Timperio, A.M.1    D'Alessandro, A.2    Pariset, L.3    D'Amici, G.M.4    Valentini, A.5    Zolla, L.6
  • 68
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D., Flügge U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Analytical Biochemistry 1984, 138:141-143.
    • (1984) Analytical Biochemistry , vol.138 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 71
    • 68949206485 scopus 로고    scopus 로고
    • The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli type 1
    • Yu S., Lowe A.W. The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli type 1. BCM Gastroenterology 2009, 9:58.
    • (2009) BCM Gastroenterology , vol.9 , pp. 58
    • Yu, S.1    Lowe, A.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.