메뉴 건너뛰기




Volumn 72, Issue 5, 2009, Pages 853-864

Solubilization methods and reference 2-DE map of cow milk fat globules

Author keywords

2 D electrophoresis; Aqueous phase; Crescent; Delipidation; Milk fat globule; Protein solubilization

Indexed keywords

5' NUCLEOTIDASE; ACTIN; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; ADIPOPHILIN; ALCOHOL DEHYDROGENASE; AUTOTAXIN; CALCIUM BINDING PROTEIN; CD14 ANTIGEN; FATTY ACID BINDING PROTEIN; FATTY ACID SYNTHASE; GELSOLIN; GLYCEROL 3 PHOSPHATE DEHYDROGENASE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; HEAT SHOCK PROTEIN; ISOCITRATE DEHYDROGENASE; LACTADHERIN; LACTOFERRIN; LIPOCORTIN 2; MALATE DEHYDROGENASE; MILK FAT; MILK PROTEIN; PEPTIDYLPROLYL ISOMERASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN P22; PYRIDOXAL KINASE; TRYPTOPHAN TRANSFER RNA LIGASE; VALOSIN CONTAINING PROTEIN; XANTHINE DEHYDROGENASE; XANTHINE OXIDASE;

EID: 67649547215     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2008.11.020     Document Type: Article
Times cited : (44)

References (91)
  • 1
    • 0015148571 scopus 로고
    • The mechanism of secretion of the milk fat globule
    • Wooding F.B.P. The mechanism of secretion of the milk fat globule. J Cell Sci 9 3 (Nov 1971) 805-821
    • (1971) J Cell Sci , vol.9 , Issue.3 , pp. 805-821
    • Wooding, F.B.P.1
  • 3
    • 0002946615 scopus 로고
    • The structure of milk: implication for sampling and storage. The milk lipid globule membrane
    • Jensen R.G. (Ed), Academic Press, San Diego
    • Keenan T.W., and Patton S. The structure of milk: implication for sampling and storage. The milk lipid globule membrane. In: Jensen R.G. (Ed). Handbook of milk composition (1995), Academic Press, San Diego 5-62
    • (1995) Handbook of milk composition , pp. 5-62
    • Keenan, T.W.1    Patton, S.2
  • 4
    • 0033769564 scopus 로고    scopus 로고
    • Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells
    • Wu C.C., Howell K.E., Neville M.C., Yates III J.R., and McManaman J.L. Proteomics reveal a link between the endoplasmic reticulum and lipid secretory mechanisms in mammary epithelial cells. Electrophoresis 21 16 (Oct 2000) 3470-3482
    • (2000) Electrophoresis , vol.21 , Issue.16 , pp. 3470-3482
    • Wu, C.C.1    Howell, K.E.2    Neville, M.C.3    Yates III, J.R.4    McManaman, J.L.5
  • 5
    • 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. Biosci Biotechnol Biochem 70 9 (Sep 2006) 2019-2027
    • (2006) Biosci Biotechnol Biochem , vol.70 , Issue.9 , pp. 2019-2027
    • Aoki, N.1
  • 7
    • 14844345210 scopus 로고    scopus 로고
    • Intracellular origin and secretion of milk fat globules
    • Heid H.W., and Keenan T.W. Intracellular origin and secretion of milk fat globules. Eur J Cell Biol 84 2-3 (Mar 2005) 245-258
    • (2005) Eur J Cell Biol , vol.84 , Issue.2-3 , pp. 245-258
    • Heid, H.W.1    Keenan, T.W.2
  • 9
    • 0014959578 scopus 로고
    • Theories of milk secretion: evidence from e electron microscopic examination of milk
    • Wooding F.B., Peaker M., and Linzell J.L. Theories of milk secretion: evidence from e electron microscopic examination of milk. Nature 226 5247 (May 23 1970) 762-764
    • (1970) Nature , vol.226 , Issue.5247 , pp. 762-764
    • Wooding, F.B.1    Peaker, M.2    Linzell, J.L.3
  • 10
    • 0025472539 scopus 로고
    • Factors related to the formation of cytoplasmic crescents on milk fat globules
    • Huston G.E., and Patton S. Factors related to the formation of cytoplasmic crescents on milk fat globules. J Dairy Sci 73 8 (Aug 1990) 2061-2066
    • (1990) J Dairy Sci , vol.73 , Issue.8 , pp. 2061-2066
    • Huston, G.E.1    Patton, S.2
  • 11
    • 84934439187 scopus 로고    scopus 로고
    • Milk fat globule membrane components-a proteomic approach
    • Cavaletto M., Giuffrida M.G., and Conti A. Milk fat globule membrane components-a proteomic approach. Adv Exp Med Biol 606 (2008) 129-141
    • (2008) Adv Exp Med Biol , vol.606 , pp. 129-141
    • Cavaletto, M.1    Giuffrida, M.G.2    Conti, A.3
  • 13
    • 33845972952 scopus 로고    scopus 로고
    • Protein and lipid composition of bovine milk-fat-globule membrane
    • Fong B.Y., Norris C.S., and MacGibbon A.K.H. Protein and lipid composition of bovine milk-fat-globule membrane. Int Dairy J 17 4 (Apr 2007) 275-288
    • (2007) Int Dairy J , vol.17 , Issue.4 , pp. 275-288
    • Fong, B.Y.1    Norris, C.S.2    MacGibbon, A.K.H.3
  • 14
    • 33750362923 scopus 로고    scopus 로고
    • Bovine milk fat globule membrane proteome
    • Reinhardt T.A., and Lippolis J.D. Bovine milk fat globule membrane proteome. J Dairy Res 73 4 (Nov 2006) 406-416
    • (2006) J Dairy Res , vol.73 , Issue.4 , pp. 406-416
    • Reinhardt, T.A.1    Lippolis, J.D.2
  • 15
    • 0030973737 scopus 로고    scopus 로고
    • Two-dimensional electrophoretic analysis of human milk-fat-globule membrane proteins with attention to apolipoprotein E patterns
    • Goldfarb M. Two-dimensional electrophoretic analysis of human milk-fat-globule membrane proteins with attention to apolipoprotein E patterns. Electrophoresis 18 3-4 (Mar-Apr 1997) 511-515
    • (1997) Electrophoresis , vol.18 , Issue.3-4 , pp. 511-515
    • Goldfarb, M.1
  • 16
    • 34248598796 scopus 로고    scopus 로고
    • Trends in sample preparation for classical and second generation proteomics
    • Cañas B., Piñeiro C., Calvo E., López-Ferrer D., and Gallardo J.M. Trends in sample preparation for classical and second generation proteomics. J Chromatogr A 1153 1-2 (Jun 15 2007) 235-258
    • (2007) J Chromatogr A , vol.1153 , Issue.1-2 , pp. 235-258
    • Cañas, B.1    Piñeiro, C.2    Calvo, E.3    López-Ferrer, D.4    Gallardo, J.M.5
  • 17
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Görg A., Weiss W., and Dunn M.J. Current two-dimensional electrophoresis technology for proteomics. Proteomics 4 12 (Dec 2004) 3665-3685
    • (2004) Proteomics , vol.4 , Issue.12 , pp. 3665-3685
    • Görg, A.1    Weiss, W.2    Dunn, M.J.3
  • 18
    • 0022415466 scopus 로고
    • Identification of the milk fat globule membrane proteins. II. Isolation of major proteins from electrophoretic gels and comparison of their amino acid compositions
    • Basch J.J., Greenberg R., and Farrell Jr. H.M. Identification of the milk fat globule membrane proteins. II. Isolation of major proteins from electrophoretic gels and comparison of their amino acid compositions. Biochim Biophys Acta 830 2 (Aug 8 1985) 127-135
    • (1985) Biochim Biophys Acta , vol.830 , Issue.2 , pp. 127-135
    • Basch, J.J.1    Greenberg, R.2    Farrell Jr., H.M.3
  • 19
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel D., and Flügge U.I. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 138 1 (Apr 1984) 141-143
    • (1984) Anal Biochem , vol.138 , Issue.1 , pp. 141-143
    • Wessel, D.1    Flügge, U.I.2
  • 20
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (May 7 1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 21
    • 0027763435 scopus 로고
    • A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale
    • Blellqvist B., Pasquali C., Ravier F., Sanchez J.C., and Hochstrasser D. A nonlinear wide-range immobilized pH gradient for two-dimensional electrophoresis and its definition in a relevant pH scale. Electrophoresis 14 12 (Dec 1993) 1357-1365
    • (1993) Electrophoresis , vol.14 , Issue.12 , pp. 1357-1365
    • Blellqvist, B.1    Pasquali, C.2    Ravier, F.3    Sanchez, J.C.4    Hochstrasser, D.5
  • 22
    • 0023768475 scopus 로고
    • The current state of two-dimensional electrophoresis with immobilized pH gradients
    • Görg A., Postel W., and Günther S. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 9 9 (Sep 1988) 531-546
    • (1988) Electrophoresis , vol.9 , Issue.9 , pp. 531-546
    • Görg, A.1    Postel, W.2    Günther, S.3
  • 24
    • 0023676995 scopus 로고
    • Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining
    • Hochstrasser D., Patchornik A., and Merril C.R. Development of polyacrylamide gels that improve the separation of proteins and their detection by silver staining. Anal Biochem 173 2 (Sep 1988) 412-423
    • (1988) Anal Biochem , vol.173 , Issue.2 , pp. 412-423
    • Hochstrasser, D.1    Patchornik, A.2    Merril, C.R.3
  • 25
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley B.R., Kirsch D.R., and Morris N.R. A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal Biochem 105 2 (Jul 1 1980) 361-363
    • (1980) Anal Biochem , vol.105 , Issue.2 , pp. 361-363
    • Oakley, B.R.1    Kirsch, D.R.2    Morris, N.R.3
  • 26
    • 0035403371 scopus 로고    scopus 로고
    • A new silver staining apparatus and procedure for matrix-assisted laser desorption/ionization-time of flight analysis of proteins after two-dimensional electrophoresis
    • Sinha P., Poland J., Schnolzer M., and Rabilloud T. A new silver staining apparatus and procedure for matrix-assisted laser desorption/ionization-time of flight analysis of proteins after two-dimensional electrophoresis. Proteomics 1 7 (Jul 2001) 835-840
    • (2001) Proteomics , vol.1 , Issue.7 , pp. 835-840
    • Sinha, P.1    Poland, J.2    Schnolzer, M.3    Rabilloud, T.4
  • 27
    • 0027521381 scopus 로고
    • The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences
    • Bjellqvist B., Hughes G.J., Pasquali C., Paquet N., Ravier F., Sanchez J.C., et al. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14 (1993) 1023-1031
    • (1993) Electrophoresis , vol.14 , pp. 1023-1031
    • Bjellqvist, B.1    Hughes, G.J.2    Pasquali, C.3    Paquet, N.4    Ravier, F.5    Sanchez, J.C.6
  • 28
    • 34248638482 scopus 로고    scopus 로고
    • Protein expression profiles of Bos taurus blood and lymphatic vessel endothelial cells
    • Bianchi L., Lorenzoni P., Bini L., Weber E., Tani C., Rossi A., et al. Protein expression profiles of Bos taurus blood and lymphatic vessel endothelial cells. Proteomics 7 (2007) 1434-1445
    • (2007) Proteomics , vol.7 , pp. 1434-1445
    • Bianchi, L.1    Lorenzoni, P.2    Bini, L.3    Weber, E.4    Tani, C.5    Rossi, A.6
  • 29
    • 0028983813 scopus 로고
    • Improvement of an "in-gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing
    • Hellman U., Wernstedt C., Gonez J., and Heldin C.H. Improvement of an "in-gel" digestion procedure for the micropreparation of internal protein fragments for amino acid sequencing. Anal Biochem 224 1 (Jan 1 1995) 451-455
    • (1995) Anal Biochem , vol.224 , Issue.1 , pp. 451-455
    • Hellman, U.1    Wernstedt, C.2    Gonez, J.3    Heldin, C.H.4
  • 30
    • 0039846981 scopus 로고    scopus 로고
    • Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor
    • Soskic V., Gorlach M., Poznanovic S., Boehmer F.D., and Godovac-Zimmermann J. Functional proteomics analysis of signal transduction pathways of the platelet-derived growth factor beta receptor. Biochemistry 38 6 (Feb 9 1999) 1757-1764
    • (1999) Biochemistry , vol.38 , Issue.6 , pp. 1757-1764
    • Soskic, V.1    Gorlach, M.2    Poznanovic, S.3    Boehmer, F.D.4    Godovac-Zimmermann, J.5
  • 31
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity
    • Gharahdaghi F., Weimberg C.R., Meagher D.A., Imai B.S., and Mische S.M. Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis 20 3 (Mar 1999) 601-605
    • (1999) Electrophoresis , vol.20 , Issue.3 , pp. 601-605
    • Gharahdaghi, F.1    Weimberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5
  • 33
    • 0036665518 scopus 로고    scopus 로고
    • Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry
    • Blonder J., Goshe M.B., Moore R.J., Pasa-Tolic L., Masselon C.D., Lipton M.S., et al. Enrichment of integral membrane proteins for proteomic analysis using liquid chromatography-tandem mass spectrometry. J Proteome Res 1 4 (Jul-Aug 2002) 351-360
    • (2002) J Proteome Res , vol.1 , Issue.4 , pp. 351-360
    • Blonder, J.1    Goshe, M.B.2    Moore, R.J.3    Pasa-Tolic, L.4    Masselon, C.D.5    Lipton, M.S.6
  • 34
    • 49049090526 scopus 로고    scopus 로고
    • Review of a current role of mass spectrometry for proteome research
    • Chen C.H. Review of a current role of mass spectrometry for proteome research. Anal Chim Acta 624 1 (Aug 22 2008) 16-36
    • (2008) Anal Chim Acta , vol.624 , Issue.1 , pp. 16-36
    • Chen, C.H.1
  • 35
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B., and Aebersold R. Mass spectrometry and protein analysis. Science 312 5771 (Apr 14 2006) 212-217
    • (2006) Science , vol.312 , Issue.5771 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 36
    • 34250657012 scopus 로고    scopus 로고
    • Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry
    • Shiio Y., and Aebersold R. Quantitative proteome analysis using isotope-coded affinity tags and mass spectrometry. Nat Protoc 1 1 (2006) 139-145
    • (2006) Nat Protoc , vol.1 , Issue.1 , pp. 139-145
    • Shiio, Y.1    Aebersold, R.2
  • 37
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • Aebersold R., and Mann M. Mass spectrometry-based proteomics. Nature 422 6928 (Mar 13 2003) 198-207
    • (2003) Nature , vol.422 , Issue.6928 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 38
    • 0038561131 scopus 로고    scopus 로고
    • A method for the comprehensive proteomic analysis of membrane proteins
    • Wu C.C., MacCoss M.J., Howell K.E., and Yates III J.R. A method for the comprehensive proteomic analysis of membrane proteins. Nat Biotechnol 21 5 (May 2003) 532-538
    • (2003) Nat Biotechnol , vol.21 , Issue.5 , pp. 532-538
    • Wu, C.C.1    MacCoss, M.J.2    Howell, K.E.3    Yates III, J.R.4
  • 40
    • 34047165349 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis in proteome expression analysis
    • López J.L. Two-dimensional electrophoresis in proteome expression analysis. J Chromatogr B Analyt Technol Biomed Life Sci 849 1-2 (Apr 15 2007) 190-202
    • (2007) J Chromatogr B Analyt Technol Biomed Life Sci , vol.849 , Issue.1-2 , pp. 190-202
    • López, J.L.1
  • 41
    • 0034630358 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients
    • Molloy M.P. Two-dimensional electrophoresis of membrane proteins using immobilized pH gradients. Anal Biochem 280 1 (Apr 10 2000) 1-10
    • (2000) Anal Biochem , vol.280 , Issue.1 , pp. 1-10
    • Molloy, M.P.1
  • 42
    • 0031823994 scopus 로고    scopus 로고
    • New zwitterionic detergents improve the analysis of membrane proteins by two-dimensional electrophoresis
    • Chevallet M., Santoni V., Poinas A., Rouquie D., Fuchs A., Kieffer S., et al. New zwitterionic detergents improve the analysis of membrane proteins by two-dimensional electrophoresis. Electrophoresis 19 11 (Aug 1998) 1901-1909
    • (1998) Electrophoresis , vol.19 , Issue.11 , pp. 1901-1909
    • Chevallet, M.1    Santoni, V.2    Poinas, A.3    Rouquie, D.4    Fuchs, A.5    Kieffer, S.6
  • 43
    • 0032616532 scopus 로고    scopus 로고
    • Analytical IPG-Dalt
    • Görg A., and Weiss W. Analytical IPG-Dalt. Methods Mol Biol 112 (1999) 189-195
    • (1999) Methods Mol Biol , vol.112 , pp. 189-195
    • Görg, A.1    Weiss, W.2
  • 44
    • 0036857488 scopus 로고    scopus 로고
    • Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry
    • Henningsen R., Gale B.L., Straub K.M., and DeNagel D.C. Application of zwitterionic detergents to the solubilization of integral membrane proteins for two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2 11 (Nov 2002) 1479-1488
    • (2002) Proteomics , vol.2 , Issue.11 , pp. 1479-1488
    • Henningsen, R.1    Gale, B.L.2    Straub, K.M.3    DeNagel, D.C.4
  • 45
    • 0037347236 scopus 로고    scopus 로고
    • Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis
    • Luche S., Santoni V., and Rabilloud T. Evaluation of nonionic and zwitterionic detergents as membrane protein solubilizers in two-dimensional electrophoresis. Proteomics 3 3 (Mar 2003) 249-253
    • (2003) Proteomics , vol.3 , Issue.3 , pp. 249-253
    • Luche, S.1    Santoni, V.2    Rabilloud, T.3
  • 46
    • 0028068353 scopus 로고
    • Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity
    • Kessi J., Poirée J.C., Wehrli E., Bachofen R., Semenza G., and Hauser H. Short-chain phosphatidylcholines as superior detergents in solubilizing membrane proteins and preserving biological activity. Biochemistry 33 35 (Sep 6 1994) 10825-10836
    • (1994) Biochemistry , vol.33 , Issue.35 , pp. 10825-10836
    • Kessi, J.1    Poirée, J.C.2    Wehrli, E.3    Bachofen, R.4    Semenza, G.5    Hauser, H.6
  • 47
    • 0346728680 scopus 로고    scopus 로고
    • Solubilization of membrane proteins for two-dimensional gel electrophoresis: identification of sarcoplasmic reticulum membrane proteins
    • Babu G.J., Wheeler D., Alzate O., and Periasamy M. Solubilization of membrane proteins for two-dimensional gel electrophoresis: identification of sarcoplasmic reticulum membrane proteins. Anal Biochem 325 1 (Feb 1 2004) 121-125
    • (2004) Anal Biochem , vol.325 , Issue.1 , pp. 121-125
    • Babu, G.J.1    Wheeler, D.2    Alzate, O.3    Periasamy, M.4
  • 48
    • 34548286709 scopus 로고    scopus 로고
    • Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis
    • Rabilloud T., Luche S., Santoni V., and Chevallet M. Detergents and chaotropes for protein solubilization before two-dimensional electrophoresis. Methods Mol Biol 355 (2007) 111-119
    • (2007) Methods Mol Biol , vol.355 , pp. 111-119
    • Rabilloud, T.1    Luche, S.2    Santoni, V.3    Chevallet, M.4
  • 49
    • 44049091965 scopus 로고    scopus 로고
    • Sample solubilization buffers for two-dimensional electrophoresis
    • Weiss W., and Görg A. Sample solubilization buffers for two-dimensional electrophoresis. Methods Mol Biol 424 (2008) 35-42
    • (2008) Methods Mol Biol , vol.424 , pp. 35-42
    • Weiss, W.1    Görg, A.2
  • 50
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • Rabilloud T. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 19 5 (May 1998) 758-760
    • (1998) Electrophoresis , vol.19 , Issue.5 , pp. 758-760
    • Rabilloud, T.1
  • 51
    • 0034132921 scopus 로고    scopus 로고
    • A review and proposed nomenclature for major proteins of the milk-fat globule membrane
    • Mather I.H. A review and proposed nomenclature for major proteins of the milk-fat globule membrane. J Dairy Sci 83 2 (Feb 2000) 203-247
    • (2000) J Dairy Sci , vol.83 , Issue.2 , pp. 203-247
    • Mather, I.H.1
  • 52
    • 47149091674 scopus 로고    scopus 로고
    • Angiogenic endothelium shows lactadherin-dependent phagocytosis of aged erythrocytes and apoptotic cells
    • Fens M.H., Mastrobattista E., de Graaff A.M., Flesch F.M., Ultee A., Rasmussen J.T., et al. Angiogenic endothelium shows lactadherin-dependent phagocytosis of aged erythrocytes and apoptotic cells. Blood 111 9 (May 1 2008) 4542-4550
    • (2008) Blood , vol.111 , Issue.9 , pp. 4542-4550
    • Fens, M.H.1    Mastrobattista, E.2    de Graaff, A.M.3    Flesch, F.M.4    Ultee, A.5    Rasmussen, J.T.6
  • 53
    • 34247524090 scopus 로고    scopus 로고
    • Lactadherin deficiency leads to apoptotic cell accumulation and accelerated atherosclerosis in mice
    • Ait-Oufella H., Kinugawa K., Zoll J., Simon T., Boddaert J., Heeneman S., et al. Lactadherin deficiency leads to apoptotic cell accumulation and accelerated atherosclerosis in mice. Circulation 115 16 (Apr 24 2007) 2168-2177
    • (2007) Circulation , vol.115 , Issue.16 , pp. 2168-2177
    • Ait-Oufella, H.1    Kinugawa, K.2    Zoll, J.3    Simon, T.4    Boddaert, J.5    Heeneman, S.6
  • 54
    • 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. Biochem J 395 1 (Apr 1 2006) 21-30
    • (2006) Biochem J , vol.395 , Issue.1 , pp. 21-30
    • Nakatani, H.1    Aoki, N.2    Nakagawa, Y.3    Jin-No, S.4    Aoyama, K.5    Oshima, K.6
  • 56
    • 8644286802 scopus 로고    scopus 로고
    • Endocytosis, intracellular sorting, and processing of exosomes by dendritic cells
    • Morelli A.E., Larregina A.T., Shufesky W.J., Sullivan M.L., Stolz D.B., Papworth G.D., et al. Endocytosis, intracellular sorting, and processing of exosomes by dendritic cells. Blood 104 10 (Nov 15 2004) 3257-3266
    • (2004) Blood , vol.104 , Issue.10 , pp. 3257-3266
    • Morelli, A.E.1    Larregina, A.T.2    Shufesky, W.J.3    Sullivan, M.L.4    Stolz, D.B.5    Papworth, G.D.6
  • 57
    • 0034705005 scopus 로고    scopus 로고
    • Functional analyses of two cellular binding domains of bovine lactadherin
    • Andersen M.H., Berglund L., Petersen T.E., and Rasmussen J.T. Functional analyses of two cellular binding domains of bovine lactadherin. Biochemistry 39 20 (May 23 2000) 6200-6206
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6200-6206
    • Andersen, M.H.1    Berglund, L.2    Petersen, T.E.3    Rasmussen, J.T.4
  • 58
    • 35748963546 scopus 로고    scopus 로고
    • Inhibitory activities of bovine macromolecular whey proteins on rotavirus infections in vitro and in vivo
    • Bojsen A., Buesa J., Montava R., Kvistgaard A.S., Kongsbak M.B., Petersen T.E., et al. Inhibitory activities of bovine macromolecular whey proteins on rotavirus infections in vitro and in vivo. J Dairy Sci 90 1 (Jan 2007) 66-74
    • (2007) J Dairy Sci , vol.90 , Issue.1 , pp. 66-74
    • Bojsen, A.1    Buesa, J.2    Montava, R.3    Kvistgaard, A.S.4    Kongsbak, M.B.5    Petersen, T.E.6
  • 59
    • 33646533356 scopus 로고    scopus 로고
    • Identification by mass spectroscopy of F4ac-fimbrial-binding proteins in porcine milk and characterization of lactadherin as an inhibitor of F4ac-positive Escherichia coli attachment to intestinal villi in vitro
    • Shahriar F., Ngeleka M., Gordon J.R., and Simko E. Identification by mass spectroscopy of F4ac-fimbrial-binding proteins in porcine milk and characterization of lactadherin as an inhibitor of F4ac-positive Escherichia coli attachment to intestinal villi in vitro. Dev Comp Immunol 30 8 (2006) 723-734
    • (2006) Dev Comp Immunol , vol.30 , Issue.8 , pp. 723-734
    • Shahriar, F.1    Ngeleka, M.2    Gordon, J.R.3    Simko, E.4
  • 60
    • 0036178402 scopus 로고    scopus 로고
    • Secretion of a peripheral membrane protein, MFG-E8, as a complex with membrane vesicles
    • Oshima K., Aoki N., Kato T., Kitajima K., and Matsuda T. Secretion of a peripheral membrane protein, MFG-E8, as a complex with membrane vesicles. Eur J Biochem 269 4 (Feb 2002) 1209-1218
    • (2002) Eur J Biochem , vol.269 , Issue.4 , pp. 1209-1218
    • Oshima, K.1    Aoki, N.2    Kato, T.3    Kitajima, K.4    Matsuda, T.5
  • 61
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • Caviston J.P., and Holzbaur E.L. Microtubule motors at the intersection of trafficking and transport. Trends Cell Biol 16 10 (Oct 2006) 530-537
    • (2006) Trends Cell Biol , vol.16 , Issue.10 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 62
    • 10644272564 scopus 로고    scopus 로고
    • Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules
    • Andrade J., Pearce S.T., Zhao H., and Barroso M. Interactions among p22, glyceraldehyde-3-phosphate dehydrogenase and microtubules. Biochem J 384 Pt 2 (Dec 1 2004) 327-336
    • (2004) Biochem J , vol.384 , Issue.PART 2 , pp. 327-336
    • Andrade, J.1    Pearce, S.T.2    Zhao, H.3    Barroso, M.4
  • 65
    • 24044500344 scopus 로고    scopus 로고
    • Myosins: tails (and heads) of functional diversity
    • Krendel M., and Mooseker M.S. Myosins: tails (and heads) of functional diversity. Physiology (Bethesda) 20 (Aug 2005) 239-251
    • (2005) Physiology (Bethesda) , vol.20 , pp. 239-251
    • Krendel, M.1    Mooseker, M.S.2
  • 66
    • 33847295719 scopus 로고    scopus 로고
    • Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics
    • Ono S. Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 258 (2007) 1-82
    • (2007) Int Rev Cytol , vol.258 , pp. 1-82
    • Ono, S.1
  • 67
    • 0035827183 scopus 로고    scopus 로고
    • Brain t-complex polypeptide 1 (TCP- 1) related to its natural substrate beta1 tubulin is decreased in Alzheimer's disease
    • Schuller E., Gulesserian T., Seidl R., Cairns N., and Lube G. Brain t-complex polypeptide 1 (TCP- 1) related to its natural substrate beta1 tubulin is decreased in Alzheimer's disease. Life Sci 69 3 (Jun 8 2001) 263-270
    • (2001) Life Sci , vol.69 , Issue.3 , pp. 263-270
    • Schuller, E.1    Gulesserian, T.2    Seidl, R.3    Cairns, N.4    Lube, G.5
  • 68
    • 0024390672 scopus 로고
    • A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells
    • Ali S.M., Geisow M.J., and Burgoyne R.D. A role for calpactin in calcium-dependent exocytosis in adrenal chromaffin cells. Nature 340 6231 (Jul 27 1989) 313-315
    • (1989) Nature , vol.340 , Issue.6231 , pp. 313-315
    • Ali, S.M.1    Geisow, M.J.2    Burgoyne, R.D.3
  • 69
    • 0023818448 scopus 로고
    • Aggregation of chromaffin granules by calpactin at micromolar levels of calcium
    • Drust D.S., and Creutz C.E. Aggregation of chromaffin granules by calpactin at micromolar levels of calcium. Nature 331 6151 (Jan 7 1988) 88-91
    • (1988) Nature , vol.331 , Issue.6151 , pp. 88-91
    • Drust, D.S.1    Creutz, C.E.2
  • 70
    • 33644526287 scopus 로고    scopus 로고
    • Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins
    • Review
    • Kahn R.A., Cherfils J., Elias M., Lovering R.C., Munro S., and Schurmann A. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J Cell Biol 172 5 (Feb 27 2006) 645-650 Review
    • (2006) J Cell Biol , vol.172 , Issue.5 , pp. 645-650
    • Kahn, R.A.1    Cherfils, J.2    Elias, M.3    Lovering, R.C.4    Munro, S.5    Schurmann, A.6
  • 71
    • 34247623568 scopus 로고    scopus 로고
    • Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle
    • Cai H., Reinisch K., and Ferro-Novick S. Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle. Dev Cell 12 5 (May 2007) 671-682
    • (2007) Dev Cell , vol.12 , Issue.5 , pp. 671-682
    • Cai, H.1    Reinisch, K.2    Ferro-Novick, S.3
  • 72
    • 52549126992 scopus 로고    scopus 로고
    • Regulation of secretory vesicle traffic by Rab small GTPases
    • Fukuda M. Regulation of secretory vesicle traffic by Rab small GTPases. Cell Mol Life Sci 65 18 (Sep 2008) 2801-2813
    • (2008) Cell Mol Life Sci , vol.65 , Issue.18 , pp. 2801-2813
    • Fukuda, M.1
  • 73
    • 44349134411 scopus 로고    scopus 로고
    • Rab proteins and Rab-associated proteins: major actors in the mechanism of protein-trafficking disorders
    • Corbeel L., and Freson K. Rab proteins and Rab-associated proteins: major actors in the mechanism of protein-trafficking disorders. Eur J Pediatr 167 7 (Jul 2008) 723-729
    • (2008) Eur J Pediatr , vol.167 , Issue.7 , pp. 723-729
    • Corbeel, L.1    Freson, K.2
  • 74
    • 46749110073 scopus 로고    scopus 로고
    • Proteomics of photoreceptor outer segments identifies a subset of SNARE and Rab proteins implicated in membrane vesicle trafficking and fusion
    • Kwok M.C., Holopainen J.M., Molday L.L., Foster L.J., and Molday R.S. Proteomics of photoreceptor outer segments identifies a subset of SNARE and Rab proteins implicated in membrane vesicle trafficking and fusion. Mol Cell Proteomics 7 6 (Jun 2008) 1053-1066
    • (2008) Mol Cell Proteomics , vol.7 , Issue.6 , pp. 1053-1066
    • Kwok, M.C.1    Holopainen, J.M.2    Molday, L.L.3    Foster, L.J.4    Molday, R.S.5
  • 75
    • 3142585284 scopus 로고    scopus 로고
    • Controlling the location and activation of Rab GTPases
    • Seabra M.C., and Wasmeier C. Controlling the location and activation of Rab GTPases. Curr Opin Cell Biol 16 4 (Aug 2004) 451-457
    • (2004) Curr Opin Cell Biol , vol.16 , Issue.4 , pp. 451-457
    • Seabra, M.C.1    Wasmeier, C.2
  • 76
    • 34347386746 scopus 로고    scopus 로고
    • Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association
    • Monetta P., Slavin I., Romero N., and Alvarez C. Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association. Mol Biol Cell 18 7 (Jul 2007) 2400-2410
    • (2007) Mol Biol Cell , vol.18 , Issue.7 , pp. 2400-2410
    • Monetta, P.1    Slavin, I.2    Romero, N.3    Alvarez, C.4
  • 77
    • 0031942615 scopus 로고    scopus 로고
    • A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion
    • Ungermann C., Nichols B.J., Pelham H.R., and Wickner W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J Cell Biol 140 1 (Jan 12 1998) 61-69
    • (1998) J Cell Biol , vol.140 , Issue.1 , pp. 61-69
    • Ungermann, C.1    Nichols, B.J.2    Pelham, H.R.3    Wickner, W.4
  • 78
    • 0032568798 scopus 로고    scopus 로고
    • LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion
    • Xu Z., Sato K., and Wickner W. LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell 93 7 (Jun 26 1998) 1125-1134
    • (1998) Cell , vol.93 , Issue.7 , pp. 1125-1134
    • Xu, Z.1    Sato, K.2    Wickner, W.3
  • 79
    • 0028587687 scopus 로고
    • Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver
    • Zhang L., Ashendel C.L., Becker G.W., and Morré D.J. Isolation and characterization of the principal ATPase associated with transitional endoplasmic reticulum of rat liver. J Cell Biol 127 6 Pt 2 (Dec 1994) 1871-1883
    • (1994) J Cell Biol , vol.127 , Issue.6 PART 2 , pp. 1871-1883
    • Zhang, L.1    Ashendel, C.L.2    Becker, G.W.3    Morré, D.J.4
  • 80
    • 37849031433 scopus 로고    scopus 로고
    • The rap GTPases regulate B cell morphology, immune-synapse formation, and signaling by particulate B cell receptor ligands
    • Lin K.B., Freeman S.A., Zabetian S., Brugger H., Weber M., Lei V., et al. The rap GTPases regulate B cell morphology, immune-synapse formation, and signaling by particulate B cell receptor ligands. Immunity 28 1 (Jan 2008) 75-87
    • (2008) Immunity , vol.28 , Issue.1 , pp. 75-87
    • Lin, K.B.1    Freeman, S.A.2    Zabetian, S.3    Brugger, H.4    Weber, M.5    Lei, V.6
  • 81
    • 22944439068 scopus 로고    scopus 로고
    • Invited review: bovine milk fat globule membrane as a potential nutraceutical
    • Review
    • Spitsberg V.L. Invited review: bovine milk fat globule membrane as a potential nutraceutical. J Dairy Sci 88 7 (Jul 2005) 2289-2294 Review
    • (2005) J Dairy Sci , vol.88 , Issue.7 , pp. 2289-2294
    • Spitsberg, V.L.1
  • 82
    • 58149121478 scopus 로고    scopus 로고
    • Effect of lactoferrin on enteric pathogens
    • Ochoa T.J., and Cleary T.G. Effect of lactoferrin on enteric pathogens. Biochimie 91 1 (Jan 2009) 30-34
    • (2009) Biochimie , vol.91 , Issue.1 , pp. 30-34
    • Ochoa, T.J.1    Cleary, T.G.2
  • 83
    • 0642309847 scopus 로고    scopus 로고
    • Antibacterial effect of bovine lactoferrin against udder pathogens
    • Kutila T., Pyörälä S., Saloniemi H., and Kaartinen L. Antibacterial effect of bovine lactoferrin against udder pathogens. Acta Vet Scand 44 1-2 (2003) 35-42
    • (2003) Acta Vet Scand , vol.44 , Issue.1-2 , pp. 35-42
    • Kutila, T.1    Pyörälä, S.2    Saloniemi, H.3    Kaartinen, L.4
  • 84
    • 47949128627 scopus 로고    scopus 로고
    • Fungistatic activity of iron-free bovin lactoferrin against several fungal plant pathogens and antagonists
    • Lahoz E., Pisacane A., Iannaccone M., Palumbo D., and Capparelli R. Fungistatic activity of iron-free bovin lactoferrin against several fungal plant pathogens and antagonists. Nat Prod Res 22 11 (2008) 955-961
    • (2008) Nat Prod Res , vol.22 , Issue.11 , pp. 955-961
    • Lahoz, E.1    Pisacane, A.2    Iannaccone, M.3    Palumbo, D.4    Capparelli, R.5
  • 85
    • 84934440654 scopus 로고    scopus 로고
    • CD14: a soluble pattern recognition receptor in milk
    • Vidal K., and Donnet-Hughes A. CD14: a soluble pattern recognition receptor in milk. Adv Exp Med Biol 606 (2008) 195-216
    • (2008) Adv Exp Med Biol , vol.606 , pp. 195-216
    • Vidal, K.1    Donnet-Hughes, A.2
  • 86
    • 22144491109 scopus 로고    scopus 로고
    • The bovine innate immune response during experimentally-induced Pseudomonas aeruginosa mastitis
    • Bannerman D.D., Chockalingam A., Paape M.J., and Hope J.C. The bovine innate immune response during experimentally-induced Pseudomonas aeruginosa mastitis. Vet Immunol Immunopathol 107 3-4 (Sep 15 2005) 201-215
    • (2005) Vet Immunol Immunopathol , vol.107 , Issue.3-4 , pp. 201-215
    • Bannerman, D.D.1    Chockalingam, A.2    Paape, M.J.3    Hope, J.C.4
  • 87
    • 0141609059 scopus 로고    scopus 로고
    • Elevated milk soluble CD14 in bovine mammary glands challenged with Escherichia coli lipopolysaccharide
    • Lee J.W., Paape M.J., Elsasser T.H., and Zhao X. Elevated milk soluble CD14 in bovine mammary glands challenged with Escherichia coli lipopolysaccharide. J Dairy Sci 86 7 (Jul 2003) 2382-2389
    • (2003) J Dairy Sci , vol.86 , Issue.7 , pp. 2382-2389
    • Lee, J.W.1    Paape, M.J.2    Elsasser, T.H.3    Zhao, X.4
  • 88
    • 0343729976 scopus 로고    scopus 로고
    • Innate recognition of bacteria in human milk is mediated by a milk-derived highly expressed pattern recognition receptor, soluble CD14
    • Labéta M.O., Vidal K., Nores J.E., Arias M., Vita N., Morgan B.P., et al. Innate recognition of bacteria in human milk is mediated by a milk-derived highly expressed pattern recognition receptor, soluble CD14. J Exp Med 191 10 (May 15 2000) 1807-1812
    • (2000) J Exp Med , vol.191 , Issue.10 , pp. 1807-1812
    • Labéta, M.O.1    Vidal, K.2    Nores, J.E.3    Arias, M.4    Vita, N.5    Morgan, B.P.6
  • 89
    • 0037817352 scopus 로고    scopus 로고
    • Transcytosis: crossing cellular barriers
    • Tuma P.L., and Hubbard A.L. Transcytosis: crossing cellular barriers. Physiol Rev 83 3 (Jul 2003) 871-932
    • (2003) Physiol Rev , vol.83 , Issue.3 , pp. 871-932
    • Tuma, P.L.1    Hubbard, A.L.2
  • 90
    • 6444242809 scopus 로고    scopus 로고
    • Albumin transcytosis across the epithelium of the lactating mouse mammary gland
    • Monks J., and Neville M.C. Albumin transcytosis across the epithelium of the lactating mouse mammary gland. J Physiol 560 Pt 1 (Oct 1 2004) 267-280
    • (2004) J Physiol , vol.560 , Issue.PART 1 , pp. 267-280
    • Monks, J.1    Neville, M.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.