메뉴 건너뛰기




Volumn 253, Issue 1, 1998, Pages 328-338

The C-terminal helix of human apolipoprotein AII promotes the fusion of unilamellar liposomes and displaces apolipoprotein AI from high-density lipoproteins

Author keywords

Apolipoprotein AI; Apolipoprotein AII; Lipid binding; Membrane fusion; Synthetic peptide

Indexed keywords

APOLIPOPROTEIN A1; APOLIPOPROTEIN A2; HIGH DENSITY LIPOPROTEIN;

EID: 7144257856     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1998.2530328.x     Document Type: Article
Times cited : (24)

References (72)
  • 1
    • 0019795714 scopus 로고
    • Displacement of apo A-I by human apo A-II from complexes of apo-A-I-phosphutidylcholine-cholcsterol
    • Rosseneu, M., Van Tornout, P., Lievens M. J. & Assman. G. (1981) Displacement of apo A-I by human apo A-II from complexes of apo-A-I-phosphutidylcholine-cholcsterol, Eur. J. Biochem. 117. 347-352.
    • (1981) Eur. J. Biochem. , vol.117 , pp. 347-352
    • Rosseneu, M.1    Van Tornout, P.2    Lievens, M.J.3    Assman, G.4
  • 2
    • 0020490835 scopus 로고
    • On the mechanism of displacement of apolipoprotein A-I by apolipoprotein A-II from the HDI. surface
    • Edelstein, C., Halari. M. & Scanu. A. M. (1982) On the mechanism of displacement of apolipoprotein A-I by apolipoprotein A-II from the HDI. surface. J. Biol. Chem. 257. 7189-7195.
    • (1982) J. Biol. Chem. , vol.257 , pp. 7189-7195
    • Edelstein, C.1    Halari, M.2    Scanu, A.M.3
  • 3
    • 0028148548 scopus 로고
    • Purification and characterization of recombinant human apolipoprotein A-II expressed in E. coli
    • Lopez, J., Latta. M., Collet. X., Vanloo. B., Jung. G., Denefle. P., Rosseneu. M. & Chambaz, J. (1995) Purification and characterization of recombinant human apolipoprotein A-II expressed in E. coli, Eur J. Biochem. 225, 1141-1150.
    • (1995) Eur J. Biochem. , vol.225 , pp. 1141-1150
    • Lopez, J.1    Latta, M.2    Collet, X.3    Vanloo, B.4    Jung, G.5    Denefle, P.6    Rosseneu, M.7    Chambaz, J.8
  • 4
    • 7144236950 scopus 로고
    • Lecithin: Cholesterol acyl transferase: effect of substrate composition upon enzyme activity
    • Fielding. C. I., Shore. V. G. & Fielding. P. E. (1972) Lecithin: cholesterol acyl transferase: effect of substrate composition upon enzyme activity. Proc. Natl Acad. Sci. USA. 81, 140-144.
    • (1972) Proc. Natl Acad. Sci. USA , vol.81 , pp. 140-144
    • Fielding, C.I.1    Shore, V.G.2    Fielding, P.E.3
  • 5
    • 0020020765 scopus 로고
    • Peptide/lipid interaction : Studies with synthetic polypeptides
    • Sparrow, J. T. & Gotto. A. M. (1981) Peptide/lipid interaction : studies with synthetic polypeptides. Crit. Rev. Biochem. 13. 87-107.
    • (1981) Crit. Rev. Biochem. , vol.13 , pp. 87-107
    • Sparrow, J.T.1    Gotto, A.M.2
  • 7
    • 0030012443 scopus 로고    scopus 로고
    • Apolipoprotein A-II influences the substrate properties of human HDL2 and HDL3 for hepatic lipase
    • Mowri. H O., Patsch. J. R., Gotto. A. M. & Patsch. W. (1996) Apolipoprotein A-II influences the substrate properties of human HDL2 and HDL3 for hepatic lipase. Arterioscler. Thromb. Vasc. Biol. 16, 755-762.
    • (1996) Arterioscler. Thromb. Vasc. Biol. , vol.16 , pp. 755-762
    • Mowri, H.O.1    Patsch, J.R.2    Gotto, A.M.3    Patsch, W.4
  • 9
    • 0025852239 scopus 로고
    • Hepatic lipase hydrolysis of lipid regulation by apolipoproteins
    • Thuren, T., Wilcox. R. W., Sisson, P. & Whaite. P. (1991) Hepatic lipase hydrolysis of lipid regulation by apolipoproteins, J. Biol. Chem. 266. 4853-4861.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4853-4861
    • Thuren, T.1    Wilcox, R.W.2    Sisson, P.3    Whaite, P.4
  • 10
    • 0029119888 scopus 로고
    • Cholesterol efflux, cholesterol esterification and cholesteryl ester transfer by Lp A-I and Lp A-I:A-II in native plasma
    • Huang, Y., Von Eckardstein, A., Wu. S. & Assmann. G. (1995) Cholesterol efflux, cholesterol esterification and cholesteryl ester transfer by Lp A-I and Lp A-I:A-II in native plasma, Arterioscler. Thromb. Vasc. Biol. 15, 1412-1418.
    • (1995) Arterioscler. Thromb. Vasc. Biol. , vol.15 , pp. 1412-1418
    • Huang, Y.1    Von Eckardstein, A.2    Wu, S.3    Assmann, G.4
  • 11
    • 0027526904 scopus 로고
    • Effects of HDL particles containing apo A-I. with or without apo A-II on intracellular cholesterol efflux
    • Oikawa. S., Mendez. A. J., Oram. J. F., Bierman, E. L. & Cheung, M. C. (1993) Effects of HDL particles containing apo A-I. with or without apo A-II on intracellular cholesterol efflux. Biochim. Biophys. Acta 1165, 327-334.
    • (1993) Biochim. Biophys. Acta , vol.1165 , pp. 327-334
    • Oikawa, S.1    Mendez, A.J.2    Oram, J.F.3    Bierman, E.L.4    Cheung, M.C.5
  • 12
    • 0029045180 scopus 로고
    • Effects of interactions of apolipoprotein A-II with apolipoproteins A-I and A-IV on cholesterol efflux and uptake in cell culture
    • Stein. O., Dabach. G., Ben-Naim. M., Oette. K. & Stein. O. (1995) Effects of interactions of apolipoprotein A-II with apolipoproteins A-I and A-IV on cholesterol efflux and uptake in cell culture. Biochim. Biophys. Acta 1257, 174-180.
    • (1995) Biochim. Biophys. Acta , vol.1257 , pp. 174-180
    • Stein, O.1    Dabach, G.2    Ben-Naim, M.3    Oette, K.4    Stein, O.5
  • 13
    • 0027373567 scopus 로고
    • Protein composition determines the anti-atherogenic properties in transgenic mice
    • Schultz. J. R., Verstuyft, J. G., Gong. E. L., Nichols, A. V. & Rubin. E. M. (1993) Protein composition determines the anti-atherogenic properties in transgenic mice. Nature .365, 762-764.
    • (1993) Nature , vol.365 , pp. 762-764
    • Schultz, J.R.1    Verstuyft, J.G.2    Gong, E.L.3    Nichols, A.V.4    Rubin, E.M.5
  • 14
    • 0027279942 scopus 로고
    • Atherosclerosis in transgenic mice overexpressing human apolipoprotein A-II
    • Warden. C. H., Hedrick. C. C., Qiao, J. H., Castellani. L. W. & Lusis. A. J. (1993) Atherosclerosis in transgenic mice overexpressing human apolipoprotein A-II. Science 261, 469-472.
    • (1993) Science , vol.261 , pp. 469-472
    • Warden, C.H.1    Hedrick, C.C.2    Qiao, J.H.3    Castellani, L.W.4    Lusis, A.J.5
  • 15
    • 0028280609 scopus 로고
    • The properties of HDL in genetically engineered mice
    • Schultz, J. R. & Rubin, E. M. (1994) The properties of HDL in genetically engineered mice. Curr. Opin. Lipidol. 5. 126- 137.
    • (1994) Curr. Opin. Lipidol. , vol.5 , pp. 126-137
    • Schultz, J.R.1    Rubin, E.M.2
  • 16
    • 0030045883 scopus 로고    scopus 로고
    • High Density Lipoprotein and coronary heart disease
    • Barter, P. J. & Rye. K. A. (1996) High Density Lipoprotein and coronary heart disease. Atheroscerosis 121. 1 -12.
    • (1996) Atheroscerosis , vol.121 , pp. 1-12
    • Barter, P.J.1    Rye, K.A.2
  • 17
    • 7144245439 scopus 로고    scopus 로고
    • Protective effect of human apo A-II overexpression on atherogenesis in transgenic mice
    • Fievet, C., Tailleux. A., Caillaud. J. M., Fruchard. J. C., Denèfle. P. & Duverger, N. (1996) Protective effect of human apo A-II overexpression on atherogenesis in transgenic mice. Circulation 94. 631-632.
    • (1996) Circulation , vol.94 , pp. 631-632
    • Fievet, C.1    Tailleux, A.2    Caillaud, J.M.3    Fruchard, J.C.4    Denèfle, P.5    Duverger, N.6
  • 18
    • 0023097589 scopus 로고
    • Cholesterol efflux from cultured adipose cells is mediated by Lp A-I-particles but not by Lp A-I:A-II-particles
    • Barbaras, R., Puchois. P., Fruchart. J. C. & Ailhaud. G. (1987) Cholesterol efflux from cultured adipose cells is mediated by Lp A-I-particles but not by Lp A-I:A-II-particles. Biochem. Biophys. Res. Commun. 142, 63-69.
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 63-69
    • Barbaras, R.1    Puchois, P.2    Fruchart, J.C.3    Ailhaud, G.4
  • 19
    • 0024996141 scopus 로고
    • Plasma HDL metabolism and relationship to atherosclerosis
    • Tall, A. R. (1990) Plasma HDL metabolism and relationship to atherosclerosis, J. Clin. Invest. 86. 379-84.
    • (1990) J. Clin. Invest. , vol.86 , pp. 379-384
    • Tall, A.R.1
  • 20
    • 0029915242 scopus 로고    scopus 로고
    • Contrasting in vivo effects of murine and human apolipoprotein A-II
    • Gong, E. L., Stoltzfus, L. J., Brion. C. M., Murugesh, D. & Rubin. E. M. (1996) Contrasting in vivo effects of murine and human apolipoprotein A-II. J. Biol. Chem. 271, 5984-5987.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5984-5987
    • Gong, E.L.1    Stoltzfus, L.J.2    Brion, C.M.3    Murugesh, D.4    Rubin, E.M.5
  • 21
    • 0030066591 scopus 로고    scopus 로고
    • The molecular structure of apolipoprotein A-II modulates the capacity of HDL to promote cholesterol efflux
    • Bernini, F., Calabresi, L., Bonfadini, G. & Franceschini. G. (1996) The molecular structure of apolipoprotein A-II modulates the capacity of HDL to promote cholesterol efflux. Biochim. Biophys. Acta 1299, 103-109.
    • (1996) Biochim. Biophys. Acta , vol.1299 , pp. 103-109
    • Bernini, F.1    Calabresi, L.2    Bonfadini, G.3    Franceschini, G.4
  • 22
    • 0029743281 scopus 로고    scopus 로고
    • Conformational studies of the amphipathic peptide corresponding to human apolipoprotein A-II residues 18-30 with a C-terminal lipid binding motif EWLNS
    • Buchko. O. W., Wang. C., Pifrens. G. K. & Cushley. R. J. (1996) Conformational studies of the amphipathic peptide corresponding to human apolipoprotein A-II residues 18-30 with a C-terminal lipid binding motif EWLNS. Int. J. Peptide Protein Res. 48. 21 - 30.
    • (1996) Int. J. Peptide Protein Res. , vol.48 , pp. 21-30
    • Buchko, O.W.1    Wang, C.2    Pifrens, G.K.3    Cushley, R.J.4
  • 24
    • 0025054302 scopus 로고
    • Orientation into the lipid bilayer of an asymetric amphipathic helical peptide at the N-terminus of viral fusion protein
    • Brasseur, R., Vandenbranden, M., Cornet, B. & Ruysschaert, J.-M. (1990) Orientation into the lipid bilayer of an asymetric amphipathic helical peptide at the N-terminus of viral fusion protein. Biochim. Biophys. Acta 1029, 267-273.
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 267-273
    • Brasseur, R.1    Vandenbranden, M.2    Cornet, B.3    Ruysschaert, J.-M.4
  • 26
    • 0027955142 scopus 로고
    • Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: An infrared spectroscopy study
    • Martin, I., Dubois, M. C., Defrise-Quertain, F., Saermark, T., Burny, A., Brasseur, R. & Ruysschaert, J.-M. (1994) Correlation between fusogenicity of synthetic modified peptides corresponding to the NH2-terminal extremity of simian immunodeficiency virus gp32 and their mode of insertion into the lipid bilayer: an infrared spectroscopy study. J. Virol. 68. 1139-1148.
    • (1994) J. Virol. , vol.68 , pp. 1139-1148
    • Martin, I.1    Dubois, M.C.2    Defrise-Quertain, F.3    Saermark, T.4    Burny, A.5    Brasseur, R.6    Ruysschaert, J.-M.7
  • 27
    • 0028820162 scopus 로고
    • Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy
    • Tatulian, S. A., Hinterdorfer, P., Baber, G. & Tamm, L. K. (1995) Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy, EMBO J. 14, 5514-5523.
    • (1995) EMBO J. , vol.14 , pp. 5514-5523
    • Tatulian, S.A.1    Hinterdorfer, P.2    Baber, G.3    Tamm, L.K.4
  • 30
    • 0026505142 scopus 로고
    • Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells
    • Vonèche, V., Portetelle, D., Kettman, R., Willems, L., Limbach, K., Paoletti, E., Ruysschaert, J.-M., Burny, A. & Brasseur, R. (1992) Fusogenic segments of bovine leukemia virus and simian immunodeficiency virus are interchangeable and mediate fusion by means of oblique insertion in the lipid bilayer of their target cells. Proc. Natl Acad. Sci. USA 89, 3810-3814.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 3810-3814
    • Vonèche, V.1    Portetelle, D.2    Kettman, R.3    Willems, L.4    Limbach, K.5    Paoletti, E.6    Ruysschaert, J.-M.7    Burny, A.8    Brasseur, R.9
  • 32
    • 0028864218 scopus 로고
    • A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of sendai virus-cell fusion: An emerging similarity with functional domains of other viruses
    • Rapaport, D., Ovadia, M. & Shai, Y. (1995) A synthetic peptide corresponding to a conserved heptad repeat domain is a potent inhibitor of sendai virus-cell fusion: an emerging similarity with functional domains of other viruses, EMBO J. 14. 5524-5531.
    • (1995) EMBO J. , vol.14 , pp. 5524-5531
    • Rapaport, D.1    Ovadia, M.2    Shai, Y.3
  • 33
    • 0029655419 scopus 로고    scopus 로고
    • Lipid membrane fusion induced by the human immunodeficiency virus type Igp41 N-terminal extremity is determined by its orientation in the lipid bilayer
    • Martin, I., Schaal, H., Scheid, A. & Ruysschaert, J.-M. (1996) Lipid membrane fusion induced by the human immunodeficiency virus type Igp41 N-terminal extremity is determined by its orientation in the lipid bilayer. J. Virol. 70, 298-304.
    • (1996) J. Virol. , vol.70 , pp. 298-304
    • Martin, I.1    Schaal, H.2    Scheid, A.3    Ruysschaert, J.-M.4
  • 34
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto, A., Martin, I., Ruysschaert. J.-M., Sen, A., Hui, S. W. & Epand, R. M. (1996) Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry 35, 980-989.
    • (1996) Biochemistry , vol.35 , pp. 980-989
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.-M.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 35
    • 0029968695 scopus 로고    scopus 로고
    • Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1 : Identification of critical glycine residues
    • Delahunty, M. D., Rhee, I., Freed, E. O. & Bonifacino, J. S. (1996) Mutational analysis of the fusion peptide of the human immunodeficiency virus type 1 : identification of critical glycine residues, Virology 218, 94-102.
    • (1996) Virology , vol.218 , pp. 94-102
    • Delahunty, M.D.1    Rhee, I.2    Freed, E.O.3    Bonifacino, J.S.4
  • 36
    • 0019315426 scopus 로고
    • Reassembly of human apo AI and apo AII proteins with unilamellar phosphatidylcholine cholesterol liposomes
    • Van Tornout, P., Vercaemst, R., Lievens, M. J., Caster, H., Rosseneu, M. & Assman, G. (1980) Reassembly of human apo AI and apo AII proteins with unilamellar phosphatidylcholine cholesterol liposomes, Biochim. Biophys. Acta 601, 509-523.
    • (1980) Biochim. Biophys. Acta , vol.601 , pp. 509-523
    • Van Tornout, P.1    Vercaemst, R.2    Lievens, M.J.3    Caster, H.4    Rosseneu, M.5    Assman, G.6
  • 37
    • 0024421097 scopus 로고
    • Separation and quantitation of free cholesterol and cholesteryl esters in a macrophage cell line by HPLC
    • Vercaemst, R., Union, A. & Rosseneu, M. (1989) Separation and quantitation of free cholesterol and cholesteryl esters in a macrophage cell line by HPLC, J. Chromatogr. 494, 43-52.
    • (1989) J. Chromatogr. , vol.494 , pp. 43-52
    • Vercaemst, R.1    Union, A.2    Rosseneu, M.3
  • 38
    • 0023050209 scopus 로고
    • Conformation and mode of organization of amphiphilic membrane components: A conformational analysis
    • Brasseur, R. & Ruysschaert, J.-M. (1986) Conformation and mode of organization of amphiphilic membrane components: a conformational analysis, Biochem. J. 238, 1-11.
    • (1986) Biochem. J. , vol.238 , pp. 1-11
    • Brasseur, R.1    Ruysschaert, J.-M.2
  • 39
    • 0025936242 scopus 로고
    • Differentiation of lipid associating helices by use of tridimensional molecular hydrophobicity potential calculation
    • Brasseur, R. (1991) Differentiation of lipid associating helices by use of tridimensional molecular hydrophobicity potential calculation, J. Biol. Chem. 266, 16120-16127.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16120-16127
    • Brasseur, R.1
  • 42
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated film
    • Goormaghtigh, E., Cabiaux, V. & Ruysschaert, J.-M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier transform infrared spectroscopy on hydrated film, Eur. J. Biochem. 193, 409-420.
    • (1990) Eur. J. Biochem. , vol.193 , pp. 409-420
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 43
    • 0024604617 scopus 로고
    • Secondary structure of DT and its fragments interacting with acidic liposomes studied by polarized infrared spectroscopy
    • Cabiaux, V., Brasseur, R., Wattiez., R., Falmagne, P., Ruysschaert, J.-M. & Goormaghtigh, E. (1989) Secondary structure of DT and its fragments interacting with acidic liposomes studied by polarized infrared spectroscopy. J. Biol. Chem. 264, 4928-4938.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4928-4938
    • Cabiaux, V.1    Brasseur, R.2    Wattiez, R.3    Falmagne, P.4    Ruysschaert, J.-M.5    Goormaghtigh, E.6
  • 44
    • 0019479713 scopus 로고
    • Infrared membrane spectroscopy
    • (Grell, E., ed.) Springer-Verlag, Berlin
    • Fringeli, U. R. & Günthard M. H. (1981) Infrared membrane spectroscopy, in Membrane spectroscopy (Grell, E., ed.) pp. 270-332, Springer-Verlag, Berlin.
    • (1981) Membrane Spectroscopy , pp. 270-332
    • Fringeli, U.R.1    Günthard, M.H.2
  • 45
    • 0021115856 scopus 로고
    • Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy
    • Gremlich, H. U., Fringeli, U. P. & Schwyzer, R. (1983) Conformational changes of adrenocorticotropin peptides upon interaction with lipid membranes revealed by infrared attenuated total reflection spectroscopy, Biochemistry 22, 4257-4264.
    • (1983) Biochemistry , vol.22 , pp. 4257-4264
    • Gremlich, H.U.1    Fringeli, U.P.2    Schwyzer, R.3
  • 47
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvoluted FTIR spectra
    • Susi, H. & Byler, D. M. (1986) Examination of the secondary structure of proteins by deconvoluted FTIR spectra, Biopolymers 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Susi, H.1    Byler, D.M.2
  • 48
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides and proteins
    • Krimm, S. & Bandekar, J. (1986) Vibrational spectroscopy and conformation of peptides, polypeptides and proteins, Adv. Protein Chem. 38, 181-364.
    • (1986) Adv. Protein Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 49
    • 0024523567 scopus 로고
    • pH-dependent bilayer destabilisation and fusion of phospholipidic large unilamellar vesicles induced by diphteria toxin and its fragments A and B
    • Defrise-Quertain, F., Cabiaux, V., Vandenbranden, M., Wattiez, R., Falmagne, P. & Ruysschaert, J.-M. (1989) pH-dependent bilayer destabilisation and fusion of phospholipidic large unilamellar vesicles induced by diphteria toxin and its fragments A and B, Biochemistry 28, 3406-3413.
    • (1989) Biochemistry , vol.28 , pp. 3406-3413
    • Defrise-Quertain, F.1    Cabiaux, V.2    Vandenbranden, M.3    Wattiez, R.4    Falmagne, P.5    Ruysschaert, J.-M.6
  • 50
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • Havel, R. J., Eder, M. A. & Bragdon, J. M. (1955) The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum, J. Clin. Invest. 34, 1345.
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345
    • Havel, R.J.1    Eder, M.A.2    Bragdon, J.M.3
  • 51
    • 0023829776 scopus 로고
    • Early incorporation of cell derived cholesterol into pre-beta migrating HDL
    • Castro, G. & Fielding, C. (1988) Early incorporation of cell derived cholesterol into pre-beta migrating HDL. Biochemistry 27, 25-29.
    • (1988) Biochemistry , vol.27 , pp. 25-29
    • Castro, G.1    Fielding, C.2
  • 52
    • 0020490580 scopus 로고
    • Reaction of human lecithin:cholesterol acyl transferase with synthetic micellar complexes of apolipoproteins A-I, phosphatidylcholine and cholesterol
    • Matz, C. E. & Jonas, A. (1982) Reaction of human lecithin:cholesterol acyl transferase with synthetic micellar complexes of apolipoproteins A-I, phosphatidylcholine and cholesterol. J. Biol. Chem. 257, 4535-4540.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4535-4540
    • Matz, C.E.1    Jonas, A.2
  • 53
    • 0000053595 scopus 로고
    • Use of membrane associated fluorescence, probes to monitor fusion of bilayer vesicles: Application to rapid kinetics using pyrene excimer/monomer fluorescence in
    • CRC Press, Oxford
    • Morris, S. J., Bradley, D., Gibson, C. C., Smith, P. D. & Blumenthal, R. (1988) Use of membrane associated fluorescence, probes to monitor fusion of bilayer vesicles: application to rapid kinetics using pyrene excimer/monomer fluorescence in Spectroscopic membrane probes I, pp. 161-191, CRC Press, Oxford.
    • (1988) Spectroscopic Membrane Probes I , pp. 161-191
    • Morris, S.J.1    Bradley, D.2    Gibson, C.C.3    Smith, P.D.4    Blumenthal, R.5
  • 54
    • 0018794362 scopus 로고
    • Apolipoprotein A-II: Chemical synthesis and biophysical properties of three peptides corresponding to fragments in the amino-terminal half
    • Chen, T., Sparrow, J. T., Gotto, A. M. & Morrisett, J. (1979) Apolipoprotein A-II: chemical synthesis and biophysical properties of three peptides corresponding to fragments in the amino-terminal half, Biochemistry 18, 1617-1626.
    • (1979) Biochemistry , vol.18 , pp. 1617-1626
    • Chen, T.1    Sparrow, J.T.2    Gotto, A.M.3    Morrisett, J.4
  • 55
    • 0019883203 scopus 로고
    • Mechanism of lipid-protein interactions in plasma apolipoproteins: Identification of a lipid binding site in apolipoprotein A-II
    • Mao, S. J., Jackson, R. L., Gotto, A. M. & Sparrow, J. T. (1981) Mechanism of lipid-protein interactions in plasma apolipoproteins: identification of a lipid binding site in apolipoprotein A-II. Biochemistry 20, 1676-1680.
    • (1981) Biochemistry , vol.20 , pp. 1676-1680
    • Mao, S.J.1    Jackson, R.L.2    Gotto, A.M.3    Sparrow, J.T.4
  • 57
    • 0019825953 scopus 로고
    • Kinetics and mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: Effect of protein structure and lipid clusters on reaction rates
    • Pownall, H. J., Pao, Q., Hickson, D., Sparrow, J. T., Kusserow, S. K. & Massey, J. B. (1981) Kinetics and mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: effect of protein structure and lipid clusters on reaction rates, Biochemistry 20, 6630-6635.
    • (1981) Biochemistry , vol.20 , pp. 6630-6635
    • Pownall, H.J.1    Pao, Q.2    Hickson, D.3    Sparrow, J.T.4    Kusserow, S.K.5    Massey, J.B.6
  • 58
    • 0021099319 scopus 로고
    • Clathrin-induced pH-dependent fusion of phosphatidylcholine vesicles
    • Blumenthal, R., Henkart, M. & Steer, C. J. (1983) Clathrin-induced pH-dependent fusion of phosphatidylcholine vesicles, J. Biol. Chem. 258, 3409-3415.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3409-3415
    • Blumenthal, R.1    Henkart, M.2    Steer, C.J.3
  • 59
    • 0023657247 scopus 로고
    • Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin and δ-hemolysin with phosphatidylcholines
    • Brauner, J. W., Mendelsohn, R. & Prendergast, F. G. (1987) Attenuated total reflectance Fourier transform infrared studies of the interaction of melittin, two fragments of melittin and δ-hemolysin with phosphatidylcholines, Biochemistry 26, 8151-8158.
    • (1987) Biochemistry , vol.26 , pp. 8151-8158
    • Brauner, J.W.1    Mendelsohn, R.2    Prendergast, F.G.3
  • 60
    • 0024587795 scopus 로고
    • Secondary structure and orientation of a chemically synthesized mitochondrial signal sequence in phospholipid bilayer
    • Goormaghtigh, E., Martin, I., Vandenbranden, M., Brasseur, R. & Ruysschaert, J.-M. (1989) Secondary structure and orientation of a chemically synthesized mitochondrial signal sequence in phospholipid bilayer, Biochem, Biophys. Res. Commun. 158, 610-616.
    • (1989) Biochem, Biophys. Res. Commun. , vol.158 , pp. 610-616
    • Goormaghtigh, E.1    Martin, I.2    Vandenbranden, M.3    Brasseur, R.4    Ruysschaert, J.-M.5
  • 61
    • 0026731832 scopus 로고
    • Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy
    • Jackson, M., Mantsch, H. H. & Spencer, J. H. (1992) Conformation of magainin-2 and related peptides in aqueous solution and membrane environments probed by Fourier transform infrared spectroscopy. Biochemistry 31, 7289-7293.
    • (1992) Biochemistry , vol.31 , pp. 7289-7293
    • Jackson, M.1    Mantsch, H.H.2    Spencer, J.H.3
  • 62
    • 0027354020 scopus 로고
    • Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy
    • Arrondo, J. L. R., Muga, A., Castresana, J. & Goni, F. M. (1993)Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59, 23-56.
    • (1993) Prog. Biophys. Mol. Biol. , vol.59 , pp. 23-56
    • Arrondo, J.L.R.1    Muga, A.2    Castresana, J.3    Goni, F.M.4
  • 63
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson, M. & Mantsch, H. H. (1995) The use and misuse of FTIR spectroscopy in the determination of protein structure, Crit. Rev. Biochem. Mol. Biol. 30, 95-120.
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 64
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA2
    • Lear, J. D. & DeGrado, W. (1987) Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA2, J. Biol. Chem. 262, 6500-6505.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6500-6505
    • Lear, J.D.1    Degrado, W.2
  • 65
    • 0023805559 scopus 로고
    • Membrane fusion by peptide analogues of influenza virus hemagglutinin
    • Wharton, S. A., Martin, R., Ruigrok, R., Skehel, J. & Wiley, D. (1988) Membrane fusion by peptide analogues of influenza virus hemagglutinin, J. Gen. Virol. 69, 1847-1857.
    • (1988) J. Gen. Virol. , vol.69 , pp. 1847-1857
    • Wharton, S.A.1    Martin, R.2    Ruigrok, R.3    Skehel, J.4    Wiley, D.5
  • 66
    • 0025139941 scopus 로고
    • Interaction of apolipoprotein A-II with recombinant HDL containing egg phosphatidylcholine, unesterified cholesterol and apolipoprotein A-I
    • Rye, C.-A. (1990) Interaction of apolipoprotein A-II with recombinant HDL containing egg phosphatidylcholine, unesterified cholesterol and apolipoprotein A-I, Biochim. Biophys. Acta 1042, 227-236
    • (1990) Biochim. Biophys. Acta , vol.1042 , pp. 227-236
    • Rye, C.-A.1
  • 67
    • 0028821067 scopus 로고
    • Recruitment of cell phospholipids and cholesterol by apo A-II and A-I: Formation of nascent apolipoprotein-specific HDL that differ in size. phospholipid composition and reactivity with LCAT
    • Forte, T. M., Bielicki, J. K., Goth-Goldstein, R., Selmek, J. & McCall, M. R. (1995) Recruitment of cell phospholipids and cholesterol by apo A-II and A-I: formation of nascent apolipoprotein-specific HDL that differ in size. phospholipid composition and reactivity with LCAT, J. Lipid Res. 36, 148-157.
    • (1995) J. Lipid Res. , vol.36 , pp. 148-157
    • Forte, T.M.1    Bielicki, J.K.2    Goth-Goldstein, R.3    Selmek, J.4    McCall, M.R.5
  • 68
    • 0031032472 scopus 로고    scopus 로고
    • Apo A-II/apo A-I molar ratio in the HDL particle influences phospholipid transfer protein-mediated HDL interconversion
    • Pussinen, P. J., Jauhiainen, M. & Enholm, C. (1997) Apo A-II/apo A-I molar ratio in the HDL particle influences phospholipid transfer protein-mediated HDL interconversion. J. Lipid Res. 38. 12-21
    • (1997) J. Lipid Res. , vol.38 , pp. 12-21
    • Pussinen, P.J.1    Jauhiainen, M.2    Enholm, C.3
  • 69
    • 0029894484 scopus 로고    scopus 로고
    • Structural relationships between nascent apo A-I containing particles that are extracellularly assembled in cell culture
    • Forte, T. M., Bielicki, J. K., Knoff, L. & McCall, M. R. (1996) Structural relationships between nascent apo A-I containing particles that are extracellularly assembled in cell culture, J. Lipid Res. 37, 1076-1085.
    • (1996) J. Lipid Res. , vol.37 , pp. 1076-1085
    • Forte, T.M.1    Bielicki, J.K.2    Knoff, L.3    McCall, M.R.4
  • 70
    • 0028049901 scopus 로고
    • Influence of apolipoprotein composition of HDL particles on CETP activity
    • Lagrost, L., Persegol, L., Lallemant, C. & Gambert, P. (1994) influence of apolipoprotein composition of HDL particles on CETP activity, J. Biol. Chem. 269, 3189-3197
    • (1994) J. Biol. Chem. , vol.269 , pp. 3189-3197
    • Lagrost, L.1    Persegol, L.2    Lallemant, C.3    Gambert, P.4
  • 72
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg, D. (1984) Three-dimensional structure of membrane and surface proteins, Annu. Rev. Biochem. 53, 595-623.
    • (1984) Annu. Rev. Biochem. , vol.53 , pp. 595-623
    • Eisenberg, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.