메뉴 건너뛰기




Volumn 387, Issue 3, 2005, Pages 747-754

Orientation and mode of lipid-binding interaction of human apolipoprotein E C-terminal domain

Author keywords

Apolipoprotein E; Cross linking; Electron microscopy; IR spectroscopy; Lipid bound conformation; Lipoprotein binding surface

Indexed keywords

CELLS; CHOLESTEROL; FLUORESCENCE; FOURIER TRANSFORM INFRARED SPECTROSCOPY; PROTEINS; QUENCHING;

EID: 18844441394     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041536     Document Type: Article
Times cited : (33)

References (63)
  • 1
    • 0026458283 scopus 로고
    • Plasma lipoprotein metabolism in transgenic mice overexposing apolipoprotein E: Accelerated clearance of lipoproteins containing apolipoprotein B
    • Shimano, H., Yamada, N., Katsuki, M., Yamamoto, K., Gotoda, T., Harada, K., Shimada, M. and Yazaki, T. (1992) Plasma lipoprotein metabolism in transgenic mice overexposing apolipoprotein E: accelerated clearance of lipoproteins containing apolipoprotein B. J. Clin. Invest. 90, 2084-2091
    • (1992) J. Clin. Invest. , vol.90 , pp. 2084-2091
    • Shimano, H.1    Yamada, N.2    Katsuki, M.3    Yamamoto, K.4    Gotoda, T.5    Harada, K.6    Shimada, M.7    Yazaki, T.8
  • 2
    • 0026592806 scopus 로고
    • Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E
    • Zhang, S. H., Reddick, R. L., Piedrahita, J. A. and Maeda, N. (1992) Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E. Science 258, 468-471
    • (1992) Science , vol.258 , pp. 468-471
    • Zhang, S.H.1    Reddick, R.L.2    Piedrahita, J.A.3    Maeda, N.4
  • 4
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholestero homeostasis
    • Brown, M. S. and Goldstein, J. L. (1986) A receptor-mediated pathway for cholestero homeostasis. Science 232, 34-47
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 5
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding, C. J. and Fielding, P. E. (1995) Molecular physiology of reverse cholesterol transport. J. Lipid Res. 36, 211-228
    • (1995) J. Lipid Res. , vol.36 , pp. 211-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 6
    • 0035170229 scopus 로고    scopus 로고
    • High density lipoproteins and arteriosclerosis: Role of cholesterol efflux and reverse cholesterol transport
    • Von Eckardstein, A., Nofer, J.-R. and Assmann, G. (2001) High density lipoproteins and arteriosclerosis: role of cholesterol efflux and reverse cholesterol transport. Arterioscler. Thromb. Vasc. Biol. 21, 13-27
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 13-27
    • Von Eckardstein, A.1    Nofer, J.-R.2    Assmann, G.3
  • 8
    • 0029924266 scopus 로고    scopus 로고
    • Apolipoprotein E: Structure, function, and possible roles in Alzheimer's disease
    • Mahley, R. W., Nathan, B. P. and Pitas, R. E. (1996) Apolipoprotein E: structure, function, and possible roles in Alzheimer's disease. Ann. N.Y. Acad. Sci. 777, 139-145
    • (1996) Ann. N.Y. Acad. Sci. , vol.777 , pp. 139-145
    • Mahley, R.W.1    Nathan, B.P.2    Pitas, R.E.3
  • 9
    • 0024299370 scopus 로고
    • Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
    • Mahley, R. W. (1988) Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science 240, 622-630
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 10
    • 0023937366 scopus 로고
    • Human apolipoprotein E3 in aqueous solution. II. Properties of the amino- and carboxyl-terminal domains
    • Aggerbeck, L. P., Wetterau, J. R., Weisgraber, K. H., Wu, C.-S. C. and Lindgren, F. T. (1988) Human apolipoprotein E3 in aqueous solution. II. Properties of the amino- and carboxyl-terminal domains. J. Biol. Chem. 263, 6249-6258
    • (1988) J. Biol. Chem. , vol.263 , pp. 6249-6258
    • Aggerbeck, L.P.1    Wetterau, J.R.2    Weisgraber, K.H.3    Wu, C.-S.C.4    Lindgren, F.T.5
  • 11
    • 0023900109 scopus 로고
    • Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains
    • Wetterau, J. R., Aggerbeck, L. P., Rall, Jr, S. C. and Weisgraber, K. H. (1988) Human apolipoprotein E3 in aqueous solution. I. Evidence for two structural domains. J. Biol. Chem. 263, 6240-6248
    • (1988) J. Biol. Chem. , vol.263 , pp. 6240-6248
    • Wetterau, J.R.1    Aggerbeck, L.P.2    Rall Jr., S.C.3    Weisgraber, K.H.4
  • 12
    • 0028303072 scopus 로고
    • Apolipoprotein E: Structure-function relationships
    • Weisgraber, K. H. (1994) Apolipoprotein E: structure-function relationships. Adv. Protein Chem. 45, 249-302
    • (1994) Adv. Protein Chem. , vol.45 , pp. 249-302
    • Weisgraber, K.H.1
  • 13
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson, C., Wardell, M. R., Weisgraber, K. H., Mahley, R. W., and Agard, D. A. (1991) Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science 252, 1817-1822
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 14
    • 0000327162 scopus 로고
    • Apolipoprotein E: Structure-function correlations
    • (Miller, N. E. and Tall, A. R., eds.), Elsevier, Amsterdam
    • Weisgraber, K. H., Lund-Katz, S. and Phillips, M. C. (1992) Apolipoprotein E: structure-function correlations. In High Density Lipoproteins and Atherosclerosis III (Miller, N. E. and Tall, A. R., eds.), pp. 175-181, Elsevier, Amsterdam
    • (1992) High Density Lipoproteins and Atherosclerosis III , pp. 175-181
    • Weisgraber, K.H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 15
    • 0032894924 scopus 로고    scopus 로고
    • Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E
    • Fisher, C. A. and Ryan, R. O. (1999) Lipid binding-induced conformational changes in the N-terminal domain of human apolipoprotein E. J. Lipid Res. 40, 93-99
    • (1999) J. Lipid Res. , vol.40 , pp. 93-99
    • Fisher, C.A.1    Ryan, R.O.2
  • 16
    • 0034721777 scopus 로고    scopus 로고
    • The lipid-associated conformation of the low density lipoprotein receptor binding domain of human apolipoprotein E
    • Fisher, C. A., Narayanaswami, V. and Ryan, R. O. (2000) The lipid-associated conformation of the low density lipoprotein receptor binding domain of human apolipoprotein E. J. Biol. Chem. 275, 33601-33606
    • (2000) J. Biol. Chem. , vol.275 , pp. 33601-33606
    • Fisher, C.A.1    Narayanaswami, V.2    Ryan, R.O.3
  • 17
    • 0033991858 scopus 로고    scopus 로고
    • Molecular basis of exchangeable apolipoprotein function
    • Narayanaswami, V. and Ryan, R. O. (2000) Molecular basis of exchangeable apolipoprotein function. Biochim. Biophys. Acta 1483, 15-36
    • (2000) Biochim. Biophys. Acta , vol.1483 , pp. 15-36
    • Narayanaswami, V.1    Ryan, R.O.2
  • 18
    • 0035798681 scopus 로고    scopus 로고
    • Lipid binding-induced conformational change in human apolipoprotein E: Evidence for two lipid-bound states on spherical particles
    • Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund-Katz, S. and Phillips, M. C. (2001) Lipid binding-induced conformational change in human apolipoprotein E: evidence for two lipid-bound states on spherical particles. J. Biol. Chem. 276, 40949-40954
    • (2001) J. Biol. Chem. , vol.276 , pp. 40949-40954
    • Saito, H.1    Dhanasekaran, P.2    Baldwin, F.3    Weisgraber, K.H.4    Lund-Katz, S.5    Phillips, M.C.6
  • 19
    • 0027186135 scopus 로고
    • Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization
    • Westerlund, J. A. and Weisgraber, K. H. (1993) Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization. J. Biol. Chem. 268, 15745-15750
    • (1993) J. Biol. Chem. , vol.268 , pp. 15745-15750
    • Westerlund, J.A.1    Weisgraber, K.H.2
  • 20
    • 0026498155 scopus 로고
    • Familial apolipoprotein E deficiency and type III hyperlipoproteinemia due to a premature stop codon in the apolipoprotein E gene
    • Lohse, P., Brewer, 3rd, H. B. Meng, M. S., Skarlatos, S. I., LaRosa, J. C. and Brewsr, Jr, H. B. (1992) Familial apolipoprotein E deficiency and type III hyperlipoproteinemia due to a premature stop codon in the apolipoprotein E gene. J. Lipid Res. 33, 1583-1590
    • (1992) J. Lipid Res. , vol.33 , pp. 1583-1590
    • Lohse, P.1    Brewer III, H.B.2    Meng, M.S.3    Skarlatos, S.I.4    LaRosa, J.C.5    Brewsr Jr., H.B.6
  • 22
    • 0022408782 scopus 로고
    • Behavior of human apolipoprotein E in aqueous solutions and at interfaces
    • Yokoyama, S., Kawai, Y., Tajima, S. and Yamamoto, A. (1985) Behavior of human apolipoprotein E in aqueous solutions and at interfaces. J. Biol. Chem. 260, 16375-16382
    • (1985) J. Biol. Chem. , vol.260 , pp. 16375-16382
    • Yokoyama, S.1    Kawai, Y.2    Tajima, S.3    Yamamoto, A.4
  • 23
    • 0034711265 scopus 로고    scopus 로고
    • Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid
    • Perugini, M. A., Schuck, P. and Howlett, G. J. (2000) Self-association of human apolipoprotein E3 and E4 in the presence and absence of phospholipid. J. Biol. Chem. 275, 36758-36765
    • (2000) J. Biol. Chem. , vol.275 , pp. 36758-36765
    • Perugini, M.A.1    Schuck, P.2    Howlett, G.J.3
  • 24
    • 0242662225 scopus 로고    scopus 로고
    • Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain
    • Choy, N., Raussens, V. and Narayanaswami, V. (2003) Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain. J. Mol. Biol. 334, 527-539
    • (2003) J. Mol. Biol. , vol.334 , pp. 527-539
    • Choy, N.1    Raussens, V.2    Narayanaswami, V.3
  • 25
    • 0031027211 scopus 로고    scopus 로고
    • α-helical protein assembly motifs
    • Kohn, W. D., Mant, C. T. and Hodges, R. S. (1997) α-Helical protein assembly motifs. J. Biol. Chem. 272, 2583-2586
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, W.D.1    Mant, C.T.2    Hodges, R.S.3
  • 26
    • 0025000302 scopus 로고
    • Self-associated tetramer of human apolipoprotein E does not lead to its accumulation on a lipid particle
    • Yokoyama, S. (1990) Self-associated tetramer of human apolipoprotein E does not lead to its accumulation on a lipid particle. Biochim. Biophys. Acta 1047, 99-101
    • (1990) Biochim. Biophys. Acta , vol.1047 , pp. 99-101
    • Yokoyama, S.1
  • 27
    • 0024573697 scopus 로고
    • Association of apolipoprotein E with the low density lipoprotein receptor: Demonstration of its co-operativity on lipid microemulsion particles
    • Funahashi, T., Yokoyama, S. and Yamamoto, A. (1989) Association of apolipoprotein E with the low density lipoprotein receptor: demonstration of its co-operativity on lipid microemulsion particles. J. Biochem. 105, 582-587
    • (1989) J. Biochem. , vol.105 , pp. 582-587
    • Funahashi, T.1    Yokoyama, S.2    Yamamoto, A.3
  • 28
    • 0034111173 scopus 로고    scopus 로고
    • Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: Effect of glycosylation
    • Weers, P. M. M., Van der Horst, D. and Ryan, R. O. (2000) Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: effect of glycosylation. J. Lipid Res. 41, 416-423
    • (2000) J. Lipid Res. , vol.41 , pp. 416-423
    • Weers, P.M.M.1    Van Der Horst, D.2    Ryan, R.O.3
  • 29
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: Evidence for a conformational change
    • Weintzek, M., Kay, C. M., Oikawa, K. and Ryan, R. O. (1994) Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: evidence for a conformational change. J. Biol. Chem. 269, 4605-4612
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Weintzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 30
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerarna, N. and Woody, R. W. (2000) Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerarna, N.1    Woody, R.W.2
  • 31
    • 0030375117 scopus 로고    scopus 로고
    • Relevance of protein thin films prepared for attenuated total reflection Fourier transform infrared spectroscopy: Significance of the pH
    • Goormaghtigh, E., de Jongh, H. H. J. and Ruysschaert, J.-M. (1996) Relevance of protein thin films prepared for attenuated total reflection Fourier transform infrared spectroscopy: significance of the pH. Appl. Spectrosc. 50, 1519-1527
    • (1996) Appl. Spectrosc. , vol.50 , pp. 1519-1527
    • Goormaghtigh, E.1    De Jongh, H.H.J.2    Ruysschaert, J.-M.3
  • 32
    • 0025005940 scopus 로고
    • Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films
    • Goormaghtigh, E., Cabiaux, V. and Ruysschaert, J.-M. (1990) Secondary structure and dosage of soluble and membrane proteins by attenuated total reflection Fourier-transform infrared spectroscopy on hydrated films. 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
  • 33
    • 0003039141 scopus 로고
    • Polarised attenuated total reflection infrared spectroscopy as a tool to investigate the conformation and orientation of membrene components
    • (Brasseur, R., ed.), CRC Press, Eoca Raton
    • Goormaghtigh, E. and Ruysschaert, J.-M. (1990) Polarised attenuated total reflection infrared spectroscopy as a tool to investigate the conformation and orientation of membrene components. In Molecular Description of Biological Membrane Components by Computer Aided Conformational Analysis (Brasseur, R., ed.), pp. 285-329, CRC Press, Eoca Raton
    • (1990) Molecular Description of Biological Membrane Components by Computer Aided Conformational Analysis , pp. 285-329
    • Goormaghtigh, E.1    Ruysschaert, J.-M.2
  • 34
    • 0343092088 scopus 로고    scopus 로고
    • Orientation of the infrared transition moments for an α-helix
    • Marsh, D., Müller, M. and Schmitt, F.-J. (2000) Orientation of the infrared transition moments for an α-helix. Biophys. J. 78, 2499-2510
    • (2000) Biophys. J. , vol.78 , pp. 2499-2510
    • Marsh, D.1    Müller, M.2    Schmitt, F.-J.3
  • 36
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • Bechinger, B., Ruysschaert, J.-M. and Goormaghtigh, E. (1999) Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys. J. 76, 552-563
    • (1999) Biophys. J. , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.-M.2    Goormaghtigh, E.3
  • 37
    • 0031914422 scopus 로고    scopus 로고
    • Fluorescence studies of exchangeable apolipoprotein-lipid interactions: Superficial association of apolipophorin III with lipoprotein surfaces
    • Sahoo, D., Narayanaswami, V., Kay, C. M. and Ryan, R. O. (1998) Fluorescence studies of exchangeable apolipoprotein-lipid interactions: superficial association of apolipophorin III with lipoprotein surfaces. J. Biol. Chem. 273, 1403-1408
    • (1998) J. Biol. Chem. , vol.273 , pp. 1403-1408
    • Sahoo, D.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 38
    • 0036384368 scopus 로고    scopus 로고
    • Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization
    • Sahoo, D., Weers, P. M., Ryan, R. O. and Narayanaswami, V. (2002) Lipid-triggered conformational switch of apolipophorin III helix bundle to an extended helix organization. J. Mol. Biol. 321, 201-214
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 39
    • 0017288499 scopus 로고
    • Exposure of tryptophanyl residues in proteins: Quantitative determination by fluorescence quenching studies
    • Eftink, M. R. and Ghiron, C. A. (1976) Exposure of tryptophanyl residues in proteins: quantitative determination by fluorescence quenching studies. Biochemistry 15, 672-680
    • (1976) Biochemistry , vol.15 , pp. 672-680
    • Eftink, M.R.1    Ghiron, C.A.2
  • 40
    • 0022556091 scopus 로고
    • Electron microscopy of negatively stained lipoproteins
    • Forte, T. M. and Nordhausen, R. W. (1986) Electron microscopy of negatively stained lipoproteins. Methods Enzymol. 128, 442-457
    • (1986) Methods Enzymol. , vol.128 , pp. 442-457
    • Forte, T.M.1    Nordhausen, R.W.2
  • 41
    • 0348224056 scopus 로고    scopus 로고
    • Role of helices and loops in the ability of apolipophorin-III to interact with native lipoproteins and form discoidal lipoprotein complexes
    • Chetty, P. S., Arrese, E. L., Rodriguez, V. and Soulages, J. L. (2003) Role of helices and loops in the ability of apolipophorin-III to interact with native lipoproteins and form discoidal lipoprotein complexes. Biochemistry 42, 15061-15067
    • (2003) Biochemistry , vol.42 , pp. 15061-15067
    • Chetty, P.S.1    Arrese, E.L.2    Rodriguez, V.3    Soulages, J.L.4
  • 42
    • 0035954398 scopus 로고    scopus 로고
    • Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migraforia, at low pH: Correlation with lipid binding
    • Weers, P. M. M., Kay, C. M. and Ryan, R. O. (2001) Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migraforia, at low pH: correlation with lipid binding. Biochemistry 40, 7754-7760
    • (2001) Biochemistry , vol.40 , pp. 7754-7760
    • Weers, P.M.M.1    Kay, C.M.2    Ryan, R.O.3
  • 43
    • 0037438653 scopus 로고    scopus 로고
    • Lipid binding ability of human apolipoprotein E N-terminal domain isoforms: Correlation with protein stability?
    • Weers, P. M., Narayanaswami, V., Choy, N., Luty, R., Hicks, L., Kay, C. M. and Ryan, R. O. (2003) Lipid binding ability of human apolipoprotein E N-terminal domain isoforms: correlation with protein stability? Biophys. Chem. 100, 481-492
    • (2003) Biophys. Chem. , vol.100 , pp. 481-492
    • Weers, P.M.1    Narayanaswami, V.2    Choy, N.3    Luty, R.4    Hicks, L.5    Kay, C.M.6    Ryan, R.O.7
  • 45
    • 0035852986 scopus 로고    scopus 로고
    • An N-terminal three-helix fragment of the exchangeable insect apolipoprotein apolipophorin III conserves the lipid binding properties of wild-type protein
    • Dettloff, M., Weers, P. M. M., Niete, M., Kay, C. M., Ryan, R. O. and Wiesner, A. (2001) An N-terminal three-helix fragment of the exchangeable insect apolipoprotein apolipophorin III conserves the lipid binding properties of wild-type protein. Biochemistry 40, 3150-3157
    • (2001) Biochemistry , vol.40 , pp. 3150-3157
    • Dettloff, M.1    Weers, P.M.M.2    Niete, M.3    Kay, C.M.4    Ryan, R.O.5    Wiesner, A.6
  • 46
    • 0028709475 scopus 로고
    • Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures
    • Goormaghtigh, E., Cabiaux, V. and Ruysschaert, J.-M. (1994) Determination of soluble and membrane protein structure by Fourier transform infrared spectroscopy. III. Secondary structures. Subcell. Biochem. 23, 405-450
    • (1994) Subcell. Biochem. , vol.23 , pp. 405-450
    • Goormaghtigh, E.1    Cabiaux, V.2    Ruysschaert, J.-M.3
  • 47
    • 0028977999 scopus 로고
    • Alignment of the apolipophorin-III α-helices in complex with dimyristoylphosphatidylcholine: A unique spatial orientation
    • Raussens, V., Narayanaswami, V., Goormaghtigh, E., Ryan, R. O. and Ruysschaert, J.-M. (1995) Alignment of the apolipophorin-III α-helices in complex with dimyristoylphosphatidylcholine: a unique spatial orientation. J. Biol. Chem. 270, 12542-12547
    • (1995) J. Biol. Chem. , vol.270 , pp. 12542-12547
    • Raussens, V.1    Narayanaswami, V.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.-M.5
  • 48
    • 0032476015 scopus 로고    scopus 로고
    • The low density lipoprotein receptor active conformation of apolipoprotein E: Helix organization in N-terminal domain-phospholipid disc particles
    • Raussens, V., Fisher, C. A., Goormaghtigh, E., Ryan, R. O. and Ruysschaert, J.-M. (1998) The low density lipoprotein receptor active conformation of apolipoprotein E: helix organization in N-terminal domain-phospholipid disc particles. J. Biol. Chem. 273, 25825-25830
    • (1998) J. Biol. Chem. , vol.273 , pp. 25825-25830
    • Raussens, V.1    Fisher, C.A.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.-M.5
  • 50
    • 0034718456 scopus 로고    scopus 로고
    • Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain
    • Morrow, J. A., Segall, M. L., Lund-Katz, S., Phillips, M. C., Knapp, M., Rupp, B. and Weisgraber, K. H. (2000) Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain. Biochemistry 39, 11657-11666
    • (2000) Biochemistry , vol.39 , pp. 11657-11666
    • Morrow, J.A.1    Segall, M.L.2    Lund-Katz, S.3    Phillips, M.C.4    Knapp, M.5    Rupp, B.6    Weisgraber, K.H.7
  • 51
    • 0026525924 scopus 로고
    • Apolipoprotein E: Phospholipid binding studies with synthetic peptides from the carboxyl terminus
    • Sparrow, J. T., Sparrow, D. A., Fernando, G., Culwell, A. R., Kovar, M. and Gotto, Jr, A. M. (1992) Apolipoprotein E: phospholipid binding studies with synthetic peptides from the carboxyl terminus. Biochemistry 31, 1065-1068
    • (1992) Biochemistry , vol.31 , pp. 1065-1068
    • Sparrow, J.T.1    Sparrow, D.A.2    Fernando, G.3    Culwell, A.R.4    Kovar, M.5    Gotto Jr., A.M.6
  • 54
    • 0026795513 scopus 로고
    • Synthetic model proteins: Positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils
    • Zhou, N. E., Kay, C. M. and Hodges, R. S. (1992) Synthetic model proteins: positional effects of interchain hydrophobic interactions on stability of two-stranded α-helical coiled-coils. J. Biol. Chem. 267, 2664-2670
    • (1992) J. Biol. Chem. , vol.267 , pp. 2664-2670
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 56
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., Rogers, D. P., Engler, J. A. and Brouillette, C. G. (1997) Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. U.S.A. 94, 12291-12296
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 58
    • 0034711217 scopus 로고    scopus 로고
    • Structural determination of lipid-bound ApoA-I using fluorescence resonance energy transfer
    • Li, H., Lyles, D. S., Thomas, M. J., Pan, W. and Sorci-Thomas, M. G. (2000) Structural determination of lipid-bound ApoA-I using fluorescence resonance energy transfer. J. Biol. Chem. 275, 37048-37054
    • (2000) J. Biol. Chem. , vol.275 , pp. 37048-37054
    • Li, H.1    Lyles, D.S.2    Thomas, M.J.3    Pan, W.4    Sorci-Thomas, M.G.5
  • 59
    • 0037131260 scopus 로고    scopus 로고
    • ApoA-I structure on discs and spheres: Variable helix registry and conformational states
    • Li, H., Lyles, D. S., Pan, W., Alexander, E., Thomas, M. J. and Sorci-Thomas, M. G. (2002) ApoA-I structure on discs and spheres: variable helix registry and conformational states. J. Biol. Chem. 277, 39093-39101
    • (2002) J. Biol. Chem. , vol.277 , pp. 39093-39101
    • Li, H.1    Lyles, D.S.2    Pan, W.3    Alexander, E.4    Thomas, M.J.5    Sorci-Thomas, M.G.6
  • 60
    • 0020558225 scopus 로고
    • Formation of cholesterol- and apoprotein E-enriched high density lipoproteins in vitro
    • Gordon, V., Innerarity, T. L. and Mahley, R. W. (1983) Formation of cholesterol- and apoprotein E-enriched high density lipoproteins in vitro. J. Biol. Chem. 258, 6202-6212
    • (1983) J. Biol. Chem. , vol.258 , pp. 6202-6212
    • Gordon, V.1    Innerarity, T.L.2    Mahley, R.W.3
  • 61
    • 0022354295 scopus 로고
    • Obligatory role of cholesterol and apolipoprotein E in the formation of large cholesterol-enriched and receptor-active high density lipoproteins
    • Koo, C., Innerarity, T. L. and Mahley, R. W. (1985) Obligatory role of cholesterol and apolipoprotein E in the formation of large cholesterol-enriched and receptor-active high density lipoproteins. J. Biol. Chem. 260, 11934-11943
    • (1985) J. Biol. Chem. , vol.260 , pp. 11934-11943
    • Koo, C.1    Innerarity, T.L.2    Mahley, R.W.3
  • 62
    • 0037443625 scopus 로고    scopus 로고
    • Homo- and hetero-complexes of exchangeable apolipoproteins in solution and in lipid-bound form
    • Dergunov, A. D., Voratnikova, Y. Y., Visvikis, S. and Siest, G. (2003) Homo- and hetero-complexes of exchangeable apolipoproteins in solution and in lipid-bound form. Spectrochim. Acta Part A 59, 1127-1137
    • (2003) Spectrochim. Acta Part A , vol.59 , pp. 1127-1137
    • Dergunov, A.D.1    Voratnikova, Y.Y.2    Visvikis, S.3    Siest, G.4
  • 63
    • 0032839621 scopus 로고    scopus 로고
    • Apolipoprotein E: From atherosclerosis to Alzheimer's disease and beyond
    • Manley, R. W. and Huang, Y. (1999) Apolipoprotein E: from atherosclerosis to Alzheimer's disease and beyond. Curr. Opin. Lipidol. 10, 207-217
    • (1999) Curr. Opin. Lipidol. , vol.10 , pp. 207-217
    • Manley, R.W.1    Huang, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.