메뉴 건너뛰기




Volumn 1483, Issue 1, 2000, Pages 15-36

Molecular basis of exchangeable apolipoprotein function

Author keywords

Apolipophorin III; Apolipoprotein A I; Apolipoprotein E; Biophysical characterization; Conformational flexibility; Exchangeable apolipoprotein; Lipid free structure; Spectroscopy

Indexed keywords

APOLIPOPHORIN III; APOLIPOPROTEIN; APOLIPOPROTEIN A1; APOLIPOPROTEIN E; LIPOPROTEIN RECEPTOR; PHOSPHATIDYLCHOLINE STEROL ACYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 0033991858     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(99)00176-6     Document Type: Review
Times cited : (160)

References (119)
  • 4
    • 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., Agard D.A. Three dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science. 252:1991;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
  • 5
    • 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., Brouillette C.G. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA. 94:1997;12291-12296.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 6
    • 0030875963 scopus 로고    scopus 로고
    • Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional NMR techniques
    • Wang J., Gagne S., Sykes B.D., Ryan R.O. Insight into lipid surface recognition and reversible conformational adaptations of an exchangeable apolipoprotein by multidimensional NMR techniques. J. Biol. Chem. 272:1997;17912-17921.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17912-17921
    • Wang, J.1    Gagne, S.2    Sykes, B.D.3    Ryan, R.O.4
  • 7
    • 0028216403 scopus 로고
    • Lipophorin: The structure of an insect lipoprotein and its role in lipid transport in insects
    • Soulages J.L., Wells M.A. Lipophorin: the structure of an insect lipoprotein and its role in lipid transport in insects. Adv. Protein Chem. 45:1994;371-415.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 371-415
    • Soulages, J.L.1    Wells, M.A.2
  • 8
    • 0030344951 scopus 로고    scopus 로고
    • Structural studies of lipoproteins and their apolipoprotein components
    • Ryan R.O. Structural studies of lipoproteins and their apolipoprotein components. Biochem. Cell Biol. 72:1996;155-164.
    • (1996) Biochem. Cell Biol. , vol.72 , pp. 155-164
    • Ryan, R.O.1
  • 9
    • 0030822665 scopus 로고    scopus 로고
    • Protein-lipid interactions of apolipophorin III, a model exchangeable amphipathic apolipoprotein
    • Narayanaswami V., Ryan R.O. Protein-lipid interactions of apolipophorin III, a model exchangeable amphipathic apolipoprotein. Biochem. Soc. Trans. 25:1997;1113-1118.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 1113-1118
    • Narayanaswami, V.1    Ryan, R.O.2
  • 10
    • 0028303072 scopus 로고
    • Apolipoprotein E: Structure-function relationships
    • Weisgraber K.H. Apolipoprotein E: structure-function relationships. Adv. Protein Chem. 45:1994;249-302.
    • (1994) Adv. Protein Chem. , vol.45 , pp. 249-302
    • Weisgraber, K.H.1
  • 12
    • 0034107475 scopus 로고    scopus 로고
    • Insect lipids: Biochemistry and role in energy production
    • in press
    • R.O. Ryan, D.J. van der Horst, Insect lipids: biochemistry and role in energy production, Annu. Rev. Entomol. 45 (2000) in press.
    • (2000) Annu. Rev. Entomol. , vol.45
    • Ryan, R.O.1    Van Der Horst, D.J.2
  • 13
    • 0031025274 scopus 로고    scopus 로고
    • Adipokinetic hormone-induced lipolysis in fat body of an insect, Manduca sexta: Synthesis of sn-1,2 diacylglycerols
    • Arresse E.L., Wells M.A. Adipokinetic hormone-induced lipolysis in fat body of an insect, Manduca sexta: synthesis of sn-1,2 diacylglycerols. J. Lipid Res. 38:1997;68-76.
    • (1997) J. Lipid Res. , vol.38 , pp. 68-76
    • Arresse, E.L.1    Wells, M.A.2
  • 15
    • 0023664091 scopus 로고
    • Role of apolipophorin III in in vivo lipoprotein interconversions in adult Manduca sexta
    • Wells M.A., Ryan R.O., Kawooya J.K., Law J.H. Role of apolipophorin III in in vivo lipoprotein interconversions in adult Manduca sexta. J. Biol. Chem. 262:1987;4172-4176.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4172-4176
    • Wells, M.A.1    Ryan, R.O.2    Kawooya, J.K.3    Law, J.H.4
  • 16
    • 0028279012 scopus 로고
    • Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin. Correlation with binding of apolipophorin III
    • Soulages J.L., Wells M.A. Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin. Correlation with binding of apolipophorin III. Biochemistry. 33:1994;2356-2362.
    • (1994) Biochemistry , vol.33 , pp. 2356-2362
    • Soulages, J.L.1    Wells, M.A.2
  • 18
    • 0027391142 scopus 로고
    • Conformational, thermodynamic and stability properties of insect apolipophorin III as determined by circular dichroism and fluorescence spectroscopy
    • Ryan R.O., Oikawa K., Kay C.M. Conformational, thermodynamic and stability properties of insect apolipophorin III as determined by circular dichroism and fluorescence spectroscopy. J. Biol. Chem. 268:1993;1525-1530.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1525-1530
    • Ryan, R.O.1    Oikawa, K.2    Kay, C.M.3
  • 19
  • 21
    • 0023900109 scopus 로고
    • Human apolipoprotein E3 in aqueous solution I. Evidence for two structural domains
    • Wetterau J.R., Aggerbeck L.P., Rall S.C. Jr., Weisgraber K.H. Human apolipoprotein E3 in aqueous solution I. Evidence for two structural domains. J. Biol. Chem. 263:1988;6240-6248.
    • (1988) J. Biol. Chem. , vol.263 , pp. 6240-6248
    • Wetterau, J.R.1    Aggerbeck, L.P.2    Rall S.C., Jr.3    Weisgraber, K.H.4
  • 22
    • 0033551071 scopus 로고    scopus 로고
    • A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein
    • Narayanaswami V., Wang J., Schieve D., Kay C.M., Ryan R.O. A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. USA. 96:1999;4366-4371.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4366-4371
    • Narayanaswami, V.1    Wang, J.2    Schieve, D.3    Kay, C.M.4    Ryan, R.O.5
  • 23
    • 0028096954 scopus 로고
    • Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta
    • Narayanaswami V., Kay C.M., Oikawa K., Ryan R.O. Structural and binding characteristics of the carboxyl terminal fragment of apolipophorin III from Manduca sexta. Biochemistry. 33:1994;13312-13320.
    • (1994) Biochemistry , vol.33 , pp. 13312-13320
    • Narayanaswami, V.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 25
    • 0031935716 scopus 로고    scopus 로고
    • Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins
    • Wang J., Narayanaswami V., Sykes B.D., Ryan R.O. Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins. Protein Sci. 7:1998;336-341.
    • (1998) Protein Sci. , vol.7 , pp. 336-341
    • Wang, J.1    Narayanaswami, V.2    Sykes, B.D.3    Ryan, R.O.4
  • 28
    • 0027405920 scopus 로고
    • Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-amino-ethylphosphonate as a constituent of a glycoprotein
    • Hård K., Van Doorn J.M., Thomas-Oates J.E., Kamerling J.P., Van der Horst D.J. Structure of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-amino-ethylphosphonate as a constituent of a glycoprotein. Biochemistry. 32:1993;766-775.
    • (1993) Biochemistry , vol.32 , pp. 766-775
    • Hård, K.1    Van Doorn, J.M.2    Thomas-Oates, J.E.3    Kamerling, J.P.4    Van Der Horst, D.J.5
  • 29
    • 0033618275 scopus 로고    scopus 로고
    • Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34 and 95 in Locusta migratoria apolipophorin III
    • Weers P.M.M., Narayanaswami V., Kay C.M., Ryan R.O. Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34 and 95 in Locusta migratoria apolipophorin III. J. Biol. Chem. 274:1999;21804-21810.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21804-21810
    • Weers, P.M.M.1    Narayanaswami, V.2    Kay, C.M.3    Ryan, R.O.4
  • 30
    • 0032512547 scopus 로고    scopus 로고
    • Role of glycosylation in the lipid binding activity of the exchangeable apolipoprotein, apolipophorin III
    • Soulages J.L., Pennington J., Bendavid O., Wells M.A. Role of glycosylation in the lipid binding activity of the exchangeable apolipoprotein, apolipophorin III. Biochem. Biophys. Res. Commun. 243:1998;372-376.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 372-376
    • Soulages, J.L.1    Pennington, J.2    Bendavid, O.3    Wells, M.A.4
  • 31
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: Evidence for a conformational change
    • Wientzek M., Kay C.M., Oikawa K., Ryan R.O. Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles: evidence for a conformational change. J. Biol. Chem. 269:1994;4605-4612.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4605-4612
    • Wientzek, M.1    Kay, C.M.2    Oikawa, K.3    Ryan, R.O.4
  • 32
    • 0027524130 scopus 로고
    • Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins
    • Liu H., Scraba D.G., Ryan R.O. Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins. FEBS Lett. 316:1993;27-33.
    • (1993) FEBS Lett. , vol.316 , pp. 27-33
    • Liu, H.1    Scraba, D.G.2    Ryan, R.O.3
  • 33
    • 0342781230 scopus 로고
    • Phagocytosis of aggregated lipoprotein by macrophages: Low density lipoprotein receptor-dependent foam cell formation
    • Suits A.G., Chait A., Aviram M., Heinecke J.W. Phagocytosis of aggregated lipoprotein by macrophages: low density lipoprotein receptor-dependent foam cell formation. Proc. Natl. Acad. Sci. USA. 86:1989;2713-2717.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2713-2717
    • Suits, A.G.1    Chait, A.2    Aviram, M.3    Heinecke, J.W.4
  • 34
    • 0026803139 scopus 로고
    • Conversion of human low density lipoprotein into a very low density lipoprotein-like particle in vitro
    • Singh T.K.A., Scraba D.G., Ryan R.O. Conversion of human low density lipoprotein into a very low density lipoprotein-like particle in vitro. J. Biol. Chem. 267:1992;9275-9280.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9275-9280
    • Singh, T.K.A.1    Scraba, D.G.2    Ryan, R.O.3
  • 35
    • 0021942104 scopus 로고
    • Fusion of low density lipoproteins with cholesterol ester-phospholipid microemulsions
    • Parks J.S., Martin J.A., Johnson F.L., Rudel L.L. Fusion of low density lipoproteins with cholesterol ester-phospholipid microemulsions. J. Biol. Chem. 260:1985;3155-3163.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3155-3163
    • Parks, J.S.1    Martin, J.A.2    Johnson, F.L.3    Rudel, L.L.4
  • 37
    • 0030270732 scopus 로고    scopus 로고
    • Fluorescence studies of lipid-association induced conformational adaptations of an exchangeable amphipathic apolipoprotein
    • Narayanaswami V., Frolov A., Schroeder F., Oikawa K., Kay C.M., Ryan R.O. Fluorescence studies of lipid-association induced conformational adaptations of an exchangeable amphipathic apolipoprotein. Arch. Biochem. Biophys. 334:1996;143-150.
    • (1996) Arch. Biochem. Biophys. , vol.334 , pp. 143-150
    • Narayanaswami, V.1    Frolov, A.2    Schroeder, F.3    Oikawa, K.4    Kay, C.M.5    Ryan, R.O.6
  • 38
    • 0029967954 scopus 로고    scopus 로고
    • Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding
    • Narayanaswami V., Wang J., Kay C.M., Scraba D.G., Ryan R.O. Disulfide bond engineering to monitor conformational opening of apolipophorin III during lipid binding. J. Biol. Chem. 271:1996;26855-26862.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26855-26862
    • Narayanaswami, V.1    Wang, J.2    Kay, C.M.3    Scraba, D.G.4    Ryan, R.O.5
  • 39
    • 0032469624 scopus 로고    scopus 로고
    • NMR evidence for a conformational adaptation of apolipophorin III upon lipid association
    • Wang J., Sahoo D., Sykes B.D., Ryan R.O. NMR evidence for a conformational adaptation of apolipophorin III upon lipid association. Biochem. Cell Biol. 76:1998;276-283.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 276-283
    • Wang, J.1    Sahoo, D.2    Sykes, B.D.3    Ryan, R.O.4
  • 40
    • 0028977999 scopus 로고
    • J Alignment of apolipophorin III α-helices in complex with dimyristoylphosphatidylcholine: A unique spatial orientation
    • Raussens V., Goormaghtigh E., Narayanaswami V., Ryan R.O., Ruysschaert J.-M. J Alignment of apolipophorin III α-helices in complex with dimyristoylphosphatidylcholine: a unique spatial orientation. J. Biol. Chem. 270:1995;12542-12547.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12542-12547
    • Raussens, V.1    Goormaghtigh, E.2    Narayanaswami, V.3    Ryan, R.O.4    Ruysschaert, J.-M.5
  • 41
    • 0029813440 scopus 로고    scopus 로고
    • Hydrogen/deuterium exchange kinetics of apolipophorin III in lipid free and phospholipid bound states. An analysis by Fourier transform infrared spectroscopy
    • Raussens V., Narayanaswami V., Goormaghtigh E., Ryan R.O., Ruysschaert J.-M. Hydrogen/deuterium exchange kinetics of apolipophorin III in lipid free and phospholipid bound states. An analysis by Fourier transform infrared spectroscopy. J. Biol. Chem. 271:1996;23089-23095.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23089-23095
    • Raussens, V.1    Narayanaswami, V.2    Goormaghtigh, E.3    Ryan, R.O.4    Ruysschaert, J.-M.5
  • 42
    • 0031914422 scopus 로고    scopus 로고
    • Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces
    • Sahoo D., Narayanaswami V., Oikawa K., Kay C.M., Ryan R.O. Fluorescence studies of exchangeable apolipoprotein-lipid interactions. Superficial association of apolipophorin III with lipoprotein surfaces. J. Biol. Chem. 273:1998;1403-1408.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1403-1408
    • Sahoo, D.1    Narayanaswami, V.2    Oikawa, K.3    Kay, C.M.4    Ryan, R.O.5
  • 43
    • 0029048818 scopus 로고
    • Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: A surface plasmon resonance spectroscopy study
    • Soulages J.L., Salamon Z., Wells M.A., Tollin G. Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: a surface plasmon resonance spectroscopy study. Proc. Natl. Acad. Sci. USA. 92:1995;5650-5654.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5650-5654
    • Soulages, J.L.1    Salamon, Z.2    Wells, M.A.3    Tollin, G.4
  • 45
    • 0028875755 scopus 로고
    • Human hepatic and lipoprotein lipase: The loop covering the catalytic site mediates lipase substrate specificity
    • Dugi K.A., Dichek H.L., Santamarina-Fojo S. Human hepatic and lipoprotein lipase: the loop covering the catalytic site mediates lipase substrate specificity. J. Biol. Chem. 270:1995;25396-25401.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25396-25401
    • Dugi, K.A.1    Dichek, H.L.2    Santamarina-Fojo, S.3
  • 46
    • 0032516486 scopus 로고    scopus 로고
    • The lipid binding activity of the exchangeable apolipoprotein apolipophorin III correlates with the formation of a partially folded conformation
    • Soulages J.L., Bendavid O.J. The lipid binding activity of the exchangeable apolipoprotein apolipophorin III correlates with the formation of a partially folded conformation. Biochemistry. 37:1998;10203-10210.
    • (1998) Biochemistry , vol.37 , pp. 10203-10210
    • Soulages, J.L.1    Bendavid, O.J.2
  • 47
    • 0024299370 scopus 로고
    • Apolipoprotein E: Cholesterol transport protein with expanding role in cell biology
    • Mahley R.W. Apolipoprotein E: cholesterol transport protein with expanding role in cell biology. Science. 240:1988;622-630.
    • (1988) Science , vol.240 , pp. 622-630
    • Mahley, R.W.1
  • 48
    • 0040177065 scopus 로고
    • Low density lipoprotein receptor-related protein mediates uptake of cholesterol esters derived from apoprotein E-enriched lipoproteins
    • Kowal R.C., Herz J., Goldstein J.L., Esser V., Brown M.S. Low density lipoprotein receptor-related protein mediates uptake of cholesterol esters derived from apoprotein E-enriched lipoproteins. Proc. Natl. Acad. Sci. USA. 86:1989;5810-5814.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5810-5814
    • Kowal, R.C.1    Herz, J.2    Goldstein, J.L.3    Esser, V.4    Brown, M.S.5
  • 49
    • 0026778830 scopus 로고
    • Rabbit very low density lipoprotein receptor: A low density lipoprotein receptor-like protein with distinct ligand specificity
    • Takahashi S., Kawarabayasi Y., Nakai Y., Saskai J., Yamamoto T. Rabbit very low density lipoprotein receptor: a low density lipoprotein receptor-like protein with distinct ligand specificity. Proc. Natl. Acad. Sci. USA. 89:1992;9252-9256.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9252-9256
    • Takahashi, S.1    Kawarabayasi, Y.2    Nakai, Y.3    Saskai, J.4    Yamamoto, T.5
  • 50
    • 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., Lindgren F.T. Human apolipoprotein E3 in aqueous solution II. Properties of the amino- and carboxyl-terminal domains. J. Biol. Chem. 263:1988;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
  • 51
    • 0025171570 scopus 로고
    • Apolipoprotein E distribution among human plasma lipoproteins: Role of cysteine-arginine interchange at position 112
    • Weisgraber K.H. Apolipoprotein E distribution among human plasma lipoproteins: role of cysteine-arginine interchange at position 112. J. Lipid Res. 31:1990;1503-1511.
    • (1990) J. Lipid Res. , vol.31 , pp. 1503-1511
    • Weisgraber, K.H.1
  • 52
    • 0027186135 scopus 로고
    • Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization
    • Westerlund J.A., Weisgraber K.H. Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization. J. Biol. Chem. 268:1993;15745-15750.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15745-15750
    • Westerlund, J.A.1    Weisgraber, K.H.2
  • 53
    • 0017663203 scopus 로고
    • Inhibition of lipoprotein binding to cell surface receptors of fibroblasts following selective modification of arginyl residues in arginine-rich and B apoproteins
    • Mahley R.W., Innerarity T.L., Pitas R.E., Weisgraber K.H., Brown J.H., Gross E. Inhibition of lipoprotein binding to cell surface receptors of fibroblasts following selective modification of arginyl residues in arginine-rich and B apoproteins. J. Biol. Chem. 252:1977;7279-7287.
    • (1977) J. Biol. Chem. , vol.252 , pp. 7279-7287
    • Mahley, R.W.1    Innerarity, T.L.2    Pitas, R.E.3    Weisgraber, K.H.4    Brown, J.H.5    Gross, E.6
  • 54
    • 0018238837 scopus 로고
    • Role of the lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts
    • Weisgraber K.H., Innerarity T.L., Mahley R.W. Role of the lysine residues of plasma lipoproteins in high affinity binding to cell surface receptors on human fibroblasts. J. Biol. Chem. 253:1978;9053-9062.
    • (1978) J. Biol. Chem. , vol.253 , pp. 9053-9062
    • Weisgraber, K.H.1    Innerarity, T.L.2    Mahley, R.W.3
  • 56
    • 0018800929 scopus 로고
    • Binding of arginine-rich (E) apolipoprotein after recombination with phospholipid vesicles to low density lipoprotein receptors of fibroblasts
    • Innerarity T.L., Pitas R.E., Mahley R.W. Binding of arginine-rich (E) apolipoprotein after recombination with phospholipid vesicles to low density lipoprotein receptors of fibroblasts. J. Biol. Chem. 254:1979;4186-4190.
    • (1979) J. Biol. Chem. , vol.254 , pp. 4186-4190
    • Innerarity, T.L.1    Pitas, R.E.2    Mahley, R.W.3
  • 57
    • 0021211156 scopus 로고
    • Normalization of receptor binding of apolipoprotein E2. Evidence for modulation of the binding site conformation
    • Innerarity T.L., Weisgraber K.H., Arnold K.S., Rall S.C. Jr., Mahley R.W. Normalization of receptor binding of apolipoprotein E2. Evidence for modulation of the binding site conformation. J. Biol. Chem. 259:1984;7261-7267.
    • (1984) J. Biol. Chem. , vol.259 , pp. 7261-7267
    • Innerarity, T.L.1    Weisgraber, K.H.2    Arnold, K.S.3    Rall S.C., Jr.4    Mahley, R.W.5
  • 60
    • 0023860891 scopus 로고
    • Apolipoprotein E polymorphism and atherosclerosis
    • Davignon J., Gregg R.E., Sing C.F. Apolipoprotein E polymorphism and atherosclerosis. Arteriosclerosis. 8:1988;1-21.
    • (1988) Arteriosclerosis , vol.8 , pp. 1-21
    • Davignon, J.1    Gregg, R.E.2    Sing, C.F.3
  • 62
    • 0028774042 scopus 로고
    • Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein
    • Wilson C., Mau T., Weisgraber K.H., Wardell M.R., Mahley R.W., Agard D.A. Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein. Structure. 2:1994;713-718.
    • (1994) Structure , vol.2 , pp. 713-718
    • Wilson, C.1    Mau, T.2    Weisgraber, K.H.3    Wardell, M.R.4    Mahley, R.W.5    Agard, D.A.6
  • 63
    • 0029766916 scopus 로고    scopus 로고
    • Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins
    • Dong L.-M., Weisgraber K.H. Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins. J. Biol. Chem. 271:1996;19053-19057.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19053-19057
    • Dong, L.-M.1    Weisgraber, K.H.2
  • 65
    • 0032894924 scopus 로고    scopus 로고
    • Lipid binding-induced conformational changes in the N-terminal domain of apolipoprotein E
    • Fisher C.A., Ryan R.O. Lipid binding-induced conformational changes in the N-terminal domain of apolipoprotein E. J. Lipid Res. 40:1999;93-99.
    • (1999) J. Lipid Res. , vol.40 , pp. 93-99
    • Fisher, C.A.1    Ryan, R.O.2
  • 66
    • 0029101725 scopus 로고
    • Comparison of lipid binding and lecithin:cholesterol acyltransferase activation of the amino- And carboxyl-terminal domains of human apolipoprotein E3
    • de Pauw M., Vanloo B., Weisgraber K.H., Rosseneu M. Comparison of lipid binding and lecithin:cholesterol acyltransferase activation of the amino- and carboxyl-terminal domains of human apolipoprotein E3. Biochemistry. 34:1995;10953-10960.
    • (1995) Biochemistry , vol.34 , pp. 10953-10960
    • De Pauw, M.1    Vanloo, B.2    Weisgraber, K.H.3    Rosseneu, M.4
  • 67
    • 0032476015 scopus 로고    scopus 로고
    • The LDL 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., Ruysschaert J.-M. The LDL receptor active conformation of apolipoprotein E. Helix organization in N-terminal domain-phospholipid disc particles. J. Biol. Chem. 273:1998;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
  • 69
    • 0023798732 scopus 로고
    • Heterogeneity of apolipoprotein E epitope expression on human lipoproteins: Importance for apolipoprotein E function
    • Krul E.S., Tikkanen M., Schonfeld G. Heterogeneity of apolipoprotein E epitope expression on human lipoproteins: importance for apolipoprotein E function. J. Lipid Res. 29:1988;1309-1325.
    • (1988) J. Lipid Res. , vol.29 , pp. 1309-1325
    • Krul, E.S.1    Tikkanen, M.2    Schonfeld, G.3
  • 70
    • 0019174354 scopus 로고
    • Determinants of hepatic uptake of triglyceride-rich lipoproteins and their remnants in the rat
    • Windler E., Chao Y., Havel R.J. Determinants of hepatic uptake of triglyceride-rich lipoproteins and their remnants in the rat. J. Biol Chem. 255:1980;5475-5480.
    • (1980) J. Biol Chem. , vol.255 , pp. 5475-5480
    • Windler, E.1    Chao, Y.2    Havel, R.J.3
  • 71
    • 0019138139 scopus 로고
    • Regulation of the hepatic uptake of triglyceride-rich lipoproteins in the rat. Opposing effects of homologous apolipoprotein E and individual C apolipoproteins
    • Windler E., Chao Y., Havel R.J. Regulation of the hepatic uptake of triglyceride-rich lipoproteins in the rat. Opposing effects of homologous apolipoprotein E and individual C apolipoproteins. J. Biol. Chem. 255:1980;8303-8307.
    • (1980) J. Biol. Chem. , vol.255 , pp. 8303-8307
    • Windler, E.1    Chao, Y.2    Havel, R.J.3
  • 72
    • 0021798836 scopus 로고
    • Inhibitory effects of C apolipoproteins from rats and humans on the uptake of triglyceride-rich lipoproteins and their remnants by perfused rat liver
    • Windler E., Havel R.J. Inhibitory effects of C apolipoproteins from rats and humans on the uptake of triglyceride-rich lipoproteins and their remnants by perfused rat liver. J. Lipid Res. 26:1985;556-565.
    • (1985) J. Lipid Res. , vol.26 , pp. 556-565
    • Windler, E.1    Havel, R.J.2
  • 73
    • 0018834489 scopus 로고
    • Effect of apoproteins on hepatic uptake of triglyceride emulsions in the rat
    • Shelburne F., Hanks J., Meyers W., Quarfordt S. Effect of apoproteins on hepatic uptake of triglyceride emulsions in the rat. J. Clin. Invest. 65:1980;652-658.
    • (1980) J. Clin. Invest. , vol.65 , pp. 652-658
    • Shelburne, F.1    Hanks, J.2    Meyers, W.3    Quarfordt, S.4
  • 74
    • 0025302165 scopus 로고
    • Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein
    • Kowal R.C., Herz J., Weisgraber K.H., Mahley R.W., Brown M.S., Goldstein J.L. Opposing effects of apolipoproteins E and C on lipoprotein binding to low density lipoprotein receptor-related protein. J. Biol. Chem. 265:1990;10771-10779.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10771-10779
    • Kowal, R.C.1    Herz, J.2    Weisgraber, K.H.3    Mahley, R.W.4    Brown, M.S.5    Goldstein, J.L.6
  • 75
    • 0025611153 scopus 로고
    • Apolipoprotein C-I modulates the interaction of apolipoprotein E with β-migrating very low density lipoproteins (β-VLDL) and inhibits binding of β-VLDL to low density lipoprotein receptor-related protein
    • Weisgraber K.H., Mahley R.W., Kowal R.C., Herz J., Goldstein J.L., Brown M.S. Apolipoprotein C-I modulates the interaction of apolipoprotein E with β-migrating very low density lipoproteins (β-VLDL) and inhibits binding of β-VLDL to low density lipoprotein receptor-related protein. J. Biol. Chem. 265:1990;22453-22459.
    • (1990) J. Biol. Chem. , vol.265 , pp. 22453-22459
    • Weisgraber, K.H.1    Mahley, R.W.2    Kowal, R.C.3    Herz, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 76
    • 0019799613 scopus 로고
    • Hepatic uptake of phospholipid-depleted chylomicrons in vivo. Comparison of uptake with chylomicron remnants
    • Borensztajn J., Kotlar T.J. Hepatic uptake of phospholipid-depleted chylomicrons in vivo. Comparison of uptake with chylomicron remnants. Biochem. J. 200:1981;547-553.
    • (1981) Biochem. J. , vol.200 , pp. 547-553
    • Borensztajn, J.1    Kotlar, T.J.2
  • 77
    • 0023740622 scopus 로고
    • Uptake of chylomicron remnants by the liver: Further evidence for the modulating role of phospholipids
    • Borensztajn J., Getz G.S., Kotlar T.J. Uptake of chylomicron remnants by the liver: further evidence for the modulating role of phospholipids. J. Lipid Res. 29:1988;1087-1096.
    • (1988) J. Lipid Res. , vol.29 , pp. 1087-1096
    • Borensztajn, J.1    Getz, G.S.2    Kotlar, T.J.3
  • 78
    • 0025835486 scopus 로고
    • Lipolysis exposes unreactive endogenous apolipoprotein E-3 in human and rat plasma very low density lipoprotein
    • Sehayek E., Lewin-Velvert U., Chajek-Shaul T., Eisenberg S. Lipolysis exposes unreactive endogenous apolipoprotein E-3 in human and rat plasma very low density lipoprotein. J. Clin. Invest. 88:1991;553-560.
    • (1991) J. Clin. Invest. , vol.88 , pp. 553-560
    • Sehayek, E.1    Lewin-Velvert, U.2    Chajek-Shaul, T.3    Eisenberg, S.4
  • 79
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolemia from structure of LDL receptor module
    • Fass D., Blacklow S., Kim P., Berger J.M. Molecular basis of familial hypercholesterolemia from structure of LDL receptor module. Nature. 388:1997;691-693.
    • (1997) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.3    Berger, J.M.4
  • 80
    • 0024806811 scopus 로고
    • Different combinations of cysteine-rich repeats mediate binding of low density lipoprotein receptor to two different proteins
    • Russell D.W., Brown M.S., Goldstein J.L. Different combinations of cysteine-rich repeats mediate binding of low density lipoprotein receptor to two different proteins. J. Biol. Chem. 264:1989;21682-21688.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21682-21688
    • Russell, D.W.1    Brown, M.S.2    Goldstein, J.L.3
  • 81
    • 0030459796 scopus 로고    scopus 로고
    • Expression and characterization of a truncated, soluble, low-density lipoprotein receptor
    • Dirlam K.A., Gretch D.G., LaCount D.J., Sturley S.L., Attie A.D. Expression and characterization of a truncated, soluble, low-density lipoprotein receptor. Protein Expr. Purif. 8:1996;489-500.
    • (1996) Protein Expr. Purif. , vol.8 , pp. 489-500
    • Dirlam, K.A.1    Gretch, D.G.2    Lacount, D.J.3    Sturley, S.L.4    Attie, A.D.5
  • 82
    • 0030830186 scopus 로고    scopus 로고
    • Human low density lipoprotein receptor fragment. Successful refolding of a functionally active ligand-binding domain produced in Escherichia coli
    • Simmons T., Newhouse Y.M., Arnold K.S., Innerarity T.L., Weisgraber K.H. Human low density lipoprotein receptor fragment. Successful refolding of a functionally active ligand-binding domain produced in Escherichia coli. J. Biol. Chem. 272:1997;25531-25536.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25531-25536
    • Simmons, T.1    Newhouse, Y.M.2    Arnold, K.S.3    Innerarity, T.L.4    Weisgraber, K.H.5
  • 83
    • 0028887870 scopus 로고
    • Molecular physiology of reverse cholesterol transport
    • Fielding C.J., Fielding P.E. Molecular physiology of reverse cholesterol transport. J. Lipid Res. 36:1995;211-228.
    • (1995) J. Lipid Res. , vol.36 , pp. 211-228
    • Fielding, C.J.1    Fielding, P.E.2
  • 84
    • 0032550773 scopus 로고    scopus 로고
    • Apolipoprotein mediated cellular cholesterol efflux
    • Yokoyama S. Apolipoprotein mediated cellular cholesterol efflux. Biochim. Biophys. Acta. 1392:1998;1-15.
    • (1998) Biochim. Biophys. Acta , vol.1392 , pp. 1-15
    • Yokoyama, S.1
  • 86
    • 0031935662 scopus 로고    scopus 로고
    • An overview of reverse cholesterol transport
    • Tall A.R. An overview of reverse cholesterol transport. Eur. Heart J. 19:1998;A31-35.
    • (1998) Eur. Heart J. , vol.19 , pp. 31-35
    • Tall, A.R.1
  • 87
    • 0031777005 scopus 로고    scopus 로고
    • High density lipoproteins and reverse cholesterol transport: Lessons from mutations
    • von Eckardstein A., Assmann G. High density lipoproteins and reverse cholesterol transport: lessons from mutations. Atherosclerosis. 137:1998;S7-11.
    • (1998) Atherosclerosis , vol.137 , pp. 7-11
    • Von Eckardstein, A.1    Assmann, G.2
  • 88
    • 0026736891 scopus 로고
    • Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism
    • Nolte R.T., Atkinson D. Conformational analysis of apolipoprotein A-I and E-3 based on primary sequence and circular dichroism. Biophys. J. 63:1992;1221-1239.
    • (1992) Biophys. J. , vol.63 , pp. 1221-1239
    • Nolte, R.T.1    Atkinson, D.2
  • 90
    • 0030820806 scopus 로고    scopus 로고
    • The carboxyl-terminal hydrophobic residues of apolipoprotein A-I affect its rate of phospholipid binding and its association with high density lipoprotein
    • Laccotrippe M., Makrides S.C., Jonas A., Zannis V.I. The carboxyl-terminal hydrophobic residues of apolipoprotein A-I affect its rate of phospholipid binding and its association with high density lipoprotein. J. Biol. Chem. 272:1997;17511-17522.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17511-17522
    • Laccotrippe, M.1    Makrides, S.C.2    Jonas, A.3    Zannis, V.I.4
  • 91
    • 0030900911 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein A-I: Limited proteolysis of methionine-reduced and-oxidized lipid-free and lipid-bound human apoA-I
    • Roberts L.M., Ray M.J., Shih T.-W., Hayden E., Reader M.M., Brouillette C.G. Structural analysis of apolipoprotein A-I: limited proteolysis of methionine-reduced and-oxidized lipid-free and lipid-bound human apoA-I. Biochemistry. 36:1997;7615-7624.
    • (1997) Biochemistry , vol.36 , pp. 7615-7624
    • Roberts, L.M.1    Ray, M.J.2    Shih, T.-W.3    Hayden, E.4    Reader, M.M.5    Brouillette, C.G.6
  • 92
    • 0033528673 scopus 로고    scopus 로고
    • Amphipathic α-helix bundle organization of lipid-free chicken apolipoprotein A-I
    • Kiss R.S., Kay C.M., Ryan R.O. Amphipathic α-helix bundle organization of lipid-free chicken apolipoprotein A-I. Biochemistry. 38:1999;4327-4334.
    • (1999) Biochemistry , vol.38 , pp. 4327-4334
    • Kiss, R.S.1    Kay, C.M.2    Ryan, R.O.3
  • 93
    • 0027257427 scopus 로고
    • Physical properties of apolipoprotein A-I from the chicken, Gallus domesticus
    • Kiss R.S., Ryan R.O., Hicks L.D., Oikawa K., Kay C.M. Physical properties of apolipoprotein A-I from the chicken, Gallus domesticus. Biochemistry. 32:1993;7872-7878.
    • (1993) Biochemistry , vol.32 , pp. 7872-7878
    • Kiss, R.S.1    Ryan, R.O.2    Hicks, L.D.3    Oikawa, K.4    Kay, C.M.5
  • 94
    • 0032972962 scopus 로고    scopus 로고
    • Effect of apolipoprotein A-I lipidation on the formation and function of pre-β And α-migrating LpA-I particles
    • Sparks D.L., Frank P.G., Braschi S., Neville T.A.-M., Marcel Y.L. Effect of apolipoprotein A-I lipidation on the formation and function of pre-β and α-migrating LpA-I particles. Biochemistry. 38:1999;1727-1735.
    • (1999) Biochemistry , vol.38 , pp. 1727-1735
    • Sparks, D.L.1    Frank, P.G.2    Braschi, S.3    Neville, T.A.-M.4    Marcel, Y.L.5
  • 98
    • 0032548464 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein A-I: Effects of amino- And carboxy-terminal deletions on the lipid-free structure
    • Rogers D.P., Roberts L.M., Lebowitz J., Engler J.A., Brouillette C.G. Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure. Biochemistry. 37:1998;945-955.
    • (1998) Biochemistry , vol.37 , pp. 945-955
    • Rogers, D.P.1    Roberts, L.M.2    Lebowitz, J.3    Engler, J.A.4    Brouillette, C.G.5
  • 99
    • 0029048822 scopus 로고
    • Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins
    • Ji Y., Jonas A. Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270:1995;11290-11297.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11290-11297
    • Ji, Y.1    Jonas, A.2
  • 100
    • 0029936973 scopus 로고    scopus 로고
    • High yield overexpression and characterization of human recombinant proapolipoprotein A-I
    • McGuire K.A., Davidson W.S., Jonas A. High yield overexpression and characterization of human recombinant proapolipoprotein A-I. J. Lipid Res. 37:1996;1519-1528.
    • (1996) J. Lipid Res. , vol.37 , pp. 1519-1528
    • McGuire, K.A.1    Davidson, W.S.2    Jonas, A.3
  • 101
    • 0020327880 scopus 로고
    • Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation
    • Reijngoud D.J., Phillips M.C. Mechanism of dissociation of human apolipoprotein A-I from complexes with dimyristoylphosphatidylcholine as studied by guanidine hydrochloride denaturation. Biochemistry. 21:1982;2969-2976.
    • (1982) Biochemistry , vol.21 , pp. 2969-2976
    • Reijngoud, D.J.1    Phillips, M.C.2
  • 106
    • 0027384540 scopus 로고
    • Apolipoprotein A-I domains involved in lecithin:cholesterol acyltransferase activation: Structure-function relationships
    • Sorci-Thomas M.G., Kearns M.W., Lee J.P. Apolipoprotein A-I domains involved in lecithin:cholesterol acyltransferase activation: structure-function relationships. J. Biol. Chem. 268:1993;21403-21409.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21403-21409
    • Sorci-Thomas, M.G.1    Kearns, M.W.2    Lee, J.P.3
  • 107
    • 0030906053 scopus 로고    scopus 로고
    • Alteration in apolipoprotein A-I 22-mer repeat order results in a decrease in lecithin:cholesterol acyltransferase reactivity
    • Sorci-Thomas M.G., Curtiss L., Parks J.S., Thomas M.J., Kearns M.W. Alteration in apolipoprotein A-I 22-mer repeat order results in a decrease in lecithin:cholesterol acyltransferase reactivity. J. Biol. Chem. 272:1997;7278-7284.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7278-7284
    • Sorci-Thomas, M.G.1    Curtiss, L.2    Parks, J.S.3    Thomas, M.J.4    Kearns, M.W.5
  • 108
    • 0029916540 scopus 로고    scopus 로고
    • High level secretion of wild-type and mutant forms of human proapoA-I using baculovirus-mediated Sf-9 cell expression
    • Sorci-Thomas M.G., Parks J.S., Kearns M.W., Pate G.N., Zhang C., Thomas M.J. High level secretion of wild-type and mutant forms of human proapoA-I using baculovirus-mediated Sf-9 cell expression. J. Lipid Res. 37:1996;673-683.
    • (1996) J. Lipid Res. , vol.37 , pp. 673-683
    • Sorci-Thomas, M.G.1    Parks, J.S.2    Kearns, M.W.3    Pate, G.N.4    Zhang, C.5    Thomas, M.J.6
  • 109
    • 0032496221 scopus 로고    scopus 로고
    • The hydrophobic face orientation of apolipoprotein A-I amphipathic helix domain 143-164 regulates lecithin:cholesterol acyltransferase activation
    • Sorci-Thomas M.G., Curtiss L., Parks J.S., Thomas M.J., Kearns M.W., Landrum M. The hydrophobic face orientation of apolipoprotein A-I amphipathic helix domain 143-164 regulates lecithin:cholesterol acyltransferase activation. J. Biol. Chem. 273:1998;11776-11782.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11776-11782
    • Sorci-Thomas, M.G.1    Curtiss, L.2    Parks, J.S.3    Thomas, M.J.4    Kearns, M.W.5    Landrum, M.6
  • 110
    • 0029783094 scopus 로고    scopus 로고
    • Effects of deletion of the carboxyl-terminal domain of apoA-I or of its substitution with helices of apoA-II on in vivo and in vitro lipoprotein association
    • Holvoet P., Zhao Z., Deridder E., Dhoest A., Collen D. Effects of deletion of the carboxyl-terminal domain of apoA-I or of its substitution with helices of apoA-II on in vivo and in vitro lipoprotein association. J. Biol. Chem. 271:1996;19395-19401.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19395-19401
    • Holvoet, P.1    Zhao, Z.2    Deridder, E.3    Dhoest, A.4    Collen, D.5
  • 111
    • 0030609862 scopus 로고    scopus 로고
    • Role of the carboxy-terminal domain of human apolipoprotein A-I in high-density-lipoprotein metabolism. A study based on deletion and substitution variants in transgenic mice
    • Holvoet P., Danloy S., Collen D. Role of the carboxy-terminal domain of human apolipoprotein A-I in high-density-lipoprotein metabolism. A study based on deletion and substitution variants in transgenic mice. Eur. J. Biochem. 245:1997;642-647.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 642-647
    • Holvoet, P.1    Danloy, S.2    Collen, D.3
  • 113
    • 0022556101 scopus 로고
    • Reconstitution of high-density lipoproteins
    • Jonas A. Reconstitution of high-density lipoproteins. Methods Enzymol. 128:1986;553-582.
    • (1986) Methods Enzymol. , vol.128 , pp. 553-582
    • Jonas, A.1
  • 114
    • 0030786781 scopus 로고    scopus 로고
    • Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks
    • Phillips J.C., Wriggers W., Li Z., Jonas A., Schulten K. Predicting the structure of apolipoprotein A-I in reconstituted high-density lipoprotein disks. Biophys. J. 73:1997;2337-2346.
    • (1997) Biophys. J. , vol.73 , pp. 2337-2346
    • Phillips, J.C.1    Wriggers, W.2    Li, Z.3    Jonas, A.4    Schulten, K.5
  • 116
    • 0029844205 scopus 로고    scopus 로고
    • Human apolipoprotein E: The Alzheimer's disease connection
    • Weisgraber K.H., Mahley R.W. Human apolipoprotein E: the Alzheimer's disease connection. FASEB J. 10:1996;1485-1494.
    • (1996) FASEB J. , vol.10 , pp. 1485-1494
    • Weisgraber, K.H.1    Mahley, R.W.2
  • 117
    • 0031779631 scopus 로고    scopus 로고
    • The role of apolipoprotein E in modulating neurite outgrowth: Potential effect of intracellular apolipoprotein E
    • Pitas R.E., Ji Z.S., Weisgraber K.H., Mahley R.W. The role of apolipoprotein E in modulating neurite outgrowth: potential effect of intracellular apolipoprotein E. Biochem. Soc. Trans. 26:1998;257-262.
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 257-262
    • Pitas, R.E.1    Ji, Z.S.2    Weisgraber, K.H.3    Mahley, R.W.4
  • 118
    • 0029943117 scopus 로고    scopus 로고
    • Secretion and processing of apolipoprotein A-I in the avian sciatic nerve during development
    • Lemieux M.J., Mezei C., Breckenridge W.C. Secretion and processing of apolipoprotein A-I in the avian sciatic nerve during development. J. Neurosci. Res. 44:1996;594-605.
    • (1996) J. Neurosci. Res. , vol.44 , pp. 594-605
    • Lemieux, M.J.1    Mezei, C.2    Breckenridge, W.C.3
  • 119
    • 0028900812 scopus 로고
    • Apolipophorin III is dramatically upregulated during the programmed cell death of insect skeletal muscle and neurons
    • Sun D., Zeigler R., Milligan C.E., Farbach S., Schwartz L.M. Apolipophorin III is dramatically upregulated during the programmed cell death of insect skeletal muscle and neurons. J. Neurobiol. 26:1995;119-129.
    • (1995) J. Neurobiol. , vol.26 , pp. 119-129
    • Sun, D.1    Zeigler, R.2    Milligan, C.E.3    Farbach, S.4    Schwartz, L.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.