메뉴 건너뛰기




Volumn 155, Issue 2, 2010, Pages 123-133

The helix bundle: A reversible lipid binding motif

Author keywords

Apolipophorin; Apolipoprotein; Cholesterol; Diacylglycerol; Lipophorin; Lipoprotein; Protein structure; Triacylglycerol

Indexed keywords

APOLIPOPHORIN III; APOLIPOPROTEIN; APOLIPOPROTEIN A1; APOLIPOPROTEIN E; INSECT PROTEIN; UNCLASSIFIED DRUG;

EID: 72049085266     PISSN: 10956433     EISSN: 15314332     Source Type: Journal    
DOI: 10.1016/j.cbpa.2009.09.009     Document Type: Review
Times cited : (54)

References (140)
  • 1
    • 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., and 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.4    Lindgren, F.T.5
  • 2
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases
    • Ajees A.A., Anantharamaiah G.M., Mishra V.K., Hussain M.M., and Murthy H.M. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. USA 103 (2006) 2126-2131
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2126-2131
    • Ajees, A.A.1    Anantharamaiah, G.M.2    Mishra, V.K.3    Hussain, M.M.4    Murthy, H.M.5
  • 3
    • 15544375933 scopus 로고    scopus 로고
    • Combined N- and C-terminal truncation of human apolipoprotein A-I yields a folded, functional central domain
    • Beckstead J.A., Block B.L., Bielicki J.K., Kay C.M., Oda M.N., and Ryan R.O. Combined N- and C-terminal truncation of human apolipoprotein A-I yields a folded, functional central domain. Biochemistry 44 (2005) 4591-4599
    • (2005) Biochemistry , vol.44 , pp. 4591-4599
    • Beckstead, J.A.1    Block, B.L.2    Bielicki, J.K.3    Kay, C.M.4    Oda, M.N.5    Ryan, R.O.6
  • 5
    • 25444491569 scopus 로고    scopus 로고
    • Intermolecular contact between globular N-terminal fold and C-terminal domain of ApoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry
    • Bhat S., Sorci-Thomas M.G., Alexander E.T., Samuel M.P., and Thomas M.J. Intermolecular contact between globular N-terminal fold and C-terminal domain of ApoA-I stabilizes its lipid-bound conformation: studies employing chemical cross-linking and mass spectrometry. J. Biol. Chem. 280 (2005) 33015-33025
    • (2005) J. Biol. Chem. , vol.280 , pp. 33015-33025
    • Bhat, S.1    Sorci-Thomas, M.G.2    Alexander, E.T.3    Samuel, M.P.4    Thomas, M.J.5
  • 6
    • 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. 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
  • 8
    • 27744536041 scopus 로고    scopus 로고
    • Förster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I
    • Brouillette C.G., Dong W.J., Yang Z.W., Ray M.J., Protasevich I.I., Cheung H.C., and Engler J.A. Förster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I. Biochemistry 44 (2005) 16413-16425
    • (2005) Biochemistry , vol.44 , pp. 16413-16425
    • Brouillette, C.G.1    Dong, W.J.2    Yang, Z.W.3    Ray, M.J.4    Protasevich, I.I.5    Cheung, H.C.6    Engler, J.A.7
  • 10
    • 0033517735 scopus 로고    scopus 로고
    • Deletion of the C-terminal domain of apolipoprotein A-I impairs cell surface binding and lipid efflux in macrophage
    • Burgess J.W., Frank P.G., Franklin V., Liang P., McManus D.C., Desforges M., Rassart E., and Marcel Y.L. Deletion of the C-terminal domain of apolipoprotein A-I impairs cell surface binding and lipid efflux in macrophage. Biochemistry 38 (1999) 14524-14533
    • (1999) Biochemistry , vol.38 , pp. 14524-14533
    • Burgess, J.W.1    Frank, P.G.2    Franklin, V.3    Liang, P.4    McManus, D.C.5    Desforges, M.6    Rassart, E.7    Marcel, Y.L.8
  • 11
    • 0141457250 scopus 로고    scopus 로고
    • In vivo lipoprotein binding assay of the insect exchangeable apolipoprotein, apolipophorin-III
    • Chetty P.S., Arrese E.L., and Soulages J.L. In vivo lipoprotein binding assay of the insect exchangeable apolipoprotein, apolipophorin-III. Protein Pept. Lett. 10 (2003) 469-473
    • (2003) Protein Pept. Lett. , vol.10 , pp. 469-473
    • Chetty, P.S.1    Arrese, E.L.2    Soulages, J.L.3
  • 12
    • 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. Role of helices and loops in the ability of apolipophorin-III to interact with native lipoproteins and form discoidal lipoprotein complexes. Biochemistry 42 (2003) 15061-15067
    • (2003) Biochemistry , vol.42 , pp. 15061-15067
    • Chetty, P.S.1    Arrese, E.L.2    Rodriguez, V.3    Soulages, J.L.4
  • 13
    • 0242662225 scopus 로고    scopus 로고
    • Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain
    • Choy N., Raussens V., and Narayanaswami V. Inter-molecular coiled-coil formation in human apolipoprotein E C-terminal domain. J. Mol. Biol. 334 (2003) 527-539
    • (2003) J. Mol. Biol. , vol.334 , pp. 527-539
    • Choy, N.1    Raussens, V.2    Narayanaswami, V.3
  • 15
    • 0021874519 scopus 로고
    • Isolation, characterization, and mapping to chromosome 19 of the human apolipoprotein E gene
    • Das H.K., McPherson J., Bruns G.A., Karathanasis S.K., and Breslow J.L. Isolation, characterization, and mapping to chromosome 19 of the human apolipoprotein E gene. J. Biol. Chem. 260 (1985) 6240-6247
    • (1985) J. Biol. Chem. , vol.260 , pp. 6240-6247
    • Das, H.K.1    McPherson, J.2    Bruns, G.A.3    Karathanasis, S.K.4    Breslow, J.L.5
  • 16
    • 0038373278 scopus 로고    scopus 로고
    • The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: a mass specrometry study
    • Davidson W.S., and Hilliard G.M. The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: a mass specrometry study. J. Biol. Chem. 278 (2003) 27199-27207
    • (2003) J. Biol. Chem. , vol.278 , pp. 27199-27207
    • Davidson, W.S.1    Hilliard, G.M.2
  • 17
    • 20544470749 scopus 로고    scopus 로고
    • Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins
    • Davidson W.S., and Silva R.A. Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins. Curr. Opin. Lipidol. 16 (2005) 295-300
    • (2005) Curr. Opin. Lipidol. , vol.16 , pp. 295-300
    • Davidson, W.S.1    Silva, R.A.2
  • 18
    • 34547927446 scopus 로고    scopus 로고
    • The structure of apolipoprotein A-I in high density lipoproteins
    • Davidson W.S., and Thompson T.B. The structure of apolipoprotein A-I in high density lipoproteins. J. Biol. Chem. 282 (2007) 22249-22253
    • (2007) J. Biol. Chem. , vol.282 , pp. 22249-22253
    • Davidson, W.S.1    Thompson, T.B.2
  • 19
    • 0033607283 scopus 로고    scopus 로고
    • Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants
    • Davidson W.S., Arnvig-McGuire K., Kennedy A., Kosman J., Hazlett T.L., and Jonas A. Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants. Biochemistry 38 (1999) 14387-14395
    • (1999) Biochemistry , vol.38 , pp. 14387-14395
    • Davidson, W.S.1    Arnvig-McGuire, K.2    Kennedy, A.3    Kosman, J.4    Hazlett, T.L.5    Jonas, A.6
  • 20
    • 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., Niere M., Kay C.M., Ryan R.O., and Wiesner A. An N-terminal three-helix fragment of the exchangeable insect apolipoprotein apolipophorin III conserves the lipid binding properties of wild-type protein. Biochemistry 40 (2001) 3150-3157
    • (2001) Biochemistry , vol.40 , pp. 3150-3157
    • Dettloff, M.1    Weers, P.M.M.2    Niere, M.3    Kay, C.M.4    Ryan, R.O.5    Wiesner, A.6
  • 22
    • 17644420761 scopus 로고    scopus 로고
    • Examination of lipid-bound conformation of apolipoprotein E4 by pyrene excimer fluorescence
    • Drury J., and Narayanaswami V. Examination of lipid-bound conformation of apolipoprotein E4 by pyrene excimer fluorescence. J. Biol. Chem. 280 (2005) 14605-14610
    • (2005) J. Biol. Chem. , vol.280 , pp. 14605-14610
    • Drury, J.1    Narayanaswami, V.2
  • 23
    • 0019332583 scopus 로고
    • Effect of guanidine hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution
    • Edelstein C., and Scanu A.M. Effect of guanidine hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution. J. Biol. Chem. 255 (1980) 5747-5754
    • (1980) J. Biol. Chem. , vol.255 , pp. 5747-5754
    • Edelstein, C.1    Scanu, A.M.2
  • 25
    • 0038418381 scopus 로고    scopus 로고
    • NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III
    • Fan D., Zheng Y., Yang D., and Wang J. NMR solution structure and dynamics of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III. J. Biol. Chem. 278 (2003) 21212-21220
    • (2003) J. Biol. Chem. , vol.278 , pp. 21212-21220
    • Fan, D.1    Zheng, Y.2    Yang, D.3    Wang, J.4
  • 26
    • 2142710086 scopus 로고    scopus 로고
    • A monomeric human apolipoprotein E carboxyl-terminal domain
    • Fan D., Li Q., Korando L., Jerome W.G., and Wang J. A monomeric human apolipoprotein E carboxyl-terminal domain. Biochemistry 43 (2004) 5055-5064
    • (2004) Biochemistry , vol.43 , pp. 5055-5064
    • Fan, D.1    Li, Q.2    Korando, L.3    Jerome, W.G.4    Wang, J.5
  • 27
    • 0038661046 scopus 로고    scopus 로고
    • Structural studies of N- and C-terminally truncated human apolipoprotein A-I
    • Fang Y., Gursky O., and Atkinson D. Structural studies of N- and C-terminally truncated human apolipoprotein A-I. Biochemistry 42 (2003) 6881-6890
    • (2003) Biochemistry , vol.42 , pp. 6881-6890
    • Fang, Y.1    Gursky, O.2    Atkinson, D.3
  • 28
    • 42149174251 scopus 로고    scopus 로고
    • Atheroprotective effects of HDL: beyond reverse cholesterol transport
    • Feig J.E., Shamir R., and Fisher E.A. Atheroprotective effects of HDL: beyond reverse cholesterol transport. Curr. Drug Targets 9 (2008) 196-203
    • (2008) Curr. Drug Targets , vol.9 , pp. 196-203
    • Feig, J.E.1    Shamir, R.2    Fisher, E.A.3
  • 29
    • 1642270170 scopus 로고    scopus 로고
    • Meat-adaptive genes and the evolution of slower aging in humans
    • Finch C.E., and Stanford C.B. Meat-adaptive genes and the evolution of slower aging in humans. Q. Rev. Biol. 79 (2004) 3-50
    • (2004) Q. Rev. Biol. , vol.79 , pp. 3-50
    • Finch, C.E.1    Stanford, C.B.2
  • 30
    • 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. The lipid-associated conformation of the low density lipoprotein receptor binding domain of human apolipoprotein E. J. Biol. Chem. 275 (2000) 33601-33606
    • (2000) J. Biol. Chem. , vol.275 , pp. 33601-33606
    • Fisher, C.A.1    Narayanaswami, V.2    Ryan, R.O.3
  • 32
    • 0037205467 scopus 로고    scopus 로고
    • Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid
    • Garda H.A., Arrese E.L., and Soulages J.L. Structure of apolipophorin III in discoidal lipoproteins. Interhelical distances in the lipid-bound state and conformational change upon binding to lipid. J. Biol. Chem. 277 (2002) 19773-19782
    • (2002) J. Biol. Chem. , vol.277 , pp. 19773-19782
    • Garda, H.A.1    Arrese, E.L.2    Soulages, J.L.3
  • 33
    • 33846004469 scopus 로고    scopus 로고
    • Lipid-induced extension of apolipoprotein E helix 4 correlates with low density lipoprotein receptor binding ability
    • Gupta V., Narayanaswami V., Budamagunta M.S., Yamamato T., Voss J.C., and Ryan R.O. Lipid-induced extension of apolipoprotein E helix 4 correlates with low density lipoprotein receptor binding ability. J. Biol. Chem. 281 (2006) 39294-39299
    • (2006) J. Biol. Chem. , vol.281 , pp. 39294-39299
    • Gupta, V.1    Narayanaswami, V.2    Budamagunta, M.S.3    Yamamato, T.4    Voss, J.C.5    Ryan, R.O.6
  • 34
    • 0029864592 scopus 로고    scopus 로고
    • Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state
    • Gursky O., and Atkinson D. Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. Proc. Natl. Acad. Sci. USA 93 (1996) 2991-2995
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2991-2995
    • Gursky, O.1    Atkinson, D.2
  • 35
    • 0027405920 scopus 로고
    • Structures of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate as a constituent of a glycoprotein
    • Hård K., Van Doorn J.M., Thomas-Oates J.E., Kamerling J.P., and Van der Horst D.J. Structures of the Asn-linked oligosaccharides of apolipophorin III from the insect Locusta migratoria. Carbohydrate-linked 2-aminoethylphosphonate 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
  • 36
    • 22544443366 scopus 로고    scopus 로고
    • Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4
    • Hatters D.M., Peters-Libeu C.A., and Weisgraber K.H. Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4. J. Biol. Chem. 280 (2005) 26477-26482
    • (2005) J. Biol. Chem. , vol.280 , pp. 26477-26482
    • Hatters, D.M.1    Peters-Libeu, C.A.2    Weisgraber, K.H.3
  • 37
    • 26644459735 scopus 로고    scopus 로고
    • Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms
    • Hatters D.M., Budamagunta M.S., Voss J.C., and Weisgraber K.H. Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms. J. Biol. Chem. 280 (2005) 34288-34295
    • (2005) J. Biol. Chem. , vol.280 , pp. 34288-34295
    • Hatters, D.M.1    Budamagunta, M.S.2    Voss, J.C.3    Weisgraber, K.H.4
  • 39
    • 0035997373 scopus 로고    scopus 로고
    • Lipoprotein receptors in the nervous system
    • Herz J., and Bock H.H. Lipoprotein receptors in the nervous system. Annu. Rev. Biochem. 71 (2002) 405-434
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 405-434
    • Herz, J.1    Bock, H.H.2
  • 40
    • 3142640798 scopus 로고    scopus 로고
    • Hickenbottom, S.J., Kimmel, A.R., Londos, C., Hurley, J.H., 2004. Structure of a lipid droplet protein: the PAT family member TIP47. Structure 12, 11-99-1207.
    • Hickenbottom, S.J., Kimmel, A.R., Londos, C., Hurley, J.H., 2004. Structure of a lipid droplet protein: the PAT family member TIP47. Structure 12, 11-99-1207.
  • 43
    • 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., and 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
  • 44
    • 0033528673 scopus 로고    scopus 로고
    • Amphipathic alpha-helix bundle organization of lipid-free chicken apolipoprotein A-I
    • Kiss R.S., Kay C.M., and Ryan R.O. Amphipathic alpha-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
  • 45
    • 0035971639 scopus 로고    scopus 로고
    • Functional similarities of human and chicken apolipoprotein A-I: dependence on secondary and tertiary rather than primary structure
    • Kiss R.S., Ryan R.O., and Francis G.A. Functional similarities of human and chicken apolipoprotein A-I: dependence on secondary and tertiary rather than primary structure. Biochim. Biophys. Acta. 1531 (2001) 251-259
    • (2001) Biochim. Biophys. Acta. , vol.1531 , pp. 251-259
    • Kiss, R.S.1    Ryan, R.O.2    Francis, G.A.3
  • 46
    • 0038497959 scopus 로고    scopus 로고
    • Structure-guided protein engineering modulates helix bundle exchangeable apolipoprotein properties
    • Kiss R.S., Weers P.M.M., Narayanaswami V., Cohen J., Kay C.M., and Ryan R.O. Structure-guided protein engineering modulates helix bundle exchangeable apolipoprotein properties. J. Biol. Chem. 278 (2003) 21952-21959
    • (2003) J. Biol. Chem. , vol.278 , pp. 21952-21959
    • Kiss, R.S.1    Weers, P.M.M.2    Narayanaswami, V.3    Cohen, J.4    Kay, C.M.5    Ryan, R.O.6
  • 47
    • 0031027211 scopus 로고    scopus 로고
    • α-Helical protein assembly motifs
    • Kohn D.W., Man C.T., and Hodges R.S. α-Helical protein assembly motifs. J. Biol. Chem. 272 (1997) 2583-2586
    • (1997) J. Biol. Chem. , vol.272 , pp. 2583-2586
    • Kohn, D.W.1    Man, C.T.2    Hodges, R.S.3
  • 48
  • 50
    • 34247857427 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution
    • Lagerstedt J.O., Budamagunta M.S., Oda M.N., and Voss J.C. Electron paramagnetic resonance spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I in solution. J. Biol. Chem. 282 (2007) 9143-9149
    • (2007) J. Biol. Chem. , vol.282 , pp. 9143-9149
    • Lagerstedt, J.O.1    Budamagunta, M.S.2    Oda, M.N.3    Voss, J.C.4
  • 52
    • 0028335242 scopus 로고
    • Native-like structure and self-association behavior of apolipoprotein A-I in a water/n-propanol solution
    • Leroy A., and Jonas A. Native-like structure and self-association behavior of apolipoprotein A-I in a water/n-propanol solution. Biochim. Biophys. Acta. 1212 (1994) 285-294
    • (1994) Biochim. Biophys. Acta. , vol.1212 , pp. 285-294
    • Leroy, A.1    Jonas, A.2
  • 53
    • 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. Structural determination of lipid-bound ApoA-I using fluorescence resonance energy transfer. J. Biol. Chem. 275 (2000) 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
  • 55
    • 0027524130 scopus 로고
    • Prevention of phospholipase-C induced aggregation of low density lipoprotein by amphipathic apolipoproteins
    • Liu H., Scraba D.G., and 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
  • 56
    • 0034617305 scopus 로고    scopus 로고
    • Conformational reorganization of the four-helix bundle of human apolipoprotein E in binding to phospholipid
    • Lu B., Morrow J.A., and Weisgraber K.H. Conformational reorganization of the four-helix bundle of human apolipoprotein E in binding to phospholipid. J. Biol. Chem. 275 (2000) 20775-20781
    • (2000) J. Biol. Chem. , vol.275 , pp. 20775-20781
    • Lu, B.1    Morrow, J.A.2    Weisgraber, K.H.3
  • 57
    • 4644356941 scopus 로고    scopus 로고
    • Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size
    • Maiorano J.N., Jandacek R.J., Horace E.M., and Davidson W.S. Identification and structural ramifications of a hinge domain in apolipoprotein A-I discoidal high-density lipoproteins of different size. Biochemistry 43 (2004) 11717-11726
    • (2004) Biochemistry , vol.43 , pp. 11717-11726
    • Maiorano, J.N.1    Jandacek, R.J.2    Horace, E.M.3    Davidson, W.S.4
  • 58
    • 0037398373 scopus 로고    scopus 로고
    • Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations
    • Marcel Y.L., and Kiss R.S. Structure-function relationships of apolipoprotein A-I: a flexible protein with dynamic lipid associations. Curr. Opin. Lipidol. 14 (2003) 151-157
    • (2003) Curr. Opin. Lipidol. , vol.14 , pp. 151-157
    • Marcel, Y.L.1    Kiss, R.S.2
  • 59
    • 33746006879 scopus 로고    scopus 로고
    • Apolipoprotein A-I assumes a "looped belt" conformation on reconstituted high density lipoprotein
    • Martin D.D., Budamagunta M.S., Ryan R.O., Voss J.C., and Oda M.N. Apolipoprotein A-I assumes a "looped belt" conformation on reconstituted high density lipoprotein. J. Biol. Chem. 281 (2006) 20418-20426
    • (2006) J. Biol. Chem. , vol.281 , pp. 20418-20426
    • Martin, D.D.1    Budamagunta, M.S.2    Ryan, R.O.3    Voss, J.C.4    Oda, M.N.5
  • 60
    • 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. Differences in stability among the human apolipoprotein E isoforms determined by the amino-terminal domain. Biochemistry 39 (2000) 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
  • 61
    • 0037184994 scopus 로고    scopus 로고
    • Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease
    • Morrow J.A., Hatters D.M., Lu B., Hochtl P., Oberg K.A., Rupp B., and Weisgraber K.H. Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease. J. Biol. Chem. 277 (2002) 50380-50385
    • (2002) J. Biol. Chem. , vol.277 , pp. 50380-50385
    • Morrow, J.A.1    Hatters, D.M.2    Lu, B.3    Hochtl, P.4    Oberg, K.A.5    Rupp, B.6    Weisgraber, K.H.7
  • 62
    • 0033991858 scopus 로고    scopus 로고
    • Molecular basis of exchangeable apolipoprotein function
    • Narayanaswami V., and Ryan R.O. Molecular basis of exchangeable apolipoprotein function. Biochim. Biophys. Acta. 1483 (2000) 15-36
    • (2000) Biochim. Biophys. Acta. , vol.1483 , pp. 15-36
    • Narayanaswami, V.1    Ryan, R.O.2
  • 63
    • 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., and 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
  • 64
    • 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., and Ryan R.O. A molecular trigger of lipid-binding induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 4366-4371
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 4366-4371
    • Narayanaswami, V.1    Wang, J.2    Schieve, D.3    Kay, C.M.4    Ryan, R.O.5
  • 65
    • 0035851137 scopus 로고    scopus 로고
    • Lipid association-induced N- and C-terminal domain reorganization in human apolipoprotein E3
    • Narayanaswami V., Szeto S.S., and Ryan R.O. Lipid association-induced N- and C-terminal domain reorganization in human apolipoprotein E3. J. Biol. Chem. 276 (2001) 37853-37860
    • (2001) J. Biol. Chem. , vol.276 , pp. 37853-37860
    • Narayanaswami, V.1    Szeto, S.S.2    Ryan, R.O.3
  • 69
    • 0035900724 scopus 로고    scopus 로고
    • Apolipoprotein A-I adopts a belt-like orientation in reconstituted high density lipoproteins
    • Panagotopulos S.E., Horace E.M., Maiorano J.N., and Davidson W.S. Apolipoprotein A-I adopts a belt-like orientation in reconstituted high density lipoproteins. J. Biol. Chem. 276 (2001) 42965-42970
    • (2001) J. Biol. Chem. , vol.276 , pp. 42965-42970
    • Panagotopulos, S.E.1    Horace, E.M.2    Maiorano, J.N.3    Davidson, W.S.4
  • 70
    • 33644861785 scopus 로고    scopus 로고
    • Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine
    • Peters-Libeu C.A., Newhouse Y., Hatters D.M., and Weisgraber K.H. Model of biologically active apolipoprotein E bound to dipalmitoylphosphatidylcholine. J. Biol. Chem. 281 (2006) 1073-1079
    • (2006) J. Biol. Chem. , vol.281 , pp. 1073-1079
    • Peters-Libeu, C.A.1    Newhouse, Y.2    Hatters, D.M.3    Weisgraber, K.H.4
  • 71
    • 34248233497 scopus 로고    scopus 로고
    • Apolipoprotein E*dipalmitoylphosphatidylcholine particles are ellipsoidal in solution
    • Peters-Libeu C.A., Newhouse Y., Hall S.C., Witkowska H.E., and Weisgraber K.H. Apolipoprotein E*dipalmitoylphosphatidylcholine particles are ellipsoidal in solution. J. Lipid Res. 2007 48 (2007) 1035-1044
    • (2007) J. Lipid Res. , vol.2007 , Issue.48 , pp. 1035-1044
    • Peters-Libeu, C.A.1    Newhouse, Y.2    Hall, S.C.3    Witkowska, H.E.4    Weisgraber, K.H.5
  • 72
    • 0026725757 scopus 로고
    • Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells
    • Plump A.S., Smith J.D., Hayek T., Aalto-Setälä K., Walsh A., Verstuyft J.G., Rubin E.M., and Breslow J.L. Severe hypercholesterolemia and atherosclerosis in apolipoprotein E-deficient mice created by homologous recombination in ES cells. Cell 71 (1992) 343-353
    • (1992) Cell , vol.71 , pp. 343-353
    • Plump, A.S.1    Smith, J.D.2    Hayek, T.3    Aalto-Setälä, K.4    Walsh, A.5    Verstuyft, J.G.6    Rubin, E.M.7    Breslow, J.L.8
  • 73
    • 0018402975 scopus 로고
    • Kinetics of lipid-protein interactions: effect of cholesterol on the association of human plasma high-density apolipoprotein A-I with L-alpha-dimyristoylphosphatidylcholine
    • Pownall H.J., Massey J.B., Kusserow S.K., and Gotto Jr. A.M. Kinetics of lipid-protein interactions: effect of cholesterol on the association of human plasma high-density apolipoprotein A-I with L-alpha-dimyristoylphosphatidylcholine. Biochemistry 18 (1979) 574-579
    • (1979) Biochemistry , vol.18 , pp. 574-579
    • Pownall, H.J.1    Massey, J.B.2    Kusserow, S.K.3    Gotto Jr., A.M.4
  • 74
    • 0028977999 scopus 로고
    • Alignment of apolipophorin III α-helices in complex with dimyristoylphosphatidylcholine: a unique spatial orientation
    • Raussens V., Goormaghtigh E., Narayanaswami V., Ryan R.O., and Ruysschaert J.M. 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
  • 75
    • 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., and 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
  • 76
    • 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. The low density lipoprotein 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
  • 81
    • 0024993524 scopus 로고
    • Dynamics of insect lipophorin metabolism
    • Ryan R.O. Dynamics of insect lipophorin metabolism. J. Lipid. Res. 31 (1990) 1725-1739
    • (1990) J. Lipid. Res. , vol.31 , pp. 1725-1739
    • Ryan, R.O.1
  • 82
    • 0034107475 scopus 로고    scopus 로고
    • Lipid transport biochemistry and role in energy production
    • Ryan R.O., and Van der Horst D.J. Lipid transport biochemistry and role in energy production. Ann. Rev. Entomol. 45 (2000) 233-260
    • (2000) Ann. Rev. Entomol. , vol.45 , pp. 233-260
    • Ryan, R.O.1    Van der Horst, D.J.2
  • 83
    • 0024279274 scopus 로고
    • Facilitated diacylglycerol exchange between insect hemolymph lipophorins. Properties of Manduca sexta lipid transfer particle
    • Ryan R.O., Senthilathipan K.R., Wells M.A., and Law J.H. Facilitated diacylglycerol exchange between insect hemolymph lipophorins. Properties of Manduca sexta lipid transfer particle. J. Biol. Chem. 263 (1988) 14140-14145
    • (1988) J. Biol. Chem. , vol.263 , pp. 14140-14145
    • Ryan, R.O.1    Senthilathipan, K.R.2    Wells, M.A.3    Law, J.H.4
  • 84
    • 0025327738 scopus 로고
    • Studies of the morphology and structure of the plasma lipid transfer particle from the tobacco hornworm, Manduca sexta
    • Ryan R.O., Howe A., and Scraba D.G. Studies of the morphology and structure of the plasma lipid transfer particle from the tobacco hornworm, Manduca sexta. J. Lipid Res. 31 (1990) 871-879
    • (1990) J. Lipid Res. , vol.31 , pp. 871-879
    • Ryan, R.O.1    Howe, A.2    Scraba, D.G.3
  • 85
    • 0027391142 scopus 로고
    • Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III
    • Ryan R.O., Oikawa K., and Kay C.M. Conformational, thermodynamic and stability properties of Manduca sexta apolipophorin III. 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
  • 86
    • 0036384368 scopus 로고    scopus 로고
    • Lipid triggered molecular switch of apoLp-III helix bundle to an extended helix conformation
    • Sahoo D., Weers P.M.M., Ryan R.O., and Narayanaswami V. Lipid triggered molecular switch of apoLp-III helix bundle to an extended helix conformation. J. Mol. Biol. 321 (2002) 201-214
    • (2002) J. Mol. Biol. , vol.321 , pp. 201-214
    • Sahoo, D.1    Weers, P.M.M.2    Ryan, R.O.3    Narayanaswami, V.4
  • 87
    • 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. Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles. J. Biol. Chem. 276 (2001) 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
  • 89
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito H., Lund-Katz S., and Phillips M.C. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 43 (2004) 350-380
    • (2004) Prog. Lipid Res. , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 90
    • 0035966120 scopus 로고    scopus 로고
    • The N-terminal globular domain and the first class A amphipathic helix of apolipoprotein A-I are important for lecithin:cholesterol acyltransferase activation and the maturation of high density lipoprotein in vivo
    • Scott B.R., McManus D.C., Franklin V., McKenzie A.G., Neville T., Sparks D.L., and Marcel Y.L. The N-terminal globular domain and the first class A amphipathic helix of apolipoprotein A-I are important for lecithin:cholesterol acyltransferase activation and the maturation of high density lipoprotein in vivo. J. Biol. Chem. 276 (2001) 48716-48724
    • (2001) J. Biol. Chem. , vol.276 , pp. 48716-48724
    • Scott, B.R.1    McManus, D.C.2    Franklin, V.3    McKenzie, A.G.4    Neville, T.5    Sparks, D.L.6    Marcel, Y.L.7
  • 92
    • 0034120113 scopus 로고    scopus 로고
    • Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding
    • Segelke B.W., Forstner M., Knapp M., Trakhanov S.D., Parkin S., Newhouse Y.M., Bellamy H.D., Weisgraber K.H., and Rupp B. Conformational flexibility in the apolipoprotein E amino-terminal domain structure determined from three new crystal forms: implications for lipid binding. Protein Sci. 9 (2000) 886-897
    • (2000) Protein Sci. , vol.9 , pp. 886-897
    • Segelke, B.W.1    Forstner, M.2    Knapp, M.3    Trakhanov, S.D.4    Parkin, S.5    Newhouse, Y.M.6    Bellamy, H.D.7    Weisgraber, K.H.8    Rupp, B.9
  • 98
    • 67649785032 scopus 로고    scopus 로고
    • A unified scheme for initiation and conformational adaptation of human apolipoprotein E N-terminal domain upon lipoprotein binding and for receptor binding activity
    • Sivashanmugam A., and Wang J. A unified scheme for initiation and conformational adaptation of human apolipoprotein E N-terminal domain upon lipoprotein binding and for receptor binding activity. J. Biol. Chem. 284 (2009) 14657-14666
    • (2009) J. Biol. Chem. , vol.284 , pp. 14657-14666
    • Sivashanmugam, A.1    Wang, J.2
  • 99
    • 17144375387 scopus 로고    scopus 로고
    • Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I
    • Smolenaars M.M., Kasperaitis M.A., Richardson P.E., Rodenburg K.W., and Van der Horst D.J. Biosynthesis and secretion of insect lipoprotein: involvement of furin in cleavage of the apoB homolog, apolipophorin-II/I. J. Lipid Res. 46 (2005) 412-421
    • (2005) J. Lipid Res. , vol.46 , pp. 412-421
    • Smolenaars, M.M.1    Kasperaitis, M.A.2    Richardson, P.E.3    Rodenburg, K.W.4    Van der Horst, D.J.5
  • 100
    • 0028216403 scopus 로고
    • Lipophorin: the structure of an insect lipoprotein and its role in lipid transport in insects
    • Soulages J.L., and Wells M.A. Lipophorin: the structure of an insect lipoprotein and its role in lipid transport in insects. Adv. Prot. Chem. 45 (1994) 371-415
    • (1994) Adv. Prot. Chem. , vol.45 , pp. 371-415
    • Soulages, J.L.1    Wells, M.A.2
  • 101
    • 0028279012 scopus 로고
    • Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin. Correlation with the binding of apolipophorin-III
    • Soulages J.L., and Wells M.A. Effect of diacylglycerol content on some physicochemical properties of the insect lipoprotein, lipophorin. Correlation with the binding of apolipophorin-III. Biochemistry 33 (1994) 2356-2362
    • (1994) Biochemistry , vol.33 , pp. 2356-2362
    • Soulages, J.L.1    Wells, M.A.2
  • 102
    • 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., and 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
  • 103
    • 0034730078 scopus 로고    scopus 로고
    • Fluorescence spectroscopy of single tryptophan mutants of apolipophorin-III in discoidal lipoproteins of dimyristoylphosphatidylcholine
    • Soulages J.L., and Arrese E.L. Fluorescence spectroscopy of single tryptophan mutants of apolipophorin-III in discoidal lipoproteins of dimyristoylphosphatidylcholine. Biochemistry 39 (2000) 10574-10580
    • (2000) Biochemistry , vol.39 , pp. 10574-10580
    • Soulages, J.L.1    Arrese, E.L.2
  • 104
    • 0035960643 scopus 로고    scopus 로고
    • Interaction of the alpha-helices of apolipophorin III with the phospholipid acyl chains in discoidal lipoprotein particles: a fluorescence quenching study
    • Soulages J.L., and Arrese E.L. Interaction of the alpha-helices of apolipophorin III with the phospholipid acyl chains in discoidal lipoprotein particles: a fluorescence quenching study. Biochemistry 40 (2001) 14279-14290
    • (2001) Biochemistry , vol.40 , pp. 14279-14290
    • Soulages, J.L.1    Arrese, E.L.2
  • 105
    • 0022972981 scopus 로고
    • Human apolipoprotein A-I forms thermally stable complexes with anionic but not with zwitterionic phospholipids
    • Surewicz W.K., Epand R.M., Pownall H.J., and Hui S.W. Human apolipoprotein A-I forms thermally stable complexes with anionic but not with zwitterionic phospholipids. J. Biol. Chem. 261 (1986) 16191-16197
    • (1986) J. Biol. Chem. , vol.261 , pp. 16191-16197
    • Surewicz, W.K.1    Epand, R.M.2    Pownall, H.J.3    Hui, S.W.4
  • 106
    • 33748645937 scopus 로고    scopus 로고
    • Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I
    • Tanaka M., Dhanasekaran P., Nguyen D., Ohta S., Lund-Katz S., Phillips M.C., and Saito H. Contributions of the N- and C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I. Biochemistry 45 (2006) 10351-10358
    • (2006) Biochemistry , vol.45 , pp. 10351-10358
    • Tanaka, M.1    Dhanasekaran, P.2    Nguyen, D.3    Ohta, S.4    Lund-Katz, S.5    Phillips, M.C.6    Saito, H.7
  • 107
    • 33646858367 scopus 로고    scopus 로고
    • The use of chemical cross-linking and mass spectrometry to elucidate the tertiary conformation of lipid-bound apolipoprotein A-I
    • Thomas M.J., Bhat S., and Sorci-Thomas M.G. The use of chemical cross-linking and mass spectrometry to elucidate the tertiary conformation of lipid-bound apolipoprotein A-I. Curr. Opin. Lipidol. 17 (2006) 214-220
    • (2006) Curr. Opin. Lipidol. , vol.17 , pp. 214-220
    • Thomas, M.J.1    Bhat, S.2    Sorci-Thomas, M.G.3
  • 108
    • 53149092105 scopus 로고    scopus 로고
    • Three-dimensional models of HDL apoA-I: implications for its assembly and function
    • Thomas M.J., Bhat S., and Sorci-Thomas M.G. Three-dimensional models of HDL apoA-I: implications for its assembly and function. J. Lipid Res. 49 (2008) 1875-1783
    • (2008) J. Lipid Res. , vol.49 , pp. 1875-1783
    • Thomas, M.J.1    Bhat, S.2    Sorci-Thomas, M.G.3
  • 109
    • 0035942337 scopus 로고    scopus 로고
    • Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments
    • Tricerri M.A., Behling Agree A.K., Sanchez S.A., Bronski J., and Jonas A. Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry 40 (2001) 5065-5074
    • (2001) Biochemistry , vol.40 , pp. 5065-5074
    • Tricerri, M.A.1    Behling Agree, A.K.2    Sanchez, S.A.3    Bronski, J.4    Jonas, A.5
  • 110
    • 0024024154 scopus 로고
    • Immunocytochemical localization of lipophorins in the flight muscles of the migratory locust (Locusta migratoria) at rest and during flight
    • Van Antwerpen R., Linnemans W.A.M., Van der Horst D.J., and Beenakkers A.M.Th. Immunocytochemical localization of lipophorins in the flight muscles of the migratory locust (Locusta migratoria) at rest and during flight. Cell Tissue Res. 252 (1988) 661-668
    • (1988) Cell Tissue Res. , vol.252 , pp. 661-668
    • Van Antwerpen, R.1    Linnemans, W.A.M.2    Van der Horst, D.J.3    Beenakkers, A.M.Th.4
  • 111
    • 0036860547 scopus 로고    scopus 로고
    • Insect lipoprotein follows a transferrin-like recycling pathway that is mediated by the insect LDL receptor homologue
    • Van Hoof D., Rodenburg K.W., and Van der Horst D.J. Insect lipoprotein follows a transferrin-like recycling pathway that is mediated by the insect LDL receptor homologue. J. Cell Sci. 115 (2002) 4001-4012
    • (2002) J. Cell Sci. , vol.115 , pp. 4001-4012
    • Van Hoof, D.1    Rodenburg, K.W.2    Van der Horst, D.J.3
  • 112
    • 0025201274 scopus 로고
    • Lipid transport function of lipoproteins in flying insects
    • Van der Horst D.J. Lipid transport function of lipoproteins in flying insects. Biochim. Biophys. Acta 1047 (1990) 195-211
    • (1990) Biochim. Biophys. Acta , vol.1047 , pp. 195-211
    • Van der Horst, D.J.1
  • 115
    • 0034786469 scopus 로고    scopus 로고
    • Adipokinetic hormones of insect: release, signal transduction, and responses
    • Van der Horst D.J., Van Marrewijk W.J.A., and Diederen J.H.B. Adipokinetic hormones of insect: release, signal transduction, and responses. Int. Rev. Cytol. 211 (2001) 179-240
    • (2001) Int. Rev. Cytol. , vol.211 , pp. 179-240
    • Van der Horst, D.J.1    Van Marrewijk, W.J.A.2    Diederen, J.H.B.3
  • 117
    • 67349275023 scopus 로고    scopus 로고
    • Circulatory lipid transport: Lipoprotein assembly and function from an evolutionary perspective
    • Van der Horst, D.J., Roosendaal, S.D., Rodenburg, K.W., 2009. Circulatory lipid transport: lipoprotein assembly and function from an evolutionary perspective. Mol. Cell. Biochem. 326, 105-119.
    • (2009) Mol. Cell. Biochem , vol.326 , pp. 105-119
    • Van der Horst, D.J.1    Roosendaal, S.D.2    Rodenburg, K.W.3
  • 118
    • 0024971523 scopus 로고
    • An insect lipid transfer particle promotes lipid loading from fat body to lipoprotein
    • Van Heusden M.C., and Law J.H. An insect lipid transfer particle promotes lipid loading from fat body to lipoprotein. J. Biol. Chem. 264 (1989) 17287-17292
    • (1989) J. Biol. Chem. , vol.264 , pp. 17287-17292
    • Van Heusden, M.C.1    Law, J.H.2
  • 119
    • 0025221262 scopus 로고
    • Investigation of the lipid domains and apolipoprotein orientation in reconstituted high density lipoproteins by fluorescence and IR methods
    • Wald J.H., Goormaghtigh E., De Meutter J., Ruysschaert J.M., and Jonas A. Investigation of the lipid domains and apolipoprotein orientation in reconstituted high density lipoproteins by fluorescence and IR methods. J. Biol. Chem. 265 (1990) 20044-20050
    • (1990) J. Biol. Chem. , vol.265 , pp. 20044-20050
    • Wald, J.H.1    Goormaghtigh, E.2    De Meutter, J.3    Ruysschaert, J.M.4    Jonas, A.5
  • 120
    • 34250214537 scopus 로고    scopus 로고
    • Molecular regulation of macrophage reverse cholesterol transport
    • Wang X., and Rader D.J. Molecular regulation of macrophage reverse cholesterol transport. Curr. Opin. Cardiol. 22 (2007) 368-372
    • (2007) Curr. Opin. Cardiol. , vol.22 , pp. 368-372
    • Wang, X.1    Rader, D.J.2
  • 121
    • 0037022281 scopus 로고    scopus 로고
    • Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein
    • Wang J., Sykes B.D., and Ryan R.O. Structural basis for the conformational adaptability of apolipophorin III, a helix-bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. USA 99 (2002) 1188-1193
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1188-1193
    • Wang, J.1    Sykes, B.D.2    Ryan, R.O.3
  • 122
    • 33645057448 scopus 로고    scopus 로고
    • Apolipophorin III: role model apolipoprotein
    • Weers P.M.M., and Ryan R.O. Apolipophorin III: role model apolipoprotein. Insect Biochem. Mol. Biol. 36 (2006) 231-240
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 231-240
    • Weers, P.M.M.1    Ryan, R.O.2
  • 123
    • 0028331057 scopus 로고
    • Factors affecting the stability and conformation of Locusta migratoria apolipophorin III
    • Weers P.M.M., Kay C.M., Oikawa K., Wientzek M., Van der Horst D.J., and Ryan R.O. Factors affecting the stability and conformation of Locusta migratoria apolipophorin III. Biochemistry 33 (1994) 3617-3624
    • (1994) Biochemistry , vol.33 , pp. 3617-3624
    • Weers, P.M.M.1    Kay, C.M.2    Oikawa, K.3    Wientzek, M.4    Van der Horst, D.J.5    Ryan, R.O.6
  • 124
    • 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., and 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
  • 125
    • 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.J., and Ryan R.O. Interaction of locust apolipophorin III with lipoproteins and phospholipid vesicles: effect of glycosylation. J. Lipid Res. 41 (2000) 416-423
    • (2000) J. Lipid Res. , vol.41 , pp. 416-423
    • Weers, P.M.M.1    Van der Horst, D.J.2    Ryan, R.O.3
  • 126
    • 0034643926 scopus 로고    scopus 로고
    • Lipid binding of the exchangeable apolipoprotein, apolipophorin III induces major changes in fluorescence properties of Trp 115 and Trp 130
    • Weers P.M.M., Prenner E.J., Kay C.M., and Ryan R.O. Lipid binding of the exchangeable apolipoprotein, apolipophorin III induces major changes in fluorescence properties of Trp 115 and Trp 130. Biochemistry 39 (2000) 6874-6880
    • (2000) Biochemistry , vol.39 , pp. 6874-6880
    • Weers, P.M.M.1    Prenner, E.J.2    Kay, C.M.3    Ryan, R.O.4
  • 127
    • 0034824483 scopus 로고    scopus 로고
    • Modulation of the lipid binding properties of the N-terminal domain of human apolipoprotein E3
    • Weers P.M.M., Narayanaswami V., and Ryan R.O. Modulation of the lipid binding properties of the N-terminal domain of human apolipoprotein E3. Eur. J. Biochem. 268 (2001) 3728-3735
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3728-3735
    • Weers, P.M.M.1    Narayanaswami, V.2    Ryan, R.O.3
  • 128
    • 0035954398 scopus 로고    scopus 로고
    • Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: correlation with lipid binding
    • Weers P.M.M., Kay C.M., and Ryan R.O. Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: correlation with lipid binding. Biochemistry 40 (2001) 7754-7760
    • (2001) Biochemistry , vol.40 , pp. 7754-7760
    • Weers, P.M.M.1    Kay, C.M.2    Ryan, R.O.3
  • 129
    • 20544455385 scopus 로고    scopus 로고
    • Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31
    • Weers P.M.M., Cabrera J., Abdullahi W.E., and Hsu T.-C. Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31. Biochemistry 44 (2005) 8810-8816
    • (2005) Biochemistry , vol.44 , pp. 8810-8816
    • Weers, P.M.M.1    Cabrera, J.2    Abdullahi, W.E.3    Hsu, T.-C.4
  • 130
    • 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
  • 131
    • 0023664091 scopus 로고
    • The role of apolipophorin III in vivo lipoprotein interconversions in adult Manduca sexta
    • Wells M.A., Ryan R.O., Kawooya J.K., and Law J.H. The role of apolipophorin III 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
  • 132
    • 0027186135 scopus 로고
    • Discrete carboxyl-terminal segments of apolipoprotein E mediate lipoprotein association and protein oligomerization
    • Westerlund J.A., and 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
  • 133
    • 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. 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 Jr., S.C.3    Weisgraber, K.H.4
  • 134
    • 0028108646 scopus 로고
    • Binding of insect apolipophorin III to dimyristoylphosphatidylcholine vesicles. Evidence for a conformational change
    • Wientzek M., Kay C.M., Oikawa K., and 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
  • 135
    • 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. 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
  • 136
    • 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., and 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
  • 137
    • 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
  • 138
    • 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. Spontaneous hypercholesterolemia and arterial lesions in mice lacking apolipoprotein E. Science 258 (1992) 468-471
    • (1992) Science , vol.258 , pp. 468-471
    • Zhang, S.H.1    Reddick, R.L.2    Piedrahita, J.A.3    Maeda, N.4
  • 140
    • 33846988253 scopus 로고    scopus 로고
    • Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I
    • Zhu H.L., and Atkinson D. Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I. Biochemistry 46 (2007) 1624-1634
    • (2007) Biochemistry , vol.46 , pp. 1624-1634
    • Zhu, H.L.1    Atkinson, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.