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Volumn 49, Issue 9, 2008, Pages 1875-1883

Three-dimensional models of HDL apoA-I: Implications for its assembly and function

Author keywords

Apolipoprotein A I; Chemical crosslinking; Cholesterol; Exchange; Hydrogen deuterium; Mass spectrometry; Molecular dynamic modeling

Indexed keywords

APOLIPOPROTEIN A1; CHYMOTRYPSIN; HIGH DENSITY LIPOPROTEIN; LIPID; METHIONINE; RECOMBINANT PROTEIN; CHOLESTEROL;

EID: 53149092105     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R800010-JLR200     Document Type: Review
Times cited : (95)

References (96)
  • 1
    • 33645422718 scopus 로고    scopus 로고
    • Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL
    • Zannis, V. I., A. Chroni, and M. Krieger. 2006. Role of apoA-I, ABCA1, LCAT, and SR-BI in the biogenesis of HDL. J. Mol. Med. 84: 276-294.
    • (2006) J. Mol. Med , vol.84 , pp. 276-294
    • Zannis, V.I.1    Chroni, A.2    Krieger, M.3
  • 3
    • 33845320131 scopus 로고    scopus 로고
    • Molecular regulation of HDL metabolism and function: Implications for novel therapies
    • Rader, D. J. 2006. Molecular regulation of HDL metabolism and function: implications for novel therapies. J. Clin. Invest. 116: 3090-3100.
    • (2006) J. Clin. Invest , vol.116 , pp. 3090-3100
    • Rader, D.J.1
  • 4
    • 0034700643 scopus 로고    scopus 로고
    • High-density lipoprotein cholesterol as an independent risk factor in cardiovascular disease: Assessing the data from Framingham to the Veterans Affairs High-Density Lipoprotein Intervention Trial
    • Boden, W. E. 2000. High-density lipoprotein cholesterol as an independent risk factor in cardiovascular disease: assessing the data from Framingham to the Veterans Affairs High-Density Lipoprotein Intervention Trial. Am. J. Cardiol. 86: 19L-22L.
    • (2000) Am. J. Cardiol , vol.86
    • Boden, W.E.1
  • 5
    • 0030787747 scopus 로고    scopus 로고
    • Gene activation, apolipoprotein A-I/high density lipoprotein, atherosclerosis prevention and longevity
    • Luoma, P. V. 1997. Gene activation, apolipoprotein A-I/high density lipoprotein, atherosclerosis prevention and longevity. Pharmacol. Toxicol. 81: 57-64.
    • (1997) Pharmacol. Toxicol , vol.81 , pp. 57-64
    • Luoma, P.V.1
  • 6
    • 27744526914 scopus 로고    scopus 로고
    • Apolipoprotein A-I induces IL-10 and PGE2 production in human monocytes and inhibits dendritic cell differentiation and maturation
    • Kim, K. D., H. Y. Lim, H. G. Lee, D. Y. Yoon, Y. K. Choe, I. Choi, S. G. Paik, Y. S. Kim, Y. Yang, and J. S. Lim. 2005. Apolipoprotein A-I induces IL-10 and PGE2 production in human monocytes and inhibits dendritic cell differentiation and maturation. Biochem. Biophys. Res. Commun. 338: 1126-1136.
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 1126-1136
    • Kim, K.D.1    Lim, H.Y.2    Lee, H.G.3    Yoon, D.Y.4    Choe, Y.K.5    Choi, I.6    Paik, S.G.7    Kim, Y.S.8    Yang, Y.9    Lim, J.S.10
  • 8
    • 36348991411 scopus 로고    scopus 로고
    • The influence of the regulatory T lymphocytes on atherosclerosis
    • Gotsman, I., R. Gupta, and A. H. Lichtman. 2007. The influence of the regulatory T lymphocytes on atherosclerosis. Arterioscler. Thromb. Vasc. Biol. 27: 2493-2495.
    • (2007) Arterioscler. Thromb. Vasc. Biol , vol.27 , pp. 2493-2495
    • Gotsman, I.1    Gupta, R.2    Lichtman, A.H.3
  • 9
    • 33745571976 scopus 로고    scopus 로고
    • The immune response in atherosclerosis: A double-edged sword
    • Hansson, G. K., and P. Libby. 2006. The immune response in atherosclerosis: a double-edged sword. Nat. Rev. Immunol. 6: 508-519.
    • (2006) Nat. Rev. Immunol , vol.6 , pp. 508-519
    • Hansson, G.K.1    Libby, P.2
  • 13
    • 25444463073 scopus 로고    scopus 로고
    • ATP-binding cassette transporter A1: A cell cholesterol exporter that protects against cardiovascular disease
    • Oram, J. F., and J. W. Heinecke. 2005. ATP-binding cassette transporter A1: a cell cholesterol exporter that protects against cardiovascular disease. Physiol. Rev. 85: 1343-1372.
    • (2005) Physiol. Rev , vol.85 , pp. 1343-1372
    • Oram, J.F.1    Heinecke, J.W.2
  • 14
    • 33750127491 scopus 로고    scopus 로고
    • Variations on a gene: Rare and common variants in ABCA1 and their impact on HDL cholesterol levels and atherosclerosis
    • Brunham, L. R., R. R. Singaraja, and M. R. Hayden. 2006. Variations on a gene: rare and common variants in ABCA1 and their impact on HDL cholesterol levels and atherosclerosis. Annu. Rev. Nutr. 26: 105-129.
    • (2006) Annu. Rev. Nutr , vol.26 , pp. 105-129
    • Brunham, L.R.1    Singaraja, R.R.2    Hayden, M.R.3
  • 15
    • 23244436992 scopus 로고    scopus 로고
    • Biogenesis and speciation of nascent apoA-I-containing particles in various cell lines
    • Krimbou, L., H. Hajj Hassan, S. Blain, S. Rashid, M. Denis, M. Marcil, and J. Genest. 2005. Biogenesis and speciation of nascent apoA-I-containing particles in various cell lines. J. Lipid Res. 46: 1668-1677.
    • (2005) J. Lipid Res , vol.46 , pp. 1668-1677
    • Krimbou, L.1    Hajj Hassan, H.2    Blain, S.3    Rashid, S.4    Denis, M.5    Marcil, M.6    Genest, J.7
  • 16
    • 33645401198 scopus 로고    scopus 로고
    • Characterization of nascent HDL particles and microparticles formed by ABCA1-mediated efflux of cellular lipids to apoA-I
    • Doung, P. T., H. L. Collins, M. Nickel, S. Lund-Katz, G. H. Rothblat, and M. C. Phillips. 2006. Characterization of nascent HDL particles and microparticles formed by ABCA1-mediated efflux of cellular lipids to apoA-I. J. Lipid Res. 47: 832-843.
    • (2006) J. Lipid Res , vol.47 , pp. 832-843
    • Doung, P.T.1    Collins, H.L.2    Nickel, M.3    Lund-Katz, S.4    Rothblat, G.H.5    Phillips, M.C.6
  • 18
    • 48749119847 scopus 로고    scopus 로고
    • Characterization and properties of preβ-HDL particles formed by ABCA1-mediated cellular lipid efflux to apoA-I
    • Doung, P. T., G. L. Weibel, S. Lund-Katz, G. H. Rothblat, and M. C. Phillips. 2008. Characterization and properties of preβ-HDL particles formed by ABCA1-mediated cellular lipid efflux to apoA-I. J. Lipid Res. 49: 1006-1014.
    • (2008) J. Lipid Res , vol.49 , pp. 1006-1014
    • Doung, P.T.1    Weibel, G.L.2    Lund-Katz, S.3    Rothblat, G.H.4    Phillips, M.C.5
  • 20
    • 0036234218 scopus 로고    scopus 로고
    • The effects of altered apolipoprotein A-I structure on plasma HDL concentration
    • Sorci-Thomas, M. G., and M. J. Thomas. 2002. The effects of altered apolipoprotein A-I structure on plasma HDL concentration. Trends Cardiovasc. Med. 12: 121-128.
    • (2002) Trends Cardiovasc. Med , vol.12 , pp. 121-128
    • Sorci-Thomas, M.G.1    Thomas, M.J.2
  • 21
    • 33646433424 scopus 로고    scopus 로고
    • Differential diagnosis of familial high density lipoprotein deficiency syndromes
    • von Eckardstein, A. 2006. Differential diagnosis of familial high density lipoprotein deficiency syndromes. Atherosclerosis. 186: 231-239.
    • (2006) Atherosclerosis , vol.186 , pp. 231-239
    • von Eckardstein, A.1
  • 22
    • 34548689363 scopus 로고    scopus 로고
    • LCAT can rescue the abnormal phenotype produced by the natural apoA-I mutations (Leu141Arg)Pisa and (Leu159Arg)FIN
    • Koukos, G., A. Chroni, A. Duka, D. Kardassis, and V. I. Zannis. 2007. LCAT can rescue the abnormal phenotype produced by the natural apoA-I mutations (Leu141Arg)Pisa and (Leu159Arg)FIN. Biochemistry. 46: 10713-10721.
    • (2007) Biochemistry , vol.46 , pp. 10713-10721
    • Koukos, G.1    Chroni, A.2    Duka, A.3    Kardassis, D.4    Zannis, V.I.5
  • 23
    • 35348990218 scopus 로고    scopus 로고
    • A dual role for lecithin:cholesterol acyltransferase (EC 2.3.1.43) in lipoprotein oxidation
    • McPherson, P. A., I. S. Young, and J. McEneny. 2007. A dual role for lecithin:cholesterol acyltransferase (EC 2.3.1.43) in lipoprotein oxidation. Free Radic. Biol. Med. 43: 1484-1493.
    • (2007) Free Radic. Biol. Med , vol.43 , pp. 1484-1493
    • McPherson, P.A.1    Young, I.S.2    McEneny, J.3
  • 25
    • 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 D. Atkinson. 1996. Thermal unfolding of human high-density apolipoprotein A-1: implications for a lipid-free molten globular state. Proc. Natl. Acad. Sci. USA. 93: 2991-2995.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2991-2995
    • Gursky, O.1    Atkinson, D.2
  • 27
    • 0024502739 scopus 로고
    • The apolipoprotein multigene family: Structure, expression, evolution, and molecular genetics
    • Chan, L. 1989. The apolipoprotein multigene family: structure, expression, evolution, and molecular genetics. Klin. Wochenschr. 67: 225-237.
    • (1989) Klin. Wochenschr , vol.67 , pp. 225-237
    • Chan, L.1
  • 28
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., D. P. Rogers, J. A. Engler, and C. G. Brouillette. 1997. Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. USA. 94: 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
  • 30
    • 27744536041 scopus 로고    scopus 로고
    • Forster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I
    • Brouillette, C. G., W. J. Dong, Z. W. Yang, M. J. Ray, I. I. Protasevich, H. C. Cheung, and J. A. Engler. 2005. Forster resonance energy transfer measurements are consistent with a helical bundle model for lipid-free apolipoprotein A-I. Biochemistry. 44: 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
  • 31
    • 0020119219 scopus 로고
    • The process of dissolving apolipoprotein A-I in an aqueous buffer
    • Yokoyama, S., S. Tajima, and A. Yamamoto. 1982. The process of dissolving apolipoprotein A-I in an aqueous buffer. J. Biochem. 91: 1267-1272.
    • (1982) J. Biochem , vol.91 , pp. 1267-1272
    • Yokoyama, S.1    Tajima, S.2    Yamamoto, A.3
  • 33
    • 0015950692 scopus 로고
    • A molecular theory of lipid-protein interactions in the plasma lipoproteins
    • Segrest, J. P., R. L. Jackson, J. D. Morrisett, and A. M. Gotto. 1974. A molecular theory of lipid-protein interactions in the plasma lipoproteins. FEBS Lett. 38: 247-258.
    • (1974) FEBS Lett , vol.38 , pp. 247-258
    • Segrest, J.P.1    Jackson, R.L.2    Morrisett, J.D.3    Gotto, A.M.4
  • 34
    • 0028360934 scopus 로고
    • Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. Evidence for the snorkel hypothesis
    • Mishra, V. K., M. N. Palgunachari, J. P. Segrest, and G. M. Anantharamaiah. 1994. Interactions of synthetic peptide analogs of the class A amphipathic helix with lipids. Evidence for the snorkel hypothesis. J. Biol. Chem. 269: 7185-7191.
    • (1994) J. Biol. Chem , vol.269 , pp. 7185-7191
    • Mishra, V.K.1    Palgunachari, M.N.2    Segrest, J.P.3    Anantharamaiah, G.M.4
  • 35
    • 3042655091 scopus 로고    scopus 로고
    • The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine
    • MacRaild, C. A., G. J. Howlett, and P. R. Gooley. 2004. The structure and interactions of human apolipoprotein C-II in dodecyl phosphocholine. Biochemistry. 43: 8084-8093.
    • (2004) Biochemistry , vol.43 , pp. 8084-8093
    • MacRaild, C.A.1    Howlett, G.J.2    Gooley, P.R.3
  • 36
    • 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., L. M. Roberts, J. Lebowitz, J. A. Engler, and C. G. Brouillette. 1998. Structural analysis of apolipoprotein A-I: effects of amino- and carboxy-terminal deletions on the lipid-free structure. Biochemistry. 37: 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
  • 37
    • 33746006879 scopus 로고    scopus 로고
    • Apolipoprotein A-I assumes a "looped belt" conformation on reconstituted high density lipoprotein
    • Martin, D. D., M. S. Budamagunta, R. O. Ryan, J. C. Voss, and M. N. Oda. 2006. Apolipoprotein A-I assumes a "looped belt" conformation on reconstituted high density lipoprotein. J. Biol. Chem. 281: 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
  • 38
    • 0018798904 scopus 로고
    • Asymmetry of apolipoprotein A-I in solution as assessed from ultracentrifugal, viscometric, and fluorescence polarization studies
    • Barbeau, D. L., A. Jonas, T. Teng, and A. M. Scanu. 1979. Asymmetry of apolipoprotein A-I in solution as assessed from ultracentrifugal, viscometric, and fluorescence polarization studies. Biochemistry. 18: 362-369.
    • (1979) Biochemistry , vol.18 , pp. 362-369
    • Barbeau, D.L.1    Jonas, A.2    Teng, T.3    Scanu, A.M.4
  • 41
    • 0025860481 scopus 로고
    • Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E
    • Wilson, C., M. R. Wardell, K. H. Weisgraber, R. W. Mahley, and D. A. Agard. 1991. Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E. Science. 252: 1817-1822.
    • (1991) Science , vol.252 , pp. 1817-1822
    • Wilson, C.1    Wardell, M.R.2    Weisgraber, K.H.3    Mahley, R.W.4    Agard, D.A.5
  • 42
    • 33144485711 scopus 로고    scopus 로고
    • Crystal structure of human apolipoprotein A-I: Insights into its protective effect against cardiovascular diseases
    • Ajees, A. A., G. M. Anantharamaiah, V. K. Mishra, M. M. Hussain, and H. M. Murthy. 2006. Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. USA. 103: 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
  • 44
    • 0037593649 scopus 로고    scopus 로고
    • Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model
    • Saito, H., P. Dhanasekaran, D. Nguyen, P. Holvoet, S. Lund-Katz, and M. C. Phillips. 2003. Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model. J. Biol. Chem. 278: 23227-23232.
    • (2003) J. Biol. Chem , vol.278 , pp. 23227-23232
    • Saito, H.1    Dhanasekaran, P.2    Nguyen, D.3    Holvoet, P.4    Lund-Katz, S.5    Phillips, M.C.6
  • 46
    • 0033607283 scopus 로고    scopus 로고
    • Structural organization of the N-terminal domain of apolipoprotein A-I: Studies of tryptophan mutants
    • Davidson, W. S., K. Arnvig-McGuire, A. Kennedy, J. Kosman, T. L. Hazlett, and A. Jonas. 1999. Structural organization of the N-terminal domain of apolipoprotein A-I: studies of tryptophan mutants. Biochemistry. 38: 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
  • 47
    • 14344258702 scopus 로고    scopus 로고
    • A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading
    • Silva, R. A., G. M. Hilliard, J. Fang, S. Macha, and W. S. Davidson. 2005. A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading. Biochemistry. 44: 2759-2769.
    • (2005) Biochemistry , vol.44 , pp. 2759-2769
    • Silva, R.A.1    Hilliard, G.M.2    Fang, J.3    Macha, S.4    Davidson, W.S.5
  • 49
    • 34247857427 scopus 로고    scopus 로고
    • EPR spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apo-AI in solution
    • Lagerstedt, J. O., M. S. Budamagunta, M. N. Oda, and J. C. Voss. 2007. EPR spectroscopy of site-directed spin labels reveals the structural heterogeneity in the N-terminal domain of apo-AI in solution. J. Biol. Chem. 282: 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
  • 50
    • 34547927446 scopus 로고    scopus 로고
    • The structure of apolipoprotein A-I in high density lipoproteins
    • Davidson, W. S., and T. B. Thompson. 2007. The structure of apolipoprotein A-I in high density lipoproteins. J. Biol. Chem. 282: 9143-9149.
    • (2007) J. Biol. Chem , vol.282 , pp. 9143-9149
    • Davidson, W.S.1    Thompson, T.B.2
  • 51
    • 0028335242 scopus 로고
    • Native-like structure and self-association behavior of apolipoprotein A-I in a water/n-propanol solution
    • Leroy, A., and A. Jonas. 1994. Native-like structure and self-association behavior of apolipoprotein A-I in a water/n-propanol solution. Biochim. Biophys. Acta. 1212: 285-294.
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 285-294
    • Leroy, A.1    Jonas, A.2
  • 52
    • 3242656580 scopus 로고    scopus 로고
    • Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins
    • Saito, H., S. Lund-Katz, and M. C. Phillips. 2004. Contributions of domain structure and lipid interaction to the functionality of exchangeable human apolipoproteins. Prog. Lipid Res. 43: 350-380.
    • (2004) Prog. Lipid Res , vol.43 , pp. 350-380
    • Saito, H.1    Lund-Katz, S.2    Phillips, M.C.3
  • 54
    • 5444226264 scopus 로고    scopus 로고
    • Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I
    • Zhu, H. L., and D. Atkinson. 2004. Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I. Biochemistry. 43: 13156-13164.
    • (2004) Biochemistry , vol.43 , pp. 13156-13164
    • Zhu, H.L.1    Atkinson, D.2
  • 56
    • 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 D. Atkinson. 2007. Conformation and lipid binding of a C-terminal (198-243) peptide of human apolipoprotein A-I. Biochemistry. 46: 1624-1634.
    • (2007) Biochemistry , vol.46 , pp. 1624-1634
    • Zhu, H.L.1    Atkinson, D.2
  • 57
    • 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
    • Laccotripe, M., S. C. Makrides, A. Jonas, and V. I. Zannis. 1997. 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: 17511-17522.
    • (1997) J. Biol. Chem , vol.272 , pp. 17511-17522
    • Laccotripe, M.1    Makrides, S.C.2    Jonas, A.3    Zannis, V.I.4
  • 58
    • 0038442816 scopus 로고    scopus 로고
    • The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger
    • Oda, M. N., T. M. Forte, R. O. Ryan, and J. C. Voss. 2003. The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger. Nat. Struct. Biol. 10: 455-460.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 455-460
    • Oda, M.N.1    Forte, T.M.2    Ryan, R.O.3    Voss, J.C.4
  • 60
    • 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., B. L. Block, J. K. Bielicki, C. M. Kay, M. N. Oda, and R. O. Ryan. 2005. Combined N- and C-terminal truncation of human apolipoprotein A-I yields a folded, functional central domain. Biochemistry. 44: 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
  • 63
    • 33646544424 scopus 로고    scopus 로고
    • Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: High resolution NMR studies of peptide. lipid discoidal complexes
    • Mishra, V. K., G. M. Anantharamaiah, J. P. Segrest, M. N. Palgunachari, M. Chaddha, S. W. Sham, and N. R. Krishna. 2006. Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide. lipid discoidal complexes. J. Biol. Chem. 281: 6511-6519.
    • (2006) J. Biol. Chem , vol.281 , pp. 6511-6519
    • Mishra, V.K.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Palgunachari, M.N.4    Chaddha, M.5    Sham, S.W.6    Krishna, N.R.7
  • 64
    • 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., A. K. Behling Agree, S. A. Sanchez, J. Bronski, and A. Jonas. 2001. Arrangement of apolipoprotein A-I in reconstituted high-density lipoprotein disks: an alternative model based on fluorescence resonance energy transfer experiments. Biochemistry. 40: 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
  • 65
    • 0034711217 scopus 로고    scopus 로고
    • Structural determination of lipid-bound apoA-I using fluorescence resonance energy transfer
    • Li, H. H., D. S. Lyles, M. J. Thomas, W. Pan, and M. G. Sorci-Thomas. 2000. Structural determination of lipid-bound apoA-I using fluorescence resonance energy transfer. J. Biol. Chem. 275: 37048-37054.
    • (2000) J. Biol. Chem , vol.275 , pp. 37048-37054
    • Li, H.H.1    Lyles, D.S.2    Thomas, M.J.3    Pan, W.4    Sorci-Thomas, M.G.5
  • 66
    • 0035664834 scopus 로고    scopus 로고
    • Preparation and incorporation of probe-labeled apoA-I for fluorescence resonance energy transfer studies of rHDL
    • Li, H. H., M. J. Thomas, W. Pan, E. Alexander, M. Samuel, and M. G. Sorci-Thomas. 2001. Preparation and incorporation of probe-labeled apoA-I for fluorescence resonance energy transfer studies of rHDL. J. Lipid Res. 42: 2084-2091.
    • (2001) J. Lipid Res , vol.42 , pp. 2084-2091
    • Li, H.H.1    Thomas, M.J.2    Pan, W.3    Alexander, E.4    Samuel, M.5    Sorci-Thomas, M.G.6
  • 67
    • 0037131260 scopus 로고    scopus 로고
    • ApoA-I structure on discs and spheres. Variable helix registry and conformational states
    • Li, H. H., D. S. Lyles, W. Pan, E. Alexander, M. J. Thomas, and M. G. Sorci-Thomas. 2002. ApoA-I structure on discs and spheres. Variable helix registry and conformational states. J. Biol. Chem. 42: 39093-39101.
    • (2002) J. Biol. Chem , vol.42 , pp. 39093-39101
    • Li, H.H.1    Lyles, D.S.2    Pan, W.3    Alexander, E.4    Thomas, M.J.5    Sorci-Thomas, M.G.6
  • 68
    • 4644356941 scopus 로고    scopus 로고
    • Identification and structural ramifications of a hinge domainin apolipoprotein A-I discoidal high-density lipoproteins of different size
    • Maiorano, J. N., R. J. Jandacek, E. M. Horace, and W. S. Davidson. 2004. Identification and structural ramifications of a hinge domainin apolipoprotein A-I discoidal high-density lipoproteins of different size. Biochemistry. 43: 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
  • 69
    • 0035907295 scopus 로고    scopus 로고
    • Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles
    • Corsico, B., J. D. Toledo, and H. A. Garda. 2001. Evidence for a central apolipoprotein A-I domain loosely bound to lipids in discoidal lipoproteins that is capable of penetrating the bilayer of phospholipid vesicles. J. Biol. Chem. 276: 16978-16985.
    • (2001) J. Biol. Chem , vol.276 , pp. 16978-16985
    • Corsico, B.1    Toledo, J.D.2    Garda, H.A.3
  • 70
    • 0038373278 scopus 로고    scopus 로고
    • The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: A mass spectrometry study
    • Davidson,W. S., and G. M. Hilliard. 2003. The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: a mass spectrometry study. J. Biol. Chem. 278: 27199-27207.
    • (2003) J. Biol. Chem , vol.278 , pp. 27199-27207
    • Davidson, W.S.1    Hilliard, G.M.2
  • 71
    • 20544444749 scopus 로고    scopus 로고
    • A mass spectrometric determination of the conformation of dimeric apolipoprotein A-I in discoidal high density lipoproteins
    • Silva, R. A., G. M. Hilliard, L. Li, J. P. Segrest, and W. S. Davidson. 2005. A mass spectrometric determination of the conformation of dimeric apolipoprotein A-I in discoidal high density lipoproteins. Biochemistry. 44: 8600-8607.
    • (2005) Biochemistry , vol.44 , pp. 8600-8607
    • Silva, R.A.1    Hilliard, G.M.2    Li, L.3    Segrest, J.P.4    Davidson, W.S.5
  • 72
    • 20544470749 scopus 로고    scopus 로고
    • Apolipoprotein structural organization in high density lipoproteins: Belts, bundles, hinges and hairpins
    • Davidson, W. S., and R. A. Silva. 2005. Apolipoprotein structural organization in high density lipoproteins: belts, bundles, hinges and hairpins. Curr. Opin. Lipidol. 16: 295-300.
    • (2005) Curr. Opin. Lipidol , vol.16 , pp. 295-300
    • Davidson, W.S.1    Silva, R.A.2
  • 73
    • 25444491569 scopus 로고    scopus 로고
    • Intermolecular contact between globular Nterminal fold and C-terminal domain of apoA-I stabilizes its lipidbound conformation: Studies employing chemical cross-linking and mass spectrometry
    • Bhat, S., M. G. Sorci-Thomas, E. T. Alexander, M. P. Samuel, and M. J. Thomas. 2005. Intermolecular contact between globular Nterminal fold and C-terminal domain of apoA-I stabilizes its lipidbound conformation: studies employing chemical cross-linking and mass spectrometry. J. Biol. Chem. 280: 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
  • 74
    • 34347356570 scopus 로고    scopus 로고
    • Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes
    • Bhat, S., M. G. Sorci-Thomas, R. Tuladhar, M. P. Samuel, and M. J. Thomas. 2007. Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes. Biochemistry. 46: 7811-7821.
    • (2007) Biochemistry , vol.46 , pp. 7811-7821
    • Bhat, S.1    Sorci-Thomas, M.G.2    Tuladhar, R.3    Samuel, M.P.4    Thomas, M.J.5
  • 75
    • 44849099036 scopus 로고    scopus 로고
    • Wu, Z., M. A. Wagner, L. Zheng, J. S. Parks, J. M. Shy III, J. D. Smith, V. Gogonea, and S. L. Hazen. 2008. The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction [erratum]. Nat. Struct. Mol. Biol. 15: 330, 651.
    • Wu, Z., M. A. Wagner, L. Zheng, J. S. Parks, J. M. Shy III, J. D. Smith, V. Gogonea, and S. L. Hazen. 2008. The refined structure of nascent HDL reveals a key functional domain for particle maturation and dysfunction [erratum]. Nat. Struct. Mol. Biol. 15: 330, 651.
  • 76
    • 45849118713 scopus 로고    scopus 로고
    • Molecular models need to be tested: The case of a solar flares discoidal HDL model
    • Shih, A. Y., S. G. Sligar, and K. Schulten. 2008. Molecular models need to be tested: the case of a solar flares discoidal HDL model. Biophys. J. 94: L87-L89.
    • (2008) Biophys. J , vol.94
    • Shih, A.Y.1    Sligar, S.G.2    Schulten, K.3
  • 77
    • 0027384540 scopus 로고
    • Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships
    • Sorci-Thomas, M. G., M. W. Kearns, and J. P. Lee. 1993. Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships. J. Biol. Chem. 268: 21403-21409.
    • (1993) J. Biol. Chem , vol.268 , pp. 21403-21409
    • Sorci-Thomas, M.G.1    Kearns, M.W.2    Lee, J.P.3
  • 78
    • 0034697316 scopus 로고    scopus 로고
    • Single repeat deletion in apoA-I blocks cholesterol esterification and results in rapid catabolism of D6 and wild-type apoA-I in transgenic mice
    • Sorci-Thomas, M. G., M. J. Thomas, L. K. Curtiss, and M. Landrum. 2000. Single repeat deletion in apoA-I blocks cholesterol esterification and results in rapid catabolism of D6 and wild-type apoA-I in transgenic mice. J. Biol. Chem. 275: 12156-12163.
    • (2000) J. Biol. Chem , vol.275 , pp. 12156-12163
    • Sorci-Thomas, M.G.1    Thomas, M.J.2    Curtiss, L.K.3    Landrum, M.4
  • 80
    • 16844370698 scopus 로고    scopus 로고
    • Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin:cholesterol acyltransferase (LCAT) reactivity
    • Alexander, E. T., S. Bhat, M. J. Thomas, R. B. Weinberg, V. R. Cook, M. S. Bharadwaj, and M. G. Sorci-Thomas. 2005. Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin:cholesterol acyltransferase (LCAT) reactivity. Biochemistry. 44: 5409-5419.
    • (2005) Biochemistry , vol.44 , pp. 5409-5419
    • Alexander, E.T.1    Bhat, S.2    Thomas, M.J.3    Weinberg, R.B.4    Cook, V.R.5    Bharadwaj, M.S.6    Sorci-Thomas, M.G.7
  • 81
    • 0037470173 scopus 로고    scopus 로고
    • The central helices of ApoAI can promote ATP-binding cassette transporter A1 (ABCA1)-mediated lipid efflux. Amino acid residues 220-231 of the wild-type apoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo
    • Chroni, A., T. Liu, I. Gorshkova, H. Y. Kan, Y. Uehara, A. Von Eckardstein, and V. I. Zannis. 2003. The central helices of ApoAI can promote ATP-binding cassette transporter A1 (ABCA1)-mediated lipid efflux. Amino acid residues 220-231 of the wild-type apoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo. J. Biol. Chem. 278: 6719-6730.
    • (2003) J. Biol. Chem , vol.278 , pp. 6719-6730
    • Chroni, A.1    Liu, T.2    Gorshkova, I.3    Kan, H.Y.4    Uehara, Y.5    Von Eckardstein, A.6    Zannis, V.I.7
  • 82
    • 34248580603 scopus 로고    scopus 로고
    • The carboxyterminal region of apoA-I is required for the ABCA1-dependent formation of alpha-HDL but not prebeta-HDL particles in vivo
    • Chroni, A., G. Koukos, A. Duka, and V. I. Zannis. 2007. The carboxyterminal region of apoA-I is required for the ABCA1-dependent formation of alpha-HDL but not prebeta-HDL particles in vivo. Biochemistry. 46: 5697-5708.
    • (2007) Biochemistry , vol.46 , pp. 5697-5708
    • Chroni, A.1    Koukos, G.2    Duka, A.3    Zannis, V.I.4
  • 84
    • 0027219389 scopus 로고
    • Structural and functional domains of apolipoprotein A-I within high density lipoproteins
    • Dalton, M. B., and J. B. Swaney. 1993. Structural and functional domains of apolipoprotein A-I within high density lipoproteins. J. Biol. Chem. 268: 19274-19283.
    • (1993) J. Biol. Chem , vol.268 , pp. 19274-19283
    • Dalton, M.B.1    Swaney, J.B.2
  • 85
    • 0029048822 scopus 로고
    • Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins
    • Ji, Y., and A. Jonas. 1995. Properties of an N-terminal proteolytic fragment of apolipoprotein A-I in solution and in reconstituted high density lipoproteins. J. Biol. Chem. 270: 11290-11297.
    • (1995) J. Biol. Chem , vol.270 , pp. 11290-11297
    • Ji, Y.1    Jonas, A.2
  • 87
    • 0030900911 scopus 로고    scopus 로고
    • Structural analysis of apolipoprotein A-I: Limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I
    • Roberts, L. M., M. J. Ray, T. W. Shih, E. Hayden, M. M. Reader, and C. G. Brouillette. 1997. Structural analysis of apolipoprotein A-I: limited proteolysis of methionine-reduced and -oxidized lipid-free and lipid-bound human apo A-I. Biochemistry. 36: 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
  • 89
    • 33847193915 scopus 로고    scopus 로고
    • Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations
    • Shih, A. Y., P. L. Freddolino, A. Arkhipov, and K. Schulten. 2007. Assembly of lipoprotein particles revealed by coarse-grained molecular dynamics simulations. J. Struct. Biol. 157: 579-592.
    • (2007) J. Struct. Biol , vol.157 , pp. 579-592
    • Shih, A.Y.1    Freddolino, P.L.2    Arkhipov, A.3    Schulten, K.4
  • 90
    • 33644893631 scopus 로고    scopus 로고
    • Coarse grained protein-lipid model with application to lipoprotein particles
    • Shih, A. Y., A. Arkhipov, P. L. Freddolino, and K. Schulten. 2006. Coarse grained protein-lipid model with application to lipoprotein particles. J. Phys. Chem. B. 110: 3674-3684.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 3674-3684
    • Shih, A.Y.1    Arkhipov, A.2    Freddolino, P.L.3    Schulten, K.4
  • 94
    • 34248233497 scopus 로고    scopus 로고
    • Apolipoprotein E*dipalmitoylphosphatidylcholine particles are ellipsoidal in solution
    • Peters-Libeu, C. A., Y. Newhouse, S. C. Hall, H. E. Witkowska, and K. H. Weisgraber. 2007. Apolipoprotein E*dipalmitoylphosphatidylcholine particles are ellipsoidal in solution. J. Lipid Res. 48: 1035-1044.
    • (2007) J. Lipid Res , vol.48 , pp. 1035-1044
    • Peters-Libeu, C.A.1    Newhouse, Y.2    Hall, S.C.3    Witkowska, H.E.4    Weisgraber, K.H.5
  • 95
    • 0033516703 scopus 로고    scopus 로고
    • An amphipathic alpha-helix at a membrane interface: A structural study using a novel X-ray diffraction method
    • Hristova, K., W. C. Wimley, V. K. Mishra, G. M. Anantharamiah, J. P. Segrest, and S. H. White. 1999. An amphipathic alpha-helix at a membrane interface: a structural study using a novel X-ray diffraction method. J. Mol. Biol. 290: 99-117.
    • (1999) J. Mol. Biol , vol.290 , pp. 99-117
    • Hristova, K.1    Wimley, W.C.2    Mishra, V.K.3    Anantharamiah, G.M.4    Segrest, J.P.5    White, S.H.6
  • 96
    • 0025648850 scopus 로고
    • Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins
    • Jonas, A., J. H. Wald, K. L. Toohill, E. S. Krul, and K. E. Kezdy. 1990. Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins. J. Biol. Chem. 265: 22123-22129.
    • (1990) J. Biol. Chem , vol.265 , pp. 22123-22129
    • Jonas, A.1    Wald, J.H.2    Toohill, K.L.3    Krul, E.S.4    Kezdy, K.E.5


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