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Volumn 48, Issue 47, 2009, Pages 11196-11210

Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACYL CHAIN; ALL-ATOM SIMULATIONS; AMPHIPATHIC; APOLIPOPROTEIN A-I; APOLIPOPROTEINS; BI-LAYER; CHOLESTEROL TRANSPORT; CHOLESTERYL ESTERS; COARSE-GRAINED; HIGH EFFICIENCY; HIGH-DENSITY LIPOPROTEINS; HYDROXYL MOIETY; MOLECULAR DYNAMICS SIMULATIONS; PARTIAL BLOCKAGE; PHOSPHOLIPASE A2; PRODUCT INHIBITION; SITE DIRECTED MUTAGENESIS; TRAJECTORY ANALYSIS;

EID: 72749109345     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901242k     Document Type: Article
Times cited : (46)

References (74)
  • 1
    • 0021838282 scopus 로고
    • Molecular pathways in the transformation of model discoidal lipoprotein complexes induced by lecithin:cholesterol acyltransferase
    • Nichols, A. V., Blanche, P. J., Gong, E. L., Shore, V. G., and Forte, T. M. (1985) Molecular pathways in the transformation of model discoidal lipoprotein complexes induced by lecithin:cholesterol acyltransferase. Biochim. Biophys. Acta 834, 285-300.
    • (1985) Biochim. Biophys. Acta , vol.834 , pp. 285-300
    • Nichols, A.V.1    Blanche, P.J.2    Gong, E.L.3    Shore, V.G.4    Forte, T.M.5
  • 2
    • 14944381287 scopus 로고    scopus 로고
    • HDL as a target in the treatment of atherosclerotic cardiovascular disease
    • Linsel-Nitschke, P., and Tall, A. R. (2005) HDL as a target in the treatment of atherosclerotic cardiovascular disease. Nat. Rev. Drug Discovery 4, 193-205.
    • (2005) Nat. Rev. Drug Discovery , vol.4 , pp. 193-205
    • Linsel-Nitschke, P.1    Tall, A.R.2
  • 4
    • 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. (2003) The spatial organization of apolipoprotein A-I on the edge of discoidal high density lipoprotein particles: A mass specrometry study. J. Biol. Chem. 278, 27199-27207.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27199-27207
    • Davidson, W.S.1    Hilliard, G.M.2
  • 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. (2005) 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, 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
    • 0034711217 scopus 로고    scopus 로고
    • Structural determination of lipid-bound apo A-I using fluorescence resonance energy transfer
    • Li, H., Lyles, D. S., Thomas,M. J., Pan, W., and Sorci-Thomas, M. G. (2000) Structural determination of lipid-bound apo A-I using fluorescence resonance energy transfer. J. Biol. Chem. 275, 37048-37054.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37048-37054
    • Li, H.1    Lyles, D.S.2    Thomas, M.J.3    Pan, W.4    Sorci-Thomas, M.G.5
  • 7
    • 34347356570 scopus 로고    scopus 로고
    • Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes
    • DOI 10.1021/bi700384t
    • Bhat, S., Sorci-Thomas, M. G., Tuladhar, R., Samuel, M. P., and Thomas, M. J. (2007) Conformational adaptation of apolipoprotein A-I to discretely sized phospholipid complexes. Biochemistry 46, 7811-7821. (Pubitemid 47016064)
    • (2007) Biochemistry , vol.46 , Issue.26 , pp. 7811-7821
    • Bhat, S.1    Sorci-Thomas, M.G.2    Tuladhar, R.3    Samuel, M.P.4    Thomas, M.J.5
  • 8
    • 34547927446 scopus 로고    scopus 로고
    • The structure of apolipoprotein A-I in high density lipoproteins
    • Davidson, W. S., and Thompson, T. B. (2007) The structure of apolipoprotein A-I in high density lipoproteins. J. Biol. Chem. 282, 22249-22253.
    • (2007) J. Biol. Chem. , vol.282 , pp. 22249-22253
    • Davidson, W.S.1    Thompson, T.B.2
  • 9
    • 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. (2001) Apolipoprotein A-I Adopts a Belt-like Orientation in Reconstituted High Density Lipoproteins. J. Biol. Chem. 276, 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
  • 10
    • 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. (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
  • 11
    • 65649096200 scopus 로고    scopus 로고
    • Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes
    • Chen, B., Ren, X., Neville, T., Jerome, W. G., Hoyt, D. W., Sparks, D., Ren, G., and Wang, J. (2009) Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes. Protein Sci. 18, 921-935.
    • (2009) Protein Sci. , vol.18 , pp. 921-935
    • Chen, B.1    Ren, X.2    Neville, T.3    Jerome, W.G.4    Hoyt, D.W.5    Sparks, D.6    Ren, G.7    Wang, J.8
  • 12
    • 0038054286 scopus 로고    scopus 로고
    • A structural and functional role for 11-mer repeats in R-synuclein and other exchangeable lipid binding proteins
    • Bussell, R.Jr., and Eliezer, D. (2003) A structural and functional role for 11-mer repeats in R-synuclein and other exchangeable lipid binding proteins. J. Mol. Biol. 329, 763-778.
    • (2003) J. Mol. Biol. , vol.329 , pp. 763-778
    • Bussell Jr., R.1    Eliezer, D.2
  • 13
    • 15244347219 scopus 로고    scopus 로고
    • Helix periodicity, topology, and dynamics of membrane-associated α-synuclein
    • Bussell, R.Jr., Ramlall, T. F., and Eliezer, D. (2005) Helix periodicity, topology, and dynamics of membrane-associated α-synuclein. Protein Sci. 14, 862-872.
    • (2005) Protein Sci. , vol.14 , pp. 862-872
    • Bussell Jr., R.1    Ramlall, T.F.2    Eliezer, D.3
  • 14
    • 0030732162 scopus 로고    scopus 로고
    • Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation
    • Borhani, D. W., Rogers, D. P., Engler, J. A., and Brouillette, C. G. (1997) Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation. Proc. Natl. Acad. Sci. U.S.A. 94, 12291-12296.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 12291-12296
    • Borhani, D.W.1    Rogers, D.P.2    Engler, J.A.3    Brouillette, C.G.4
  • 17
    • 58849161366 scopus 로고    scopus 로고
    • Thermal stability of apolipoprotein A-I in high-density lipoproteins by molecular dynamics
    • Jones, M. K.,Catte,A., Patterson, J. C.,Gu, F., Chen, J., Li, L., and Segrest, J. P. (2009) Thermal stability of apolipoprotein A-I in high-density lipoproteins by molecular dynamics. Biophys. J. 96, 354-371.
    • (2009) Biophys. J. , vol.96 , pp. 354-371
    • Jones, M.K.1    Catte, A.2    Patterson, J.C.3    Gu, F.4    Chen, J.5    Li, L.6    Segrest, J.P.7
  • 18
    • 0028070549 scopus 로고
    • Parallel helix bundles and ion channels: Molecular modeling via simulated annealing and restrained molecular dynamics
    • Kerr, I. D., Sankararamakrishnan, R., Smart, O. S., and Sansom, M. S. (1994) Parallel helix bundles and ion channels: Molecular modeling via simulated annealing and restrained molecular dynamics. Biophys. J. 67, 1501-1515. (Pubitemid 24304323)
    • (1994) Biophysical Journal , vol.67 , Issue.4 , pp. 1501-1515
    • Kerr, I.D.1    Sankararamakrishnan, R.2    Smart, O.S.3    Sansom, M.S.P.4
  • 19
    • 0029042687 scopus 로고
    • Structural features of isolated M2 helices of nicotinic receptors. Simulated annealing via molecular dynamics studies
    • Sankararamakrishnan, R., and Sansom, M. S. (1995) Structural features of isolated M2 helices of nicotinic receptors. Simulated annealing via molecular dynamics studies. Biophys. Chem. 55, 215-230.
    • (1995) Biophys. Chem. , vol.55 , pp. 215-230
    • Sankararamakrishnan, R.1    Sansom, M.S.2
  • 20
    • 0030000521 scopus 로고    scopus 로고
    • Simulated annealing with restrained molecular dynamics using a flexible restraint potential: Theory and evaluation with simulated NMR constraints
    • Bassolino-Klimas, D., Tejero, R., Krystek, S. R., Metzler, W. J., Montelione, G. T., and Bruccoleri, R. E. (1996) Simulated annealing with restrained molecular dynamics using a flexible restraint potential: Theory and evaluation with simulatedNMR constraints. Protein Sci. 5, 593-603. (Pubitemid 26119493)
    • (1996) Protein Science , vol.5 , Issue.4 , pp. 593-603
    • Bassolino-Klimas, D.1    Tejero, R.2    Krystek, S.R.3    Metzler, W.J.4    Montelione, G.T.5    Bruccoleri, R.E.6
  • 21
    • 0030956593 scopus 로고    scopus 로고
    • Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: Application in predicting the three-dimensional structure of murine homeodomain Msx-1
    • Li, H., Tejero, R., Monleon, D., Bassolino-Klimas, D., Abate-Shen, C., Bruccoleri, R. E., and Montelione, G. T. (1997) Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: Application in predicting the three-dimensional structure of murine homeodomain Msx-1. Protein Sci. 6, 956-970.
    • (1997) Protein Sci. , vol.6 , pp. 956-970
    • Li, H.1    Tejero, R.2    Monleon, D.3    Bassolino-Klimas, D.4    Abate-Shen, C.5    Bruccoleri, R.E.6    Montelione, G.T.7
  • 22
    • 0036841535 scopus 로고    scopus 로고
    • Molecular dynamics simulation of spontaneous membrane fusion during a cubic-hexagonal phase transition
    • Marrink, S. J., and Tieleman, D. P. (2002) Molecular dynamics simulation of spontaneous membrane fusion during a cubic-hexagonal phase transition. Biophys. J. 83, 2386-2392. (Pubitemid 35265735)
    • (2002) Biophysical Journal , vol.83 , Issue.5 , pp. 2386-2392
    • Marrink, S.-J.1    Peter Tieleman, D.2
  • 23
    • 33644893631 scopus 로고    scopus 로고
    • Coarse grained protein-lipid model with application to lipoprotein particles
    • Shih, A. Y., Arkhipov, A., Freddolino, P. L., and Schulten, K. (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
  • 25
    • 0029080806 scopus 로고
    • Specificity of lecithin:cholesterol acyltransferase and atherogenic risk: Comparative studies on the plasma composition and in vitro synthesis of cholesteryl esters in 14 vertebrate species
    • Liu, M., Bagdade, J. D., and Subbaiah, P. V. (1995) Specificity of lecithin:cholesterol acyltransferase and atherogenic risk: Comparative studies on the plasma composition and in vitro synthesis of cholesteryl esters in 14 vertebrate species. J. Lipid Res. 36, 1813-1824.
    • (1995) J. Lipid Res. , vol.36 , pp. 1813-1824
    • Liu, M.1    Bagdade, J.D.2    Subbaiah, P.V.3
  • 26
    • 0028051474 scopus 로고
    • Role of sn-2 acyl group of phosphatidylcholine in determining the positional specificity of lecithin-cholesterol acyltransferase
    • DOI 10.1021/bi00249a012
    • Subbaiah, P. V., Liu, M., and Paltauf, F. (1994) Role of sn-2 acyl group of phosphatidylcholine in determining the positional specificity of lecithin-cholesterol acyltransferase. Biochemistry 33, 13259-13266. (Pubitemid 24373240)
    • (1994) Biochemistry , vol.33 , Issue.45 , pp. 13259-13266
    • Subbaiah, P.V.1    Liu, M.2    Paltauf, F.3
  • 27
    • 0024593757 scopus 로고
    • Human plasma lecithin-cholesterol acyltransferase. Inhibition of the phospholipase A2-like activity by sn-2-difluoroketone phosphatidylcholine analogues
    • Jauhiainen, M., Yuan, W., Gelb, M. H., and Dolphin, P. J. (1989) Human plasma lecithin-cholesterol acyltransferase. Inhibition of the phospholipase A2-like activity by sn-2-difluoroketone phosphatidylcholine analogues. J. Biol. Chem. 264, 1963-1967.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1963-1967
    • Jauhiainen, M.1    Yuan, W.2    Gelb, M.H.3    Dolphin, P.J.4
  • 28
    • 0027050786 scopus 로고
    • Continuous fluorescence assay for lecithin:cholesterol acyltransferase using a water-soluble phosphatidylcholine
    • Bonelli, F. S., and Jonas, A. (1992) Continuous fluorescence assay for lecithin:cholesterol acyltransferase using a water-soluble phosphatidylcholine. J. Lipid Res. 33, 1863-1869.
    • (1992) J. Lipid Res. , vol.33 , pp. 1863-1869
    • Bonelli, F.S.1    Jonas, A.2
  • 29
    • 0034672281 scopus 로고    scopus 로고
    • Lecithin cholesterol acyltransferase
    • Jonas, A. (2000) Lecithin cholesterol acyltransferase. Biochim. Biophys. Acta 1529, 245-256.
    • (2000) Biochim. Biophys. Acta , vol.1529 , pp. 245-256
    • Jonas, A.1
  • 30
    • 0036926084 scopus 로고    scopus 로고
    • Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model
    • Klon, A. E., Segrest, J. P., and Harvey, S. C. (2002) Molecular dynamics simulations on discoidal HDL particles suggest a mechanism for rotation in the apo A-I belt model. J. Mol. Biol. 324, 703-721.
    • (2002) J. Mol. Biol. , vol.324 , pp. 703-721
    • Klon, A.E.1    Segrest, J.P.2    Harvey, S.C.3
  • 31
    • 0001430231 scopus 로고    scopus 로고
    • The flying ice cube: Velocity rescaling in molecular dynamics leads to violation of energy equipartition
    • Harvey, S. C., Tan, R. K. Z., and Cheatham, T. E. (1998) The flying ice cube: Velocity rescaling in molecular dynamics leads to violation of energy equipartition. J. Comput. Chem. 19, 726-740.
    • (1998) J. Comput. Chem. , vol.19 , pp. 726-740
    • Harvey, S.C.1    Tan, R.K.Z.2    Cheatham, T.E.3
  • 34
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen, W. L., Chandrasekhar, J., and Madura, J. D. (1983) Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 79, 926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 37
    • 0031309462 scopus 로고    scopus 로고
    • Length scales of lipid dynamics and molecular dynamics
    • Feller, S. E., and Pastor, R. W. (1997) Length scales of lipid dynamics and molecular dynamics. Pac. Symp. Biocomput. '97, 142-150.
    • (1997) Pac. Symp. Biocomput. '97 , pp. 142-150
    • Feller, S.E.1    Pastor, R.W.2
  • 40
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess, B., Kutzner, C., van der Spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation. J. Chem. Theory Comput. 4, 435-447.
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 41
    • 1642485164 scopus 로고    scopus 로고
    • Coarse grained model for semiquantitative lipid simulations
    • Marrink, S. J., de Vries, A. H., and Mark, A. E. (2004) Coarse grained model for semiquantitative lipid simulations. J. Phys. Chem. B 108, 750-760.
    • (2004) J. Phys. Chem. B , vol.108 , pp. 750-760
    • Marrink, S.J.1    De Vries, A.H.2    Mark, A.E.3
  • 42
    • 0034466399 scopus 로고    scopus 로고
    • Detailed molecular model of apolipoprotein A-I on the surface of high-density lipoproteins and its functional implications
    • Segrest, J. P., Harvey, S. C., and Zannis, V. (2000) Detailed molecular model of apolipoprotein A-I on the surface of high-density lipoproteins and its functional implications. Trends Cardiovasc. Med. 10, 246-252.
    • (2000) Trends Cardiovasc. Med. , vol.10 , pp. 246-252
    • Segrest, J.P.1    Harvey, S.C.2    Zannis, V.3
  • 45
    • 0014264541 scopus 로고
    • The plasma lecithins:cholesterol acyltransferase reaction
    • Glomset, J. A. (1968) The plasma lecithins:cholesterol acyltransferase reaction. J. Lipid Res. 9, 155-167.
    • (1968) J. Lipid Res. , vol.9 , pp. 155-167
    • Glomset, J.A.1
  • 47
    • 0035065367 scopus 로고    scopus 로고
    • Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: Cholesterol acyltransferase and in HDL rearrangements
    • Cho, K. H., Durbin, D. M., and Jonas, A. (2001) Role of individual amino acids of apolipoprotein A-I in the activation of lecithin: cholesterol acyltransferase and in HDL rearrangements. J. Lipid Res. 42, 379-389.
    • (2001) J. Lipid Res. , vol.42 , pp. 379-389
    • Cho, K.H.1    Durbin, D.M.2    Jonas, A.3
  • 49
    • 4043125999 scopus 로고    scopus 로고
    • Substitutions of glutamate 110 and 111 in the middle helix 4 of human apolipoprotein A-I (apoA-I) by alanine affect the structure and in vitro functions of apoA-I and induce severe hypertriglyceridemia in apoA-I-deficient mice
    • Chroni, A., Kan, H. Y., Kypreos, K. E., Gorshkova, I. N., Shkodrani, A., and Zannis, V. I. (2004) Substitutions of glutamate 110 and 111 in the middle helix 4 of human apolipoprotein A-I (apoA-I) by alanine affect the structure and in vitro functions of apoA-I and induce severe hypertriglyceridemia in apoA-I-deficient mice. Biochemistry 43, 10442-10457.
    • (2004) Biochemistry , vol.43 , pp. 10442-10457
    • Chroni, A.1    Kan, H.Y.2    Kypreos, K.E.3    Gorshkova, I.N.4    Shkodrani, A.5    Zannis, V.I.6
  • 51
    • 0027519147 scopus 로고
    • The number of amphipathic α-helical segments of apolipoproteins A-I, E, and A-IV determines the size and functional properties of their reconstituted lipoprotein particles
    • Jonas, A., Steinmetz, A., and Churgay, L. (1993) The number of amphipathic α-helical segments of apolipoproteins A-I, E, and A-IV determines the size and functional properties of their reconstituted lipoprotein particles. J. Biol. Chem. 268, 1596-1602.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1596-1602
    • Jonas, A.1    Steinmetz, A.2    Churgay, L.3
  • 52
    • 0030894376 scopus 로고    scopus 로고
    • Long-chain polyunsaturated fatty acids in the sn-2 position of phosphatidylcholine decrease the stability of recombinant high density lipoprotein apolipoprotein A-I and the activation energy of the lecithin:cholesterol acyltransferase reaction
    • Parks, J. S., and Gebre, A. K. (1997) Long-chain polyunsaturated fatty acids in the sn-2 position of phosphatidylcholine decrease the stability of recombinant high density lipoprotein apolipoprotein A-I and the activation energy of the lecithin:cholesterol acyltransferase reaction. J. Lipid Res. 38, 266-275.
    • (1997) J. Lipid Res. , vol.38 , pp. 266-275
    • Parks, J.S.1    Gebre, A.K.2
  • 53
    • 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. (2001) 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, 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
  • 54
    • 0026331991 scopus 로고
    • Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase
    • Banka, C. L., Bonnet, D. J., Black, A. S., Smith, R. S., and Curtiss, L. K. (1991) Localization of an apolipoprotein A-I epitope critical for activation of lecithin-cholesterol acyltransferase. J. Biol. Chem. 266, 23886-23892.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23886-23892
    • Banka, C.L.1    Bonnet, D.J.2    Black, A.S.3    Smith, R.S.4    Curtiss, L.K.5
  • 55
    • 0027293797 scopus 로고
    • Apolipoprotein A-I domains involved in the activation of lecithin: Cholesterol acyltransferase. Importance of the central domain
    • Meng, Q. H., Calabresi, L., Fruchart, J. C., and Marcel, Y. L. (1993) Apolipoprotein A-I domains involved in the activation of lecithin: cholesterol acyltransferase. Importance of the central domain. J. Biol. Chem. 268, 16966-16973.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16966-16973
    • Meng, Q.H.1    Calabresi, L.2    Fruchart, J.C.3    Marcel, Y.L.4
  • 56
    • 0027384540 scopus 로고
    • Apolipoprotein A-I domains involved in lecithin-cholesterol acyltransferase activation. Structure:function relationships
    • Sorci-Thomas, M., Kearns, M. W., and Lee, J. P. (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.1    Kearns, M.W.2    Lee, J.P.3
  • 58
    • 0030451848 scopus 로고    scopus 로고
    • Localization of apolipoprotein A-I epitopes involved in the activation of lecithin: Cholesterol acyltransferase
    • Uboldi, P., Spoladore, M., Fantappie, S., Marcovina, S., and Catapano, A. L. (1996) Localization of apolipoprotein A-I epitopes involved in the activation of lecithin:cholesterol acyltransferase. J. Lipid Res. 37, 2557-2568. (Pubitemid 27051503)
    • (1996) Journal of Lipid Research , vol.37 , Issue.12 , pp. 2557-2568
    • Uboldi, P.1    Spoladore, M.2    Fantappie, S.3    Marcovina, S.4    Catapano, A.L.5
  • 59
    • 0030610546 scopus 로고    scopus 로고
    • Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation
    • Dhoest, A., Zhao, Z., De Geest, B., Deridder, E., Sillen, A., Engelborghs, Y., Collen, D., and Holvoet, P. (1997) Role of the Arg123-Tyr166 paired helix of apolipoprotein A-I in lecithin:cholesterol acyltransferase activation. J. Biol. Chem. 272, 15967-15972.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15967-15972
    • Dhoest, A.1    Zhao, Z.2    De Geest, B.3    Deridder, E.4    Sillen, A.5    Engelborghs, Y.6    Collen, D.7    Holvoet, P.8
  • 60
    • 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., and Kearns, M. W. (1997) Alteration in apolipoprotein A-I 22-mer repeat order results in a decrease in lecithin:cholesterol acyltransferase reactivity. J. Biol. Chem. 272, 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
  • 61
    • 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., and Landrum, M. (1998) The hydrophobic face orientation of apolipoprotein A-I amphipathic helix domain 143-164 regulates lecithin:cholesterol acyltransferase activation. J. Biol. Chem. 273, 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
  • 62
    • 0034681418 scopus 로고    scopus 로고
    • Distinct central amphipathic α-helices in apolipoprotein A-I contribute to the in vivo maturation of high density lipoprotein by either activating lecithin-cholesterol acyltransferase or binding lipids
    • McManus, D. C., Scott, B. R., Frank, P. G., Franklin, V., Schultz, J. R., and Marcel, Y. L. (2000) Distinct central amphipathic α-helices in apolipoprotein A-I contribute to the in vivo maturation of high density lipoprotein by either activating lecithin-cholesterol acyltransferase or binding lipids. J. Biol. Chem. 275, 5043-5051.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5043-5051
    • McManus, D.C.1    Scott, B.R.2    Frank, P.G.3    Franklin, V.4    Schultz, J.R.5    Marcel, Y.L.6
  • 63
    • 16844370698 scopus 로고    scopus 로고
    • Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity
    • DOI 10.1021/bi047412v
    • Alexander, E. T., Bhat, S., Thomas, M. J., Weinberg, R. B., Cook, V. R., Bharadwaj, M. S., and Sorci-Thomas, M. (2005) Apolipoprotein A-I helix 6 negatively charged residues attenuate lecithin-cholesterol acyltransferase (LCAT) reactivity. Biochemistry 44, 5409-5419. (Pubitemid 40489980)
    • (2005) Biochemistry , vol.44 , Issue.14 , 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.7
  • 64
    • 0033920731 scopus 로고    scopus 로고
    • Apolipoprotein A-I: Structure-function relationships
    • Frank, P. G., and Marcel, Y. L. (2000) Apolipoprotein A-I: Structure-function relationships. J. Lipid Res. 41, 853-872.
    • (2000) J. Lipid Res. , vol.41 , pp. 853-872
    • Frank, P.G.1    Marcel, Y.L.2
  • 66
    • 0019128929 scopus 로고
    • The mechanism of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I and an amphiphilic peptide
    • Yokoyama, S., Fukushima, D., Kupferberg, J. P., Kezdy, F. J., and Kaiser, E. T. (1980) The mechanism of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-I and an amphiphilic peptide. J. Biol. Chem. 255, 7333-7339.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7333-7339
    • Yokoyama, S.1    Fukushima, D.2    Kupferberg, J.P.3    Kezdy, F.J.4    Kaiser, E.T.5
  • 67
    • 0025014667 scopus 로고
    • Use of synthetic peptide analogues to localize lecithin:cholesterol acyltransferase activating domain in apolipoprotein A-I
    • Anantharamaiah, G. M., Venkatachalapathi, Y. V., Brouillette, C. G., and Segrest, J. P. (1990) Use of synthetic peptide analogues to localize lecithin:cholesterol acyltransferase activating domain in apolipoprotein A-I. Arteriosclerosis 10, 95-105.
    • (1990) Arteriosclerosis , vol.10 , pp. 95-105
    • Anantharamaiah, G.M.1    Venkatachalapathi, Y.V.2    Brouillette, C.G.3    Segrest, J.P.4
  • 68
    • 68849087475 scopus 로고    scopus 로고
    • Smaller discoidal high-density lipoprotein particles form saddle surfaces, but not planar bilayers
    • Miyazaki, M., Nakano, M., Fukuda, M., and Handa, T. (2009) Smaller discoidal high-density lipoprotein particles form saddle surfaces, but not planar bilayers. Biochemistry 48, 7756-7763.
    • (2009) Biochemistry , vol.48 , pp. 7756-7763
    • Miyazaki, M.1    Nakano, M.2    Fukuda, M.3    Handa, T.4
  • 69
    • 0025648850 scopus 로고
    • Apolipoprotein A-I structure and lipid properties in homogeneous, reconstituted spherical and discoidal high density lipoproteins
    • Jonas, A., Wald, J. H., Toohill, K. L., Krul, E. S., and Kezdy, K. E. (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
  • 72
    • 0343067147 scopus 로고    scopus 로고
    • Cholesterol effects on the phosphatidylcholine bilayer polar region: A molecular simulation study
    • Pasenkiewicz-Gierula, M., Rog, T., Kitamura, K., and Kusumi, A. (2000) Cholesterol effects on the phosphatidylcholine bilayer polar region: A molecular simulation study. Biophys. J. 78, 1376-1389. (Pubitemid 30141562)
    • (2000) Biophysical Journal , vol.78 , Issue.3 , pp. 1376-1389
    • Pasenkiewicz-Gierula, M.1    Rog, T.2    Kitamura, K.3    Kusumi, A.4
  • 73
    • 46849085354 scopus 로고    scopus 로고
    • Cholesterol is found to reside in the center of a polyunsaturated lipid membrane
    • DOI 10.1021/bi800123b
    • Harroun, T. A., Katsaras, J., and Wassall, S. R. (2008) Cholesterol is found to reside in the center of a polyunsaturated lipid membrane. Biochemistry 47, 7090-7096. (Pubitemid 351956358)
    • (2008) Biochemistry , vol.47 , Issue.27 , pp. 7090-7096
    • Harroun, T.A.1    Katsaras, J.2    Wassall, S.R.3
  • 74


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