메뉴 건너뛰기




Volumn 48, Issue 11, 2009, Pages 2529-2537

Interaction between the N- and C-Terminal domains modulates the stability and lipid binding of apolipoprotein A-I

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN A-I; APOLIPOPROTEIN A-I (APOA-I); C-TERMINAL DOMAINS; CHEMICAL DENATURATIONS; CONFORMATIONAL STABILITIES; DIMYRISTOYL; HELICAL SEGMENTS; HELIX BUNDLES; INTRA-MOLECULAR INTERACTIONS; LIPID BINDINGS; N- AND C- TERMINAL DOMAINS; N-TERMINAL DOMAINS; N-TERMINAL HELIXES; PHOSPHATIDYLCHOLINE; PROTEIN STABILITIES; SITE SPECIFICS; SPATIAL PROXIMITIES; TERTIARY STRUCTURES; TWO DOMAINS;

EID: 64849086373     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802317v     Document Type: Article
Times cited : (39)

References (68)
  • 2
    • 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
  • 3
    • 42649134146 scopus 로고    scopus 로고
    • HDL, ABC transporters, and cholesterol efflux: Implications for the treatment of atherosclerosis
    • Tall, A. R., Yvan-Charvet, L., Terasaka, N., Pagler, T., and Wang, N. (2008) HDL, ABC transporters, and cholesterol efflux: implications for the treatment of atherosclerosis. Cell Metab. 7, 365-375.
    • (2008) Cell Metab , vol.7 , pp. 365-375
    • Tall, A.R.1    Yvan-Charvet, L.2    Terasaka, N.3    Pagler, T.4    Wang, N.5
  • 4
    • 33646893082 scopus 로고    scopus 로고
    • New insights into the biogenesis of human high-density lipoproteins
    • Krimbou, L., Marcil, M., and Genest, J. (2006) New insights into the biogenesis of human high-density lipoproteins. Curr. Opin. Lipidol. 17, 258-267.
    • (2006) Curr. Opin. Lipidol , vol.17 , pp. 258-267
    • Krimbou, L.1    Marcil, M.2    Genest, J.3
  • 5
    • 33750927892 scopus 로고    scopus 로고
    • ATP-Binding cassette cholesterol transporters and cardiovascular disease
    • Oram, J. F., and Vaughan, A. M. (2006) ATP-Binding cassette cholesterol transporters and cardiovascular disease. Circ. Res. 99, 1031-1043.
    • (2006) Circ. Res , vol.99 , pp. 1031-1043
    • Oram, J.F.1    Vaughan, A.M.2
  • 6
    • 1242285439 scopus 로고    scopus 로고
    • Cross-linking and lipid efflux properties of apoA-I mutants suggest direct association between apoA-I helices and ABCA1
    • Chroni, A., Liu, T., Fitzgerald, M. L., Freeman, M. W., and Zannis, V. I. (2004) Cross-linking and lipid efflux properties of apoA-I mutants suggest direct association between apoA-I helices and ABCA1. Biochemistry 43, 2126-2139.
    • (2004) Biochemistry , vol.43 , pp. 2126-2139
    • Chroni, A.1    Liu, T.2    Fitzgerald, M.L.3    Freeman, M.W.4    Zannis, V.I.5
  • 7
    • 34548364160 scopus 로고    scopus 로고
    • Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles
    • Vedhachalam, C., Duong, P. T., Nickel, M., Nguyen, D., Dhanasekaran, P., Saito, H., Rothblat, G. H., Lund-Katz, S., and Phillips, M. C. (2007) Mechanism of ATP-binding cassette transporter A1-mediated cellular lipid efflux to apolipoprotein A-I and formation of high density lipoprotein particles. J. Biol. Chem. 282, 25123-25130.
    • (2007) J. Biol. Chem , vol.282 , pp. 25123-25130
    • Vedhachalam, C.1    Duong, P.T.2    Nickel, M.3    Nguyen, D.4    Dhanasekaran, P.5    Saito, H.6    Rothblat, G.H.7    Lund-Katz, S.8    Phillips, M.C.9
  • 8
    • 35848942798 scopus 로고    scopus 로고
    • Identification of an ABCA1- dependent phospholipid-rich plasma membrane apolipoprotein A-I binding site for nascent HDL formation: Implications for current models of HDL biogenesis
    • Hassan, H. H., Denis, M., Lee, D. Y., Iatan, I., Nyholt, D., Ruel, I., Krimbou, L., and Genest, J. (2007) Identification of an ABCA1- dependent phospholipid-rich plasma membrane apolipoprotein A-I binding site for nascent HDL formation: implications for current models of HDL biogenesis. J. Lipid Res. 48, 2428-2442.
    • (2007) J. Lipid Res , vol.48 , pp. 2428-2442
    • Hassan, H.H.1    Denis, M.2    Lee, D.Y.3    Iatan, I.4    Nyholt, D.5    Ruel, I.6    Krimbou, L.7    Genest, J.8
  • 12
    • 35649022609 scopus 로고    scopus 로고
    • The N-terminal (1-44) and C-terminal (198-243) peptides of apolipoprotein A-I behave differently at the triolein/water interface
    • Wang, L., Hua, N., Atkinson, D., and Small, D. M. (2007) The N-terminal (1-44) and C-terminal (198-243) peptides of apolipoprotein A-I behave differently at the triolein/water interface. Biochemistry 46, 12140-12151.
    • (2007) Biochemistry , vol.46 , pp. 12140-12151
    • Wang, L.1    Hua, N.2    Atkinson, D.3    Small, D.M.4
  • 13
    • 0038661046 scopus 로고    scopus 로고
    • Structural studies of N- and C-terminally truncated human apolipoprotein A-I
    • Fang, Y., Gursky, O., and Atkinson, D. (2003) Structural studies of N- and C-terminally truncated human apolipoprotein A-I. Biochemistry 42, 6881-6890.
    • (2003) Biochemistry , vol.42 , pp. 6881-6890
    • Fang, Y.1    Gursky, O.2    Atkinson, D.3
  • 14
    • 33748645937 scopus 로고    scopus 로고
    • Contributions of the Nand 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. (2006) Contributions of the Nand C-terminal helical segments to the lipid-free structure and lipid interaction of apolipoprotein A-I. Biochemistry 45, 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
  • 15
    • 0037593649 scopus 로고    scopus 로고
    • Domain structure and lipid interaction in human apolipoproteins A-I and E, a general model
    • Saito, H., Dhanasekaran, P., Nguyen, D., Holvoet, P., Lund-Katz, S., and Phillips, M. C. (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
  • 16
    • 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., Hilliard, G. M., Fang, J., Macha, S., and Davidson, W. S. (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
  • 17
    • 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. (2006) Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. Proc. Natl. Acad. Sci. U.S.A. 103, 2126- 2131.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , 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
  • 19
    • 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. (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
  • 20
    • 0037155808 scopus 로고    scopus 로고
    • Apolipoprotein A-I alpha-helices 7 and 8 modulate high density lipoprotein subclass distribution
    • Reschly, E. J., Sorci-Thomas, M. G., Davidson, W. S., Meredith, S. C., Reardon, C. A., and Getz, G. S. (2002) Apolipoprotein A-I alpha-helices 7 and 8 modulate high density lipoprotein subclass distribution. J. Biol. Chem. 277, 9645-9654.
    • (2002) J. Biol. Chem , vol.277 , pp. 9645-9654
    • Reschly, E.J.1    Sorci-Thomas, M.G.2    Davidson, W.S.3    Meredith, S.C.4    Reardon, C.A.5    Getz, G.S.6
  • 21
    • 0026057848 scopus 로고
    • Expression of human apolipoprotein A-I in transgenic mice results in reduced plasma levels of murine apolipoprotein A-I and the appearance of two new high density lipoprotein size subclasses
    • Rubin, E. M., Ishida, B. Y., Clift, S. M., and Krauss, R. M. (1991) Expression of human apolipoprotein A-I in transgenic mice results in reduced plasma levels of murine apolipoprotein A-I and the appearance of two new high density lipoprotein size subclasses. Proc. Natl. Acad. Sci. U.S.A. 88, 434-438.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 434-438
    • Rubin, E.M.1    Ishida, B.Y.2    Clift, S.M.3    Krauss, R.M.4
  • 22
    • 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
  • 23
    • 53149092105 scopus 로고    scopus 로고
    • Three dimensional models of high density lipoprotein apoA-I: Implications for its assembly and function
    • Thomas, M. J., Bhat, S., and Sorci-Thomas, M. G. (2008) Three dimensional models of high density lipoprotein apoA-I: Implications for its assembly and function. J. Lipid Res. 49, 1875-1883.
    • (2008) J. Lipid Res , vol.49 , pp. 1875-1883
    • Thomas, M.J.1    Bhat, S.2    Sorci-Thomas, M.G.3
  • 25
    • 34247857427 scopus 로고    scopus 로고
    • Electron paramagnetic resonance spectroscopy of sitedirected 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. (2007) Electron paramagnetic resonance spectroscopy of sitedirected spin labels reveals the structural heterogeneity in the N-terminal domain of apoA-I 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
  • 26
    • 0038442816 scopus 로고    scopus 로고
    • The C-terminal domain of apolipoprotein A-I contains a lipid-sensitive conformational trigger
    • Oda, M. N., Forte, T. M., Ryan, R. O., and Voss, J. C. (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
  • 27
    • 33645789374 scopus 로고    scopus 로고
    • A novel folding intermediate state for apolipoprotein A-I: Role of the amino and carboxy termini
    • Gross, E., Peng, D. Q., Hazen, S. L., and Smith, J. D. (2006) A novel folding intermediate state for apolipoprotein A-I: role of the amino and carboxy termini. Biophys. J. 90, 1362-1370.
    • (2006) Biophys. J , vol.90 , pp. 1362-1370
    • Gross, E.1    Peng, D.Q.2    Hazen, S.L.3    Smith, J.D.4
  • 28
    • 0034727648 scopus 로고    scopus 로고
    • Characterization of apolipoprotein A-I structure using a cysteine-specific fluorescence probe
    • Tricerri, M. A., Behling Agree, A. K., Sanchez, S. A., and Jonas, A. (2000) Characterization of apolipoprotein A-I structure using a cysteine-specific fluorescence probe. Biochemistry 39, 14682- 14691.
    • (2000) Biochemistry , vol.39 , pp. 14682-14691
    • Tricerri, M.A.1    Behling Agree, A.K.2    Sanchez, S.A.3    Jonas, A.4
  • 29
    • 0037060463 scopus 로고    scopus 로고
    • Folding and stability of the C-terminal half of apolipoprotein A-I examined with a Cys-specific fluorescence probe
    • Behling Agree, A. K., Tricerri, M. A., Arnvig McGuire, K., Tian, S. M., and Jonas, A. (2002) Folding and stability of the C-terminal half of apolipoprotein A-I examined with a Cys-specific fluorescence probe. Biochim. Biophys. Acta 1594, 286-296.
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 286-296
    • Behling Agree, A.K.1    Tricerri, M.A.2    Arnvig McGuire, K.3    Tian, S.M.4    Jonas, A.5
  • 30
    • 0242485159 scopus 로고    scopus 로고
    • Lipid-binding studies of human apolipoprotein A-I and its terminally truncated mutants
    • Fang, Y., Gursky, O., and Atkinson, D. (2003) Lipid-binding studies of human apolipoprotein A-I and its terminally truncated mutants. Biochemistry 42, 13260-13268.
    • (2003) Biochemistry , vol.42 , pp. 13260-13268
    • Fang, Y.1    Gursky, O.2    Atkinson, D.3
  • 31
    • 0037470173 scopus 로고    scopus 로고
    • The central helices of ApoA-I can promote ATP-binding cassette transporter A1 (ABCA1)- mediated lipid efflux. Amino acid residues 220-231 of the wildtype ApoA-I are required for lipid efflux in vitro and high density lipoprotein formation in vivo
    • Chroni, A., Liu, T., Gorshkova, I., Kan, H. Y., Uehara, Y., Von Eckardstein, A., and Zannis, V. I. (2003) The central helices of ApoA-I can promote ATP-binding cassette transporter A1 (ABCA1)- mediated lipid efflux. Amino acid residues 220-231 of the wildtype 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
  • 32
    • 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. (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
  • 33
    • 0027076642 scopus 로고
    • The charge and structural stability of apolipoprotein A-I in discoidal and spherical recombinant high density lipoprotein particles
    • Sparks, D. L., Lund-Katz, S., and Phillips, M. C. (1992) The charge and structural stability of apolipoprotein A-I in discoidal and spherical recombinant high density lipoprotein particles. J. Biol. Chem. 267, 25839-25847.
    • (1992) J. Biol. Chem , vol.267 , pp. 25839-25847
    • Sparks, D.L.1    Lund-Katz, S.2    Phillips, M.C.3
  • 34
    • 0025742883 scopus 로고
    • Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence
    • Parasassi, T., De Stasio, G., Ravagnan, G., Rusch, R. M., and Gratton, E. (1991) Quantitation of lipid phases in phospholipid vesicles by the generalized polarization of Laurdan fluorescence. Biophys. J. 60, 179-189.
    • (1991) Biophys. J , vol.60 , pp. 179-189
    • Parasassi, T.1    De Stasio, G.2    Ravagnan, G.3    Rusch, R.M.4    Gratton, E.5
  • 35
    • 0029946687 scopus 로고    scopus 로고
    • Physical states of surface and core lipids in lipid emulsions and apolipoprotein binding to the emulsion surface
    • Saito, H., Minamida, T., Arimoto, I., Handa, T., and Miyajima, K. (1996) Physical states of surface and core lipids in lipid emulsions and apolipoprotein binding to the emulsion surface. J. Biol. Chem. 271, 15515-15520.
    • (1996) J. Biol. Chem , vol.271 , pp. 15515-15520
    • Saito, H.1    Minamida, T.2    Arimoto, I.3    Handa, T.4    Miyajima, K.5
  • 36
    • 0031852954 scopus 로고    scopus 로고
    • Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods
    • Flora, K., Brennan, J. D., Baker, G. A., Doody, M. A., and Bright, F. V. (1998) Unfolding of acrylodan-labeled human serum albumin probed by steady-state and time-resolved fluorescence methods. Biophys. J. 75, 1084-1096.
    • (1998) Biophys. J , vol.75 , pp. 1084-1096
    • Flora, K.1    Brennan, J.D.2    Baker, G.A.3    Doody, M.A.4    Bright, F.V.5
  • 37
    • 40149092972 scopus 로고    scopus 로고
    • Contributions of the carboxyl-terminal helical segment to the self-association and lipoprotein preferences of human apolipoprotein E3 and E4 isoforms
    • Sakamoto, T., Tanaka, M., Vedhachalam, C., Nickel, M., Nguyen, D., Dhanasekaran, P., Phillips, M. C., Lund-Katz, S., and Saito, H. (2008) Contributions of the carboxyl-terminal helical segment to the self-association and lipoprotein preferences of human apolipoprotein E3 and E4 isoforms. Biochemistry 47, 2968-2977.
    • (2008) Biochemistry , vol.47 , pp. 2968-2977
    • Sakamoto, T.1    Tanaka, M.2    Vedhachalam, C.3    Nickel, M.4    Nguyen, D.5    Dhanasekaran, P.6    Phillips, M.C.7    Lund-Katz, S.8    Saito, H.9
  • 38
    • 0035798681 scopus 로고    scopus 로고
    • Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles
    • Saito, H., Dhanasekaran, P., Baldwin, F., Weisgraber, K. H., Lund- Katz, S., and Phillips, M. C. (2001) Lipid binding-induced conformational change in human apolipoprotein E. Evidence for two lipid-bound states on spherical particles. J. Biol. Chem. 276, 40949-40954.
    • (2001) J. Biol. Chem , vol.276 , pp. 40949-40954
    • Saito, H.1    Dhanasekaran, P.2    Baldwin, F.3    Weisgraber, K.H.4    Lund- Katz, S.5    Phillips, M.C.6
  • 40
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions
    • Monera, O. D., Kay, C. M., and Hodges, R. S. (1994) Protein denaturation with guanidine hydrochloride or urea provides a different estimate of stability depending on the contributions of electrostatic interactions. Protein Sci. 3, 1984-1991.
    • (1994) Protein Sci , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 41
    • 0029113051 scopus 로고
    • Modified spectrophotometer for multi-dimensional circular dichroism/ fluorescence data acquisition in titration experiments: Application to the pH and guanidine-HCI induced unfolding of apomyoglobin
    • Ramsay, G., Ionescu, R., and Eftink, M. R. (1995) Modified spectrophotometer for multi-dimensional circular dichroism/ fluorescence data acquisition in titration experiments: application to the pH and guanidine-HCI induced unfolding of apomyoglobin. Biophys. J. 69, 701-707.
    • (1995) Biophys. J , vol.69 , pp. 701-707
    • Ramsay, G.1    Ionescu, R.2    Eftink, M.R.3
  • 44
    • 20444474976 scopus 로고    scopus 로고
    • Structural insights into a yeast prion illuminate nucleation and strain diversity
    • Krishnan, R., and Lindquist, S. L. (2005) Structural insights into a yeast prion illuminate nucleation and strain diversity. Nature 435, 765-772.
    • (2005) Nature , vol.435 , pp. 765-772
    • Krishnan, R.1    Lindquist, S.L.2
  • 45
    • 34247856087 scopus 로고    scopus 로고
    • Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure
    • Sun, Y., Breydo, L., Makarava, N., Yang, Q., Bocharova, O. V., and Baskakov, I. V. (2007) Site-specific conformational studies of prion protein (PrP) amyloid fibrils revealed two cooperative folding domains within amyloid structure. J. Biol. Chem. 282, 9090-9097.
    • (2007) J. Biol. Chem , vol.282 , pp. 9090-9097
    • Sun, Y.1    Breydo, L.2    Makarava, N.3    Yang, Q.4    Bocharova, O.V.5    Baskakov, I.V.6
  • 46
    • 54849438885 scopus 로고    scopus 로고
    • Conformational flexibility of the N-terminal domain of apolipoprotein a-I bound to spherical lipid particles
    • Kono, M., Okumura, Y., Tanaka, M., Nguyen, D., Dhanasekaran, P., Lund-Katz, S., Phillips, M. C., and Saito, H. (2008) Conformational flexibility of the N-terminal domain of apolipoprotein a-I bound to spherical lipid particles. Biochemistry 47, 11340-11347.
    • (2008) Biochemistry , vol.47 , pp. 11340-11347
    • Kono, M.1    Okumura, Y.2    Tanaka, M.3    Nguyen, D.4    Dhanasekaran, P.5    Lund-Katz, S.6    Phillips, M.C.7    Saito, H.8
  • 47
    • 0031916981 scopus 로고    scopus 로고
    • Prodan as a membrane surface fluorescence probe: Partitioning between water and phospholipid phases
    • Krasnowska, E. K., Gratton, E., and Parasassi, T. (1998) Prodan as a membrane surface fluorescence probe: partitioning between water and phospholipid phases. Biophys. J. 74, 1984-1993.
    • (1998) Biophys. J , vol.74 , pp. 1984-1993
    • Krasnowska, E.K.1    Gratton, E.2    Parasassi, T.3
  • 48
    • 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. (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
  • 50
    • 49749136969 scopus 로고    scopus 로고
    • The N-terminus of apolipoprotein A-V adopts a helix bundle molecular architecture
    • Wong, K., Beckstead, J. A., Lee, D., Weers, P. M., Guigard, E., Kay, C. M., and Ryan, R. O. (2008) The N-terminus of apolipoprotein A-V adopts a helix bundle molecular architecture. Biochemistry 47, 8768-8774.
    • (2008) Biochemistry , vol.47 , pp. 8768-8774
    • Wong, K.1    Beckstead, J.A.2    Lee, D.3    Weers, P.M.4    Guigard, E.5    Kay, C.M.6    Ryan, R.O.7
  • 51
    • 12844284527 scopus 로고    scopus 로고
    • The N-terminal to C-terminal motif in protein folding and function
    • Krishna, M. M., and Englander, S. W. (2005) The N-terminal to C-terminal motif in protein folding and function. Proc. Natl. Acad. Sci. U.S.A. 102, 1053-1058.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 1053-1058
    • Krishna, M.M.1    Englander, S.W.2
  • 52
    • 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. (2005) Modulation of apolipoprotein E structure by domain interaction: differences in lipid-bound and lipid-free forms. J. Biol. Chem. 280, 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
  • 53
    • 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
  • 54
    • 0029766916 scopus 로고    scopus 로고
    • Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins
    • Dong, L. M., and Weisgraber, K. H. (1996) Human apolipoprotein E4 domain interaction. Arginine 61 and glutamic acid 255 interact to direct the preference for very low density lipoproteins. J. Biol. Chem. 271, 19053-19057.
    • (1996) J. Biol. Chem , vol.271 , pp. 19053-19057
    • Dong, L.M.1    Weisgraber, K.H.2
  • 56
    • 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. (1999) A molecular trigger of lipid binding-induced opening of a helix bundle exchangeable apolipoprotein. Proc. Natl. Acad. Sci. U.S.A. 96, 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
  • 57
    • 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. (2000) Conformational reorganization of the four-helix bundle of human apolipoprotein E in binding to phospholipid. J. Biol. Chem. 275, 20775- 20781.
    • (2000) J. Biol. Chem , vol.275 , pp. 20775-20781
    • Lu, B.1    Morrow, J.A.2    Weisgraber, K.H.3
  • 58
    • 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. (2002) Apolipoprotein E4 forms a molten globule. A potential basis for its association with disease. J. Biol. Chem. 277, 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
  • 59
    • 55249108015 scopus 로고    scopus 로고
    • Correlation of structural stability with functional remodeling of high-density lipoproteins: The importance of being disordered
    • Guha, M., Gao, X., Jayaraman, S., and Gursky, O. (2008) Correlation of structural stability with functional remodeling of high-density lipoproteins: the importance of being disordered. Biochemistry 47, 11393-11397.
    • (2008) Biochemistry , vol.47 , pp. 11393-11397
    • Guha, M.1    Gao, X.2    Jayaraman, S.3    Gursky, O.4
  • 60
    • 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., Kay, C. M., and Ryan, R. O. (2001) Conformational changes of an exchangeable apolipoprotein, apolipophorin III from Locusta migratoria, at low pH: correlation with lipid binding. Biochemistry 40, 7754-7760.
    • (2001) Biochemistry , vol.40 , pp. 7754-7760
    • Weers, P.M.1    Kay, C.M.2    Ryan, R.O.3
  • 61
    • 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., Abdullahi, W. E., Cabrera, J. M., and Hsu, T. C. (2005) Role of buried polar residues in helix bundle stability and lipid binding of apolipophorin III: destabilization by threonine 31. Biochemistry 44, 8810-8816.
    • (2005) Biochemistry , vol.44 , pp. 8810-8816
    • Weers, P.M.1    Abdullahi, W.E.2    Cabrera, J.M.3    Hsu, T.C.4
  • 62
    • 0037438653 scopus 로고    scopus 로고
    • Lipid binding ability of human apolipoprotein E N-terminal domain isoforms: Correlation with protein stability?
    • Weers, P. M., Narayanaswami, V., Choy, N., Luty, R., Hicks, L., Kay, C. M., and Ryan, R. O. (2003) Lipid binding ability of human apolipoprotein E N-terminal domain isoforms: correlation with protein stability? Biophys. Chem. 100, 481-492.
    • (2003) Biophys. Chem , vol.100 , pp. 481-492
    • Weers, P.M.1    Narayanaswami, V.2    Choy, N.3    Luty, R.4    Hicks, L.5    Kay, C.M.6    Ryan, R.O.7
  • 63
    • 58149469594 scopus 로고    scopus 로고
    • Conformational change of apolipoprotein A-I and HDL formation from model membranes under intracellular acidic conditions
    • Fukuda, M., Nakano, M., Miyazaki, M., Tanaka, M., Saito, H., Kobayashi, S., Ueno, M., and Handa, T. (2008) Conformational change of apolipoprotein A-I and HDL formation from model membranes under intracellular acidic conditions. J. Lipid Res. 49, 2419-2426.
    • (2008) J. Lipid Res , vol.49 , pp. 2419-2426
    • Fukuda, M.1    Nakano, M.2    Miyazaki, M.3    Tanaka, M.4    Saito, H.5    Kobayashi, S.6    Ueno, M.7    Handa, T.8
  • 64
    • 0036520326 scopus 로고    scopus 로고
    • The structural basis for amyloid formation by plasma apolipoproteins: A review
    • Hatters, D. M., and Howlett, G. J. (2002) The structural basis for amyloid formation by plasma apolipoproteins: a review. Eur. Biophys. J. 31, 2-8.
    • (2002) Eur. Biophys. J , vol.31 , pp. 2-8
    • Hatters, D.M.1    Howlett, G.J.2
  • 65
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N., and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded. Biochim. Biophys. Acta 1698, 131-153.
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 66
    • 0036234218 scopus 로고    scopus 로고
    • The effects of altered apolipoprotein A-I structure on plasma HDL concentration
    • Sorci-Thomas, M. G., and Thomas, M. J. (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
  • 68
    • 35848967214 scopus 로고    scopus 로고
    • ApoA-I cleaved by transthyretin has reduced ability to promote cholesterol efflux and increased amyloidogenicity
    • Liz, M. A., Gomes, C. M., Saraiva, M. J., and Sousa, M. M. (2007) ApoA-I cleaved by transthyretin has reduced ability to promote cholesterol efflux and increased amyloidogenicity. J. Lipid Res. 48, 2385-2395.
    • (2007) J. Lipid Res , vol.48 , pp. 2385-2395
    • Liz, M.A.1    Gomes, C.M.2    Saraiva, M.J.3    Sousa, M.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.