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Volumn 264, Issue 1, 1999, Pages 183-190

Apolipoprotein A-I(Milano) unfolds via an intermediate state as studied by differential scanning calorimetry and circular dichroism

Author keywords

Apolipoprotein A I(M); Intermediate state; Molten globular state; Protein denaturation; Thermal unfolding

Indexed keywords

APOLIPOPROTEIN A1;

EID: 0033567265     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00604.x     Document Type: Article
Times cited : (11)

References (20)
  • 1
    • 0029591840 scopus 로고
    • Binding of molten globule-like conformations to lipid bilayers
    • 1. Banuelos, S. & Muga, A. (1995) Binding of molten globule-like conformations to lipid bilayers. J. Biol. Chem. 270, 29910-29915.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29910-29915
    • Banuelos, S.1    Muga, A.2
  • 2
    • 0030726361 scopus 로고    scopus 로고
    • pH and temperature-induced molten globule-like denatured states of equinatoxin II: A study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence
    • 2. Poklar, N., Lah, J., Salobir, M., Macek, P. & Vesnaver, G. (1997) pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far-and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36, 14345-14352.
    • (1997) Biochemistry , vol.36 , pp. 14345-14352
    • Poklar, N.1    Lah, J.2    Salobir, M.3    Macek, P.4    Vesnaver, G.5
  • 3
    • 0029132790 scopus 로고
    • Thermodynamics of partly folded intermediates in proteins
    • 3. Freire, E. (1995) Thermodynamics of partly folded intermediates in proteins. Annu. Rev. Biophys. Biomol. Struct. 24, 141-165.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 141-165
    • Freire, E.1
  • 4
    • 0014264541 scopus 로고
    • The plasma lecithin: Cholesterol acyltransferase reaction
    • 4. Glomset, J.A. (1968) The plasma lecithin: cholesterol acyltransferase reaction. J. Lipid Res. 9, 155-162.
    • (1968) J. Lipid Res. , vol.9 , pp. 155-162
    • Glomset, J.A.1
  • 5
    • 0024449985 scopus 로고
    • High-density lipoprotein - The clinical implications of recent studies
    • 5. Gordon, D.J. & Rifkind, B.M. (1989) High-density lipoprotein -the clinical implications of recent studies. N. Engl. J. Med. 321, 1311-1316.
    • (1989) N. Engl. J. Med. , vol.321 , pp. 1311-1316
    • Gordon, D.J.1    Rifkind, B.M.2
  • 8
    • 0018798904 scopus 로고
    • Asymmetry of apolipoprotein A-I in solution assessed from ultracentrifugal, viscometric, and fluorescence polarization studies
    • 8. Barbeau, D.L., Jonas, A., Teng, T.-I. & Scanu, A.M. (1979) Asymmetry of apolipoprotein A-I in solution 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.-I.3    Scanu, A.M.4
  • 9
    • 0029864592 scopus 로고    scopus 로고
    • Thermal unfolding of human high-density apolipoprotein A-I: Implications for a lipid-free molten globular state
    • 9. Gursky, O. & Atkinson, D. (1996) Thermal unfolding of human high-density apolipoprotein A-I: 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
  • 13
    • 0017064087 scopus 로고
    • Conformational and thermodynamic properties of apo A-I of human plasma high density lipoproteins
    • 13. Tall, A.R., Shipley, G.G. & Small, D.M. (1976) Conformational and thermodynamic properties of apo A-I of human plasma high density lipoproteins. J. Biol. Chem. 251, 3749-3755.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3749-3755
    • Tall, A.R.1    Shipley, G.G.2    Small, D.M.3
  • 14
    • 0002527319 scopus 로고    scopus 로고
    • Thermodynamic background to differential scanning calorimetry
    • Ladbury, J.E. & Chowdry, B.Z., eds, Wiley, Chichester
    • 14. Leharne, S.A. & Chowdry, B.Z. (1998) Thermodynamic background to differential scanning calorimetry. In Biocalorimetry: Applications in the Biological Sciences (Ladbury, J.E. & Chowdry, B.Z., eds), pp. 157-182. Wiley, Chichester.
    • (1998) Biocalorimetry: Applications in the Biological Sciences , pp. 157-182
    • Leharne, S.A.1    Chowdry, B.Z.2
  • 15
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • 15. Sturtevant, J.M. (1987) Biochemical applications of differential scanning calorimetry. Annu. Rev. Phys. Chem. 38, 463-488.
    • (1987) Annu. Rev. Phys. Chem. , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 16
    • 0028348303 scopus 로고
    • Induction of secondary structure in the peptide hormone motilin by interaction with phospholipid vesicles
    • 16. Backlund, B.-M., Wikander, G., Peeters, T.L. & Gräslund, A. (1994) Induction of secondary structure in the peptide hormone motilin by interaction with phospholipid vesicles. Biochim. Biophys. Acta 1190, 337-344.
    • (1994) Biochim. Biophys. Acta , vol.1190 , pp. 337-344
    • Backlund, B.-M.1    Wikander, G.2    Peeters, T.L.3    Gräslund, A.4
  • 17
    • 0025179832 scopus 로고
    • Protein folding
    • 17. Creighton, T.E. (1990) Protein folding. Biochem. J. 270, 1-16.
    • (1990) Biochem. J. , vol.270 , pp. 1-16
    • Creighton, T.E.1
  • 18
    • 0001220959 scopus 로고
    • Salt-induced formation of the molten globular state of apomyoglobin studied by isothermal titration calorimetry
    • 18. Hamada, D., Fukada, H., Takahashi, K. & Goto, Y. (1995) Salt-induced formation of the molten globular state of apomyoglobin studied by isothermal titration calorimetry. Thermochim. Acta 266, 385-400.
    • (1995) Thermochim. Acta , vol.266 , pp. 385-400
    • Hamada, D.1    Fukada, H.2    Takahashi, K.3    Goto, Y.4
  • 19
    • 0019332583 scopus 로고
    • Effect of guanidine hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution
    • 19. Edelstein, C. & Scanu, A.M. (1980) Effect of guanidine hydrochloride on the hydrodynamic and thermodynamic properties of human apolipoprotein A-I in solution. J. Biol. Chem. 255, 5747-5754.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5747-5754
    • Edelstein, C.1    Scanu, A.M.2
  • 20
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c
    • 20. Hagihara, Y., Tan, Y. & Goto, Y. (1994) Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. J. Mol. Biol. 237, 336-348.
    • (1994) J. Mol. Biol. , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.