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Volumn 1601, Issue 2, 2002, Pages 185-191

Structural and drug-binding properties of α1-acid glycoprotein in reverse micelles

Author keywords

1 Acid glycoprotein; Conformational transition; Drug binding; Reverse micelle

Indexed keywords

CHLORPROMAZINE; OROSOMUCOID; PROGESTERONE; SODIUM CHLORIDE; STEROID HORMONE; DICOUMAROL;

EID: 0037121465     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1570-9639(02)00465-X     Document Type: Article
Times cited : (28)

References (37)
  • 2
    • 0023690101 scopus 로고
    • Drug binding to human alpha-1-acid glycoprotein in health and disease [Review]
    • Kremer J.M., Wilting J., Janssen L.H. Drug binding to human alpha-1-acid glycoprotein in health and disease [Review]. Pharmacol. Rev. 40(1):1988;1-47.
    • (1988) Pharmacol. Rev. , vol.40 , Issue.1 , pp. 1-47
    • Kremer, J.M.1    Wilting, J.2    Janssen, L.H.3
  • 3
    • 0026574265 scopus 로고
    • Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein
    • Treuheit M.J., Costello C.E., Halsall H.B. Analysis of the five glycosylation sites of human alpha 1-acid glycoprotein. Biochem. J. 283(1):1992;105-112.
    • (1992) Biochem. J. , vol.283 , Issue.1 , pp. 105-112
    • Treuheit, M.J.1    Costello, C.E.2    Halsall, H.B.3
  • 4
    • 0021435555 scopus 로고
    • Structure of mouse major urinary protein genes: Different splicing configurations in the 3′-non-coding region
    • Clark A.J., Clissold P.M., Al Shawi R., Beattie P., Bishop J. Structure of mouse major urinary protein genes: different splicing configurations in the 3′-non-coding region. EMBO J. 3(5):1984;1045-1052.
    • (1984) EMBO J. , vol.3 , Issue.5 , pp. 1045-1052
    • Clark, A.J.1    Clissold, P.M.2    Al Shawi, R.3    Beattie, P.4    Bishop, J.5
  • 5
    • 0019450585 scopus 로고
    • Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances
    • Weisiger R., Gollan J., Ockner R. Receptor for albumin on the liver cell surface may mediate uptake of fatty acids and other albumin-bound substances. Science. 211(4486):1981;1048-1051.
    • (1981) Science , vol.211 , Issue.4486 , pp. 1048-1051
    • Weisiger, R.1    Gollan, J.2    Ockner, R.3
  • 6
    • 0019425855 scopus 로고
    • Albumin helps mediate removal of taurocholate by rat liver
    • Forker E.L., Luxon B.A. Albumin helps mediate removal of taurocholate by rat liver. J. Clin. Invest. 67(5):1981;1517-1522.
    • (1981) J. Clin. Invest. , vol.67 , Issue.5 , pp. 1517-1522
    • Forker, E.L.1    Luxon, B.A.2
  • 7
    • 0021029231 scopus 로고
    • Albumin-mediated transport of rose bengal by perfused rat liver. Kinetics of the reaction at the cell surface
    • Forker E.L., Luxon B.A. Albumin-mediated transport of rose bengal by perfused rat liver. Kinetics of the reaction at the cell surface. J. Clin. Invest. 72(5):1983;1764-1771.
    • (1983) J. Clin. Invest. , vol.72 , Issue.5 , pp. 1764-1771
    • Forker, E.L.1    Luxon, B.A.2
  • 8
    • 0023916444 scopus 로고
    • Conformational change in plasma albumin due to interaction with isolated rat hepatocyte
    • Horie T., Mizuma T., Kasai S., Awazu S. Conformational change in plasma albumin due to interaction with isolated rat hepatocyte. Am. J. Physiol. 254(4 Pt. 1):1988;G465-G470.
    • (1988) Am. J. Physiol. , vol.254 , Issue.4 PART 1 , pp. 465-G470
    • Horie, T.1    Mizuma, T.2    Kasai, S.3    Awazu, S.4
  • 9
    • 0024963570 scopus 로고
    • Conformational states of beta-lactoglobulin: Molten-globule states at acidic and alkaline pH with high salt
    • Goto Y., Fink A.L. Conformational states of beta-lactoglobulin: molten-globule states at acidic and alkaline pH with high salt. Biochemistry. 28(3):1989;945-952.
    • (1989) Biochemistry , vol.28 , Issue.3 , pp. 945-952
    • Goto, Y.1    Fink, A.L.2
  • 11
    • 0025026407 scopus 로고
    • Phase diagram for acidic conformational states of apomyoglobin
    • Goto Y., Fink A.L. Phase diagram for acidic conformational states of apomyoglobin. J. Mol. Biol. 214(4):1990;803-805.
    • (1990) J. Mol. Biol. , vol.214 , Issue.4 , pp. 803-805
    • Goto, Y.1    Fink, A.L.2
  • 12
    • 0023489606 scopus 로고
    • Activity and conformation of enzymes in reverse micellar solutions
    • Luisi P.L., Steinmann-Hofmann B. Activity and conformation of enzymes in reverse micellar solutions. Methods Enzymol. 136:1987;188-216.
    • (1987) Methods Enzymol. , vol.136 , pp. 188-216
    • Luisi, P.L.1    Steinmann-Hofmann, B.2
  • 13
    • 0014425856 scopus 로고
    • Steroid-protein interactions studies by fluorescence quenching
    • Attallah N.A., Lata G.F. Steroid-protein interactions studies by fluorescence quenching. Biochim. Biophys. Acta. 168(2):1968;321-333.
    • (1968) Biochim. Biophys. Acta , vol.168 , Issue.2 , pp. 321-333
    • Attallah, N.A.1    Lata, G.F.2
  • 14
    • 0022388178 scopus 로고
    • Fluorescence quenching of human orosomucoid. Accessibility to drugs and small quenching agents
    • Friedman M.L., Schlueter K.T., Kirley T.L., Halsall H.B. Fluorescence quenching of human orosomucoid. Accessibility to drugs and small quenching agents. Biochem. J. 232(3):1985;863-867.
    • (1985) Biochem. J. , vol.232 , Issue.3 , pp. 863-867
    • Friedman, M.L.1    Schlueter, K.T.2    Kirley, T.L.3    Halsall, H.B.4
  • 16
    • 0002829561 scopus 로고    scopus 로고
    • Molten globule-like state of human serum albumin at low pH
    • Muzammil S., Kumar Y., Tayyab S. Molten globule-like state of human serum albumin at low pH. Eur. J. Biochem. 266(1):1999;26-32.
    • (1999) Eur. J. Biochem. , vol.266 , Issue.1 , pp. 26-32
    • Muzammil, S.1    Kumar, Y.2    Tayyab, S.3
  • 17
    • 0034728379 scopus 로고    scopus 로고
    • The single mutation Phe173-Ala induces a molten globule-like state in murine interleukin-6
    • Matthews J.M., Norton R.S., Hammacher A., Simpson R.J. The single mutation Phe173-Ala induces a molten globule-like state in murine interleukin-6. Biochemistry. 39(8):2000;1942-1950.
    • (2000) Biochemistry , vol.39 , Issue.8 , pp. 1942-1950
    • Matthews, J.M.1    Norton, R.S.2    Hammacher, A.3    Simpson, R.J.4
  • 18
    • 0033554860 scopus 로고    scopus 로고
    • Folding and assembly of dimeric human glutathione transferase A1-1
    • Wallace L.A., Dirr H.W. Folding and assembly of dimeric human glutathione transferase A1-1. Biochemistry. 38(50):1999;16686-16694.
    • (1999) Biochemistry , vol.38 , Issue.50 , pp. 16686-16694
    • Wallace, L.A.1    Dirr, H.W.2
  • 19
    • 0032568455 scopus 로고    scopus 로고
    • Transcytosis of alpha1-acidic glycoprotein in the continuous microvascular endothelium
    • Predescu D., Predescu S., McQuistan T., Palade G.E. Transcytosis of alpha1-acidic glycoprotein in the continuous microvascular endothelium. Proc. Natl. Acad. Sci. U. S. A. 95(11):1998;6175-6180.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , Issue.11 , pp. 6175-6180
    • Predescu, D.1    Predescu, S.2    McQuistan, T.3    Palade, G.E.4
  • 20
    • 0027136215 scopus 로고
    • Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding
    • Kemmink J., Creighton T.E. Local conformations of peptides representing the entire sequence of bovine pancreatic trypsin inhibitor and their roles in folding. J. Mol. Biol. 234(3):1993;861-878.
    • (1993) J. Mol. Biol. , vol.234 , Issue.3 , pp. 861-878
    • Kemmink, J.1    Creighton, T.E.2
  • 21
    • 0029124248 scopus 로고
    • Molten globule and protein folding
    • (Review, 423 references)
    • Ptitsyn O.B. Molten globule and protein folding. (Review, 423 references) Adv. Protein Chem. 47:1995;83-229.
    • (1995) Adv. Protein Chem. , vol.47 , pp. 83-229
    • Ptitsyn, O.B.1
  • 22
    • 0026574178 scopus 로고
    • Diphtheria toxin: Membrane interaction and membrane translocation
    • (Review, 216 references)
    • London E. Diphtheria toxin: membrane interaction and membrane translocation. (Review, 216 references) Biochim. Biophys. Acta. 1113(1):1992;25-51.
    • (1992) Biochim. Biophys. Acta , vol.1113 , Issue.1 , pp. 25-51
    • London, E.1
  • 24
    • 0026603603 scopus 로고
    • A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate
    • Jongh H.H., Killian J.A., Kruijff B. A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate. Biochemistry. 31(6):1992;1636-1643.
    • (1992) Biochemistry , vol.31 , Issue.6 , pp. 1636-1643
    • Jongh, H.H.1    Killian, J.A.2    Kruijff, B.3
  • 25
    • 0029591840 scopus 로고
    • Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes
    • Banuelos S., Muga A. Binding of molten globule-like conformations to lipid bilayers. Structure of native and partially folded alpha-lactalbumin bound to model membranes. J. Biol. Chem. 270(50):1995;29910-29915.
    • (1995) J. Biol. Chem. , vol.270 , Issue.50 , pp. 29910-29915
    • Banuelos, S.1    Muga, A.2
  • 26
    • 0032491199 scopus 로고    scopus 로고
    • Ligand-induced conformational change in transferrins: Crystal structure of the open form of the N-terminal half-molecule of human transferrin
    • Jeffrey P.D., Bewley M.C., MacGillivray R.T., Mason A.B., Woodworth R.C., Baker E.N. Ligand-induced conformational change in transferrins: crystal structure of the open form of the N-terminal half-molecule of human transferrin. Biochemistry. 37(40):1998;13978-13986.
    • (1998) Biochemistry , vol.37 , Issue.40 , pp. 13978-13986
    • Jeffrey, P.D.1    Bewley, M.C.2    MacGillivray, R.T.3    Mason, A.B.4    Woodworth, R.C.5    Baker, E.N.6
  • 27
    • 0030593483 scopus 로고    scopus 로고
    • Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin
    • Smith E.R., Storch J. Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin. J. Mol. Biol. 260(3):1996;312-316.
    • (1996) J. Mol. Biol. , vol.260 , Issue.3 , pp. 312-316
    • Smith, E.R.1    Storch, J.2
  • 29
    • 0029740071 scopus 로고    scopus 로고
    • Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein
    • Hamada D., Segawa S., Goto Y. Non-native alpha-helical intermediate in the refolding of beta-lactoglobulin, a predominantly beta-sheet protein. Nat. Struct. Biol. 3(10):1996;868-873.
    • (1996) Nat. Struct. Biol. , vol.3 , Issue.10 , pp. 868-873
    • Hamada, D.1    Segawa, S.2    Goto, Y.3
  • 31
    • 0029022692 scopus 로고
    • Molecular evolution of plasminogen activator inhibitor-1 functional stability
    • Berkenpas M.B., Lawrence D.A., Ginsburg D. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO. J. 14(13):1995;2969-2977.
    • (1995) EMBO. J. , vol.14 , Issue.13 , pp. 2969-2977
    • Berkenpas, M.B.1    Lawrence, D.A.2    Ginsburg, D.3
  • 33
    • 0033601248 scopus 로고    scopus 로고
    • Membrane environment alters the conformational structure of the recombinant human prion protein
    • Morillas M., Swietnicki W., Gambetti P., Surewicz W.K. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274(52):1999;36859-36865.
    • (1999) J. Biol. Chem. , vol.274 , Issue.52 , pp. 36859-36865
    • Morillas, M.1    Swietnicki, W.2    Gambetti, P.3    Surewicz, W.K.4
  • 34
    • 0036306046 scopus 로고    scopus 로고
    • Binding of prion protein to lipid membranes and implications for prion conversion
    • Sanghera N., Pinheiro T.J. Binding of prion protein to lipid membranes and implications for prion conversion. J. Mol. Biol. 315(5):2002;1241-1256.
    • (2002) J. Mol. Biol. , vol.315 , Issue.5 , pp. 1241-1256
    • Sanghera, N.1    Pinheiro, T.J.2
  • 35
    • 0345771832 scopus 로고
    • Immunosuppression by human plasma alpha 1-acid glycoprotein: Importance of the carbohydrate moiety
    • Bennett M., Schmid K. Immunosuppression by human plasma alpha 1-acid glycoprotein: importance of the carbohydrate moiety. Proc. Natl. Acad. Sci. U. S. A. 77(10):1980;6109-6113.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , Issue.10 , pp. 6109-6113
    • Bennett, M.1    Schmid, K.2
  • 36
    • 0020702161 scopus 로고
    • Leucocyte-associated plasma proteins. Association of prealbumin, albumin, orosomucoid, alpha 1-antitrypsin, transferrin and haptoglobin with human lymphocytes, monocytes, granulocytes and a promyelocytic leukaemic cell line (HL 60)
    • Andersen M.M. Leucocyte-associated plasma proteins. Association of prealbumin, albumin, orosomucoid, alpha 1-antitrypsin, transferrin and haptoglobin with human lymphocytes, monocytes, granulocytes and a promyelocytic leukaemic cell line (HL 60). Scand. J. Clin. Lab. Invest. 43(1):1983;49-59.
    • (1983) Scand. J. Clin. Lab. Invest. , vol.43 , Issue.1 , pp. 49-59
    • Andersen, M.M.1
  • 37
    • 0021259068 scopus 로고
    • Leucocyte-associated plasma proteins in leucocytes during disease states, and in leukaemic cells
    • Andersen M.M. Leucocyte-associated plasma proteins in leucocytes during disease states, and in leukaemic cells. Scand. J. Clin. Lab. Invest. 44(3):1984;257-265.
    • (1984) Scand. J. Clin. Lab. Invest. , vol.44 , Issue.3 , pp. 257-265
    • Andersen, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.