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Volumn 272, Issue 10, 2005, Pages 2399-2406

The lipid/protein interface as xenobiotic target site: Kinetic analysis of tadpole narcosis

Author keywords

Adair theory; Kinetic modelling; Lipid protein interface; Nicotinic acetylcholine receptor; Tadpole narcosis

Indexed keywords

ALCOHOL; ANESTHETIC AGENT; CYCLOHEPTANOL; CYCLOHEXANOL; CYCLOOCTANOL; HEPTANOL; HEXANOL; LIPID; MEMBRANE PROTEIN; NICOTINIC AGENT; NICOTINIC RECEPTOR; OCTANOL; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 18944369267     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04657.x     Document Type: Article
Times cited : (1)

References (45)
  • 1
    • 0035424669 scopus 로고    scopus 로고
    • High-resolution structures and dynamics of membrane protein-lipid complexes: A critique
    • Pebay-Peyroula E & Rosenbusch JP (2001) High-resolution structures and dynamics of membrane protein-lipid complexes: a critique. Curr Opin Struct Biol 11, 427-432.
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 427-432
    • Pebay-Peyroula, E.1    Rosenbusch, J.P.2
  • 2
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • Lee AG (2003) Lipid-protein interactions in biological membranes: a structural perspective. Biochim Biophys Acta 1612, 1-40.
    • (2003) Biochim Biophys Acta , vol.1612 , pp. 1-40
    • Lee, A.G.1
  • 3
    • 2942564630 scopus 로고    scopus 로고
    • Structural commonalities among integral membrane enzymes
    • Bracey MH, Cravatt BF & Stevens RC (2004) Structural commonalities among integral membrane enzymes. FEBS Lett 567, 159-165.
    • (2004) FEBS Lett , vol.567 , pp. 159-165
    • Bracey, M.H.1    Cravatt, B.F.2    Stevens, R.C.3
  • 4
    • 7044274626 scopus 로고    scopus 로고
    • Lipids in membrane protein structures
    • Palsdottir H & Hunte C (2004) Lipids in membrane protein structures. Biochim Biophys Acta 1666, 2-18.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 2-18
    • Palsdottir, H.1    Hunte, C.2
  • 5
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • Marsh D & Horvath LI (1998) Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim Biophys Acta 1376, 267-296.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 6
    • 7044224839 scopus 로고    scopus 로고
    • The protein-lipid interface: Perspectives from magnetic resonance and crystal structures
    • Marsh D & Páli T (2004) The protein-lipid interface: perspectives from magnetic resonance and crystal structures. Biochim Biophys Acta 1666, 118-141.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 118-141
    • Marsh, D.1    Páli, T.2
  • 7
    • 0344982085 scopus 로고    scopus 로고
    • Interactions of anionic phospholipids and phospatidylenethanolamine with the potassium channel KcsA
    • Alvis SJ, Williamson IM, East JM & Lee AG (2002) Interactions of anionic phospholipids and phospatidylenethanolamine with the potassium channel KcsA. Biophys J 85, 3828-3838.
    • (2002) Biophys J , vol.85 , pp. 3828-3838
    • Alvis, S.J.1    Williamson, I.M.2    East, J.M.3    Lee, A.G.4
  • 8
    • 0037070567 scopus 로고    scopus 로고
    • High free energy of lipid/protein interaction in biological membranes
    • Sandermann H (2002) High free energy of lipid/protein interaction in biological membranes. FEBS Lett 514, 340-342.
    • (2002) FEBS Lett , vol.514 , pp. 340-342
    • Sandermann, H.1
  • 9
    • 0022974551 scopus 로고
    • Site-site interaction in the phospholipid activation of D-β-hydroxybutyrate dehydrogenase
    • Sandermann H, McIntyre JO & Fleischer S (1986) Site-site interaction in the phospholipid activation of D-β-hydroxybutyrate dehydrogenase. J Biol Chem 261, 6201-6208.
    • (1986) J Biol Chem , vol.261 , pp. 6201-6208
    • Sandermann, H.1    McIntyre, J.O.2    Fleischer, S.3
  • 10
    • 0034601775 scopus 로고    scopus 로고
    • (R)-3-Hydroxybutyrate dehydrogenase: Selective phosphatidylcholine binding by the C-terminal domain
    • Loeb-Hennard C & McIntyre JO (2000) (R)-3-Hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain. Biochemistry 39, 11928-11938.
    • (2000) Biochemistry , vol.39 , pp. 11928-11938
    • Loeb-Hennard, C.1    McIntyre, J.O.2
  • 11
    • 0038518286 scopus 로고    scopus 로고
    • Assembly of cytochrome c oxidase within the mitochondrion
    • Carr HS & Winge DR (2003) Assembly of cytochrome c oxidase within the mitochondrion. Acc Chem Res 36, 309-316.
    • (2003) Acc Chem Res , vol.36 , pp. 309-316
    • Carr, H.S.1    Winge, D.R.2
  • 12
    • 0037174138 scopus 로고    scopus 로고
    • Cardiolipin: A proton trap for oxidative phosphorylation
    • Haines TH & Dencher NA (2002) Cardiolipin: a proton trap for oxidative phosphorylation. FEBS Lett 528, 35-39.
    • (2002) FEBS Lett , vol.528 , pp. 35-39
    • Haines, T.H.1    Dencher, N.A.2
  • 13
    • 0015460446 scopus 로고
    • The membrane actions of anesthetics and tranquilizers
    • Seeman P (1972) The membrane actions of anesthetics and tranquilizers. Pharmacol Rev 24, 583-655.
    • (1972) Pharmacol Rev , vol.24 , pp. 583-655
    • Seeman, P.1
  • 14
    • 0022309995 scopus 로고
    • The nature of the site of general anesthesia
    • Miller KW (1985) The nature of the site of general anesthesia. Int Rev Neurobiol 27, 1-61.
    • (1985) Int Rev Neurobiol , vol.27 , pp. 1-61
    • Miller, K.W.1
  • 15
    • 0028140369 scopus 로고
    • Molecular and cellular mechanisms of general anaesthesia
    • Franks NP & Lieb WR (1994) Molecular and cellular mechanisms of general anaesthesia. Nature 367, 607-614.
    • (1994) Nature , vol.367 , pp. 607-614
    • Franks, N.P.1    Lieb, W.R.2
  • 16
    • 18244389816 scopus 로고    scopus 로고
    • Which molecular targets are most relevant to general anaesthesia?
    • Franks NP & Lieb WR (1998) Which molecular targets are most relevant to general anaesthesia? Toxicol Lett 100-101, 1-8.
    • (1998) Toxicol Lett , vol.100-101 , pp. 1-8
    • Franks, N.P.1    Lieb, W.R.2
  • 19
    • 0142027322 scopus 로고    scopus 로고
    • Modulation of the nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains
    • Barrantes FJ (2003) Modulation of the nicotinic acetylcholine receptor function through the outer and middle rings of transmembrane domains. Curr Opin Drug Discov Devel 6, 620-632.
    • (2003) Curr Opin Drug Discov Devel , vol.6 , pp. 620-632
    • Barrantes, F.J.1
  • 20
    • 0036069233 scopus 로고    scopus 로고
    • The nature of sites of general anaesthetic action
    • Miller KW (2002) The nature of sites of general anaesthetic action. Br J Anaesth 89, 17-31.
    • (2002) Br J Anaesth , vol.89 , pp. 17-31
    • Miller, K.W.1
  • 21
    • 0027236471 scopus 로고
    • Induction of lipid-protein mismatch by xenobiotics with general membrane targets
    • Sandermann H (1993) Induction of lipid-protein mismatch by xenobiotics with general membrane targets. Biochim Biophys Acta 1150, 130-133.
    • (1993) Biochim Biophys Acta , vol.1150 , pp. 130-133
    • Sandermann, H.1
  • 22
    • 0029886066 scopus 로고    scopus 로고
    • Induction of lipid-protein mismatch by xenobiotics: Kinetic cooperativity
    • Sandermann H & Pflugmacher D (1996) Induction of lipid-protein mismatch by xenobiotics: kinetic cooperativity. Biochim Biophys Acta 1300, 219-225.
    • (1996) Biochim Biophys Acta , vol.1300 , pp. 219-225
    • Sandermann, H.1    Pflugmacher, D.2
  • 23
    • 0035834626 scopus 로고    scopus 로고
    • The lipid/protein interface as xenobiotic target site: Kinetic analysis of the nicotinic acetylcholine receptor
    • Walcher S, Altschuh J & Sandermann H (2001) The lipid/protein interface as xenobiotic target site: kinetic analysis of the nicotinic acetylcholine receptor. J Biol Chem 276, 42191-42195.
    • (2001) J Biol Chem , vol.276 , pp. 42191-42195
    • Walcher, S.1    Altschuh, J.2    Sandermann, H.3
  • 25
    • 0037059803 scopus 로고    scopus 로고
    • Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane
    • Antollini SS & Barrantes FJ (2002) Unique effects of different fatty acid species on the physical properties of the Torpedo acetylcholine receptor membrane. J Biol Chem 277, 1249-1254.
    • (2002) J Biol Chem , vol.277 , pp. 1249-1254
    • Antollini, S.S.1    Barrantes, F.J.2
  • 26
    • 0043166978 scopus 로고    scopus 로고
    • Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ
    • Mantipragada SB, Horvath LI, Arias HR, Schwarzmann G, Sandhoff K, Barrantes FJ & Marsh D (2003) Lipid-protein interactions and effect of local anesthetics in acetylcholine receptor-rich membranes from Torpedo marmorata electric organ. Biochemistry 42, 9167-9175.
    • (2003) Biochemistry , vol.42 , pp. 9167-9175
    • Mantipragada, S.B.1    Horvath, L.I.2    Arias, H.R.3    Schwarzmann, G.4    Sandhoff, K.5    Barrantes, F.J.6    Marsh, D.7
  • 27
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • Miyazawa A, Fujiyoshi Y & Unwin N (2003) Structure and gating mechanism of the acetylcholine receptor pore. Nature 423, 949-955.
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 28
    • 0020185443 scopus 로고
    • Lipid-dependent membrane enzymes. A kinetic model for cooperative activation in the absence of cooperativity in lipid binding
    • Sandermann H (1982) Lipid-dependent membrane enzymes. A kinetic model for cooperative activation in the absence of cooperativity in lipid binding. Eur J Biochem 127, 123-128.
    • (1982) Eur J Biochem , vol.127 , pp. 123-128
    • Sandermann, H.1
  • 29
    • 0024495884 scopus 로고
    • Anaesthetic potencies of primary alcohols: Implications for the molecular dimensions of the anaesthetic site
    • Alifimoff JK, Firestone LL & Miller KW (1986) Anaesthetic potencies of primary alcohols: implications for the molecular dimensions of the anaesthetic site. Br J Pharmacol 96, 9-16.
    • (1986) Br J Pharmacol , vol.96 , pp. 9-16
    • Alifimoff, J.K.1    Firestone, L.L.2    Miller, K.W.3
  • 30
    • 0025910551 scopus 로고
    • Probing the molecular dimensions of general anaesthetic target sites in tadpoles (Xenopus laevis) and model systems using cycloalcohols
    • Curry S, Moss GWJ, Dickinson R, Lieb WR & Franks NP (1991) Probing the molecular dimensions of general anaesthetic target sites in tadpoles (Xenopus laevis) and model systems using cycloalcohols. Br J Pharmacol 102, 167-173.
    • (1991) Br J Pharmacol , vol.102 , pp. 167-173
    • Curry, S.1    Moss, G.W.J.2    Dickinson, R.3    Lieb, W.R.4    Franks, N.P.5
  • 32
    • 0028848223 scopus 로고
    • A discrete site for general anesthetics on a postsynaptic receptor
    • Forman SA, Miller KW & Yellen G (1995) A discrete site for general anesthetics on a postsynaptic receptor. Mol Pharmacol 48, 574-581.
    • (1995) Mol Pharmacol , vol.48 , pp. 574-581
    • Forman, S.A.1    Miller, K.W.2    Yellen, G.3
  • 33
    • 0032440807 scopus 로고    scopus 로고
    • Direct interactions of anesthetics and nonanesthetics with the nicotinic acetylcholine receptor pore
    • Forman SA (1998) Direct interactions of anesthetics and nonanesthetics with the nicotinic acetylcholine receptor pore. Toxicol Lett 100-101, 169-178.
    • (1998) Toxicol Lett , vol.100-101 , pp. 169-178
    • Forman, S.A.1
  • 37
    • 0036713907 scopus 로고    scopus 로고
    • Mice with glycine receptor subunit mutations are both sensitive and resistant to volatile anesthetics
    • Quinlan JJ, Ferguson C, Jester K, Firestone LL & Homanics GE (2002) Mice with glycine receptor subunit mutations are both sensitive and resistant to volatile anesthetics. Anesth Analges 95, 578-582.
    • (2002) Anesth Analges , vol.95 , pp. 578-582
    • Quinlan, J.J.1    Ferguson, C.2    Jester, K.3    Firestone, L.L.4    Homanics, G.E.5
  • 40
    • 1242352964 scopus 로고    scopus 로고
    • Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor
    • Miller AS & Falke JJ (2004) Side chains at the membrane-water interface modulate the signaling state of a transmembrane receptor. Biochemistry 43, 1763-1770.
    • (2004) Biochemistry , vol.43 , pp. 1763-1770
    • Miller, A.S.1    Falke, J.J.2
  • 41
    • 0037058912 scopus 로고    scopus 로고
    • Large-scale molecular dynamics simulations of general anesthetic effects on the ion channel in the fully hydrated membrane: The implication of molecular mechanisms of general anesthesia
    • Tang P & Xu Y (2002) Large-scale molecular dynamics simulations of general anesthetic effects on the ion channel in the fully hydrated membrane: the implication of molecular mechanisms of general anesthesia. Proc Natl Acad Sci USA 99, 16035-16040.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16035-16040
    • Tang, P.1    Xu, Y.2
  • 42
    • 0021110283 scopus 로고
    • Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor
    • Ellena JF, Blazing MA & McNamee MG (1983) Lipid-protein interactions in reconstituted membranes containing acetylcholine receptor. Biochemistry 22, 5523-5535.
    • (1983) Biochemistry , vol.22 , pp. 5523-5535
    • Ellena, J.F.1    Blazing, M.A.2    McNamee, M.G.3
  • 44
    • 0003956970 scopus 로고
    • Addison-Wesley, Reading, MA
    • Lang S (1965) Algebra. Addison-Wesley, Reading, MA.
    • (1965) Algebra
    • Lang, S.1
  • 45
    • 0035273631 scopus 로고    scopus 로고
    • Internet software for the calculation of the lipophilicity and aqueous solubility of chemical compounds
    • Tetko IV, Tanchuk VY, Kasheva TN & Villa AEP (2001) Internet software for the calculation of the lipophilicity and aqueous solubility of chemical compounds. J Chem Inf Comput Sci 41, 246-252.
    • (2001) J Chem Inf Comput Sci , vol.41 , pp. 246-252
    • Tetko, I.V.1    Tanchuk, V.Y.2    Kasheva, T.N.3    Villa, A.E.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.