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Volumn 81, Issue 2, 1996, Pages 185-195

The effects of non-lamellar forming lipids on membrane protein-lipid interactions

Author keywords

Curvature stress; Non lamellar forming lipids; Polymorphism; Protein lipid interactions

Indexed keywords

CHOLESTEROL; DIACYLGLYCEROL; MEMBRANE LIPID; MEMBRANE PROTEIN; PHORBOL ESTER; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPID; PROTEIN KINASE C;

EID: 0030586160     PISSN: 00093084     EISSN: None     Source Type: Journal    
DOI: 10.1016/0009-3084(96)02581-9     Document Type: Article
Times cited : (55)

References (71)
  • 1
    • 0026525339 scopus 로고
    • Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes
    • Bazzi, M.D., Youakim, M.A. and Nelsestuen, G.L. (1992) Importance of phosphatidylethanolamine for association of protein kinase C and other cytoplasmic proteins with membranes. Biochemistry 31, 1125-1134.
    • (1992) Biochemistry , vol.31 , pp. 1125-1134
    • Bazzi, M.D.1    Youakim, M.A.2    Nelsestuen, G.L.3
  • 2
    • 0023109718 scopus 로고
    • Association of protein kinase C with phospholipid vesicles
    • Bazzi, M.D. and Nelsestuen, G.L. (1987) Association of protein kinase C with phospholipid vesicles. Biochemistry 26, 115-122.
    • (1987) Biochemistry , vol.26 , pp. 115-122
    • Bazzi, M.D.1    Nelsestuen, G.L.2
  • 3
    • 0025804529 scopus 로고
    • Lipid activation of protein kinase C
    • Bell, R.M. and Burns, D.J. (1991) Lipid activation of protein kinase C. J. Biol. Chem. 266, 4661-4664.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4661-4664
    • Bell, R.M.1    Burns, D.J.2
  • 4
    • 0025939859 scopus 로고
    • Complexities of the protein kinase C pathway
    • Blumberg, P.M. (1991) Complexities of the protein kinase C pathway. Mol. Carcinog. 4, 339-344.
    • (1991) Mol. Carcinog. , vol.4 , pp. 339-344
    • Blumberg, P.M.1
  • 5
    • 0026729365 scopus 로고
    • Effect of phospholipid unsaturation on protein kinase C activation
    • Bolen, E.J. and Sando, J.J. (1992) Effect of phospholipid unsaturation on protein kinase C activation. Biochemistry 31, 5945-5951.
    • (1992) Biochemistry , vol.31 , pp. 5945-5951
    • Bolen, E.J.1    Sando, J.J.2
  • 6
    • 0027506131 scopus 로고
    • Circular dichroism analysis of ligand-induced conformational changes in protein kinase C
    • Bosca, L. and Moran, F. (1993) Circular dichroism analysis of ligand-induced conformational changes in protein kinase C. Biochem. J. 290, 827-832.
    • (1993) Biochem. J. , vol.290 , pp. 827-832
    • Bosca, L.1    Moran, F.2
  • 7
    • 0026667564 scopus 로고
    • Inhibition of protein kinase C by cationic amphiphiles
    • Bottega, R. and Epand, R.M. (1992) Inhibition of protein kinase C by cationic amphiphiles. Biochemistry 31, 9025-9030.
    • (1992) Biochemistry , vol.31 , pp. 9025-9030
    • Bottega, R.1    Epand, R.M.2
  • 8
    • 0025265401 scopus 로고
    • Protein kinase C penetration into lipid bilayers
    • Brumfeld, V. and Lester, D.S. (1990) Protein kinase C penetration into lipid bilayers. Arch. Biochem. Biophys. 277, 318-323.
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 318-323
    • Brumfeld, V.1    Lester, D.S.2
  • 9
    • 0026754037 scopus 로고
    • Quantitation of lateral stress in lipid layer containing non-bilayer phase preferring lipids by frequency-domain fluorescence spectroscopy
    • Chen, S.Y., Cheng, K.H. and van der Meer, B.W. (1992) Quantitation of lateral stress in lipid layer containing non-bilayer phase preferring lipids by frequency-domain fluorescence spectroscopy. Biochemistry 31, 3759-3768.
    • (1992) Biochemistry , vol.31 , pp. 3759-3768
    • Chen, S.Y.1    Cheng, K.H.2    Van Der Meer, B.W.3
  • 10
    • 0025778806 scopus 로고
    • Regulation of CTP: Phosphocholine cytidyltransferase by lipids. 2. Surface curvature, acyl chain length and lipid phase dependence for activation
    • Cornell, R.B. (1991) Regulation of CTP: phosphocholine cytidyltransferase by lipids. 2. Surface curvature, acyl chain length and lipid phase dependence for activation. Biochemistry 30, 5881-5888.
    • (1991) Biochemistry , vol.30 , pp. 5881-5888
    • Cornell, R.B.1
  • 11
    • 0018171572 scopus 로고
    • Effects of cholesterol on the properties of equimolar mixtures of synthetic phosphatidylethanolamine and phosphatidylcholine
    • Cullis, P.R., van Dijck, P.W.M., de Kruijff, B. and de Gier, J. (1978) Effects of cholesterol on the properties of equimolar mixtures of synthetic phosphatidylethanolamine and phosphatidylcholine. Biochim. Biophys. Acta 513, 21-30.
    • (1978) Biochim. Biophys. Acta , vol.513 , pp. 21-30
    • Cullis, P.R.1    Van Dijck, P.W.M.2    De Kruijff, B.A.3    De Gier, J.4
  • 12
    • 0024496968 scopus 로고
    • Enzymatic and physical characterization of diacylglycerol-phosphatidylcholine interactions in bilayers and monolayers
    • Cunningham, B.A., Tsujita, T. and Brockman, H.L. (1989) Enzymatic and physical characterization of diacylglycerol-phosphatidylcholine interactions in bilayers and monolayers. Biochemistry 28, 32-40.
    • (1989) Biochemistry , vol.28 , pp. 32-40
    • Cunningham, B.A.1    Tsujita, T.2    Brockman, H.L.3
  • 13
    • 0022469893 scopus 로고
    • Modification by diacylglycerol of the structure and interaction of various phospholipid bilayer membranes
    • Das, S. and Rand, R.P. (1986) Modification by diacylglycerol of the structure and interaction of various phospholipid bilayer membranes. Biochemistry 25, 2882-2889.
    • (1986) Biochemistry , vol.25 , pp. 2882-2889
    • Das, S.1    Rand, R.P.2
  • 14
    • 0021688160 scopus 로고
    • Diacylglycerol causes major structural transitions in phospholipid bilayer membranes
    • Das, S. and Rand, R.P. (1984) Diacylglycerol causes major structural transitions in phospholipid bilayer membranes. Biochem. Biophys. Res. Comm. 124, 491-496.
    • (1984) Biochem. Biophys. Res. Comm. , vol.124 , pp. 491-496
    • Das, S.1    Rand, R.P.2
  • 15
    • 33646282474 scopus 로고
    • The properties of polyunsaturated lecithins in monolayers and liposomes and the interactions of these lecithins with cholesterol
    • Demel, R.A., Geurts van Kessel, W.S.M. and van Deenen, L.L.M. (1972) The properties of polyunsaturated lecithins in monolayers and liposomes and the interactions of these lecithins with cholesterol. Biochim. Biophys. Acta 266, 26-40.
    • (1972) Biochim. Biophys. Acta , vol.266 , pp. 26-40
    • Demel, R.A.1    Geurts Van Kessel, W.S.M.2    Van Deenen, L.L.M.3
  • 16
    • 0026776759 scopus 로고
    • Zwitterionic amphiphiles that raise the bilayer to hexagonal phase transition temperature inhibit protein kinase C
    • Epand, R.M., Stafford, A., Wang, J. and Epand, R.F. (1992) Zwitterionic amphiphiles that raise the bilayer to hexagonal phase transition temperature inhibit protein kinase C. FEBS Lett. 245-248.
    • (1992) FEBS Lett. , pp. 245-248
    • Epand, R.M.1    Stafford, A.2    Wang, J.3    Epand, R.F.4
  • 17
    • 0026519683 scopus 로고
    • Hexagonal phase forming propensity detected in phospholipid bilayers with fluorescent probes
    • Epand, R.M. and Leon, B.T. (1992) Hexagonal phase forming propensity detected in phospholipid bilayers with fluorescent probes. Biochemistry 31, 1550-1554.
    • (1992) Biochemistry , vol.31 , pp. 1550-1554
    • Epand, R.M.1    Leon, B.T.2
  • 19
    • 0025334605 scopus 로고
    • The role of membrane biophysical properties in the regulation of protein kinase C activity
    • Epand, R.M. and Lester, D.S. (1990) The role of membrane biophysical properties in the regulation of protein kinase C activity. Trends Pharmacol. Sci. 11, 317-320.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 317-320
    • Epand, R.M.1    Lester, D.S.2
  • 20
    • 0023773284 scopus 로고
    • Determination of the phase behaviour of phosphatidylethanolamine admixed with other lipids and the effects of calcium chloride: Implications for protein kinase C regulation
    • Epand, R.M. and Bottega, R. (1988) Determination of the phase behaviour of phosphatidylethanolamine admixed with other lipids and the effects of calcium chloride: implications for protein kinase C regulation. Biochim. Biophys. Acta 944, 144-154.
    • (1988) Biochim. Biophys. Acta , vol.944 , pp. 144-154
    • Epand, R.M.1    Bottega, R.2
  • 21
    • 0022418382 scopus 로고
    • Diacylglycerols, lysolecithin or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines
    • Epand, R.M. (1985) Diacylglycerols, lysolecithin or hydrocarbons markedly alter the bilayer to hexagonal phase transition temperature of phosphatidylethanolamines. Biochemistry 24, 7092-7095.
    • (1985) Biochemistry , vol.24 , pp. 7092-7095
    • Epand, R.M.1
  • 22
    • 0022080948 scopus 로고
    • Intrinsic curvature hypothesis for biomembrane lipid composition: A role for non-bilayer lipids
    • Gruner, S.M. (1985) Intrinsic curvature hypothesis for biomembrane lipid composition: a role for non-bilayer lipids. Proc. Natl. Acad. Sci. USA 82, 3665-3669.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 3665-3669
    • Gruner, S.M.1
  • 24
    • 0028233768 scopus 로고
    • Effects of halothane and propofol on purified rat brain protein kinase C activation
    • Hemmings, H.C.J. and Adamo, A.I.B. (1994) Effects of halothane and propofol on purified rat brain protein kinase C activation. Anesthesiology 81, 147-155.
    • (1994) Anesthesiology , vol.81 , pp. 147-155
    • Hemmings, H.C.J.1    Adamo, A.I.B.2
  • 25
    • 0029074355 scopus 로고
    • Hydration and order in lipid bilayers
    • Ho, C., Slater, S.J. and Stubbs, C.D. (1995) Hydration and order in lipid bilayers. Biochemistry 34, 6188-6195.
    • (1995) Biochemistry , vol.34 , pp. 6188-6195
    • Ho, C.1    Slater, S.J.2    Stubbs, C.D.3
  • 26
    • 0019781006 scopus 로고
    • Influence of local and neutral anaesthetics on the polymorphic phase preferences of egg yolk phosphatidylethanolamine
    • Hornby, A.P. and Cullis, P.R. (1981) Influence of local and neutral anaesthetics on the polymorphic phase preferences of egg yolk phosphatidylethanolamine. Biochim. Biophys. Acta 647, 285-292.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 285-292
    • Hornby, A.P.1    Cullis, P.R.2
  • 27
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • House, C. and Kemp, B.E. (1987) Protein kinase C contains a pseudosubstrate prototope in its regulatory domain. Science 238, 1726-1728.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 28
    • 0024711084 scopus 로고
    • Effects of lipid packing on polymorphic phase behaviour and membrane properties
    • Hui, S.W. and Sen, A. (1989) Effects of lipid packing on polymorphic phase behaviour and membrane properties. Proc. Natl. Acad. Sci. USA 86, 5825-5829.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5825-5829
    • Hui, S.W.1    Sen, A.2
  • 30
    • 0019888266 scopus 로고
    • Co-operative roles of various membrane phospholipids in the activation of calcium-activated, phospholipid-dependent protein kinase
    • Kaibuchi, K., Takai, Y. and Nishizuka, Y. (1981) Co-operative roles of various membrane phospholipids in the activation of calcium-activated, phospholipid-dependent protein kinase. J. Biol. Chem. 256, 7146-7149.
    • (1981) J. Biol. Chem. , vol.256 , pp. 7146-7149
    • Kaibuchi, K.1    Takai, Y.2    Nishizuka, Y.3
  • 31
    • 0026779291 scopus 로고
    • Differential irreversible insertion of protein kinase C into phospholipid vesicles by phorbol esters and related activators
    • Kazanietz, M.G., Krausz, K.W. and Blumberg, P.M. (1992) Differential irreversible insertion of protein kinase C into phospholipid vesicles by phorbol esters and related activators. J. Biol. Chem. 267, 20878-20886.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20878-20886
    • Kazanietz, M.G.1    Krausz, K.W.2    Blumberg, P.M.3
  • 32
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with non-lamellar tendency of bilayer phospholipids
    • Keller, S.L., Bezrukov, S.M., Gruner, S.M., Tate, M.W., Vodyanoy, I. and Parsegian, V.A. (1993) Probability of alamethicin conductance states varies with non-lamellar tendency of bilayer phospholipids. Biophys. J. 65, 23-27.
    • (1993) Biophys. J. , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 33
    • 0021824442 scopus 로고
    • Dissociation of protein kinase C activation from phorbol ester-induced maturation of HL-60 leukemia cells
    • Kreutter, D., Caldwell, A.B. and Morin, M.J. (1985) Dissociation of protein kinase C activation from phorbol ester-induced maturation of HL-60 leukemia cells. J. Biol. Chem. 260, 5979-5984.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5979-5984
    • Kreutter, D.1    Caldwell, A.B.2    Morin, M.J.3
  • 34
  • 35
    • 0020107384 scopus 로고
    • Measurement of the lateral compressibility of several phospholipid bilayers
    • Lis, L.J., McAlister, M., Fuller, N., Rand, R.P. and Parsegian, V.A. (1982) Measurement of the lateral compressibility of several phospholipid bilayers. Biophys. J. 37, 667-672.
    • (1982) Biophys. J. , vol.37 , pp. 667-672
    • Lis, L.J.1    McAlister, M.2    Fuller, N.3    Rand, R.P.4    Parsegian, V.A.5
  • 36
    • 0022309995 scopus 로고
    • The nature of the site of general anesthesia
    • Miller, K.W. (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
  • 37
    • 0023664913 scopus 로고
    • Disparate effects of activation of protein kinase C on HL-60 promylocytic leukemia cell differentiation
    • Morin, M.J., Kreutter, D., Rasmussen, H. and Sartorelli, A.C. (1987) Disparate effects of activation of protein kinase C on HL-60 promylocytic leukemia cell differentiation. J. Biol. Chem. 262, 11758-11763.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11758-11763
    • Morin, M.J.1    Kreutter, D.2    Rasmussen, H.3    Sartorelli, A.C.4
  • 38
    • 0029921355 scopus 로고    scopus 로고
    • Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: Evidence for a lack of a specific binding site for phosphatidylserine
    • Mosior, M., Golini, E. and Epand, R.M. (1996) Chemical specificity and physical properties of the lipid bilayer in the regulation of protein kinase C by anionic phospholipids: evidence for a lack of a specific binding site for phosphatidylserine. Proc. Natl. Acad. Sci. USA 93, 1907-1912.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1907-1912
    • Mosior, M.1    Golini, E.2    Epand, R.M.3
  • 39
    • 0027470669 scopus 로고
    • Mechanism of activation of protein kinase C: Roles of diolein and phosphatidylserine
    • Mosior, M. and Epand, R.M. (1993) Mechanism of activation of protein kinase C: roles of diolein and phosphatidylserine. Biochemistry 32, 66-75.
    • (1993) Biochemistry , vol.32 , pp. 66-75
    • Mosior, M.1    Epand, R.M.2
  • 40
    • 0028811653 scopus 로고    scopus 로고
    • Protein kinase C: Structure function and regulation
    • Newton, A.C. (1996) Protein kinase C: structure function and regulation. J. Biol. Chem. 48, 28495-28498.
    • (1996) J. Biol. Chem. , vol.48 , pp. 28495-28498
    • Newton, A.C.1
  • 41
    • 0028341564 scopus 로고
    • Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes
    • Newton, A.C. and Keranen, L.M. (1994) Phosphatidyl-L-serine is necessary for protein kinase C's high-affinity interaction with diacylglycerol-containing membranes. Biochemistry 33, 6651-6658.
    • (1994) Biochemistry , vol.33 , pp. 6651-6658
    • Newton, A.C.1    Keranen, L.M.2
  • 42
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka, Y. (1995) Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 9, 484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 44
    • 0026741799 scopus 로고
    • Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol
    • Orr, J.W., Keranen, L.M. and Newton, A.C. (1992) Reversible exposure of the pseudosubstrate domain of protein kinase C by phosphatidylserine and diacylglycerol. J. Biol. Chem. 267, 15263-15266.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15263-15266
    • Orr, J.W.1    Keranen, L.M.2    Newton, A.C.3
  • 45
    • 0026635971 scopus 로고
    • Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation
    • Orr, J.W. and Newton, A.C. (1992) Interaction of protein kinase C with phosphatidylserine. 2. Specificity and regulation. Biochemistry 31, 4667-4673.
    • (1992) Biochemistry , vol.31 , pp. 4667-4673
    • Orr, J.W.1    Newton, A.C.2
  • 46
    • 0026682675 scopus 로고
    • Interaction of protein kinase C with phosphatidylserine. 1. Co-operativity in lipid binding
    • Orr, J.W. and Newton, A.C. (1992) Interaction of protein kinase C with phosphatidylserine. 1. Co-operativity in lipid binding. Biochemistry 31, 4661-4667.
    • (1992) Biochemistry , vol.31 , pp. 4661-4667
    • Orr, J.W.1    Newton, A.C.2
  • 47
    • 0025198526 scopus 로고
    • Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation
    • Pears, C.J., Kour, G., House, C., Kemp, B.E. and Parker, P.J. (1990) Mutagenesis of the pseudosubstrate site of protein kinase C leads to activation. Eur. J. Biochem. 194, 89-94.
    • (1990) Eur. J. Biochem. , vol.194 , pp. 89-94
    • Pears, C.J.1    Kour, G.2    House, C.3    Kemp, B.E.4    Parker, P.J.5
  • 48
    • 0028030740 scopus 로고
    • A phorbol ester binding domain of protein kinase C γ
    • Quest, A.F.G., Bardes, E.S.G. and Bell, R.M. (1994) A phorbol ester binding domain of protein kinase C γ. J. Biol. Chem. 269, 2953-2960.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2953-2960
    • Quest, A.F.G.1    Bardes, E.S.G.2    Bell, R.M.3
  • 49
    • 0028021161 scopus 로고
    • The regulatory region of protein kinase C γ
    • Quest, A.F.G. and Bell, R.M. (1994) The regulatory region of protein kinase C γ. J. Biol. Chem. 269, 20000-20012.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20000-20012
    • Quest, A.F.G.1    Bell, R.M.2
  • 50
    • 0027323946 scopus 로고
    • Sensitivity of phospholipase C (Bacillus cereus) activity to lipid packing in sonicated lipid mixtures
    • Rao, N.M. and Sundaram, C.S. (1993) Sensitivity of phospholipase C (Bacillus cereus) activity to lipid packing in sonicated lipid mixtures. Biochemistry 32, 8547-8552.
    • (1993) Biochemistry , vol.32 , pp. 8547-8552
    • Rao, N.M.1    Sundaram, C.S.2
  • 51
    • 0027179178 scopus 로고
    • Role of membrane defects in the regulation of the activity of protein kinase C
    • Senisterra, G. and Epand, R.M. (1993) Role of membrane defects in the regulation of the activity of protein kinase C. Arch. Biochem. Biophys. 300, 378-383.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 378-383
    • Senisterra, G.1    Epand, R.M.2
  • 52
    • 1842394775 scopus 로고
    • Competitive inhibition by diacylglycerol of specific phorbol ester binding
    • Sharkey, N.A., Leach, K.L. and Blumberg, P.M. (1984) Competitive inhibition by diacylglycerol of specific phorbol ester binding. Proc. Natl. Acad. Sci. USA 81, 607-610.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 607-610
    • Sharkey, N.A.1    Leach, K.L.2    Blumberg, P.M.3
  • 53
    • 0029670030 scopus 로고    scopus 로고
    • Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities
    • Slater, S.J., Ho, C., Kelly, M.B., Larkin, J.D., Taddeo, F.J., Yeager, M.D. and Stubbs, C. (1996a) Protein kinase Cα contains two activator binding sites that bind phorbol esters and diacylglycerols with opposite affinities. J. Biol. Chem. 271, 4627-4631.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4627-4631
    • Slater, S.J.1    Ho, C.2    Kelly, M.B.3    Larkin, J.D.4    Taddeo, F.J.5    Yeager, M.D.6    Stubbs, C.7
  • 54
    • 0029915868 scopus 로고    scopus 로고
    • Polyunsaturation in cell membranes and lipid bilayers and its effects on membrane proteins
    • Slater, S.J., Kelly, M.B., Yeager, M.D., Larkin, J., Ho, C. and Stubbs, C.D. (1996b) Polyunsaturation in cell membranes and lipid bilayers and its effects on membrane proteins. Lipids 31, S-189-S-192.
    • (1996) Lipids , vol.31
    • Slater, S.J.1    Kelly, M.B.2    Yeager, M.D.3    Larkin, J.4    Ho, C.5    Stubbs, C.D.6
  • 56
    • 0028075333 scopus 로고
    • The modulation of protein kinase C activity by membrane lipid bilayer structure
    • Slater, S.J., Kelly, M.B., Taddeo, F.J., Ho, C., Rubin, E. and Stubbs, C.D. (1994a) The modulation of protein kinase C activity by membrane lipid bilayer structure. J. Biol. Chem. 269, 4866-4871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4866-4871
    • Slater, S.J.1    Kelly, M.B.2    Taddeo, F.J.3    Ho, C.4    Rubin, E.5    Stubbs, C.D.6
  • 57
    • 0028238355 scopus 로고
    • Evidence for discrete diacylglycerol and phorbol ester binding sites on protein kinase C
    • Slater, S.J., Kelly, M.B., Taddeo, F.J., Rubin, E. and Stubbs, C.D. (1994b) Evidence for discrete diacylglycerol and phorbol ester binding sites on protein kinase C. J. Biol. Chem. 269, 17160-17165.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17160-17165
    • Slater, S.J.1    Kelly, M.B.2    Taddeo, F.J.3    Rubin, E.4    Stubbs, C.D.5
  • 58
    • 0027207081 scopus 로고
    • Contribution of hydrogen bonding to lipid-lipid interactions in membranes and the role of lipid order: Effects of cholesterol, increased phospholipid unsaturation, and ethanol
    • Slater, S.J., Ho, C., Taddeo, F.J., Kelly, M.B. and Stubbs, C.D. (1993) Contribution of hydrogen bonding to lipid-lipid interactions in membranes and the role of lipid order: effects of cholesterol, increased phospholipid unsaturation, and ethanol. Biochemistry 32, 3714-3721.
    • (1993) Biochemistry , vol.32 , pp. 3714-3721
    • Slater, S.J.1    Ho, C.2    Taddeo, F.J.3    Kelly, M.B.4    Stubbs, C.D.5
  • 59
    • 0023795223 scopus 로고
    • The role of hydrophobic interactions in the phospholipid-dependent activation of protein kinase C
    • Snoek, G.T., Feijen, A., Hage, W.J., van Rotterdam, W. and de Laat, S.W. (1988) The role of hydrophobic interactions in the phospholipid-dependent activation of protein kinase C. Biochem. J. 255, 629-637.
    • (1988) Biochem. J. , vol.255 , pp. 629-637
    • Snoek, G.T.1    Feijen, A.2    Hage, W.J.3    Van Rotterdam, W.A.4    De Laat, S.W.5
  • 62
    • 0028037553 scopus 로고
    • The reconstituted mitochondrial adenine nucleotide translocator: Effects of lipid polymorphism
    • Streicher-Scott, J., Lapidus, R. and Sokolove, P.M. (1994) The reconstituted mitochondrial adenine nucleotide translocator: effects of lipid polymorphism. Arch. Biochem. Biophys. 315, 548-554.
    • (1994) Arch. Biochem. Biophys. , vol.315 , pp. 548-554
    • Streicher-Scott, J.1    Lapidus, R.2    Sokolove, P.M.3
  • 63
    • 0019885896 scopus 로고
    • Effect of double bonds on the dynamic properties of the hydrocarbon region of lecithin bilayers
    • Stubbs, C.D., Kouyama, T., Kinosita, K. and Ikegami, A. (1981) Effect of double bonds on the dynamic properties of the hydrocarbon region of lecithin bilayers. Biochemistry 20, 4257-4262.
    • (1981) Biochemistry , vol.20 , pp. 4257-4262
    • Stubbs, C.D.1    Kouyama, T.2    Kinosita, K.3    Ikegami, A.4
  • 64
    • 0027173199 scopus 로고
    • Curvature, order and dynamics of lipid hexagonal phases studied by deuterium NMR spectroscopy
    • Thurmond, R.L., Lindblom, G. and Brown, M.F. (1993) Curvature, order and dynamics of lipid hexagonal phases studied by deuterium NMR spectroscopy. Biochemistry 32, 5394-5410.
    • (1993) Biochemistry , vol.32 , pp. 5394-5410
    • Thurmond, R.L.1    Lindblom, G.2    Brown, M.F.3
  • 65
    • 0021755651 scopus 로고    scopus 로고
    • Cation dependent segregation phenomena and phase behavior in model membrane systems containing phosphatidylserine: Influence of cholesterol and acyl chain composition
    • Tilcock, C.P.S., Bally, M.B., Farren, S.B., Cullis, P.R. and Gruner, S.M. (1996) Cation dependent segregation phenomena and phase behavior in model membrane systems containing phosphatidylserine: influence of cholesterol and acyl chain composition. Biochemistry 23, 2696-2703.
    • (1996) Biochemistry , vol.23 , pp. 2696-2703
    • Tilcock, C.P.S.1    Bally, M.B.2    Farren, S.B.3    Cullis, P.R.4    Gruner, S.M.5
  • 66
    • 0024281308 scopus 로고
    • Calcium induced phase separation phenomena in multicomponent unsaturated lipid mixtures
    • Tilcock, C.P.S., Cullis, P.R. and Gruner, S.M. (1988) Calcium induced phase separation phenomena in multicomponent unsaturated lipid mixtures. Biochemistry 27, 1415-1420.
    • (1988) Biochemistry , vol.27 , pp. 1415-1420
    • Tilcock, C.P.S.1    Cullis, P.R.2    Gruner, S.M.3
  • 69
    • 0024599261 scopus 로고
    • Lipid regulation of cell membrane structure and function
    • Yeagle, P.L. (1989) Lipid regulation of cell membrane structure and function. FASEB J. 3, 1833-1842.
    • (1989) FASEB J. , vol.3 , pp. 1833-1842
    • Yeagle, P.L.1
  • 70
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle, P.L. (1985) Cholesterol and the cell membrane. Biochim. Biophys. Acta 822, 267-287.
    • (1985) Biochim. Biophys. Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 71
    • 0026505747 scopus 로고
    • The mechanism of activation of protein kinase C: A biophysical perspective
    • Zidovetzki, R. and Lester, D.S. (1992) The mechanism of activation of protein kinase C: a biophysical perspective. Biochim. Biophys. Acta 1134, 261-272.
    • (1992) Biochim. Biophys. Acta , vol.1134 , pp. 261-272
    • Zidovetzki, R.1    Lester, D.S.2


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