메뉴 건너뛰기




Volumn 88, Issue 6, 2005, Pages 4084-4094

Membrane fluidity is a key modulator of membrane binding, insertion, and activity of 5-lipoxygenase

Author keywords

[No Author keywords available]

Indexed keywords

1 PALMITOYL 2 ARACHIDONOLYLGLYCERO 2 PHOSPHOCHOLINE; 1 PALMITOYL 2 DOCOSAHEXAENOYLGLYCERO 3 PHOSPHOCHOLINE; 1 PALMITOYL 2 LINOLEOYLGLYCERO 3 PHOSPHOCHOLINE; 2 OLEOYL 1 PALMITOYLPHOSPHATIDYLCHOLINE; ARACHIDONATE 5 LIPOXYGENASE; ARACHIDONIC ACID; CHOLESTEROL; DIPALMITOYLPHOSPHATIDYLCHOLINE; MEMBRANE LIPID; NITROXIDE; PHOSPHOLIPID; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 22244452942     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.056788     Document Type: Article
Times cited : (92)

References (70)
  • 1
    • 0027323992 scopus 로고
    • 5-Lipoxygenase-activating protein stimulates the utilization of arachidonic acid by 5-lipoxygenase
    • Abramovitz, M., E. Wong, M. E. Cox, C. D. Richardson, C. Li, and P. J. Vickers. 1993. 5-lipoxygenase-activating protein stimulates the utilization of arachidonic acid by 5-lipoxygenase. Eur. J. Biochem. 215:105-111.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 105-111
    • Abramovitz, M.1    Wong, E.2    Cox, M.E.3    Richardson, C.D.4    Li, C.5    Vickers, P.J.6
  • 2
    • 0030853562 scopus 로고    scopus 로고
    • Effect of lipid composition on rat liver nuclear membrane fluidity
    • Albi, E., M. L. Tomassoni, and M. Viola-Magni. 1997. Effect of lipid composition on rat liver nuclear membrane fluidity. Cell Biochem. Funct. 3:181-190.
    • (1997) Cell Biochem. Funct. , vol.3 , pp. 181-190
    • Albi, E.1    Tomassoni, M.L.2    Viola-Magni, M.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0029098680 scopus 로고
    • Translocation and leukotriene synthetic capacity of nuclear 5-lipoxygenase in rat basophilic leukemia cells and alveolar macrophages
    • Brock, T. G., R. W. McNish, and M. Peters-Golden. 1995. Translocation and leukotriene synthetic capacity of nuclear 5-lipoxygenase in rat basophilic leukemia cells and alveolar macrophages. J. Biol. Chem. 270: 21652-21658.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21652-21658
    • Brock, T.G.1    McNish, R.W.2    Peters-Golden, M.3
  • 6
    • 0023746627 scopus 로고
    • Arachidonate released upon agonist stimulation preferentially originates from arachidonate most recently incorporated into nuclear membrane phospholipids
    • Capriotti, A. M., E. E. Furth, M. E. Arrasmith, and M. Laposata. 1988. Arachidonate released upon agonist stimulation preferentially originates from arachidonate most recently incorporated into nuclear membrane phospholipids. J. Biol. Chem. 263:10029-10034.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10029-10034
    • Capriotti, A.M.1    Furth, E.E.2    Arrasmith, M.E.3    Laposata, M.4
  • 7
    • 0025788404 scopus 로고
    • How membrane chain-melting phase-transition temperature is affected by the lipid chain asymmetry and degree of unsaturation: An effective chain-length model
    • Cevc, G. 1991. How membrane chain-melting phase-transition temperature is affected by the lipid chain asymmetry and degree of unsaturation: an effective chain-length model. Biochemistry. 30:7186-7193.
    • (1991) Biochemistry , vol.30 , pp. 7186-7193
    • Cevc, G.1
  • 8
    • 0035808471 scopus 로고    scopus 로고
    • The N-terminal "β-barrel" domain of 5-lipoxygenase is essential for nuclear membrane translocation
    • Chen, X.-S., and C. D. Funk. 2001. The N-terminal "β- barrel" domain of 5-lipoxygenase is essential for nuclear membrane translocation. J. Biol. Chem. 276:811-818.
    • (2001) J. Biol. Chem. , vol.276 , pp. 811-818
    • Chen, X.-S.1    Funk, C.D.2
  • 9
    • 0043095584 scopus 로고    scopus 로고
    • Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin
    • Chen, X., N. Li, S. Wang, N. Wu, J. Hong, X. Jiao, M. J. Krasna, D. G. Beer, and C. S. Yang. 2003. Leukotriene A4 hydrolase in rat and human esophageal adenocarcinomas and inhibitory effects of bestatin. J. Natl. Cancer Inst. 95:1053-1061.
    • (2003) J. Natl. Cancer Inst. , vol.95 , pp. 1053-1061
    • Chen, X.1    Li, N.2    Wang, S.3    Wu, N.4    Hong, J.5    Jiao, X.6    Krasna, M.J.7    Beer, D.G.8    Yang, C.S.9
  • 10
    • 0034307059 scopus 로고    scopus 로고
    • Lipid-protein interactions in rat renal subcellular membranes: A biophysical and biochemical study
    • D'Antuono, C., M. C. Fernandez-Tome, N. Sterin-Speziale, and D. L. Bernik. 2000. Lipid-protein interactions in rat renal subcellular membranes: a biophysical and biochemical study. Arch. Biochem. Biophys. 382:39-47.
    • (2000) Arch. Biochem. Biophys. , vol.382 , pp. 39-47
    • D'Antuono, C.1    Fernandez-Tome, M.C.2    Sterin-Speziale, N.3    Bernik, D.L.4
  • 11
    • 0141642121 scopus 로고    scopus 로고
    • Sphingomyelin/ phosphatidylcholine/cholesterol phase diagram: Boundaries and composition of lipid rafts
    • de Almeida, R. F., A. Fedorov, and M. Prieto. 2003. Sphingomyelin/ phosphatidylcholine/cholesterol phase diagram: boundaries and composition of lipid rafts. Biophys. J. 85:2406-2416.
    • (2003) Biophys. J. , vol.85 , pp. 2406-2416
    • Almeida, R.F.1    Fedorov, A.2    Prieto, M.3
  • 12
    • 0033594398 scopus 로고    scopus 로고
    • Nuclei contain two differentially regulated pools of diacylglycerol
    • D'Santos, C. S., J. H. Clarke, R. F. Irvine, and N. Divecha. 1999. Nuclei contain two differentially regulated pools of diacylglycerol. Curr. Biol. 9:437-440.
    • (1999) Curr. Biol. , vol.9 , pp. 437-440
    • D'Santos, C.S.1    Clarke, J.H.2    Irvine, R.F.3    Divecha, N.4
  • 14
  • 15
    • 0037435606 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling
    • Frazier, A. A., C. R. Roller, J. J. Havelka, A. Hinderliter, and D. S. Cafiso. 2003. Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling. Biochemistry. 42:96-105.
    • (2003) Biochemistry , vol.42 , pp. 96-105
    • Frazier, A.A.1    Roller, C.R.2    Havelka, J.J.3    Hinderliter, A.4    Cafiso, D.S.5
  • 16
    • 0034465463 scopus 로고    scopus 로고
    • Central role of arachidonate 5-lipoxygenase in the regulation of cell growth and apoptosis in human prostate cancer cells
    • Ghosh, J., and C. E. Myers. 1999. Central role of arachidonate 5-lipoxygenase in the regulation of cell growth and apoptosis in human prostate cancer cells. Adv. Exp. Med. Biol. 469:577-582.
    • (1999) Adv. Exp. Med. Biol. , vol.469 , pp. 577-582
    • Ghosh, J.1    Myers, C.E.2
  • 17
    • 0030736867 scopus 로고    scopus 로고
    • The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity
    • Gillmor, S. A., A. Villaseñor, R. Fletterick, E. Sigal, and M. F. Browner. 1997. The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity. Nat. Struct. Biol. 4:1003-1009.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 1003-1009
    • Gillmor, S.A.1    Villaseñor, A.2    Fletterick, R.3    Sigal, E.4    Browner, M.F.5
  • 18
    • 0142092620 scopus 로고    scopus 로고
    • Leukotriene B4 and BLT1 control cytotoxic effector T cell recruitment to inflamed tissues
    • Goodarzi, K., M. Goodarzi, A. M. Tager, A. D. Luster, and U. H. von Andrian. 2003. Leukotriene B4 and BLT1 control cytotoxic effector T cell recruitment to inflamed tissues. Nat. Immunol. 4:965-973.
    • (2003) Nat. Immunol. , vol.4 , pp. 965-973
    • Goodarzi, K.1    Goodarzi, M.2    Tager, A.M.3    Luster, A.D.4    Von Andrian, U.H.5
  • 19
    • 0034624019 scopus 로고    scopus 로고
    • The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity
    • Hammarberg, T., P. Provost, B. Persson, and O. Rådmark. 2000. The N-terminal domain of 5-lipoxygenase binds calcium and mediates calcium stimulation of enzyme activity. J. Biol. Chem. 275:38787-38793.
    • (2000) J. Biol. Chem. , vol.275 , pp. 38787-38793
    • Hammarberg, T.1    Provost, P.2    Persson, B.3    Rådmark, O.4
  • 21
    • 0037144117 scopus 로고    scopus 로고
    • Use of laurdan fluorescence intensity and polarization to distinguish between changes in membrane fluidity and phospholipid order
    • Harris, F. M., K. B. Best, and J. D. Bell. 2002. Use of laurdan fluorescence intensity and polarization to distinguish between changes in membrane fluidity and phospholipid order. Biochim. Biophys. Acta. 1565:123-128.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 123-128
    • Harris, F.M.1    Best, K.B.2    Bell, J.D.3
  • 22
    • 0023647347 scopus 로고
    • The influence of unsaturation on the phase transition temperatures of a series of heteroacid phosphatidylcholines containing twenty-carbon chains
    • Keough, K. M., B. Giffin, and N. Kariel. 1987. The influence of unsaturation on the phase transition temperatures of a series of heteroacid phosphatidylcholines containing twenty-carbon chains. Biochim. Biophys. Acta. 902:1-10.
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 1-10
    • Keough, K.M.1    Giffin, B.2    Kariel, N.3
  • 23
    • 0015240308 scopus 로고
    • The fatty acid composition of individual phospholipids from rat liver nuclear membrane and nuclei
    • Khandwala, A. S., and C. B. Kasper. 1971. The fatty acid composition of individual phospholipids from rat liver nuclear membrane and nuclei. J. Biol. Chem. 246:6242-6246.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6242-6246
    • Khandwala, A.S.1    Kasper, C.B.2
  • 24
    • 0347298574 scopus 로고    scopus 로고
    • C2 domain of protein kinase Ca: Elucidation of the membrane docking surface by site-directed fluorescence and spin labeling
    • Kohout, S. C., S. Corbalan-Garcia, J. C. Gomez-Fernandez, and J. J. Falke. 2003. C2 domain of protein kinase Ca: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry. 42:1254-1265.
    • (2003) Biochemistry , vol.42 , pp. 1254-1265
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Falke, J.J.4
  • 26
    • 0037066761 scopus 로고    scopus 로고
    • Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase
    • Kulkarni, S., S. Das, C. D. Funk, D. Murray, and W. Cho. 2002. Molecular basis of the specific subcellular localization of the C2-like domain of 5-lipoxygenase. J. Biol. Chem. 277:13167-13174.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13167-13174
    • Kulkarni, S.1    Das, S.2    Funk, C.D.3    Murray, D.4    Cho, W.5
  • 28
    • 0032491210 scopus 로고    scopus 로고
    • 2 is necessary for its interfacial catalysis and arachidonate specificity
    • 2 is necessary for its interfacial catalysis and arachidonate specificity. Biochemistry. 37:14128-14136.
    • (1998) Biochemistry , vol.37 , pp. 14128-14136
    • Lichtenbergova, L.1    Yoon, E.T.2    Cho, W.3
  • 29
    • 0026018961 scopus 로고
    • Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellar phosphatidylcholine dispersions
    • Litman, B. J., E. N. Lewis, and I. W. Levin. 1991. Packing characteristics of highly unsaturated bilayer lipids: Raman spectroscopic studies of multilamellar phosphatidylcholine dispersions. Biochemistry. 30:313-319.
    • (1991) Biochemistry , vol.30 , pp. 313-319
    • Litman, B.J.1    Lewis, E.N.2    Levin, I.W.3
  • 30
    • 0027419575 scopus 로고
    • Reversible translocation of 5-lipoxygenase in mast cells upon IgE/antigen stimulation
    • Malaviya, R., R. Malaviya, and B. A. Jakschik. 1993. Reversible translocation of 5-lipoxygenase in mast cells upon IgE/antigen stimulation. J. Biol Chem. 268:4939-4944.
    • (1993) J. Biol Chem. , vol.268 , pp. 4939-4944
    • Malaviya, R.1    Malaviya, R.2    Jakschik, B.A.3
  • 31
    • 0242401834 scopus 로고    scopus 로고
    • 2 C2 domain: Detailed structural analysis of the protein-membrane interface via site-directed spin-labeling
    • 2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling. Biochemistry. 42:13227-13240.
    • (2003) Biochemistry , vol.42 , pp. 13227-13240
    • Malmberg, N.J.1    Van Buskirk, D.R.2    Falke, J.J.3
  • 32
    • 0034067897 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin H synthase-2 in a human amnion cell line: Implications for nuclear localized prostaglandin signaling pathways
    • Marvin, K. W., R. L. Eykholt, and M. D. Mitchell. 2000. Subcellular localization of prostaglandin H synthase-2 in a human amnion cell line: implications for nuclear localized prostaglandin signaling pathways. Prostaglandins Leukot. Essent. Fatty Acids. 62:7-11.
    • (2000) Prostaglandins Leukot. Essent. Fatty Acids , vol.62 , pp. 7-11
    • Marvin, K.W.1    Eykholt, R.L.2    Mitchell, M.D.3
  • 34
    • 0023111150 scopus 로고
    • Determination of the depth of bromine atoms in bilayers formed from bromolipid probes
    • McIntosh, T. J., and P. W. Holloway. 1987. Determination of the depth of bromine atoms in bilayers formed from bromolipid probes. Biochemistry. 26:1783-1788.
    • (1987) Biochemistry , vol.26 , pp. 1783-1788
    • McIntosh, T.J.1    Holloway, P.W.2
  • 35
    • 0028783935 scopus 로고
    • 2 and sphingomyelinase activities in rat liver nuclear membrane and matrix
    • 2 and sphingomyelinase activities in rat liver nuclear membrane and matrix. Int. J. Biochem. Cell Biol. 27:995-1001.
    • (1995) Int. J. Biochem. Cell Biol. , vol.27 , pp. 995-1001
    • Neitcheva, T.1    Peeva, D.2
  • 36
    • 0022415541 scopus 로고
    • 3H]arachidonic acid in murine fibrosarcoma cells measured by electron microscope autoradiography
    • 3H]arachidonic acid in murine fibrosarcoma cells measured by electron microscope autoradiography. J. Cell Biol. 101:573-581.
    • (1985) J. Cell Biol. , vol.101 , pp. 573-581
    • Neufeld, E.J.1    Majerus, P.W.2    Krueger, C.M.3    Saffitz, J.E.4
  • 37
    • 0028572490 scopus 로고
    • Human 5-lipoxygenase associates with phosphatidylcholine liposomes and modulates LTA4 synthetase activity
    • Noguchi, M., M. Miyano, T. Matsumoto, and M. Noma. 1994. Human 5-lipoxygenase associates with phosphatidylcholine liposomes and modulates LTA4 synthetase activity. Biochim. Biophys. Acta. 1215:300-306.
    • (1994) Biochim. Biophys. Acta , vol.1215 , pp. 300-306
    • Noguchi, M.1    Miyano, M.2    Matsumoto, T.3    Noma, M.4
  • 38
    • 0037304544 scopus 로고    scopus 로고
    • Properties of palmitoyl phosphacidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules
    • Nyholm, T., M. Nylund, A. Soderholm, and J. P. Slotte. 2003. Properties of palmitoyl phosphacidylcholine, sphingomyelin, and dihydrosphingomyelin bilayer membranes as reported by different fluorescent reporter molecules. Biophys. J. 84:987-997.
    • (2003) Biophys. J. , vol.84 , pp. 987-997
    • Nyholm, T.1    Nylund, M.2    Soderholm, A.3    Slotte, J.P.4
  • 39
    • 8744267513 scopus 로고    scopus 로고
    • Modulation of human 5-lipoxygenase activity by membrane lipids
    • Pande, A. H., D. Moe, K. N. Nemec, S. Qin, S. Tan, and S. A. Tatulian. 2004. Modulation of human 5-lipoxygenase activity by membrane lipids. Biochemistry. 43:14653-14666.
    • (2004) Biochemistry , vol.43 , pp. 14653-14666
    • Pande, A.H.1    Moe, D.2    Nemec, K.N.3    Qin, S.4    Tan, S.5    Tatulian, S.A.6
  • 40
    • 0027957293 scopus 로고
    • Influence of cholesterol on phospholipid bilayers phase domains as detected by Laurdan fluorescence
    • Parasassi, T., M. Di Stefano, M. Loiero, G. Ravagnan, and E. Gratton. 1994. Influence of cholesterol on phospholipid bilayers phase domains as detected by Laurdan fluorescence. Biophys. J. 66:120-132.
    • (1994) Biophys. J. , vol.66 , pp. 120-132
    • Parasassi, T.1    Di Stefano, M.2    Loiero, M.3    Ravagnan, G.4    Gratton, E.5
  • 41
    • 0025883217 scopus 로고
    • Human 5-lipoxygenase contains an essential iron
    • Percival, M. D. 1991. Human 5-lipoxygenase contains an essential iron. J. Biol. Chem. 266:10058-10061.
    • (1991) J. Biol. Chem. , vol.266 , pp. 10058-10061
    • Percival, M.D.1
  • 42
    • 0042122498 scopus 로고    scopus 로고
    • 5-Lipoxygenase and FLAP. Prostaglandins Leukot
    • Peters-Golden, M., and T. G. Brock. 2003. 5-lipoxygenase and FLAP. Prostaglandins Leukot. Essent. Fatty Acids. 69:99-109.
    • (2003) Essent. Fatty Acids , vol.69 , pp. 99-109
    • Peters-Golden, M.1    Brock, T.G.2
  • 43
    • 0028301140 scopus 로고
    • Prostaglandin H synthase: Implications for membrane structure
    • Picot, D., and R. M. Garavito. 1994. Prostaglandin H synthase: implications for membrane structure. FEBS Lett. 346:21-25.
    • (1994) FEBS Lett. , vol.346 , pp. 21-25
    • Picot, D.1    Garavito, R.M.2
  • 44
    • 0031430230 scopus 로고    scopus 로고
    • X-ray crystallographic study of the structure of prostaglandin H synthase
    • Picot, D., P. J. Loll, and R. M. Garavito. 1997. X-ray crystallographic study of the structure of prostaglandin H synthase. Adv. Exp. Med. Biol. 400A: 107-111.
    • (1997) Adv. Exp. Med. Biol. , vol.400 A , pp. 107-111
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 47
    • 7044269246 scopus 로고    scopus 로고
    • 2 determines productive-mode orientation of the enzyme at the membrane surface
    • 2 determines productive-mode orientation of the enzyme at the membrane surface. J. Mol. Biol. 344:71-89.
    • (2004) J. Mol. Biol. , vol.344 , pp. 71-89
    • Qin, S.1    Pande, A.H.2    Nemec, K.N.3    Tatulian, S.A.4
  • 48
    • 0242357690 scopus 로고    scopus 로고
    • The molecular biology and regulation of 5-lipoxygenase
    • Radmark, O. P. 2000. The molecular biology and regulation of 5-lipoxygenase. Am. J. Respir. Crit. Care Med. 161:S11-S15.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161
    • Radmark, O.P.1
  • 49
    • 0034700934 scopus 로고    scopus 로고
    • 2+ activates 5-lipoxygenase in vitro: Dependency on concentrations of phosphatidyl-choline and arachidonic acid
    • 2+ activates 5-lipoxygenase in vitro: dependency on concentrations of phosphatidyl-choline and arachidonic acid. Biochemistry. 39:1840-1848.
    • (2000) Biochemistry , vol.39 , pp. 1840-1848
    • Reddy, K.V.1    Hammarberg, T.2    Radmark, O.3
  • 51
    • 0023803150 scopus 로고
    • Translocation of 5-lipoxygenase to the membrane in human leukocytes challenged with ionophore A23187
    • Rouzer, C. A., and S. Kargman. 1988. Translocation of 5-lipoxygenase to the membrane in human leukocytes challenged with ionophore A23187. J. Biol. Chem. 263:10980-10988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10980-10988
    • Rouzer, C.A.1    Kargman, S.2
  • 52
    • 11844254393 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling
    • Rufener, E., A. A. Frazier, C. M. Wieser, A. Hinderliter, and D. S. Cafiso. 2005. Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling. Biochemistry. 44:18-28.
    • (2005) Biochemistry , vol.44 , pp. 18-28
    • Rufener, E.1    Frazier, A.A.2    Wieser, C.M.3    Hinderliter, A.4    Cafiso, D.S.5
  • 53
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., J. Kopp, N. Guex, and M. C. Peitsch. 2003. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31: 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 54
    • 0032474476 scopus 로고    scopus 로고
    • Calcium is not required for 5-lipoxygenase activity at high phosphatidylcholine vesicle concentrations
    • Skorey, K. I., and M. J. Gresser. 1998. Calcium is not required for 5-lipoxygenase activity at high phosphatidylcholine vesicle concentrations. Biochemistry. 37:8027-8034.
    • (1998) Biochemistry , vol.37 , pp. 8027-8034
    • Skorey, K.I.1    Gresser, M.J.2
  • 55
    • 0032540344 scopus 로고    scopus 로고
    • Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy
    • Spencer, A. G., J. W, Woods, T. Arakawa, I. I. Singer, and W. L. Smith, 1998. Subcellular localization of prostaglandin endoperoxide H synthases-1 and -2 by immunoelectron microscopy. J. Biol. Chem. 273: 9886-9893.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9886-9893
    • Spencer, A.G.1    Woods, J.W.2    Arakawa, T.3    Singer, I.I.4    Smith, W.L.5
  • 56
    • 0142059080 scopus 로고    scopus 로고
    • Docosahexaenoic acid: Membrane properties of a unique fatty acid
    • Stillwell, W., and S. R. Wassall. 2003. Docosahexaenoic acid: membrane properties of a unique fatty acid. Chem. Phys. Lipids. 126:1-27.
    • (2003) Chem. Phys. Lipids , vol.126 , pp. 1-27
    • Stillwell, W.1    Wassall, S.R.2
  • 57
    • 0019885896 scopus 로고
    • Effect of double bonds on the dynamic properties of the hydrocarbon region of lecithin bilayers
    • Stubbs, C. D., T. Kouyama, K. Kinosita, and A. Ikegami. 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
  • 58
    • 0032032450 scopus 로고    scopus 로고
    • The distribution and metabolism of arachidonate-containing phospholipids in cellular nuclei
    • Surette, M. E., and F. H. Chilton. 1998. The distribution and metabolism of arachidonate-containing phospholipids in cellular nuclei. Biochem. J. 330:915-921.
    • (1998) Biochem. J. , vol.330 , pp. 915-921
    • Surette, M.E.1    Chilton, F.H.2
  • 59
    • 0032480811 scopus 로고    scopus 로고
    • Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1
    • Tatulian, S. A., J. Steczko, and W. Minor. 1998. Uncovering a calcium-regulated membrane-binding mechanism for soybean lipoxygenase-1. Biochemistry. 37:15481-15490.
    • (1998) Biochemistry , vol.37 , pp. 15481-15490
    • Tatulian, S.A.1    Steczko, J.2    Minor, W.3
  • 60
    • 33748701459 scopus 로고    scopus 로고
    • Thermal unbinding of highly oriented phospholipid membranes
    • Vogel, M., C. Münster, W. Fenzl. and T. Salditt. 2000. Thermal unbinding of highly oriented phospholipid membranes. Phys. Rev. Lett. 84:390-393.
    • (2000) Phys. Rev. Lett. , vol.84 , pp. 390-393
    • Vogel, M.1    Münster, C.2    Fenzl, W.3    Salditt, T.4
  • 61
    • 0037178834 scopus 로고    scopus 로고
    • The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding
    • Walther, M., M. Anton, M. Wiedmann, R. Fletterick, and H. Kühn. 2002. The N-terminal domain of the reticulocyte-type 15-lipoxygenase is not essential for enzymatic activity but contains determinants for membrane binding. J. Biol. Chem. 277:27360-27366.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27360-27366
    • Walther, M.1    Anton, M.2    Wiedmann, M.3    Fletterick, R.4    Kühn, H.5
  • 62
    • 0942276361 scopus 로고    scopus 로고
    • Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic role of surface-exposed hydrophobic amino acids and calcium
    • Walther, M., R. Wiesner, and H. Kühn. 2004. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. Mechanistic role of surface-exposed hydrophobic amino acids and calcium. J. Biol. Chem. 279:3717-3725.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3717-3725
    • Walther, M.1    Wiesner, R.2    Kühn, H.3
  • 63
    • 0036464591 scopus 로고    scopus 로고
    • Activation of 5-lipoxygenase by cell stress is calcium independent in human polymorphonuclear leukocytes
    • Werz, O., E. Bürkert, B. Samuelsson, O. Rådmark, and D. Steinhilber. 2002. Activation of 5-lipoxygenase by cell stress is calcium independent in human polymorphonuclear leukocytes. Blood. 99:1044-1052.
    • (2002) Blood , vol.99 , pp. 1044-1052
    • Werz, O.1    Bürkert, E.2    Samuelsson, B.3    Rådmark, O.4    Steinhilber, D.5
  • 64
    • 0034625136 scopus 로고    scopus 로고
    • 5-Lipoxygenase is phosphorylated by p38 kinase-dependent MAPKAP kinases
    • Werz, O., J. Klemm, B. Samuelsson, and O. Rådmark. 2000. 5-lipoxygenase is phosphorylated by p38 kinase-dependent MAPKAP kinases. Proc. Natl. Acad. Sci. USA. 97:5261-5266.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5261-5266
    • Werz, O.1    Klemm, J.2    Samuelsson, B.3    Rådmark, O.4
  • 65
    • 0026014460 scopus 로고
    • Influx of extracellular calcium is required for the membrane translocation of 5-lipoxygenase and leukotriene synthesis
    • Wong, A., M. N. Cook, J. J. Foley, H. M. Sarau, P. Marshall, and S. M. Hwang. 1991. Influx of extracellular calcium is required for the membrane translocation of 5-lipoxygenase and leukotriene synthesis. Biochemistry. 30:9346-9354.
    • (1991) Biochemistry , vol.30 , pp. 9346-9354
    • Wong, A.1    Cook, M.N.2    Foley, J.J.3    Sarau, H.M.4    Marshall, P.5    Hwang, S.M.6
  • 66
  • 67
    • 0028937635 scopus 로고
    • 5-Lipoxygenase is located in the euchromatin of the nucleus in resting human alveolar macrophages and translocates to the nuclear envelope upon cell activation
    • Woods, J. W., M. J, Coffey, T. G. Brock, I. I. Singer, and M. Peters-Golden. 1995. 5-Lipoxygenase is located in the euchromatin of the nucleus in resting human alveolar macrophages and translocates to the nuclear envelope upon cell activation. J. Clin. Invest. 95:2035-2046.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2035-2046
    • Woods, J.W.1    Coffey, M.J.2    Brock, T.G.3    Singer, I.I.4    Peters-Golden, M.5
  • 68
    • 0032552880 scopus 로고    scopus 로고
    • The preference of tryptophan for membrane interfaces
    • Yau, W.-M., W. C. Wimley, K. Gawrisch, and S. H. White. 1998. The preference of tryptophan for membrane interfaces. Biochemistry. 37: 14713-14718.
    • (1998) Biochemistry , vol.37 , pp. 14713-14718
    • Yau, W.-M.1    Wimley, W.C.2    Gawrisch, K.3    White, S.H.4
  • 69
    • 0030048608 scopus 로고    scopus 로고
    • Fluorescence generalized polarization of cell membranes: A two-photon scanning microscopy approach
    • Yu, W., P. T. So, T. French, and E. Gratton. 1996. Fluorescence generalized polarization of cell membranes: a two-photon scanning microscopy approach. Biophys. J. 70:626-636.
    • (1996) Biophys. J. , vol.70 , pp. 626-636
    • Yu, W.1    So, P.T.2    French, T.3    Gratton, E.4
  • 70
    • 0026567751 scopus 로고
    • Mutagenesis of some conserved residues in human 5-lipoxygenase: Effects on enzyme activity
    • Zhang, Y. Y., O. Rådmark, and B. Samuelsson. 1992. Mutagenesis of some conserved residues in human 5-lipoxygenase: effects on enzyme activity. Proc. Natl. Acad. Sci. USA. 89:485-489.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 485-489
    • Zhang, Y.Y.1    Rådmark, O.2    Samuelsson, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.