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Volumn 35, Issue 4-5, 1999, Pages 237-250

Structure of COX-1 and COX-2 enzymes and their interaction with inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

5 (4 FLUOROPHENYL) 1 [(4 METHYLSULFONYL)PHENYL] 3 TRIFLUOROMETHYLPYRAZOLE; 5 BROMO 2 (4 FLUOROPHENYL) 3 (4 METHYLSULFONYLPHENYL)THIOPHENE; 6 (2,4 DIFLUOROPHENYLTHIO) 5 METHANESULFONAMIDO 1 INDANONE; CELECOXIB; CYCLOOXYGENASE 1; CYCLOOXYGENASE 1 INHIBITOR; CYCLOOXYGENASE 2; CYCLOOXYGENASE 2 INHIBITOR; IBUPROFEN; INDOMETACIN; N (2 CYCLOHEXYLOXY 4 NITROPHENYL)METHANESULFONAMIDE; NIMESULIDE; RS 5706700; SULFONAMIDE; SULFONE; UNCLASSIFIED DRUG;

EID: 0032788120     PISSN: 16993993     EISSN: 16994019     Source Type: Journal    
DOI: 10.1358/dot.1999.35.4-5.552200     Document Type: Conference Paper
Times cited : (23)

References (70)
  • 1
  • 2
    • 0030049390 scopus 로고    scopus 로고
    • Prostaglandin synthase 2
    • Herschman, H.R. Prostaglandin synthase 2. Biochem Biophys Acta 1996, 1299: 125-40.
    • (1996) Biochem Biophys Acta , vol.1299 , pp. 125-140
    • Herschman, H.R.1
  • 3
    • 0029904828 scopus 로고    scopus 로고
    • Cyclooxygenase-2 and its regulation in inflammation
    • Bakhle, Y.S., Botting, R.M. Cyclooxygenase-2 and its regulation in inflammation. Med Inflamm 1996, 5: 305-23.
    • (1996) Med Inflamm , vol.5 , pp. 305-323
    • Bakhle, Y.S.1    Botting, R.M.2
  • 4
    • 0029983843 scopus 로고    scopus 로고
    • Constitutive cyclooxygenase (COX-1) and inducible cyclooxygenase (COX-2): Rationale for selective inhibition and progress to date
    • Griswold, D.E., Adams, J.L. Constitutive cyclooxygenase (COX-1) and inducible cyclooxygenase (COX-2): rationale for selective inhibition and progress to date. Med Res Rev 1996, 16: 181-206.
    • (1996) Med Res Rev , vol.16 , pp. 181-206
    • Griswold, D.E.1    Adams, J.L.2
  • 5
    • 0030911815 scopus 로고    scopus 로고
    • Cyclooxygenase isoenzymes. How recent findings affect thinking about non-steroidal anti-inflammatory drugs
    • Jouzeau, J.-Y., Terlain, B., Abid, A., Nedelec, E., Netter, P. Cyclooxygenase isoenzymes. How recent findings affect thinking about non-steroidal anti-inflammatory drugs. Drugs 1997, 53: 563-82.
    • (1997) Drugs , vol.53 , pp. 563-582
    • Jouzeau, J.-Y.1    Terlain, B.2    Abid, A.3    Nedelec, E.4    Netter, P.5
  • 7
    • 0028047951 scopus 로고
    • Characterization of the genomic structure, chromosomal location and promoter of human prostaglandin H synthase-2 gene
    • Tazawa, R., Xu, X.M., Wu, K.K., Wang, L.H. Characterization of the genomic structure, chromosomal location and promoter of human prostaglandin H synthase-2 gene. Biochem Biophys Res Commun 1994, 203: 190-9.
    • (1994) Biochem Biophys Res Commun , vol.203 , pp. 190-199
    • Tazawa, R.1    Xu, X.M.2    Wu, K.K.3    Wang, L.H.4
  • 8
    • 0028226265 scopus 로고
    • 2) encoding prostaglandin-endoperoxide synthase 2
    • 2) encoding prostaglandin-endoperoxide synthase 2. Eur J Biochem 1994, 221: 889-97.
    • (1994) Eur J Biochem , vol.221 , pp. 889-897
    • Kosaka, T.1    Miyata, A.2    Ihara, H.3
  • 9
    • 0027162479 scopus 로고
    • Structural determination and promoter analysis of the chicken mitogen-inducible prostaglandin G/H synthase gene and genetic mapping of the murine homolog
    • Xie, W., Merrill, J.R., Bradshaw, W.S., Simmons, D.L. Structural determination and promoter analysis of the chicken mitogen-inducible prostaglandin G/H synthase gene and genetic mapping of the murine homolog. Arch Biochem Biophys 1993, 300: 247-52.
    • (1993) Arch Biochem Biophys , vol.300 , pp. 247-252
    • Xie, W.1    Merrill, J.R.2    Bradshaw, W.S.3    Simmons, D.L.4
  • 12
    • 0028069896 scopus 로고
    • The cyclic AMP response element plays an essential role in the expression of the human prostaglandin-endoperoxide synthase 2 gene in differentiated U937 monocytic cells
    • Inoue, H., Nanayama, T., Hara, S., Yokoyama, C., Tanabe, T. The cyclic AMP response element plays an essential role in the expression of the human prostaglandin-endoperoxide synthase 2 gene in differentiated U937 monocytic cells. FEBS Lett 1994, 350: 51-4.
    • (1994) FEBS Lett , vol.350 , pp. 51-54
    • Inoue, H.1    Nanayama, T.2    Hara, S.3    Yokoyama, C.4    Tanabe, T.5
  • 13
    • 0028824312 scopus 로고
    • Translational regulation of human prostaglandin-endoperoxide synthase-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cells
    • Inoue, H., Yokoyama, C., Hara, S., Tone, Y., Tanabe, T. Translational regulation of human prostaglandin-endoperoxide synthase-2 gene by lipopolysaccharide and phorbol ester in vascular endothelial cells. J Biol Chem 1995, 270: 24965-71.
    • (1995) J Biol Chem , vol.270 , pp. 24965-24971
    • Inoue, H.1    Yokoyama, C.2    Hara, S.3    Tone, Y.4    Tanabe, T.5
  • 14
    • 0027141004 scopus 로고
    • Cloning two isoforms of rat cyclooxygenase: Differential regulation of their expression
    • Feng, L., Sun, W., Xia, Y. et al. Cloning two isoforms of rat cyclooxygenase: Differential regulation of their expression. Arch Biochem Biophys 1993, 307: 361-8.
    • (1993) Arch Biochem Biophys , vol.307 , pp. 361-368
    • Feng, L.1    Sun, W.2    Xia, Y.3
  • 15
    • 0028180129 scopus 로고
    • Induction of cyclooxygenase-2 by interleukin-1α. Evidence for posttranscriptional regulation
    • Ristimaki, A., Garfinkel, S., Wessendorf, J., Maciag, T., Hla, T. Induction of cyclooxygenase-2 by interleukin-1α. Evidence for posttranscriptional regulation. J Biol Chem 1994, 269: 11769-75.
    • (1994) J Biol Chem , vol.269 , pp. 11769-11775
    • Ristimaki, A.1    Garfinkel, S.2    Wessendorf, J.3    Maciag, T.4    Hla, T.5
  • 16
    • 0027279249 scopus 로고
    • Phorbol ester and epidermal growth factor enhance the expression of two inducible prostaglandin H synthase genes in rat tracheal epithelial cells
    • Hamasaki, Y., Kitzler, J., Hardman, R., Nettesheim, P., Eling, T.E. Phorbol ester and epidermal growth factor enhance the expression of two inducible prostaglandin H synthase genes in rat tracheal epithelial cells. Arch Biochem Biophys 1993, 304: 226-34.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 226-234
    • Hamasaki, Y.1    Kitzler, J.2    Hardman, R.3    Nettesheim, P.4    Eling, T.E.5
  • 17
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3'-untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw, G., Kamen, R. A conserved AU sequence from the 3'-untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 1986, 46: 659-67.
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 18
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2
    • Luong, C., Miller, A., Barnett, J., Chow, J., Ramesha, C., Browner, M.F. Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2. Nat Struct Biol 1996, 3: 927-33.
    • (1996) Nat Struct Biol , vol.3 , pp. 927-933
    • Luong, C.1    Miller, A.2    Barnett, J.3    Chow, J.4    Ramesha, C.5    Browner, M.F.6
  • 19
    • 0030461132 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents
    • Kurumbail, R.G., Stevens, A.M., Gierse, J.K., et al. Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature 1996, 384: 644-8.
    • (1996) Nature , vol.384 , pp. 644-648
    • Kurumbail, R.G.1    Stevens, A.M.2    Gierse, J.K.3
  • 20
    • 0031213634 scopus 로고    scopus 로고
    • Comparison of prostaglandin H synthase isoform structures using limited proteolytic digestion
    • Guo, Q., Chang, S., Diekman, L., Xiao, G., Kulmacz, R.J. Comparison of prostaglandin H synthase isoform structures using limited proteolytic digestion. Arch Biochem Biophys 1997, 344: 150-8.
    • (1997) Arch Biochem Biophys , vol.344 , pp. 150-158
    • Guo, Q.1    Chang, S.2    Diekman, L.3    Xiao, G.4    Kulmacz, R.J.5
  • 21
    • 0030964929 scopus 로고    scopus 로고
    • Conversion of prostaglandin G/H synthase-1 into an enzyme sensitive to PGHS-2-selective inhibitors by a double His513 to Arg and lle523 to Val mutation
    • Wong, E., Bayly, C., Waterman, H.L., Riendeau, D., Mancini, J.A. Conversion of prostaglandin G/H synthase-1 into an enzyme sensitive to PGHS-2-selective inhibitors by a double His513 to Arg and lle523 to Val mutation. J Biol Chem 1997, 272: 9280-6.
    • (1997) J Biol Chem , vol.272 , pp. 9280-9286
    • Wong, E.1    Bayly, C.2    Waterman, H.L.3    Riendeau, D.4    Mancini, J.A.5
  • 23
    • 0028339780 scopus 로고
    • Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin
    • Lecomte, M., Laneuville, O., Ji, C., DeWitt, D.L., Smith, W.L. Acetylation of human prostaglandin endoperoxide synthase-2 (cyclooxygenase-2) by aspirin. J Biol Chem 1994, 269: 13207-15.
    • (1994) J Biol Chem , vol.269 , pp. 13207-13215
    • Lecomte, M.1    Laneuville, O.2    Ji, C.3    DeWitt, D.L.4    Smith, W.L.5
  • 24
    • 0028033328 scopus 로고
    • Characterization of the tyrosyl radicals in ovine prostaglandin H synthase-1 by isotope replacement and site-directed mutagenesis
    • Tsai, A., Hsi, L.C., Kulmacz, R.J., Palmer, G., Smith, W.L. Characterization of the tyrosyl radicals in ovine prostaglandin H synthase-1 by isotope replacement and site-directed mutagenesis. J Biol Chem 1994, 269: 5085-91.
    • (1994) J Biol Chem , vol.269 , pp. 5085-5091
    • Tsai, A.1    Hsi, L.C.2    Kulmacz, R.J.3    Palmer, G.4    Smith, W.L.5
  • 25
    • 0028059103 scopus 로고
    • Interaction between peroxidase and cyclooxygenase activities in prostaglandin-endoperoxide synthase. Interpretation of reaction kinetics
    • Kulmacz, R.J., Pendleton, R.B., Lands, W.E. Interaction between peroxidase and cyclooxygenase activities in prostaglandin-endoperoxide synthase. Interpretation of reaction kinetics. J Biol Chem 1994, 269: 5527-36.
    • (1994) J Biol Chem , vol.269 , pp. 5527-5536
    • Kulmacz, R.J.1    Pendleton, R.B.2    Lands, W.E.3
  • 26
    • 0028301140 scopus 로고
    • Prostaglandin H synthase: Implications for membrane structure
    • Picot, D., Garavito, R.M. Prostaglandin H synthase: Implications for membrane structure. FEBS Lett 1994, 346: 21-5.
    • (1994) FEBS Lett , vol.346 , pp. 21-25
    • Picot, D.1    Garavito, R.M.2
  • 27
    • 0028295135 scopus 로고
    • Mutation of serine-516 in human prostaglandin G/H synthase-2 to methionine or aspirin acetylation of this residue stimulates 15-R-HETE synthesis
    • Mancini, J.A., O'Neill, G.P., Bayly, C., Vickers, P.J. Mutation of serine-516 in human prostaglandin G/H synthase-2 to methionine or aspirin acetylation of this residue stimulates 15-R-HETE synthesis. FEBS Lett 1994, 342: 33-7.
    • (1994) FEBS Lett , vol.342 , pp. 33-37
    • Mancini, J.A.1    O'Neill, G.P.2    Bayly, C.3    Vickers, P.J.4
  • 28
    • 0028123502 scopus 로고
    • Overexpression of human prostaglandin G/H synthase-1 and -2 by recombinant vaccinia virus: Inhibition by nonsteroidal anti-inflammatory drugs and biosynthesis of 15-hydroxye-icosatetraenoic acid
    • O'Neill, G.P., Mancini, J.A., Kargman, S., et al. Overexpression of human prostaglandin G/H synthase-1 and -2 by recombinant vaccinia virus: inhibition by nonsteroidal anti-inflammatory drugs and biosynthesis of 15-hydroxye-icosatetraenoic acid. Mol Pharmacol 1994, 45: 245-54.
    • (1994) Mol Pharmacol , vol.45 , pp. 245-254
    • O'Neill, G.P.1    Mancini, J.A.2    Kargman, S.3
  • 30
    • 0028783912 scopus 로고
    • Arginine 120 of prostaglandin G/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety
    • Mancini, J.A., Riendeau, D., Falgueyret, J.P., Vickers, P.J., O'Neill, G.P. Arginine 120 of prostaglandin G/H synthase-1 is required for the inhibition by nonsteroidal anti-inflammatory drugs containing a carboxylic acid moiety. J Biol Chem 1995, 270: 29372-7.
    • (1995) J Biol Chem , vol.270 , pp. 29372-29377
    • Mancini, J.A.1    Riendeau, D.2    Falgueyret, J.P.3    Vickers, P.J.4    O'Neill, G.P.5
  • 31
    • 0030068054 scopus 로고    scopus 로고
    • Involvement of Arginine 120, Glutamate 524 and Tyrosine 355 in the binding of arachidonate and 2-phenyl-propionic acid inhibitors to the cyclooxygenase active site of ovine prostaglandin endoperoxide H synthase-1
    • Bhattacharyya, D.K., Lecomte, M., Rieke, C.J., Garavito, R.M., Smith, W.L. Involvement of Arginine 120, Glutamate 524 and Tyrosine 355 in the binding of arachidonate and 2-phenyl-propionic acid inhibitors to the cyclooxygenase active site of ovine prostaglandin endoperoxide H synthase-1. J Biol Chem 1996, 271: 2179-84.
    • (1996) J Biol Chem , vol.271 , pp. 2179-2184
    • Bhattacharyya, D.K.1    Lecomte, M.2    Rieke, C.J.3    Garavito, R.M.4    Smith, W.L.5
  • 32
    • 0029899186 scopus 로고    scopus 로고
    • A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors
    • Gierse, J.K., McDonald, J.J., Hauser, S.D., Rangwala, S.H., Koboldt, C.M., Seibert, K. A single amino acid difference between cyclooxygenase-1 (COX-1) and -2 (COX-2) reverses the selectivity of COX-2 specific inhibitors. J Biol Chem 1996, 271: 15810-4.
    • (1996) J Biol Chem , vol.271 , pp. 15810-15814
    • Gierse, J.K.1    McDonald, J.J.2    Hauser, S.D.3    Rangwala, S.H.4    Koboldt, C.M.5    Seibert, K.6
  • 33
    • 0029666486 scopus 로고    scopus 로고
    • Role of Val509 in time-dependent inhibition of human prostaglandin H synthase-2 cyclooxygenase activity by isoform-selective agents
    • Guo, Q., Wang, L., Ruan, K., Kulmacz, R.J. Role of Val509 in time-dependent inhibition of human prostaglandin H synthase-2 cyclooxygenase activity by isoform-selective agents. J Biol Chem 1996, 271: 19134-9.
    • (1996) J Biol Chem , vol.271 , pp. 19134-19139
    • Guo, Q.1    Wang, L.2    Ruan, K.3    Kulmacz, R.J.4
  • 34
    • 0028139275 scopus 로고
    • Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase
    • Copeland, R.A., Williams, J.M., Giannaras, J., et al. Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase. Proc Natl Acad Sci USA 1994, 91: 11202-6.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11202-11206
    • Copeland, R.A.1    Williams, J.M.2    Giannaras, J.3
  • 35
    • 0028831977 scopus 로고
    • Effect of inhibitor time-dependency on selectivity towards cyclooxygenase isoforms
    • Quellet, M., Percival, M.D. Effect of inhibitor time-dependency on selectivity towards cyclooxygenase isoforms. Biochem J 1995, 306: 247-51.
    • (1995) Biochem J , vol.306 , pp. 247-251
    • Quellet, M.1    Percival, M.D.2
  • 36
    • 0342716460 scopus 로고    scopus 로고
    • Mechanistic studies on the selective inhibition of cyclooxygenase-2 by indanone derivatives
    • Klein, T., Nusing, R.M., Wiesenberg-Boettcher, I., Ullrich, V. Mechanistic studies on the selective inhibition of cyclooxygenase-2 by indanone derivatives. Biochem Pharmacol 1996, 51: 285-90.
    • (1996) Biochem Pharmacol , vol.51 , pp. 285-290
    • Klein, T.1    Nusing, R.M.2    Wiesenberg-Boettcher, I.3    Ullrich, V.4
  • 37
    • 0028830109 scopus 로고
    • Expression and selective inhibition of the constitutive and inducible forms of human cyclooxygenase
    • Gierse, J.K., Hauser, S.D., Creely, D.P. et al. Expression and selective inhibition of the constitutive and inducible forms of human cyclooxygenase. Biochem J 1995, 305: 479-84.
    • (1995) Biochem J , vol.305 , pp. 479-484
    • Gierse, J.K.1    Hauser, S.D.2    Creely, D.P.3
  • 38
    • 0028883342 scopus 로고
    • An examination of the source of the tyrosyl radical in ovine prostaglandin endoperoxide synthase-1
    • Hsi, L.C., Hoganson, C.W., Babcock, G.T., Garavito, R.M., Smith, W.L. An examination of the source of the tyrosyl radical in ovine prostaglandin endoperoxide synthase-1. Biochem Biophys Res Commun 1995, 207: 652-60.
    • (1995) Biochem Biophys Res Commun , vol.207 , pp. 652-660
    • Hsi, L.C.1    Hoganson, C.W.2    Babcock, G.T.3    Garavito, R.M.4    Smith, W.L.5
  • 39
    • 0027997107 scopus 로고
    • The isoforms of cyclooxygenase: Structure and function
    • Loll, P.J., Garavito, R.M. The isoforms of cyclooxygenase: Structure and function. Exp Opin Invest Drugs 1994, 3: 1171-80.
    • (1994) Exp Opin Invest Drugs , vol.3 , pp. 1171-1180
    • Loll, P.J.1    Garavito, R.M.2
  • 40
    • 0027944075 scopus 로고
    • Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain
    • Seibert, K., Zhang, Y., Leahy, K. et al. Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain. Proc Natl Acad Sci USA 1994, 91: 12013-7.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12013-12017
    • Seibert, K.1    Zhang, Y.2    Leahy, K.3
  • 41
    • 13444266910 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of the 1,5-diarylpyrazole class of cyclooxygenase-2 inhibitors: Identification of 4-[5-(4-methyl-phenyl)-3-(tri-fluoromethyl)-1H-pyrazol-1-yl]-benzenesulfonamide (SC-58635, celecoxib)
    • Penning, T.D., Talley, J.J., Bertenshaw, S.R. et al. Synthesis and biological evaluation of the 1,5-diarylpyrazole class of cyclooxygenase-2 inhibitors: Identification of 4-[5-(4-methyl-phenyl)-3-(tri-fluoromethyl)-1H-pyrazol-1-yl]-benzenesulfonamide (SC-58635, celecoxib). J Med Chem 1997, 40: 1347-65.
    • (1997) J Med Chem , vol.40 , pp. 1347-1365
    • Penning, T.D.1    Talley, J.J.2    Bertenshaw, S.R.3
  • 42
    • 0029033219 scopus 로고
    • Pharmacology of a selective cyclooxygenase-2 inhibitor, L-745,337: A novel nonsteroidal anti-inflammatory agent with an ulcerogenic sparing effect in rat and non-human primate stomach
    • Chan, C.-C., Boyce, S., Brideau, C. et al. Pharmacology of a selective cyclooxygenase-2 inhibitor, L-745,337: A novel nonsteroidal anti-inflammatory agent with an ulcerogenic sparing effect in rat and non-human primate stomach. J Pharmacol Exp Ther 1995, 274: 1531-7.
    • (1995) J Pharmacol Exp Ther , vol.274 , pp. 1531-1537
    • Chan, C.-C.1    Boyce, S.2    Brideau, C.3
  • 43
    • 8244255009 scopus 로고    scopus 로고
    • Biochemical and pharmacological profile of a tetrasubstituted furanone as a highly selective COX-2 inhibitor
    • Riendeau, D., Percival, M.D., Boyce, S. et al. Biochemical and pharmacological profile of a tetrasubstituted furanone as a highly selective COX-2 inhibitor. Br J Pharmacol 1997, 121: 105-17.
    • (1997) Br J Pharmacol , vol.121 , pp. 105-117
    • Riendeau, D.1    Percival, M.D.2    Boyce, S.3
  • 44
    • 0015510101 scopus 로고
    • Oxygenation of polyunsaturated fatty acids during prostaglandin biosynthesis by sheep vesicular gland
    • Smith, W.L., Lands, W.E. Oxygenation of polyunsaturated fatty acids during prostaglandin biosynthesis by sheep vesicular gland. Biochemistry 1972, 11: 3276-85.
    • (1972) Biochemistry , vol.11 , pp. 3276-3285
    • Smith, W.L.1    Lands, W.E.2
  • 45
    • 0028929688 scopus 로고
    • Pre-steady-state kinetics and modelling of the oxygenase and cyclooxygenase reactions of prostaglandin endoperoxide synthase
    • Bakovic, M., Dunford, H.B. Pre-steady-state kinetics and modelling of the oxygenase and cyclooxygenase reactions of prostaglandin endoperoxide synthase. Biophys Chem 1995, 54: 237-51.
    • (1995) Biophys Chem , vol.54 , pp. 237-251
    • Bakovic, M.1    Dunford, H.B.2
  • 47
    • 0028810964 scopus 로고
    • Comparison of hydroperoxide initiator requirements for the cyclooxygenase activities of prostaglandin h synthase-1 and -2
    • Kulmacz, R.J., Wang, L.-H. Comparison of hydroperoxide initiator requirements for the cyclooxygenase activities of prostaglandin H synthase-1 and -2. J Biol Chem 1995, 270: 24019-23.
    • (1995) J Biol Chem , vol.270 , pp. 24019-24023
    • Kulmacz, R.J.1    Wang, L.-H.2
  • 49
    • 0018976320 scopus 로고
    • Evidence for a peroxide-initiated free radical mechanism of prostaglandin biosynthesis
    • Hemler, M.E., Lands, W.E. Evidence for a peroxide-initiated free radical mechanism of prostaglandin biosynthesis. J Biol Chem 1980, 255: 6253-61.
    • (1980) J Biol Chem , vol.255 , pp. 6253-6261
    • Hemler, M.E.1    Lands, W.E.2
  • 50
    • 0030842344 scopus 로고    scopus 로고
    • Low concentrations of lipid hydroperoxides prime human platelet aggregation specifically via cyclooxygenase activation
    • Calzada, C., Vericel, E., Lagarde, M. Low concentrations of lipid hydroperoxides prime human platelet aggregation specifically via cyclooxygenase activation. Biochem J 1997, 325: 495-500.
    • (1997) Biochem J , vol.325 , pp. 495-500
    • Calzada, C.1    Vericel, E.2    Lagarde, M.3
  • 51
    • 9844255580 scopus 로고    scopus 로고
    • 2,6-di-tert-butylphenols: A new class of potent and selective PGHS-2 inhibitor
    • Song, Y., Connor, D.T., Sorenson, R.J. et al. 2,6-di-tert-butylphenols: A new class of potent and selective PGHS-2 inhibitor. Inflamm Res 1997, 46: S141-2.
    • (1997) Inflamm Res , vol.46
    • Song, Y.1    Connor, D.T.2    Sorenson, R.J.3
  • 53
    • 0028037571 scopus 로고
    • The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum
    • Otto, J.C., Smith, W.L. The orientation of prostaglandin endoperoxide synthases-1 and -2 in the endoplasmic reticulum. J Biol Chem 1994, 269: 19868-75.
    • (1994) J Biol Chem , vol.269 , pp. 19868-19875
    • Otto, J.C.1    Smith, W.L.2
  • 54
    • 0027200551 scopus 로고
    • Subcellular localization of prostaglandin endoperoxide synthase-2 in murine 373 cells
    • Regier, M.K., DeWitt, D.L., Schindler, M.S., Smith, W.L. Subcellular localization of prostaglandin endoperoxide synthase-2 in murine 373 cells. Arch Biochem Biophys 1993, 301: 439-44.
    • (1993) Arch Biochem Biophys , vol.301 , pp. 439-444
    • Regier, M.K.1    DeWitt, D.L.2    Schindler, M.S.3    Smith, W.L.4
  • 55
    • 0028969527 scopus 로고
    • Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2
    • Morita, I., Schindler, M.S., Regier, M.K. et al. Different intracellular locations for prostaglandin endoperoxide H synthase-1 and -2. J Biol Chem 1995, 270: 10902-8.
    • (1995) J Biol Chem , vol.270 , pp. 10902-10908
    • Morita, I.1    Schindler, M.S.2    Regier, M.K.3
  • 57
    • 0025225456 scopus 로고
    • The retention signal for soluble proteins of the endoplasmic reticulum
    • Pelham, H.R. The retention signal for soluble proteins of the endoplasmic reticulum. Trends Biochem Sci 1990, 15: 483-6.
    • (1990) Trends Biochem Sci , vol.15 , pp. 483-486
    • Pelham, H.R.1
  • 58
    • 0028961611 scopus 로고
    • Prostaglandin H synthase-1: Evaluation of C-terminus function
    • Ren, Y., Loose-Mitchell, D.S., Kulmacz, R.J. Prostaglandin H synthase-1: Evaluation of C-terminus function. Arch Biochem Biophys 1995, 316: 751-7.
    • (1995) Arch Biochem Biophys , vol.316 , pp. 751-757
    • Ren, Y.1    Kulmacz, R.J.2
  • 59
    • 0028032575 scopus 로고
    • Investigation of the role of cysteines in catalysis by prostaglandin endoperoxide synthase
    • Kennedy, T.A., Smith, C.J., Marnett, L.J. Investigation of the role of cysteines in catalysis by prostaglandin endoperoxide synthase. J Biol Chem 1994, 269: 27357-64.
    • (1994) J Biol Chem , vol.269 , pp. 27357-27364
    • Kennedy, T.A.1    Smith, C.J.2    Marnett, L.J.3
  • 60
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf, D.J., Evans, R.M. The RXR heterodimers and orphan receptors. Cell 1995, 83: 841-50.
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 63
    • 0028802627 scopus 로고
    • Differential activation of peroxisome proliferator-activated receptors by eicosanoids
    • Yu, K., Bayona, W., Kallen, C.B. et al. Differential activation of peroxisome proliferator-activated receptors by eicosanoids. J Biol Chem 1995, 270: 23975-83.
    • (1995) J Biol Chem , vol.270 , pp. 23975-23983
    • Yu, K.1    Bayona, W.2    Kallen, C.B.3
  • 66
    • 0028302217 scopus 로고
    • Prostaglandins in the treatment of cancer
    • Sasaki, H., Fukushima, M. Prostaglandins in the treatment of cancer. Anticancer Drugs 1994, 5: 131-8.
    • (1994) Anticancer Drugs , vol.5 , pp. 131-138
    • Sasaki, H.1    Fukushima, M.2
  • 69
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • Willis, D., Moore, A.R., Frederick, R., Willoughby, D.A. Heme oxygenase: A novel target for the modulation of the inflammatory response. Nat Med 1996, 2: 87-90.
    • (1996) Nat Med , vol.2 , pp. 87-90
    • Willis, D.1    Moore, A.R.2    Frederick, R.3    Willoughby, D.A.4
  • 70
    • 0028803728 scopus 로고
    • Alterations in cellular adhesion and apoptosis in epithelial cells overexpressing prostaglandin endoperoxide synthase 2
    • Tsuji, M., Dubois, R.N. Alterations in cellular adhesion and apoptosis in epithelial cells overexpressing prostaglandin endoperoxide synthase 2. Cell 1995, 83: 493-501.
    • (1995) Cell , vol.83 , pp. 493-501
    • Tsuji, M.1    Dubois, R.N.2


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