메뉴 건너뛰기




Volumn 2, Issue 3, 2003, Pages 179-191

The development of COX2 inhibitors

Author keywords

[No Author keywords available]

Indexed keywords

5 BROMO 2 (4 FLUOROPHENYL) 3 (4 METHYLSULFONYLPHENYL)THIOPHENE; ACETYLSALICYLIC ACID; ANTIINFLAMMATORY AGENT; CELECOXIB; CYCLOOXYGENASE 2 INHIBITOR; DICLOFENAC; ETODOLAC; FLOSULIDE; FLUFENAMIC ACID; FLURBIPROFEN; IBUPROFEN; INDOMETACIN; KETOPROFEN; MECLOFENAMIC ACID; MEFENAMIC ACID; MELOXICAM; N (2 CYCLOHEXYLOXY 4 NITROPHENYL)METHANESULFONAMIDE; NAPROXEN; NIMESULIDE; NONSTEROID ANTIINFLAMMATORY AGENT; OXYPHENBUTAZONE; PARACETAMOL; PHENACETIN; PHENYLBUTAZONE; PIROXICAM; PROSTAGLANDIN INHIBITOR; PROSTAGLANDIN SYNTHASE; ROFECOXIB; SALICYLIC ACID; UNINDEXED DRUG; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; ISOENZYME; MEMBRANE PROTEIN; PROSTAGLANDIN SYNTHASE INHIBITOR; PTGS1 PROTEIN, HUMAN; PTGS2 PROTEIN, HUMAN;

EID: 0037364161     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1034     Document Type: Review
Times cited : (422)

References (143)
  • 3
    • 0014651374 scopus 로고
    • A pharmacological analysis of aspirin
    • Collier, H. O. J. A pharmacological analysis of aspirin. Adv. Pharmacol. Chemother. 7, 333-405 (1969).
    • (1969) Adv. Pharmacol. Chemother. , vol.7 , pp. 333-405
    • Collier, H.O.J.1
  • 4
    • 0242325380 scopus 로고
    • Prostaglandins and the aspirin like drugs
    • March
    • Vane, J. R. Prostaglandins and the aspirin like drugs. Hosp. Pract. March, 61-71 (1972).
    • (1972) Hosp. Pract. , pp. 61-71
    • Vane, J.R.1
  • 5
    • 0015237292 scopus 로고
    • Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs
    • Vane, J. R. Inhibition of prostaglandin synthesis as a mechanism of action for aspirin-like drugs. Nat. New Biol. 231, 232-235 (1971).
    • (1971) Nat. New Biol. , vol.231 , pp. 232-235
    • Vane, J.R.1
  • 6
    • 0015237263 scopus 로고
    • Indomethacin and aspirin abolish prostaglandin release from the spleen
    • Ferreira, S. H., Moncada, S. & Vane, J. R. Indomethacin and aspirin abolish prostaglandin release from the spleen. Nat. New Biol. 231, 237-239 (1971).
    • (1971) Nat. New Biol. , vol.231 , pp. 237-239
    • Ferreira, S.H.1    Moncada, S.2    Vane, J.R.3
  • 7
    • 0015237275 scopus 로고
    • Aspirin selectively inhibits prostaglandin production in human platelets
    • Smith, J. B. & Willis, A. L. Aspirin selectively inhibits prostaglandin production in human platelets. Nat. New Biol. 231, 235-237 (1971).
    • (1971) Nat. New Biol. , vol.231 , pp. 235-237
    • Smith, J.B.1    Willis, A.L.2
  • 8
    • 0015229602 scopus 로고
    • Effect of aspirin on human seminal prostaglandins
    • Collier, J. G. & Flower, R. J. Effect of aspirin on human seminal prostaglandins. Lancet 2, 852-853 (1971).
    • (1971) Lancet , vol.2 , pp. 852-853
    • Collier, J.G.1    Flower, R.J.2
  • 10
    • 0014339832 scopus 로고
    • Effect of prostaglandin E1 on gastric secretion and ulcer formation in the rat
    • Robert, A., Nezamis, J. E. & Phillips, J. P. Effect of prostaglandin E1 on gastric secretion and ulcer formation in the rat. Gastroenterology 55, 481-487 (1968).
    • (1968) Gastroenterology , vol.55 , pp. 481-487
    • Robert, A.1    Nezamis, J.E.2    Phillips, J.P.3
  • 12
    • 0015530368 scopus 로고
    • Relationship between inhibition of prostaglandin synthesis and drug efficacy: Support for the current theory on mode of action of aspirin-like drugs
    • Tomlinson, R. V. & Ringold, H. J. Relationship between inhibition of prostaglandin synthesis and drug efficacy: support for the current theory on mode of action of aspirin-like drugs. Biochem. Biophys. Res. Commun. 46, 552-559 (1972).
    • (1972) Biochem. Biophys. Res. Commun. , vol.46 , pp. 552-559
    • Tomlinson, R.V.1    Ringold, H.J.2
  • 13
    • 0016227738 scopus 로고
    • Drugs which inhibit prostaglandin biosynthesis
    • Flower, R. J. Drugs which inhibit prostaglandin biosynthesis. Pharmacol. Rev. 26, 33-67 (1974).
    • (1974) Pharmacol. Rev. , vol.26 , pp. 33-67
    • Flower, R.J.1
  • 14
    • 0015511847 scopus 로고
    • Inhibition of prostaglandin synthetase in brain explains the anti-pyretic activity of paracetamol (4-acetamidophenol)
    • Flower, R. J. & Vane, J. R. Inhibition of prostaglandin synthetase in brain explains the anti-pyretic activity of paracetamol (4-acetamidophenol). Nature 240, 410-411 (1972).
    • (1972) Nature , vol.240 , pp. 410-411
    • Flower, R.J.1    Vane, J.R.2
  • 15
    • 0015841951 scopus 로고
    • Inhibition of the PG synthetase system in ocular tissue by indomethacin
    • Bhattacherjee, P. & Eakins, K. Inhibition of the PG synthetase system in ocular tissue by indomethacin. Pharmacologist 15, 209-215 (1973).
    • (1973) Pharmacologist , vol.15 , pp. 209-215
    • Bhattacherjee, P.1    Eakins, K.2
  • 17
    • 0033551847 scopus 로고    scopus 로고
    • Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition
    • Marnett, L. J., Rowlinson, S. W., Goodwin, D. C., Kalgutkar, A. S. & Lanzo, C. A. Arachidonic acid oxygenation by COX-1 and COX-2. Mechanisms of catalysis and inhibition. J. Biol. Chem. 274, 22903-22906 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 22903-22906
    • Marnett, L.J.1    Rowlinson, S.W.2    Goodwin, D.C.3    Kalgutkar, A.S.4    Lanzo, C.A.5
  • 18
    • 0023855416 scopus 로고
    • Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase)
    • Merlie, J. P., Fagan, D., Mudd, J. & Needleman, P. Isolation and characterization of the complementary DNA for sheep seminal vesicle prostaglandin endoperoxide synthase (cyclooxygenase). J. Biol. Chem. 263, 3550-3553 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 3550-3553
    • Merlie, J.P.1    Fagan, D.2    Mudd, J.3    Needleman, P.4
  • 20
    • 0015150481 scopus 로고
    • Stimulation and blockade of prostaglandin biosynthesis
    • Smith, W. L. & Lands, W. E. Stimulation and blockade of prostaglandin biosynthesis. J. Biol. Chem. 246, 6700-6702 (1971).
    • (1971) J. Biol. Chem. , vol.246 , pp. 6700-6702
    • Smith, W.L.1    Lands, W.E.2
  • 22
    • 0018265071 scopus 로고
    • Acetylation of the NH2-terminal serine of prostaglandin synthetase by aspirin
    • Roth, G. J. & Siok, C. J. Acetylation of the NH2-terminal serine of prostaglandin synthetase by aspirin. J. Biol. Chem. 253, 3782-3784 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 3782-3784
    • Roth, G.J.1    Siok, C.J.2
  • 23
    • 0017704589 scopus 로고
    • Exaggerated prostaglandin biosynthesis and its influence on renal resistance in the isolated hydronephrotic rabbit kidney
    • Nishikawa, K., Morrison, A. & Needleman, P. Exaggerated prostaglandin biosynthesis and its influence on renal resistance in the isolated hydronephrotic rabbit kidney. J. Clin. Invest. 59, 1143-1150 (1977).
    • (1977) J. Clin. Invest. , vol.59 , pp. 1143-1150
    • Nishikawa, K.1    Morrison, A.2    Needleman, P.3
  • 24
    • 0018223989 scopus 로고
    • Mechanism of enhanced renal prostaglandin biosynthesis in ureter obstruction. Role of de novo protein synthesis
    • Morrison, A. R., Moritz, H. & Needleman, P. Mechanism of enhanced renal prostaglandin biosynthesis in ureter obstruction. Role of de novo protein synthesis. J. Biol. Chem. 253, 8210-8212 (1978).
    • (1978) J. Biol. Chem. , vol.253 , pp. 8210-8212
    • Morrison, A.R.1    Moritz, H.2    Needleman, P.3
  • 25
    • 0020039317 scopus 로고
    • Evidence for two distinct forms of fatty acid cyclooxygenase in brain
    • Lysz, T. W. & Needleman, P. Evidence for two distinct forms of fatty acid cyclooxygenase in brain. J. Neurochem. 38, 1111-1117 (1982).
    • (1982) J. Neurochem. , vol.38 , pp. 1111-1117
    • Lysz, T.W.1    Needleman, P.2
  • 26
    • 0018904225 scopus 로고
    • Selective inhibition of prostaglandin production in inflammatory exudates and gastric mucosa
    • Whittle, B. J., Higgs, G. A., Eakins, K. E., Moncada, S. & Vane, J. R. Selective inhibition of prostaglandin production in inflammatory exudates and gastric mucosa. Nature 284, 271-273 (1980).
    • (1980) Nature , vol.284 , pp. 271-273
    • Whittle, B.J.1    Higgs, G.A.2    Eakins, K.E.3    Moncada, S.4    Vane, J.R.5
  • 27
    • 0023814286 scopus 로고
    • Inhibition by corticosteroids of epidermal growth factor-induced recovery of cyclooxygenase after aspirin inactivation
    • Pash, J. M. & Bailey, J. M. Inhibition by corticosteroids of epidermal growth factor-induced recovery of cyclooxygenase after aspirin inactivation. FASEB J. 2, 2613-2618 (1988).
    • (1988) FASEB J. , vol.2 , pp. 2613-2618
    • Pash, J.M.1    Bailey, J.M.2
  • 28
    • 0023854087 scopus 로고
    • Regulation of fibroblast cyclooxygenase synthesis by interleukin-1
    • Raz, A., Wyche, A., Siegel, N. & Needleman, P. Regulation of fibroblast cyclooxygenase synthesis by interleukin-1. J. Biol. Chem. 263, 3022-3028 (1988).
    • (1988) J. Biol. Chem. , vol.263 , pp. 3022-3028
    • Raz, A.1    Wyche, A.2    Siegel, N.3    Needleman, P.4
  • 29
    • 0001208476 scopus 로고
    • Temporal and pharmacological division of fibroblast cyclooxygenase expression into transcriptional and translational phases
    • Raz, A., Wyche, A. & Needleman, P. Temporal and pharmacological division of fibroblast cyclooxygenase expression into transcriptional and translational phases. Proc. Natl Acad. Sci. USA 86, 1657-1661 (1989).
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 1657-1661
    • Raz, A.1    Wyche, A.2    Needleman, P.3
  • 31
    • 0025187588 scopus 로고
    • Selective regulation of cellUlar cyclooxygenase by dexamethasone and endotoxin in mice
    • Masferrer, J. L., Zweifel, B. S., Seibert, K. & Needleman, P. Selective regulation of cellUlar cyclooxygenase by dexamethasone and endotoxin in mice. J. Clin. Invest. 86, 1375-1379 (1990).
    • (1990) J. Clin. Invest. , vol.86 , pp. 1375-1379
    • Masferrer, J.L.1    Zweifel, B.S.2    Seibert, K.3    Needleman, P.4
  • 33
    • 0024408107 scopus 로고
    • Rapid induction of prostaglandin endoperoxide synthase in rat preovulatory follicles by luteinizing hormone and cAMP is blocked by inhibitors of transcription and translation
    • Wong, W. Y., DeWitt, D. L., Smith, W. L. & Richards, J. S. Rapid induction of prostaglandin endoperoxide synthase in rat preovulatory follicles by luteinizing hormone and cAMP is blocked by inhibitors of transcription and translation. Mol. Endocrinol. 3, 1714-1723 (1989).
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1714-1723
    • Wong, W.Y.1    DeWitt, D.L.2    Smith, W.L.3    Richards, J.S.4
  • 34
    • 0025754779 scopus 로고
    • Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing
    • Xie, W. L., Chipman, J. G., Robertson, D. L., Erikson, R. L. & Simmons, D. L. Expression of a mitogen-responsive gene encoding prostaglandin synthase is regulated by mRNA splicing. Proc. Natl Acad. Sci. USA 88, 2692-2696 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2692-2696
    • Xie, W.L.1    Chipman, J.G.2    Robertson, D.L.3    Erikson, R.L.4    Simmons, D.L.5
  • 35
    • 0025871150 scopus 로고
    • TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue
    • Kujubu, D. A., Fletcher, B. S., Varnum, B. C., Lim, R. W. & Herschman, H. R. TIS10, a phorbol ester tumor promoter-inducible mRNA from Swiss 3T3 cells, encodes a novel prostaglandin synthase/cyclooxygenase homologue. J. Biol. Chem. 266, 12866-12872 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12866-12872
    • Kujubu, D.A.1    Fletcher, B.S.2    Varnum, B.C.3    Lim, R.W.4    Herschman, H.R.5
  • 36
    • 0026702494 scopus 로고
    • Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional prostaglandin G/H synthase
    • Fletcher, B. S., Kujubu, D. A., Perrin, D. M. & Herschman, H. R. Structure of the mitogen-inducible TIS10 gene and demonstration that the TIS10-encoded protein is a functional prostaglandin G/H synthase. J. Biol. Chem. 267, 4338-4344 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4338-4344
    • Fletcher, B.S.1    Kujubu, D.A.2    Perrin, D.M.3    Herschman, H.R.4
  • 37
    • 0026662385 scopus 로고
    • Dexamethasone inhibits mitogen induction of the TIS10 prostaglandin synthase/cyclooxygenase gene
    • Kujubu, D. A. & Herschman, H. R. Dexamethasone inhibits mitogen induction of the TIS10 prostaglandin synthase/cyclooxygenase gene. J. Biol. Chem. 267, 7991-7994 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 7991-7994
    • Kujubu, D.A.1    Herschman, H.R.2
  • 38
    • 0026322957 scopus 로고
    • A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein
    • O'Banion, M. K., Sadowski, H. B., Winn, V. & Young, D. A. A serum- and glucocorticoid-regulated 4-kilobase mRNA encodes a cyclooxygenase-related protein. J. Biol. Chem. 266, 23261-23267 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 23261-23267
    • O'Banion, M.K.1    Sadowski, H.B.2    Winn, V.3    Young, D.A.4
  • 39
    • 0025759338 scopus 로고
    • Regulation of prostaglandin endoperoxide synthase gene expression in cultured rat mesangial cells: Induction by serum via a protein kinase-C-dependent mechanism
    • Simonson, M. S., Wolfe, J. A., Konieczkowski, M., Sedor, J. R. & Dunn, M. J. Regulation of prostaglandin endoperoxide synthase gene expression in cultured rat mesangial cells: induction by serum via a protein kinase-C-dependent mechanism. Mol. Endocrinol. 5, 441-451 (1991).
    • (1991) Mol. Endocrinol. , vol.5 , pp. 441-451
    • Simonson, M.S.1    Wolfe, J.A.2    Konieczkowski, M.3    Sedor, J.R.4    Dunn, M.J.5
  • 40
    • 0026533306 scopus 로고
    • A collection of mRNA species that are inducible in the RAW 264.7 mouse macrophage cell line by gamma interferon and other agents
    • Farber, J. M. A collection of mRNA species that are inducible in the RAW 264.7 mouse macrophage cell line by gamma interferon and other agents. Mol. Cell Biol. 12, 1535-1545 (1992).
    • (1992) Mol. Cell Biol. , vol.12 , pp. 1535-1545
    • Farber, J.M.1
  • 41
    • 0027076645 scopus 로고
    • Selective expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide
    • Lee, S. H. et al. Selective expression of mitogen-inducible cyclooxygenase in macrophages stimulated with lipopolysaccharide. J. Biol. Chem. 267, 25934-25938 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 25934-25938
    • Lee, S.H.1
  • 42
    • 0026777810 scopus 로고
    • Lipopolysaccharride priming of alveolar macrophages for enhanced synthesis of prostanoids involves induction of a novel prostaglandin H synthase
    • O'Sullivan, M. G., Chilton, F. H., Huggins, E. M. Jr & McCall, C. E. Lipopolysaccharride priming of alveolar macrophages for enhanced synthesis of prostanoids involves induction of a novel prostaglandin H synthase. J. Biol. Chem. 267, 14547-14550 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 14547-14550
    • O'Sullivan, M.G.1    Chilton, F.H.2    Huggins Jr., E.M.3    McCall, C.E.4
  • 43
    • 0026774117 scopus 로고
    • Hormonal regulation of messenger ribonucleic acid encoding a novel isoform of prostaglandin endoperoxide H synthase in rat preovulatory follicles. Induction in vivo and in vitro
    • Sirois, J., Simmons, D. L. & Richards, J. S. Hormonal regulation of messenger ribonucleic acid encoding a novel isoform of prostaglandin endoperoxide H synthase in rat preovulatory follicles. Induction in vivo and in vitro. J. Biol. Chem. 267, 11586-11592 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 11586-11592
    • Sirois, J.1    Simmons, D.L.2    Richards, J.S.3
  • 44
    • 0026744831 scopus 로고
    • Purification and characterization of a novel, distinct isoform of prostaglandin endoperoxide synthase induced by human chorionic gonadotropin in granulosa cells of rat preovulatory follicles
    • Sirois, J. & Richards, J. S. Purification and characterization of a novel, distinct isoform of prostaglandin endoperoxide synthase induced by human chorionic gonadotropin in granulosa cells of rat preovulatory follicles, J. Biol. Chem. 267, 6382-6388 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 6382-6388
    • Sirois, J.1    Richards, J.S.2
  • 45
    • 0026899637 scopus 로고
    • Identification of an immediate early gene, pghs-B, whose protein product has prostaglandin synthase/cyclooxygenase activity
    • Ryseck, R. P. et al. Identification of an immediate early gene, pghs-B, whose protein product has prostaglandin synthase/cyclooxygenase activity. Cell Growth Differ. 3, 443-450 (1992).
    • (1992) Cell Growth Differ. , vol.3 , pp. 443-450
    • Ryseck, R.P.1
  • 46
    • 0027141004 scopus 로고
    • Cloning two isoforms of rat cyclooxygenase: Differential regulation of their expression
    • Feng, L. et al. Cloning two isoforms of rat cyclooxygenase: differential regulation of their expression. Arch. Biochem. Biophys. 307, 361-368 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 361-368
    • Feng, L.1
  • 47
    • 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. 300, 247-252 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 247-252
    • Xie, W.1    Merrill, J.R.2    Bradshaw, W.S.3    Simmons, D.L.4
  • 48
    • 0028226265 scopus 로고
    • Characterization of the human gene (PTGS2) encoding prostaglandin-endoperoxide synthase 2
    • Kosaka, T. et al. Characterization of the human gene (PTGS2) encoding prostaglandin-endoperoxide synthase 2. Eur. J. Biochem. 221, 889-897 (1994).
    • (1994) Eur. J. Biochem. , vol.221 , pp. 889-897
    • Kosaka, T.1
  • 49
    • 0027293391 scopus 로고
    • Expression of mRNA for cyclooxygenase-1 and cyclooxygenase-2 in human tissues
    • O'Neill, G. P. & Ford-Hutchinson, A. W. Expression of mRNA for cyclooxygenase-1 and cyclooxygenase-2 in human tissues. FEBS Lett. 330, 156-160 (1993).
    • (1993) FEBS Lett. , vol.330 , pp. 156-160
    • O'Neill, G.P.1    Ford-Hutchinson, A.W.2
  • 50
    • 0027379123 scopus 로고
    • Prostaglandin G/H synthase isoenzyme 2 expression in fibroblasts: Regulation by dexamethasone, mitogens, and oncogenes
    • Evett, G. E., Xie, W., Chipman, J. G., Robertson, D. L. & Simmons, D. L. Prostaglandin G/H synthase isoenzyme 2 expression in fibroblasts: regulation by dexamethasone, mitogens, and oncogenes. Arch. Biochem. Biophys. 306, 169-177 (1993).
    • (1993) Arch. Biochem. Biophys. , vol.306 , pp. 169-177
    • Evett, G.E.1    Xie, W.2    Chipman, J.G.3    Robertson, D.L.4    Simmons, D.L.5
  • 51
    • 0030017042 scopus 로고    scopus 로고
    • Characterization of prostaglandin G/H synthase 1 and 2 in rat, dog, monkey, and human gastrointestinal tracts
    • Kargman, S. et al. Characterization of prostaglandin G/H synthase 1 and 2 in rat, dog, monkey, and human gastrointestinal tracts. Gastroenterology 111, 445-454 (1996).
    • (1996) Gastroenterology , vol.111 , pp. 445-454
    • Kargman, S.1
  • 52
    • 0027146692 scopus 로고
    • Selectivity of nonsteroidal anti-inflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase
    • Mitchell, J. A., Akarasereenont, P., Thiemermann, C., Flower, R. J. & Vane, J. R. Selectivity of nonsteroidal anti-inflammatory drugs as inhibitors of constitutive and inducible cyclooxygenase. Proc. Natl Acad. Sci. USA 90, 11693-11697 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11693-11697
    • Mitchell, J.A.1    Akarasereenont, P.2    Thiemermann, C.3    Flower, R.J.4    Vane, J.R.5
  • 53
    • 0027480087 scopus 로고
    • Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs
    • Meade, E. A., Smith, W. L. & DeWitt, D. L. Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs. J. Biol. Chem. 268, 6610-6614 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 6610-6614
    • Meade, E.A.1    Smith, W.L.2    DeWitt, D.L.3
  • 54
    • 0027912932 scopus 로고
    • PGH synthase isoenzyme selectivity: The potential for safer nonsteroidal anti-inflammatory drugs
    • DeWitt, D. L., Meade, E. A. & Smith, W. L. PGH synthase isoenzyme selectivity: the potential for safer nonsteroidal anti-inflammatory drugs. Am. J. Med. 95, S40-S44 (1993).
    • (1993) Am. J. Med. , vol.95
    • DeWitt, D.L.1    Meade, E.A.2    Smith, W.L.3
  • 55
    • 0028843881 scopus 로고
    • Prostaglandin synthase 1 gene disruption in mice reduces arachidonic acid-induced inflammation and indomethacin-induced gastric ulceration
    • Langenbach, R. et al. Prostaglandin synthase 1 gene disruption in mice reduces arachidonic acid-induced inflammation and indomethacin-induced gastric ulceration. Cell 83, 483-492 (1995).
    • (1995) Cell , vol.83 , pp. 483-492
    • Langenbach, R.1
  • 56
    • 0028818913 scopus 로고
    • Renal abnormalities and an altered inflammatory response in mice lacking cyclooxygenase II
    • Dinchuk, J. E. et al. Renal abnormalities and an altered inflammatory response in mice lacking cyclooxygenase II. Nature 378, 406-409 (1995).
    • (1995) Nature , vol.378 , pp. 406-409
    • Dinchuk, J.E.1
  • 57
    • 0025160887 scopus 로고
    • Anti-inflammatory and safety profile of DuP 697, a novel orally effective prostaglandin synthesis inhibitor
    • Gans K. R. et al. Anti-inflammatory and safety profile of DuP 697, a novel orally effective prostaglandin synthesis inhibitor. J. Pharmacol. Exp. Ther. 254, 180-187 (1990).
    • (1990) J. Pharmacol. Exp. Ther. , vol.254 , pp. 180-187
    • Gans, K.R.1
  • 59
    • 0027201818 scopus 로고
    • Selective inhibition of NS-398 on prostanoid production in inflamed tissue in rat carrageenan-air-pouch inflammation
    • Futaki, N. et al. Selective inhibition of NS-398 on prostanoid production in inflamed tissue in rat carrageenan-air-pouch inflammation. J. Pharm. Pharmacol. 45, 753-755 (1993).
    • (1993) J. Pharm. Pharmacol. , vol.45 , pp. 753-755
    • Futaki, N.1
  • 60
    • 0028089109 scopus 로고
    • NS-398, a new anti-inflammatory agent, selectively inhibits prostaglandin G/H synthase/cyclooxygenase (COX-2) activity in vitro
    • Futaki, N. et al. NS-398, a new anti-inflammatory agent, selectively inhibits prostaglandin G/H synthase/cyclooxygenase (COX-2) activity in vitro. Prostaglandins 47, 55-59 (1994).
    • (1994) Prostaglandins , vol.47 , pp. 55-59
    • Futaki, N.1
  • 61
    • 0028213334 scopus 로고
    • Cyclooxygenase-1 and-2 expression in rheumatoid synovial tissues. Effects of interleukin-1 beta, phorbol ester, and corticosteroids
    • Crofford, L. J. et al. Cyclooxygenase-1 and-2 expression in rheumatoid synovial tissues. Effects of interleukin-1 beta, phorbol ester, and corticosteroids. J. Clin. Invest. 93, 1095-1101 (1994).
    • (1994) J. Clin. Invest. , vol.93 , pp. 1095-1101
    • Crofford, L.J.1
  • 62
    • 0029000419 scopus 로고
    • Regulation of cyclooxygenase-2 expression in normal human articular chondrocytes
    • Geng, Y., Blanco, F. J., Cornelisson, M. & Lotz, M. Regulation of cyclooxygenase-2 expression in normal human articular chondrocytes. J. Immunol. 155, 796-801 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 796-801
    • Geng, Y.1    Blanco, F.J.2    Cornelisson, M.3    Lotz, M.4
  • 63
    • 0028322893 scopus 로고
    • Selective inhibition of inducible cyclooxygenase 2 in vivo is antiinflammatory and nonulcerogenic
    • Masferrer, J. L. et al. Selective inhibition of inducible cyclooxygenase 2 in vivo is antiinflammatory and nonulcerogenic. Proc. Natl Acad. Sci. USA 91, 3228-3232 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3228-3232
    • Masferrer, J.L.1
  • 64
    • 0027944075 scopus 로고
    • Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain
    • Seibert, K. et al. Pharmacological and biochemical demonstration of the role of cyclooxygenase 2 in inflammation and pain. Proc. Natl Acad. Sci. USA 91, 12013-12017 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12013-12017
    • Seibert, K.1
  • 65
    • 0029888972 scopus 로고    scopus 로고
    • Selective inhibition of cyclooxygenase (COX)-2 reverses inflammation and expression of COX-2 and interleukin 6 in rat adjuvant arthritis
    • Anderson, G. D. et al. Selective inhibition of cyclooxygenase (COX)-2 reverses inflammation and expression of COX-2 and interleukin 6 in rat adjuvant arthritis. J. Clin. Invest. 97, 2672-2679 (1996).
    • (1996) J. Clin. Invest. , vol.97 , pp. 2672-2679
    • Anderson, G.D.1
  • 66
    • 13144260638 scopus 로고    scopus 로고
    • Pharmacological analysis of cyclooxygenase-1 in inflammation
    • Smith, C. J. et al. Pharmacological analysis of cyclooxygenase-1 in inflammation. Proc. Natl Acad. Sci. USA 95, 13313-13318 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13313-13318
    • Smith, C.J.1
  • 67
    • 0031473814 scopus 로고    scopus 로고
    • Inhibition of cyclooxygenase-2 rapidly reverses inflammatory hyperalgesia and prostaglandin E2 production
    • Zhang, Y., Shaffer, A., Portanova, J., Seibert, K. & Isakson, P. C. Inhibition of cyclooxygenase-2 rapidly reverses inflammatory hyperalgesia and prostaglandin E2 production. J. Pharmacol. Exp. Ther. 283, 1069-1075 (1997).
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 1069-1075
    • Zhang, Y.1    Shaffer, A.2    Portanova, J.3    Seibert, K.4    Isakson, P.C.5
  • 68
    • 0031808163 scopus 로고    scopus 로고
    • Effect of COX-1 and COX-2 inhibition on induction and maintenance of carrageenan-evoked thermal hyperalgesia in rats
    • Dirig, D. M., Isakson, P. C. & Yaksh, T. L. Effect of COX-1 and COX-2 inhibition on induction and maintenance of carrageenan-evoked thermal hyperalgesia in rats. J. Pharmacol. Exp. Ther. 285, 1031-1038 (1998).
    • (1998) J. Pharmacol. Exp. Ther. , vol.285 , pp. 1031-1038
    • Dirig, D.M.1    Isakson, P.C.2    Yaksh, T.L.3
  • 69
    • 0028830109 scopus 로고
    • Expression and selective inhibition of the constitutive and inducible forms of human cyclo-oxygenase
    • Gierse, J. K. et al. Expression and selective inhibition of the constitutive and inducible forms of human cyclo-oxygenase. Biochem. J. 305, 479-484 (1995).
    • (1995) Biochem. J. , vol.305 , pp. 479-484
    • Gierse, J.K.1
  • 70
    • 0028951334 scopus 로고
    • Selective inhibitors of COX-2
    • O'Neill, G. P. et al. Selective inhibitors of COX-2. Agents Actions Suppl. 46, 159-168 (1995).
    • (1995) Agents Actions Suppl. , vol.46 , pp. 159-168
    • O'Neill, G.P.1
  • 71
    • 0028009093 scopus 로고
    • The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1
    • Picot, D., Loll, P. J. & Garavito, R. M. The X-ray crystal structure of the membrane protein prostaglandin H2 synthase-1. Nature 367, 243-249 (1994).
    • (1994) Nature , vol.367 , pp. 243-249
    • Picot, D.1    Loll, P.J.2    Garavito, R.M.3
  • 72
    • 0030461132 scopus 로고    scopus 로고
    • Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents
    • Kurumbail, R. G. et al. Structural basis for selective inhibition of cyclooxygenase-2 by anti-inflammatory agents. Nature 384, 644-648 (1996).
    • (1996) Nature , vol.384 , pp. 644-648
    • Kurumbail, R.G.1
  • 73
    • 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. et al. 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. 271, 15810-15814 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 15810-15814
    • Gierse, J.K.1
  • 74
    • 0030783709 scopus 로고    scopus 로고
    • The interaction of arginine 106 of human prostaglandin G/H synthase-2 with inhibitors is not a universal component of inhibition mediated by nonsteroidal anti-inflammatory drugs
    • Greig, G. M. et al. The interaction of arginine 106 of human prostaglandin G/H synthase-2 with inhibitors is not a universal component of inhibition mediated by nonsteroidal anti-inflammatory drugs. Mol. Pharmacol. 52, 829-838 (1997).
    • (1997) Mol. Pharmacol. , vol.52 , pp. 829-838
    • Greig, G.M.1
  • 75
    • 0032489522 scopus 로고    scopus 로고
    • The dynamics of prostaglandin H synthases. Studies with prostaglandin h synthase 2 Y355F unmask mechanisms of time-dependent inhibition and allosteric activation
    • So, O. Y., Scarafia, L. E., Mak, A. Y., Callan, O. H. & Swinney, D. C. The dynamics of prostaglandin H synthases. Studies with prostaglandin h synthase 2 Y355F unmask mechanisms of time-dependent inhibition and allosteric activation. J. Biol. Chem. 273, 5801-5807 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 5801-5807
    • So, O.Y.1    Scarafia, L.E.2    Mak, A.Y.3    Callan, O.H.4    Swinney, D.C.5
  • 76
    • 0028139275 scopus 로고
    • Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase
    • Copeland, R. A. et al. Mechanism of selective inhibition of the inducible isoform of prostaglandin G/H synthase. Proc. Natl Acad. Sci. USA 91, 11202-11206 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11202-11206
    • Copeland, R.A.1
  • 81
    • 0029088821 scopus 로고
    • Etodolac selectively inhibits human prostaglandin G/H synthase 2 (PGHS-2) versus human PGHS-1
    • Glaser, K. et al. Etodolac selectively inhibits human prostaglandin G/H synthase 2 (PGHS-2) versus human PGHS-1. Eur. J. Pharmacol. 281, 107-111 (1995).
    • (1995) Eur. J. Pharmacol. , vol.281 , pp. 107-111
    • Glaser, K.1
  • 82
    • 0028846183 scopus 로고
    • Activity of nimesulide on constitutive and inducible cyclooxygenases
    • Tavares, I. A., Bishai, P. M. & Bennett, A. Activity of nimesulide on constitutive and inducible cyclooxygenases. Arzneimittelforschung 45, 1093-1095 (1995).
    • (1995) Arzneimittelforschung , vol.45 , pp. 1093-1095
    • Tavares, I.A.1    Bishai, P.M.2    Bennett, A.3
  • 83
    • 0028793984 scopus 로고
    • Effect of nimesulide action time dependence on selectivity towards prostaglandin G/H synthase/cyclooxygenase activity
    • Vago, T., Bevilacqua, M. & Norbiato, G. Effect of nimesulide action time dependence on selectivity towards prostaglandin G/H synthase/cyclooxygenase activity. Arzneimittelforschung 45, 1096-1098 (1995).
    • (1995) Arzneimittelforschung , vol.45 , pp. 1096-1098
    • Vago, T.1    Bevilacqua, M.2    Norbiato, G.3
  • 84
    • 0033594911 scopus 로고    scopus 로고
    • Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: A full in vitro analysis
    • Warner, T. D. et al. Nonsteroid drug selectivities for cyclo-oxygenase-1 rather than cyclo-oxygenase-2 are associated with human gastrointestinal toxicity: a full in vitro analysis. Proc. Natl Acad. Sci. USA 96, 7563-7568 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7563-7568
    • Warner, T.D.1
  • 85
    • 0028902109 scopus 로고
    • Characterization of inducible cyclooxygenase in rat brain
    • Breder, C. D., Dewitt, D. & Kraig, R. P. Characterization of inducible cyclooxygenase in rat brain. J. Comp. Neurol. 355, 296-315 (1995).
    • (1995) J. Comp. Neurol. , vol.355 , pp. 296-315
    • Breder, C.D.1    Dewitt, D.2    Kraig, R.P.3
  • 86
    • 0028846219 scopus 로고
    • Induction by lipopolysaccharide of cyclooxygenase-2 mRNA in rat brain; its possible role in the febrile response
    • Cao, C., Matsumura, K., Yamagata, K. & Watanabe, Y. Induction by lipopolysaccharide of cyclooxygenase-2 mRNA in rat brain; its possible role in the febrile response. Brain Res. 697, 187-196 (1995).
    • (1995) Brain Res. , vol.697 , pp. 187-196
    • Cao, C.1    Matsumura, K.2    Yamagata, K.3    Watanabe, Y.4
  • 87
    • 0028034970 scopus 로고
    • Cyclooxygenase-2 is associated with the macula densa of rat kidney and increases with salt restriction
    • Harris, R. C. et al. Cyclooxygenase-2 is associated with the macula densa of rat kidney and increases with salt restriction. J. Clin. Invest. 94, 2504-2510 (1994).
    • (1994) J. Clin. Invest. , vol.94 , pp. 2504-2510
    • Harris, R.C.1
  • 88
    • 0036830135 scopus 로고    scopus 로고
    • Effects of celecoxib and rofecoxib on blood pressure and edema in patients > or =65 years of age with systemic hypertension and osteoarthritis
    • Whelton, A., White, W. B., Bello, A. E., Puma, J. A. & Fort, J. G. Effects of celecoxib and rofecoxib on blood pressure and edema in patients > or =65 years of age with systemic hypertension and osteoarthritis. Am. J. Cardiol. 90, 959-963 (2002).
    • (2002) Am. J. Cardiol. , vol.90 , pp. 959-963
    • Whelton, A.1    White, W.B.2    Bello, A.E.3    Puma, J.A.4    Fort, J.G.5
  • 89
    • 0031420664 scopus 로고    scopus 로고
    • Induction of prostaglandin endoperoxide synthase-1 (COX-1) in a human promonocytic cell line by treatment with the differentiating agent TPA
    • Smith, C. J., Morrow, J. D., Roberts, L. J., 2nd & Marnett, F. J. Induction of prostaglandin endoperoxide synthase-1 (COX-1) in a human promonocytic cell line by treatment with the differentiating agent TPA. Adv. Exp. Med. Biol. 400A, 99-106 (1997).
    • (1997) Adv. Exp. Med. Biol. , vol.400 A , pp. 99-106
    • Smith, C.J.1    Morrow, J.D.2    Roberts II, L.J.3    Marnett, F.J.4
  • 90
    • 0028906162 scopus 로고
    • Mechanisms of mucosal injury and healing: The role of non-steroidal anti-inflammatory drugs
    • McCarthy, D. M. Mechanisms of mucosal injury and healing: the role of non-steroidal anti-inflammatory drugs, Scand. J. Gastroenterol. Suppl. 208, 24-29 (1995).
    • (1995) Scand. J. Gastroenterol. Suppl. , vol.208 , pp. 24-29
    • McCarthy, D.M.1
  • 91
    • 0032416415 scopus 로고    scopus 로고
    • Selective inhibitors of cyclooxygenase-2: Are they really effective, selective, and GI-safe?
    • Wallace, J. L., Reuter, B. K., McKnight, W. & Bak, A. Selective inhibitors of cyclooxygenase-2: are they really effective, selective, and GI-safe? J. Clin. Gastroenterol. 27 Suppl 1, S28-S34 (1998).
    • (1998) J. Clin. Gastroenterol. , vol.27 , Issue.SUPPL. 1
    • Wallace, J.L.1    Reuter, B.K.2    McKnight, W.3    Bak, A.4
  • 92
    • 0031884213 scopus 로고    scopus 로고
    • Effects of inhibition of prostaglandin endoperoxide synthase-2 in chronic gastrointestinal ulcer models in rats
    • Schmassmann, A. et al. Effects of inhibition of prostaglandin endoperoxide synthase-2 in chronic gastrointestinal ulcer models in rats. Br. J. Pharmacol. 123, 795-804 (1998).
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 795-804
    • Schmassmann, A.1
  • 93
    • 0032540132 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs may delay the repair of gastric mucosa by suppressing prostaglandin-mediated increase of hepatocyte growth factor production
    • Bamba, H., Ota, S., Kato, A. & Matsuzaki, F. Nonsteroidal anti-inflammatory drugs may delay the repair of gastric mucosa by suppressing prostaglandin-mediated increase of hepatocyte growth factor production. Biochem. Biophys. Res. Commun. 245, 567-571 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.245 , pp. 567-571
    • Bamba, H.1    Ota, S.2    Kato, A.3    Matsuzaki, F.4
  • 94
    • 0029347138 scopus 로고
    • Distribution of cyclooxygenase isoforms in murine chronic granulomatous inflammation. Implications for future anti-inflammatory therapy
    • Appleton, I., Tomlinson, A., Mitchell, J. A. & Willoughby, D. A. Distribution of cyclooxygenase isoforms in murine chronic granulomatous inflammation. Implications for future anti-inflammatory therapy. J. Pathol. 176, 413-420 (1995).
    • (1995) J. Pathol. , vol.176 , pp. 413-420
    • Appleton, I.1    Tomlinson, A.2    Mitchell, J.A.3    Willoughby, D.A.4
  • 95
    • 0033524421 scopus 로고    scopus 로고
    • Systemic biosynthesis of prostacyclin by cyclooxygenase (COX)-2: The human pharmacology of a selective inhibitor of COX-2
    • McAdam, B. F. et al. Systemic biosynthesis of prostacyclin by cyclooxygenase (COX)-2: the human pharmacology of a selective inhibitor of COX-2. Proc. Natl Acad. Sci. USA 96, 272-277 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 272-277
    • McAdam, B.F.1
  • 96
    • 0033851568 scopus 로고    scopus 로고
    • NSAID-induced gastric damage in rats: Requirement for inhibition of both cyclooxygenase 1 and 2
    • Wallace, J. L., McKnight, W., Reuter, B. K. & Vergnolle, N. NSAID-induced gastric damage in rats: requirement for inhibition of both cyclooxygenase 1 and 2. Gastroenterology 119, 706-714 (2000).
    • (2000) Gastroenterology , vol.119 , pp. 706-714
    • Wallace, J.L.1    McKnight, W.2    Reuter, B.K.3    Vergnolle, N.4
  • 97
    • 0036828285 scopus 로고    scopus 로고
    • 4 increases gastric resistance to aspirin-induced damage
    • 4 increases gastric resistance to aspirin-induced damage. Gastroenterology 123, 1598-1606 (2002).
    • (2002) Gastroenterology , vol.123 , pp. 1598-1606
    • Fiorucci, S.1
  • 98
    • 0030733305 scopus 로고    scopus 로고
    • Comparison of the cyclooxygenase-1 inhibitory properties of nonsteroidal anti-inflammatory drugs (NSAIDs) and selective COX-2 inhibitors, using sensitive microsomal and platelet assays
    • Riendeau, D. et al. Comparison of the cyclooxygenase-1 inhibitory properties of nonsteroidal anti-inflammatory drugs (NSAIDs) and selective COX-2 inhibitors, using sensitive microsomal and platelet assays. Can. J. Physiol. Pharmacol. 75, 1088-1095 (1997).
    • (1997) Can. J. Physiol. Pharmacol. , vol.75 , pp. 1088-1095
    • Riendeau, D.1
  • 100
    • 0001023001 scopus 로고    scopus 로고
    • Interpreting the clinical significance of the differential inhibition of cyclooxygenase-1 and cyclooxygenase-2
    • Brooks, P. et al. Interpreting the clinical significance of the differential inhibition of cyclooxygenase-1 and cyclooxygenase-2. Rheumatology (Oxford) 38, 779-788 (1999).
    • (1999) Rheumatology (Oxford) , vol.38 , pp. 779-788
    • Brooks, P.1
  • 101
    • 0027940487 scopus 로고
    • Biochemical and pharmacological characterization of the cyclooxygenase activity of human blood prostaglandin endoperoxide synthases
    • Patrignani, P. et al. Biochemical and pharmacological characterization of the cyclooxygenase activity of human blood prostaglandin endoperoxide synthases. J. Pharmacol. Exp. Ther. 271, 1705-1712 (1994).
    • (1994) J. Pharmacol. Exp. Ther. , vol.271 , pp. 1705-1712
    • Patrignani, P.1
  • 102
    • 0031034254 scopus 로고    scopus 로고
    • A classification of NSAIDs according to the relative inhibition of cyclooxygenase isoenzymes
    • Frolich, J. C. A classification of NSAIDs according to the relative inhibition of cyclooxygenase isoenzymes. Trends Pharmacol. Sci. 18, 30-34 (1997).
    • (1997) Trends Pharmacol. Sci. , vol.18 , pp. 30-34
    • Frolich, J.C.1
  • 103
    • 0034699923 scopus 로고    scopus 로고
    • Nomenclature for COX-2 inhibitors
    • Vane, J. R. & Warner, T. D. Nomenclature for COX-2 inhibitors. Lancet 356, 1373-1374 (2000).
    • (2000) Lancet , vol.356 , pp. 1373-1374
    • Vane, J.R.1    Warner, T.D.2
  • 104
    • 0034707105 scopus 로고    scopus 로고
    • Comparison of upper gastrointestinal toxicity of rofecoxib and naproxen in patients with rheumatoid arthritis
    • VIGOR Study Group 2 p following 1528
    • Bombardier, C. et al. Comparison of upper gastrointestinal toxicity of rofecoxib and naproxen in patients with rheumatoid arthritis. VIGOR Study Group. N. Engl. J. Med. 343, 1520-1528, 2 p following 1528 (2000).
    • (2000) N. Engl. J. Med. , vol.343 , pp. 1520-1528
    • Bombardier, C.1
  • 105
    • 0034644396 scopus 로고    scopus 로고
    • Gastrointestinal toxicity with celecoxib vs nonsteroidal anti-inflammatory drugs for osteoarthritis and rheumatoid arthritis: The CLASS study: A randomized controlled trial. Celecoxib Long-term Arthritis Safety Study
    • Silverstein, F. E. et al. Gastrointestinal toxicity with celecoxib vs nonsteroidal anti-inflammatory drugs for osteoarthritis and rheumatoid arthritis: the CLASS study: A randomized controlled trial. Celecoxib Long-term Arthritis Safety Study. JAMA 284, 1247-1255 (2000).
    • (2000) JAMA , vol.284 , pp. 1247-1255
    • Silverstein, F.E.1
  • 106
    • 0035833502 scopus 로고    scopus 로고
    • The coxibs, selective inhibitors of cyclooxygenase-2
    • FitzGerald, G. A. & Patrono, C. The coxibs, selective inhibitors of cyclooxygenase-2. N. Engl. J. Med. 345, 433-442 (2001).
    • (2001) N. Engl. J. Med. , vol.345 , pp. 433-442
    • FitzGerald, G.A.1    Patrono, C.2
  • 107
    • 0015421059 scopus 로고
    • Inhibition of prostaglandin synthesis in man
    • Hamberg, M. Inhibition of prostaglandin synthesis in man. Biochem. Biophys. Res. Commun. 49, 720-726 (1972).
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 720-726
    • Hamberg, M.1
  • 108
    • 0033943280 scopus 로고    scopus 로고
    • Salicylate metabolites inhibit cyclooxygenase-2-dependent prostaglandin E(2) synthesis in murine macrophages
    • Hinz, B., Kraus, V., Pahl, A. & Brune, K. Salicylate metabolites inhibit cyclooxygenase-2-dependent prostaglandin E(2) synthesis in murine macrophages. Biochem. Biophys. Res. Commun. 274, 197-202 (2000).
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 197-202
    • Hinz, B.1    Kraus, V.2    Pahl, A.3    Brune, K.4
  • 109
    • 0029870463 scopus 로고    scopus 로고
    • Salicylates inhibit I kappa B-alpha phosphorylation, endothelial-leukocyte adhesion molecule expression, and neutrophil transmigration
    • Pierce, J. W., Read, M. A., Ding, H., Luscinskas, F. W. & Collins, T. Salicylates inhibit I kappa B-alpha phosphorylation, endothelial-leukocyte adhesion molecule expression, and neutrophil transmigration. J. Immunol. 156, 3961-3969 (1996).
    • (1996) J. Immunol. , vol.156 , pp. 3961-3969
    • Pierce, J.W.1    Read, M.A.2    Ding, H.3    Luscinskas, F.W.4    Collins, T.5
  • 110
    • 17144462683 scopus 로고    scopus 로고
    • Inhibition of cyclooxygenase-2 expression by 4-trifluoromethyl derivatives of salicylate, triflusal, and its deacetylated metabolite, 2-hydroxy-4-trifluoromethylbenzoic acid
    • Fernandez de Arriba, A. et al. Inhibition of cyclooxygenase-2 expression by 4-trifluoromethyl derivatives of salicylate, triflusal, and its deacetylated metabolite, 2-hydroxy-4-trifluoromethylbenzoic acid. Mol. Pharmacol. 55, 753-760 (1999).
    • (1999) Mol. Pharmacol. , vol.55 , pp. 753-760
    • Fernandez de Arriba, A.1
  • 111
    • 0033609144 scopus 로고    scopus 로고
    • Suppression of inducible cyclooxygenase 2 gene transcription by aspirin and sodium salicylate
    • Xu, X. M. et al. Suppression of inducible cyclooxygenase 2 gene transcription by aspirin and sodium salicylate. Proc. Natl Acad. Sci. USA 96, 5292-5297 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5292-5297
    • Xu, X.M.1
  • 112
    • 0030001631 scopus 로고    scopus 로고
    • Salicylate or aspirin inhibits the induction of the inducible nitric oxide synthase in rat cardiac fibroblasts
    • Farivar, R. S., Chobanian, A. V. & Brecher, F. Salicylate or aspirin inhibits the induction of the inducible nitric oxide synthase in rat cardiac fibroblasts. Circ. Res. 78, 759-768 (1996).
    • (1996) Circ. Res. , vol.78 , pp. 759-768
    • Farivar, R.S.1    Chobanian, A.V.2    Brecher, F.3
  • 113
    • 0030976878 scopus 로고    scopus 로고
    • Sodium salicylate inhibits cyclo-oxygenase-2 activity independently of transcription factor (nuclear factor kappaB) activation: Role of arachidonic acid
    • Mitchell, J. A., Saunders, M., Barnes, P. J., Newton, R. & Belvisi, M. G. Sodium salicylate inhibits cyclo-oxygenase-2 activity independently of transcription factor (nuclear factor kappaB) activation: role of arachidonic acid. Mol. Pharmacol. 51, 907-912 (1997).
    • (1997) Mol. Pharmacol. , vol.51 , pp. 907-912
    • Mitchell, J.A.1    Saunders, M.2    Barnes, P.J.3    Newton, R.4    Belvisi, M.G.5
  • 114
    • 0032564358 scopus 로고    scopus 로고
    • Modes of action of aspirin-like drugs: Salicylates inhibit erk activation and integrin-dependent neutrophil adhesion
    • Pillinger, M. H. et al. Modes of action of aspirin-like drugs: salicylates inhibit erk activation and integrin-dependent neutrophil adhesion. Proc. Natl Acad. Sci. USA 95, 14540-14545 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14540-14545
    • Pillinger, M.H.1
  • 115
    • 0032978740 scopus 로고    scopus 로고
    • Cell-type-specific activation of c-Jun N-terminal kinase by salicylates
    • Schwenger, P., Alpert, D., Skolnik, E. Y. & Vilcek, J. Cell-type-specific activation of c-Jun N-terminal kinase by salicylates. J. Cell Physiol. 179, 109-114 (1999).
    • (1999) J. Cell Physiol. , vol.179 , pp. 109-114
    • Schwenger, P.1    Alpert, D.2    Skolnik, E.Y.3    Vilcek, J.4
  • 116
    • 0033166175 scopus 로고    scopus 로고
    • Sites of action for future therapy: An adenosine-dependent mechanism by which aspirin retains its anti-inflammatory activity in cyclooxygenase-2 and NFκB knockout mice
    • Cronstein B. N., Montesinos, M. C. & Weissmann, G. Sites of action for future therapy: an adenosine-dependent mechanism by which aspirin retains its anti-inflammatory activity in cyclooxygenase-2 and NFκB knockout mice. Osteoarthritis Cartilage 7, 361-363 (1999).
    • (1999) Osteoarthritis Cartilage , vol.7 , pp. 361-363
    • Cronstein, B.N.1    Montesinos, M.C.2    Weissmann, G.3
  • 117
    • 0032992467 scopus 로고    scopus 로고
    • Salicylates and sulfasalazine, but not glucocorticoids, inhibit leukocyte accumulation by an adenosine-dependent mechanism that is independent of inhibition of prostaglandin synthesis and p105 of NFκB
    • Cronstein, B. N., Montesinos, M. C. & Weissmann, G. Salicylates and sulfasalazine, but not glucocorticoids, inhibit leukocyte accumulation by an adenosine-dependent mechanism that is independent of inhibition of prostaglandin synthesis and p105 of NFκB. Proc. Natl Acad. Sci. USA 96, 6377-6381 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6377-6381
    • Cronstein, B.N.1    Montesinos, M.C.2    Weissmann, G.3
  • 118
    • 0034725721 scopus 로고    scopus 로고
    • Treatment of low back pain exacerbations with willow bark extract: A randomized double-blind study
    • Chrubasik, S. et al. Treatment of low back pain exacerbations with willow bark extract: a randomized double-blind study. Am. J. Med. 109, 9-14 (2000).
    • (2000) Am. J. Med. , vol.109 , pp. 9-14
    • Chrubasik, S.1
  • 119
    • 0033013466 scopus 로고    scopus 로고
    • Induction of an Acetaminophen-sensitive cyclooxygenase with reduced sensitivity to nonsteroid anti-inflammatory drugs
    • Simmons, D. L., Botting, R. M., Robertson, P. M., Madsen, M. L. & Vane, J. R. Induction of an Acetaminophen-sensitive cyclooxygenase with reduced sensitivity to nonsteroid anti-inflammatory drugs. Proc. Natl Acad. Sci. USA 96, 3275-3280 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3275-3280
    • Simmons, D.L.1    Botting, R.M.2    Robertson, P.M.3    Madsen, M.L.4    Vane, J.R.5
  • 120
    • 0034458153 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs, acetaminophen, cyclooxygenase 2, and fever
    • Simmons, D. L., Wagner, D. & Westover, K. Nonsteroidal anti-inflammatory drugs, acetaminophen, cyclooxygenase 2, and fever. Clin. Infect. Dis. 31 Suppl 5, S211-S218 (2000).
    • (2000) Clin. Infect. Dis. , vol.31 , Issue.SUPPL. 5
    • Simmons, D.L.1    Wagner, D.2    Westover, K.3
  • 121
    • 0032753154 scopus 로고    scopus 로고
    • Non-steroidal anti-inflammatory drugs: Back to the future
    • Flower, R. J. Non-steroidal anti-inflammatory drugs: back to the future. Rheumatology (Oxford) 38, 693-696 (1999).
    • (1999) Rheumatology (Oxford) , vol.38 , pp. 693-696
    • Flower, R.J.1
  • 122
    • 0034457719 scopus 로고    scopus 로고
    • Mechanism of action of acetaminophen: Is there a cyclooxygenase 3?
    • Botting R. M. Mechanism of action of acetaminophen: is there a cyclooxygenase 3? Clin. Infect. Dis. 31 Suppl 5, S202-S210 (2000).
    • (2000) Clin. Infect. Dis. , vol.31 , Issue.SUPPL. 5
    • Botting, R.M.1
  • 123
    • 0034685192 scopus 로고    scopus 로고
    • COX-1, COX-2, and COX-3 and the future treatment of chronic inflammatory disease
    • Willoughby, D. A., Moore, A. R. & Colville-Nash, P. R. COX-1, COX-2, and COX-3 and the future treatment of chronic inflammatory disease. Lancet 355, 646-648 (2000).
    • (2000) Lancet , vol.355 , pp. 646-648
    • Willoughby, D.A.1    Moore, A.R.2    Colville-Nash, P.R.3
  • 124
    • 0037108979 scopus 로고    scopus 로고
    • COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other analgesic/antipyretic drugs: Cloning, structure, and expression
    • Chandrasekharan, N. V. et al. COX-3, a cyclooxygenase-1 variant inhibited by acetaminophen and other analgesic/antipyretic drugs: cloning, structure, and expression. Proc. Natl Acad. Sci. USA 99, 13926-13931 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13926-13931
    • Chandrasekharan, N.V.1
  • 125
    • 0036124437 scopus 로고    scopus 로고
    • Involvement of peripheral cyclooxygenase-1 and cyclooxygenase-2 in inflammatory pain
    • Martinez, R. V. at al. Involvement of peripheral cyclooxygenase-1 and cyclooxygenase-2 in inflammatory pain. J. Pharm. Pharmacol. 54, 405-412 (2002).
    • (2002) J. Pharm. Pharmacol. , vol.54 , pp. 405-412
    • Martinez, R.V.1
  • 126
    • 0034629473 scopus 로고    scopus 로고
    • The analgesic effect profile of FR122047, a selective cyclooxygenase-1 inhibitor, in chemical nociceptive models
    • Ochi, T., Motoyama, Y. & Goto, T. The analgesic effect profile of FR122047, a selective cyclooxygenase-1 inhibitor, in chemical nociceptive models. Eur. J. Pharmacol. 391, 49-54 (2000).
    • (2000) Eur. J. Pharmacol. , vol.391 , pp. 49-54
    • Ochi, T.1    Motoyama, Y.2    Goto, T.3
  • 127
    • 0033051086 scopus 로고    scopus 로고
    • Cyclooxygenase-2 inhibition by rofecoxib reverses naturally occurring fever in humans
    • Schwartz, J. I. et al. Cyclooxygenase-2 inhibition by rofecoxib reverses naturally occurring fever in humans. Clin. Pharmacol. Ther. 65, 653-660 (1999).
    • (1999) Clin. Pharmacol. Ther. , vol.65 , pp. 653-660
    • Schwartz, J.I.1
  • 128
    • 0033577548 scopus 로고    scopus 로고
    • The febrile response to lipopolysaccharide is blocked in cyclooxygenase-2(-/-), but not in cyclooxygonase-1(-/-) mice
    • Li, S. et al. The febrile response to lipopolysaccharide is blocked in cyclooxygenase-2(-/-), but not in cyclooxygonase-1(-/-) mice. Brain Res. 825, 86-94 (1999).
    • (1999) Brain Res. , vol.825 , pp. 86-94
    • Li, S.1
  • 129
    • 0037076347 scopus 로고    scopus 로고
    • Determinants of the cellular specificity of acetaminophen as an inhibitor of prostaglandin H(2) synthases
    • Boutaud, O., Aronoff, D. M., Richardson, J. H., Marnett, L. J. & Oates, J. A. Determinants of the cellular specificity of acetaminophen as an inhibitor of prostaglandin H(2) synthases. Proc. Natl Acad. Sci. USA 99, 7130-7135 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7130-7135
    • Boutaud, O.1    Aronoff, D.M.2    Richardson, J.H.3    Marnett, L.J.4    Oates, J.A.5
  • 130
    • 0035866579 scopus 로고    scopus 로고
    • Mechanism of acetaminophen inhibition of cyclooxygenase isoforms
    • Ouellet, M. & Percival, M. D. Mechanism of acetaminophen inhibition of cyclooxygenase isoforms. Arch. Biochem. Biophys. 387, 273-280 (2001).
    • (2001) Arch. Biochem. Biophys. , vol.387 , pp. 273-280
    • Ouellet, M.1    Percival, M.D.2
  • 131
    • 13344261416 scopus 로고    scopus 로고
    • Diarylspiro[2. 4]heptenes as orally active, highly selective cyclooxygenase-2 inhibitors: Synthesis and structure-activity relationships
    • Huang, H. C. et al. Diarylspiro[2. 4]heptenes as orally active, highly selective cyclooxygenase-2 inhibitors: synthesis and structure-activity relationships. J. Med. Chem. 39, 253-266 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 253-266
    • Huang, H.C.1
  • 132
    • 15844425962 scopus 로고    scopus 로고
    • Novel terphenyls as selective cyclooxygenase-2 inhibitors and orally active anti-inflammatory agents
    • Li, J. J. et al. Novel terphenyls as selective cyclooxygenase-2 inhibitors and orally active anti-inflammatory agents. J. Med. Chem. 39, 1846-1856 (1996).
    • (1996) J. Med. Chem. , vol.39 , pp. 1846-1856
    • Li, J.J.1
  • 133
    • 8244255009 scopus 로고    scopus 로고
    • Biochemical and pharmacological profile of a tetrasubstituted furanone as a highly selective COX-2 inhibitor
    • Riendeau, D. et al. Biochemical and pharmacological profile of a tetrasubstituted furanone as a highly selective COX-2 inhibitor. Br. J. Pharmacol. 121, 105-117 (1997).
    • (1997) Br. J. Pharmacol. , vol.121 , pp. 105-117
    • Riendeau, D.1
  • 134
    • 0032557710 scopus 로고    scopus 로고
    • Aspirin-like molecules that covalently inactivate cyclooxygenase-2
    • Kalgutkar, A. S. et al. Aspirin-like molecules that covalently inactivate cyclooxygenase-2. Science 280, 1268-1270 (1998).
    • (1998) Science , vol.280 , pp. 1268-1270
    • Kalgutkar, A.S.1
  • 135
    • 0032548140 scopus 로고    scopus 로고
    • Covalent modification of cyclooxygenase-2 (COX-2) by 2-acetoxyphenyl alkyl sulfides, a new class of selective COX-2 inactivators
    • Kalgutkar, A. S., Kozak, K. R., Crews, B. C., Hochgesang, G. P. Jr & Marnett, L. J. Covalent modification of cyclooxygenase-2 (COX-2) by 2-acetoxyphenyl alkyl sulfides, a new class of selective COX-2 inactivators. J. Med. Chem. 41, 4800-4818 (1998).
    • (1998) J. Med. Chem. , vol.41 , pp. 4800-4818
    • Kalgutkar, A.S.1    Kozak, K.R.2    Crews, B.C.3    Hochgesang Jr., G.P.4    Marnett, L.J.5
  • 136
    • 0034681109 scopus 로고    scopus 로고
    • Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: Facile conversion of nonsteroidal anti-inflammatory drugs to potent and highly selective COX-2 inhibitors
    • Kalgutkar, A. S. et al. Biochemically based design of cyclooxygenase-2 (COX-2) inhibitors: facile conversion of nonsteroidal anti-inflammatory drugs to potent and highly selective COX-2 inhibitors. Proc. Natl Acad. Sci. USA 97, 925-930 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 925-930
    • Kalgutkar, A.S.1
  • 137
    • 0034721194 scopus 로고    scopus 로고
    • Ester and amide derivatives of the nonsteroidal anti-inflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors
    • Kalgutkar, A. S., Marnett, A. B., Crews, B. C., Remmel, R. P. & Marnett, F. J. Ester and amide derivatives of the nonsteroidal anti-inflammatory drug, indomethacin, as selective cyclooxygenase-2 inhibitors. J. Med. Chem. 43, 2860-2870 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 2860-2870
    • Kalgutkar, A.S.1    Marnett, A.B.2    Crews, B.C.3    Remmel, R.P.4    Marnett, F.J.5
  • 138
    • 0030299879 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs, eicosanoids, and colorectal cancer prevention
    • DuBois, R. N., Giardiello, F. M. & Smalley, W. E. Nonsteroidal anti-inflammatory drugs, eicosanoids, and colorectal cancer prevention. Gastroenterol. Clin. North Am. 25, 773-791 (1996).
    • (1996) Gastroenterol. Clin. North Am. , vol.25 , pp. 773-791
    • DuBois, R.N.1    Giardiello, F.M.2    Smalley, W.E.3
  • 139
    • 17744418769 scopus 로고    scopus 로고
    • The effect of celecoxib, a cyclooxygenase-2 inhibitor, in familial adenomatous polyposis
    • Steinbach, G. et al. The effect of celecoxib, a cyclooxygenase-2 inhibitor, in familial adenomatous polyposis. N. Engl. J. Med. 342, 1946-1952 (2000).
    • (2000) N. Engl. J. Med. , vol.342 , pp. 1946-1952
    • Steinbach, G.1
  • 140
    • 0030897133 scopus 로고    scopus 로고
    • Risk of Alzheimer's disease and duration of NSAID use
    • Stewart, W. F., Kawas, C., Corrada, M. & Metter, E. J. Risk of Alzheimer's disease and duration of NSAID use. Neurology 48, 626-632 (1997).
    • (1997) Neurology , vol.48 , pp. 626-632
    • Stewart, W.F.1    Kawas, C.2    Corrada, M.3    Metter, E.J.4
  • 141
    • 0032551633 scopus 로고    scopus 로고
    • Cyclooxygenase-2 expression is increased in frontal cortex of Alzheimer's disease brain
    • Pasinetti, G. M. & Aisen, P. S. Cyclooxygenase-2 expression is increased in frontal cortex of Alzheimer's disease brain. Neuroscience 87, 319-324 (1998).
    • (1998) Neuroscience , vol.87 , pp. 319-324
    • Pasinetti, G.M.1    Aisen, P.S.2
  • 142
    • 0029911267 scopus 로고    scopus 로고
    • Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2
    • Luong, C. et al. Flexibility of the NSAID binding site in the structure of human cyclooxygenase-2. Nature Struct. Biol. 3, 927-933 (1996).
    • (1996) Nature Struct. Biol. , vol.3 , pp. 927-933
    • Luong, C.1
  • 143
    • 0037078983 scopus 로고    scopus 로고
    • Lipid signals in pain control
    • Bazan, N. & Flower, R. Lipid signals in pain control. Nature 420, 135-138 (2002).
    • (2002) Nature , vol.420 , pp. 135-138
    • Bazan, N.1    Flower, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.