메뉴 건너뛰기




Volumn 3, Issue 5, 2004, Pages 401-416

Inflammatory resolution: New opportunities for drug discovery

Author keywords

[No Author keywords available]

Indexed keywords

3 [2 [(2 TERT BUTYLPHENYLAMINOOXALYL)AMINO]PROPIONYLAMINO] 4 OXO 5 (2,3,5,6 TETRAFLUOROPHENOXY)PENTANOIC ACID; ACETYLSALICYLIC ACID; ANTIINFLAMMATORY AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BRADYKININ; CASPASE INHIBITOR; CD40 LIGAND MONOCLONAL ANTIBODY; CELL ADHESION MOLECULE; COBROTOXIN; CYCLOSPORIN A; CYTOCHROME P450; CYTOKINE; DELTA12 PROSTAGLANDIN J2; FIBRONECTIN; GLUCOCORTICOID; HEME OXYGENASE 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LEUKOTRIENE; LIPOCORTIN 1; LIPOXIN A; LIPOXIN B; METHOTREXATE; NONSTEROID ANTIINFLAMMATORY AGENT; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PROSTAGLANDIN D2; PROSTAGLANDIN J2; SALAZOSULFAPYRIDINE; SUBSTANCE P; TACROLIMUS; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 2442445450     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1383     Document Type: Review
Times cited : (669)

References (151)
  • 4
    • 0000915343 scopus 로고
    • The production of arthritis in rabbits by an immunological reaction to fibrin
    • Dumonde, D. C. & Glynn, L. E. The production of arthritis in rabbits by an immunological reaction to fibrin. Br. J. Exp. Pathol. 43, 373 (1962).
    • (1962) Br. J. Exp. Pathol. , vol.43 , pp. 373
    • Dumonde, D.C.1    Glynn, L.E.2
  • 5
    • 0013803781 scopus 로고
    • The reaction of guinea-pigs to autologous and heterologous fibrin implants
    • Dumonde, D. C. & Glynn, L. E. The reaction of guinea-pigs to autologous and heterologous fibrin implants. J. Pathol. Bacteriol. 90, 649-657 (1965).
    • (1965) J. Pathol. Bacteriol. , vol.90 , pp. 649-657
    • Dumonde, D.C.1    Glynn, L.E.2
  • 6
    • 0345210507 scopus 로고
    • Studies on lysozymes. VII. Acute and chronic arthritis produced by intra-articular injections of streptolysin 'S' in rabbits
    • Weissmann, G., Becher G., Wiedermann, G. & Bernheimer, A. W. Studies on lysozymes. VII. Acute and chronic arthritis produced by intra-articular injections of streptolysin 'S' in rabbits. Am. J. Pathol. 46, 129 (1965).
    • (1965) Am. J. Pathol. , vol.46 , pp. 129
    • Weissmann, G.1    Becher, G.2    Wiedermann, G.3    Bernheimer, A.W.4
  • 7
    • 0014810625 scopus 로고
    • Evidence for a possible endogenous antigen in chronic inflammation
    • Willoughby, D. A. & Ryan, G. B. Evidence for a possible endogenous antigen in chronic inflammation. J. Pathol. 101, 233-239 (1970).
    • (1970) J. Pathol. , vol.101 , pp. 233-239
    • Willoughby, D.A.1    Ryan, G.B.2
  • 8
    • 0034944221 scopus 로고    scopus 로고
    • Recommendations for the prevention and treatment of glucocorticoid-induced osteoporosis: 2001 update. Amercan College of Rheumatology Ad Hoc Committee on Glucocoritcoid-Induced Osteoporosis
    • Recommendations for the prevention and treatment of glucocorticoid-induced osteoporosis: 2001 update. Amercan College of Rheumatology Ad Hoc Committee on Glucocoritcoid-Induced Osteoporosis. Arthritis Rheum. 44, 1496-1503 (2001).
    • (2001) Arthritis Rheum. , vol.44 , pp. 1496-1503
  • 9
    • 0033628284 scopus 로고    scopus 로고
    • Glucocorticoid-regulated gene expression during cutaneous wound repair
    • Beer H. D., Fassler, R. & Werner, S. Glucocorticoid-regulated gene expression during cutaneous wound repair. Vitam. Horm. 59, 217-239 (2000).
    • (2000) Vitam. Horm. , vol.59 , pp. 217-239
    • Beer, H.D.1    Fassler, R.2    Werner, S.3
  • 10
    • 0036496843 scopus 로고    scopus 로고
    • Selective cyclooxygenase-2 (COX-2) inhibitors and potential risk of cardiovascular events
    • Mukherjee, D. Selective cyclooxygenase-2 (COX-2) inhibitors and potential risk of cardiovascular events. Biochem. Pharmacol. 63, 817-821 (2002).
    • (2002) Biochem. Pharmacol. , vol.63 , pp. 817-821
    • Mukherjee, D.1
  • 11
    • 0036401088 scopus 로고    scopus 로고
    • Side effects of anti-TNF therapy: Current knowledge
    • Antoni, C. & Braun, J. Side effects of anti-TNF therapy: current knowledge. Clin. Exp. Rheumatol. 20, S152-S157 (2002).
    • (2002) Clin. Exp. Rheumatol. , vol.20
    • Antoni, C.1    Braun, J.2
  • 12
    • 0033627825 scopus 로고    scopus 로고
    • Prostaglandin D synthase: Structure and function
    • Urade, Y. & Hayaishi, O. Prostaglandin D synthase: structure and function. Vitam. Horm. 58, 89-120 (2000).
    • (2000) Vitam. Horm. , vol.58 , pp. 89-120
    • Urade, Y.1    Hayaishi, O.2
  • 13
    • 0035053973 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins: New insights on biological activities and cellular targets
    • Straus, D. S. & Glass, C. K. Cyclopentenone prostaglandins: new insights on biological activities and cellular targets. Med. Res. Rev. 21, 185-210 (2001).
    • (2001) Med. Res. Rev. , vol.21 , pp. 185-210
    • Straus, D.S.1    Glass, C.K.2
  • 14
    • 0031888958 scopus 로고    scopus 로고
    • PPAR-gamma agonists inhibit production of monocyte inflammatory cytokines
    • Jiang, C., Ting, A. T. & Seed, B. PPAR-gamma agonists inhibit production of monocyte inflammatory cytokines. Nature 391, 82-86 (1998).
    • (1998) Nature , vol.391 , pp. 82-86
    • Jiang, C.1    Ting, A.T.2    Seed, B.3
  • 15
    • 0031886864 scopus 로고    scopus 로고
    • The peroxisome proliferator-activated receptor-gamma is a negative regulator of macrophage activation
    • Ricote, M., Li, A. C., Willson, T. M., Kelly, C. J. & Glass, C. K. The peroxisome proliferator-activated receptor-gamma is a negative regulator of macrophage activation. Nature 391, 79-82 (1998).
    • (1998) Nature , vol.391 , pp. 79-82
    • Ricote, M.1    Li, A.C.2    Willson, T.M.3    Kelly, C.J.4    Glass, C.K.5
  • 16
    • 0036010555 scopus 로고    scopus 로고
    • Natural ligands of PPARgamma: Are prostaglandin J(2) derivatives really playing the part?
    • Nosjean, O. & Boutin, J. A. Natural ligands of PPARgamma: are prostaglandin J(2) derivatives really playing the part? Cell Signal. 14, 573-583 (2002).
    • (2002) Cell Signal. , vol.14 , pp. 573-583
    • Nosjean, O.1    Boutin, J.A.2
  • 17
    • 0034712933 scopus 로고    scopus 로고
    • 15-deoxy-delta 12,14-prostaglandin J2 inhibits multiple steps in the NF-kappa B signaling pathway
    • Straus, D. S. et al. 15-deoxy-delta 12,14-prostaglandin J2 inhibits multiple steps in the NF-kappa B signaling pathway. Proc. Natl Acad. Sci. USA 97, 4844-4849 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4844-4849
    • Straus, D.S.1
  • 18
    • 0346435097 scopus 로고    scopus 로고
    • Molecular basis for the direct inhibition of AP-1 DNA binding by 15-deoxy-Delta 12,14-prostaglandin J2
    • Perez-Sala, D., Cernuda-Morollon, E. & Canada, F. J. Molecular basis for the direct inhibition of AP-1 DNA binding by 15-deoxy-Delta 12,14-prostaglandin J2. J. Biol. Chem. 278, 51251-51260 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51251-51260
    • Perez-Sala, D.1    Cernuda-Morollon, E.2    Canada, F.J.3
  • 19
    • 0038448230 scopus 로고    scopus 로고
    • Inhibition of IFN-gamma-mediated inducible nitric oxide synthase induction by the peroxisome proliferator-activated receptor gamma agonist, 15-deoxy-delta 12, 14-prostaglandin J2, involves inhibition of the upstream Janus kinase/STAT1 signaling pathway
    • Chen, C. W., Chang, Y. H., Tsi, C. J. & Lin, W. W. Inhibition of IFN-gamma-mediated inducible nitric oxide synthase induction by the peroxisome proliferator-activated receptor gamma agonist, 15-deoxy-delta 12, 14-prostaglandin J2, involves inhibition of the upstream Janus kinase/STAT1 signaling pathway. J. Immunol. 171, 970-988 (2003).
    • (2003) J. Immunol. , vol.171 , pp. 970-988
    • Chen, C.W.1    Chang, Y.H.2    Tsi, C.J.3    Lin, W.W.4
  • 20
    • 0343415083 scopus 로고    scopus 로고
    • Anti-inflammatory actions of 15-deoxy-delta 12,14-prostaglandin J2 and troglitazone: Evidence for heat shock-dependent and-independent inhibition of cytokine-induced inducible nitric oxide synthase expression
    • Maggi, L. B. Jr et al. Anti-inflammatory actions of 15-deoxy-delta 12,14-prostaglandin J2 and troglitazone: evidence for heat shock-dependent and-independent inhibition of cytokine-induced inducible nitric oxide synthase expression. Diabetes 49, 346-355 (2000).
    • (2000) Diabetes , vol.49 , pp. 346-355
    • Maggi Jr., L.B.1
  • 21
    • 0033551134 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins suppress activation of microglia: Down-regulation of inducible nitric-oxide synthase by 15-deoxy-Delta 12,14-prostaglandin J2
    • Petrova, T. V., Akama, K. T. & Van Eldik, L. J. Cyclopentenone prostaglandins suppress activation of microglia: down-regulation of inducible nitric-oxide synthase by 15-deoxy-Delta 12,14-prostaglandin J2. Proc. Natl Acad. Sci. USA 96, 4668-4673 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4668-4673
    • Petrova, T.V.1    Akama, K.T.2    Van Eldik, L.J.3
  • 22
    • 0033944415 scopus 로고    scopus 로고
    • Role of the peroxisome proliferator-activated receptor-gamma (PPAR-gamma) and its natural ligand 15-deoxy-Delta 12, 14-prostaglandin J2 in the regulation of microglial functions
    • Bernardo, A., Levi, G. & Minghetti, L. Role of the peroxisome proliferator-activated receptor-gamma (PPAR-gamma) and its natural ligand 15-deoxy-Delta 12, 14-prostaglandin J2 in the regulation of microglial functions. Eur. J. Neurosci. 12, 2215-2223 (2000).
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 2215-2223
    • Bernardo, A.1    Levi, G.2    Minghetti, L.3
  • 23
    • 0037988825 scopus 로고    scopus 로고
    • Prostaglandin D2 affects the maturation of human monocyte-derived dendritic cells: Consequence on the polarization of naive Th cells
    • Gosset, P. et al. Prostaglandin D2 affects the maturation of human monocyte-derived dendritic cells: consequence on the polarization of naive Th cells. J. Immunol. 170, 494349-494362 (2003).
    • (2003) J. Immunol. , vol.170 , pp. 494349-494362
    • Gosset, P.1
  • 24
    • 0032847680 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor activators target human endothelial cells to inhibit leukocyte-endothelial cell interaction
    • Jackson, S. M. et al. Peroxisome proliferator-activated receptor activators target human endothelial cells to inhibit leukocyte-endothelial cell interaction. Arterioscler. Thromb. Vasc. Biol. 19, 2094-2104 (1999).
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2094-2104
    • Jackson, S.M.1
  • 25
    • 0034711678 scopus 로고    scopus 로고
    • Modulation of vascular inflammation in vitro and in vivo by peroxisome proliferator-activated receptor-gamma activators
    • Pasceri, V., Wu, H. D., Willerson, J. T. & Yeh, E. T. Modulation of vascular inflammation in vitro and in vivo by peroxisome proliferator-activated receptor-gamma activators. Circulation 101, 235-238 (2000).
    • (2000) Circulation , vol.101 , pp. 235-238
    • Pasceri, V.1    Wu, H.D.2    Willerson, J.T.3    Yeh, E.T.4
  • 26
    • 0035876919 scopus 로고    scopus 로고
    • Differential regulation of chemokine gene expression by 15-deoxy-delta 12,14 prostaglandin J2
    • Zhang, X., Wang, J. M., Gong, W. H., Mukaida, N. & Young, H. A. Differential regulation of chemokine gene expression by 15-deoxy-delta 12,14 prostaglandin J2. J. Immunol. 166, 7104-7111 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 7104-7111
    • Zhang, X.1    Wang, J.M.2    Gong, W.H.3    Mukaida, N.4    Young, H.A.5
  • 27
    • 0037903144 scopus 로고    scopus 로고
    • Suppression of endothelial adhesion molecule up-regulation with cyclopentenone prostaglandins is dissociated from IkappaB-alpha kinase inhibition and cell death induction
    • Zernecke, A., Erl, W., Fraemohs, L., Lietz, M. & Weber, C. Suppression of endothelial adhesion molecule up-regulation with cyclopentenone prostaglandins is dissociated from IkappaB-alpha kinase inhibition and cell death induction. FASEB J. 17, 1099-1101 (2003).
    • (2003) FASEB J. , vol.17 , pp. 1099-1101
    • Zernecke, A.1    Erl, W.2    Fraemohs, L.3    Lietz, M.4    Weber, C.5
  • 28
    • 0031667976 scopus 로고    scopus 로고
    • Differential effects of inhibitors of cydooxygenase (cyclooxygenase 1 and cyclooxygenase 2) in acute inflammation
    • Gilroy, D. W., Tomlinson, A. & Willoughby D. A. Differential effects of inhibitors of cydooxygenase (cyclooxygenase 1 and cyclooxygenase 2) in acute inflammation. Eur. J. Pharmacol. 355, 211-217 (1998).
    • (1998) Eur. J. Pharmacol. , vol.355 , pp. 211-217
    • Gilroy, D.W.1    Tomlinson, A.2    Willoughby, D.A.3
  • 29
    • 0033000906 scopus 로고    scopus 로고
    • Inducible cyclooxygenase may have anti-inflammatory properties
    • Gilroy, D. W. et al. Inducible cyclooxygenase may have anti-inflammatory properties. Nature Med. 5, 698-701 (1999).
    • (1999) Nature Med. , vol.5 , pp. 698-701
    • Gilroy, D.W.1
  • 30
    • 1542283687 scopus 로고    scopus 로고
    • A novel role for phospholipase A2 isoforms in the checkpoint control of acute inflammation
    • Gilroy, D. W., Newson, J., Sawmynaden, P., Willoughby, D. A. & Croxtall, J. D. A novel role for phospholipase A2 isoforms in the checkpoint control of acute inflammation. FASEB J. 18, 480-498 (2004).
    • (2004) FASEB J. , vol.18 , pp. 480-498
    • Gilroy, D.W.1    Newson, J.2    Sawmynaden, P.3    Willoughby, D.A.4    Croxtall, J.D.5
  • 31
    • 0642364442 scopus 로고    scopus 로고
    • Inducible cyclooxygenase-derived 15-deoxy(Delta)12-14PGJ2 brings about acute inflammatory resolution in rat pleurisy by inducing neutrophil and macrophage apoptosis
    • Gilroy, D. W. et al. Inducible cyclooxygenase-derived 15-deoxy(Delta)12-14PGJ2 brings about acute inflammatory resolution in rat pleurisy by inducing neutrophil and macrophage apoptosis. FASEB J. 17, 2269-2271 (2003).
    • (2003) FASEB J. , vol.17 , pp. 2269-2271
    • Gilroy, D.W.1
  • 32
    • 0037096205 scopus 로고    scopus 로고
    • Prostaglandin D2 and its metabolites induce caspase-dependent granulocyte apoptosis that is mediated via inhibition of I kappa B alpha degradation using a peroxisome proliferator-activated receptor-gamma-independent mechanism
    • Ward, C. et al. Prostaglandin D2 and its metabolites induce caspase-dependent granulocyte apoptosis that is mediated via inhibition of I kappa B alpha degradation using a peroxisome proliferator-activated receptor-gamma-independent mechanism. J. Immunol 168, 6232-6243 (2002).
    • (2002) J. Immunol , vol.168 , pp. 6232-6243
    • Ward, C.1
  • 33
    • 0037315485 scopus 로고    scopus 로고
    • Potentiation of protein kinase C zeta activity by 15-deoxy-delta(12,14)-prostaglandin J(2) induces an imbalance between mitogen-activated protein kinases and NF-kappaB that promotes apoptosis in macrophages
    • Castrillo, A. et al. Potentiation of protein kinase C zeta activity by 15-deoxy-delta(12,14)-prostaglandin J(2) induces an imbalance between mitogen-activated protein kinases and NF-kappaB that promotes apoptosis in macrophages. Mol. Cell Biol. 23, 1196-1208 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 1196-1208
    • Castrillo, A.1
  • 34
    • 0035851123 scopus 로고    scopus 로고
    • 15-deoxy-delta 12,14-prostaglandin J2 induces apoptosis of human hepatic myofibroblasts. A pathway involving oxidative stress independently of peroxisome-proliferator-activated receptors
    • Li, L. et al. 15-deoxy-delta 12,14-prostaglandin J2 induces apoptosis of human hepatic myofibroblasts. A pathway involving oxidative stress independently of peroxisome-proliferator-activated receptors. J. Biol. Chem. 276, 38152-38158 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 38152-38158
    • Li, L.1
  • 35
    • 2442617659 scopus 로고    scopus 로고
    • Reference deleted in proof
    • Reference deleted in proof.
  • 36
    • 0035210586 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma haploinsufficiency enhances B cell proliferative responses and exacerbates experimentally induced arthritis
    • Setoguchi, K. et al. Peroxisome proliferator-activated receptor-gamma haploinsufficiency enhances B cell proliferative responses and exacerbates experimentally induced arthritis. J. Clin. Invest. 108, 1667-1675 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 1667-1675
    • Setoguchi, K.1
  • 37
    • 20244368762 scopus 로고    scopus 로고
    • Retrovirally introduced prostaglandin D2 synthase suppresses lung injury induced by bleomycin
    • Ando, M. et al. Retrovirally introduced prostaglandin D2 synthase suppresses lung injury induced by bleomycin. Am. J. Respir. Cell. Mol. Biol. 28, 582-591 (2003).
    • (2003) Am. J. Respir. Cell. Mol. Biol. , vol.28 , pp. 582-591
    • Ando, M.1
  • 38
    • 0037295323 scopus 로고    scopus 로고
    • 2 attenuates the development of colon injury caused by dinitrobenzene sulphonic acid in the rat
    • 2 attenuates the development of colon injury caused by dinitrobenzene sulphonic acid in the rat. Br. J. Pharmacol. 138, 678-688 (2003).
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 678-688
    • Cuzzocrea, S.1
  • 39
    • 10744231560 scopus 로고    scopus 로고
    • The cyclopentenone prostaglandin 15-deoxy-Delta(12,14)-prostaglandin J(2) ameliorates ischemic acute renal failure
    • Chatterjee, P. K. et al. The cyclopentenone prostaglandin 15-deoxy-Delta(12,14)-prostaglandin J(2) ameliorates ischemic acute renal failure. Cardiovasc. Res. 61, 630-643 (2004).
    • (2004) Cardiovasc. Res. , vol.61 , pp. 630-643
    • Chatterjee, P.K.1
  • 40
    • 0033925031 scopus 로고    scopus 로고
    • 15-deoxy-delta(12,14)-PGJ(2) induces synoviocyte apoptosis and suppresses adjuvant-induced arthritis in rats
    • Kawahito, Y. et al. 15-deoxy-delta(12,14)-PGJ(2) induces synoviocyte apoptosis and suppresses adjuvant-induced arthritis in rats. J. Clin. Invest. 106, 189-197 (2000).
    • (2000) J. Clin. Invest. , vol.106 , pp. 189-197
    • Kawahito, Y.1
  • 41
    • 0036499074 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma agonist 15-deoxy-delta(12,14)-prostaglandin J(2) ameliorates experimental autoimmune encephalomyelitis
    • Diab, A. et al. Peroxisome proliferator-activated receptor-gamma agonist 15-deoxy-delta(12,14)-prostaglandin J(2) ameliorates experimental autoimmune encephalomyelitis. J. Immunol. 168, 2508-2515 (2002).
    • (2002) J. Immunol. , vol.168 , pp. 2508-2515
    • Diab, A.1
  • 42
    • 0034677595 scopus 로고    scopus 로고
    • Prostaglandin D2 as a mediator of allergic asthma
    • Matsuoka, T. et al. Prostaglandin D2 as a mediator of allergic asthma. Science 287, 2013-2017 (2000).
    • (2000) Science , vol.287 , pp. 2013-2017
    • Matsuoka, T.1
  • 43
    • 0041920928 scopus 로고    scopus 로고
    • H2 type inflammatory responses of airways to low-dose antigen through bronchial expression of macrophage-derived chemokine
    • H2 type inflammatory responses of airways to low-dose antigen through bronchial expression of macrophage-derived chemokine. J. Exp. Med. 198, 533-543 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 533-543
    • Honda, K.1
  • 44
    • 0038143233 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 expression in murine macrophages is essential for the anti-inflammatory effect of low dose 15-deoxy-delta 12,14-prostaglandin J2
    • Lee, T. S., Tsai, H. L. & Chau, L. Y. Induction of heme oxygenase-1 expression in murine macrophages is essential for the anti-inflammatory effect of low dose 15-deoxy-delta 12,14-prostaglandin J2. J. Biol. Chem. 278, 19325-19330 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 19325-19330
    • Lee, T.S.1    Tsai, H.L.2    Chau, L.Y.3
  • 45
    • 4243550127 scopus 로고    scopus 로고
    • Heme oxygenase/carbon monoxide signaling pathways: Regulation and functional significance
    • Ryter, S. W., Otterbein, L. E., Morse, D. & Choi, A. M. Heme oxygenase/carbon monoxide signaling pathways: regulation and functional significance. Mol. Cell. Biochem. 234-235, 249-263 (2002).
    • (2002) Mol. Cell. Biochem. , vol.234-235 , pp. 249-263
    • Ryter, S.W.1    Otterbein, L.E.2    Morse, D.3    Choi, A.M.4
  • 46
    • 0030045835 scopus 로고    scopus 로고
    • Heme oxygenase: A novel target for the modulation of the inflammatory response
    • Willis, D. M. A., Frederick, R. & Willoughby, D. A. Heme oxygenase: a novel target for the modulation of the inflammatory response. Nature Med. 2, 87-90 (1996).
    • (1996) Nature Med. , vol.2 , pp. 87-90
    • Willis, D.M.A.1    Frederick, R.2    Willoughby, D.A.3
  • 48
    • 0141988655 scopus 로고    scopus 로고
    • Anti-inflammatory actions of the heme oxygenase-1 pathway
    • Alcaraz, M. J., Fernandez, P. & Guillen, M. I. Anti-inflammatory actions of the heme oxygenase-1 pathway. Curr. Pharm. Des. 9, 2541-2551 (2003).
    • (2003) Curr. Pharm. Des. , vol.9 , pp. 2541-2551
    • Alcaraz, M.J.1    Fernandez, P.2    Guillen, M.I.3
  • 49
    • 0035869629 scopus 로고    scopus 로고
    • Carbon monoxide generated by heme oxygenase-1 suppresses the rejection of mouse-to-rat cardiac transplants
    • Sato, K. et al. Carbon monoxide generated by heme oxygenase-1 suppresses the rejection of mouse-to-rat cardiac transplants. J. Immunol. 166, 4185-4194 (2001).
    • (2001) J. Immunol. , vol.166 , pp. 4185-4194
    • Sato, K.1
  • 50
    • 0031757984 scopus 로고    scopus 로고
    • Antibody-induced transplant arteriosclerosis is prevented by graft expression of anti-oxidant and anti-apoptotic genes
    • Hancock, W. W., Buelow, R., Sayegh, M. H. & Turka, L. A. Antibody-induced transplant arteriosclerosis is prevented by graft expression of anti-oxidant and anti-apoptotic genes. Nature Med. 4, 1392-1396 (1998).
    • (1998) Nature Med. , vol.4 , pp. 1392-1396
    • Hancock, W.W.1    Buelow, R.2    Sayegh, M.H.3    Turka, L.A.4
  • 51
    • 0034011211 scopus 로고    scopus 로고
    • Alleviation of graft-versus-host disease after conditioning with cobalt-protoporphyrin, an inducer of heme oxygenase-1
    • Woo, J., Iyer, S., Mori, N. & Buelow, R. Alleviation of graft-versus-host disease after conditioning with cobalt-protoporphyrin, an inducer of heme oxygenase-1. Transplantation 89, 623-633 (2000).
    • (2000) Transplantation , vol.89 , pp. 623-633
    • Woo, J.1    Iyer, S.2    Mori, N.3    Buelow, R.4
  • 52
    • 0034916569 scopus 로고    scopus 로고
    • Lipid mediator class switching during acute inflammation: Signals in resolution
    • Levy, B. D., Clish, C. B., Schmidt, B., Gronert, K. & Serhan, C. N. Lipid mediator class switching during acute inflammation: signals in resolution. Nature Immunol. 2, 612-619 (2001).
    • (2001) Nature Immunol. , vol.2 , pp. 612-619
    • Levy, B.D.1    Clish, C.B.2    Schmidt, B.3    Gronert, K.4    Serhan, C.N.5
  • 53
    • 0029670175 scopus 로고    scopus 로고
    • Lipoxin A4 and B4 inhibit leukotriene-stimulated interactions of human neutrophils and endothelial cells
    • Papayianni, A., Serhan, C. N. & Brady, H. R. Lipoxin A4 and B4 inhibit leukotriene-stimulated interactions of human neutrophils and endothelial cells. J. Immunol. 156, 2264-2272 (1996).
    • (1996) J. Immunol. , vol.156 , pp. 2264-2272
    • Papayianni, A.1    Serhan, C.N.2    Brady, H.R.3
  • 54
    • 0034464716 scopus 로고    scopus 로고
    • Aspidn-triggered 15-epi-lipoxin A4 and novel lipoxin B4 stable analogs inhibit neutrophil-madiated changes in vascular permeability
    • Serhan, C. N., Takano, T., Clish, C. B., Gronert K. & Petasis, N. Aspidn-triggered 15-epi-lipoxin A4 and novel lipoxin B4 stable analogs inhibit neutrophil-madiated changes in vascular permeability. Adv. Exp. Med. Biol. 469, 287-293 (1999).
    • (1999) Adv. Exp. Med. Biol. , vol.469 , pp. 287-293
    • Serhan, C.N.1    Takano, T.2    Clish, C.B.3    Gronert, K.4    Petasis, N.5
  • 55
    • 0029671266 scopus 로고    scopus 로고
    • Lipoxin A4 and B4 are potent stimuli for human monocyte migration and adhesion: Selective inactivation by dehydrogenation and reduction
    • Maddox, J. F. & Serhan, C. N. Lipoxin A4 and B4 are potent stimuli for human monocyte migration and adhesion: selective inactivation by dehydrogenation and reduction. J. Exp. Med. 183, 137-146 (1996).
    • (1996) J. Exp. Med. , vol.183 , pp. 137-146
    • Maddox, J.F.1    Serhan, C.N.2
  • 56
    • 0030614870 scopus 로고    scopus 로고
    • Lipoxin A4 stable analogs are potent mimetics that stimulate human monocytes and THP-1 cells via a G-protein-linked lipoxin A4 receptor
    • Maddox, J. F. et al. Lipoxin A4 stable analogs are potent mimetics that stimulate human monocytes and THP-1 cells via a G-protein-linked lipoxin A4 receptor. J. Biol. Chem. 272, 6972-6978 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 6972-6978
    • Maddox, J.F.1
  • 57
    • 0036771772 scopus 로고    scopus 로고
    • Lipoxin A4 and aspirin-triggered 15-epi-lipoxin A4 inhibit peroxynitrite formation, NF-kappa B and AP-1 activation, and IL-8 gene expression in human leukocytes
    • Jozsef, L., Zouki, C., Petasis, N. A., Serhan, C. N. & Filep, J. G. Lipoxin A4 and aspirin-triggered 15-epi-lipoxin A4 inhibit peroxynitrite formation, NF-kappa B and AP-1 activation, and IL-8 gene expression in human leukocytes. Proc. Natl Acad. Sci. USA 99, 13266-13271 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13266-13271
    • Jozsef, L.1    Zouki, C.2    Petasis, N.A.3    Serhan, C.N.4    Filep, J.G.5
  • 58
    • 0034650789 scopus 로고    scopus 로고
    • Cyclooxygenase-2-derived prostaglandin E2 and lipoxin A4 accelerate resolution of allergic edema in Angiostrongylus costaricensis-infected rats: Relationship with concurrent eosinophilla
    • Bandeira-Melo, C. et al. Cyclooxygenase-2-derived prostaglandin E2 and lipoxin A4 accelerate resolution of allergic edema in Angiostrongylus costaricensis-infected rats: relationship with concurrent eosinophilla. J. Immunol. 164, 1029-1036 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 1029-1036
    • Bandeira-Melo, C.1
  • 59
    • 0034651737 scopus 로고    scopus 로고
    • Cutting edge: Lipoxins rapidly stimulate nonphlogistic phagocytosis of apoptotic neutrophils by monocyte-derived macrophages
    • Godson, C. et al. Cutting edge: lipoxins rapidly stimulate nonphlogistic phagocytosis of apoptotic neutrophils by monocyte-derived macrophages. J. Immunol. 164, 1663-1667 (2000).
    • (2000) J. Immunol. , vol.164 , pp. 1663-1667
    • Godson, C.1
  • 60
    • 18544378668 scopus 로고    scopus 로고
    • Lipoxins, aspirin-triggerad epi-lipoxins, lipoxin stable analogues, and the resolution of inflammation: Stimulation of macrophage phagocytosis of apoptotic neutrophils in vivo
    • Mitchell, S. et al. Lipoxins, aspirin-triggerad epi-lipoxins, lipoxin stable analogues, and the resolution of inflammation: stimulation of macrophage phagocytosis of apoptotic neutrophils in vivo. J. Am. Soc. Nephrol. 13, 2497-2507 (2002).
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 2497-2507
    • Mitchell, S.1
  • 61
    • 0037372846 scopus 로고    scopus 로고
    • Nomenclature for leukotriene and lipoxin receptors
    • International Union of Pharmacology XXXVII
    • Brink, C. et al. International Union of Pharmacology XXXVII. Nomenclature for leukotriene and lipoxin receptors. Pharmacol. Rev. 55, 195-227 (2003).
    • (2003) Pharmacol. Rev. , vol.55 , pp. 195-227
    • Brink, C.1
  • 62
    • 0034163279 scopus 로고    scopus 로고
    • Cutting edge: Lipoxin (LX) A4 and aspirin-triggered 15-epi-LXA4 block allergen-induced eosinophil trafficking
    • Bandeira-Melo, C. et al. Cutting edge: lipoxin (LX) A4 and aspirin-triggered 15-epi-LXA4 block allergen-induced eosinophil trafficking. J. Immunol 164, 2267-2271 (2000).
    • (2000) J. Immunol , vol.164 , pp. 2267-2271
    • Bandeira-Melo, C.1
  • 63
    • 0034675852 scopus 로고    scopus 로고
    • Novel functional sets of lipid-derived mediators with antiinflammatory actions generated from omega-3 fatty acids via cyclooxygenase 2-nonsteroidal antiinflammatory drugs and transcellular processing
    • Serhan, C. N. et al. Novel functional sets of lipid-derived mediators with antiinflammatory actions generated from omega-3 fatty acids via cyclooxygenase 2-nonsteroidal antiinflammatory drugs and transcellular processing. J. Exp. Med. 192, 1197-1204 (2000).
    • (2000) J. Exp. Med. , vol.192 , pp. 1197-1204
    • Serhan, C.N.1
  • 64
    • 0037152160 scopus 로고    scopus 로고
    • Resolvins: A family of bioactive products of omega-3 fatty acid transformation circuits initiated by aspirin treatment that counter proinflammation signals
    • Serhan, C. N. et al. Resolvins: a family of bioactive products of omega-3 fatty acid transformation circuits initiated by aspirin treatment that counter proinflammation signals. J. Exp. Med. 196, 1025-1037 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 1025-1037
    • Serhan, C.N.1
  • 65
    • 0038013967 scopus 로고    scopus 로고
    • Novel docosatrienes and 17S-resolvins generated from docosahexaenoic acid in murine brain, human blood and glial cells. Autacoids in anti-inflammation
    • Hong, S., Gronert, K., Devchand, P. R., Moussignac, R. L. & Serhan, C. N. Novel docosatrienes and 17S-resolvins generated from docosahexaenoic acid in murine brain, human blood and glial cells. Autacoids in anti-inflammation. J. Biol. Chem. 278, 14677-14687 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 14677-14687
    • Hong, S.1    Gronert, K.2    Devchand, P.R.3    Moussignac, R.L.4    Serhan, C.N.5
  • 66
    • 0026680341 scopus 로고
    • Angioplasty triggers intracoronary leukotrienes and lipoxin A4. Impact of aspirin therapy
    • Brezinski, D. A., Nesto, R. W. & Serhan, C. N. Angioplasty triggers intracoronary leukotrienes and lipoxin A4. Impact of aspirin therapy. Circulation 86, 56-63 (1992).
    • (1992) Circulation , vol.86 , pp. 56-63
    • Brezinski, D.A.1    Nesto, R.W.2    Serhan, C.N.3
  • 67
    • 0037315708 scopus 로고    scopus 로고
    • Resolution of inflammation: A new paradigm for the pathogenesis of periodontal diseases
    • Van Dyke, T. E. & Serhan, C. N. Resolution of inflammation: a new paradigm for the pathogenesis of periodontal diseases. J. Dent. Res. 82, 82-90 (2003).
    • (2003) J. Dent. Res. , vol.82 , pp. 82-90
    • Van Dyke, T.E.1    Serhan, C.N.2
  • 68
    • 0031800823 scopus 로고    scopus 로고
    • Altered biosynthesis of leukotrienes and lipoxins and host defense disorders in patients with cirrhosis and ascites
    • Caria, J. et al. Altered biosynthesis of leukotrienes and lipoxins and host defense disorders in patients with cirrhosis and ascites. Gastroenterology 115, 147-156 (1998).
    • (1998) Gastroenterology , vol.115 , pp. 147-156
    • Caria, J.1
  • 69
    • 0036734152 scopus 로고    scopus 로고
    • Multi-pronged inhibition of airway hyper-responsiveness and inflammation by lipoxin A(4)
    • Levy B. D. et al. Multi-pronged inhibition of airway hyper-responsiveness and inflammation by lipoxin A(4). Nature Med. 8, 1018-1023 (2002).
    • (2002) Nature Med. , vol.8 , pp. 1018-1023
    • Levy, B.D.1
  • 70
    • 0033539695 scopus 로고    scopus 로고
    • Transfection of rat kidney with human 15-lipoxygenase suppresses inflammation and preserves function in experimental glomerulonephritis
    • Munger, K. A. et al. Transfection of rat kidney with human 15-lipoxygenase suppresses inflammation and preserves function in experimental glomerulonephritis. Proc. Natl Acad. Sci. USA 96, 13375-13380 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13375-13380
    • Munger, K.A.1
  • 71
    • 0036014949 scopus 로고    scopus 로고
    • 15-Epi-16-(para-fluorophenoxy)-lipoxin A(4)-methyl ester, a synthetic analogue of 15-epi-lipoxin A(4), is protective in experimental ischemic acute renal failure
    • Leonard, M. O. et al. 15-Epi-16-(para-fluorophenoxy)-lipoxin A(4)-methyl ester, a synthetic analogue of 15-epi-lipoxin A(4), is protective in experimental ischemic acute renal failure. J. Am. Soc. Nephrol. 13, 1657-1662 (2002).
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 1657-1662
    • Leonard, M.O.1
  • 72
    • 0037114166 scopus 로고    scopus 로고
    • An aspirin-triggered lipoxin A4 stable analog displays a unique topical anti-inflammatory profile
    • Schottelius, A. J. et al. An aspirin-triggered lipoxin A4 stable analog displays a unique topical anti-inflammatory profile. J. Immunol. 189, 7063-7070 (2002).
    • (2002) J. Immunol. , vol.189 , pp. 7063-7070
    • Schottelius, A.J.1
  • 74
    • 0031021556 scopus 로고    scopus 로고
    • Neutrophil fate in experimental glomerular capillary injury in the rat. Emigration exceeds lin situ clearance by apoptosis
    • Hughes, J. et al. Neutrophil fate in experimental glomerular capillary injury in the rat. Emigration exceeds lin situ clearance by apoptosis. Am. J. Pathol. 150, 223-234 (1997).
    • (1997) Am. J. Pathol. , vol.150 , pp. 223-234
    • Hughes, J.1
  • 75
    • 0142188265 scopus 로고    scopus 로고
    • Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence
    • Martin, C. et al. Chemokines acting via CXCR2 and CXCR4 control the release of neutrophils from the bone marrow and their return following senescence. Immunity 19, 583-593 (2003).
    • (2003) Immunity , vol.19 , pp. 583-593
    • Martin, C.1
  • 76
    • 0030587122 scopus 로고    scopus 로고
    • In vivo fate of the inflammatory macrophage during the resolution of inflammation: Inflammatory macrophages do not die locally, but emigrate to the draining lymph nodes
    • Bellingan, G. J., Celdwell, H., Howie, S. E., Dransfield, I. & Hasiett, C. In vivo fate of the inflammatory macrophage during the resolution of inflammation: inflammatory macrophages do not die locally, but emigrate to the draining lymph nodes. J. Immunol. 157, 2577-2585 (1996).
    • (1996) J. Immunol. , vol.157 , pp. 2577-2585
    • Bellingan, G.J.1    Celdwell, H.2    Howie, S.E.3    Dransfield, I.4    Hasiett, C.5
  • 77
    • 0037011067 scopus 로고    scopus 로고
    • Adhesion molecule-dependent mechanisms regulate the rate of macrophage clearance during the resolution of peritoneal inflammation
    • Bellingan, G. J. et al. Adhesion molecule-dependent mechanisms regulate the rate of macrophage clearance during the resolution of peritoneal inflammation. J. Exp. Med. 196, 1515-1521 (2002).
    • (2002) J. Exp. Med. , vol.196 , pp. 1515-1521
    • Bellingan, G.J.1
  • 78
    • 0034641931 scopus 로고    scopus 로고
    • Corpse clearance defines the meaning of cell death
    • Savill, J. & Fadok, V. Corpse clearance defines the meaning of cell death. Nature 407, 784-788 (2000).
    • (2000) Nature , vol.407 , pp. 784-788
    • Savill, J.1    Fadok, V.2
  • 79
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson, D. W. From bench to clinic with apoptosis-based therapeutic agents. Nature 407, 810-816 (2000).
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 80
    • 0345447009 scopus 로고    scopus 로고
    • Apoptosis in disease: About shortage and excess
    • Brunner, T. & Mueller, C. Apoptosis in disease: about shortage and excess. Essays Biochem. 39, 119-130 (2003).
    • (2003) Essays Biochem. , vol.39 , pp. 119-130
    • Brunner, T.1    Mueller, C.2
  • 81
    • 0034795821 scopus 로고    scopus 로고
    • Phagocyte receptors for apoptotic cells: Recognition, uptake, and consequences
    • Fadok, V. A., Bratton, D. L. & Henson, P. M. Phagocyte receptors for apoptotic cells: recognition, uptake, and consequences. J. Clin. Invest. 108, 957-962 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 957-962
    • Fadok, V.A.1    Bratton, D.L.2    Henson, P.M.3
  • 82
    • 0036884424 scopus 로고    scopus 로고
    • A blast from the past: Clearance of apoptotic cells regulates immune responses
    • Savill, J., Dransfield, I., Gregory, C. & Haslett, C. A blast from the past: clearance of apoptotic cells regulates immune responses. Nature Rev. Immunol 2, 965-975 (2002).
    • (2002) Nature Rev. Immunol. , vol.2 , pp. 965-975
    • Savill, J.1    Dransfield, I.2    Gregory, C.3    Haslett, C.4
  • 83
    • 0001378970 scopus 로고    scopus 로고
    • Pharmacological manipulation of granulocyte apoptosis: Potential therapeutic targets
    • Ward, C., Dransfield, I., Chilvers, E. R., Haslett, C. & Rossi, A. Pharmacological manipulation of granulocyte apoptosis: potential therapeutic targets. Trends Pharmacol. Sci. 20, 503-509 (1999).
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 503-509
    • Ward, C.1    Dransfield, I.2    Chilvers, E.R.3    Haslett, C.4    Rossi, A.5
  • 85
    • 0032055850 scopus 로고    scopus 로고
    • Regulation of macrophage phagocytosis of apoptotic cells by cAMP
    • Rossi, A. G. et al. Regulation of macrophage phagocytosis of apoptotic cells by cAMP. J. Immunol. 160, 3562-3568 (1998).
    • (1998) J. Immunol. , vol.160 , pp. 3562-3568
    • Rossi, A.G.1
  • 86
    • 0033559878 scopus 로고    scopus 로고
    • Glucocorticoids promote nonphlogistic phagocytosis of apoptotic leukocytes
    • Liu, Y. et al. Glucocorticoids promote nonphlogistic phagocytosis of apoptotic leukocytes. J. Immunol. 162, 3634-3646 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 3634-3646
    • Liu, Y.1
  • 87
    • 0035879302 scopus 로고    scopus 로고
    • Glucocorticoid augmentation of macrophage capacity for phagocytosis of apoptotic cells is associated with reduced p130Cas expression, loss of paxillin/pyk2 phosphorylation, and high levels of active Rac
    • Giles, K. M. et al. Glucocorticoid augmentation of macrophage capacity for phagocytosis of apoptotic cells is associated with reduced p130Cas expression, loss of paxillin/pyk2 phosphorylation, and high levels of active Rac. J. Immunol. 167, 976-986 (2001).
    • (2001) J. Immunol. , vol.167 , pp. 976-986
    • Giles, K.M.1
  • 88
    • 0028947880 scopus 로고
    • Proinflammatory cytokines potentiate thrombospondin-mediated phagocytosis of neutrophils undergoing apoptosis
    • Ren, Y. & Savill, J. Proinflammatory cytokines potentiate thrombospondin-mediated phagocytosis of neutrophils undergoing apoptosis. J. Immunol. 154, 2366-2374 (1995).
    • (1995) J. Immunol. , vol.154 , pp. 2366-2374
    • Ren, Y.1    Savill, J.2
  • 89
    • 0031790235 scopus 로고    scopus 로고
    • Regulation of macrophage phagocytosis of apoptotic neutrophils by adhesion to fibronectin
    • McCutcheon, J. C. et al. Regulation of macrophage phagocytosis of apoptotic neutrophils by adhesion to fibronectin. J. Leukoc., Biol. 64, 600-607 (1998).
    • (1998) J. Leukoc. Biol. , vol.64 , pp. 600-607
    • McCutcheon, J.C.1
  • 90
    • 0031570880 scopus 로고    scopus 로고
    • CD44 regulates phagocytosis of apoptotic neutrophil granulocytes, but not apoptotic lymphocytes, by human macrophages
    • Hart, S. P., Dougherty, G. J., Haslett, C. & Dransfield, I. CD44 regulates phagocytosis of apoptotic neutrophil granulocytes, but not apoptotic lymphocytes, by human macrophages. J. Immunol. 159, 919-925 (1997).
    • (1997) J. Immunol. , vol.159 , pp. 919-925
    • Hart, S.P.1    Dougherty, G.J.2    Haslett, C.3    Dransfield, I.4
  • 91
    • 0037023364 scopus 로고    scopus 로고
    • Resolution of lung inflammation by CD44
    • Teder, P. et al. Resolution of lung inflammation by CD44. Science 296, 155-158 (2002).
    • (2002) Science , vol.296 , pp. 155-158
    • Teder, P.1
  • 92
    • 0030035298 scopus 로고    scopus 로고
    • Eosinophil apoptosis and the resolution of airway inflammation in asthma
    • Woolley, K. L. et al. Eosinophil apoptosis and the resolution of airway inflammation in asthma. Am. J. Respir. Crit. Care Med. 154, 237-243 (1996).
    • (1996) Am. J. Respir. Crit. Care Med. , vol.154 , pp. 237-243
    • Woolley, K.L.1
  • 93
    • 0344584830 scopus 로고    scopus 로고
    • Therapeutic approaches to the modulation of apoptosis
    • Murphy, F. J., Seery, L. T. & Hayes, I. Therapeutic approaches to the modulation of apoptosis. Essays Biochem. 39, 131-153 (2003).
    • (2003) Essays Biochem. , vol.39 , pp. 131-153
    • Murphy, F.J.1    Seery, L.T.2    Hayes, I.3
  • 94
    • 0347601880 scopus 로고    scopus 로고
    • A decade of caspases
    • Degterev, A., Boyce, M. & Yuan, J. A decade of caspases. Oncogene 22, 8543-8567 (2003).
    • (2003) Oncogene , vol.22 , pp. 8543-8567
    • Degterev, A.1    Boyce, M.2    Yuan, J.3
  • 95
    • 0032885388 scopus 로고    scopus 로고
    • Mammallan caspases: Structure, activation, substrates, and functions during apoptosis
    • Eamshaw, W. C., Martins, L. M. & Kaufmann, S. H. Mammallan caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383-424 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Eamshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 96
    • 0036985895 scopus 로고    scopus 로고
    • Caspase inhibitors as anti-inflammatory and antiapoptotic agents
    • Graczyk, P. P. Caspase inhibitors as anti-inflammatory and antiapoptotic agents. Prog. Med. Chem. 39, 1-72 (2002).
    • (2002) Prog. Med. Chem. , vol.39 , pp. 1-72
    • Graczyk, P.P.1
  • 97
    • 0037105527 scopus 로고    scopus 로고
    • The caspase inhibitor z-VAD is more effective than CD18 adhesion blockade in reducing muscle ischemia-reperfusion injury: Implication for clinical trials
    • Iwata, A., Harlan, J. M., Vedder, N. B. & Winn, R. K. The caspase inhibitor z-VAD is more effective than CD18 adhesion blockade in reducing muscle ischemia-reperfusion injury: implication for clinical trials. Blood 100, 2077-2080 (2002).
    • (2002) Blood , vol.100 , pp. 2077-2080
    • Iwata, A.1    Harlan, J.M.2    Vedder, N.B.3    Winn, R.K.4
  • 98
    • 0037342981 scopus 로고    scopus 로고
    • The caspase inhibitor IDN-6556 prevents caspase activation and apoptosis in sinusoidal endothelial cells during liver preservation injury
    • Natori, S., Higuchi, H., Contreras, P. & Gores, G. J. The caspase inhibitor IDN-6556 prevents caspase activation and apoptosis in sinusoidal endothelial cells during liver preservation injury. Liver Transpl. 9, 278-284 (2003).
    • (2003) Liver Transpl. , vol.9 , pp. 278-284
    • Natori, S.1    Higuchi, H.2    Contreras, P.3    Gores, G.J.4
  • 99
    • 2442437272 scopus 로고    scopus 로고
    • Characterization of IDN-6556: A liver-targeted caspase inhibitor
    • 23 Jan [epub ahead of print]
    • Hoglen, N. C. et al. Characterization of IDN-6556: a liver-targeted caspase inhibitor J. Pharmacol. Exp. Ther. 23 Jan 2004 [epub ahead of print].
    • (2004) J. Pharmacol. Exp. Ther.
    • Hoglen, N.C.1
  • 100
    • 0141996262 scopus 로고    scopus 로고
    • First clinical trial of a novel caspase inhibitor: Anti-apoptotic caspase inhibitor, IDN-6556, improves liver enzymes
    • Valentino, K. L., Gutierrez, M., Sanchez, R., Winship, M. J. & Shapiro, D. A. First clinical trial of a novel caspase inhibitor: anti-apoptotic caspase inhibitor, IDN-6556, improves liver enzymes. Int. J. Clin. Pharmacol. Ther. 41, 441-449 (2003).
    • (2003) Int. J. Clin. Pharmacol. Ther. , vol.41 , pp. 441-449
    • Valentino, K.L.1    Gutierrez, M.2    Sanchez, R.3    Winship, M.J.4    Shapiro, D.A.5
  • 101
    • 0032524357 scopus 로고    scopus 로고
    • New twists in gone regulation by glucocorticoid receptor: Is DNA binding dispensable?
    • Karin, M. New twists in gone regulation by glucocorticoid receptor: is DNA binding dispensable? Cell 93, 487-490 (1998).
    • (1998) Cell , vol.93 , pp. 487-490
    • Karin, M.1
  • 102
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh, S., May, M. J. & Kopp, E. B. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16, 225-260 (1998).
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 103
    • 0034663779 scopus 로고    scopus 로고
    • The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes
    • Khoshnan, A. et al. The NF-kappa B cascade is important in Bcl-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes. J. Immunol. 165, 1743-1754 (2000).
    • (2000) J. Immunol. , vol.165 , pp. 1743-1754
    • Khoshnan, A.1
  • 104
    • 0033547876 scopus 로고    scopus 로고
    • NF-kappaB activation is a critical regulator of human granulocyte apoptosis in vitro
    • Ward, C. et al. NF-kappaB activation is a critical regulator of human granulocyte apoptosis in vitro. J. Biol. Chem. 274, 4309-4318 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 4309-4318
    • Ward, C.1
  • 105
  • 106
    • 0032489828 scopus 로고    scopus 로고
    • Chronic inflammation and susceptibility to bacterial infections in mice lacking the polypeptide (p)105 precursor (NF-kappaB1) but expressing p50
    • Ishikawa, H. et al. Chronic inflammation and susceptibility to bacterial infections in mice lacking the polypeptide (p)105 precursor (NF-kappaB1) but expressing p50. J. Exp. Med. 187, 985-996 (1998).
    • (1998) J. Exp. Med. , vol.187 , pp. 985-996
    • Ishikawa, H.1
  • 107
    • 0032211810 scopus 로고    scopus 로고
    • Regulation of an essential innate immune response by the p50 subunit of NF-kappaB
    • Bohuslav, J. et al. Regulation of an essential innate immune response by the p50 subunit of NF-kappaB. J. Clin. Invest. 102, 1645-1652 (1998).
    • (1998) J. Clin. Invest. , vol.102 , pp. 1645-1652
    • Bohuslav, J.1
  • 108
    • 0038587747 scopus 로고    scopus 로고
    • The two faces of IKK and NF-kappaB inhibition: Prevention of systemic inflammation but increased local injury following intestinal ischemia-reperfusion
    • Chen, L. W. et al. The two faces of IKK and NF-kappaB inhibition: prevention of systemic inflammation but increased local injury following intestinal ischemia-reperfusion. Nature Med. 9, 575-681 (2003).
    • (2003) Nature Med. , vol.9 , pp. 575-681
    • Chen, L.W.1
  • 109
    • 0021724901 scopus 로고
    • Physiological functions of glucocorticoids in stress and their relation to pharmacological actions
    • Munck, A., Guyre, P. M. & Holbrook, N. J. Physiological functions of glucocorticoids in stress and their relation to pharmacological actions. Endocr. Rev. 5, 25-44 (1984).
    • (1984) Endocr. Rev. , vol.5 , pp. 25-44
    • Munck, A.1    Guyre, P.M.2    Holbrook, N.J.3
  • 110
    • 0022637522 scopus 로고
    • A comparison of the acute inflammatory response in adrenalectomised and sham-operated rats
    • Flower, R. J., Parente, L., Persico, P. & Salmon, J. A. A comparison of the acute inflammatory response in adrenalectomised and sham-operated rats. Br. J. Pharmacol. 87, 57-62 (1986).
    • (1986) Br. J. Pharmacol. , vol.87 , pp. 57-62
    • Flower, R.J.1    Parente, L.2    Persico, P.3    Salmon, J.A.4
  • 111
    • 0024847428 scopus 로고
    • The effect of adrenalectomy on interleukin-1 release in vitro and in vivo
    • Perretti, M., Becherucci, C., Scapigliati, G. & Parente, L. The effect of adrenalectomy on interleukin-1 release in vitro and in vivo. Br. J. Pharmacol. 98, 1137-1142 (1989).
    • (1989) Br. J. Pharmacol. , vol.98 , pp. 1137-1142
    • Perretti, M.1    Becherucci, C.2    Scapigliati, G.3    Parente, L.4
  • 112
    • 0033773479 scopus 로고    scopus 로고
    • Molecular mechanisms of glucocorticosteroid actions
    • Adcock, I. M. Molecular mechanisms of glucocorticosteroid actions. Pulm. Pharmacol. Ther. 13, 115-126 (2000).
    • (2000) Pulm. Pharmacol. Ther. , vol.13 , pp. 115-126
    • Adcock, I.M.1
  • 113
    • 0028867899 scopus 로고
    • Immunosuppression by glucocorticoids: Inhibition of NF-kappa B activity through induction of I kappa B synthesis
    • Auphan, N., DiDonato, J. A., Rosette, C., Helmberg, A. & Karin, M. Immunosuppression by glucocorticoids: inhibition of NF-kappa B activity through induction of I kappa B synthesis. Science 270, 286-290 (1995).
    • (1995) Science , vol.270 , pp. 286-290
    • Auphan, N.1    DiDonato, J.A.2    Rosette, C.3    Helmberg, A.4    Karin, M.5
  • 114
    • 0034177660 scopus 로고    scopus 로고
    • Bioenergetics of immune functions: Fundamental and therapeutic aspects
    • Buttgereit, F., Burmester, G. R. & Brand, M. D. Bioenergetics of immune functions: fundamental and therapeutic aspects. Immunol. Today 21, 192-199 (2000).
    • (2000) Immunol. Today , vol.21 , pp. 192-199
    • Buttgereit, F.1    Burmester, G.R.2    Brand, M.D.3
  • 115
    • 0034665748 scopus 로고    scopus 로고
    • The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain
    • Nissen, R. M. & Yamamoto, K. R. The glucocorticoid receptor inhibits NFkappaB by interfering with serine-2 phosphorylation of the RNA polymerase II carboxy-terminal domain. Genes Dev. 14, 2314-2329 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2314-2329
    • Nissen, R.M.1    Yamamoto, K.R.2
  • 116
    • 0023751736 scopus 로고
    • Eleventh Gaddum memorial lecture. Lipocortin and the mechanism of action of the glucocorticoids
    • Flower, R. J. Eleventh Gaddum memorial lecture. Lipocortin and the mechanism of action of the glucocorticoids. Br. J. Pharmacol. 94, 987-1015 (1988).
    • (1988) Br. J. Pharmacol. , vol.94 , pp. 987-1015
    • Flower, R.J.1
  • 117
    • 0026607559 scopus 로고
    • Lipocortin 1 mediates dexamethasone-induced growth arrest of the A549 lung adenocarcinoma cell line
    • Croxtall, J. D. & Flower, R. J. Lipocortin 1 mediates dexamethasone-induced growth arrest of the A549 lung adenocarcinoma cell line. Proc. Natl Acad. Sci. USA 89, 3571-3575 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3571-3575
    • Croxtall, J.D.1    Flower, R.J.2
  • 118
    • 0027771507 scopus 로고
    • Macrophage-specific eicosanoid synthesis inhibition and lipocortin-1 induction by glucocorticoids
    • De Caterina, R. et al. Macrophage-specific eicosanoid synthesis inhibition and lipocortin-1 induction by glucocorticoids. J. Appl. Physiol. 75, 2368-2375 (1993).
    • (1993) J. Appl. Physiol. , vol.75 , pp. 2368-2375
    • De Caterina, R.1
  • 119
    • 0029015987 scopus 로고
    • Leukocyte transmigration, but not rolling or adhesion, is selectively inhibited by dexamethasone in the hamster post-capillary venule. Involvement of endogenous lipocortin 1
    • Mancuso, F., Flower, R. J. & Perretti, M. Leukocyte transmigration, but not rolling or adhesion, is selectively inhibited by dexamethasone in the hamster post-capillary venule. Involvement of endogenous lipocortin 1. J. Immunol. 155, 377-386 (1995).
    • (1995) J. Immunol. , vol.155 , pp. 377-386
    • Mancuso, F.1    Flower, R.J.2    Perretti, M.3
  • 120
    • 0027379886 scopus 로고
    • Lipocortin-1 fragments inhibit neutrophil accumulation and neutrophil-dependent edema in the mouse. A qualitative comparison with an anti-CD11b monoclonal antibody
    • Perretti, M., Ahluwalia, A., Harris, J. G., Goulding, N. J. & Flower, R. J. Lipocortin-1 fragments inhibit neutrophil accumulation and neutrophil-dependent edema in the mouse. A qualitative comparison with an anti-CD11b monoclonal antibody. J. Immunol. 151, 4306-4314 (1993).
    • (1993) J. Immunol. , vol.151 , pp. 4306-4314
    • Perretti, M.1    Ahluwalia, A.2    Harris, J.G.3    Goulding, N.J.4    Flower, R.J.5
  • 121
    • 0036083696 scopus 로고    scopus 로고
    • Annexins: From structure to function
    • Gerke, V. & Moss, S. E. Annexins: from structure to function. Physiol. Rev. 82, 331-371 (2002).
    • (2002) Physiol. Rev. , vol.82 , pp. 331-371
    • Gerke, V.1    Moss, S.E.2
  • 122
    • 0036852720 scopus 로고    scopus 로고
    • Endogenous lipid- and peptide-derived anti-inflammatory pathways generated with glucocorticoid and aspirin treatment activate the lipoxin A4 receptor
    • Perretti, M. et al. Endogenous lipid- and peptide-derived anti-inflammatory pathways generated with glucocorticoid and aspirin treatment activate the lipoxin A4 receptor. Nature Med. 8, 1296-1302 (2002).
    • (2002) Nature Med. , vol.8 , pp. 1296-1302
    • Perretti, M.1
  • 123
    • 0036839229 scopus 로고    scopus 로고
    • Formyl-peptide receptors revisited
    • Le, Y., Murphy, P. M. & Wang, J. M. Formyl-peptide receptors revisited. Trends Immunol. 23, 541-548 (2002).
    • (2002) Trends Immunol. , vol.23 , pp. 541-548
    • Le, Y.1    Murphy, P.M.2    Wang, J.M.3
  • 124
    • 0037398446 scopus 로고    scopus 로고
    • Annexin 1: An endogenous anti-inflammatory protein
    • Perretti, M. & Gavins, F. N. Annexin 1: an endogenous anti-inflammatory protein. News Physiol. Sci. 18, 60-64 (2003).
    • (2003) News Physiol. Sci. , vol.18 , pp. 60-64
    • Perretti, M.1    Gavins, F.N.2
  • 125
    • 0029928850 scopus 로고    scopus 로고
    • Acute inflammatory response in the mouse: Exacerbation by immunoneutralization of lipocortin 1
    • Parretti, M. et al. Acute inflammatory response in the mouse: exacerbation by immunoneutralization of lipocortin 1. Br. J. Pharmacol. 117, 1145-1154 (1996).
    • (1996) Br. J. Pharmacol. , vol.117 , pp. 1145-1154
    • Parretti, M.1
  • 126
    • 0037315827 scopus 로고    scopus 로고
    • Aberrant inflammation and resistance to glucocorticoids in annexin 1-/-mouse
    • Hannon, R. et al. Aberrant inflammation and resistance to glucocorticoids in annexin 1-/-mouse. FASEB J. 17, 253-255 (2003).
    • (2003) FASEB J. , vol.17 , pp. 253-255
    • Hannon, R.1
  • 127
    • 12144291153 scopus 로고    scopus 로고
    • Modulation of inflammation and response to dexamethasone by Annexin 1 in antigien-induced arthritis
    • Yang, Y. H. et al. Modulation of inflammation and response to dexamethasone by Annexin 1 in antigien-induced arthritis. Arthritis Rheum. 50, 976-964 (2004).
    • (2004) Arthritis Rheum. , vol.50 , pp. 976-984
    • Yang, Y.H.1
  • 128
    • 0242352558 scopus 로고    scopus 로고
    • The annexin 1 receptor(s): Is the plot unraveling?
    • Perretti, M. The annexin 1 receptor(s): is the plot unraveling? Trends Pharmacol. Sci. 24, 574-579 (2003).
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 574-579
    • Perretti, M.1
  • 129
    • 0348222661 scopus 로고    scopus 로고
    • Adenosine: An endogenous regulator of innate immunity
    • Hasko, G. & Cronstein, B. N. Adenosine: an endogenous regulator of innate immunity. Trends Immunol. 25, 33-39 (2004).
    • (2004) Trends Immunol. , vol.25 , pp. 33-39
    • Hasko, G.1    Cronstein, B.N.2
  • 130
    • 0037441343 scopus 로고    scopus 로고
    • Use of the A(2A) adenosine receptor as a physiological immunosuppressor and to engineer inflammation in vivo
    • Sitkovsky, M. V. Use of the A(2A) adenosine receptor as a physiological immunosuppressor and to engineer inflammation in vivo. Biochem. Pharmacol. 65, 493-501 (2003).
    • (2003) Biochem. Pharmacol. , vol.65 , pp. 493-501
    • Sitkovsky, M.V.1
  • 131
    • 0025967399 scopus 로고
    • Methotrexate inhibits neutrophil function by stimulating adenosine release from connective tissue cells
    • Cronstein, B. N., Eberle, M. A., Gruber, H. E. & Levin, R. I. Methotrexate inhibits neutrophil function by stimulating adenosine release from connective tissue cells. Proc. Natl Acad. Sci. USA 88, 2441-2446 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2441-2446
    • Cronstein, B.N.1    Eberle, M.A.2    Gruber, H.E.3    Levin, R.I.4
  • 132
    • 0027139914 scopus 로고
    • The antinflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation
    • Cronstein, B. N., Naime, D. & Ostad, E. The antinflammatory mechanism of methotrexate. Increased adenosine release at inflamed sites diminishes leukocyte accumulation in an in vivo model of inflammation. J. Clin. Invest. 92, 2675-2682 (1993).
    • (1993) J. Clin. Invest. , vol.92 , pp. 2675-2682
    • Cronstein, B.N.1    Naime, D.2    Ostad, E.3
  • 133
    • 0037207972 scopus 로고    scopus 로고
    • Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68
    • Montesinos, M. C. et al. Adenosine A2A or A3 receptors are required for inhibition of inflammation by methotrexate and its analog MX-68. Arthritis Rheum. 48, 240-247 (2003).
    • (2003) Arthritis Rheum. , vol.48 , pp. 240-247
    • Montesinos, M.C.1
  • 134
    • 0033559904 scopus 로고    scopus 로고
    • IFN-gamma up-ragulates the A2B adenosine receptor expression in macrophages: A mechanism of macrophage deactivation
    • Xaus, J. et al. IFN-gamma up-ragulates the A2B adenosine receptor expression in macrophages: a mechanism of macrophage deactivation. J. Immunol. 162, 3607-3614 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 3607-3614
    • Xaus, J.1
  • 135
    • 0036667395 scopus 로고    scopus 로고
    • Adenosine: A potential mediator of immunosuppression in multiple organ failure
    • Hasko, G., Deitch, E. A., Szabo, C., Nemeth, Z. H. & Vizi, E. S. Adenosine: a potential mediator of immunosuppression in multiple organ failure. Curr. Opin. Pharmacol 2, 440-444 (2002).
    • (2002) Curr. Opin. Pharmacol , vol.2 , pp. 440-444
    • Hasko, G.1    Deitch, E.A.2    Szabo, C.3    Nemeth, Z.H.4    Vizi, E.S.5
  • 136
    • 0037305002 scopus 로고    scopus 로고
    • Too much of a good thing: Adenosine overload in adenosine-deaminase-deficient mice
    • Blackburn, M. R. Too much of a good thing: adenosine overload in adenosine-deaminase-deficient mice. Trends Pharmacol. Sci. 24, 66-70 (2003).
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 66-70
    • Blackburn, M.R.1
  • 137
    • 1542347163 scopus 로고    scopus 로고
    • Targeting melanocortin receptors as a novel strategy to control inflammation
    • Catania, A., Gatti, S., Colombo, G. & Lipton, J. M. Targeting melanocortin receptors as a novel strategy to control inflammation. Pharmacol. Rev. 56, 1-29 (2004).
    • (2004) Pharmacol. Rev. , vol.56 , pp. 1-29
    • Catania, A.1    Gatti, S.2    Colombo, G.3    Lipton, J.M.4
  • 138
    • 0031849291 scopus 로고    scopus 로고
    • The role of phosphatidylserine in recognition of apoptotic cells by phagocytes
    • Fadok, V. A., Bratton, D. L., Frasch, S. C., Warner, M. L. & Henson, P. M. The role of phosphatidylserine in recognition of apoptotic cells by phagocytes. Cell Death Differ. 5, 551-562 (1998).
    • (1998) Cell Death Differ. , vol.5 , pp. 551-562
    • Fadok, V.A.1    Bratton, D.L.2    Frasch, S.C.3    Warner, M.L.4    Henson, P.M.5
  • 139
    • 0037390598 scopus 로고    scopus 로고
    • Annexin I is an endogenous ligand that mediates apoptotic cell engulfment
    • Arur, S. et al. Annexin I is an endogenous ligand that mediates apoptotic cell engulfment. Dev. Cell 4, 587-598 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 587-598
    • Arur, S.1
  • 140
    • 0036143018 scopus 로고    scopus 로고
    • Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation
    • Huynh, M. L., Fadok, V. A. & Henson, P. M. Phosphatidylserine-dependent ingestion of apoptotic cells promotes TGF-beta1 secretion and the resolution of inflammation. J. Clin. Invest. 109, 41-50 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 41-50
    • Huynh, M.L.1    Fadok, V.A.2    Henson, P.M.3
  • 141
    • 25944452163 scopus 로고    scopus 로고
    • Skewed balances in regulation of stimulating and inhibitory FC gamma receptors on macrophages of CIA sensitive mice
    • Blom, A. B., van Lent, P. L., Holthuysen, A. E. & van den Berg, W. B. Skewed balances in regulation of stimulating and inhibitory FC gamma receptors on macrophages of CIA sensitive mice. Inflamm. Res. 50 (Suppl. 3), S155 (2001).
    • (2001) Inflamm. Res. , vol.50 , Issue.SUPPL. 3
    • Blom, A.B.1    van Lent, P.L.2    Holthuysen, A.E.3    van den Berg, W.B.4
  • 142
    • 0024212633 scopus 로고
    • Transcellular conversion of endogenous arachidonic acid to lipoxins in mixed human platelet-granulocyte suspensions
    • Edenius, C., Haeggstrom, J. & Lindgren, J. A. Transcellular conversion of endogenous arachidonic acid to lipoxins in mixed human platelet-granulocyte suspensions. Biochem. Biophys. Res. Commun. 157, 801-807 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.157 , pp. 801-807
    • Edenius, C.1    Haeggstrom, J.2    Lindgren, J.A.3
  • 143
    • 0025008523 scopus 로고
    • Formation of lipoxins and leukotrienes during receptor-mediated interactions of human platelets and recombinant human granulocyte/macrophage colony-stimulating factor-primed neutrophils
    • Fiore, S. & Serhan, C. N. Formation of lipoxins and leukotrienes during receptor-mediated interactions of human platelets and recombinant human granulocyte/macrophage colony-stimulating factor-primed neutrophils. J. Exp. Med. 172, 1451-1457 (1990).
    • (1990) J. Exp. Med. , vol.172 , pp. 1451-1457
    • Fiore, S.1    Serhan, C.N.2
  • 144
    • 1542591247 scopus 로고
    • Lipoxins: Novel series of biologically active compounds formed from arachidonic acid in human leukocytes
    • Serhan, C. N., Hamberg, M. & Samuelsson, B. Lipoxins: novel series of biologically active compounds formed from arachidonic acid in human leukocytes. Proc. Natl Acad. Sci. USA 81, 5335-5339 (1984).
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5335-5339
    • Serhan, C.N.1    Hamberg, M.2    Samuelsson, B.3
  • 145
    • 0028818271 scopus 로고
    • Aspirin triggers previously undescribed bioactive eicosanoids by human endothelial cell-leukocyte interactions
    • Claria, J. & Serhan, C. N. Aspirin triggers previously undescribed bioactive eicosanoids by human endothelial cell-leukocyte interactions. Proc. Natl Acad. Sci. USA 92, 9475-9479 (1995).
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9475-9479
    • Claria, J.1    Serhan, C.N.2
  • 146
    • 85047689521 scopus 로고    scopus 로고
    • Interplay between IFN-gamma and IL-6 signaling governs neutrophil trafficking and apoptosis during acute inflammation
    • McLoughlin, R. M. et al. Interplay between IFN-gamma and IL-6 signaling governs neutrophil trafficking and apoptosis during acute inflammation. J. Clin. Invest. 112, 598-607 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 598-607
    • McLoughlin, R.M.1
  • 147
    • 0034960582 scopus 로고    scopus 로고
    • II-6 and its soluble receptor orchestrate a temporal switch in the pattern of leukocyte recruitment seen during acute inflammation
    • Hurst S. M. et al. II-6 and its soluble receptor orchestrate a temporal switch in the pattern of leukocyte recruitment seen during acute inflammation. Immunity 14, 705-714 (2001).
    • (2001) Immunity , vol.14 , pp. 705-714
    • Hurst, S.M.1
  • 148
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi, A. et al. Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403, 103-108 (2000).
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1
  • 149
    • 0033622133 scopus 로고    scopus 로고
    • Inhibition of IkappaB kinase and IkappaB phosphorylation by 15-deoxy-delta(12,14)-prostaglandin J(2) in activated murine macrophages
    • Castrillo, A., Diaz-Guerra, M. J., Hortelano, S., Martin-Sanz, P. & Bosca, L. Inhibition of IkappaB kinase and IkappaB phosphorylation by 15-deoxy-delta(12,14)-prostaglandin J(2) in activated murine macrophages. Mol. Cell. Biol. 20, 1692-1698 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 1692-1698
    • Castrillo, A.1    Diaz-Guerra, M.J.2    Hortelano, S.3    Martin-Sanz, P.4    Bosca, L.5
  • 150
    • 0035929592 scopus 로고    scopus 로고
    • 15-Deoxy-delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit
    • Cemuda-Morollon, E., Pineda-Molina, E., Canada, F. J. & Perez-Sala, D. 15-Deoxy-delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit. J. Biol. Chem. 276, 35530-35536 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35530-35536
    • Cemuda-Morollon, E.1    Pineda-Molina, E.2    Canada, F.J.3    Perez-Sala, D.4
  • 151
    • 0142186679 scopus 로고    scopus 로고
    • Biosynthesis of 15-deoxy delta 12,14-PGJ2 and the ligation of PPARgamma
    • Bell-Parikh, L. C. et al. Biosynthesis of 15-deoxy delta 12,14-PGJ2 and the ligation of PPARgamma. J. Clin. Invest. 112, 945-955 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 945-955
    • Bell-Parikh, L.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.