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Volumn 42, Issue 13, 1999, Pages 2295-2314

Therapeutic potential and strategies for inhibiting tumor necrosis factor-α

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 [4 (2 CARBOXYETHYL)PHENETHYLAMINO]ADENOSINE 5' (N ETHYLCARBOXAMIDE); 3 [5 (2,3 DIMETHOXY 6 METHYL 1,4 BENZOQUINOYL)] 2 NONYL 2 PROPENOIC ACID; 4 (1,1 DIMETHYLHEPTYL) 1',2',3',4',5',6' HEXAHYDRO 2,3' DIHYDROXY 6' (3 HYDROXYPROPYL)BIPHENYL; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 [2 [3 (CYCLOPENTYLOXY) 4 METHOXYPHENYL] 2 PHENYLETHYL]PYRIDINE; 5 (4 CHLORO 3 METHYLPHENYL) 1 (4 METHYLBENZYL) N (1,3,3 TRIMETHYLBICYCLO[2.2.1]HEPTAN 2 YL) 3 PYRAZOLECARBOXAMIDE; 5 (4 PYRIDINYL) 4 (4 FLUOROPHENYL) 1 (4 PIPERIDINYL)IMIDAZOLE; 6 (4 FLUOROPHENYL) 2,3 DIHYDRO 5 (4 PYRIDYL)IMIDAZO[2,1 B]THIAZOLE; AZELASTINE; BAY 103356; CILOMILAST; CYCLIC AMP; CYCLIC AMP PHOSPHODIESTERASE; DENBUFYLLINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MDL 201449A; METALLOPROTEINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; NEUTRALIZING ANTIBODY; NITRAQUAZONE; PHOSPHODIESTERASE INHIBITOR; PICLAMILAST; RESINIFERATOXIN; ROLIPRAM; SB 206718; SPHINGOMYELIN PHOSPHODIESTERASE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; THALIDOMIDE DERIVATIVE; TRISTETRAPROLIN; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA ANTIBODY; TUMOR NECROSIS FACTOR ALPHA RECEPTOR; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 0033168031     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm980541n     Document Type: Review
Times cited : (191)

References (249)
  • 2
    • 0022369998 scopus 로고
    • Tumor necrosis factor (TNF)
    • Old, L. Tumor necrosis factor (TNF). Science 1985, 230, 630-632.
    • (1985) Science , vol.230 , pp. 630-632
    • Old, L.1
  • 4
    • 0028143211 scopus 로고
    • Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor α (cA2) versus placebo in rheumatoid arthritis
    • Elliott, M.; Maini, R.; Feldmann, M.; Kalden, J.; Antoni, C.; Smolen, J.; Leeb, B.; Breedveld, F.; Macfarlane, J.; Bijl, H.; Woody, J. Randomised double-blind comparison of chimeric monoclonal antibody to tumour necrosis factor α (cA2) versus placebo in rheumatoid arthritis. Lancet 1994, 344, 1105-1110.
    • (1994) Lancet , vol.344 , pp. 1105-1110
    • Elliott, M.1    Maini, R.2    Feldmann, M.3    Kalden, J.4    Antoni, C.5    Smolen, J.6    Leeb, B.7    Breedveld, F.8    Macfarlane, J.9    Bijl, H.10    Woody, J.11
  • 8
    • 0028931724 scopus 로고
    • Increased adipose tissue expression of tumor necrosis factor-α in human obesity and insulin resistance
    • Hotamisligil, G.; Arner, P.; Caro, J.; Atkinson, R.; Spiegelman, B. Increased adipose tissue expression of tumor necrosis factor-α in human obesity and insulin resistance. J. Clin. Invest. 1995, 95, 2409-2415.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2409-2415
    • Hotamisligil, G.1    Arner, P.2    Caro, J.3    Atkinson, R.4    Spiegelman, B.5
  • 9
    • 0025852567 scopus 로고
    • Identification of lymphotoxin and tumor necrosis factor in multiple sclerosis lesions
    • Selmaj, K.; Raine, C.; Cannella, B.; Brosnan, C. Identification of lymphotoxin and tumor necrosis factor in multiple sclerosis lesions. J. Clin. Invest. 1991, 87, 949-954.
    • (1991) J. Clin. Invest. , vol.87 , pp. 949-954
    • Selmaj, K.1    Raine, C.2    Cannella, B.3    Brosnan, C.4
  • 10
    • 0028149025 scopus 로고
    • Splanchnic ischaemia and its role in multiple organ failure
    • Landow, L.; Andersen, L. Splanchnic ischaemia and its role in multiple organ failure. Acta Anaesthesiol. Scand. 1994, 38, 626-639.
    • (1994) Acta Anaesthesiol. Scand. , vol.38 , pp. 626-639
    • Landow, L.1    Andersen, L.2
  • 11
    • 0029114675 scopus 로고
    • Expression of a tumor necrosis factor-α transgene in murine lung causes lymphocytic and fibrosing alveolitis. A mouse model of progressive pulmonary fibrosis
    • Miyazaki, Y.; Araki, K.; Vesin, C.; Garcia, I.; Kapanci, Y.; Whitsett, J.; Piguet, P.; Vassalli, P. Expression of a tumor necrosis factor-α transgene in murine lung causes lymphocytic and fibrosing alveolitis. A mouse model of progressive pulmonary fibrosis. J. Clin. Invest. 1995, 96, 250-259.
    • (1995) J. Clin. Invest. , vol.96 , pp. 250-259
    • Miyazaki, Y.1    Araki, K.2    Vesin, C.3    Garcia, I.4    Kapanci, Y.5    Whitsett, J.6    Piguet, P.7    Vassalli, P.8
  • 12
    • 0025895853 scopus 로고
    • Tumor necrosis factor-alpha in human arterial wall with atherosclerosis
    • Rus, H.; Niculescu, F.; Vlaicu, R. Tumor necrosis factor-alpha in human arterial wall with atherosclerosis. Atherosclerosis 1991, 89, 247-254.
    • (1991) Atherosclerosis , vol.89 , pp. 247-254
    • Rus, H.1    Niculescu, F.2    Vlaicu, R.3
  • 13
    • 0027297663 scopus 로고
    • Mice deficient for the 55 kD tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection
    • Pfeffer, K.; Matsuyama, T.; Kundig, T.; Wakeham, A.; Kishihara, K.; Shahinian, A.; Wiegmann, K.; Ohaski, P.; Kronke, M.; Mak, T. Mice deficient for the 55 kD tumor necrosis factor receptor are resistant to endotoxic shock, yet succumb to L. monocytogenes infection. Cell 1993, 73, 457-467.
    • (1993) Cell , vol.73 , pp. 457-467
    • Pfeffer, K.1    Matsuyama, T.2    Kundig, T.3    Wakeham, A.4    Kishihara, K.5    Shahinian, A.6    Wiegmann, K.7    Ohaski, P.8    Kronke, M.9    Mak, T.10
  • 14
    • 0027327619 scopus 로고
    • Mice lacking the tumour necrosis factor receptor 1 are resistant to TNF-mediated toxicity but highly susceptible to infection by Listeria monocytogenes
    • Rothe, J.; Lesslauer, W.; Lotscher, H.; Lang, Y.; Koebel, P.; Kontgen, F.; Althage, A.; Zinkernagel, R.; Steinmetz, M.; Bluethmann, H. Mice lacking the tumour necrosis factor receptor 1 are resistant to TNF-mediated toxicity but highly susceptible to infection by Listeria monocytogenes. Nature 1993, 364, 798-802.
    • (1993) Nature , vol.364 , pp. 798-802
    • Rothe, J.1    Lesslauer, W.2    Lotscher, H.3    Lang, Y.4    Koebel, P.5    Kontgen, F.6    Althage, A.7    Zinkernagel, R.8    Steinmetz, M.9    Bluethmann, H.10
  • 15
    • 0030267786 scopus 로고    scopus 로고
    • Attenuation of collagen-induced arthritis in 55-kDa TNF receptor type 1 (TNFR1)-IgG1-treated and TNFR1-deficient mice
    • Mon, L.; Iselin, S.; De Libero, G.; Lesslauer, W. Attenuation of collagen-induced arthritis in 55-kDa TNF receptor type 1 (TNFR1)-IgG1-treated and TNFR1-deficient mice. J. Immunol. 1996, 157, 3178-3182.
    • (1996) J. Immunol. , vol.157 , pp. 3178-3182
    • Mon, L.1    Iselin, S.2    De Libero, G.3    Lesslauer, W.4
  • 17
    • 0029891052 scopus 로고    scopus 로고
    • Transmembrane TNF is sufficient to induce localized tissue toxicity and chronic inflammatory arthritis in transgenic mice
    • Georgopoulos, S.; Plows, D.; Kolias, G. Transmembrane TNF is sufficient to induce localized tissue toxicity and chronic inflammatory arthritis in transgenic mice. J. Inflamm. 1996, 46, 86-97.
    • (1996) J. Inflamm. , vol.46 , pp. 86-97
    • Georgopoulos, S.1    Plows, D.2    Kolias, G.3
  • 18
    • 0026039673 scopus 로고
    • Transgenic mice expressing human tumour necrosis factor: A predictive genetic model of arthritis
    • Keffer, J.; Probert, L.; Cazlaris, H.; Georgopoulos, S.; Kaslaris, E.; Kioussis, D.; Kollias, G. Transgenic mice expressing human tumour necrosis factor: a predictive genetic model of arthritis. EMBO J. 1991, 10, 4025-4031.
    • (1991) EMBO J. , vol.10 , pp. 4025-4031
    • Keffer, J.1    Probert, L.2    Cazlaris, H.3    Georgopoulos, S.4    Kaslaris, E.5    Kioussis, D.6    Kollias, G.7
  • 19
    • 0031028140 scopus 로고    scopus 로고
    • Initiation of liver growth by tumor necrosis factor: Deficient liver regeneration in mice lacking type I tumor necrosis factor receptor
    • Yamada, Y.; Kirillova, I.; Peschon, J.; Fausto, N. Initiation of liver growth by tumor necrosis factor: Deficient liver regeneration in mice lacking type I tumor necrosis factor receptor. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 1441-1446.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 1441-1446
    • Yamada, Y.1    Kirillova, I.2    Peschon, J.3    Fausto, N.4
  • 20
    • 0030240764 scopus 로고    scopus 로고
    • TNF receptors in murine Candida albicans infection: Evidence for an important role of TNF receptor p55 in antifungal defense
    • Steinshamm, S.; Bemelmans, M.; van Tits, L.; Bergh, K.; Buurman, W.; Waage, A. TNF receptors in murine Candida albicans infection: evidence for an important role of TNF receptor p55 in antifungal defense. J. Immunol. 1996, 157, 2155-2159.
    • (1996) J. Immunol. , vol.157 , pp. 2155-2159
    • Steinshamm, S.1    Bemelmans, M.2    Van Tits, L.3    Bergh, K.4    Buurman, W.5    Waage, A.6
  • 21
    • 0029982872 scopus 로고    scopus 로고
    • Mice lacking the TNF receptor p55 fail to resolve lesions caused by infection with Leishmania major, but control parasite replication
    • Vieira, L.; Goldschmidt, M.; Nashleanas, M.; Pfeffer, K.; Mak, T.; Scott, P. Mice lacking the TNF receptor p55 fail to resolve lesions caused by infection with Leishmania major, but control parasite replication. J. Immunol. 1996, 157, 827-835.
    • (1996) J. Immunol. , vol.157 , pp. 827-835
    • Vieira, L.1    Goldschmidt, M.2    Nashleanas, M.3    Pfeffer, K.4    Mak, T.5    Scott, P.6
  • 22
    • 0029991923 scopus 로고    scopus 로고
    • Role of lymphotoxin and the type I TNF receptor in the formation of germinal centers
    • Matsumoto, M.; Mariathasan, S.; Nahm, M.; Baranyay, F.; Peschon, J.; Chaplin, D. Role of lymphotoxin and the type I TNF receptor in the formation of germinal centers. Science 1996, 271, 1289-1291.
    • (1996) Science , vol.271 , pp. 1289-1291
    • Matsumoto, M.1    Mariathasan, S.2    Nahm, M.3    Baranyay, F.4    Peschon, J.5    Chaplin, D.6
  • 23
    • 0032103992 scopus 로고    scopus 로고
    • Control of Leishmania major infection in mice lacking TNF receptors
    • Nashleanas, M.; Kanaly, S.; Scott, P. Control of Leishmania major infection in mice lacking TNF receptors. J. Immunol. 1998, 160, 5506-5513.
    • (1998) J. Immunol. , vol.160 , pp. 5506-5513
    • Nashleanas, M.1    Kanaly, S.2    Scott, P.3
  • 24
    • 0030798465 scopus 로고    scopus 로고
    • Therapeutic potential of TNF-α inhibitors old and new
    • Marriott, J.; Westby, M.; Dalgleish, A. Therapeutic potential of TNF-α inhibitors old and new. Drug Discovery Today 1997, 2, 273-282.
    • (1997) Drug Discovery Today , vol.2 , pp. 273-282
    • Marriott, J.1    Westby, M.2    Dalgleish, A.3
  • 25
    • 0031896013 scopus 로고    scopus 로고
    • TNF-α inhibitors and rheumatoid arthritis
    • Shire, M.; Muller, G. TNF-α inhibitors and rheumatoid arthritis. Exp. Opin. Ther. Patents 1998, 8, 531-544.
    • (1998) Exp. Opin. Ther. Patents , vol.8 , pp. 531-544
    • Shire, M.1    Muller, G.2
  • 26
    • 77956747089 scopus 로고    scopus 로고
    • Agents that block TNF-α synthesis or activity
    • Black, R.; Bird, T.; Mohler, K. Agents that block TNF-α synthesis or activity. Annu. Rep. Med. Chem. 1997, 32, 241-250.
    • (1997) Annu. Rep. Med. Chem. , vol.32 , pp. 241-250
    • Black, R.1    Bird, T.2    Mohler, K.3
  • 27
    • 0029928366 scopus 로고    scopus 로고
    • Tumor necrosis factors: Developments during the past decade
    • Aggarwal, B.; Natarajan, K. Tumor necrosis factors: developments during the past decade. Eur. Cytokine. Network 1996, 7, 93-124.
    • (1996) Eur. Cytokine. Network , vol.7 , pp. 93-124
    • Aggarwal, B.1    Natarajan, K.2
  • 29
    • 0030002564 scopus 로고    scopus 로고
    • Authentic 17kDa tumour necrosis factor α is synthesized and released by canine mast cells and up-regulated by stem cell factor
    • Thomas, P.; Pennington, D.; Schreck, R.; Levine, T.; Lazarus, S. Authentic 17kDa tumour necrosis factor α is synthesized and released by canine mast cells and up-regulated by stem cell factor. Clin. Exp. Allergy 1996, 26, 710-718.
    • (1996) Clin. Exp. Allergy , vol.26 , pp. 710-718
    • Thomas, P.1    Pennington, D.2    Schreck, R.3    Levine, T.4    Lazarus, S.5
  • 30
    • 0031571737 scopus 로고    scopus 로고
    • Suppression of TNF-α secretion by azelastine in a rat mast cell (RBL-2H3) cell iine: Evidence for differential regulation of TNF-α release, transcription, and degranulation
    • Hide, I.; Toriu, N.; Nuibe, T.; Inoue, A.; Hide, M.; Yamamoto, S.; Nakata, Y. Suppression of TNF-α secretion by azelastine in a rat mast cell (RBL-2H3) cell iine: evidence for differential regulation of TNF-α release, transcription, and degranulation. J. Immunol. 1997, 159, 2932-2940.
    • (1997) J. Immunol. , vol.159 , pp. 2932-2940
    • Hide, I.1    Toriu, N.2    Nuibe, T.3    Inoue, A.4    Hide, M.5    Yamamoto, S.6    Nakata, Y.7
  • 32
    • 0031776896 scopus 로고    scopus 로고
    • LPS-binding proteins and receptors
    • Fenton, M.; Golenbock, D. LPS-binding proteins and receptors. J. Leukocyte Biol. 1998, 64, 25-32.
    • (1998) J. Leukocyte Biol. , vol.64 , pp. 25-32
    • Fenton, M.1    Golenbock, D.2
  • 33
    • 0026061116 scopus 로고
    • Multiple receptors for endotoxin
    • Wright, S. Multiple receptors for endotoxin. Curr. Opin. Immunol. 1991, 3, 83-90.
    • (1991) Curr. Opin. Immunol. , vol.3 , pp. 83-90
    • Wright, S.1
  • 35
    • 0026653049 scopus 로고
    • Lipopolysaccharide antagonists
    • Lynn, W.; Golenbock, D. Lipopolysaccharide antagonists. Immunol. Today 1992, 13, 271-276.
    • (1992) Immunol. Today , vol.13 , pp. 271-276
    • Lynn, W.1    Golenbock, D.2
  • 36
    • 0025853887 scopus 로고
    • Urate crystals stimulate production of tumor necrosis factor alpha from human blood monocytes and synovial cells. Cytokine mRNA and protein kinetics, and cellular distribution
    • di Giovine, F.; Malawista, S.; Thornton, E.; Duff, G. Urate crystals stimulate production of tumor necrosis factor alpha from human blood monocytes and synovial cells. Cytokine mRNA and protein kinetics, and cellular distribution. J. Clin. Invest. 1991, 87, 1375-1381.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1375-1381
    • Di Giovine, F.1    Malawista, S.2    Thornton, E.3    Duff, G.4
  • 37
    • 0026546935 scopus 로고
    • Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes
    • Beezhold, D.; Personius, C. Fibronectin fragments stimulate tumor necrosis factor secretion by human monocytes. J. Leukocyte Biol. 1992, 51, 59-64.
    • (1992) J. Leukocyte Biol. , vol.51 , pp. 59-64
    • Beezhold, D.1    Personius, C.2
  • 38
    • 0028903979 scopus 로고
    • Effects of fibronectin and group B streptococci on tumour necrosis factor-α production by human culture-derived macrophages
    • Peat, E.; Augustine, N.; Drummond, W.; Bohnsack, J.; Hill, H. Effects of fibronectin and group B streptococci on tumour necrosis factor-α production by human culture-derived macrophages. Immunology 1995, 84, 440-445.
    • (1995) Immunology , vol.84 , pp. 440-445
    • Peat, E.1    Augustine, N.2    Drummond, W.3    Bohnsack, J.4    Hill, H.5
  • 41
    • 0030613758 scopus 로고    scopus 로고
    • NF-κB activation: The IκB kinase revealed?
    • Stancovski, I.; Baltimore, D. NF-κB activation: the IκB kinase revealed? Cell 1997, 91, 299-302.
    • (1997) Cell , vol.91 , pp. 299-302
    • Stancovski, I.1    Baltimore, D.2
  • 42
    • 0030271387 scopus 로고    scopus 로고
    • NF-κB: Ten years after
    • Baeuerle, P.; Baltimore, D. NF-κB: Ten years after. Cell 1996, 87, 13-20.
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.1    Baltimore, D.2
  • 43
    • 0028817585 scopus 로고
    • Multiorgan inflammation and hematopoietic abnormalities in mice with targeted disruption of RelB, a member of the NF-κB/Rel family
    • Weih, F.; Carrasco, D.; SK, D.; Barton, D.; Rizzo, C.; Ryseck, R.; Lira, S.; Bravo, R. Multiorgan inflammation and hematopoietic abnormalities in mice with targeted disruption of RelB, a member of the NF-κB/Rel family. Cell 1995, 80, 331-340.
    • (1995) Cell , vol.80 , pp. 331-340
    • Weih, F.1    Carrasco, D.2    Sk, D.3    Barton, D.4    Rizzo, C.5    Ryseck, R.6    Lira, S.7    Bravo, R.8
  • 44
    • 0029150389 scopus 로고
    • Mice lacking the c-rel protooncogene exhibit defects in lymphocyte proliferation, humoral immunity and interleukin-2 expression
    • Koentgen, F.; Grumont, R.; Strasser, A.; Metcalf, D.; Li, R.; Tarlinton, D.; Gerondakis, S. Mice lacking the c-rel protooncogene exhibit defects in lymphocyte proliferation, humoral immunity and interleukin-2 expression. Genes Dev. 1995, 9, 1965-1977.
    • (1995) Genes Dev. , vol.9 , pp. 1965-1977
    • Koentgen, F.1    Grumont, R.2    Strasser, A.3    Metcalf, D.4    Li, R.5    Tarlinton, D.6    Gerondakis, S.7
  • 45
    • 0031298532 scopus 로고    scopus 로고
    • IL-11 regulates macrophage effector function through the inhibition of nuclear factor-κB
    • Trepicchio, W.; Wang, L.; Bozza, M.; Dorner, A. IL-11 regulates macrophage effector function through the inhibition of nuclear factor-κB. J. Immunol. 1997, 159, 5661-5670.
    • (1997) J. Immunol. , vol.159 , pp. 5661-5670
    • Trepicchio, W.1    Wang, L.2    Bozza, M.3    Dorner, A.4
  • 46
    • 0028867899 scopus 로고
    • Immunosuppression by glucocorticoids: Inhibition of NF-κB activity through induction of IκB synthesis
    • Auphan, N.; DiDonato, J.; Rosette, C.; Helmberg, A.; Karin, M. Immunosuppression by glucocorticoids: Inhibition of NF-κB activity through induction of IκB synthesis. Science 1995, 270, 286-290.
    • (1995) Science , vol.270 , pp. 286-290
    • Auphan, N.1    DiDonato, J.2    Rosette, C.3    Helmberg, A.4    Karin, M.5
  • 47
    • 0031586174 scopus 로고    scopus 로고
    • Identification and characterizationof an IκB kinase
    • Regnier, C.; Song, H.; Gao, X.; Goeddel, D.; Cao, Z.; Rothe, M. Identification and characterizationof an IκB kinase. Cell 1997, 90, 373-383.
    • (1997) Cell , vol.90 , pp. 373-383
    • Regnier, C.1    Song, H.2    Gao, X.3    Goeddel, D.4    Cao, Z.5    Rothe, M.6
  • 49
    • 0030611595 scopus 로고    scopus 로고
    • IκB kinase-B: NF-κB activation and complex formation with IκB kinase-α and NIK
    • Woronicz, J.; Gao, X.; Cao, Z.; Rothe, M.; Goeddel, D. IκB kinase-B: NF-κB activation and complex formation with IκB kinase-α and NIK. Science 1997, 278, 866-869.
    • (1997) Science , vol.278 , pp. 866-869
    • Woronicz, J.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.5
  • 50
    • 0028971289 scopus 로고
    • Rel/NF-κB/IκB family: Intimate tales of association and dissociation
    • Verma, I.; Stevenson, J.; Schwarz, E.; Van Antwerp, D.; Miyamoto, S. Rel/NF-κB/IκB family: intimate tales of association and dissociation. Genes Dev. 1995, 9, 2723-2735.
    • (1995) Genes Dev. , vol.9 , pp. 2723-2735
    • Verma, I.1    Stevenson, J.2    Schwarz, E.3    Van Antwerp, D.4    Miyamoto, S.5
  • 51
    • 0031017618 scopus 로고    scopus 로고
    • MAP3K-related kinase invovled in NF-κB induction by TNF, CD95 and IL-1
    • Malinin, N.; Boldin, M.; Kovalenko, A.; Wallach, D. MAP3K-related kinase invovled in NF-κB induction by TNF, CD95 and IL-1. Nature 1997, 385, 540-544.
    • (1997) Nature , vol.385 , pp. 540-544
    • Malinin, N.1    Boldin, M.2    Kovalenko, A.3    Wallach, D.4
  • 52
    • 0028884935 scopus 로고
    • Studies into the effect of the tyrosine kinase inhibitor herbimycin A on NF-κB activation in T lymphocytes: Evidence for covalent modification of the p50 subunit
    • Mahon, T.; O'Neill, L. Studies into the effect of the tyrosine kinase inhibitor herbimycin A on NF-κB activation in T lymphocytes: evidence for covalent modification of the p50 subunit. J. Biol Chem. 1995, 270, 28557-28563.
    • (1995) J. Biol Chem. , vol.270 , pp. 28557-28563
    • Mahon, T.1    O'Neill, L.2
  • 53
    • 0030588541 scopus 로고    scopus 로고
    • Capsaicin (8-methyl-N-vanillyl-6-nonenamide) is a potent inhibitor of nuclear transcription factor-κB activation by diverse agents
    • Singh, S.; Natarajan, K.; Aggarwal, B. Capsaicin (8-methyl-N-vanillyl-6-nonenamide) is a potent inhibitor of nuclear transcription factor-κB activation by diverse agents. J. Immunol. 1996, 157, 4412-4420.
    • (1996) J. Immunol. , vol.157 , pp. 4412-4420
    • Singh, S.1    Natarajan, K.2    Aggarwal, B.3
  • 54
    • 0028172869 scopus 로고
    • Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors
    • Finco, T.; Beg, A.; Baldwin, A. Inducible phosphorylation of IκBα is not sufficient for its dissociation from NF-κB and is inhibited by protease inhibitors. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 11884-11888.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11884-11888
    • Finco, T.1    Beg, A.2    Baldwin, A.3
  • 55
    • 0030587830 scopus 로고    scopus 로고
    • Postinduction transcriptional repression of E-selectin and vascular cell adhesion molecule-1
    • Read, M.; Neish, A.; Gerritsen, M.; Collins, T. Postinduction transcriptional repression of E-selectin and vascular cell adhesion molecule-1. J. Immunol. 1996, 157, 3472-3479.
    • (1996) J. Immunol. , vol.157 , pp. 3472-3479
    • Read, M.1    Neish, A.2    Gerritsen, M.3    Collins, T.4
  • 57
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs, M.; Harrison, S. Structure of an IκBα/NF-κB complex. Cell 1998, 95, 749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.1    Harrison, S.2
  • 58
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-IκB inactivat ion
    • Huxford, T.; Huang, D.; Malek, S.; Ghosh, G. The crystal structure of the IκBα/NF-κB complex reveals mechanisms of NF-IκB inactivat ion. Cell 1998, 95, 759-770.
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.2    Malek, S.3    Ghosh, G.4
  • 59
    • 0032493278 scopus 로고    scopus 로고
    • Efficient adenoviral infection with iκbα reveals that macrophage tumor necrosis factor α production in rheumatoid arthritis is NF-κB dependent
    • Foxwell, B.; Browne, K.; Bondeson, J.; Clarke, C.; de Martin, R.; Brennan, F.; Feldmann, M. Efficient adenoviral infection with IκBα reveals that macrophage tumor necrosis factor α production in rheumatoid arthritis is NF-κB dependent. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 8211-8215.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8211-8215
    • Foxwell, B.1    Browne, K.2    Bondeson, J.3    Clarke, C.4    De Martin, R.5    Brennan, F.6    Feldmann, M.7
  • 60
    • 0028175616 scopus 로고
    • The vanilloid (capsaicin) receptor: Receptor types and species differences
    • Szallasi, A. The vanilloid (capsaicin) receptor: receptor types and species differences. Gen. Pharmacol. 1994, 25, 223-225.
    • (1994) Gen. Pharmacol. , vol.25 , pp. 223-225
    • Szallasi, A.1
  • 62
    • 0028099150 scopus 로고
    • Signal transduction for nuclear factor-κB activation: Proposed location of antioxidant-inhibitable step
    • Suzuki, Y.; Mizuno, M.; Packer, L. Signal transduction for nuclear factor-κB activation: proposed location of antioxidant-inhibitable step. J. Immunol. 1994, 153, 5008-5013.
    • (1994) J. Immunol. , vol.153 , pp. 5008-5013
    • Suzuki, Y.1    Mizuno, M.2    Packer, L.3
  • 63
    • 0031936187 scopus 로고    scopus 로고
    • Preexposure to oxidative stress decreases the nuclear factor-κB-dependent transcription in T lymphocytes
    • Lahdenpohja, N.; Savinainen, K.; Hurme, M. Preexposure to oxidative stress decreases the nuclear factor-κB-dependent transcription in T lymphocytes. J. Immunol. 1998, 160, 1354-1358.
    • (1998) J. Immunol. , vol.160 , pp. 1354-1358
    • Lahdenpohja, N.1    Savinainen, K.2    Hurme, M.3
  • 64
    • 0031904316 scopus 로고    scopus 로고
    • Antioxidants attenuate anthralin-induced skin inflammation in BALB/c mice: Role of specific proinflammatory cytokines
    • Lange, R.; Germolec, D.; Foley, J.; Luster, M. Antioxidants attenuate anthralin-induced skin inflammation in BALB/c mice: role of specific proinflammatory cytokines. J. Leukocyte Biol. 1998, 64, 170-176.
    • (1998) J. Leukocyte Biol. , vol.64 , pp. 170-176
    • Lange, R.1    Germolec, D.2    Foley, J.3    Luster, M.4
  • 65
    • 0031942859 scopus 로고    scopus 로고
    • Anthralin stimulates keratinocyte-derived proinflammatory cytokines via generation of reactive oxygen species
    • Lange, R.; Hayden, P.; Chignell, C.; Luster, M. Anthralin stimulates keratinocyte-derived proinflammatory cytokines via generation of reactive oxygen species. Inflamm. Res. 1998, 47, 174-181.
    • (1998) Inflamm. Res. , vol.47 , pp. 174-181
    • Lange, R.1    Hayden, P.2    Chignell, C.3    Luster, M.4
  • 66
    • 0028810276 scopus 로고
    • Inhibitory effects of bisbenzyl-isoquinoline alkaloids on induction of proinflammatory cytokines, interleukin-1 and tumor necrosis factor-α
    • Onai, N.; Tsunokawa, Y.; Suda, M.; Watanabe, N.; Nakamura, K.; Sugimoto, Y.; Kobayashi, Y. Inhibitory effects of bisbenzyl-isoquinoline alkaloids on induction of proinflammatory cytokines, interleukin-1 and tumor necrosis factor-α. Planta Med. 1995, 61, 497-501.
    • (1995) Planta Med. , vol.61 , pp. 497-501
    • Onai, N.1    Tsunokawa, Y.2    Suda, M.3    Watanabe, N.4    Nakamura, K.5    Sugimoto, Y.6    Kobayashi, Y.7
  • 67
    • 0030032524 scopus 로고    scopus 로고
    • Intracellular pathways involved in tumor necrosis factor-α release by human monocytes on stimulation with lipopolysaccharide or staphlococcal peptidoglycan are partly similar
    • Mattsson, E.; Van Dijk, H.; Van Kessel, K.; Verhoef, J.; Fleer, A.; Rollof, J. Intracellular pathways involved in tumor necrosis factor-α release by human monocytes on stimulation with lipopolysaccharide or staphlococcal peptidoglycan are partly similar. J. Infect. Dis. 1996, 173, 212-218.
    • (1996) J. Infect. Dis. , vol.173 , pp. 212-218
    • Mattsson, E.1    Van Dijk, H.2    Van Kessel, K.3    Verhoef, J.4    Fleer, A.5    Rollof, J.6
  • 68
    • 0032055394 scopus 로고    scopus 로고
    • Inhibition of nuclear factor kappa-B by direct modification in whole cells - Mechanism of action of nordihydroguaiaritic acid, curcumin and thiol modifiers
    • Brennan, P.; O'Neill, L. Inhibition of nuclear factor kappa-B by direct modification in whole cells - mechanism of action of nordihydroguaiaritic acid, curcumin and thiol modifiers. Biochem. Pharmacol. 1998, 55, 965-973.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 965-973
    • Brennan, P.1    O'Neill, L.2
  • 69
    • 0028941827 scopus 로고
    • Antiinflammatory activity of salmetrol: Down-regulation of cytokine production
    • Sekut, L.; Champion, B.; Page, K.; Menius, J., Jr.; Connolly, K. Antiinflammatory activity of salmetrol: down-regulation of cytokine production. Clin. Exp. Immunol. 1995, 99, 461-466.
    • (1995) Clin. Exp. Immunol. , vol.99 , pp. 461-466
    • Sekut, L.1    Champion, B.2    Page, K.3    Menius J., Jr.4    Connolly, K.5
  • 70
    • 0028608842 scopus 로고
    • Antitumor necrosis factor properties of non-peptide drugs in acute-phase responses
    • Chen, Y.; Le Vraux, V.; Giroud, J.; Chauvelot-Moachon, L. Antitumor necrosis factor properties of non-peptide drugs in acute-phase responses. Eur. J. Pharmacol. 1994, 271, 319-327.
    • (1994) Eur. J. Pharmacol. , vol.271 , pp. 319-327
    • Chen, Y.1    Le Vraux, V.2    Giroud, J.3    Chauvelot-Moachon, L.4
  • 71
    • 0030019450 scopus 로고    scopus 로고
    • Inhibition of primary murine macrophage cytokine production in vitro following treatment with the κ-opioid agonist U50,488H
    • Alicea, C.; Belkowski, S.; Eisenstein, T.; Adler, M.; Rogers, T. Inhibition of primary murine macrophage cytokine production in vitro following treatment with the κ-opioid agonist U50,488H. J. Neuroimmunol. 1996, 64, 83-90.
    • (1996) J. Neuroimmunol. , vol.64 , pp. 83-90
    • Alicea, C.1    Belkowski, S.2    Eisenstein, T.3    Adler, M.4    Rogers, T.5
  • 72
    • 0001620703 scopus 로고
    • Forskolin, cyclic AMP and cellular physiology
    • Seamon, K; Daly, J. Forskolin, cyclic AMP and cellular physiology. Trends Pharmacol. Sci. 1983, 4, 120-123.
    • (1983) Trends Pharmacol. Sci. , vol.4 , pp. 120-123
    • Seamon, K.1    Daly, J.2
  • 73
    • 0023938335 scopus 로고
    • The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response
    • Kammer, G. The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response. Immunol. Today 1988, 9, 222-229.
    • (1988) Immunol. Today , vol.9 , pp. 222-229
    • Kammer, G.1
  • 74
    • 0028843942 scopus 로고
    • Immunosuppressive retroviral peptides: cAMP and cytokine patterns
    • Haraguchi, S.; Good, R.; Day, N. Immunosuppressive retroviral peptides: cAMP and cytokine patterns. Immunol. Today 1995, 16, 595-603.
    • (1995) Immunol. Today , vol.16 , pp. 595-603
    • Haraguchi, S.1    Good, R.2    Day, N.3
  • 75
    • 0031081561 scopus 로고    scopus 로고
    • Inhibition of tumour necrosis factor production in endotoxin-stimulated human mononuclear leukocytes by the prostacyclin analogue iloprost: Cellular mechanisms
    • Jorres, A.; Dinter, H.; Topley, N.; Gahl, G.; Frei, U.; Scholz, P. Inhibition of tumour necrosis factor production in endotoxin-stimulated human mononuclear leukocytes by the prostacyclin analogue iloprost: cellular mechanisms. Cytokine 1997, 9, 119-125.
    • (1997) Cytokine , vol.9 , pp. 119-125
    • Jorres, A.1    Dinter, H.2    Topley, N.3    Gahl, G.4    Frei, U.5    Scholz, P.6
  • 76
    • 0025878233 scopus 로고
    • Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity
    • Hai, T.; Curran, T. Cross-family dimerization of transcription factors Fos/Jun and ATF/CREB alters DNA binding specificity. Proc. Natl. Acad. Sci. U.S.A. 1991, 88, 3720-3724.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3720-3724
    • Hai, T.1    Curran, T.2
  • 77
    • 84989558482 scopus 로고
    • Suppression of lipopolysaccharide-stimulated release of tumor necrosis factor by adenosine: Evidence for A2 receptors on rat Kupffer cells
    • Reinstein, J.; Lichtman, S.; Currin, R.; Wang, J.; Thurman, R.; Lemasters, J. Suppression of lipopolysaccharide-stimulated release of tumor necrosis factor by adenosine: evidence for A2 receptors on rat Kupffer cells. Hepatology 1994, 19, 1445-1449.
    • (1994) Hepatology , vol.19 , pp. 1445-1449
    • Reinstein, J.1    Lichtman, S.2    Currin, R.3    Wang, J.4    Thurman, R.5    Lemasters, J.6
  • 78
    • 0028061703 scopus 로고
    • Differential regulatory effects of adenosine on cytokine release by activated human monocytes
    • Bouma, M.; Stad, R.; van den Wildenberg, A.; Buurman, W. Differential regulatory effects of adenosine on cytokine release by activated human monocytes. J. Immunol. 1994, 153, 4159-4168.
    • (1994) J. Immunol. , vol.153 , pp. 4159-4168
    • Bouma, M.1    Stad, R.2    Van Den Wildenberg, A.3    Buurman, W.4
  • 79
    • 0030605935 scopus 로고    scopus 로고
    • Activation of adenosine A3 receptors on J774.1 murine macrophages inhibits transcription of LPS-induced tumor necrosis factor-a by blocking NF-κB nuclear translocation
    • McWhinney, C.; De, M.; Dudley, M.; Bowlin, T.; Peet, N.; Schook, L.; Bradshaw, M.; De, D.; Borcherding, D.; Edwards, C. Activation of adenosine A3 receptors on J774.1 murine macrophages inhibits transcription of LPS-induced tumor necrosis factor-a by blocking NF-κB nuclear translocation. Eur. J. Pharmacol. 1996, 310, 209-216.
    • (1996) Eur. J. Pharmacol. , vol.310 , pp. 209-216
    • McWhinney, C.1    De, M.2    Dudley, M.3    Bowlin, T.4    Peet, N.5    Schook, L.6    Bradshaw, M.7    De, D.8    Borcherding, D.9    Edwards, C.10
  • 80
    • 0029915543 scopus 로고    scopus 로고
    • Inhibition of TNF-α expression by adenosine. Role of A3 adenosine receptors
    • Sajjadi, F.; Takabayashi, K.; Foster, A.; Domingo, R.; Firestein, G. Inhibition of TNF-α expression by adenosine. Role of A3 adenosine receptors. J. Immunol. 1996, 156, 3435-3442.
    • (1996) J. Immunol. , vol.156 , pp. 3435-3442
    • Sajjadi, F.1    Takabayashi, K.2    Foster, A.3    Domingo, R.4    Firestein, G.5
  • 81
    • 0030588630 scopus 로고    scopus 로고
    • Adenosine receptor agonists differentially regulate IL-10, TNF-a, and nitric oxide production in RAW 264.7 macrophages and in endotoxemic mice
    • Hasko, G.; Szabo, C.; Nemeth, Z.; Kvetan, V.; Pastores, S.; Vizi, E. Adenosine receptor agonists differentially regulate IL-10, TNF-a, and nitric oxide production in RAW 264.7 macrophages and in endotoxemic mice. J. Immunol. 1996, 157, 4634-4640.
    • (1996) J. Immunol. , vol.157 , pp. 4634-4640
    • Hasko, G.1    Szabo, C.2    Nemeth, Z.3    Kvetan, V.4    Pastores, S.5    Vizi, E.6
  • 82
    • 0029063510 scopus 로고
    • Specfic transcriptional inhibition of bone marrow derived macrophage TNF gene expression and protein production using novel enantomeric carbocyclic nucleoside analogues
    • Bradshaw, M.; Rutherford, M.; Schook, L.; Borcherding, D.; McWhinney, C.; Hoeper, B.; Edwards, C. Specfic transcriptional inhibition of bone marrow derived macrophage TNF gene expression and protein production using novel enantomeric carbocyclic nucleoside analogues. J. Pharmacol Exp. Ther. 1995, 273, 1506-1518.
    • (1995) J. Pharmacol Exp. Ther. , vol.273 , pp. 1506-1518
    • Bradshaw, M.1    Rutherford, M.2    Schook, L.3    Borcherding, D.4    McWhinney, C.5    Hoeper, B.6    Edwards, C.7
  • 83
    • 0027181961 scopus 로고
    • Adenosine and a related carbocyclic nucleoside analogue selectively inhibit tumor necrosis factor-α production and protect mice against endotoxin challenge
    • Parmely, M.; Zhou, W.; Edwards, C.; Borcherding, D.; Silverstein, R.; Morrison, D. Adenosine and a related carbocyclic nucleoside analogue selectively inhibit tumor necrosis factor-α production and protect mice against endotoxin challenge. J. Immunol. 1993, 151, 389-396.
    • (1993) J. Immunol. , vol.151 , pp. 389-396
    • Parmely, M.1    Zhou, W.2    Edwards, C.3    Borcherding, D.4    Silverstein, R.5    Morrison, D.6
  • 85
    • 0027515373 scopus 로고
    • Molecular characterization of a peripheral receptor for cannabinoids
    • Munro, S.; Thomas, K.; Abu-Shaar, M. Molecular characterization of a peripheral receptor for cannabinoids. Nature 1993, 365, 61-65.
    • (1993) Nature , vol.365 , pp. 61-65
    • Munro, S.1    Thomas, K.2    Abu-Shaar, M.3
  • 86
    • 0027999501 scopus 로고
    • Anadamide, an endogenous cannabinoid receptor agonist inhibits lymphocyte proliferation and induces apoptosis
    • Schwarz, H.; Blanco, F.; Lotz, M. Anadamide, an endogenous cannabinoid receptor agonist inhibits lymphocyte proliferation and induces apoptosis. J. Neuroimmunol. 1994, 55, 107-115.
    • (1994) J. Neuroimmunol. , vol.55 , pp. 107-115
    • Schwarz, H.1    Blanco, F.2    Lotz, M.3
  • 88
    • 0024355977 scopus 로고
    • In vitro activation and nuclear translocation of NF-κB catalyzed by cyclic AMP-dependent protein kinase and protein kinase C
    • Shirakawa, F.; Mizel, S. In vitro activation and nuclear translocation of NF-κB catalyzed by cyclic AMP-dependent protein kinase and protein kinase C. Mol. Cell. Biol. 1989, 9, 2424-2430.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 2424-2430
    • Shirakawa, F.1    Mizel, S.2
  • 89
    • 0029790065 scopus 로고    scopus 로고
    • Attenuation of inducible nitric oxide synthase gene expression by tetrahydrocannabinol is mediated through the inhibition of nuclear factor-κB/Rel activation
    • Jeon, Y.; Yang, K.; Pulaski, J.; Kaminski, N. Attenuation of inducible nitric oxide synthase gene expression by tetrahydrocannabinol is mediated through the inhibition of nuclear factor-κB/Rel activation. Mol. Pharmacol. 1996, 50, 334-341.
    • (1996) Mol. Pharmacol. , vol.50 , pp. 334-341
    • Jeon, Y.1    Yang, K.2    Pulaski, J.3    Kaminski, N.4
  • 90
    • 0029846519 scopus 로고    scopus 로고
    • Synthesis and pharmacology of a very potent cannabinoid lacking a phenolic hydroxyl with high affinity for the CB2 receptor
    • Huffman, J.; Yu, S.; Showalter, V.; Abood, M.; Wiley, J.; Compton, D.; Martin, B.; Bramblett, R.; Reggio, P. Synthesis and pharmacology of a very potent cannabinoid lacking a phenolic hydroxyl with high affinity for the CB2 receptor. J. Med. Chem. 1996, 39, 3875-3877.
    • (1996) J. Med. Chem. , vol.39 , pp. 3875-3877
    • Huffman, J.1    Yu, S.2    Showalter, V.3    Abood, M.4    Wiley, J.5    Compton, D.6    Martin, B.7    Bramblett, R.8    Reggio, P.9
  • 92
    • 0029031827 scopus 로고
    • Phosphodiesterase IV inhibitors: Structural diversity and therapeutic potential in asthma
    • Cavalla, D.; Frith, R. Phosphodiesterase IV inhibitors: Structural diversity and therapeutic potential in asthma. Curr. Med. Chem. 1995, 2, 561-572.
    • (1995) Curr. Med. Chem. , vol.2 , pp. 561-572
    • Cavalla, D.1    Frith, R.2
  • 93
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • Beavo, J.; Conti, M.; Heaslip, R. Multiple cyclic nucleotide phosphodiesterases. Mol. Pharmacol. 1994, 46, 399-405.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 399-405
    • Beavo, J.1    Conti, M.2    Heaslip, R.3
  • 94
    • 0028802726 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterases: Functional implications of multiple isoforms
    • Beavo, J. Cyclic nucleotide phosphodiesterases: Functional implications of multiple isoforms. Physiol. Rev. 1996, 75, 725-748.
    • (1996) Physiol. Rev. , vol.75 , pp. 725-748
    • Beavo, J.1
  • 95
    • 0025999955 scopus 로고
    • Cyclic nucleotide phosphodiesterases pharmacology biochemistry and function
    • Thompson, W. Cyclic nucleotide phosphodiesterases pharmacology biochemistry and function. Pharmacol. Ther. 1991, 51, 13-34.
    • (1991) Pharmacol. Ther. , vol.51 , pp. 13-34
    • Thompson, W.1
  • 96
    • 77956840791 scopus 로고
    • Isozyme-selective phosphodiesterase inhibitors as antiasthmatic agents
    • Christensen, S.; Torphy, T. Isozyme-selective phosphodiesterase inhibitors as antiasthmatic agents. Annu. Rep. Med. Chem. 1994, 185-194.
    • (1994) Annu. Rep. Med. Chem. , pp. 185-194
    • Christensen, S.1    Torphy, T.2
  • 98
    • 0032576647 scopus 로고    scopus 로고
    • Striking effect of hydroxamic acid substitution on the phosphodiesterase type 4 (PDE4) and TNF-alpha inhibitory activity of two series of rolipram analogues: Implications for a new active site model of PDE4
    • Kleinman, E.; Campbell, E.; Giordano, L.; Cohan, V.; Jenkinson, T.; Cheng, J.; Shirley, J.; Pettipher, E.; Salter, E.; Hibbs, T.; Dicapua, F.; Bordner, J. Striking effect of hydroxamic acid substitution on the phosphodiesterase type 4 (PDE4) and TNF-alpha inhibitory activity of two series of rolipram analogues: Implications for a new active site model of PDE4. J. Med. Chem. 1998, 41, 266-270.
    • (1998) J. Med. Chem. , vol.41 , pp. 266-270
    • Kleinman, E.1    Campbell, E.2    Giordano, L.3    Cohan, V.4    Jenkinson, T.5    Cheng, J.6    Shirley, J.7    Pettipher, E.8    Salter, E.9    Hibbs, T.10    Dicapua, F.11    Bordner, J.12
  • 100
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson, M.; Cobb, M. Mitogen-activated protein kinase pathways. Curr. Opin. Cell. Biol. 1997, 9, 180-186.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 180-186
    • Robinson, M.1    Cobb, M.2
  • 102
    • 0032521266 scopus 로고    scopus 로고
    • Inhibition of T cell activation by pharmacologic disruption of the MEK1/ERK MAP kinase or calcineurin signaling pathways results in differential modulation of cytokine production
    • Dumont, F.; Staruch, M.; Fischer, P.; DaSilva, C.; Camacho, R. Inhibition of T cell activation by pharmacologic disruption of the MEK1/ERK MAP kinase or calcineurin signaling pathways results in differential modulation of cytokine production. J. Immunol. 1998, 160, 2579-2589.
    • (1998) J. Immunol. , vol.160 , pp. 2579-2589
    • Dumont, F.1    Staruch, M.2    Fischer, P.3    DaSilva, C.4    Camacho, R.5
  • 103
    • 0031114648 scopus 로고    scopus 로고
    • FCγ receptor cross-linking activates p42, p38, and JNK/SAPK mitogen-activated protein kinases in murine macrophages: Role for p42 MAPK in FCγ receptor-stimulated TNF-α synthesis
    • Rose, D.; Winston, B.; Chan, E.; Riches, D.; Gerwins, P.; Johnson, G.; Henson, P. FCγ receptor cross-linking activates p42, p38, and JNK/SAPK mitogen-activated protein kinases in murine macrophages: role for p42 MAPK in FCγ receptor-stimulated TNF-α synthesis. J. Immunol. 1997, 158, 3433-3438.
    • (1997) J. Immunol. , vol.158 , pp. 3433-3438
    • Rose, D.1    Winston, B.2    Chan, E.3    Riches, D.4    Gerwins, P.5    Johnson, G.6    Henson, P.7
  • 104
    • 0030977398 scopus 로고    scopus 로고
    • Mitogen-activated protein (MAP) kinase regulates production of tumor necrosis-factor-α and release of arachionic acid in mast cells: Indication of communication between p38 and p42 MAP kinases
    • Zhang, C.; Baumgartner, R.; Yamada, K.; Beaven, M. Mitogen-activated protein (MAP) kinase regulates production of tumor necrosis-factor-α and release of arachionic acid in mast cells: indication of communication between p38 and p42 MAP kinases. J. Biol. Chem. 1997, 272, 13397-13402.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13397-13402
    • Zhang, C.1    Baumgartner, R.2    Yamada, K.3    Beaven, M.4
  • 105
    • 0029947996 scopus 로고    scopus 로고
    • MEK kinase is involved in tumor necrosis factor α-induced NF-κB activation and degradation of IκB-α
    • Hirano, M.; Osada, S,; Aoki, T.; Hirai, S.; Hosaka, M.; Inoue, J.; Ohno, S. MEK kinase is involved in tumor necrosis factor α-induced NF-κB activation and degradation of IκB-α. J. Biol. Chem. 1996, 271, 13234-13238.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13234-13238
    • Hirano, M.1    Osada, S.2    Aoki, T.3    Hirai, S.4    Hosaka, M.5    Inoue, J.6    Ohno, S.7
  • 106
    • 0031780201 scopus 로고    scopus 로고
    • YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-alpha production and downregulation of the MAP kinases p38 and JNK
    • Palmer, L.; Hobbie, S.; Galan, J.; Bliska, J. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF-alpha production and downregulation of the MAP kinases p38 and JNK. Mol. Microbiol. 1998, 27, 953-965.
    • (1998) Mol. Microbiol. , vol.27 , pp. 953-965
    • Palmer, L.1    Hobbie, S.2    Galan, J.3    Bliska, J.4
  • 107
    • 0022219890 scopus 로고
    • Preparation and antiarthritic and analgesic activity of 4 5 diaryl-2-substituted thio-1h-imidazoles and their sulfoxides and sulfones
    • Sharpe, T.; Cherkofsky, S.; Hewes, W.; Smith, D.; Gregory, W.; Haber, S.; Leadbetter, M.; Whitney, J. Preparation and antiarthritic and analgesic activity of 4 5 diaryl-2-substituted thio-1h-imidazoles and their sulfoxides and sulfones. J. Med. Chem. 1985, 28, 1188-1194.
    • (1985) J. Med. Chem. , vol.28 , pp. 1188-1194
    • Sharpe, T.1    Cherkofsky, S.2    Hewes, W.3    Smith, D.4    Gregory, W.5    Haber, S.6    Leadbetter, M.7    Whitney, J.8
  • 109
    • 0029090620 scopus 로고
    • Mechanism of action of bicyclic imidazoles defines a translational regulatory pathway for tumor necrosis factor alpha
    • Prichett, W.; Hand, A.; Sheilds, J.; Dunnington, D. Mechanism of action of bicyclic imidazoles defines a translational regulatory pathway for tumor necrosis factor alpha. J. Inflamm. 1995, 45, 97-105.
    • (1995) J. Inflamm. , vol.45 , pp. 97-105
    • Prichett, W.1    Hand, A.2    Sheilds, J.3    Dunnington, D.4
  • 112
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAP kinase kinase (MKK6)
    • Han, J.; Lee, J.; Jiang, Y.; Li, Z.; Feng, L.; Ulevitch, R. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J. Biol. Chem. 1996, 271, 2886-2891.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2886-2891
    • Han, J.1    Lee, J.2    Jiang, Y.3    Z, L.4    Feng, L.5    Ulevitch, R.6
  • 113
    • 0023740078 scopus 로고
    • Inhibition of monocyte IL-1 production by the antiinflammatory compound SKF-86002
    • Lee, J.; Griswold, D.; Votta, B.; Hanna, N. Inhibition of monocyte IL-1 production by the antiinflammatory compound SKF-86002. Int. J. Immunopharmacol. 1988, 10, 835-844.
    • (1988) Int. J. Immunopharmacol. , vol.10 , pp. 835-844
    • Lee, J.1    Griswold, D.2    Votta, B.3    Hanna, N.4
  • 116
    • 0030954172 scopus 로고    scopus 로고
    • A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket
    • Tong, L.; Pav, S.; White, D.; Rogers, S.; Crane, K.; Cywin, C. A highly specific inhibitor of human p38 MAP kinase binds in the ATP pocket. Nature Struct. Biol. 1997, 4, 311-316.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 311-316
    • Tong, L.1    Pav, S.2    White, D.3    Rogers, S.4    Crane, K.5    Cywin, C.6
  • 119
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda, A.; Rouse, J.; Doza, Y. N.; Meier, R.; Cohen, P.; Gallagher, T. F.; Young, P. R.; Lee, J. C. SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett. 1995, 364, 229-233.
    • (1995) FEBS Lett. , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 121
    • 0029982777 scopus 로고    scopus 로고
    • Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors
    • Xu, R.; Carmel, G.; Kuret, J.; Cheng, X. Structural basis for selectivity of the isoquinoline sulfonamide family of protein kinase inhibitors. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 6308-6313.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6308-6313
    • Xu, R.1    Carmel, G.2    Kuret, J.3    Cheng, X.4
  • 123
    • 0030458635 scopus 로고    scopus 로고
    • Pharmacology of cytokine suppressive antiinflammatory drug binding protein (CSBP), a novel stress-induced kinase
    • Griswold, D.; Young, P. Pharmacology of cytokine suppressive antiinflammatory drug binding protein (CSBP), a novel stress-induced kinase. Pharmacol. Commun. 1996, 7, 323-329.
    • (1996) Pharmacol. Commun. , vol.7 , pp. 323-329
    • Griswold, D.1    Young, P.2
  • 125
    • 0029565539 scopus 로고
    • Substance P induces tumor necrosis factor in anex vivo model system
    • Nair, M.; Schwartz, S. Substance P induces tumor necrosis factor in anex vivo model system. Cell. Immunol. 1995, 166, 286-290.
    • (1995) Cell. Immunol. , vol.166 , pp. 286-290
    • Nair, M.1    Schwartz, S.2
  • 127
    • 0030641290 scopus 로고    scopus 로고
    • Regulation of tumor necrosis factor-α and IL-1β synthesis by thromboxane A2 in nonadherent human monocytes
    • Caughey, G.; Pouliot, M.; Cleland, L.; James, M. Regulation of tumor necrosis factor-α and IL-1β synthesis by thromboxane A2 in nonadherent human monocytes. J. Immunol. 1997, 158, 351-358.
    • (1997) J. Immunol. , vol.158 , pp. 351-358
    • Caughey, G.1    Pouliot, M.2    Cleland, L.3    James, M.4
  • 128
    • 0031058155 scopus 로고    scopus 로고
    • Suppression of tumor necrosis factor-α production by interleukin-10 is enhanced by cAMP-elevating agents
    • Siegmund, B.; Eigler, A.; Moeller, J.; Greten, T.; Hartmann, G.; Endres, S. Suppression of tumor necrosis factor-α production by interleukin-10 is enhanced by cAMP-elevating agents. Eur. J. Pharmacol 1997, 321, 231-239.
    • (1997) Eur. J. Pharmacol , vol.321 , pp. 231-239
    • Siegmund, B.1    Eigler, A.2    Moeller, J.3    Greten, T.4    Hartmann, G.5    Endres, S.6
  • 129
    • 0028176655 scopus 로고
    • Interleukin 13, an interleukin 4-like cytokine that acts on monocytes and B cells, but not on T cells
    • Zurawski, G.; deVries, J. Interleukin 13, an interleukin 4-like cytokine that acts on monocytes and B cells, but not on T cells. Immunol. Today 1994,
    • (1994) Immunol. Today
    • Zurawski, G.1    DeVries, J.2
  • 130
    • 0032525051 scopus 로고    scopus 로고
    • Regulation of TNF-α production in activated mouse macrophages by progesterone
    • Miller, L.; Hunt, J. Regulation of TNF-α production in activated mouse macrophages by progesterone. J. Immunol. 1998, 160, 5098-5104.
    • (1998) J. Immunol. , vol.160 , pp. 5098-5104
    • Miller, L.1    Hunt, J.2
  • 131
    • 0029557984 scopus 로고
    • Fenspiride: An antiinflammatory drug with potential benefits in the treatment of endotoxemia
    • De Castro, C.; Nahori, M.; Dumarey, C.; Vargaftig, B.; Bachelet, M. Fenspiride: an antiinflammatory drug with potential benefits in the treatment of endotoxemia. Eur. J. Pharmacol. 1995, 294, 669-676.
    • (1995) Eur. J. Pharmacol. , vol.294 , pp. 669-676
    • De Castro, C.1    Nahori, M.2    Dumarey, C.3    Vargaftig, B.4    Bachelet, M.5
  • 132
    • 0029947010 scopus 로고    scopus 로고
    • Effects of bisphosphonates on interleukin 1, tumor necrosis factor α, and β2 microglobulin in rheumatoid arthritis
    • Cantatore, F.; Introsso, A.; Carrozzo, M. Effects of bisphosphonates on interleukin 1, tumor necrosis factor α, and β2 microglobulin in rheumatoid arthritis. J. Rheumatol. 1996, 23, 1117-1118.
    • (1996) J. Rheumatol. , vol.23 , pp. 1117-1118
    • Cantatore, F.1    Introsso, A.2    Carrozzo, M.3
  • 134
    • 0030882762 scopus 로고    scopus 로고
    • Taming TNF: Strategies to restrain this proinflammatory cytokine
    • Eigler, A.; Sinha, B.; Hartmann, G.; Endres, S. Taming TNF: strategies to restrain this proinflammatory cytokine. Immunol. Today 1997, 10, 487-492.
    • (1997) Immunol. Today , vol.10 , pp. 487-492
    • Eigler, A.1    Sinha, B.2    Hartmann, G.3    Endres, S.4
  • 135
    • 0025282043 scopus 로고
    • Dexamethasone and pentoxyfylline inhibit endotoxin-induced cachectin/tumor necrosis factor synthesis at separate points in the signaling pathway
    • Han, J.; Thompson, P.; Beutler, B. Dexamethasone and pentoxyfylline inhibit endotoxin-induced cachectin/tumor necrosis factor synthesis at separate points in the signaling pathway. J. Exp. Med. 1990, 172, 391-394.
    • (1990) J. Exp. Med. , vol.172 , pp. 391-394
    • Han, J.1    Thompson, P.2    Beutler, B.3
  • 136
    • 0026080801 scopus 로고
    • Thalidomide selectively inhibits tumor necrosis factor α production by stimulated human monocytes
    • Sampaio, E.; Sarno, E.; Galilly, R.; Cohn, S.; Kaplan, G. Thalidomide selectively inhibits tumor necrosis factor α production by stimulated human monocytes. J. Exp. Med. 1991, 173, 699-705.
    • (1991) J. Exp. Med. , vol.173 , pp. 699-705
    • Sampaio, E.1    Sarno, E.2    Galilly, R.3    Cohn, S.4    Kaplan, G.5
  • 137
    • 0030730162 scopus 로고    scopus 로고
    • Thalidomide and derivatives: Immunological investigations of tumour necrosis factor-alpha (TNF-α) inhibition suggest drugs capable of selective gene regulation
    • McHugh, S.; Rowland, T. Thalidomide and derivatives: immunological investigations of tumour necrosis factor-alpha (TNF-α) inhibition suggest drugs capable of selective gene regulation. Clin. Exp. Immunol. 1997, 110, 151-154.
    • (1997) Clin. Exp. Immunol. , vol.110 , pp. 151-154
    • McHugh, S.1    Rowland, T.2
  • 138
    • 0013442966 scopus 로고
    • Genes for the tumor necrosis factors alpha and beta are linked to the human major histocompatibility complex
    • Spies, T.; Morton, C.; Nedospasov, S.; Fiers, W.; Pious, D.; Strominger, J. Genes for the tumor necrosis factors alpha and beta are linked to the human major histocompatibility complex. Proc. Natl Acad. Sci. U.S.A. 1986, 83, 8699-8702.
    • (1986) Proc. Natl Acad. Sci. U.S.A. , vol.83 , pp. 8699-8702
    • Spies, T.1    Morton, C.2    Nedospasov, S.3    Fiers, W.4    Pious, D.5    Strominger, J.6
  • 141
    • 0025223225 scopus 로고
    • Structural analysis of the rabbit TNF locus, containing the genes encoding TNF-β (lymphotoxin) and TNF-α (tumor necrosis factor)
    • Shakhov, A.; Kuprash, D.; Azizov, M.; Jongeneel, C.; Nedospasov, S. Structural analysis of the rabbit TNF locus, containing the genes encoding TNF-β (lymphotoxin) and TNF-α (tumor necrosis factor). Gene 1990, 95, 215-221.
    • (1990) Gene , vol.95 , pp. 215-221
    • Shakhov, A.1    Kuprash, D.2    Azizov, M.3    Jongeneel, C.4    Nedospasov, S.5
  • 142
    • 0027359797 scopus 로고
    • Cloning and characterization of human TNF alpha promoter region
    • Takashiba, S.; Shapira, L.; Amar, S.; Van Dyke, T. Cloning and characterization of human TNF alpha promoter region. Gene 1993, 131, 307-308.
    • (1993) Gene , vol.131 , pp. 307-308
    • Takashiba, S.1    Shapira, L.2    Amar, S.3    Van Dyke, T.4
  • 143
    • 0025186678 scopus 로고
    • κB-type enhancers are involved in LPS-mediated transcriptional activation of the TNF-α gene in primary macrophages
    • Shakhov, A.; Collart, M.; Vassali, P.; Nedospasov, S.; Jongeneel, C. κB-type enhancers are involved in LPS-mediated transcriptional activation of the TNF-α gene in primary macrophages. J. Exp. Med. 1990, 171, 35-48.
    • (1990) J. Exp. Med. , vol.171 , pp. 35-48
    • Shakhov, A.1    Collart, M.2    Vassali, P.3    Nedospasov, S.4    Jongeneel, C.5
  • 144
    • 0031895658 scopus 로고    scopus 로고
    • Tumor-necrosis-factor-alpha gene-regulation - Enhancement of C/EBP-beta-induced activation by c-jun
    • Zagariya, A.; Mungre, S.; Lovis, R.; Birrer, M.; Ness, S.; Thimmapaya, B.; Pope, R. Tumor-necrosis-factor-alpha gene-regulation - enhancement of C/EBP-beta-induced activation by c-jun. Mol. Cell. Biol. 1998, 18, 2815-2824.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2815-2824
    • Zagariya, A.1    Mungre, S.2    Lovis, R.3    Birrer, M.4    Ness, S.5    Thimmapaya, B.6    Pope, R.7
  • 146
    • 0030050784 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp
    • Tsai, E.; Jain, J.; Pesavento, P.; Rao, A.; Goldfield, A. Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp. Mol. Cell. Biol. 1996, 16, 459-467.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 459-467
    • Tsai, E.1    Jain, J.2    Pesavento, P.3    Rao, A.4    Goldfield, A.5
  • 148
    • 0028167846 scopus 로고
    • Inhibition of NF-kappa B by sodium salicylate and aspirin
    • Kopp, E.; Ghosh, S. Inhibition of NF-kappa B by sodium salicylate and aspirin. Science 1994, 265, 956-959.
    • (1994) Science , vol.265 , pp. 956-959
    • Kopp, E.1    Ghosh, S.2
  • 149
    • 0029799831 scopus 로고    scopus 로고
    • Neuroprotection by aspirin and sodium salicylate through blockade of NF-κB activation
    • Grilli, M.; Pizzi, M.; Memo, M.; Spano, P. Neuroprotection by aspirin and sodium salicylate through blockade of NF-κB activation. Science 1996, 274, 1383-1385.
    • (1996) Science , vol.274 , pp. 1383-1385
    • Grilli, M.1    Pizzi, M.2    Memo, M.3    Spano, P.4
  • 150
    • 0030013325 scopus 로고    scopus 로고
    • 2-aminopurine selectively inhibits splicing of tumor necrosis factor alpha mRNA
    • Jarrous, N.; Osman, F.; Kaempfer, R. 2-aminopurine selectively inhibits splicing of tumor necrosis factor alpha mRNA. Mol. Cell. Biol. 1996, 16, 2814-2822.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2814-2822
    • Jarrous, N.1    Osman, F.2    Kaempfer, R.3
  • 152
    • 0029894439 scopus 로고    scopus 로고
    • Binding of a protein to an AU-rich domain of tumour necrosis factor α mRNA as a 35 kDa complex and its regulation in primary rat astrocytes
    • Kim, Y.; Rus, H.; Fisher, S.; Pitha, P.; Shin, M. Binding of a protein to an AU-rich domain of tumour necrosis factor α mRNA as a 35 kDa complex and its regulation in primary rat astrocytes. Biochem. J. 1996, 316, 455-460.
    • (1996) Biochem. J. , vol.316 , pp. 455-460
    • Kim, Y.1    Rus, H.2    Fisher, S.3    Pitha, P.4    Shin, M.5
  • 153
    • 0031047431 scopus 로고    scopus 로고
    • Cytokine production in the brain following closed head injury: Dexanabinol (HU-211) is a novel TNF-α inhibitor and an effective neuroprotectant
    • Shohami, E.; Gallily, R.; Mechoulam, R.; Bass, R.; Ben-Hur, T. Cytokine production in the brain following closed head injury: dexanabinol (HU-211) is a novel TNF-α inhibitor and an effective neuroprotectant. J. Neuroimmunol. 1997, 72, 169-177.
    • (1997) J. Neuroimmunol. , vol.72 , pp. 169-177
    • Shohami, E.1    Gallily, R.2    Mechoulam, R.3    Bass, R.4    Ben-Hur, T.5
  • 155
    • 0028820623 scopus 로고
    • ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions
    • Wolfsberg, T.; Primakoff, P.; Myles, D.; White, J. ADAM, a novel family of membrane proteins containing a disintegrin and metalloprotease domain: Multipotential functions in cell-cell and cell-matrix interactions, J. Cell. Biol. 1995, 131, 275-278.
    • (1995) J. Cell. Biol. , vol.131 , pp. 275-278
    • Wolfsberg, T.1    Primakoff, P.2    Myles, D.3    White, J.4
  • 165
    • 0023091045 scopus 로고
    • Tumour necrosis factor is a compact trimer
    • Wingfield, P.; Pain, R.; Craig, S. Tumour necrosis factor is a compact trimer. FEBS Lett. 1987, 211, 179-184.
    • (1987) FEBS Lett. , vol.211 , pp. 179-184
    • Wingfield, P.1    Pain, R.2    Craig, S.3
  • 166
    • 0027211704 scopus 로고
    • Crystal structure of the soluble human 55kd TNF receptor-human TNF/β complex: Implications for TNF receptor activation
    • Banner, D.; D'Arcy, A.; Janes, W.; Gentz, R.; Schoenfeld, H.; Broger, C.; Loetscher, H.; Lesslauer, W. Crystal structure of the soluble human 55kd TNF receptor-human TNF/β complex: implications for TNF receptor activation. Cell 1993, 73, 431-445.
    • (1993) Cell , vol.73 , pp. 431-445
    • Banner, D.1    D'Arcy, A.2    Janes, W.3    Gentz, R.4    Schoenfeld, H.5    Broger, C.6    Loetscher, H.7    Lesslauer, W.8
  • 167
    • 0007511791 scopus 로고    scopus 로고
    • Use of anti-TNFa therapies as potential treatments for rheumatoid arthritis
    • Heath, P. Use of anti-TNFa therapies as potential treatments for rheumatoid arthritis. ID Res. Alert 1997, 1, 235-240.
    • (1997) ID Res. Alert , vol.1 , pp. 235-240
    • Heath, P.1
  • 169
    • 0030881463 scopus 로고    scopus 로고
    • Anaemia of chronic disease in rheumatoid arthritis: In vivo effects of tumor necrosis factor α blockade
    • Davis, D.; Charles, P.; Potter, A.; Feldmann, M.; Maini, R.; Elliott, M. Anaemia of chronic disease in rheumatoid arthritis: in vivo effects of tumor necrosis factor α blockade. Br. J. Rheumatol. 1997, 36, 950-956.
    • (1997) Br. J. Rheumatol. , vol.36 , pp. 950-956
    • Davis, D.1    Charles, P.2    Potter, A.3    Feldmann, M.4    Maini, R.5    Elliott, M.6
  • 170
    • 0029751983 scopus 로고    scopus 로고
    • Increased MRI activity and immune activation in two multiple sclerosis patients treated with the monoclonal antitumor necrosis factor antibody cA2
    • van Oosten, B.; Barkhof, F.; Truyen, L.; Boringa, J.; Bertelsmann, F.; von Blomberg, B.; Woody, J.; Hartung, H.; Polman, C. Increased MRI activity and immune activation in two multiple sclerosis patients treated with the monoclonal antitumor necrosis factor antibody cA2. Neurology 1996, 47, 1531-1534.
    • (1996) Neurology , vol.47 , pp. 1531-1534
    • Van Oosten, B.1    Barkhof, F.2    Truyen, L.3    Boringa, J.4    Bertelsmann, F.5    Von Blomberg, B.6    Woody, J.7    Hartung, H.8    Polman, C.9
  • 171
    • 0029044028 scopus 로고
    • The therapeutic effects of an engineered human anti-tumour necrosis factor antibody (CDP571) in rheumatoid arthritis
    • Rankin, E. C.; Choy, E. H.; Kassimos, D.; Kingsley, G. H.; Sopwith, A. M.; Isenberg, D. A.; Panayi, G. S. The therapeutic effects of an engineered human anti-tumour necrosis factor antibody (CDP571) in rheumatoid arthritis. Br. J. Rheumatol. 1995, 34, 334-342.
    • (1995) Br. J. Rheumatol. , vol.34 , pp. 334-342
    • Rankin, E.C.1    Choy, E.H.2    Kassimos, D.3    Kingsley, G.H.4    Sopwith, A.M.5    Isenberg, D.A.6    Panayi, G.S.7
  • 173
  • 175
    • 0025347603 scopus 로고
    • Characterization of a tumor necrosis factor α (TNF-α) inhibitor: Evidence of immunological cross-reactivity with the TNF receptor
    • Seckinger, P.; Zhang, J.; Hauptmann, B.; Dayer, J. Characterization of a tumor necrosis factor α (TNF-α) inhibitor: Evidence of immunological cross-reactivity with the TNF receptor. Proc. Natl. Acad. Sci. U.S.A. 1990, 87, 5188-5192.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5188-5192
    • Seckinger, P.1    Zhang, J.2    Hauptmann, B.3    Dayer, J.4
  • 176
    • 0025165135 scopus 로고
    • Two tumor necrosis factor-binding proteins purified from human urine: Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors
    • Engelmann, H.; Novick, D.; Wallach, D. Two tumor necrosis factor-binding proteins purified from human urine: Evidence for immunological cross-reactivity with cell surface tumor necrosis factor receptors. J. Biol. Chem. 1990, 265, 1531-1536.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1531-1536
    • Engelmann, H.1    Novick, D.2    Wallach, D.3
  • 177
    • 0025113598 scopus 로고
    • Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor
    • Nophar, Y.; Kemper, O.; Brakebusch, C.; Engelmann, H.; Zwang, R.; Aderka, D.; Holtmann, H.; Wallach, D. Soluble forms of tumor necrosis factor receptors (TNF-Rs). The cDNA for the type I TNF-R, cloned using amino acid sequence data of its soluble form, encodes both the cell surface and a soluble form of the receptor. EMBO J. 1990, 9, 3269-3278.
    • (1990) EMBO J. , vol.9 , pp. 3269-3278
    • Nophar, Y.1    Kemper, O.2    Brakebusch, C.3    Engelmann, H.4    Zwang, R.5    Aderka, D.6    Holtmann, H.7    Wallach, D.8
  • 178
    • 0028043394 scopus 로고
    • Protective effect of 55-but not 75-kD soluble tumor necrosis factor receptor-immunoglobulin G fusion proteins in an animal model of gram-negative sepsis
    • Evans, T.; Moyes, D.; Carpenter, A.; Martin, R.; Loetscher, H.; Lesslauer, W.; Cohen, J. Protective effect of 55-but not 75-kD soluble tumor necrosis factor receptor-immunoglobulin G fusion proteins in an animal model of gram-negative sepsis. J. Exp. Med. 1994, 180, 2173-2179.
    • (1994) J. Exp. Med. , vol.180 , pp. 2173-2179
    • Evans, T.1    Moyes, D.2    Carpenter, A.3    Martin, R.4    Loetscher, H.5    Lesslauer, W.6    Cohen, J.7
  • 179
    • 0030300135 scopus 로고    scopus 로고
    • Production of prostaglandin EZ and collagenase is inhibited by the recombinant soluble tumour necrosis factor receptor p55-human γ3 fusion protein at concentrations a 100-fold lower than those decreasing T cell activation
    • Nicod, L.; Isler, P.; Chicheportiche, R.; Songeon, F.; Dayer, J. Production of prostaglandin EZ and collagenase is inhibited by the recombinant soluble tumour necrosis factor receptor p55-human γ3 fusion protein at concentrations a 100-fold lower than those decreasing T cell activation. Eur. Cytokine Network 1996, 7, 757-763.
    • (1996) Eur. Cytokine Network , vol.7 , pp. 757-763
    • Nicod, L.1    Isler, P.2    Chicheportiche, R.3    Songeon, F.4    Dayer, J.5
  • 180
    • 0028104632 scopus 로고
    • Effects of therapy with soluble tumour necrosis factor receptor fusion protein on pulmonary cytokine expression and lung injury following haemorrhage and resuscitation
    • Abraham, E.; Coulson, W.; Schwartz, M.; Allbee, J. Effects of therapy with soluble tumour necrosis factor receptor fusion protein on pulmonary cytokine expression and lung injury following haemorrhage and resuscitation. Clin. Exp. Immunol. 1994, 98, 29-34.
    • (1994) Clin. Exp. Immunol. , vol.98 , pp. 29-34
    • Abraham, E.1    Coulson, W.2    Schwartz, M.3    Allbee, J.4
  • 183
    • 0025880218 scopus 로고
    • Myxoma virus expresses a screted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence
    • Upton, C.; Macen, J.; Schreiber, M.; McFadden, G. Myxoma virus expresses a screted protein with homology to the tumor necrosis factor receptor gene family that contributes to viral virulence. Virology 1991, 184, 370-382.
    • (1991) Virology , vol.184 , pp. 370-382
    • Upton, C.1    Macen, J.2    Schreiber, M.3    McFadden, G.4
  • 184
    • 0028149960 scopus 로고
    • Differential responses of fibroblasts from wild-type and TNF-R55-deficient mice to mouse and human TNF-α
    • Mackay, F.; Rothe, J.; Bluethmann, H.; Loetscher, H.; Lesslauer, W. Differential responses of fibroblasts from wild-type and TNF-R55-deficient mice to mouse and human TNF-α activation. J. Immunol. 1994, 153, 5274-5284.
    • (1994) J. Immunol. , vol.153 , pp. 5274-5284
    • Mackay, F.1    Rothe, J.2    Bluethmann, H.3    Loetscher, H.4    Lesslauer, W.5
  • 185
    • 0027301244 scopus 로고
    • Ligand passing: The 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor
    • Tartaglia, L.;Pennica, D.; Goeddel, D. Ligand passing: The 75-kDa tumor necrosis factor (TNF) receptor recruits TNF for signaling by the 55-kDa TNF receptor. J. Biol. Chem. 1993, 268, 18542-18548.
    • (1993) J. Biol. Chem. , vol.268 , pp. 18542-18548
    • Tartaglia, L.1    Pennica, D.2    Goeddel, D.3
  • 186
    • 0029611281 scopus 로고
    • How do tumor necrosis factor receptors work?
    • Bazzoni, F.; Beutler, B. How do tumor necrosis factor receptors work? J. Inflamm. 1995, 45, 221-238.
    • (1995) J. Inflamm. , vol.45 , pp. 221-238
    • Bazzoni, F.1    Beutler, B.2
  • 187
    • 0030990123 scopus 로고    scopus 로고
    • Induced expression of trimerized intracellular domains of the human tumor necrosis factor (TNF) p55 receptor elicits TNF effects
    • Vandevoorde, V.; Haegeman, G.; Fiers, W. Induced expression of trimerized intracellular domains of the human tumor necrosis factor (TNF) p55 receptor elicits TNF effects. J. Cell. Biol. 1997, 137, 1627-1638.
    • (1997) J. Cell. Biol. , vol.137 , pp. 1627-1638
    • Vandevoorde, V.1    Haegeman, G.2    Fiers, W.3
  • 188
    • 0028985261 scopus 로고
    • Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects
    • Boldin, M.; Mett, I.; Varfolomeev, E.; Chumakov, I.; Shemer-Avni, Y.; Camonis, J.; Wallach, D. Self-association of the "death domains" of the p55 tumor necrosis factor (TNF) receptor and Fas/APO1 prompts signaling for TNF and Fas/APO1 effects. J. Biol. Chem. 1995, 270, 387-391.
    • (1995) J. Biol. Chem. , vol.270 , pp. 387-391
    • Boldin, M.1    Mett, I.2    Varfolomeev, E.3    Chumakov, I.4    Shemer-Avni, Y.5    Camonis, J.6    Wallach, D.7
  • 189
    • 0028588080 scopus 로고
    • Structural requirements for inducible shedding of hte p55 tumor necrosis factor receptor
    • Brakebusch, C.; Varfolomeev, E.; Batkin, M.; Wallach, D. Structural requirements for inducible shedding of hte p55 tumor necrosis factor receptor. J. Biol. Chem. 1994, 269, 32488-32496.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32488-32496
    • Brakebusch, C.1    Varfolomeev, E.2    Batkin, M.3    Wallach, D.4
  • 190
    • 0028919856 scopus 로고
    • A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T-lymphocytes
    • Crowe, P.; Wlater, B.; Mohler, K.; Otten-Evans, C.; Black, R.; Ware, C. A metalloprotease inhibitor blocks shedding of the 80-kD TNF receptor and TNF processing in T-lymphocytes. J. Exp. Med. 1995, 181, 1205-1209.
    • (1995) J. Exp. Med. , vol.181 , pp. 1205-1209
    • Crowe, P.1    Wlater, B.2    Mohler, K.3    Otten-Evans, C.4    Black, R.5    Ware, C.6
  • 191
    • 0032030670 scopus 로고    scopus 로고
    • Mutation of proline 211 reduces shedding of the human p75 TNF receptor
    • Herman, C.; Chernajovsky, Y. Mutation of proline 211 reduces shedding of the human p75 TNF receptor. J. Immunol. 1998, 160, 2478-2487.
    • (1998) J. Immunol. , vol.160 , pp. 2478-2487
    • Herman, C.1    Chernajovsky, Y.2
  • 192
    • 0027934198 scopus 로고
    • Tumor necrosis factor induces a selective shedding of its p75 receptor from human neutrophils
    • Porteu, F.; Hieblot, C. Tumor necrosis factor induces a selective shedding of its p75 receptor from human neutrophils. J. Biol. Chem. 1994, 269, 2834-2840.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2834-2840
    • Porteu, F.1    Hieblot, C.2
  • 193
    • 0030987071 scopus 로고    scopus 로고
    • Transducing signals of life and death
    • Yuan, J. Transducing signals of life and death. Curr. Opin. Cell. Biol. 1997, 9, 247-251.
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 247-251
    • Yuan, J.1
  • 194
    • 0029007855 scopus 로고
    • The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation
    • Hsu, H.; Xiong, J.; Goeddel, D. The TNF receptor 1-associated protein TRADD signals cell death and NF-κB activation. Cell 1995, 81, 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.3
  • 195
    • 0029026548 scopus 로고
    • FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis
    • Chinnaiyan, A.; O'Rourke, K.; Tewari, M.; Dixit, V. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell 1995, 81, 505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.4
  • 196
    • 0031406386 scopus 로고    scopus 로고
    • Death receptor-5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappa-B pathway
    • Chaudhary, P.; Eby, M.; Jasmin, A.; Bookwalter, A.; Murray, J.; Hood, L. Death receptor-5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappa-B pathway. Immunity 1997, 7, 821-830.
    • (1997) Immunity , vol.7 , pp. 821-830
    • Chaudhary, P.1    Eby, M.2    Jasmin, A.3    Bookwalter, A.4    Murray, J.5    Hood, L.6
  • 198
    • 0031405585 scopus 로고    scopus 로고
    • TRAIL receptor-1 (DR4) and receptor-2 (DR5) signal FADD-dependent apoptosis and activate NF-kappa-B
    • Schneider, P.; Thome, M.; Burns, K.; Bodmer, J.; Hofmann, K.; Kataoka, T.; Holler, N.; Tschopp, J. TRAIL receptor-1 (DR4) and receptor-2 (DR5) signal FADD-dependent apoptosis and activate NF-kappa-B. Immunity 1997, 7, 831-836.
    • (1997) Immunity , vol.7 , pp. 831-836
    • Schneider, P.1    Thome, M.2    Burns, K.3    Bodmer, J.4    Hofmann, K.5    Kataoka, T.6    Holler, N.7    Tschopp, J.8
  • 199
    • 0032518446 scopus 로고    scopus 로고
    • Dominant-negative FADD inhibits TNFR60-mediated, FAS/APO1-mediated and TRAIL-R/APO2-mediated cell-death but not gene induction
    • Wajant, H.; Johannes, F.; Haas, E., Siemienski, K.; Schwenzer, R.; Schubert, G.; Weiss, T.; Grell, M.; Scheurich, P. Dominant-negative FADD inhibits TNFR60-mediated, FAS/APO1-mediated and TRAIL-R/APO2-mediated cell-death but not gene induction. Curr. Biol. 1997, 8, 113-116.
    • (1997) Curr. Biol. , vol.8 , pp. 113-116
    • Wajant, H.1    Johannes, F.2    Haas, E.3    Siemienski, K.4    Schwenzer, R.5    Schubert, G.6    Weiss, T.7    Grell, M.8    Scheurich, P.9
  • 201
    • 0030011398 scopus 로고    scopus 로고
    • Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death
    • Boldin, M. P.; Goncharov, T. M.; Goltsev, Y. V.; Wallach, D. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death. Cell 1996, 85, 803-815.
    • (1996) Cell , vol.85 , pp. 803-815
    • Boldin, M.P.1    Goncharov, T.M.2    Goltsev, Y.V.3    Wallach, D.4
  • 202
    • 0030826338 scopus 로고    scopus 로고
    • FLICE is predominatly expressed as 2 functionally active isoforms, caspase-8/a and caspase-8/b
    • Scaffidi, C.; Medema, J.; Krammer, P.; Peter, M. FLICE is predominatly expressed as 2 functionally active isoforms, caspase-8/a and caspase-8/b. J. Biol. Chem. 1997, 272, 26953-26958.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26953-26958
    • Scaffidi, C.1    Medema, J.2    Krammer, P.3    Peter, M.4
  • 203
    • 0029949257 scopus 로고    scopus 로고
    • TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex
    • Hsu, H.; Huang, J.; Shu, H.; Baichwal, V.; Goeddel, D. TNF-dependent recruitment of the protein kinase RIP to the TNF receptor-1 signaling complex. Immunity 1996, 4, 387-396.
    • (1996) Immunity , vol.4 , pp. 387-396
    • Hsu, H.1    Huang, J.2    Shu, H.3    Baichwal, V.4    Goeddel, D.5
  • 204
    • 0032479145 scopus 로고    scopus 로고
    • RIP2 is a novel NK-κB-activating and cell death-inducing kinase
    • McCarthy, J.; Ni, J.; Dixit, V. RIP2 is a novel NK-κB-activating and cell death-inducing kinase. J. Biol Chem. 1998, 273, 16968-16975.
    • (1998) J. Biol Chem. , vol.273 , pp. 16968-16975
    • McCarthy, J.1    Ni, J.2    Dixit, V.3
  • 205
    • 0032033132 scopus 로고    scopus 로고
    • The death domain kinase RIP mediates the TNF-induced NF-kappa-B signal
    • Kelliher, M.; Grimm, S.; Ishida, Y.; Kuo, F.; Stanger, B.; Leder, P. The death domain kinase RIP mediates the TNF-induced NF-kappa-B signal. Immunity 1998, 8, 297-303.
    • (1998) Immunity , vol.8 , pp. 297-303
    • Kelliher, M.1    Grimm, S.2    Ishida, Y.3    Kuo, F.4    Stanger, B.5    Leder, P.6
  • 206
    • 0030032106 scopus 로고    scopus 로고
    • TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways
    • Hsu, H.; Shum, H.; Pan, M.; Goeddel, D. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways. Cell 1996, 84, 299-308.
    • (1996) Cell , vol.84 , pp. 299-308
    • Hsu, H.1    Shum, H.2    Pan, M.3    Goeddel, D.4
  • 207
    • 0030916237 scopus 로고    scopus 로고
    • Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-α is mediated by the nuclear factor-κB heterodimers p65/p65 and p65/cRel in the absence of p50
    • Aoudjit, F.; Brochu, N.; Belanger, B.; Stratowa, C.; Hiscott, J.; Audette, M. Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-α is mediated by the nuclear factor-κB heterodimers p65/p65 and p65/cRel in the absence of p50. Cell Growth Differ. 1997, 8, 335-342.
    • (1997) Cell Growth Differ. , vol.8 , pp. 335-342
    • Aoudjit, F.1    Brochu, N.2    Belanger, B.3    Stratowa, C.4    Hiscott, J.5    Audette, M.6
  • 208
    • 12644272789 scopus 로고    scopus 로고
    • Tumor necrosis factor (TNF)-mediated kinase cascades: Bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2
    • Song, H. Y.; Regnier, C. H.; Kirschning, C. J.; Goeddel, D. V.; Rothe, M. Tumor necrosis factor (TNF)-mediated kinase cascades: bifurcation of nuclear factor-kappaB and c-jun N-terminal kinase (JNK/SAPK) pathways at TNF receptor-associated factor 2. Proc. Natl. Acad. Sci. U.S.A. 1997, 94, 9792-9796.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9792-9796
    • Song, H.Y.1    Regnier, C.H.2    Kirschning, C.J.3    Goeddel, D.V.4    Rothe, M.5
  • 209
    • 0031906851 scopus 로고    scopus 로고
    • PEG3/PW1 is an imprinted gene involved in the TNF-NF-kappa-B signal transduction pathway
    • Relaix, F.; Wei, X.; Wu, X.; Sassoon, D. PEG3/PW1 is an imprinted gene involved in the TNF-NF-kappa-B signal transduction pathway. Nature Genet. 1998, 18, 287-291.
    • (1998) Nature Genet. , vol.18 , pp. 287-291
    • Relaix, F.1    Wei, X.2    Wu, X.3    Sassoon, D.4
  • 210
    • 0028954475 scopus 로고
    • Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor
    • Song, H.; Dunbar, J.; Zhang, Y.; Guo, D.; Donner, D. Identification of a protein with homology to hsp90 that binds the type 1 tumor necrosis factor receptor. J. Biol. Chem. 1995, 270, 3574-3581.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3574-3581
    • Song, H.1    Dunbar, J.2    Zhang, Y.3    Guo, D.4    Donner, D.5
  • 211
    • 0031135534 scopus 로고    scopus 로고
    • Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor
    • Dunbar, J.; Song, H.; Guo, D.; Wu, L.; Donner, D. Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor. J. Immunol. 1997, 158, 4252-4259.
    • (1997) J. Immunol. , vol.158 , pp. 4252-4259
    • Dunbar, J.1    Song, H.2    Guo, D.3    Wu, L.4    Donner, D.5
  • 212
    • 0027965717 scopus 로고
    • TNF receptors TR60 and TR80 can mediate apoptosis via induction of distinct signal pathways
    • Grell, M.; Zimmermann, G.; Hulser, G.; Pfizenmaier, K.; Scheurich, P. TNF receptors TR60 and TR80 can mediate apoptosis via induction of distinct signal pathways. J. Immunol. 1994, 153, 1963-1968.
    • (1994) J. Immunol. , vol.153 , pp. 1963-1968
    • Grell, M.1    Zimmermann, G.2    Hulser, G.3    Pfizenmaier, K.4    Scheurich, P.5
  • 213
    • 0032571131 scopus 로고    scopus 로고
    • Mutations which abolish phosphorylation of the TRAF-binding domain of TNF receptor-2 enhance receptor mediated NF-kappa-B activation
    • Ng, P.; Janicke, R.; Porter, A. Mutations which abolish phosphorylation of the TRAF-binding domain of TNF receptor-2 enhance receptor mediated NF-kappa-B activation. Biochem. Biophys. Res. Commun. 1998, 244, 756-762.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 756-762
    • Ng, P.1    Janicke, R.2    Porter, A.3
  • 214
    • 0028124428 scopus 로고
    • A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor
    • Rothe, M.; Wong, S.; Henzel, W.; Goeddel, D. A novel family of putative signal transducers associated with the cytoplasmic domain of the 75 kDa tumor necrosis factor receptor. Cell 1994, 78, 681-692.
    • (1994) Cell , vol.78 , pp. 681-692
    • Rothe, M.1    Wong, S.2    Henzel, W.3    Goeddel, D.4
  • 215
    • 0031092638 scopus 로고    scopus 로고
    • Enhancement of TNF receptor p60-mediated cytotoxicity by TNF receptor p80. Requirement of the TNF receptor-associated factor-2 binding site
    • Weiss, T.; Grell, M.; Hessabi, B.; Bourteele, S.; Muller, G.; Scheurih, P.; Wajant, H. Enhancement of TNF receptor p60-mediated cytotoxicity by TNF receptor p80. Requirement of the TNF receptor-associated factor-2 binding site. J. Immunol. 1997, 158, 2398-2404.
    • (1997) J. Immunol. , vol.158 , pp. 2398-2404
    • Weiss, T.1    Grell, M.2    Hessabi, B.3    Bourteele, S.4    Muller, G.5    Scheurih, P.6    Wajant, H.7
  • 216
    • 0029953942 scopus 로고    scopus 로고
    • Cloning and expression of apoptosis inhibitory protein homologues that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors
    • Uren, A.; Pakusch, M.; Hawkins, C.; Puls, K.; Vaux, D. Cloning and expression of apoptosis inhibitory protein homologues that function to inhibit apoptosis and/or bind tumor necrosis factor receptor-associated factors. Proc. Natl. Acad. Sci. U.S.A 1996, 93, 4974-4978.
    • (1996) Proc. Natl. Acad. Sci. U.S.A , vol.93 , pp. 4974-4978
    • Uren, A.1    Pakusch, M.2    Hawkins, C.3    Puls, K.4    Vaux, D.5
  • 217
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy, N.; Deveraux, Q.; Takahashi, R.; Salvesen, G.; Reed, J. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 1997, 16, 6914-6925.
    • (1997) EMBO J. , vol.16 , pp. 6914-6925
    • Roy, N.1    Deveraux, Q.2    Takahashi, R.3    Salvesen, G.4    Reed, J.5
  • 219
    • 0032489389 scopus 로고    scopus 로고
    • Interaction of the adenovirus 14.7 kDa protein with FLICE inhibits Fas ligand induced apoptosis
    • Chen, P.; Tian, J.; Kovesdi, I.; Bruder, J. Interaction of the adenovirus 14.7 kDa protein with FLICE inhibits Fas ligand induced apoptosis. J. Biol. Chem. 1998, 273, 5815-5820.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5815-5820
    • Chen, P.1    Tian, J.2    Kovesdi, I.3    Bruder, J.4
  • 220
    • 0030827216 scopus 로고    scopus 로고
    • Bovine herpesvirus-4 BORFE2 protein inhibits Fas-induced and tumor necrosis factor receptor-1 induced apoptosis and contains death effector domains shared with other gamma-2 herpesviruses
    • Wang, G.; Bertin, J.; Wang, Y.; Martin, D.; Wang, J. Bovine herpesvirus-4 BORFE2 protein inhibits Fas-induced and tumor necrosis factor receptor-1 induced apoptosis and contains death effector domains shared with other gamma-2 herpesviruses. J. Virol. 1997, 71, 8928-8932.
    • (1997) J. Virol. , vol.71 , pp. 8928-8932
    • Wang, G.1    Bertin, J.2    Wang, Y.3    Martin, D.4    Wang, J.5
  • 221
    • 0032548502 scopus 로고    scopus 로고
    • Bcl-x(L) functions downstream of caspase-8 to inhibit Fas necrosis factor and tumor necrosis factor receptor-1 induced apoptosis of MCF7 breast cancinoma cells
    • Srinivasan, A.; Li, F.; Wong, A.; Kodandapani, L.; Smidt, R.; Krebs, J.; Fritz, L.; Wu, J.; Tomaselli, K. Bcl-x(L) functions downstream of caspase-8 to inhibit Fas necrosis factor and tumor necrosis factor receptor-1 induced apoptosis of MCF7 breast cancinoma cells. J. Biol. Chem. 1998, 273, 4523-4529.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4523-4529
    • Srinivasan, A.1    Li, F.2    Wong, A.3    Kodandapani, L.4    Smidt, R.5    Krebs, J.6    Fritz, L.7    Wu, J.8    Tomaselli, K.9
  • 222
    • 0032488664 scopus 로고    scopus 로고
    • Bcl-x(L) acts downstream of caspase-8 activation by the CD95 death inducing signaling complex
    • Medema, J.; Scaffidi, C.; Krammer, P.; Peter, M. Bcl-x(L) acts downstream of caspase-8 activation by the CD95 death inducing signaling complex. J. Biol. Chem. 1998, 273, 3388-3393.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3388-3393
    • Medema, J.1    Scaffidi, C.2    Krammer, P.3    Peter, M.4
  • 223
    • 0032512738 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended ring finger domain that inhibits TNFR2 mediated NF-kappa-B activation
    • Brink, R.; Lodish, H. Tumor necrosis factor receptor (TNFR)-associated factor 2A (TRAF2A), a TRAF2 splice variant with an extended ring finger domain that inhibits TNFR2 mediated NF-kappa-B activation. J. Biol. Chem. 1998, 273, 4129-4134.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4129-4134
    • Brink, R.1    Lodish, H.2
  • 224
    • 0000564581 scopus 로고    scopus 로고
    • The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κ-B activation
    • Song, H.; Rothe, M.; Goeddel, D. The tumor necrosis factor-inducible zinc finger protein A20 interacts with TRAF1/TRAF2 and inhibits NF-κ-B activation. Proc. Natl. Acad. Sci. U.S.A. 1996, 93, 6721-6725.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 6721-6725
    • Song, H.1    Rothe, M.2    Goeddel, D.3
  • 225
    • 0029976817 scopus 로고    scopus 로고
    • An essential role for NF-κB in preventing TNF-α-induced cell death
    • Beg, A.; Baltimore, D. An essential role for NF-κB in preventing TNF-α-induced cell death. Science 1996, 274, 782-784.
    • (1996) Science , vol.274 , pp. 782-784
    • Beg, A.1    Baltimore, D.2
  • 226
    • 0029858387 scopus 로고    scopus 로고
    • TNF- and cancer therapy-induced apoptosis: Potentiation by inhibition of NF-κB
    • Wang, C.; Mayo, M.; Baldwin, A., Jr. TNF- and cancer therapy-induced apoptosis: potentiation by inhibition of NF-κB. Science 1996, 274, 784-787.
    • (1996) Science , vol.274 , pp. 784-787
    • Wang, C.1    Mayo, M.2    Baldwin A., Jr.3
  • 227
    • 0029992609 scopus 로고    scopus 로고
    • Suppression of TNF-α-induced apoptosis by NF-κ-B
    • Van Antwerp, D.; Martin, S.; Kafri, T.; Green, D.; Verma, I. Suppression of TNF-α-induced apoptosis by NF-κ-B. Science 1996, 274, 787-789.
    • (1996) Science , vol.274 , pp. 787-789
    • Van Antwerp, D.1    Martin, S.2    Kafri, T.3    Green, D.4    Verma, I.5
  • 228
    • 0030298294 scopus 로고    scopus 로고
    • Dissection of TNF receptor 1 effector function: JNK activation is not linked to apoptosis while NFκB activation prevents cell death
    • Liu, Z.; Hsu, H.; Goeddel, D. Dissection of TNF receptor 1 effector function: JNK activation is not linked to apoptosis while NFκB activation prevents cell death. Cell 1996, 87, 565-576.
    • (1996) Cell , vol.87 , pp. 565-576
    • Liu, Z.1    Hsu, H.2    Goeddel, D.3
  • 229
    • 0032516651 scopus 로고    scopus 로고
    • IEX-1L, an apoptosis inhibitor involved in NF-κB-mediated cell survival
    • Wu, M.; Ao, Z.; Prasad, K.; Wu, R.; Schlossman, S. IEX-1L, an apoptosis inhibitor involved in NF-κB-mediated cell survival. Science 1998, 281, 998-1001.
    • (1998) Science , vol.281 , pp. 998-1001
    • Wu, M.1    Ao, Z.2    Prasad, K.3    Wu, R.4    Schlossman, S.5
  • 230
    • 0032055940 scopus 로고    scopus 로고
    • A20 inhibits NFκB activation in endothelial-cells without sensitizing to tumor necrosis factor-mediated apoptosis
    • Ferran, C.; Stroka, D.; Badrichani, A.; Cooper, J.; Wrighton, C.; Soares, M.; Grey, S.; Bach, F. A20 inhibits NFκB activation in endothelial-cells without sensitizing to tumor necrosis factor-mediated apoptosis. Blood 1998, 91, 2249-2258.
    • (1998) Blood , vol.91 , pp. 2249-2258
    • Ferran, C.1    Stroka, D.2    Badrichani, A.3    Cooper, J.4    Wrighton, C.5    Soares, M.6    Grey, S.7    Bach, F.8
  • 231
    • 0032489554 scopus 로고    scopus 로고
    • TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase
    • Schwandner, R.; Wiegmann, K.; Bernardo, K.; Kreder, D.; Kronke, M. TNF receptor death domain-associated proteins TRADD and FADD signal activation of acid sphingomyelinase. J. Biol. Chem. 1998, 273, 5916-5922.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5916-5922
    • Schwandner, R.1    Wiegmann, K.2    Bernardo, K.3    Kreder, D.4    Kronke, M.5
  • 232
    • 0032549509 scopus 로고    scopus 로고
    • Inhibition of sphingolipid induced apoptosis by caspase inhibitors indicates that sphingosine acts in an earlier part of the apoptotic pathway than ceramide
    • Sweeney, E.; Inokuchi, J.; Igarashi, Y. Inhibition of sphingolipid induced apoptosis by caspase inhibitors indicates that sphingosine acts in an earlier part of the apoptotic pathway than ceramide. FEBS Lett. 1998, 425, 61-65.
    • (1998) FEBS Lett. , vol.425 , pp. 61-65
    • Sweeney, E.1    Inokuchi, J.2    Igarashi, Y.3
  • 233
    • 0031041448 scopus 로고    scopus 로고
    • Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-α: CrmA and Bcl-2 target distinct components in the apoptotic pathway
    • Dbaibo, G.; Perry, D.; Gamard, C.; Platt, R.; Poirier, G.; Obeid, L.; Hannun, Y. Cytokine response modifier A (CrmA) inhibits ceramide formation in response to tumor necrosis factor (TNF)-α: CrmA and Bcl-2 target distinct components in the apoptotic pathway. J. Exp. Med. 1997, 185, 481-490.
    • (1997) J. Exp. Med. , vol.185 , pp. 481-490
    • Dbaibo, G.1    Perry, D.2    Gamard, C.3    Platt, R.4    Poirier, G.5    Obeid, L.6    Hannun, Y.7
  • 234
    • 0032571251 scopus 로고    scopus 로고
    • CD95 (FAS/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase
    • Boesendecock, J.; Tepper, A.; DeVries, E.; Van Blitterswijk, W.; Borst, J. CD95 (FAS/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase. J. Biol. Chem. 1998, 273, 7560-7565.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7560-7565
    • Boesendecock, J.1    Tepper, A.2    DeVries, E.3    Van Blitterswijk, W.4    Borst, J.5
  • 235
    • 0032518448 scopus 로고    scopus 로고
    • Role of an acidic compartment in tumor necrosis factor alpha induced production of ceramide, activation of caspase-3 and apoptosis
    • Monney, L.; Olivier, R.; Otter, I.; Jansen, B.; Poirier, G.; Borner, C. Role of an acidic compartment in tumor necrosis factor alpha induced production of ceramide, activation of caspase-3 and apoptosis. Eur. J. Biochern. 1998, 251, 295-303.
    • (1998) Eur. J. Biochern. , vol.251 , pp. 295-303
    • Monney, L.1    Olivier, R.2    Otter, I.3    Jansen, B.4    Poirier, G.5    Borner, C.6
  • 236
    • 0030702895 scopus 로고    scopus 로고
    • A novel SAPK/JNK kinase, MKK7, stimulated by TNFα and cellular stresses
    • Moriguchi, T.; Toyoshima, F.; Masuyama, N.; Hanafusa, H.; Gotoh, Y.; Nishida, E. A novel SAPK/JNK kinase, MKK7, stimulated by TNFα and cellular stresses. EMBO J. 1997, 16, 7045-7053.
    • (1997) EMBO J. , vol.16 , pp. 7045-7053
    • Toyoshima, F.1    Masuyama, N.2    Hanafusa, H.3    Gotoh, Y.4    Nishida, E.5
  • 237
    • 0031013545 scopus 로고    scopus 로고
    • Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2-dependent pathway
    • Natoli, G.; Costanzo, A.; Ianni, A.; Templeton, D.; Woodgett, J.; Balsano, C.; Levrero, M. Activation of SAPK/JNK by TNF receptor 1 through a noncytotoxic TRAF2-dependent pathway. Science 1997, 275, 200-203.
    • (1997) Science , vol.275 , pp. 200-203
    • Natoli, G.1    Costanzo, A.2    Ianni, A.3    Templeton, D.4    Woodgett, J.5    Balsano, C.6    Levrero, M.7
  • 238
    • 0030614745 scopus 로고    scopus 로고
    • Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-α activation of SAPK in melanoma cells
    • Marti, A.; Luo, Z.; Cunningham, C.; Ohta, Y.; Hartwig, J.; Stossel, T.; Kyriakis, J.; Avruch, J. Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-α activation of SAPK in melanoma cells. J. Biol. Chem. 1997, 272, 2620-2628.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2620-2628
    • Marti, A.1    Luo, Z.2    Cunningham, C.3    Ohta, Y.4    Hartwig, J.5    Stossel, T.6    Kyriakis, J.7    Avruch, J.8
  • 239
    • 0031285250 scopus 로고    scopus 로고
    • Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway
    • Lee, F.; Hagler, J.; Chen, Z.; Maniatis, T. Activation of the IκBα kinase complex by MEKK1, a kinase of the JNK pathway. Cell 1997, 88, 213-222.
    • (1997) Cell , vol.88 , pp. 213-222
    • Lee, F.1    Hagler, J.2    Chen, Z.3    Maniatis, T.4
  • 241
    • 0031279104 scopus 로고    scopus 로고
    • Activation of p38mapk, MKK3, and MKK4 by TNF-α in mouse bone marrow-derived macrophages
    • Winston, B.; Chan, E.; Johnson, G.; Riches, D. Activation of p38mapk, MKK3, and MKK4 by TNF-α in mouse bone marrow-derived macrophages. J. Immunol. 1997, 159, 4491-4497.
    • (1997) J. Immunol. , vol.159 , pp. 4491-4497
    • Winston, B.1    Chan, E.2    Johnson, G.3    Riches, D.4
  • 242
    • 0032571569 scopus 로고    scopus 로고
    • TRAF2 plays a dual role in NFκB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IκB kinase pathways
    • Carpentier, I.; Declercq, W.; Malinin, N.; Wallach, D.; Fiers, W.; Beyaert, R. TRAF2 plays a dual role in NFκB-dependent gene activation by mediating the TNF-induced activation of p38 MAPK and IκB kinase pathways. FEBS Lett. 1998, 425, 195-198.
    • (1998) FEBS Lett. , vol.425 , pp. 195-198
    • Carpentier, I.1    Declercq, W.2    Malinin, N.3    Wallach, D.4    Fiers, W.5    Beyaert, R.6
  • 243
    • 0032519736 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or FMLP stimulation
    • Zu, Y.; Qi, J.; Gilchrist, A.; Fernandez, G.; Vazquez-Abad, D.; Kreutzer, D.; Huang, C.; Sha'afi, R. p38 mitogen-activated protein kinase activation is required for human neutrophil function triggered by TNF-α or FMLP stimulation. J. Immunol. 1998, 160, 1982-1989.
    • (1998) J. Immunol. , vol.160 , pp. 1982-1989
    • Zu, Y.1    Qi, J.2    Gilchrist, A.3    Fernandez, G.4    Vazquez-Abad, D.5    Kreutzer, D.6    Huang, C.7    Sha'afi, R.8
  • 244
    • 0032488837 scopus 로고    scopus 로고
    • P38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor
    • Vanden Berghe, W.; Plaisance, S.; Boone, E.; De Bosscher, K.; Lienhard Schmitz, M.; Fiers, W.; Haegeman, G. p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor. J. Biol. Chem. 1998, 273, 3285-3290.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3285-3290
    • Vanden Berghe, W.1    Plaisance, S.2    Boone, E.3    De Bosscher, K.4    Lienhard Schmitz, M.5    Fiers, W.6    Haegeman, G.7
  • 246
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance
    • Hotamisligil, G.; Peraldi, P.; Budavari, A.; Ellis, R.; White, M.; Spiegelman, B. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-α- and obesity-induced insulin resistance. Science 1996, 271, 665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Hotamisligil, G.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.5    Spiegelman, B.6
  • 247
    • 0032521284 scopus 로고    scopus 로고
    • Induction of Jak/STAT signaling by activation of the type 1 TNF receptor
    • Guo, D.; Dunbar, J.; Yang, C.; Pfeffer, L.; Donner, D. Induction of Jak/STAT signaling by activation of the type 1 TNF receptor. J. Immunol. 1998, 160, 2742-2750.
    • (1998) J. Immunol. , vol.160 , pp. 2742-2750
    • Guo, D.1    Dunbar, J.2    Yang, C.3    Pfeffer, L.4    Donner, D.5
  • 248
    • 0031047829 scopus 로고    scopus 로고
    • A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase
    • Castellino, A.; Parker, G.; Boronenkov, I.; Anderson, R.; Chao, M. A novel interaction between the juxtamembrane region of the p55 tumor necrosis factor receptor and phosphatidylinositol-4-phosphate 5-kinase. J. Biol. Chem. 1997, 272, 5861-5870.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5861-5870
    • Castellino, A.1    Parker, G.2    Boronenkov, I.3    Anderson, R.4    Chao, M.5
  • 249
    • 0032549174 scopus 로고    scopus 로고
    • I-kappa-B-alpha degradation and nuclear factor-kappa-B DNA binding are insufficient for interleukin-1 beta and tumor necrosis factor alpha incuded kappa-B-dependent transcription - Requirement for an additional activation pathway
    • Bergmann, M.; Hart, L.; Lindsay, M.; Barnes, P.; Newton, R. I-kappa-B-alpha degradation and nuclear factor-kappa-B DNA binding are insufficient for interleukin-1 beta and tumor necrosis factor alpha incuded kappa-B-dependent transcription - requirement for an additional activation pathway. J. Biol. Chem. 1998, 273, 6607-6610.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6607-6610
    • Bergmann, M.1    Hart, L.2    Lindsay, M.3    Barnes, P.4    Newton, R.5


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