메뉴 건너뛰기




Volumn 46, Issue 5, 1999, Pages 257-266

Tumor necrosis factor-α: Molecular-biological aspects minireview

Author keywords

Pentoxifylline; RT PCR; TNF assaying; TNF expression; TNF signal transduction; Tumor necrosis factor

Indexed keywords

MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; PENTOXIFYLLINE; PHOSPHOLIPASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEINASE; SPHINGOMYELIN PHOSPHODIESTERASE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA;

EID: 0345634202     PISSN: 00282685     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (34)

References (80)
  • 1
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • ABATE, C., PATEL, L., RAUSCHER, F.J. 3RD, CURRAN, T.: Redox regulation of fos and jun DNA-binding activity in vitro. Science, 249, 1990, 1157-1161.
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher F.J. III3    Curran, T.4
  • 2
    • 0032548944 scopus 로고    scopus 로고
    • Role of activating protein-1 in the regulation of the vascular cell adhesion molecule-1 gene expression by tumor necrosis factor-alpha
    • AHMAD, M., THEOFANIDIS, P., MEDFORD, R.M.: Role of activating protein-1 in the regulation of the vascular cell adhesion molecule-1 gene expression by tumor necrosis factor-alpha. J. Biol. Chem., 273, 1998, 4616-4621.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4616-4621
    • Ahmad, M.1    Theofanidis, P.2    Medford, R.M.3
  • 4
    • 0022067755 scopus 로고
    • Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate
    • ANSORGE, W.: Fast and sensitive detection of protein and DNA bands by treatment with potassium permanganate. J. Biochem. Biophys. Methods, 11, 1985, 13-20.
    • (1985) J. Biochem. Biophys. Methods , vol.11 , pp. 13-20
    • Ansorge, W.1
  • 5
  • 6
    • 0026033385 scopus 로고
    • IP-1: A dominant inhibitor of Fos/Jun whose activity is modulated by phosphorylation
    • AUWERX, J., SASSONE-CORSI, P.: IP-1: A dominant inhibitor of Fos/Jun whose activity is modulated by phosphorylation. Cell, 64, 1991, 983-993.
    • (1991) Cell , vol.64 , pp. 983-993
    • Auwerx, J.1    Sassone-Corsi, P.2
  • 7
    • 0004118473 scopus 로고
    • New York, Oxford University Press
    • BALKWILL, F.R.: Cytokines. New York, Oxford University Press 1991.
    • (1991) Cytokines
    • Balkwill, F.R.1
  • 9
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
    • BOYLE, W.J., SMEAL, T., DEFIZE, L.H., ANGEL, P., WOODGETT, J.R., KARIN, M., HUNTER, T.: Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell, 64, 1991, 573-584.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6    Hunter, T.7
  • 11
    • 0031569536 scopus 로고    scopus 로고
    • Glucocorticoids inhibit E-selectin expression by targeting NF-kappaB and not ATF/c-jun
    • BROSTJAN, C., ANRATHER, J., CSIZMADIA, V., NATARAJAN, G., WINKLER, H.: Glucocorticoids inhibit E-selectin expression by targeting NF-kappaB and not ATF/c-jun. J. Immunol., 158, 1997, 3836-3844.
    • (1997) J. Immunol. , vol.158 , pp. 3836-3844
    • Brostjan, C.1    Anrather, J.2    Csizmadia, V.3    Natarajan, G.4    Winkler, H.5
  • 12
    • 0029026548 scopus 로고
    • FADD, a novel death domain - Containing protein, interacts with the death domain of Fas and initiates apoptosis
    • CHINNAIYAN, A.M., O'ROURKE, K., TEWARI, M., DIXIT, V. M.: FADD, a novel death domain - containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell, 81, 1995, 505-512.
    • (1995) Cell , vol.81 , pp. 505-512
    • Chinnaiyan, A.M.1    O'Rourke, K.2    Tewari, M.3    Dixit, V.M.4
  • 13
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executors of apoptosis
    • COHEN, G.M.: Caspases: The executors of apoptosis. Biochem. J., 326, 1997, 1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 14
    • 0029554095 scopus 로고
    • CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase domain
    • CONNELLY, M.A., MARCU, K.B.: CHUK, a new member of the helix-loop-helix and leucine zipper families of interacting proteins, contains a serine-threonine kinase domain. Cell. Mol. Biol. Res., 41, 1995, 537-549.
    • (1995) Cell. Mol. Biol. Res. , vol.41 , pp. 537-549
    • Connelly, M.A.1    Marcu, K.B.2
  • 15
    • 0032055198 scopus 로고    scopus 로고
    • Crucial role of TNF-receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis
    • DECKERT-SCHLUTER, M., BLUETHMANN, H., RANG, A., HOF, H., SCHLUTER, D.: Crucial role of TNF-receptor type 1 (p55), but not of TNF receptor type 2 (p75), in murine toxoplasmosis. J. Immunol., 160, 1998, 3427-3436.
    • (1998) J. Immunol. , vol.160 , pp. 3427-3436
    • Deckert-Schluter, M.1    Bluethmann, H.2    Rang, A.3    Hof, H.4    Schluter, D.5
  • 17
    • 0029551821 scopus 로고
    • Pentoxifylline for the treatment of HIV infection and its complications
    • DEZUBE, B.J., LEDERMAN, M.M.: Pentoxifylline for the treatment of HIV infection and its complications. J. Cardiovasc. Pharmacol., 25, 1995, S139-S142.
    • (1995) J. Cardiovasc. Pharmacol. , vol.25
    • Dezube, B.J.1    Lederman, M.M.2
  • 18
    • 0031021356 scopus 로고    scopus 로고
    • RAIDD is a new "death" adaptor molecule
    • DUAN, H., DIXIT, V.M.: RAIDD is a new "death" adaptor molecule. Nature, 385, 1997, 86-89.
    • (1997) Nature , vol.385 , pp. 86-89
    • Duan, H.1    Dixit, V.M.2
  • 19
    • 0031298259 scopus 로고    scopus 로고
    • Cleavage of poly(ADP-ribose) polymerase: A sensitive parameter to study cell death
    • DURIEZ, P.J., SHAH, G.M.: Cleavage of poly(ADP-ribose) polymerase: A sensitive parameter to study cell death. Biochem. Cell. Biol., 75, 1997, 337-349.
    • (1997) Biochem. Cell. Biol. , vol.75 , pp. 337-349
    • Duriez, P.J.1    Shah, G.M.2
  • 21
    • 0025884625 scopus 로고
    • Tumor necrosis factor: Characterization at the molecular, cellular and in vivo level
    • FIERS, W.: Tumor necrosis factor: Characterization at the molecular, cellular and in vivo level. FEBS Lett., 285, 1991, 199-212.
    • (1991) FEBS Lett. , vol.285 , pp. 199-212
    • Fiers, W.1
  • 22
    • 0029564859 scopus 로고
    • Constitutively active MAP kinase kinase (MEK1) stimulates SAP kinase and c-jun transcriptional activity in U937 human leukemic cells
    • FRANKLIN, C.C., KRAFT, A.S.: Constitutively active MAP kinase kinase (MEK1) stimulates SAP kinase and c-jun transcriptional activity in U937 human leukemic cells. Oncogene, 11, 1995, 2365-2374.
    • (1995) Oncogene , vol.11 , pp. 2365-2374
    • Franklin, C.C.1    Kraft, A.S.2
  • 23
    • 0027196986 scopus 로고
    • Mechanisms of endotoxin shock and endotoxin hypersensitivity
    • GALANOS, C., FREUDENBERG, M.A.: Mechanisms of endotoxin shock and endotoxin hypersensitivity. Immunobiology, 187, 1993, 346-356.
    • (1993) Immunobiology , vol.187 , pp. 346-356
    • Galanos, C.1    Freudenberg, M.A.2
  • 24
    • 0031662251 scopus 로고    scopus 로고
    • BRE: A modulator of TNF-alpha action
    • GU, C., CASTELLINO, A., CHAN, J.Y., CHAO, M.V.: BRE: A modulator of TNF-alpha action. FASEB J., 12, 1998, 1101-1108.
    • (1998) FASEB J. , vol.12 , pp. 1101-1108
    • Gu, C.1    Castellino, A.2    Chan, J.Y.3    Chao, M.V.4
  • 25
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • GUPTA, S., CAMPBELL, D., DERIJARD, B., DAVIS, R.J.: Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science, 267, 1995, 389-393.
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Derijard, B.3    Davis, R.J.4
  • 26
    • 0023541536 scopus 로고
    • Modulation of tumor necrosis factor-alpha cytotoxicity in L929 cells by bacterial toxins, hydrocortisone and inhibitors of arachidonic acid metabolism
    • HEPBURN, A., BOEYNAEMS, J.M., FIERS, W., DUMONT, J.E.: Modulation of tumor necrosis factor-alpha cytotoxicity in L929 cells by bacterial toxins, hydrocortisone and inhibitors of arachidonic acid metabolism. Biochem. Biophys. Res. Commun., 149, 1987, 815-822.
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 815-822
    • Hepburn, A.1    Boeynaems, J.M.2    Fiers, W.3    Dumont, J.E.4
  • 27
    • 0025061601 scopus 로고
    • Tumor necrosis factor-alpha and -beta bind to the same two types of tumor necrosis factor receptors and maximally activate the transcription factor NF-kappaB at low receptor occupancy and within minutes after receptor binding
    • HOHMANN, H.P., REMY, R., POSCHL, B., VAN LOON, A.P.G.M.: Tumor necrosis factor-alpha and -beta bind to the same two types of tumor necrosis factor receptors and maximally activate the transcription factor NF-kappaB at low receptor occupancy and within minutes after receptor binding. J. Biol. Chem., 265, 1990, 15 183-15 188.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15183-15188
    • Hohmann, H.P.1    Remy, R.2    Poschl, B.3    Van Loon, A.P.G.M.4
  • 28
    • 0029007855 scopus 로고
    • The TNF receptor 1 -associated protein TRADD signals cell death and NF-κB activation
    • Hsu, H., XIONG, J., GOEDDEL, D.V: The TNF receptor 1 -associated protein TRADD signals cell death and NF-κB activation. Cell, 81, 1995, 495-504.
    • (1995) Cell , vol.81 , pp. 495-504
    • Hsu, H.1    Xiong, J.2    Goeddel, D.V.3
  • 29
    • 0024846311 scopus 로고
    • TNF stimulates expression of mouse MHC class I genes by inducing an NF kappaB-like enhancer binding activity which displaces constitutive factors
    • ISRAEL, A., LE BAIL, O., HATAT, D., PIETTE, J., KIERAN, M., LOGEAT, F., WALLACH, D., FELLOUS, M., KOURILSKY, P.: TNF stimulates expression of mouse MHC class I genes by inducing an NF kappaB-like enhancer binding activity which displaces constitutive factors. EMBO J., 8, 1989, 3793-3800.
    • (1989) EMBO J. , vol.8 , pp. 3793-3800
    • Israel, A.1    Le Bail, O.2    Hatat, D.3    Piette, J.4    Kieran, M.5    Logeat, F.6    Wallach, D.7    Fellous, M.8    Kourilsky, P.9
  • 30
    • 0029116298 scopus 로고
    • Defects in signal transduction pathways in chronic B lymphocytic leukemia cells
    • JABBAR, S.A., HOFFBRAND, A.V., WICKREMASINGHE, R.G.: Defects in signal transduction pathways in chronic B lymphocytic leukemia cells. Leuk. Lymphoma, 18, 1995, 163-170.
    • (1995) Leuk. Lymphoma , vol.18 , pp. 163-170
    • Jabbar, S.A.1    Hoffbrand, A.V.2    Wickremasinghe, R.G.3
  • 31
    • 0028802362 scopus 로고
    • The regulation of protein transport to the nucleus by phosphorylation
    • JANS, D.A.: The regulation of protein transport to the nucleus by phosphorylation. Biochem. J., 311, 1995, 705-716.
    • (1995) Biochem. J. , vol.311 , pp. 705-716
    • Jans, D.A.1
  • 32
    • 0028224199 scopus 로고
    • High-resolution molecular discrimination by RNA
    • JENISON, R.D., GILL, S.C., PARDI, A., POLISKY, B.: High-resolution molecular discrimination by RNA. Science, 263, 1994, 1425-1429.
    • (1994) Science , vol.263 , pp. 1425-1429
    • Jenison, R.D.1    Gill, S.C.2    Pardi, A.3    Polisky, B.4
  • 33
    • 0031810458 scopus 로고    scopus 로고
    • Inhibition of nuclear factor kappaB activation attenuates apoptosis resistance in lymphoid cells
    • JEREMIAS, I., KUPATT, C., BAUMANN, B., HERR, I., WIRTH, T., DEBATIN, K.M.: Inhibition of nuclear factor kappaB activation attenuates apoptosis resistance in lymphoid cells. Blood, 91, 1998, 4624-4631.
    • (1998) Blood , vol.91 , pp. 4624-4631
    • Jeremias, I.1    Kupatt, C.2    Baumann, B.3    Herr, I.4    Wirth, T.5    Debatin, K.M.6
  • 35
    • 0028609209 scopus 로고
    • JNK2 contains a specificity determining region responsible for efficient c-Jun binding and phosphorylation
    • KALLUNKI, T., SU, B., TSIGELNY, I., SLUSS, H.K., DERIJARD, B., MOORE, G., DAVIS, R., KARIN, M.: JNK2 contains a specificity determining region responsible for efficient c-Jun binding and phosphorylation. Genes Dev., 8, 1994, 2996-3007.
    • (1994) Genes Dev. , vol.8 , pp. 2996-3007
    • Kallunki, T.1    Su, B.2    Tsigelny, I.3    Sluss, H.K.4    Derijard, B.5    Moore, G.6    Davis, R.7    Karin, M.8
  • 36
    • 0029033544 scopus 로고
    • Rapid, comprehensive analysis of human cytokine mRNA and its application to the study of acute allograft rejection
    • KIRK, A.D., BOLLINGER, R.R., FINN, O.J.: Rapid, comprehensive analysis of human cytokine mRNA and its application to the study of acute allograft rejection. Hum. Immunol., 43, 1995, 113-128.
    • (1995) Hum. Immunol. , vol.43 , pp. 113-128
    • Kirk, A.D.1    Bollinger, R.R.2    Finn, O.J.3
  • 37
    • 0032574745 scopus 로고    scopus 로고
    • ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases
    • KOSEKI, T., INOHARA, N., CHEN, S., NUNEZ, G.: ARC, an inhibitor of apoptosis expressed in skeletal muscle and heart that interacts selectively with caspases. Proc. Natl. Acad. Sci. USA, 95, 1998, 5156-5160.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5156-5160
    • Koseki, T.1    Inohara, N.2    Chen, S.3    Nunez, G.4
  • 39
    • 0030007235 scopus 로고    scopus 로고
    • Intramolecular inhibition of activating transcription factor-2 function by its DNA-binding domain
    • LI, X.Y., GREEN, M.R.: Intramolecular inhibition of activating transcription factor-2 function by its DNA-binding domain. Genes Dev., 10, 1996, 517-527.
    • (1996) Genes Dev. , vol.10 , pp. 517-527
    • Li, X.Y.1    Green, M.R.2
  • 40
    • 0032583947 scopus 로고    scopus 로고
    • NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176
    • LING, L., CAO, Z., GOEDDEL, D.V: NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of Ser-176. Proc. Natl. Acad. Sci. USA, 95, 1998, 3792-3797.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 41
    • 0032168147 scopus 로고    scopus 로고
    • Acid sphingomyelinase-derived ceramide is not required for inflammatory cytokine signalling in murine macrophages
    • MANTHEY, C.L., SCHUCHMAN, E.H.: Acid sphingomyelinase-derived ceramide is not required for inflammatory cytokine signalling in murine macrophages. Cytokine, 10, 1998, 654-661.
    • (1998) Cytokine , vol.10 , pp. 654-661
    • Manthey, C.L.1    Schuchman, E.H.2
  • 42
    • 0023616299 scopus 로고
    • Tumor cell killing by tumor necrosis factor: Inhibition by anaerobic conditions, free-radical scavengers and inhibitors of arachidonate metabolism
    • MATTHEWS, N., NEALE, M.L., JACKSON, S.K., STARK, J.M.: Tumor cell killing by tumor necrosis factor: Inhibition by anaerobic conditions, free-radical scavengers and inhibitors of arachidonate metabolism. Immunology, 62, 1987, 153-155.
    • (1987) Immunology , vol.62 , pp. 153-155
    • Matthews, N.1    Neale, M.L.2    Jackson, S.K.3    Stark, J.M.4
  • 44
    • 0021967811 scopus 로고
    • Rapid induction of the expression of proto-oncogene fos during human monocylic differentiation
    • MITCHELL, R.L., ZOKAS, L., SCHREIBER, R.D., VERMA, I. M.: Rapid induction of the expression of proto-oncogene fos during human monocylic differentiation. Cell, 40, 1985, 209-217.
    • (1985) Cell , vol.40 , pp. 209-217
    • Mitchell, R.L.1    Zokas, L.2    Schreiber, R.D.3    Verma, I.M.4
  • 46
    • 0027264083 scopus 로고
    • Nuclear Factor kappa B, a mediator of lipopolysaccharide effects
    • MULLER, J.M., ZIEGLER-HEITBROCK, H.W., BAUERLE, P.A.: Nuclear Factor kappa B, a mediator of lipopolysaccharide effects. Immunobiology, 187, 1993, 233-256.
    • (1993) Immunobiology , vol.187 , pp. 233-256
    • Muller, J.M.1    Ziegler-Heitbrock, H.W.2    Bauerle, P.A.3
  • 47
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation of IkappaB kinase alpha and beta by upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK
    • NAKANO, H., SHINDO, M., SAKON, S., NISHINAKA, S., MIHARA, M., YAGITA, H., OKUMURA, K. : Differential regulation of IkappaB kinase alpha and beta by upstream kinases, NF-kappaB-inducing kinase and mitogen-activated protein kinase/ERK. Proc. Natl. Acad. Sci. USA, 95, 1998, 3537-3542.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3    Nishinaka, S.4    Mihara, M.5    Yagita, H.6    Okumura, K.7
  • 48
    • 0028092929 scopus 로고
    • Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-α gene
    • NEWELL, C.L., DEISSEROTH, A.B., LOPEZ-BERESTEIN, G.: Interaction of nuclear proteins with an AP-1/CRE-like promoter sequence in the human TNF-α gene. J. Leuk. Biol., 56, 1994, 27-35.
    • (1994) J. Leuk. Biol. , vol.56 , pp. 27-35
    • Newell, C.L.1    Deisseroth, A.B.2    Lopez-Berestein, G.3
  • 49
    • 0018749490 scopus 로고
    • Role of superoxide dismutase in cancer
    • OBERLEY, L.W., BUETTNER, G.R.: Role of superoxide dismutase in cancer. Cancer Res., 39, 1979, 1141-1149.
    • (1979) Cancer Res. , vol.39 , pp. 1141-1149
    • Oberley, L.W.1    Buettner, G.R.2
  • 50
    • 0342742310 scopus 로고
    • Tumor necrosis factor α and interleukin 1 stimulate the human immunodeficiency virus enhancer by activation of the nuclear factor κB
    • OSBORN, L., KUNKEL, S., NABEL, G.J.: Tumor necrosis factor α and interleukin 1 stimulate the human immunodeficiency virus enhancer by activation of the nuclear factor κB. Proc. Natl. Acad. Sci. USA, 86, 1989, 2336-2340.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 2336-2340
    • Osborn, L.1    Kunkel, S.2    Nabel, G.J.3
  • 51
    • 0027971696 scopus 로고
    • Control of tumor necrosis factor gene expression
    • PAULI, U.: Control of tumor necrosis factor gene expression. Crit. Rev. Eukaryotic Gene Exp., 4, 1994, 323-344.
    • (1994) Crit. Rev. Eukaryotic Gene Exp. , vol.4 , pp. 323-344
    • Pauli, U.1
  • 52
    • 0028957419 scopus 로고
    • Up-regulation of monocytic IL-10 by tumor necrosis factor-alpha and cAMP elevating drugs
    • PLATZER, C., MEISEL, C., VOGT, K., PLATZER, M., VOLK, H.D.: Up-regulation of monocytic IL-10 by tumor necrosis factor-alpha and cAMP elevating drugs. Int. Immunol., 7, 1995, 514-523.
    • (1995) Int. Immunol. , vol.7 , pp. 514-523
    • Platzer, C.1    Meisel, C.2    Vogt, K.3    Platzer, M.4    Volk, H.D.5
  • 53
    • 0027246226 scopus 로고
    • Elevated cyclic AMP inhibits endothelial cell synthesis and expression of TNF-induced endothelial leukocyte adhesion molecule-1, and vascular cell adhesion molecule-1, but not intercellular adhesion molecule-1
    • POBER, J.S., SLOWIK, M.R., DE LUCA, L.G., RITCHIE, A.J.: Elevated cyclic AMP inhibits endothelial cell synthesis and expression of TNF-induced endothelial leukocyte adhesion molecule-1, and vascular cell adhesion molecule-1, but not intercellular adhesion molecule-1. J. Immunol., 150, 1993, 5114-5123.
    • (1993) J. Immunol. , vol.150 , pp. 5114-5123
    • Pober, J.S.1    Slowik, M.R.2    De Luca, L.G.3    Ritchie, A.J.4
  • 55
    • 0031586174 scopus 로고    scopus 로고
    • Identification and characterization of an IkappaB kinase
    • REGNIER, C.H., SONG, H.Y., GAO, X., GOEDDEL, D.V., CAO, Z., ROTHE, M.: Identification and characterization of an IkappaB kinase. Cell, 90, 1997, 373-383.
    • (1997) Cell , vol.90 , pp. 373-383
    • Regnier, C.H.1    Song, H.Y.2    Gao, X.3    Goeddel, D.V.4    Cao, Z.5    Rothe, M.6
  • 56
    • 0029557622 scopus 로고
    • Applied molecular biology of sepsis
    • REMICK, D.G.: Applied molecular biology of sepsis. J. Crit. Care, 10, 1995, 198-212.
    • (1995) J. Crit. Care , vol.10 , pp. 198-212
    • Remick, D.G.1
  • 58
    • 0026352625 scopus 로고
    • Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein kinase C
    • SAKURAI, A., MAEKAWA, T., SUDO, T., ISHII, S., KISHIMOTO, A.: Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein kinase C. Biochem. Biophys. Res. Commun., 181, 1991, 629-635.
    • (1991) Biochem. Biophys. Res. Commun. , vol.181 , pp. 629-635
    • Sakurai, A.1    Maekawa, T.2    Sudo, T.3    Ishii, S.4    Kishimoto, A.5
  • 59
    • 0032512552 scopus 로고    scopus 로고
    • TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an NF-kappa B-inducing kinase-independent mechanism
    • SAKURAI, H., SHIGEMORI, N., HASEGAWA, K., SUGITA, T.: TGF-beta-activated kinase 1 stimulates NF-kappa B activation by an NF-kappa B-inducing kinase-independent mechanism. Biochem. Biophys. Res. Commun., 243, 1998, 545-549.
    • (1998) Biochem. Biophys. Res. Commun. , vol.243 , pp. 545-549
    • Sakurai, H.1    Shigemori, N.2    Hasegawa, K.3    Sugita, T.4
  • 60
    • 0020629944 scopus 로고
    • Kinetics and distribution of antigen-specific IgE-secreted cells during the primary antibody response in the rat
    • SEDGWICK, J.D., HOLT, P.G.: Kinetics and distribution of antigen-specific IgE-secreted cells during the primary antibody response in the rat. J. Exp. Med., 157, 1983, 2178-2183.
    • (1983) J. Exp. Med. , vol.157 , pp. 2178-2183
    • Sedgwick, J.D.1    Holt, P.G.2
  • 61
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • SEN, R., BALTIMORE, D.: Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell, 46, 1986, 705-716.
    • (1986) Cell , vol.46 , pp. 705-716
    • Sen, R.1    Baltimore, D.2
  • 63
    • 0030910313 scopus 로고    scopus 로고
    • MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase
    • SCHIEVELLA, A.R., CHEN, J.H., GRAHAM, J.R., LIN, L.L.: MADD, a novel death domain protein that interacts with the type 1 tumor necrosis factor receptor and activates mitogen-activated protein kinase. J. Biol. Chem., 272, 1997, 12 069-12 075.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12069-12075
    • Schievella, A.R.1    Chen, J.H.2    Graham, J.R.3    Lin, L.L.4
  • 64
    • 0031004569 scopus 로고    scopus 로고
    • Sodium salicylate induces apoptosis via p38 mitogen-activated protein kinase but inhibits tumor necrosis factor - Induced c-jun N-terminal kinase/stress-activated protein kinase activation
    • SCHWENGER, P., BELLOSTA, P., VIETOR, I., BASILICO, C., SKOLNIK, E.Y., VILCEK, J.: Sodium salicylate induces apoptosis via p38 mitogen-activated protein kinase but inhibits tumor necrosis factor - induced c-jun N-terminal kinase/stress-activated protein kinase activation. Proc. Natl. Acad. Sci. USA, 94, 1997, 2869-2873.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2869-2873
    • Schwenger, P.1    Bellosta, P.2    Vietor, I.3    Basilico, C.4    Skolnik, E.Y.5    Vilcek, J.6
  • 65
    • 0026696344 scopus 로고
    • Oncoprotein-mediated signaling cascade stimulates c-jun activity by phosphorylation of serines 63 and 73
    • SMEAL, T., BINETRUY, B., MERCOLA, D., GROVER-BARDWICK, A., HEIDECKER, G., RAPP, U.R., KARIN, M.: Oncoprotein-mediated signaling cascade stimulates c-jun activity by phosphorylation of serines 63 and 73. Mol. Cell Biol., 12, 1992, 3507-3513.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 3507-3513
    • Smeal, T.1    Binetruy, B.2    Mercola, D.3    Grover-Bardwick, A.4    Heidecker, G.5    Rapp, U.R.6    Karin, M.7
  • 66
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • SPRINGER, T.A.: Adhesion receptors of the immune system. Nature, 346, 1990, 425-34.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 68
    • 0029054725 scopus 로고
    • RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death
    • STANGER, B.Z., LEDER, P., LEE, T.H., KIM, E., SEED, B.: RIP: A novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death. Cell, 81, 1995, 513-523.
    • (1995) Cell , vol.81 , pp. 513-523
    • Stanger, B.Z.1    Leder, P.2    Lee, T.H.3    Kim, E.4    Seed, B.5
  • 69
    • 0027488676 scopus 로고
    • Role of tumor necrosis factor-α in disease states and inflammation
    • STRIETER, R.M., KUNKEL, S.L., BONE, R.C.: Role of tumor necrosis factor-α in disease states and inflammation. Crit. Care Med., 21, 1993, S447-S463.
    • (1993) Crit. Care Med. , vol.21
    • Strieter, R.M.1    Kunkel, S.L.2    Bone, R.C.3
  • 70
    • 0023582835 scopus 로고
    • Reduced tumor necrosis factor-α induced cytotoxicity by inhibitors of the arachidonic acid metabolism
    • SUFFYS, P., BEYAERT, R., VAN ROY, F, FIERS, W.: Reduced tumor necrosis factor-α induced cytotoxicity by inhibitors of the arachidonic acid metabolism. Biochem. Biophys. Res. Commun., 149, 1987, 735-743.
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 735-743
    • Suffys, P.1    Beyaert, R.2    Van Roy, F.3    Fiers, W.4
  • 71
    • 0026100924 scopus 로고
    • Tumor necrosis factor - Mediated cytotoxicity is correlated with phospholipase-A2 activity, but not with arachidonic acid release per se
    • SUFFYS, P., BEYAERT, R., DE VALCK, D., VANHAESEBROECK, B., VAN ROY, F., FIERS, W.: Tumor necrosis factor - mediated cytotoxicity is correlated with phospholipase-A2 activity, but not with arachidonic acid release per se. Eur. J. Biochem., 195, 1991, 465-475.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 465-475
    • Suffys, P.1    Beyaert, R.2    De Valck, D.3    Vanhaesebroeck, B.4    Van Roy, F.5    Fiers, W.6
  • 72
    • 0023727896 scopus 로고
    • Tumor necrosis factor increases the production of plasminogen activator inhibitor in human endothelial cells in vitro and in rats in vivo
    • VAN HINSBERG, V.W., KOOISTRA, T., VAN DER BERG, E.A., PRINCEN, H.M., FIERS, W., EMEIS, J.J.: Tumor necrosis factor increases the production of plasminogen activator inhibitor in human endothelial cells in vitro and in rats in vivo. Blood, 72, 1988, 1467-1473.
    • (1988) Blood , vol.72 , pp. 1467-1473
    • Van Hinsberg, V.W.1    Kooistra, T.2    Van Der Berg, E.A.3    Princen, H.M.4    Fiers, W.5    Emeis, J.J.6
  • 73
    • 0031398183 scopus 로고    scopus 로고
    • Examining a paradox in the pathogenesis of human pulmonary tuberculosis: Immune activation and suppression/anergy
    • VANHAM, G., TOOSI, Z., HIRSCH, C.S., WALLIS, R.S., SCHWANDER, S.K., RICH, E.A., ELLNER, J.J.: Examining a paradox in the pathogenesis of human pulmonary tuberculosis: Immune activation and suppression/anergy. Tuber. Lung Dis., 78, 1997, 145-158.
    • (1997) Tuber. Lung Dis. , vol.78 , pp. 145-158
    • Vanham, G.1    Toosi, Z.2    Hirsch, C.S.3    Wallis, R.S.4    Schwander, S.K.5    Rich, E.A.6    Ellner, J.J.7
  • 74
    • 0029994975 scopus 로고    scopus 로고
    • CCAAT box enhancer binding protein α (C/EBP-α) stimulates κB element-mediated transcription in transfected cells
    • VIETOR, I., OLIVEIRA, I.C., VILCEK, J.: CCAAT box enhancer binding protein α (C/EBP-α) stimulates κB element-mediated transcription in transfected cells. J. Biol. Chem., 271, 1996, 5595-5602.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5595-5602
    • Vietor, I.1    Oliveira, I.C.2    Vilcek, J.3
  • 76
    • 0031985628 scopus 로고    scopus 로고
    • Perforin-deficient CD8+ T cells provide immunity to Listeria monocytogenes by a mechanism that is independent of CD95 and IFN-gamma but requires TNF-alpha
    • WHITE, D.W., HARTY, J.T.: Perforin-deficient CD8+ T cells provide immunity to Listeria monocytogenes by a mechanism that is independent of CD95 and IFN-gamma but requires TNF-alpha. J. Immunol., 160, 1998, 898-905.
    • (1998) J. Immunol. , vol.160 , pp. 898-905
    • White, D.W.1    Harty, J.T.2
  • 77
    • 0024428198 scopus 로고
    • Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • WONG, G.H., ELWELL, J.H., OBERLEY, L.W., GOEDDEL, D.V.: Manganous Superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell, 58, 1989, 923-931.
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 79
    • 0031626410 scopus 로고    scopus 로고
    • Molecular mechanisms responsible for endotoxin tolerance
    • YOZA, B., LARUE, K., MCCALL, C.: Molecular mechanisms responsible for endotoxin tolerance. Prog. Clin. Biol. Res., 397, 1998, 209-215.
    • (1998) Prog. Clin. Biol. Res. , vol.397 , pp. 209-215
    • Yoza, B.1    Larue, K.2    Mccall, C.3
  • 80
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • ZANDI, E., ROTHWARF, D.M., DELHASE, M., HAYAKAWA, M., KARIN, M.: The IkappaB complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell, 91, 1997, 243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.