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Volumn 91, Issue , 2004, Pages 169-200

Raf-1 kinase inhibitor protein: Structure, function, regulation of cell signaling, and pivotal role in apoptosis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CISPLATIN; DOXORUBICIN; G PROTEIN COUPLED RECEPTOR KINASE 2; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INHIBITOR PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; PACLITAXEL; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; RAF PROTEIN; RITUXIMAB; UNCLASSIFIED DRUG;

EID: 4344607453     PISSN: 0065230X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-230X(04)91005-6     Document Type: Article
Times cited : (170)

References (75)
  • 1
    • 0027729196 scopus 로고
    • The MAP kinase cascade: Discovery of a new signal transduction pathway
    • Ahn N.G. The MAP kinase cascade: Discovery of a new signal transduction pathway. Mol. Cell. Biochem. 127128:1993;201-209
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 201-209
    • Ahn, N.G.1
  • 2
    • 0035393595 scopus 로고    scopus 로고
    • Rituximab inactivates STAT3 activity in B-non-Hodgkin's lymphoma through inhibition of the interleukin 10 autocrineparacrine loop and results in downregulation of Bcl-2 and sensitization to cytotoxic drugs
    • Alas S., Bonavida B. Rituximab inactivates STAT3 activity in B-non-Hodgkin's lymphoma through inhibition of the interleukin 10 autocrineparacrine loop and results in downregulation of Bcl-2 and sensitization to cytotoxic drugs. Cancer Res. 61:2001;5137-5144
    • (2001) Cancer Res. , vol.61 , pp. 5137-5144
    • Alas, S.1    Bonavida, B.2
  • 3
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors: Signaling and modulation. Science. 281:1998;1305-1308
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 4
    • 0031026293 scopus 로고    scopus 로고
    • Characterization of the transcriptional regulator YY1: The bipartite transactivation domain is independent of interaction with the TATA box-binding protein, transcription factor IIB, TAFII55, or cAMP-responsive element-binding protein (CBP)-binding protein
    • Austen M., Luscher B., Luscher-Firlaf J.M. Characterization of the transcriptional regulator YY1: The bipartite transactivation domain is independent of interaction with the TATA box-binding protein, transcription factor IIB, TAFII55, or cAMP-responsive element-binding protein (CBP)-binding protein. J. Biol. Chem. 272:1997;1709-1717
    • (1997) J. Biol. Chem. , vol.272 , pp. 1709-1717
    • Austen, M.1    Luscher, B.2    Luscher-Firlaf, J.M.3
  • 5
    • 0032532458 scopus 로고    scopus 로고
    • Function from structure? the crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction
    • Banfield M.J., Barker J.J., Perry A.C., Brady R.L. Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 6:1998;1245-1254
    • (1998) Structure , vol.6 , pp. 1245-1254
    • Banfield, M.J.1    Barker, J.J.2    Perry, A.C.3    Brady, R.L.4
  • 6
    • 0021751250 scopus 로고
    • Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain
    • Bernier I., Jolles P. Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain. Biochim. Biophys. Acta. 790:1984;174-181
    • (1984) Biochim. Biophys. Acta , vol.790 , pp. 174-181
    • Bernier, I.1    Jolles, P.2
  • 7
    • 0033580901 scopus 로고    scopus 로고
    • Caspases induce cytochrome c release from mitochondria by activating cytosolic factors
    • Bossy-Wetzel E., Green D.R. Caspases induce cytochrome c release from mitochondria by activating cytosolic factors. J. Biol. Chem. 274:1999;17484-17490
    • (1999) J. Biol. Chem. , vol.274 , pp. 17484-17490
    • Bossy-Wetzel, E.1    Green, D.R.2
  • 8
    • 0026596576 scopus 로고
    • Serum, TPA and Ras-induced expression from Ap-1Cts-driven promoter require Raf-1 kinase
    • Bruder J.T., Heidecher G., Rapp U.R. Serum, TPA and Ras-induced expression from Ap-1Cts-driven promoter require Raf-1 kinase. Genes Dev. 6:1992;545-556
    • (1992) Genes Dev. , vol.6 , pp. 545-556
    • Bruder, J.T.1    Heidecher, G.2    Rapp, U.R.3
  • 9
    • 0035476242 scopus 로고    scopus 로고
    • Induction of apoptosis in 9-nitrocamptothecin-treated DU145 human prostate carcinoma cells correlates with de novo synthesis of CD95 and CD95 ligand and down-regulation of c-FLIP (short)
    • Chatterjee D., Schmitz I., Krueger A., Yeung K., Kirchhoff S., Krammer P.H., Peter M.E., Wyche J.H., Pantazis P. Induction of apoptosis in 9-nitrocamptothecin-treated DU145 human prostate carcinoma cells correlates with de novo synthesis of CD95 and CD95 ligand and down-regulation of c-FLIP (short). Cancer Res. 61:2001;7148-7154
    • (2001) Cancer Res. , vol.61 , pp. 7148-7154
    • Chatterjee, D.1    Schmitz, I.2    Krueger, A.3    Yeung, K.4    Kirchhoff, S.5    Krammer, P.H.6    Peter, M.E.7    Wyche, J.H.8    Pantazis, P.9
  • 11
    • 0037362016 scopus 로고    scopus 로고
    • Monoclonal antibodies combined to chemotherapy for the treatment of patients with lymphoma
    • Coiffier B. Monoclonal antibodies combined to chemotherapy for the treatment of patients with lymphoma. Blood Rev. 17:2003;25-31
    • (2003) Blood Rev. , vol.17 , pp. 25-31
    • Coiffier, B.1
  • 12
    • 0037631323 scopus 로고    scopus 로고
    • Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein
    • Corbit K.C., Trakul N., Eves E.M., Diaz B., Marshall M., Rosner M.R. Activation of Raf-1 signaling by protein kinase C through a mechanism involving Raf kinase inhibitory protein. J. Biol. Chem. 278:2003;13061-13068
    • (2003) J. Biol. Chem. , vol.278 , pp. 13061-13068
    • Corbit, K.C.1    Trakul, N.2    Eves, E.M.3    Diaz, B.4    Marshall, M.5    Rosner, M.R.6
  • 13
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:1988;10881-10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 14
    • 0030800131 scopus 로고    scopus 로고
    • Chimeric anti-CD20 (IDEC-C2B8) monoclonal antibody sensitizes a B cell lymphoma cell line to cell killing by cytotoxic drugs
    • Demidem A., Lam T., Alas S., Hariharan K., Hanna N., Bonavida B. Chimeric anti-CD20 (IDEC-C2B8) monoclonal antibody sensitizes a B cell lymphoma cell line to cell killing by cytotoxic drugs. Cancer Biother. Radiopharm. 12:1997;177
    • (1997) Cancer Biother. Radiopharm. , vol.12 , pp. 177
    • Demidem, A.1    Lam, T.2    Alas, S.3    Hariharan, K.4    Hanna, N.5    Bonavida, B.6
  • 16
    • 0036928350 scopus 로고    scopus 로고
    • Rituximab-mediated sensitization of non-Hodgkin's lymphoma (NHL) B-cells to cytotoxicity induced by paclitaxel, gemcitabine and vinorelbine
    • Emmanouilides C., Jazirehi A.R., Bonavida B. Rituximab-mediated sensitization of non-Hodgkin's lymphoma (NHL) B-cells to cytotoxicity induced by paclitaxel, gemcitabine and vinorelbine. Cancer Biother. Radiopharm. 17:2002;621-630
    • (2002) Cancer Biother. Radiopharm. , vol.17 , pp. 621-630
    • Emmanouilides, C.1    Jazirehi, A.R.2    Bonavida, B.3
  • 17
    • 0032748447 scopus 로고    scopus 로고
    • Localisation of phosphotidylethanolamine-binding protein in the brain and other tissues of the rat
    • Frayne J., Ingram C., Love S., Hall L. Localisation of phosphotidylethanolamine-binding protein in the brain and other tissues of the rat. Cell Tissue Res. 298:1999;415-423
    • (1999) Cell Tissue Res. , vol.298 , pp. 415-423
    • Frayne, J.1    Ingram, C.2    Love, S.3    Hall, L.4
  • 18
    • 0036535187 scopus 로고    scopus 로고
    • Osteoblasts produce soluble factors that induced a gene expression pattern in non metastatic prostate cells, similar to that found in bone metastatic cancer cells
    • Fu Z., Dozmorov I., Keller E. Osteoblasts produce soluble factors that induced a gene expression pattern in non metastatic prostate cells, similar to that found in bone metastatic cancer cells. Prostate. 51:2002;10-20
    • (2002) Prostate , vol.51 , pp. 10-20
    • Fu, Z.1    Dozmorov, I.2    Keller, E.3
  • 20
    • 0035399797 scopus 로고    scopus 로고
    • Nitric oxide inhibits the transcription repressor Yin-Yang 1 binding activity at the silencer region of the Fas promoter: A pivotal role for nitric oxide in the up-regulation of Fas gene expression in human tumor cells
    • Garban H., Bonavida B. Nitric oxide inhibits the transcription repressor Yin-Yang 1 binding activity at the silencer region of the Fas promoter: A pivotal role for nitric oxide in the up-regulation of Fas gene expression in human tumor cells. J. Immunol. 167:2001;75-81
    • (2001) J. Immunol. , vol.167 , pp. 75-81
    • Garban, H.1    Bonavida, B.2
  • 21
    • 0034092777 scopus 로고    scopus 로고
    • Ras regulation and function in lymphocytes
    • Genot E., Cantrell D.A. Ras regulation and function in lymphocytes. Curr. Opin. Immunol. 12:2000;289-294
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 289-294
    • Genot, E.1    Cantrell, D.A.2
  • 22
    • 0031897632 scopus 로고    scopus 로고
    • NF-κB and Rel proteins: Evolutionary conserved mediators of immune responses
    • Ghosh S., May M.J., Kopp E.B. NF-κB and Rel proteins: Evolutionary conserved mediators of immune responses. Annu. Rev. Immunol. 16:1998;225-260
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 24
    • 0035808362 scopus 로고    scopus 로고
    • The phosphatidyl ethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors
    • Hengst U., Albrecht H., Hess D., Monard D. The phosphatidyl ethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. J. Biol. Chem. 276:2001;535-540
    • (2001) J. Biol. Chem. , vol.276 , pp. 535-540
    • Hengst, U.1    Albrecht, H.2    Hess, D.3    Monard, D.4
  • 26
    • 3042737429 scopus 로고    scopus 로고
    • Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inactivation of NF-kappaB and inhibition of Bcl-(xL) expression
    • [Epub ahead of print].
    • Huerta-Yepez S., Vega M., Jazirehi A., Garban H., Hongo F., Cheng G., Bonavida B. Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inactivation of NF-kappaB and inhibition of Bcl-(xL) expression. Oncogene. 2004;. [Epub ahead of print].
    • (2004) Oncogene.
    • Huerta-Yepez, S.1    Vega, M.2    Jazirehi, A.3    Garban, H.4    Hongo, F.5    Cheng, G.6    Bonavida, B.7
  • 28
    • 85112378525 scopus 로고    scopus 로고
    • Rituximab sensitizes non-Hodgkin's lymphoma (NHL) B cell lines to Taxol-mediated cytotoxicity and synergy is achieved in both apoptosis and necrosis [abstract 563]
    • Jazirehi A.R., Emmanoluides C., Bonavida B. Rituximab sensitizes non-Hodgkin's lymphoma (NHL) B cell lines to Taxol-mediated cytotoxicity and synergy is achieved in both apoptosis and necrosis [abstract 563]. Blood. 96:2000;131a
    • (2000) Blood , vol.96
    • Jazirehi, A.R.1    Emmanoluides, C.2    Bonavida, B.3
  • 33
    • 0036546501 scopus 로고    scopus 로고
    • NF-κB in cancer: From innocent bystander to major culprit
    • Karin M., Cao Y., Greten F.R., Li Z.-W. NF-κB in cancer: From innocent bystander to major culprit. Nat. Rev. 2:2002;301
    • (2002) Nat. Rev. , vol.2 , pp. 301
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.-W.4
  • 34
    • 0030584787 scopus 로고    scopus 로고
    • CD45 ligation induces programmed cell death in T and B lymphocytes
    • Klaus S.J., Sidorenko S.P., Clark E.A. CD45 ligation induces programmed cell death in T and B lymphocytes. J. Immunol. 156:1996;2743-2753
    • (1996) J. Immunol. , vol.156 , pp. 2743-2753
    • Klaus, S.J.1    Sidorenko, S.P.2    Clark, E.A.3
  • 35
    • 0037362947 scopus 로고    scopus 로고
    • Metastasis suppression: The evolving role of metastasis suppressor genes for regulating cancer cell growth at the secondary site
    • Kauffman E.C., Robinson V.L., Stadler W.M., Sokoloff M.H., Rinker-Schaeffer C.W. Metastasis suppression: The evolving role of metastasis suppressor genes for regulating cancer cell growth at the secondary site. J. Urol. 169:2003;1122-1133
    • (2003) J. Urol. , vol.169 , pp. 1122-1133
    • Kauffman, E.C.1    Robinson, V.L.2    Stadler, W.M.3    Sokoloff, M.H.4    Rinker-Schaeffer, C.W.5
  • 36
    • 0036848530 scopus 로고    scopus 로고
    • Steroid hormones, endometrial gene regulation and the Sp1 family of proteins
    • Krikun G., Lockwood C.J. Steroid hormones, endometrial gene regulation and the Sp1 family of proteins. J. Soc. Gynecol. Invest. 9:2002;329-334
    • (2002) J. Soc. Gynecol. Invest. , vol.9 , pp. 329-334
    • Krikun, G.1    Lockwood, C.J.2
  • 37
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling
    • Kroslak T., Koch T., Kahl E., Hollt V. Human phosphatidylethanolamine- binding protein facilitates heterotrimeric G protein-dependent signaling. J. Biol. Chem. 276:2001;39772-39778
    • (2001) J. Biol. Chem. , vol.276 , pp. 39772-39778
    • Kroslak, T.1    Koch, T.2    Kahl, E.3    Hollt, V.4
  • 38
    • 0031747997 scopus 로고    scopus 로고
    • The role of receptor kinases and arrestins in G-protein coupled receptor regulation
    • Krupuilk J.G., Benovic J.L. The role of receptor kinases and arrestins in G-protein coupled receptor regulation. Am. Rev. Pharmacol. Toxicol. 38:1998;289-319
    • (1998) Am. Rev. Pharmacol. Toxicol. , vol.38 , pp. 289-319
    • Krupuilk, J.G.1    Benovic, J.L.2
  • 39
    • 0344310763 scopus 로고    scopus 로고
    • Mechanisms of β-adrenergic receptor desensitization and resensitization
    • Lefkowitz R.J., Pitcher J., Krueger K., Daak Y. Mechanisms of β-adrenergic receptor desensitization and resensitization. Adv. Pharmacol. 42:1998;416-420
    • (1998) Adv. Pharmacol. , vol.42 , pp. 416-420
    • Lefkowitz, R.J.1    Pitcher, J.2    Krueger, K.3    Daak, Y.4
  • 40
    • 0036009909 scopus 로고    scopus 로고
    • NF-κB-dependent signaling pathways
    • Li X., Stark G.R. NF-κB-dependent signaling pathways. Exp. Hematol. 30:2002;285-296
    • (2002) Exp. Hematol. , vol.30 , pp. 285-296
    • Li, X.1    Stark, G.R.2
  • 41
    • 0346874333 scopus 로고    scopus 로고
    • Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2
    • Lorenz K., Lohse M.J., Quitterer U. Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature. 426:2003;574-579
    • (2003) Nature , vol.426 , pp. 574-579
    • Lorenz, K.1    Lohse, M.J.2    Quitterer, U.3
  • 43
    • 0029855237 scopus 로고    scopus 로고
    • Control of the ERK MAP kinase cascade by Ras and Raf
    • [Review: Marks, D. B., Marks, A. D., and Smith, C. M. (1996). "Basic Medical Biochemistry: A Clinical Approach." Lippincott Williams & Wilkins, Philadelphia, PA.]
    • Marais R., Marshall C.J. Control of the ERK MAP kinase cascade by Ras and Raf. [Review: Marks, D. B., Marks, A. D., and Smith, C. M. (1996). "Basic Medical Biochemistry: A Clinical Approach." Lippincott Williams & Wilkins, Philadelphia, PA.] Cancer Surv. 27:1996;101-125
    • (1996) Cancer Surv. , vol.27 , pp. 101-125
    • Marais, R.1    Marshall, C.J.2
  • 44
    • 0037453219 scopus 로고    scopus 로고
    • Assessment by molecular dynamics simulations of the structural determinants of DNA-binding specificity for transcription factor Sp1
    • Marco E., Garcia-Nieto R., Gago F. Assessment by molecular dynamics simulations of the structural determinants of DNA-binding specificity for transcription factor Sp1. J. Mol. Biol. 328:2003;9-32
    • (2003) J. Mol. Biol. , vol.328 , pp. 9-32
    • Marco, E.1    Garcia-Nieto, R.2    Gago, F.3
  • 46
    • 0027337519 scopus 로고
    • Complexes of Ras:GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie S.A., Willumsen B.M., Weber M.J., Wolfman A. Complexes of Ras:GTP with Raf-1 and mitogen-activated protein kinase kinase. Science. 260:1993;1658-1661
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 47
  • 48
    • 0036391746 scopus 로고    scopus 로고
    • A new challenge for successful immunotherapy by tumors that are resistant to apoptosis: Two complementary signals to overcome cross-resistance
    • Ng C.-P., Bonavida B. A new challenge for successful immunotherapy by tumors that are resistant to apoptosis: Two complementary signals to overcome cross-resistance. Adv. Cancer Res. 85:2002;145-174
    • (2002) Adv. Cancer Res. , vol.85 , pp. 145-174
    • Ng, C.-P.1    Bonavida, B.2
  • 50
    • 0033607313 scopus 로고    scopus 로고
    • The NF-κB activation pathway: A paradigm in information transfer from membrane to nucleus [review]
    • Rothwarf D.M., Karin M. The NF-κB activation pathway: A paradigm in information transfer from membrane to nucleus [review]. Sci. STKE. 5:1999;RE1
    • (1999) Sci. STKE , vol.5 , pp. 1
    • Rothwarf, D.M.1    Karin, M.2
  • 51
    • 0037868957 scopus 로고    scopus 로고
    • Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons
    • Ryu H., Lee H., Zaman K., Kubilis J., Ferrante R., Ross B.D., Neve R., Ratan R.R. Sp1 and Sp3 are oxidative stress-inducible, antideath transcription factors in cortical neurons. J. Neurosci. 23:2003;3597-3606
    • (2003) J. Neurosci. , vol.23 , pp. 3597-3606
    • Ryu, H.1    Lee, H.2    Zaman, K.3    Kubilis, J.4    Ferrante, R.5    Ross, B.D.6    Neve, R.7    Ratan, R.R.8
  • 52
    • 0033587066 scopus 로고    scopus 로고
    • Apoptotic nuclear morphological change without DNA fragmentation
    • Sakahira H., Enari M., Ohsawa Y., Uchiyama Y., Nagata S. Apoptotic nuclear morphological change without DNA fragmentation. Curr. Biol. 9:1999;543-546
    • (1999) Curr. Biol. , vol.9 , pp. 543-546
    • Sakahira, H.1    Enari, M.2    Ohsawa, Y.3    Uchiyama, Y.4    Nagata, S.5
  • 54
    • 0029123401 scopus 로고
    • From structure to function: Possible biological roles of a new wide-spread protein family binding hydrophobic ligands and displaying a nucleotide binding site
    • Schoentgen F., Jolles P. From structure to function: Possible biological roles of a new wide-spread protein family binding hydrophobic ligands and displaying a nucleotide binding site. FEBS Lett. 369:1995;22-26
    • (1995) FEBS Lett. , vol.369 , pp. 22-26
    • Schoentgen, F.1    Jolles, P.2
  • 55
    • 0023655581 scopus 로고
    • Complete amino acid sequence of basic 21-kDa protein from bovine brain cytosol
    • Schoentgen F., Saccoccio F., Jolles J., Bernier I., Jolles P. Complete amino acid sequence of basic 21-kDa protein from bovine brain cytosol. Eur. J. Biochem. 166:1987;333-338
    • (1987) Eur. J. Biochem. , vol.166 , pp. 333-338
    • Schoentgen, F.1    Saccoccio, F.2    Jolles, J.3    Bernier, I.4    Jolles, P.5
  • 56
    • 4344616065 scopus 로고    scopus 로고
    • TESS: Transcription Element Search Software on the WWW. Technical report CBIL-TR-1997-1001-v0.0. URL:
    • Schug J., Overton G.C. TESS: Transcription Element Search Software on the WWW. Technical report CBIL-TR-1997-1001-v0.0. URL: http:www.cbil.upenn.edutess: 1997
    • (1997)
    • Schug, J.1    Overton, G.C.2
  • 57
    • 0030046845 scopus 로고    scopus 로고
    • Characterization and localization of the rat, mouse, and human testicular phosphatidylethanolamine binding protein
    • Seddiqi N., Segretain D., Bucquoy S., Jegou B., Jolles P., Schoentgen F. Characterization and localization of the rat, mouse, and human testicular phosphatidylethanolamine binding protein. Experientia. 52:1996;101-110
    • (1996) Experientia , vol.52 , pp. 101-110
    • Seddiqi, N.1    Segretain, D.2    Bucquoy, S.3    Jegou, B.4    Jolles, P.5    Schoentgen, F.6
  • 58
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • Shaulian E., Karin M. AP-1 as a regulator of cell life and death. Nat. Cell Biol. 4:2002;E131-E136
    • (2002) Nat. Cell Biol. , vol.4
    • Shaulian, E.1    Karin, M.2
  • 60
    • 0036077621 scopus 로고    scopus 로고
    • The crystal structure of PEBP-2, a homologue of the PEBPRKIP family
    • Simister P.C., Banfield M.J., Brady R.L. The crystal structure of PEBP-2, a homologue of the PEBPRKIP family. Acta Crystallogr. D. 58:2002;1077-1080
    • (2002) Acta Crystallogr. D , vol.58 , pp. 1077-1080
    • Simister, P.C.1    Banfield, M.J.2    Brady, R.L.3
  • 63
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of diseases
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of diseases. Science. 267:1995;1456
    • (1995) Science , vol.267 , pp. 1456
    • Thompson, C.B.1
  • 64
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: Enemies within. Science. 281:1998;1312-1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 65
  • 66
    • 0033571741 scopus 로고    scopus 로고
    • Stability and physicochemical properties of the bovine brain phosphatidylethanolamine-binding protein
    • Vallee B., Teyssier C., Maget-Dana R., Ramstein J., Bureaud N., Schoentgen F. Stability and physicochemical properties of the bovine brain phosphatidylethanolamine-binding protein. Eur. J. Biochem. 266:1999;40-52
    • (1999) Eur. J. Biochem. , vol.266 , pp. 40-52
    • Vallee, B.1    Teyssier, C.2    Maget-Dana, R.3    Ramstein, J.4    Bureaud, N.5    Schoentgen, F.6
  • 67
    • 2442684327 scopus 로고    scopus 로고
    • Rituximab inhibits p38 MAPK activity in 2F7 B NHL and decreases IL-10 transcription: Pivotal role of p38 MAPK in drug resistance
    • Vega M.I., Huerta-Yepez S., Garban H., Jazirehi A., Emmanouilides C., Bonavida B. Rituximab inhibits p38 MAPK activity in 2F7 B NHL and decreases IL-10 transcription: Pivotal role of p38 MAPK in drug resistance. Oncogene. 23:2004;3530-3540
    • (2004) Oncogene , vol.23 , pp. 3530-3540
    • Vega, M.I.1    Huerta-Yepez, S.2    Garban, H.3    Jazirehi, A.4    Emmanouilides, C.5    Bonavida, B.6
  • 69
    • 0035001054 scopus 로고    scopus 로고
    • Blocking Sp1 transcription factor broadly inhibits extracellular matrix gene expression in vitro and in vivo: Implications for the treatment of tissue fibrosis
    • Verrecchia F., Rossert J., Nayvuekm A. Blocking Sp1 transcription factor broadly inhibits extracellular matrix gene expression in vitro and in vivo: Implications for the treatment of tissue fibrosis. J. Invest. Dermatol. 116:2001;755-763
    • (2001) J. Invest. Dermatol. , vol.116 , pp. 755-763
    • Verrecchia, F.1    Rossert, J.2    Nayvuekm, A.3
  • 70
    • 0038718523 scopus 로고    scopus 로고
    • A new member of the growing family of metastasis suppressors identified in prostate cancer
    • Welsh D.R., Hunter T.W. A new member of the growing family of metastasis suppressors identified in prostate cancer. J. Natl. Cancer Inst. 95:2003;839-841
    • (2003) J. Natl. Cancer Inst. , vol.95 , pp. 839-841
    • Welsh, D.R.1    Hunter, T.W.2
  • 71
    • 0029808748 scopus 로고    scopus 로고
    • Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways
    • Whitmarsh A.J., Davis R.J. Transcription factor AP-1 regulation by mitogen-activated protein kinase signal transduction pathways. J. Mol. Med. 74:1996;589-607
    • (1996) J. Mol. Med. , vol.74 , pp. 589-607
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 72
    • 0033604640 scopus 로고
    • AP-1: One switch for many signals
    • Wisdom R. AP-1: One switch for many signals. Exp. Cell Res. 253:1992;180-185
    • (1992) Exp. Cell Res. , vol.253 , pp. 180-185
    • Wisdom, R.1
  • 74
    • 0034003003 scopus 로고    scopus 로고
    • Mechanism of suppression of the RafMEKextracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein
    • Yeung K., Janosch P., McFerran B., Rose D.W., Mischak H., Sedivy J.M., Kolch W. Mechanism of suppression of the RafMEKextracellular signal-regulated kinase pathway by the Raf kinase inhibitor protein. Mol. Cell. Biol. 20:2000;3079-3085
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3079-3085
    • Yeung, K.1    Janosch, P.2    McFerran, B.3    Rose, D.W.4    Mischak, H.5    Sedivy, J.M.6    Kolch, W.7


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