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Volumn 246, Issue , 2005, Pages 1-29

Redundancy of biological regulation as the basis of emergence of multidrug resistance

Author keywords

Anticancer drugs; Gene expression; Multidrug resistance; P glycoprotein; Signal transduction

Indexed keywords

5 AZA 2' DEOXYCYTIDINE; ADENOSINE TRIPHOSPHATE DEPENDENT PROTEINASE; ANTIINFECTIVE AGENT; ANTINEOPLASTIC AGENT; CALCIUM ION; DACTINOMYCIN; DNA METHYLTRANSFERASE INHIBITOR; HISTONE DEACETYLASE INHIBITOR; I KAPPA B; I KAPPA B KINASE GAMMA; I KAPPA B KINASE INHIBITOR; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MULTIDRUG RESISTANCE PROTEIN 1; PHORBOL ESTER; PHOSPHOLIPASE C; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; PYRROLIDINE DITHIOCARBAMATE; SALICYLIC ACID DERIVATIVE; TOSYLPHENYLALANYL CHLOROMETHYL KETONE; TRICHOSTATIN A; VINCRISTINE; XENOBIOTIC AGENT; CALCIUM; GLYCOPROTEIN P; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; TRANSCRIPTION FACTOR;

EID: 25144494203     PISSN: 00747696     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0074-7696(05)46001-5     Document Type: Review
Times cited : (38)

References (158)
  • 1
    • 0028884033 scopus 로고
    • PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo
    • Alessi D.R., Cuenda A., Cohen P., Dudley D.T, and Saltiel A.R. PD 098059 is a specific inhibitor of the activation of mitogen-activated protein kinase kinase in vitro and in vivo J. Biol. Chem. 270 1995 27489 27494
    • (1995) J. Biol. Chem. , vol.270 , pp. 27489-27494
    • Alessi, D.R.1    Cuenda, A.2    Cohen, P.3    Dudley, D.T.4    Saltiel, A.R.5
  • 2
    • 0028970734 scopus 로고
    • Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway
    • Alkalay I., Yaron A., Hatzubai A., Orian A., and Ciechanover A. Stimulation-dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin-proteasome pathway Proc. Natl. Acad. Sci. USA 92 1995 10599 10603
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10599-10603
    • Alkalay, I.1    Yaron, A.2    Hatzubai, A.3    Orian, A.4    Ciechanover, A.5
  • 4
    • 0026673345 scopus 로고
    • The protein kinase C and protein kinase C related gene families
    • Azzi A., Boscoboinik D., and Hensey C. The protein kinase C and protein kinase C related gene families Eur. J. Biochem. 208 1992 547 557
    • (1992) Eur. J. Biochem. , vol.208 , pp. 547-557
    • Azzi, A.1    Boscoboinik, D.2    Hensey, C.3
  • 5
    • 0028789109 scopus 로고
    • Oncogenic transformation alters cisplatin induced apoptosis in rat embryo fibroblasts
    • Basu A., and Cline J.S. Oncogenic transformation alters cisplatin induced apoptosis in rat embryo fibroblasts Int. J. Cancer 63 1995 597 603
    • (1995) Int. J. Cancer , vol.63 , pp. 597-603
    • Basu, A.1    Cline, J.S.2
  • 6
    • 0024460547 scopus 로고
    • Expression of a drug resistance gene in human neuroblastoma cell lines: Modulation by retinoic acid-induced differentiation
    • Bates S.E., Mickley L.A., Chen Y.N., Richert N., Rudick J., Biedler J.L., and Fojo A.T. Expression of a drug resistance gene in human neuroblastoma cell lines: Modulation by retinoic acid-induced differentiation Mol. Cell. Biol. 9 1989 4337 4344
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4337-4344
    • Bates, S.E.1    Mickley, L.A.2    Chen, Y.N.3    Richert, N.4    Rudick, J.5    Biedler, J.L.6    Fojo, A.T.7
  • 7
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signaling
    • Berridge M.J. Inositol trisphosphate and calcium signaling Nature 361 1993 315 325
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 8
    • 0032170560 scopus 로고    scopus 로고
    • Regulation of expression of the DNA repair gene O6-methylguanine-DNA methyltransferase via protein kinase C-mediated signaling
    • Boldogh I., Ramana C.V., Chen Z., Biswas T., Hazra T.K., Grosch S., Grombacher T., Mitra S., and Kaina B. Regulation of expression of the DNA repair gene O6-methylguanine-DNA methyltransferase via protein kinase C-mediated signaling Cancer Res. 58 1998 3950 3956
    • (1998) Cancer Res. , vol.58 , pp. 3950-3956
    • Boldogh, I.1    Ramana, C.V.2    Chen, Z.3    Biswas, T.4    Hazra, T.K.5    Grosch, S.6    Grombacher, T.7    Mitra, S.8    Kaina, B.9
  • 9
    • 0029148660 scopus 로고
    • Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals
    • Bose R., Verheij M., Haimovitz-Friedman A., Scotto K., Fuks Z., and Kolesnick R. Ceramide synthase mediates daunorubicin-induced apoptosis: An alternative mechanism for generating death signals Cell 82 1995 405 414
    • (1995) Cell , vol.82 , pp. 405-414
    • Bose, R.1    Verheij, M.2    Haimovitz-friedman, A.3    Scotto, K.4    Fuks, Z.5    Kolesnick, R.6
  • 10
    • 0028986075 scopus 로고
    • Control of IκBα proteolysis by site-specific, signal-induced phosphorylation
    • Brown K., Gerstberger S., Carlson L., Franzoso G., and Siebenlist U. Control of IκBα proteolysis by site-specific, signal-induced phosphorylation Science 267 1995 1485 1488
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 11
    • 0034705110 scopus 로고    scopus 로고
    • NF-κB inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells
    • Cahir-McFarland E.D., Davidson D.M., Schauer S.L., Duong J., and Kieff E. NF-κB inhibition causes spontaneous apoptosis in Epstein-Barr virus-transformed lymphoblastoid cells Proc. Natl. Acad. Sci. USA 97 2000 6055 6060
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6055-6060
    • Cahir-mcfarland, E.D.1    Davidson, D.M.2    Schauer, S.L.3    Duong, J.4    Kieff, E.5
  • 12
    • 0032948005 scopus 로고    scopus 로고
    • Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer
    • Cameron E.E., Bachman K.E., Myohanen S., Herman J.G., and Baylin S.B. Synergy of demethylation and histone deacetylase inhibition in the re-expression of genes silenced in cancer Nature (Genetics) 21 1999 103 107
    • (1999) Nature (Genetics) , vol.21 , pp. 103-107
    • Cameron, E.E.1    Bachman, K.E.2    Myohanen, S.3    Herman, J.G.4    Baylin, S.B.5
  • 13
    • 0028052255 scopus 로고
    • Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun
    • Cano E., Hazzalin C., and Mahadevan L. Anisomycin-activated protein kinases p45 and p55 but not mitogen-activated protein kinases ERK-1 and -2 are implicated in the induction of c-fos and c-jun Mol. Cell. Biol. 14 1994 7352 7362
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7352-7362
    • Cano, E.1    Hazzalin, C.2    Mahadevan, L.3
  • 14
    • 0030177190 scopus 로고    scopus 로고
    • Modulation of chemosensitivity in human colon carcinoma cells by down-regulating protein kinase C alpha expression
    • Chakrabarty S., and Huang S. Modulation of chemosensitivity in human colon carcinoma cells by down-regulating protein kinase C alpha expression J. Exp. Ther. Oncol. 1 1996 218 221
    • (1996) J. Exp. Ther. Oncol. , vol.1 , pp. 218-221
    • Chakrabarty, S.1    Huang, S.2
  • 16
    • 0027005480 scopus 로고
    • Activation of MDR1 (P-glycoprotein) gene expression in human cells by protein kinase C agonists
    • Chaudhary P.M., and Roninson I.B. Activation of MDR1 (P-glycoprotein) gene expression in human cells by protein kinase C agonists Oncol. Res. 4 1992 281 290
    • (1992) Oncol. Res. , vol.4 , pp. 281-290
    • Chaudhary, P.M.1    Roninson, I.B.2
  • 17
    • 0027506202 scopus 로고
    • Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs
    • Chaudhary P.M., and Roninson I.B. Induction of multidrug resistance in human cells by transient exposure to different chemotherapeutic drugs J. Natl. Cancer Inst. 85 1993 632 639
    • (1993) J. Natl. Cancer Inst. , vol.85 , pp. 632-639
    • Chaudhary, P.M.1    Roninson, I.B.2
  • 18
    • 1842483291 scopus 로고    scopus 로고
    • Effect of mitogen-activated protein kinase signal transduction pathway on multidrug resistance induced by vincristine in gastric cancer cell line MGC803
    • Chen B., Jin F., Lu P., Lu X.L., Wang P.P., Liu Y.P., Yao F., and Wang S.B. Effect of mitogen-activated protein kinase signal transduction pathway on multidrug resistance induced by vincristine in gastric cancer cell line MGC803 World J. Gastroenterol. 10 2004 795 799
    • (2004) World J. Gastroenterol. , vol.10 , pp. 795-799
    • Chen, B.1    Jin, F.2    Lu, P.3    Lu, X.L.4    Wang, P.P.5    Liu, Y.P.6    Yao, F.7    Wang, S.B.8
  • 19
    • 0028131915 scopus 로고
    • Selective degradation of early-response-gene mRNAs: Functional analyses of sequence features of the AU-rich elements
    • Chen C.-Y., and Shyu A.-B. Selective degradation of early-response-gene mRNAs: Functional analyses of sequence features of the AU-rich elements Mol. Cell. Biol. 14 1994 8471 8482
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8471-8482
    • Chen, C.-Y.1    Shyu, A.-B.2
  • 20
  • 21
    • 0024414605 scopus 로고
    • Structure and expression of the human MDR (P-glycoprotein) gene family
    • Chin J.E., Soffir R., Noonan K.E., Choi K., and Roninson I.B. Structure and expression of the human MDR (P-glycoprotein) gene family Mol. Cell. Biol. 9 1989 3808 3820
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 3808-3820
    • Chin, J.E.1    Soffir, R.2    Noonan, K.E.3    Choi, K.4    Roninson, I.B.5
  • 22
    • 0025060257 scopus 로고
    • Heat shock and arsenite increase expression of the multidrug resistance (MDR1) gene in human renal carcinoma cells
    • Chin K.V., Tanaka S., Darlington G., Pastan I., and Gottesman M.M. Heat shock and arsenite increase expression of the multidrug resistance (MDR1) gene in human renal carcinoma cells J. Biol. Chem. 265 1990 221 226
    • (1990) J. Biol. Chem. , vol.265 , pp. 221-226
    • Chin, K.V.1    Tanaka, S.2    Darlington, G.3    Pastan, I.4    Gottesman, M.M.5
  • 25
    • 0037203313 scopus 로고    scopus 로고
    • Phosphatidylcholine and cell death
    • Cui Z., and Houweling M. Phosphatidylcholine and cell death Biochem. Biophys. Acta 1585 2002 87 96
    • (2002) Biochem. Biophys. Acta , vol.1585 , pp. 87-96
    • Cui, Z.1    Houweling, M.2
  • 26
    • 0030610472 scopus 로고    scopus 로고
    • Activation of NF-kappaB by antineoplastic agents. Role of protein kinase C
    • Das K.C., and White C.W. Activation of NF-kappaB by antineoplastic agents. Role of protein kinase C J. Biol. Chem. 272 1997 14914 14920
    • (1997) J. Biol. Chem. , vol.272 , pp. 14914-14920
    • Das, K.C.1    White, C.W.2
  • 28
    • 0035200658 scopus 로고    scopus 로고
    • Cellular thiols and reactive oxygen species in drug-induced apoptosis
    • Davis W. Jr., Ronai Z., and Tew K.D. Cellular thiols and reactive oxygen species in drug-induced apoptosis J. Pharmacol. Exp. Ther. 296 2001 1 6
    • (2001) J. Pharmacol. Exp. Ther. , vol.296 , pp. 1-6
    • Davis Jr., W.1    Ronai, Z.2    Tew, K.D.3
  • 29
    • 0033963650 scopus 로고    scopus 로고
    • P-glycoprotein is localized in caveolae in resistant cells and in brain capillaries
    • Demeule M., Jodoin J., Gingras D., and Béliveau R. P-glycoprotein is localized in caveolae in resistant cells and in brain capillaries FEBS Letters 466 2000 219 224
    • (2000) FEBS Letters , vol.466 , pp. 219-224
    • Demeule, M.1    Jodoin, J.2    Gingras, D.3    Béliveau, R.4
  • 30
    • 0031865310 scopus 로고    scopus 로고
    • Demethylation of the human MDR1 5′ region accompanies activation of P-glycoprotein expression in a HL60 multidrug resistant subline
    • Desiderato L., Davey M.W., and Piper A.A. Demethylation of the human MDR1 5′ region accompanies activation of P-glycoprotein expression in a HL60 multidrug resistant subline Somat. Cell Mol. Genet. 23 1997 391 400
    • (1997) Somat. Cell Mol. Genet. , vol.23 , pp. 391-400
    • Desiderato, L.1    Davey, M.W.2    Piper, A.A.3
  • 31
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J.A., Mercurio F., Rosette C., Wu-Li J., Suyang H., Ghosh S., and Karin M. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation Mol. Cell. Biol. 16 1996 1295 1304
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1295-1304
    • Didonato, J.A.1    Mercurio, F.2    Rosette, C.3    Wu-li, J.4    Suyang, H.5    Ghosh, S.6    Karin, M.7
  • 32
    • 0035914258 scopus 로고    scopus 로고
    • Cross-talk between signalling pathways and the multidrug resistant protein MDR-1
    • Ding S., Chamberlain M., McLaren A., Goh L., Duncan I., and Wolf C.R. Cross-talk between signalling pathways and the multidrug resistant protein MDR-1 Br. J. Cancer 85 2001 1175 1184
    • (2001) Br. J. Cancer , vol.85 , pp. 1175-1184
    • Ding, S.1    Chamberlain, M.2    McLaren, A.3    Goh, L.4    Duncan, I.5    Wolf, C.R.6
  • 33
    • 0032104059 scopus 로고    scopus 로고
    • Apoptosis is induced in glioma cells by antisense oligonucleotides to protein kinase C alpha and is enhanced by cycloheximide
    • Dooley N.P., Baltuch G.H., Groome N., Villemure J.G., and Yong V.W. Apoptosis is induced in glioma cells by antisense oligonucleotides to protein kinase C alpha and is enhanced by cycloheximide Neuroreport 9 1998 1727 1733
    • (1998) Neuroreport , vol.9 , pp. 1727-1733
    • Dooley, N.P.1    Baltuch, G.H.2    Groome, N.3    Villemure, J.G.4    Yong, V.W.5
  • 34
    • 0032585532 scopus 로고    scopus 로고
    • Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1)
    • Dutil E.M., Toker A., and Newton A.C. Regulation of conventional protein kinase C isozymes by phosphoinositide-dependent kinase 1 (PDK-1) Curr. Biol. 8 1998 1366 1375
    • (1998) Curr. Biol. , vol.8 , pp. 1366-1375
    • Dutil, E.M.1    Toker, A.2    Newton, A.C.3
  • 35
  • 38
    • 0001550821 scopus 로고    scopus 로고
    • Activation of MDR1 transcription by ATRA in neuroblastoma cells is mediated by a complex interplay of multiple Sp family members
    • Friedman D., Thayer S., and Scotto K.W. Activation of MDR1 transcription by ATRA in neuroblastoma cells is mediated by a complex interplay of multiple Sp family members Proc. Amer. Assoc. Cancer Res. 41 1999 666
    • (1999) Proc. Amer. Assoc. Cancer Res. , vol.41 , pp. 666
    • Friedman, D.1    Thayer, S.2    Scotto, K.W.3
  • 39
    • 0032969236 scopus 로고    scopus 로고
    • Methylation analysis of the human multidrug resistance 1 gene in normal and leukemic hematopoietic cells
    • Fryxell K.B., McGee S.B., Simoneaux D.K., Willman C.L., and Cornwell M.M. Methylation analysis of the human multidrug resistance 1 gene in normal and leukemic hematopoietic cells Leukemia 13 1999 910 917
    • (1999) Leukemia , vol.13 , pp. 910-917
    • Fryxell, K.B.1    McGee, S.B.2    Simoneaux, D.K.3    Willman, C.L.4    Cornwell, M.M.5
  • 41
    • 0342656954 scopus 로고    scopus 로고
    • Regulation of RANTES chemokine gene expression requires cooperativity between NF-κB and IFN-regulatory factor transcription factors
    • Genin P., Algarte M., Roof P., Lin R., and Hiscott J. Regulation of RANTES chemokine gene expression requires cooperativity between NF-κB and IFN-regulatory factor transcription factors J.Immunol. 164 2000 5352 5361
    • (2000) J.Immunol. , vol.164 , pp. 5352-5361
    • Genin, P.1    Algarte, M.2    Roof, P.3    Lin, R.4    Hiscott, J.5
  • 42
    • 0347407794 scopus 로고    scopus 로고
    • Akt in prostate cancer: Possible role in androgen-independence
    • Ghosh P.M., Malik S., Bedolla R., and Kreisberg J.I. Akt in prostate cancer: Possible role in androgen-independence Curr. Drug Metab. 4 2003 487 496
    • (2003) Curr. Drug Metab. , vol.4 , pp. 487-496
    • Ghosh, P.M.1    Malik, S.2    Bedolla, R.3    Kreisberg, J.I.4
  • 43
    • 0027232067 scopus 로고
    • NF-kappa B and Rel: Participants in a multiform transcriptional regulatory system
    • Grilli M., Chiu J.J.-S., and Lenardo M.J. NF-kappa B and Rel: Participants in a multiform transcriptional regulatory system Int. Rev. Cytol. 143 1993 1 62
    • (1993) Int. Rev. Cytol. , vol.143 , pp. 1-62
    • Grilli, M.1    Chiu, J.J.-S.2    Lenardo, M.J.3
  • 44
    • 0024541436 scopus 로고
    • Functions of sphingolipids and sphingolipid breakdown products in cellular regulation
    • Hannun Y.Q., and Bell R.M. Functions of sphingolipids and sphingolipid breakdown products in cellular regulation Science 243 1989 500 507
    • (1989) Science , vol.243 , pp. 500-507
    • Hannun, Y.Q.1    Bell, R.M.2
  • 45
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • Hendrich B., and Bird A. Identification and characterization of a family of mammalian methyl-CpG binding proteins Mol. Cell. Biol. 18 1998 6538 6547
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 46
    • 0034055278 scopus 로고    scopus 로고
    • Mammalian methyltransferases and methyl-CpG-binding domains: Proteins involved in DNA methylation
    • Hendrich B., and Bird A. Mammalian methyltransferases and methyl-CpG-binding domains: Proteins involved in DNA methylation Curr. Top. Microbiol. Immunol. 249 2000 55 74
    • (2000) Curr. Top. Microbiol. Immunol. , vol.249 , pp. 55-74
    • Hendrich, B.1    Bird, A.2
  • 47
    • 0034095131 scopus 로고    scopus 로고
    • Promoter-region hypermethylation and gene silencing in human cancer
    • Herman J.G., and Baylin S.B. Promoter-region hypermethylation and gene silencing in human cancer Curr. Top. Microbiol. Immunol. 249 2000 35 54
    • (2000) Curr. Top. Microbiol. Immunol. , vol.249 , pp. 35-54
    • Herman, J.G.1    Baylin, S.B.2
  • 51
    • 1542619344 scopus 로고    scopus 로고
    • Protein kinase C isozymes as potential targets for anticancer therapy
    • Hofmann J. Protein kinase C isozymes as potential targets for anticancer therapy Curr. Cancer Drug Targets 4 2004 125 146
    • (2004) Curr. Cancer Drug Targets , vol.4 , pp. 125-146
    • Hofmann, J.1
  • 52
    • 0346328321 scopus 로고    scopus 로고
    • Antitumor effect of a novel nuclear factor-kappa B activation inhibitor in bladder cancer cells
    • Horiguchi Y., Kuroda K., Nakashima J., Murai M., and Umezawa K. Antitumor effect of a novel nuclear factor-kappa B activation inhibitor in bladder cancer cells Expert Rev. Anticancer Ther. 3 2003 793 798
    • (2003) Expert Rev. Anticancer Ther. , vol.3 , pp. 793-798
    • Horiguchi, Y.1    Kuroda, K.2    Nakashima, J.3    Murai, M.4    Umezawa, K.5
  • 54
    • 3042737429 scopus 로고    scopus 로고
    • Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inaclivation of NF-kappa B and inhibition of Bcl-xl expression
    • Huerta-Yepez S., Vega M., Jazirehi A., Garban H., Hongo F., Cheng G., and Bonavida B. Nitric oxide sensitizes prostate carcinoma cell lines to TRAIL-mediated apoptosis via inaclivation of NF-kappa B and inhibition of Bcl-xl expression Oncogene 23 2004 4993 5003
    • (2004) Oncogene , vol.23 , pp. 4993-5003
    • Huerta-yepez, S.1    Vega, M.2    Jazirehi, A.3    Garban, H.4    Hongo, F.5    Cheng, G.6    Bonavida, B.7
  • 55
    • 0027322679 scopus 로고
    • Protein kinase C isozymes: Divergence in signal transduction?
    • Hug H., and Sarre T.F. Protein kinase C isozymes: Divergence in signal transduction? Biochem. J. 291 1993 329 342
    • (1993) Biochem. J. , vol.291 , pp. 329-342
    • Hug, H.1    Sarre, T.F.2
  • 56
    • 0028928140 scopus 로고
    • Differential utilization of multiple transcription start points accompanies the overexpression of the P-glycoprotein-encoding gene in Chinese hamster lung cells
    • Ince T., and Scotto K.W. Differential utilization of multiple transcription start points accompanies the overexpression of the P-glycoprotein-encoding gene in Chinese hamster lung cells Gene 156 1995 287 290
    • (1995) Gene , vol.156 , pp. 287-290
    • Ince, T.1    Scotto, K.W.2
  • 57
    • 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., and 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
  • 58
    • 0036087691 scopus 로고    scopus 로고
    • MAP kinases contribute to IL-8 secretion by intestinal epithelial cells via a posttranscriptional mechanism
    • Jijon H.B., Panenka W.J., Madsen K.L., and Parsons H.G. MAP kinases contribute to IL-8 secretion by intestinal epithelial cells via a posttranscriptional mechanism Am. J. Physiol. Cell Physiol. 283 2002 C31 C41
    • (2002) Am. J. Physiol. Cell Physiol. , vol.283
    • Jijon, H.B.1    Panenka, W.J.2    Madsen, K.L.3    Parsons, H.G.4
  • 59
    • 0031861729 scopus 로고    scopus 로고
    • Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y
    • Jin S., and Scotto K.W. Transcriptional regulation of the MDR1 gene by histone acetyltransferase and deacetylase is mediated by NF-Y Mol. Cell. Biol. 18 1998 4377 4384
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4377-4384
    • Jin, S.1    Scotto, K.W.2
  • 60
    • 6344233096 scopus 로고    scopus 로고
    • Oxidative stress and the JNK pathway as a potential therapeutic target for diabetes
    • Kaneto H., Kawamori D., Nakatani Y., Gorogawa S., and Matsuoka T.A. Oxidative stress and the JNK pathway as a potential therapeutic target for diabetes Drug News Perspect. 17 2004 447 453
    • (2004) Drug News Perspect. , vol.17 , pp. 447-453
    • Kaneto, H.1    Kawamori, D.2    Nakatani, Y.3    Gorogawa, S.4    Matsuoka, T.A.5
  • 62
    • 0029032249 scopus 로고
    • The regulation of AP-1 activity by mitogen-activated protein kinases
    • Karin M. The regulation of AP-1 activity by mitogen-activated protein kinases J.Biol. Chem. 270 1995 16483 16486
    • (1995) J.Biol. Chem. , vol.270 , pp. 16483-16486
    • Karin, M.1
  • 63
    • 0033595893 scopus 로고    scopus 로고
    • How NFκB is activated: The role of IκB kinase (IKK) complex
    • Karin M. How NFκB is activated: The role of IκB kinase (IKK) complex Oncogene 18 1999 6867 6874
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 64
    • 1642543836 scopus 로고    scopus 로고
    • A 'molecular switchboard'-covalent modifications to proteins and their impact on transcription
    • Khidekel N., and Hsieh-Wilson L.C. A 'molecular switchboard'-covalent modifications to proteins and their impact on transcription Org. Biomol. Chem. 2 2004 1 7
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1-7
    • Khidekel, N.1    Hsieh-wilson, L.C.2
  • 65
    • 0029071790 scopus 로고
    • Chloromethyl ketones block induction of nitric oxide synthase in murine macrophages by preventing activation of nuclear factor-κB
    • Kim H., Lee H.S., Chang K.T., Ko T.H., Baek K.J., and Kwon N.S. Chloromethyl ketones block induction of nitric oxide synthase in murine macrophages by preventing activation of nuclear factor-κB J. Immunol. 154 1995 4741 4748
    • (1995) J. Immunol. , vol.154 , pp. 4741-4748
    • Kim, H.1    Lee, H.S.2    Chang, K.T.3    Ko, T.H.4    Baek, K.J.5    Kwon, N.S.6
  • 67
    • 0031609164 scopus 로고    scopus 로고
    • Activation of the LRP (lung resistance-related protein) gene by short-term exposure of human leukemia cells to phorbol ester and cytarabine
    • Komarov P., Shtil A., Holian O., Tee L., Buckingham L., Mechetner E., Roninson I., and Coon J. Activation of the LRP (lung resistance-related protein) gene by short-term exposure of human leukemia cells to phorbol ester and cytarabine Oncology Res. 10 1998 185 192
    • (1998) Oncology Res. , vol.10 , pp. 185-192
    • Komarov, P.1    Shtil, A.2    Holian, O.3    Tee, L.4    Buckingham, L.5    Mechetner, E.6    Roninson, I.7    Coon, J.8
  • 68
    • 0028167846 scopus 로고
    • Inhibition of NFκB by sodium salicylate and aspirin
    • Kopp E., and Ghosh S. Inhibition of NFκB by sodium salicylate and aspirin Science 265 1994 956 959
    • (1994) Science , vol.265 , pp. 956-959
    • Kopp, E.1    Ghosh, S.2
  • 69
    • 0036878551 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription-3 and phosphatidylinositol-3 kinase as coordinate regulators of melanoma cell response to glucocorticoid hormones
    • Krasil'nikov M.A., and Shatskaya V.A. Signal transducer and activator of transcription-3 and phosphatidylinositol-3 kinase as coordinate regulators of melanoma cell response to glucocorticoid hormones J. Steroid Biochem. Mol. Biol. 82 2002 369 376
    • (2002) J. Steroid Biochem. Mol. Biol. , vol.82 , pp. 369-376
    • Krasil'Nikov, M.A.1    Shatskaya, V.A.2
  • 70
    • 0029902680 scopus 로고    scopus 로고
    • Alterations in mRNA stability during rat liver regeneration
    • Kren B.T., Trembley J.H., and Steer C.J. Alterations in mRNA stability during rat liver regeneration Am. J. Physiol. 270 1996 G763 G777
    • (1996) Am. J. Physiol. , vol.270
    • Kren, B.T.1    Trembley, J.H.2    Steer, C.J.3
  • 71
    • 0037150228 scopus 로고    scopus 로고
    • Induction of human MDR1 gene expression by 2-acetylaminofluorene is mediated by effectors of the phosphoinositide 3-kinase pathway that activate NF-kappaB signaling
    • Kuo M.T., Liu Z., Wei Y., Lin-Lee Y.C., Tatebe S., Mills G.B., and Unate H. Induction of human MDR1 gene expression by 2-acetylaminofluorene is mediated by effectors of the phosphoinositide 3-kinase pathway that activate NF-kappaB signaling Oncogene 21 2002 1945 1954
    • (2002) Oncogene , vol.21 , pp. 1945-1954
    • Kuo, M.T.1    Liu, Z.2    Wei, Y.3    Lin-lee, Y.C.4    Tatebe, S.5    Mills, G.B.6    Unate, H.7
  • 72
    • 0033564370 scopus 로고    scopus 로고
    • Association of 5′CpG demethylation and altered chromatin structure in the promoter region with transcriptional activation of the multidrug resistance 1 gene in human cancer cells
    • Kusaba H., Nakayama M., Harada T., Nomoto M., Kohno K., Kuwano M., and Wada M. Association of 5′CpG demethylation and altered chromatin structure in the promoter region with transcriptional activation of the multidrug resistance 1 gene in human cancer cells Eur. J. Biochem. 262 1999 924 932
    • (1999) Eur. J. Biochem. , vol.262 , pp. 924-932
    • Kusaba, H.1    Nakayama, M.2    Harada, T.3    Nomoto, M.4    Kohno, K.5    Kuwano, M.6    Wada, M.7
  • 73
    • 0042844654 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase inhibitor anthra(1,9-cd)pyrazol-6(2H)-one reduces inducible nitric-oxide synthase expression by destabilizing mRNA in activated macrophages
    • Lahti A., Jalonen U., Kankaanranta H., and Moilanen E. c-Jun NH2-terminal kinase inhibitor anthra(1,9-cd)pyrazol-6(2H)-one reduces inducible nitric-oxide synthase expression by destabilizing mRNA in activated macrophages Mol. Pharmacol. 64 2003 308 315
    • (2003) Mol. Pharmacol. , vol.64 , pp. 308-315
    • Lahti, A.1    Jalonen, U.2    Kankaanranta, H.3    Moilanen, E.4
  • 74
    • 0242610852 scopus 로고    scopus 로고
    • Glucose depletion enhances P-glycoprotein expression in hepatoma cells: Role of endoplasmic reticulum stress response
    • Ledoux S., Yang R., Friedlander G., and Laouari D. Glucose depletion enhances P-glycoprotein expression in hepatoma cells: Role of endoplasmic reticulum stress response Cancer Res. 63 2003 7284 7290
    • (2003) Cancer Res. , vol.63 , pp. 7284-7290
    • Ledoux, S.1    Yang, R.2    Friedlander, G.3    Laouari, D.4
  • 75
    • 0028966586 scopus 로고
    • Overexpression of the class II P-glycoprotein gene in primary rat hepatocyte culture: Evidence for increased mRNA stability
    • Lee C.H., Bradley G., and Ling V. Overexpression of the class II P-glycoprotein gene in primary rat hepatocyte culture: Evidence for increased mRNA stability Cell Growth Diff. 6 1995 347 354
    • (1995) Cell Growth Diff. , vol.6 , pp. 347-354
    • Lee, C.H.1    Bradley, G.2    Ling, V.3
  • 76
    • 0032566691 scopus 로고    scopus 로고
    • Protein kinase C isotypes controlled by phosphoinositide-3-kinase through the protein kinase PDK1
    • Le Good A.J., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P., and Parker P.J. Protein kinase C isotypes controlled by phosphoinositide-3-kinase through the protein kinase PDK1 Science 281 1998 2042 2045
    • (1998) Science , vol.281 , pp. 2042-2045
    • Le Good, A.J.1    Ziegler, W.H.2    Parekh, D.B.3    Alessi, D.R.4    Cohen, P.5    Parker, P.J.6
  • 77
    • 0025343895 scopus 로고
    • Activation of interleukin-6 gene expression through the NFκB transcription factor
    • Libermann T.A., and Baltimore D. Activation of interleukin-6 gene expression through the NFκB transcription factor Mol.Cell. Biol. 10 1990 2327 2334
    • (1990) Mol.Cell. Biol. , vol.10 , pp. 2327-2334
    • Libermann, T.A.1    Baltimore, D.2
  • 79
    • 0025386379 scopus 로고
    • Regulation of the multidrug resistance gene in regenerating rat liver
    • Marino P.A., Gottesman M.M., and Pastan I. Regulation of the multidrug resistance gene in regenerating rat liver Cell Growth Diff. 1 1990 57 62
    • (1990) Cell Growth Diff. , vol.1 , pp. 57-62
    • Marino, P.A.1    Gottesman, M.M.2    Pastan, I.3
  • 80
    • 0027483327 scopus 로고
    • Identification of 5′ and 3′ sequences involved in the regulation of transcription of the human mdr1 gene in vivo
    • Madden M.J., Morrow C.S., Nakagawa M., Goldsmith M.E., Fairchild C.R., and Cowan K.H. Identification of 5′ and 3′ sequences involved in the regulation of transcription of the human mdr1 gene in vivo J. Biol. Chem. 268 1993 8290 8297
    • (1993) J. Biol. Chem. , vol.268 , pp. 8290-8297
    • Madden, M.J.1    Morrow, C.S.2    Nakagawa, M.3    Goldsmith, M.E.4    Fairchild, C.R.5    Cowan, K.H.6
  • 81
    • 0028820126 scopus 로고
    • 12-O-tetradecanoylphorbol-13-acetate activation of the MDR1 promoter is mediated by EGR1
    • McCoy C., Smith D.E., and Cornwell M.M. 12-O-tetradecanoylphorbol-13- acetate activation of the MDR1 promoter is mediated by EGR1 Mol. Cell. Biol. 15 1995 6100 6108
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6100-6108
    • McCoy, C.1    Smith, D.E.2    Cornwell, M.M.3
  • 82
    • 0033021651 scopus 로고    scopus 로고
    • The Wilms' tumor suppressor, WT1, inhibits 12-O-tetradecanoylphorbol-13- acetate activation of the multidrug resistance-1 promoter
    • McCoy C., McGee S.B., and Cornwell M.M. The Wilms' tumor suppressor, WT1, inhibits 12-O-tetradecanoylphorbol-13-acetate activation of the multidrug resistance-1 promoter Cell Growth Diff. 10 1999 377 386
    • (1999) Cell Growth Diff. , vol.10 , pp. 377-386
    • McCoy, C.1    McGee, S.B.2    Cornwell, M.M.3
  • 84
    • 0033216629 scopus 로고    scopus 로고
    • NF-κB as a primary regulator of the stress response
    • Mercurio F., and Manning A.M. NF-κB as a primary regulator of the stress response Oncogene 18 1999 6163 6171
    • (1999) Oncogene , vol.18 , pp. 6163-6171
    • Mercurio, F.1    Manning, A.M.2
  • 85
    • 0024455628 scopus 로고
    • Modulation of the expression of a multidrug resistance gene (mdr1/P-glycoprotein) by differentiating agents
    • Mickley L.A., Bates S.E., Richert N.D., Currier S., Tanaka S., Foss F., Rosen N., and Fojo A.T. Modulation of the expression of a multidrug resistance gene (mdr1/P-glycoprotein) by differentiating agents J. Biol. Chem. 264 1989 18031 18040
    • (1989) J. Biol. Chem. , vol.264 , pp. 18031-18040
    • Mickley, L.A.1    Bates, S.E.2    Richert, N.D.3    Currier, S.4    Tanaka, S.5    Foss, F.6    Rosen, N.7    Fojo, A.T.8
  • 86
    • 0031964645 scopus 로고    scopus 로고
    • Anchoring proteins for protein kinase C: A means for isozyme selectivity
    • Mochly-Rosen D., and Gordon A.S. Anchoring proteins for protein kinase C: A means for isozyme selectivity FASEB J. 12 1998 35 42
    • (1998) FASEB J. , vol.12 , pp. 35-42
    • Mochly-rosen, D.1    Gordon, A.S.2
  • 87
    • 0141781040 scopus 로고    scopus 로고
    • Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor
    • Monje P., Marinissen M.J., and Gutkind J.S. Phosphorylation of the carboxyl-terminal transactivation domain of c-Fos by extracellular signal-regulated kinase mediates the transcriptional activation of AP-1 and cellular transformation induced by platelet-derived growth factor Mol. Cell. Biol. 23 2003 7030 7043
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7030-7043
    • Monje, P.1    Marinissen, M.J.2    Gutkind, J.S.3
  • 88
    • 0032403478 scopus 로고    scopus 로고
    • Hypomethylation status of CpG site at the promoter region and overexpression of the human MDR1 gene in acute myeloid leukemias
    • Nakayama M., Wada M., Harada T., Nagayama J., Kusaba H., Ohshima K., Kozuru M., Komatsu H., Ueda R., and Kuwano M. Hypomethylation status of CpG site at the promoter region and overexpression of the human MDR1 gene in acute myeloid leukemias Blood 92 1998 4296 4307
    • (1998) Blood , vol.92 , pp. 4296-4307
    • Nakayama, M.1    Wada, M.2    Harada, T.3    Nagayama, J.4    Kusaba, H.5    Ohshima, K.6    Kozuru, M.7    Komatsu, H.8    Ueda, R.9    Kuwano, M.10
  • 89
    • 0028811653 scopus 로고
    • Protein kinase C: Structure, function, and regulation
    • Newton A.C. Protein kinase C: Structure, function, and regulation J. Biol. Chem. 270 1995 28495 28498
    • (1995) J. Biol. Chem. , vol.270 , pp. 28495-28498
    • Newton, A.C.1
  • 90
    • 0023833803 scopus 로고
    • Use of fluorescent dyes as molecular probes for the study of multidrug resistance
    • Neyfakh A.A. Use of fluorescent dyes as molecular probes for the study of multidrug resistance Exp. Cell Res. 174 1988 168 176
    • (1988) Exp. Cell Res. , vol.174 , pp. 168-176
    • Neyfakh, A.A.1
  • 91
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C Science 258 1992 607 614
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 92
    • 0029610692 scopus 로고
    • Lipid mediators and protein kinase C for intracellular signaling
    • Nishizuka Y., and Nakamura S. Lipid mediators and protein kinase C for intracellular signaling Clin. Exp. Pharmacol. Physiol. 22 Suppl. 1 1995 S202 S203
    • (1995) Clin. Exp. Pharmacol. Physiol. , vol.22 , Issue.SUPPL. 1
    • Nishizuka, Y.1    Nakamura, S.2
  • 93
    • 0032582525 scopus 로고    scopus 로고
    • Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals
    • Oancea E., and Meyer T. Protein kinase C as a molecular machine for decoding calcium and diacylglycerol signals Cell 95 1998 307 318
    • (1998) Cell , vol.95 , pp. 307-318
    • Oancea, E.1    Meyer, T.2
  • 94
    • 0029450955 scopus 로고
    • The tumor promoter receptor protein kinase C: A novel target for chemoprevention and therapy of human colon cancer
    • O'Brian C.A., Ward N.E., Gravitt K.R., and Gupta K.P. The tumor promoter receptor protein kinase C: A novel target for chemoprevention and therapy of human colon cancer Prog. Clin.Biol. Res. 391 1995 117 120
    • (1995) Prog. Clin.Biol. Res. , vol.391 , pp. 117-120
    • O'Brian, C.A.1    Ward, N.E.2    Gravitt, K.R.3    Gupta, K.P.4
  • 96
    • 0033573850 scopus 로고    scopus 로고
    • Negative regulation of MDR1 promoter activity in MCF-7, but not in multidrug resistant MCF-7/Adr, cells by cross-coupled NFκB/p65 and c-Fos transcription factors and their interaction with the CAAT region
    • Ogretmen B., and Safa A.R. Negative regulation of MDR1 promoter activity in MCF-7, but not in multidrug resistant MCF-7/Adr, cells by cross-coupled NFκB/p65 and c-Fos transcription factors and their interaction with the CAAT region Biochemistry 38 1999 2189 2199
    • (1999) Biochemistry , vol.38 , pp. 2189-2199
    • Ogretmen, B.1    Safa, A.R.2
  • 97
    • 0034635186 scopus 로고    scopus 로고
    • Identification and characterization of the MDR1 promoter-enhancing factor 1 (MEF1) in the multidrug resistant HL60/VCR human acute myeloid leukemia cell line
    • Ogretmen B., and Safa A.R. Identification and characterization of the MDR1 promoter-enhancing factor 1 (MEF1) in the multidrug resistant HL60/VCR human acute myeloid leukemia cell line Biochemistry 39 2000 194 204
    • (2000) Biochemistry , vol.39 , pp. 194-204
    • Ogretmen, B.1    Safa, A.R.2
  • 98
    • 0031455589 scopus 로고    scopus 로고
    • Caveolin interaction with protein kinase C. Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide
    • Oka N., Yamamoto M., Schwenke C., Kawabe J., Ebina T., Ohno S., Couet J., Lisanti M.P., and Ishikawa Y. Caveolin interaction with protein kinase C. Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide J. Biol. Chem. 272 1997 33416 33421
    • (1997) J. Biol. Chem. , vol.272 , pp. 33416-33421
    • Oka, N.1    Yamamoto, M.2    Schwenke, C.3    Kawabe, J.4    Ebina, T.5    Ohno, S.6    Couet, J.7    Lisanti, M.P.8    Ishikawa, Y.9
  • 99
    • 0029851730 scopus 로고    scopus 로고
    • Role of the stress-activated/c-Jun NH2-terminal protein kinase pathway in the cellular response to adriamycin and other chemotherapeutic drugs
    • Osborn M.T., and Chambers T.C. Role of the stress-activated/c-Jun NH2-terminal protein kinase pathway in the cellular response to adriamycin and other chemotherapeutic drugs J. Biol Chem. 271 1996 30950 30955
    • (1996) J. Biol Chem. , vol.271 , pp. 30950-30955
    • Osborn, M.T.1    Chambers, T.C.2
  • 100
    • 0033554588 scopus 로고    scopus 로고
    • Phorbol ester induced MDR1 expression in K562 cells occurs independently of mitogen-activated protein kinase signaling pathways
    • Osborn M.T., Berry A., Ruberu M.S., Ning B., Bell L.M., and Chambers T.C. Phorbol ester induced MDR1 expression in K562 cells occurs independently of mitogen-activated protein kinase signaling pathways Oncogene 18 1999 5756 5764
    • (1999) Oncogene , vol.18 , pp. 5756-5764
    • Osborn, M.T.1    Berry, A.2    Ruberu, M.S.3    Ning, B.4    Bell, L.M.5    Chambers, T.C.6
  • 101
    • 2442464889 scopus 로고    scopus 로고
    • Apoptosis defects and chemotherapy resistance: Molecular interaction maps and networks
    • Pommier Y., Sordet O., Antony S., Hayward R.L., and Kohn K.W. Apoptosis defects and chemotherapy resistance: Molecular interaction maps and networks Oncogene 23 2004 2934 2949
    • (2004) Oncogene , vol.23 , pp. 2934-2949
    • Pommier, Y.1    Sordet, O.2    Antony, S.3    Hayward, R.L.4    Kohn, K.W.5
  • 102
    • 0033546734 scopus 로고    scopus 로고
    • The AU-rich 3′-untranslated region of human MDR1 mRNA is an inefficient mRNA destabilizer
    • Prokipcak R.D., Raouf A., and Lee C. The AU-rich 3′-untranslated region of human MDR1 mRNA is an inefficient mRNA destabilizer Biochem. Biophys. Res. Commun. 261 1999 627 634
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 627-634
    • Prokipcak, R.D.1    Raouf, A.2    Lee, C.3
  • 103
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression
    • Rahman I., Marwick J., and Kirkham P. Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-kappaB and pro-inflammatory gene expression Biochem. Pharrnacol. 68 2004 1255 1267
    • (2004) Biochem. Pharrnacol. , vol.68 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 104
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • Rao R.V., Ellerby H.M., and Bredesen D.E. Coupling endoplasmic reticulum stress to the cell death program Cell Deat Diff. 11 2004 372 380
    • (2004) Cell Deat Diff. , vol.11 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 105
    • 8544221913 scopus 로고    scopus 로고
    • Inhibition of extracellular-signal regulated kinases 1/2 is required for apoptosis of human colon cancer cells in vitro by sulindac metabolites
    • Rice P.L., Beard K.S., Driggers L.J., and Ahnen D.J. Inhibition of extracellular-signal regulated kinases 1/2 is required for apoptosis of human colon cancer cells in vitro by sulindac metabolites Cancer Res. 64 2004 8148 8151
    • (2004) Cancer Res. , vol.64 , pp. 8148-8151
    • Rice, P.L.1    Beard, K.S.2    Driggers, L.J.3    Ahnen, D.J.4
  • 109
    • 0344667552 scopus 로고    scopus 로고
    • NF-kappaB activation pathways induced by T cell costimulation
    • Schmitz M.L., Bacher S., and Dienz O. NF-kappaB activation pathways induced by T cell costimulation FASEB J. 17 2003 2187 2193
    • (2003) FASEB J. , vol.17 , pp. 2187-2193
    • Schmitz, M.L.1    Bacher, S.2    Dienz, O.3
  • 110
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor κb activation in intact cells
    • Schreck R., Meier B., Mannel D.N., Droge W., and Bauerle P.A. Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells J. Exp. Med. 175 1992 1181 1194
    • (1992) J. Exp. Med. , vol.175 , pp. 1181-1194
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Bauerle, P.A.5
  • 111
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G., and Kamen R. A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation Cell 46 1986 659 667
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 112
    • 0032524977 scopus 로고    scopus 로고
    • Induction of apoptosis in glioblastoma cells by inhibition of protein kinase C and its association with the rapid accumulation of p53 and induction of the insulin-like growth factor-1-binding protein 3
    • Shen L., and Glazer R.I. Induction of apoptosis in glioblastoma cells by inhibition of protein kinase C and its association with the rapid accumulation of p53 and induction of the insulin-like growth factor-1-binding protein 3 Biochem. Pharmacol. 55 1998 1711 1719
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 1711-1719
    • Shen, L.1    Glazer, R.I.2
  • 114
    • 29244433921 scopus 로고    scopus 로고
    • Dissection of signal transduction pathways regulating the induction of MDR1 gene expression in human leukemia cells
    • Stevenson WA
    • Shtil A.A., and Roninson I.B. Dissection of signal transduction pathways regulating the induction of MDR1 gene expression in human leukemia cells AACR Special Conf. 'Inducible Genomic Responses,' 1996 Stevenson WA, B-14.
    • (1996) AACR Special Conf. 'Inducible Genomic Responses,'
    • Shtil, A.A.1    Roninson, I.B.2
  • 115
    • 0001554639 scopus 로고    scopus 로고
    • Differential regulation of mitogen-activated protein kinases by microtubule-binding agents in human breast cancer cells
    • Shtil A.A., Mandlekar S., Yu R., Walter R., Hagen K., Roninson I., Tan T.-H., and Kong T. Differential regulation of mitogen-activated protein kinases by microtubule-binding agents in human breast cancer cells Oncogene 18 1999 377 384
    • (1999) Oncogene , vol.18 , pp. 377-384
    • Shtil, A.A.1    Mandlekar, S.2    Yu, R.3    Walter, R.4    Hagen, K.5    Roninson, I.6    Tan, T.-H.7    Kong, T.8
  • 116
    • 0034241420 scopus 로고    scopus 로고
    • Overexpression of the MDR1 gene is associated with a decreased mitochondrial transmembrane potential in K562 human leukemia cells selected for P-glycoprotein-mediated multidrug resistance
    • Shtil A.A., Grinchuk T.M., Tee L., Mechetner E.B., and Ignatova T.N. Overexpression of the MDR1 gene is associated with a decreased mitochondrial transmembrane potential in K562 human leukemia cells selected for P-glycoprotein-mediated multidrug resistance Int. J. Oncol. 17 2000 387 392
    • (2000) Int. J. Oncol. , vol.17 , pp. 387-392
    • Shtil, A.A.1    Grinchuk, T.M.2    Tee, L.3    Mechetner, E.B.4    Ignatova, T.N.5
  • 117
    • 0035146570 scopus 로고    scopus 로고
    • Ceramide inhibits protein kinase C (PKC) activity and activates the MDR1 gene in human leukemia cells: Evidence for a PKC-independent mechanism of up-regulation of multidrug resistance
    • Shtil A.A., Ktitorova O.V., Kakpakova E.S., and Holian O. Ceramide inhibits protein kinase C (PKC) activity and activates the MDR1 gene in human leukemia cells: Evidence for a PKC-independent mechanism of up-regulation of multidrug resistance Leuk. Lymphoma 40 2000 191 195
    • (2000) Leuk. Lymphoma , vol.40 , pp. 191-195
    • Shtil, A.A.1    Ktitorova, O.V.2    Kakpakova, E.S.3    Holian, O.4
  • 118
    • 0035031007 scopus 로고    scopus 로고
    • Signal transduction pathways and transcriptional mechanisms as targets for prevention of emergence of multidrug resistance in human cancer cells
    • Shtil A.A. Signal transduction pathways and transcriptional mechanisms as targets for prevention of emergence of multidrug resistance in human cancer cells Curr. Drug Targets 2 2001 57 77
    • (2001) Curr. Drug Targets , vol.2 , pp. 57-77
    • Shtil, A.A.1
  • 119
    • 0036227439 scopus 로고    scopus 로고
    • Multifactorial drug resistance: P-glycoprotein on the apex of the pyramid
    • Shtil A.A. Multifactorial drug resistance: P-glycoprotein on the apex of the pyramid J. Hematother. Stem Cell Res. 11 2002 437 439
    • (2002) J. Hematother. Stem Cell Res. , vol.11 , pp. 437-439
    • Shtil, A.A.1
  • 120
    • 2442424073 scopus 로고    scopus 로고
    • Suppression of constitutive and tumor necrosis factor alpha-induced nuclear factor (NF)- kappaB activation and induction of apoptosis by apigenin in human prostate carcinoma PC-3 cells: Correlation with down-regulation of NF-kappaB-responsive genes
    • Shukla S., and Gupta S. Suppression of constitutive and tumor necrosis factor alpha-induced nuclear factor (NF)- kappaB activation and induction of apoptosis by apigenin in human prostate carcinoma PC-3 cells: Correlation with down-regulation of NF-kappaB-responsive genes Clin. Cancer Res. 10 2004 3169 3178
    • (2004) Clin. Cancer Res. , vol.10 , pp. 3169-3178
    • Shukla, S.1    Gupta, S.2
  • 122
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Stokoe D., Macdonald S., Cadwallader K., Symons M., and Hancock J.F. Activation of Raf as a result of recruitment to the plasma membrane Science 264 1994 1463 1467
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    MacDonald, S.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 123
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications Nature 403 2000 41 45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 124
    • 0032030770 scopus 로고    scopus 로고
    • Histone acetylation and transcriptional regulatory mechanisms
    • Struhl K. Histone acetylation and transcriptional regulatory mechanisms Genes Dev. 12 1998 599 606
    • (1998) Genes Dev. , vol.12 , pp. 599-606
    • Struhl, K.1
  • 125
    • 3042658499 scopus 로고    scopus 로고
    • DNA demethylation and cancer: Therapeutic implications
    • Szyf M., Pakneshan P., and Rabbani S.A. DNA demethylation and cancer: Therapeutic implications Cancer Lett. 211 2004 133 143
    • (2004) Cancer Lett. , vol.211 , pp. 133-143
    • Szyf, M.1    Pakneshan, P.2    Rabbani, S.A.3
  • 127
    • 0141680278 scopus 로고    scopus 로고
    • Molecular target-based cancer therapy: Tyrosine kinase inhibitors
    • Tamura K., and Fukuoka M. Molecular target-based cancer therapy: Tyrosine kinase inhibitors Int. J. Clin. Oncol. 8 2003 207 211
    • (2003) Int. J. Clin. Oncol. , vol.8 , pp. 207-211
    • Tamura, K.1    Fukuoka, M.2
  • 128
    • 3843069106 scopus 로고    scopus 로고
    • Androgen receptor: A key molecule in the progression of prostate cancer to hormone independence
    • Taplin M.E., and Balk S.P. Androgen receptor: A key molecule in the progression of prostate cancer to hormone independence J. Cell. Biochem. 91 2004 483 490
    • (2004) J. Cell. Biochem. , vol.91 , pp. 483-490
    • Taplin, M.E.1    Balk, S.P.2
  • 129
    • 0023095571 scopus 로고
    • The calcium mobilizing tumor promoting agent, thapsigargin elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. a possible mechanism of action for the tumor promotion
    • Thastrup O., Foder B., and Scharff O. The calcium mobilizing tumor promoting agent, thapsigargin elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. A possible mechanism of action for the tumor promotion Biochem. Biophys. Res. Commun. 142 1987 654 660
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 654-660
    • Thastrup, O.1    Foder, B.2    Scharff, O.3
  • 130
    • 0034695660 scopus 로고    scopus 로고
    • Up-regulation of multidrug resistance P-glycoprotein via nuclear factor -κB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis
    • Thévenod F., Friedmann J.M., Katsen A.D., and Hauser I.A. Up-regulation of multidrug resistance P-glycoprotein via nuclear factor -κB activation protects kidney proximal tubule cells from cadmium- and reactive oxygen species-induced apoptosis J. Biol. Chem. 275 2000 1887 1896
    • (2000) J. Biol. Chem. , vol.275 , pp. 1887-1896
    • Thévenod, F.1    Friedmann, J.M.2    Katsen, A.D.3    Hauser, I.A.4
  • 131
    • 0642374221 scopus 로고    scopus 로고
    • The role of glutathione-S-transferase in anti-cancer drug resistance
    • Townsend D.M., and Tew K.D. The role of glutathione-S-transferase in anti-cancer drug resistance Oncogene 22 2003 7369 7375
    • (2003) Oncogene , vol.22 , pp. 7369-7375
    • Townsend, D.M.1    Tew, K.D.2
  • 132
    • 0033556387 scopus 로고    scopus 로고
    • Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation
    • Townsend K.J., Zhou P., Qian L., Bieszczad C.K., Lowrey C.H., Yen A., and Craig R.W. Regulation of MCL1 through a serum response factor/Elk-1-mediated mechanism links expression of a viability-promoting member of the BCL2 family to the induction of hematopoietic cell differentiation J. Biol. Chem. 274 1999 1801 1813
    • (1999) J. Biol. Chem. , vol.274 , pp. 1801-1813
    • Townsend, K.J.1    Zhou, P.2    Qian, L.3    Bieszczad, C.K.4    Lowrey, C.H.5    Yen, A.6    Craig, R.W.7
  • 133
    • 0028148227 scopus 로고
    • A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is bound to NF-κB
    • Traeckner E.B., Wilk S., and Bauerle P.A. A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is bound to NF-κB EMBO J. 13 1994 5433 5441
    • (1994) EMBO J. , vol.13 , pp. 5433-5441
    • Traeckner, E.B.1    Wilk, S.2    Bauerle, P.A.3
  • 134
    • 0000229735 scopus 로고
    • Chromosomal localization in normal human cells and CHO cells of a sequence derived from P-glycoprotein (PGY1)
    • Trent J., Bell D., Willard H., and Ling V. Chromosomal localization in normal human cells and CHO cells of a sequence derived from P-glycoprotein (PGY1) Hum. Gene Mapping 8 1985 761 762
    • (1985) Hum. Gene Mapping , vol.8 , pp. 761-762
    • Trent, J.1    Bell, D.2    Willard, H.3    Ling, V.4
  • 135
    • 6944256675 scopus 로고    scopus 로고
    • Modulation of cellular cholesterol alters P-glycoprotein activity in multidrug-resistant cells
    • Troost J., Lindenmaier H., Haefeli W.E., and Weiss J. Modulation of cellular cholesterol alters P-glycoprotein activity in multidrug-resistant cells Mol. Pharmacol. 66 2004 1332 1339
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1332-1339
    • Troost, J.1    Lindenmaier, H.2    Haefeli, W.E.3    Weiss, J.4
  • 136
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien R.Y. New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures Biochemistry 19 1980 2396 2404
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 137
    • 0027564360 scopus 로고
    • Enhanced expression of the human multidrug resistance 1 gene in response to UV light irradiation
    • Uchiumi T., Kohno K., Tanimura H., Matsuo K., Sato S., Uchida Y., and Kuwano M. Enhanced expression of the human multidrug resistance 1 gene in response to UV light irradiation Cell Growth Diff. 4 1993 147 157
    • (1993) Cell Growth Diff. , vol.4 , pp. 147-157
    • Uchiumi, T.1    Kohno, K.2    Tanimura, H.3    Matsuo, K.4    Sato, S.5    Uchida, Y.6    Kuwano, M.7
  • 139
  • 140
    • 0037206564 scopus 로고    scopus 로고
    • Molecular design and biological activities of NF-kappaB inhibitors
    • Umezawa K., and Chaicharoenpong C. Molecular design and biological activities of NF-kappaB inhibitors Mol. Cells 14 2002 163 167
    • (2002) Mol. Cells , vol.14 , pp. 163-167
    • Umezawa, K.1    Chaicharoenpong, C.2
  • 141
    • 4944237502 scopus 로고    scopus 로고
    • Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence
    • Unni E., Sun S., Nan B., McPhaul M.J., Cheskis B., Mancini M.A., and Marcelli M. Changes in androgen receptor nongenotropic signaling correlate with transition of LNCaP cells to androgen independence Cancer Res. 64 2004 7156 7168
    • (2004) Cancer Res. , vol.64 , pp. 7156-7168
    • Unni, E.1    Sun, S.2    Nan, B.3    McPhaul, M.J.4    Cheskis, B.5    Mancini, M.A.6    Marcelli, M.7
  • 142
    • 10044265209 scopus 로고    scopus 로고
    • JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species
    • Ventura J.J., Cogswell P., Flavell R.A., Baldwin A.S. Jr., and Davis R.J. JNK potentiates TNF-stimulated necrosis by increasing the production of cytotoxic reactive oxygen species Genes Dev. 18 2004 2905 2915
    • (2004) Genes Dev. , vol.18 , pp. 2905-2915
    • Ventura, J.J.1    Cogswell, P.2    Flavell, R.A.3    Baldwin Jr., A.S.4    Davis, R.J.5
  • 144
    • 0034528256 scopus 로고    scopus 로고
    • Protein kinase C-alpha is an upstream activator of the IkappaB kinase complex in the TPA signal transduction pathway to NF-kappaB in U2OS cells
    • Vertegaal A.C., Kuiperij H.B., Yamaoka S., Courtois G., van der Eb A.J., and Zantema A. Protein kinase C-alpha is an upstream activator of the IkappaB kinase complex in the TPA signal transduction pathway to NF-kappaB in U2OS cells Cell Signal. 12 2000 759 768
    • (2000) Cell Signal. , vol.12 , pp. 759-768
    • Vertegaal, A.C.1    Kuiperij, H.B.2    Yamaoka, S.3    Courtois, G.4    Van Der Eb, A.J.5    Zantema, A.6
  • 145
    • 0032497838 scopus 로고    scopus 로고
    • Diacylglycerol - when it is an intracellular messenger?
    • Wakelam M.J.O. Diacylglycerol - when it is an intracellular messenger? Biochim. Biophys. Acta 1436 1998 117 126
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 117-126
    • Wakelam, M.J.O.1
  • 146
    • 0031056657 scopus 로고    scopus 로고
    • 60 Hz electric fields inhibit protein kinase C activity and multidrug resistance gene (MDR1) up-regulation
    • Walter R., Shtil A., Roninson I., and Holian O. 60 Hz electric fields inhibit protein kinase C activity and multidrug resistance gene (MDR1) up-regulation Radiation Res. 147 1997 369 375
    • (1997) Radiation Res. , vol.147 , pp. 369-375
    • Walter, R.1    Shtil, A.2    Roninson, I.3    Holian, O.4
  • 148
    • 0032537024 scopus 로고    scopus 로고
    • Oncogene loss of protein kinase C function induces an apoptotic response
    • Whelan R.D., and Parker P.J. Oncogene loss of protein kinase C function induces an apoptotic response Oncogene 16 1998 1939 1944
    • (1998) Oncogene , vol.16 , pp. 1939-1944
    • Whelan, R.D.1    Parker, P.J.2
  • 149
    • 0030612643 scopus 로고    scopus 로고
    • Protein kinase C betaII activation by 1-beta-D-arabinofuranosylcytosine is antagonistic to stimulation of apoptosis and Bcl-2-alpha down-regulation
    • Whitman S.P., Civoli F., and Daniel L.W. Protein kinase C betaII activation by 1-beta-D-arabinofuranosylcytosine is antagonistic to stimulation of apoptosis and Bcl-2-alpha down-regulation J. Biol. Chem. 272 1997 23481 23484
    • (1997) J. Biol. Chem. , vol.272 , pp. 23481-23484
    • Whitman, S.P.1    Civoli, F.2    Daniel, L.W.3
  • 150
    • 0028108015 scopus 로고
    • Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling
    • Wiegmann K., Schutze S., Machleidt T., Witte D., and Kronke M. Functional dichotomy of neutral and acidic sphingomyelinases in tumor necrosis factor signaling Cell 78 1994 1005 1015
    • (1994) Cell , vol.78 , pp. 1005-1015
    • Wiegmann, K.1    Schutze, S.2    MacHleidt, T.3    Witte, D.4    Kronke, M.5
  • 151
    • 0032516651 scopus 로고    scopus 로고
    • IEX-1L, an apoptosis inhibitor involved in NFκB-mediated cell survival
    • Wu M.X., Ao Z., Prasad K.V., Wu R., and Schlossman S.F. IEX-1L, an apoptosis inhibitor involved in NFκB-mediated cell survival Science 281 1998 998 1001
    • (1998) Science , vol.281 , pp. 998-1001
    • Wu, M.X.1    Ao, Z.2    Prasad, K.V.3    Wu, R.4    Schlossman, S.F.5
  • 152
    • 0028880006 scopus 로고
    • Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis
    • Xia Z., Dickens M., Raingeuad J., Davis R.J., and Greenberg M.E. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis Science 270 1995 1326 1331
    • (1995) Science , vol.270 , pp. 1326-1331
    • Xia, Z.1    Dickens, M.2    Raingeuad, J.3    Davis, R.J.4    Greenberg, M.E.5
  • 153
    • 0034807617 scopus 로고    scopus 로고
    • Activation of phospholipase C induces the expression of the multidrug resistance (MDR1) gene through the Raf-MAPK pathway
    • Yang J.M., Vassil A.D., and Hait W.N. Activation of phospholipase C induces the expression of the multidrug resistance (MDR1) gene through the Raf-MAPK pathway Mol. Pharmacol. 60 2001 674 680
    • (2001) Mol. Pharmacol. , vol.60 , pp. 674-680
    • Yang, J.M.1    Vassil, A.D.2    Hait, W.N.3
  • 154
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F., Hoberg J.E., Ramsey C.S., Keller M.D., Jones D.R., Frye R.A., and Mayo M.W. Modulation of NF-kappaB-dependent transcription and cell survival by the SIRT1 deacetylase EMBO J. 23 2004 2369 2380
    • (2004) EMBO J. , vol.23 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6    Mayo, M.W.7
  • 155
    • 0032487857 scopus 로고    scopus 로고
    • The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β
    • Yin M.-J., Yamamoto Y., and Gaynor R.B. The anti-inflammatory agents aspirin and salicylate inhibit the activity of IκB kinase-β Nature 396 1998 77 80
    • (1998) Nature , vol.396 , pp. 77-80
    • Yin, M.-J.1    Yamamoto, Y.2    Gaynor, R.B.3
  • 156
    • 0026611036 scopus 로고
    • 2+ oscillations in response to cholecystokinin and carbachol but not to JMV-180 in rat pancreatic acinar cells
    • 2+ oscillations in response to cholecystokinin and carbachol but not to JMV-180 in rat pancreatic acinar cells J. Biol. Chem. 267 1992 13830 13835
    • (1992) J. Biol. Chem. , vol.267 , pp. 13830-13835
    • Yule, D.I.1    Williams, J.A.2


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