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Volumn 83, Issue 8, 2012, Pages 1063-1072

Regulation of chemoresistance via alternative messenger RNA splicing

Author keywords

Alternative splicing; c FLIP; Cyclin D1; Drug resistance; Spliceosome

Indexed keywords

ANDROGEN RECEPTOR; CAMPTOTHECIN; CISPLATIN; CYCLIN D1; CYCLIN DEPENDENT KINASE 4; CYCLIN DEPENDENT KINASE 6; DOXORUBICIN; FLICE INHIBITORY PROTEIN; FLOXURIDINE PHOSPHATE; FLUOROURACIL; GEMCITABINE; HEAT SHOCK PROTEIN 90; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON; IRINOTECAN; JANUS KINASE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE P38; OXALIPLATIN; PROTEIN BAX; PROTEIN P53; PROTEOME; RNA POLYMERASE II; STAT2 PROTEIN; STAUROSPORINE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; UNINDEXED DRUG;

EID: 84858003339     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2011.12.041     Document Type: Review
Times cited : (21)

References (140)
  • 1
    • 79954524112 scopus 로고    scopus 로고
    • Mechanism of cell adaptation: When and how do cancer cells develop chemoresistance?
    • Fodale V, Pierobon M, Liotta L, Petricoin E. Mechanism of cell adaptation: when and how do cancer cells develop chemoresistance? Cancer J 2011;17:89-95.
    • (2011) Cancer J , vol.17 , pp. 89-95
    • Fodale, V.1    Pierobon, M.2    Liotta, L.3    Petricoin, E.4
  • 2
    • 79961172897 scopus 로고    scopus 로고
    • Degrade, move, regroup: Signaling control of splicing proteins
    • Heyd F, Lynch KW. Degrade, move, regroup: signaling control of splicing proteins. Trends Biochem Sci 2011;36:397-404.
    • (2011) Trends Biochem Sci , vol.36 , pp. 397-404
    • Heyd, F.1    Lynch, K.W.2
  • 3
    • 0037069651 scopus 로고    scopus 로고
    • Signal-dependent regulation of splicing via phosphorylation of Sam68
    • DOI 10.1038/nature01153
    • Matter N, Herrlich P, Konig H. Signal-dependent regulation of splicing via phosphorylation of Sam68. Nature 2002;420:691-5. (Pubitemid 36764503)
    • (2002) Nature , vol.420 , Issue.6916 , pp. 691-695
    • Matter, N.1    Herrlich, P.2    Konig, H.3
  • 4
    • 78549234102 scopus 로고    scopus 로고
    • Alternative splicing of caspase 9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a
    • Shultz JC, Goehe RW, Wijesinghe DS, Murudkar C, Hawkins AJ, Shay JW, et al. Alternative splicing of caspase 9 is modulated by the phosphoinositide 3-kinase/Akt pathway via phosphorylation of SRp30a. Cancer Res 2010;70:9185-96.
    • (2010) Cancer Res , vol.70 , pp. 9185-9196
    • Shultz, J.C.1    Goehe, R.W.2    Wijesinghe, D.S.3    Murudkar, C.4    Hawkins, A.J.5    Shay, J.W.6
  • 5
    • 33746516731 scopus 로고    scopus 로고
    • hnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • DOI 10.1128/MCB.00224-06
    • Guil S, Long JC, Caceres JF. hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol Cell Biol 2006;26:5744-58. (Pubitemid 44134331)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.15 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.F.3
  • 6
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • DOI 10.1083/jcb.149.2.307
    • van der Houven van Oordt W, Diaz-Meco MT, Lozano J, Krainer AR, Moscat J, Caceres JF. The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J Cell Biol 2000;149:307-16. (Pubitemid 30227149)
    • (2000) Journal of Cell Biology , vol.149 , Issue.2 , pp. 307-316
    • Van Oordt, W.V.D.H.1    Diaz-Meco, M.T.2    Lozano, J.3    Krainer, A.R.4    Moscat, J.5    Caceres, J.F.6
  • 9
    • 33745899048 scopus 로고    scopus 로고
    • Alternative Splicing: New Insights from Global Analyses
    • DOI 10.1016/j.cell.2006.06.023, PII S0092867406008178
    • Blencowe BJ. Alternative splicing: new insights from global analyses. Cell 2006;126:37-47. (Pubitemid 44040990)
    • (2006) Cell , vol.126 , Issue.1 , pp. 37-47
    • Blencowe, B.J.1
  • 10
    • 0035393343 scopus 로고    scopus 로고
    • Genome-wide detection of alternative splicing in expressed sequences of human genes
    • Modrek B, Resch A, Grasso C, Lee C. Genome-wide detection of alternative splicing in expressed sequences of human genes. Nucleic Acids Res 2001;29:2850-9. (Pubitemid 32685050)
    • (2001) Nucleic Acids Research , vol.29 , Issue.13 , pp. 2850-2859
    • Modrek, B.1    Resch, A.2    Grasso, C.3    Lee, C.4
  • 11
    • 34347237604 scopus 로고    scopus 로고
    • Genomic analysis of RNA alternative splicing in cancers
    • Xing Y. Genomic analysis of RNA alternative splicing in cancers. Front Biosci 2007;12:4034-41.
    • (2007) Front Biosci , vol.12 , pp. 4034-4041
    • Xing, Y.1
  • 13
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • DOI 10.1016/S0955-0674(00)00211-8
    • Will CL, Luhrmann R. Spliceosomal UsnRNP biogenesis, structure and function. Curr Opin Cell Biol 2001;13:290-301. (Pubitemid 32429493)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 14
    • 0035370845 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the new millennium
    • DOI 10.1016/S0955-0674(00)00212-X
    • Hastings ML, Krainer AR. Pre-mRNA splicing in the new millennium. Curr Opin Cell Biol 2001;13:302-9. (Pubitemid 32429494)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 302-309
    • Hastings, M.L.1    Krainer, A.R.2
  • 15
    • 78449290661 scopus 로고    scopus 로고
    • The spliceosomal proteome: At the heart of the largest cellular ribonucleoprotein machine
    • Valadkhan S, Jaladat Y. The spliceosomal proteome: at the heart of the largest cellular ribonucleoprotein machine. Proteomics 2010;10:4128-41.
    • (2010) Proteomics , vol.10 , pp. 4128-4141
    • Valadkhan, S.1    Jaladat, Y.2
  • 16
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • DOI 10.1146/annurev.biochem.72.121801.161720
    • Black DL. Mechanisms of alternative pre-messenger RNA splicing. Annu Rev Biochem 2003;72:291-336. (Pubitemid 36930448)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 291-336
    • Black, D.L.1
  • 17
    • 21244439380 scopus 로고    scopus 로고
    • Regulation of apoptosis by alternative pre-mRNA splicing
    • DOI 10.1016/j.molcel.2005.05.026, PII S1097276505013754
    • Schwerk C, Schulze-Osthoff K. Regulation of apoptosis by alternative premRNA splicing. Mol Cell 2005;19:1-13. (Pubitemid 40884653)
    • (2005) Molecular Cell , vol.19 , Issue.1 , pp. 1-13
    • Schwerk, C.1    Schulze-Osthoff, K.2
  • 19
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human spliceosome
    • DOI 10.1101/gr.473902
    • Rappsilber J, Ryder U, Lamond AI, Mann M. Large-scale proteomic analysis of the human spliceosome. Genome Res 2002;12:1231-45. (Pubitemid 41264425)
    • (2002) Genome Research , vol.12 , Issue.8 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 21
    • 77956927823 scopus 로고    scopus 로고
    • The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation
    • Tripathi V, Ellis JD, Shen Z, Song DY, Pan Q, Watt AT, et al. The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation. Mol Cell 2010;39:925-38.
    • (2010) Mol Cell , vol.39 , pp. 925-938
    • Tripathi, V.1    Ellis, J.D.2    Shen, Z.3    Song, D.Y.4    Pan, Q.5    Watt, A.T.6
  • 22
    • 0029767662 scopus 로고    scopus 로고
    • SR proteins and splicing control
    • Manley JL, Tacke R. SR proteins and splicing control. Genes Dev 1996;10:1569-79. (Pubitemid 26268863)
    • (1996) Genes and Development , vol.10 , Issue.13 , pp. 1569-1579
    • Manley, J.L.1    Tacke, R.2
  • 23
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR. Sorting out the complexity of SR protein functions. RNA 2000;6:1197-211.
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 24
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda A, Munroe SH, Caceres JF, Krainer AR. Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. Embo J 1994;13:5483-95. (Pubitemid 24351827)
    • (1994) EMBO Journal , vol.13 , Issue.22 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 26
    • 0030863326 scopus 로고    scopus 로고
    • In vivo regulation of alternative pre-mRNA splicing by the Clk1 protein kinase
    • Duncan PI, Stojdl DF, Marius RM, Bell JC. In vivo regulation of alternative premRNA splicing by the Clk1 protein kinase. Mol Cell Biol 1997;17:5996-6001. (Pubitemid 27411107)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.10 , pp. 5996-6001
    • Duncan, P.I.1    Stojdl, D.F.2    Marius, R.M.3    Bell, J.C.4
  • 27
    • 0030028882 scopus 로고    scopus 로고
    • The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution
    • Colwill K, Pawson T, Andrews B, Prasad J, Manley JL, Bell JC, et al. The Clk/Sty protein kinase phosphorylates SR splicing factors and regulates their intranuclear distribution. Embo J 1996;15:265-75. (Pubitemid 26029629)
    • (1996) EMBO Journal , vol.15 , Issue.2 , pp. 265-275
    • Colwill, K.1    Pawson, T.2    Andrews, B.3    Prasad, J.4    Manley, J.L.5    Bell, J.C.6    Duncan, P.I.7
  • 28
    • 78049448047 scopus 로고    scopus 로고
    • hnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing
    • Goehe RW, Shultz JC, Murudkar C, Usanovic S, Lamour NF, Massey DH, et al. hnRNP L regulates the tumorigenic capacity of lung cancer xenografts in mice via caspase-9 pre-mRNA processing. J Clin Invest 2010;120:3923-39.
    • (2010) J Clin Invest , vol.120 , pp. 3923-3939
    • Goehe, R.W.1    Shultz, J.C.2    Murudkar, C.3    Usanovic, S.4    Lamour, N.F.5    Massey, D.H.6
  • 29
    • 0032547829 scopus 로고    scopus 로고
    • Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo
    • DOI 10.1083/jcb.143.2.297
    • Misteli T, Caceres JF, Clement JQ, Krainer AR, Wilkinson MF, Spector DL. Serine phosphorylation of SR proteins is required for their recruitment to sites of transcription in vivo. J Cell Biol 1998;143:297-307. (Pubitemid 28487851)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 297-307
    • Misteli, T.1    Caceres, J.F.2    Clement, J.Q.3    Krainer, A.R.4    Wilkinson, M.F.5    Spector, D.L.6
  • 30
    • 0026731973 scopus 로고
    • Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing
    • Mermoud JE, Cohen P, Lamond AI. Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucleic Acids Res 1992;20:5263-9.
    • (1992) Nucleic Acids Res , vol.20 , pp. 5263-5269
    • Mermoud, J.E.1    Cohen, P.2    Lamond, A.I.3
  • 31
    • 27644592554 scopus 로고    scopus 로고
    • Dephosphorylation-dependent sorting of SR splicing factors during mRNP maturation
    • DOI 10.1016/j.molcel.2005.09.015, PII S1097276505016369
    • Lin S, Xiao R, Sun P, Xu X, Fu XD. Dephosphorylation-dependent sorting of SR splicing factors during mRNP maturation. Mol Cell 2005;20:413-25. (Pubitemid 41572298)
    • (2005) Molecular Cell , vol.20 , Issue.3 , pp. 413-425
    • Lin, S.1    Xiao, R.2    Sun, P.3    Xu, X.4    Fu, X.-D.5
  • 32
    • 0037451327 scopus 로고    scopus 로고
    • A novel splicing regulator shares a nuclear import pathway with SR proteins
    • Lai MC, Kuo HW, Chang WC, Tarn WY. A novel splicing regulator shares a nuclear import pathway with SR proteins. Embo J 2003;22:1359-69.
    • (2003) Embo J , vol.22 , pp. 1359-1369
    • Lai, M.C.1    Kuo, H.W.2    Chang, W.C.3    Tarn, W.Y.4
  • 33
    • 0035898616 scopus 로고    scopus 로고
    • The RNA binding protein YB-1 binds A/C-rich exon enhancers and stimulates splicing of the CD44 alternative exon v4
    • DOI 10.1093/emboj/20.14.3821
    • Stickeler E, Fraser SD, Honig A, Chen AL, Berget SM, Cooper TA. The RNA binding protein YB-1 binds A/C-rich exon enhancers and stimulates splicing of the CD44 alternative exon v4. Embo J 2001;20:3821-30. (Pubitemid 32691793)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3821-3830
    • Stickeler, E.1    Fraser, S.D.2    Honig, A.3    Chen, A.L.4    Berget, S.M.5    Cooper, T.A.6
  • 35
    • 0038401969 scopus 로고    scopus 로고
    • Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity
    • DOI 10.1083/jcb.138.2.225
    • Caceres JF, Misteli T, Screaton GR, Spector DL, Krainer AR. Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity. J Cell Biol 1997;138:225-38. (Pubitemid 27323527)
    • (1997) Journal of Cell Biology , vol.138 , Issue.2 , pp. 225-238
    • Caceres, J.F.1    Misteli, T.2    Screaton, G.R.3    Spector, D.L.4    Krainer, A.R.5
  • 36
    • 0344074646 scopus 로고    scopus 로고
    • Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors
    • Hanamura A, Caceres JF, Mayeda A, Franza Jr BR, Krainer AR. Regulated tissue-specific expression of antagonistic pre-mRNA splicing factors. RNA 1998;4:430-44. (Pubitemid 28160784)
    • (1998) RNA , vol.4 , Issue.4 , pp. 430-444
    • Hanamura, A.1    Caceres, J.F.2    Mayeda, A.3    Franza Jr., B.R.4    Krainer, A.R.5
  • 38
    • 55549143293 scopus 로고    scopus 로고
    • The emerging role of splicing factors in cancer
    • Grosso AR, Martins S, Carmo-Fonseca M. The emerging role of splicing factors in cancer. EMBO Rep 2008;9:1087-93.
    • (2008) EMBO Rep , vol.9 , pp. 1087-1093
    • Grosso, A.R.1    Martins, S.2    Carmo-Fonseca, M.3
  • 41
    • 0037013146 scopus 로고    scopus 로고
    • Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45
    • DOI 10.1016/S0092-8674(02)00730-4
    • Lallena MJ, Chalmers KJ, Llamazares S, Lamond AI, Valcarcel J. Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45. Cell 2002;109:285-96. (Pubitemid 34606872)
    • (2002) Cell , vol.109 , Issue.3 , pp. 285-296
    • Lallena, M.J.1    Chalmers, K.J.2    Llamazares, S.3    Lamond, A.I.4    Valcarcel, J.5
  • 42
    • 0033200012 scopus 로고    scopus 로고
    • G-patch: A new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins
    • DOI 10.1016/S0968-0004(99)01437-1, PII S0968000499014371
    • Aravind L, Koonin EV. G-patch: a new conserved domain in eukaryotic RNA-processing proteins and type D retroviral polyproteins. Trends Biochem Sci 1999;24:342-4. (Pubitemid 29421808)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.9 , pp. 342-344
    • Aravind, L.1    Koonin, E.V.2
  • 43
    • 8644284892 scopus 로고    scopus 로고
    • Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase that is critical for splicing
    • DOI 10.1128/MCB.24.23.10101-10110.2004
    • Silverman EJ, Maeda A, Wei J, Smith P, Beggs JD, Lin RJ. Interaction between a G-patch protein and a spliceosomal DEXD/H-box ATPase that is critical for splicing. Mol Cell Biol 2004;24:10101-10. (Pubitemid 39507850)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.23 , pp. 10101-10110
    • Silverman, E.J.1    Maeda, A.2    Wei, J.3    Smith, P.4    Beggs, J.D.5    Lin, R.-J.6
  • 44
    • 4944256316 scopus 로고    scopus 로고
    • Proteinases of betaretroviruses bind single-stranded nucleic acids through a novel interaction module, the G-patch
    • DOI 10.1016/j.febslet.2004.09.010, PII S001457930401124X
    • Svec M, Bauerova H, Pichova I, Konvalinka J, Strisovsky K. Proteinases of betaretroviruses bind single-stranded nucleic acids through a novel interaction module, the G-patch. FEBS Lett 2004;576:271-6. (Pubitemid 39330496)
    • (2004) FEBS Letters , vol.576 , Issue.1-2 , pp. 271-276
    • Svec, M.1    Bauerova, H.2    Pichova, I.3    Konvalinka, J.4    Strisovsky, K.5
  • 45
    • 33645914121 scopus 로고    scopus 로고
    • Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii
    • Frenal K, Callebaut I, Wecker K, Prochnicka-Chalufour A, Dendouga N, Zinn-Justin S, et al. Structural and functional characterization of the TgDRE multidomain protein, a DNA repair enzyme from Toxoplasma gondii. Biochemistry 2006;45:4867-74.
    • (2006) Biochemistry , vol.45 , pp. 4867-4874
    • Frenal, K.1    Callebaut, I.2    Wecker, K.3    Prochnicka-Chalufour, A.4    Dendouga, N.5    Zinn-Justin, S.6
  • 47
    • 23744492690 scopus 로고    scopus 로고
    • Regulation of fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition
    • DOI 10.1016/j.molcel.2005.06.015, PII S1097276505014188
    • Izquierdo JM, Majos N, Bonnal S, Martinez C, Castelo R, Guigo R, et al. Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol Cell 2005;19:475-84. (Pubitemid 41140005)
    • (2005) Molecular Cell , vol.19 , Issue.4 , pp. 475-484
    • Izquierdo, J.M.1    Majos, N.2    Bonnal, S.3    Martinez, C.4    Castelo, R.5    Guigo, R.6    Bilbao, D.7    Valcarcel, J.8
  • 48
    • 38349085591 scopus 로고    scopus 로고
    • Regulation of alternative splicing by reversible protein phosphorylation
    • Stamm S. Regulation of alternative splicing by reversible protein phosphorylation. J Biol Chem 2008;283:1223-7.
    • (2008) J Biol Chem , vol.283 , pp. 1223-1227
    • Stamm, S.1
  • 52
    • 0033800091 scopus 로고    scopus 로고
    • Multicellular resistance: A paradigm for clinical resistance?
    • Desoize B, Jardillier J. Multicellular resistance: a paradigm for clinical resistance? Crit Rev Oncol Hematol 2000;36:193-207.
    • (2000) Crit Rev Oncol Hematol , vol.36 , pp. 193-207
    • Desoize, B.1    Jardillier, J.2
  • 54
    • 63449105639 scopus 로고    scopus 로고
    • Compact spheroid formation by ovarian cancer cells is associated with contractile behavior and an invasive phenotype
    • Sodek KL, Ringuette MJ, Brown TJ. Compact spheroid formation by ovarian cancer cells is associated with contractile behavior and an invasive phenotype. Int J Cancer 2009;124:2060-70.
    • (2009) Int J Cancer , vol.124 , pp. 2060-2070
    • Sodek, K.L.1    Ringuette, M.J.2    Brown, T.J.3
  • 55
    • 0027286404 scopus 로고
    • Two cDNAs from the plant Arabidopsis thaliana that partially restore recombination proficiency and DNA-damage resistance to E.Coli mutants lacking recombination-intermediate-resolution activities
    • Pang Q, Hays JB, Rajagopal I. Two cDNAs from the plant Arabidopsis thaliana that partially restore recombination proficiency and DNA-damage resistance to E. coli mutants lacking recombination-intermediate-resolution activities. Nucleic Acids Res 1993;21:1647-53. (Pubitemid 23146334)
    • (1993) Nucleic Acids Research , vol.21 , Issue.7 , pp. 1647-1653
    • Pang, Q.1    Hays, J.B.2    Rajagopal, I.3
  • 56
    • 33846031127 scopus 로고    scopus 로고
    • Drosophila SPF45: A Bifunctional Protein with Roles in Both Splicing and DNA Repair
    • Chaouki AS, Salz HK. Drosophila SPF45: A Bifunctional Protein with Roles in Both Splicing and DNA Repair. PLoS Genet 2006;2:e178.
    • (2006) PLoS Genet , vol.2
    • Chaouki, A.S.1    Salz, H.K.2
  • 59
    • 33947223157 scopus 로고    scopus 로고
    • Serine-arginine protein kinase 1 overexpression is associated with tumorigenic imbalance in mitogen-activated protein kinase pathways in breast, colonic, and pancreatic carcinomas
    • DOI 10.1158/0008-5472.CAN-06-2969
    • Hayes GM, Carrigan PE, Miller LJ. Serine-arginine protein kinase 1 overexpression is associated with tumorigenic imbalance in mitogen-activated protein kinase pathways in breast, colonic, and pancreatic carcinomas. Cancer Res 2007;67:2072-80. (Pubitemid 46424225)
    • (2007) Cancer Research , vol.67 , Issue.5 , pp. 2072-2080
    • Hayes, G.M.1    Carrigan, P.E.2    Miller, L.J.3
  • 60
    • 33645746620 scopus 로고    scopus 로고
    • Targeting the RNA splicing machinery as a novel treatment strategy for pancreatic carcinoma
    • Hayes GM, Carrigan PE, Beck AM, Miller LJ. Targeting the RNA splicing machinery as a novel treatment strategy for pancreatic carcinoma. Cancer Res 2006;66:3819-27.
    • (2006) Cancer Res , vol.66 , pp. 3819-3827
    • Hayes, G.M.1    Carrigan, P.E.2    Beck, A.M.3    Miller, L.J.4
  • 61
    • 0028225858 scopus 로고
    • A ligand-dependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences
    • Zhou ZX, Sar M, Simental JA, Lane MV, Wilson EM. A ligand-dependent bipartite nuclear targeting signal in the human androgen receptor. Requirement for the DNA-binding domain and modulation by NH2-terminal and carboxyl-terminal sequences. J Biol Chem 1994;269:13115-23.
    • (1994) J Biol Chem , vol.269 , pp. 13115-13123
    • Zhou, Z.X.1    Sar, M.2    Simental, J.A.3    Lane, M.V.4    Wilson, E.M.5
  • 62
    • 0037447330 scopus 로고    scopus 로고
    • Constitutive activation of the Ras/mitogen-activated protein kinase signaling pathway promotes androgen hypersensitivity in LNCaP prostate cancer cells
    • Bakin RE, Gioeli D, Sikes RA, Bissonette EA, Weber MJ. Constitutive activation of the Ras/mitogen-activated protein kinase signaling pathway promotes androgen hypersensitivity in LNCaP prostate cancer cells. Cancer Res 2003;63:1981-9. (Pubitemid 36460867)
    • (2003) Cancer Research , vol.63 , Issue.8 , pp. 1981-1989
    • Bakin, R.E.1    Gioeli, D.2    Sikes, R.A.3    Bissonette, E.A.4    Weber, M.J.5
  • 63
    • 0037447154 scopus 로고    scopus 로고
    • Attenuation of Ras signaling restores androgen sensitivity to hormone-refractory C4-2 prostate cancer cells
    • Bakin RE, Gioeli D, Bissonette EA, Weber MJ. Attenuation of Ras signaling restores androgen sensitivity to hormone-refractory C4-2 prostate cancer cells. Cancer Res 2003;63:1975-80. (Pubitemid 36460866)
    • (2003) Cancer Research , vol.63 , Issue.8 , pp. 1975-1980
    • Bakin, R.E.1    Gioeli, D.2    Bissonette, E.A.3    Weber, M.J.4
  • 64
    • 0033555967 scopus 로고    scopus 로고
    • Activation of mitogen-activated protein kinase associated with prostate cancer progression
    • Gioeli D, Mandell JW, Petroni GR, Frierson Jr HF, Weber MJ. Activation of mitogen-activated protein kinase associated with prostate cancer progression. Cancer Res 1999;59:279-84. (Pubitemid 29048852)
    • (1999) Cancer Research , vol.59 , Issue.2 , pp. 279-284
    • Gioeli, D.1    Mandell, J.W.2    Petroni, G.R.3    Frierson Jr., H.F.4    Weber, M.J.5
  • 65
    • 19044380048 scopus 로고    scopus 로고
    • Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites
    • Gioeli D, Ficarro SB, Kwiek JJ, Aaronson D, Hancock M, Catling AD, et al. Androgen receptor phosphorylation. Regulation and identification of the phosphorylation sites. J Biol Chem 2002;277:29304-1.
    • (2002) J Biol Chem , vol.277 , pp. 29304-29311
    • Gioeli, D.1    Ficarro, S.B.2    Kwiek, J.J.3    Aaronson, D.4    Hancock, M.5    Catling, A.D.6
  • 67
    • 80054931284 scopus 로고    scopus 로고
    • Alternatively spliced androgen receptor variants
    • Dehm SM, Tindall DJ. Alternatively spliced androgen receptor variants. Endocr Relat Cancer 2011;18:R183-96.
    • (2011) Endocr Relat Cancer , vol.18
    • Dehm, S.M.1    Tindall, D.J.2
  • 68
    • 0037112372 scopus 로고    scopus 로고
    • Characterization of a novel androgen receptor mutation in a relapsed CWR22 prostate cancer xenograft and cell line
    • Tepper CG, Boucher DL, Ryan PE, Ma AH, Xia L, Lee LF, et al. Characterization of a novel androgen receptor mutation in a relapsed CWR22 prostate cancer xenograft and cell line. Cancer Res 2002;62:6606-14. (Pubitemid 35364127)
    • (2002) Cancer Research , vol.62 , Issue.22 , pp. 6606-6614
    • Tepper, C.G.1    Boucher, D.L.2    Ryan, P.E.3    Ma, A.-H.4    Xia, L.5    Lee, L.-F.6    Pretlow, T.G.7    Kung, H.-J.8
  • 69
    • 35148833549 scopus 로고    scopus 로고
    • Evidence for calpain-mediated androgen receptor cleavage as a mechanism for androgen independence
    • DOI 10.1158/0008-5472.CAN-07-1072
    • Libertini SJ, Tepper CG, Rodriguez V, Asmuth DM, Kung HJ, Mudryj M. Evidence for calpain-mediated androgen receptor cleavage as a mechanism for androgen independence. Cancer Res 2007;67:9001-5. (Pubitemid 47535881)
    • (2007) Cancer Research , vol.67 , Issue.19 , pp. 9001-9005
    • Libertini, S.J.1    Tepper, C.G.2    Rodriguez, V.3    Asmuth, D.M.4    Kung, H.-J.5    Mudryj, M.6
  • 70
    • 48549089747 scopus 로고    scopus 로고
    • Splicing of a novel androgenreceptor exongenerates a constitutivelyactive androgenreceptor that mediates prostate cancer therapy resistance
    • Dehm SM, Schmidt LJ, Heemers HV, Vessella RL, Tindall DJ. Splicing of a novel androgenreceptor exongenerates a constitutivelyactive androgenreceptor that mediates prostate cancer therapy resistance. Cancer Res 2008;68:5469-77.
    • (2008) Cancer Res , vol.68 , pp. 5469-5477
    • Dehm, S.M.1    Schmidt, L.J.2    Heemers, H.V.3    Vessella, R.L.4    Tindall, D.J.5
  • 71
    • 80054931284 scopus 로고    scopus 로고
    • Alternatively spliced androgen receptor variants
    • Dehm S, Tindall DJ. Alternatively spliced androgen receptor variants. Endocr Relat Cancer 2011.
    • (2011) Endocr Relat Cancer
    • Dehm, S.1    Tindall, D.J.2
  • 72
    • 58249110391 scopus 로고    scopus 로고
    • Ligand-independent androgen receptor variants derived from splicing of cryptic exons signify hormone-refractory prostate cancer
    • Hu R, Dunn TA, Wei S, Isharwal S, Veltri RW, Humphreys E, et al. Ligand-independent androgen receptor variants derived from splicing of cryptic exons signify hormone-refractory prostate cancer. Cancer Res 2009;69:16-22.
    • (2009) Cancer Res , vol.69 , pp. 16-22
    • Hu, R.1    Dunn, T.A.2    Wei, S.3    Isharwal, S.4    Veltri, R.W.5    Humphreys, E.6
  • 73
    • 79959312739 scopus 로고    scopus 로고
    • A snapshot of the expression signature of androgen receptor splicing variants and their distinctive transcriptional activities
    • Hu R, Isaacs WB, Luo J. A snapshot of the expression signature of androgen receptor splicing variants and their distinctive transcriptional activities. Prostate 2011;71:1656-67.
    • (2011) Prostate , vol.71 , pp. 1656-1667
    • Hu, R.1    Isaacs, W.B.2    Luo, J.3
  • 74
    • 74049109753 scopus 로고    scopus 로고
    • Identification of novel truncated androgen receptor (AR) mutants including unreported pre-mRNA splicing variants in the 22Rv1 hormone-refractory prostate cancer (PCa) cell line
    • Marcias G, Erdmann E, Lapouge G, Siebert C, Barthelemy P, Duclos B, et al. Identification of novel truncated androgen receptor (AR) mutants including unreported pre-mRNA splicing variants in the 22Rv1 hormone-refractory prostate cancer (PCa) cell line. Hum Mutat 2010;31:74-80.
    • (2010) Hum Mutat , vol.31 , pp. 74-80
    • Marcias, G.1    Erdmann, E.2    Lapouge, G.3    Siebert, C.4    Barthelemy, P.5    Duclos, B.6
  • 75
    • 0033664255 scopus 로고    scopus 로고
    • How does interferon-alpha exert its antitumour activity in multiple myeloma?
    • Grander D. How does interferon-alpha exert its antitumour activity in multiple myeloma? Acta Oncol 2000;39:801-5.
    • (2000) Acta Oncol , vol.39 , pp. 801-805
    • Grander, D.1
  • 76
    • 0034157415 scopus 로고    scopus 로고
    • Treatment advances in non-Hodgkin's lymphoma
    • Tan BR, Bartlett NL. Treatment advances in non-Hodgkin's lymphoma. Expert Opin Pharmacother 2000;1:451-66.
    • (2000) Expert Opin Pharmacother , vol.1 , pp. 451-466
    • Tan, B.R.1    Bartlett, N.L.2
  • 77
    • 79955909579 scopus 로고    scopus 로고
    • Immunomodulatory cytokines as therapeutic agents for melanoma
    • Nicholas C, Lesinski GB. Immunomodulatory cytokines as therapeutic agents for melanoma. Immunotherapy 2011;3:673-90.
    • (2011) Immunotherapy , vol.3 , pp. 673-690
    • Nicholas, C.1    Lesinski, G.B.2
  • 78
    • 0036269757 scopus 로고    scopus 로고
    • Cancer immunotherapy: The interferon-alpha experience
    • Kirkwood J. Cancer immunotherapy: the interferon-alpha experience. Semin Oncol 2002;29:18-26.
    • (2002) Semin Oncol , vol.29 , pp. 18-26
    • Kirkwood, J.1
  • 80
    • 0029133702 scopus 로고
    • Requirement for MAP kinase (ERK2) activity in interferon alpha- And interferon beta-stimulated gene expression through STAT proteins
    • David M, Petricoin 3rd E, Benjamin C, Pine R, Weber MJ, Larner AC. Requirement for MAP kinase (ERK2) activity in interferon alpha- and interferon beta-stimulated gene expression through STAT proteins. Science 1995;269:1721-3.
    • (1995) Science , vol.269 , pp. 1721-1723
    • David, M.1    Petricoin III, E.2    Benjamin, C.3    Pine, R.4    Weber, M.J.5    Larner, A.C.6
  • 81
    • 70350435094 scopus 로고    scopus 로고
    • Interferon-resistant Daudi cell line with a Stat2 defect is resistant to apoptosis induced by chemotherapeutic agents
    • Du Z, Fan M, Kim JG, Eckerle D, Lothstein L, Wei L, et al. Interferon-resistant Daudi cell line with a Stat2 defect is resistant to apoptosis induced by chemotherapeutic agents. J Biol Chem 2009;284:27808-15.
    • (2009) J Biol Chem , vol.284 , pp. 27808-27815
    • Du, Z.1    Fan, M.2    Kim, J.G.3    Eckerle, D.4    Lothstein, L.5    Wei, L.6
  • 82
    • 0029987787 scopus 로고    scopus 로고
    • Identification of alternative splicing form of stat2
    • DOI 10.1016/0014-5793(96)00121-4
    • Sugiyama T, Nishio Y, Kishimoto T, Akira S. Identification of alternative splicing form of Stat2. FEBS Lett 1996;381:191-4. (Pubitemid 26080337)
    • (1996) FEBS Letters , vol.381 , Issue.3 , pp. 191-194
    • Sugiyama, T.1    Nishio, Y.2    Kishimoto, T.3    Akira, S.4
  • 85
    • 0032533881 scopus 로고    scopus 로고
    • Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1
    • Zwijsen RM, Buckle RS, Hijmans EM, Loomans CJ, Bernards R. Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1. Genes Dev 1998;12:3488-98. (Pubitemid 28553241)
    • (1998) Genes and Development , vol.12 , Issue.22 , pp. 3488-3498
    • Zwijsen, R.M.L.1    Buckle, R.S.2    Hijmans, E.M.3    Loomans, C.J.M.4    Bernards, R.5
  • 86
    • 23044508946 scopus 로고    scopus 로고
    • Cyclin D1 in breast cancer pathogenesis
    • DOI 10.1200/JCO.2005.05.064
    • Arnold A, Papanikolaou A. Cyclin D1 in breast cancer pathogenesis. J Clin Oncol 2005;23:4215-24. (Pubitemid 46211327)
    • (2005) Journal of Clinical Oncology , vol.23 , Issue.18 , pp. 4215-4224
    • Arnold, A.1    Papanikolaou, A.2
  • 87
    • 0013439945 scopus 로고    scopus 로고
    • Cycling to cancer with cyclin D1
    • Diehl JA. Cycling to cancer with cyclin D1. Cancer Biol Ther 2002;1:226-31.
    • (2002) Cancer Biol Ther , vol.1 , pp. 226-231
    • Diehl, J.A.1
  • 89
    • 0028129951 scopus 로고
    • The PRAD-1/cyclin D1 oncogene product accumulates aberrantly in a subset of colorectal carcinomas
    • Bartkova J, Lukas J, Strauss M, Bartek J. The PRAD-1/cyclin D1 oncogene product accumulates aberrantly in a subset of colorectal carcinomas. Int J Cancer 1994;58:568-73. (Pubitemid 24268101)
    • (1994) International Journal of Cancer , vol.58 , Issue.4 , pp. 568-573
    • Bartkova, J.1    Lukas, J.2    Strauss, M.3    Bartek, J.4
  • 90
    • 0034671768 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation
    • DOI 10.1101/gad.854900
    • Alt JR, Cleveland JL, Hannink M, Diehl JA. Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation. Genes Dev 2000;14:3102-14. (Pubitemid 32015129)
    • (2000) Genes and Development , vol.14 , Issue.24 , pp. 3102-3114
    • Alt, J.R.1    Cleveland, J.L.2    Hannink, M.3    Diehl, J.A.4
  • 91
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta; regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussel MF, Sherr CJ. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 1998;12:3499-511. (Pubitemid 28553242)
    • (1998) Genes and Development , vol.12 , Issue.22 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 92
    • 0034697022 scopus 로고    scopus 로고
    • Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286
    • DOI 10.1074/jbc.275.16.12074
    • Germain D, Russell A, Thompson A, Hendley J. Ubiquitination of free cyclin D1 is independent of phosphorylation on threonine 286. J Biol Chem 2000;275:12074-9. (Pubitemid 30237782)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.16 , pp. 12074-12079
    • Germain, D.1    Russell, A.2    Thompson, A.3    Hendley, J.4
  • 94
    • 0031586763 scopus 로고    scopus 로고
    • Cyclin D1 (PRAD1) alternative transcript b: Full-length cDNA cloning and expression in breast cancers
    • DOI 10.1016/S0304-3835(97)04605-3, PII S0304383597046053
    • Hosokawa Y, Gadd M, Smith AP, Koerner FC, Schmidt EV, Arnold A. Cyclin D1 (PRAD1) alternative transcript b: full-length cDNA cloning and expression in breast cancers. Cancer Lett 1997;113:123-30. (Pubitemid 27113238)
    • (1997) Cancer Letters , vol.113 , Issue.1-2 , pp. 123-130
    • Hosokawa, Y.1    Gadd, M.2    Smith, A.P.3    Koerner, F.C.4    Schmidt, E.V.5    Arnold, A.6
  • 95
    • 48649103464 scopus 로고    scopus 로고
    • Cyclin D1b is aberrantly regulated in response to therapeutic challenge and promotes resistance to estrogen antagonists
    • Wang Y, Dean JL, Millar EK, Tran TH, McNeil CM, Burd CJ, et al. Cyclin D1b is aberrantly regulated in response to therapeutic challenge and promotes resistance to estrogen antagonists. Cancer Res 2008;68:5628-38.
    • (2008) Cancer Res , vol.68 , pp. 5628-5638
    • Wang, Y.1    Dean, J.L.2    Millar, E.K.3    Tran, T.H.4    McNeil, C.M.5    Burd, C.J.6
  • 96
    • 33645118564 scopus 로고    scopus 로고
    • Cyclin D1: Polymorphism, aberrant splicing and cancer risk
    • Knudsen KE, Diehl JA, Haiman CA, Knudsen ES. Cyclin D1: polymorphism, aberrant splicing and cancer risk. Oncogene 2006;25:1620-8.
    • (2006) Oncogene , vol.25 , pp. 1620-1628
    • Knudsen, K.E.1    Diehl, J.A.2    Haiman, C.A.3    Knudsen, E.S.4
  • 97
    • 77953732182 scopus 로고    scopus 로고
    • Cyclin D1b in human breast carcinoma and coexpression with cyclin D1a is associated with poor outcome
    • Abramson VG, Troxel AB, Feldman M, Mies C, Wang Y, Sherman L, et al. Cyclin D1b in human breast carcinoma and coexpression with cyclin D1a is associated with poor outcome. Anticancer Res 2010;30:1279-85.
    • (2010) Anticancer Res , vol.30 , pp. 1279-1285
    • Abramson, V.G.1    Troxel, A.B.2    Feldman, M.3    Mies, C.4    Wang, Y.5    Sherman, L.6
  • 98
    • 65049084565 scopus 로고    scopus 로고
    • Cyclin D1b protein expression in breast cancer is independent of cyclin D1a and associated with poor disease outcome
    • Millar EK, Dean JL, McNeil CM, O'Toole SA, Henshall SM, Tran T, et al. Cyclin D1b protein expression in breast cancer is independent of cyclin D1a and associated with poor disease outcome. Oncogene 2009;28:1812-20.
    • (2009) Oncogene , vol.28 , pp. 1812-1820
    • Millar, E.K.1    Dean, J.L.2    McNeil, C.M.3    O'Toole, S.A.4    Henshall, S.M.5    Tran, T.6
  • 102
    • 3042818713 scopus 로고    scopus 로고
    • Polymorphism within the cyclin D1 gene is associated with an increased risk of carcinoma in situ in patients with superficial bladder cancer
    • DOI 10.1016/j.urology.2004.03.001, PII S0090429504003164
    • Ito M, Habuchi T, Watanabe J, Higashi S, Nishiyama H, Wang L, et al. Polymorphism within the cyclin D1 gene is associated with an increased risk of carcinoma in situ in patients with superficial bladder cancer. Urology 2004;64:74-8. (Pubitemid 38887582)
    • (2004) Urology , vol.64 , Issue.1 , pp. 74-78
    • Ito, M.1    Habuchi, T.2    Watanabe, J.3    Higashi, S.4    Nishiyama, H.5    Wang, L.6    Tsuchiya, N.7    Kamoto, T.8    Ogawa, O.9
  • 104
  • 106
    • 77952796886 scopus 로고    scopus 로고
    • Identification of ASF/SF2 as a critical, allele-specific effector of the cyclin D1b oncogene
    • Olshavsky NA, Comstock CE, Schiewer MJ, Augello MA, Hyslop T, Sette C, et al. Identification of ASF/SF2 as a critical, allele-specific effector of the cyclin D1b oncogene. Cancer Res 2010;70:3975-84.
    • (2010) Cancer Res , vol.70 , pp. 3975-3984
    • Olshavsky, N.A.1    Comstock, C.E.2    Schiewer, M.J.3    Augello, M.A.4    Hyslop, T.5    Sette, C.6
  • 107
    • 75149187424 scopus 로고    scopus 로고
    • Alternative splicing of the cyclin D1 proto-oncogene is regulated by the RNA-binding protein Sam68
    • Paronetto MP, Cappellari M, Busa R, Pedrotti S, Vitali R, Comstock C, et al. Alternative splicing of the cyclin D1 proto-oncogene is regulated by the RNA-binding protein Sam68. Cancer Res 2010;70:229-39.
    • (2010) Cancer Res , vol.70 , pp. 229-239
    • Paronetto, M.P.1    Cappellari, M.2    Busa, R.3    Pedrotti, S.4    Vitali, R.5    Comstock, C.6
  • 108
    • 0242526150 scopus 로고    scopus 로고
    • An Alternatively Spliced Cyclin D1 Isoform, Cyclin D1b, Is a Nuclear Oncogene
    • Lu F, Gladden AB, Diehl JA. An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene. Cancer Res 2003;63:7056-61. (Pubitemid 37413439)
    • (2003) Cancer Research , vol.63 , Issue.21 , pp. 7056-7061
    • Lu, F.1    Gladden, A.B.2    Diehl, J.A.3
  • 110
    • 0034616913 scopus 로고    scopus 로고
    • Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage
    • Agami R, Bernards R. Distinct initiation and maintenance mechanisms cooperate to induce G1 cell cycle arrest in response to DNA damage. Cell 2000;102:55-66.
    • (2000) Cell , vol.102 , pp. 55-66
    • Agami, R.1    Bernards, R.2
  • 112
    • 0035496099 scopus 로고    scopus 로고
    • Regulation of lymphocyte proliferation and death by flip
    • Thome M, Tschopp J. Regulation of lymphocyte proliferation and death by FLIP. Nat Rev Immunol 2001;1:50-8. (Pubitemid 33741975)
    • (2001) Nature Reviews Immunology , vol.1 , Issue.1 , pp. 50-58
    • Thome, M.1    Tschopp, J.2
  • 113
    • 33344476184 scopus 로고    scopus 로고
    • cFLIP regulation of lymphocyte activation and development
    • DOI 10.1038/nri1787
    • Budd RC, Yeh WC, Tschopp J. cFLIP regulation of lymphocyte activation and development. Nat Rev Immunol 2006;6:196-204. (Pubitemid 43290989)
    • (2006) Nature Reviews Immunology , vol.6 , Issue.3 , pp. 196-204
    • Budd, R.C.1    Yeh, W.-C.2    Tschopp, J.3
  • 114
    • 0035192884 scopus 로고    scopus 로고
    • FLICE-inhibitory proteins: Regulators of death receptor-mediated apoptosis
    • DOI 10.1128/MCB.21.24.8247-8254.2001
    • Krueger A, Baumann S, Krammer PH, Kirchhoff S. FLICE-inhibitory proteins: regulators of death receptor-mediated apoptosis. Mol Cell Biol 2001;21:8247-54. (Pubitemid 33108586)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.24 , pp. 8247-8254
    • Krueger, A.1    Baumann, S.2    Krammer, P.H.3    Kirchhoff, S.4
  • 115
    • 0035827569 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex
    • Krueger A, Schmitz I, Baumann S, Krammer PH, Kirchhoff S. Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex. J Biol Chem 2001;276:20633-40.
    • (2001) J Biol Chem , vol.276 , pp. 20633-20640
    • Krueger, A.1    Schmitz, I.2    Baumann, S.3    Krammer, P.H.4    Kirchhoff, S.5
  • 116
    • 21444446872 scopus 로고    scopus 로고
    • Selective knockdown of the long variant of cellular FLICE inhibitory protein augments death receptor-mediated caspase-8 activation and apoptosis
    • DOI 10.1074/jbc.M413962200
    • Sharp DA, Lawrence DA, Ashkenazi A. Selective knockdown of the long variant of cellular FLICE inhibitory protein augments death receptor-mediated caspase-8 activation and apoptosis. J Biol Chem 2005;280:19401-9. (Pubitemid 41379648)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.19 , pp. 19401-19409
    • Sharp, D.A.1    Lawrence, D.A.2    Ashkenazi, A.3
  • 118
    • 40949149811 scopus 로고    scopus 로고
    • R, the only murine short FLIP isoform, reveal requirements for DISC recruitment
    • DOI 10.1038/sj.cdd.4402314, PII 4402314, The biology of Hypoxia-inducible factors
    • Ueffing N, Keil E, Freund C, Kuhne R, Schulze-Osthoff K, Schmitz I. Mutational analyses of c-FLIPR, the only murine short FLIP isoform, reveal requirements for DISC recruitment. Cell Death Differ 2008;15:773-82. (Pubitemid 351405082)
    • (2008) Cell Death and Differentiation , vol.15 , Issue.4 , pp. 773-782
    • Ueffing, N.1    Keil, E.2    Freund, C.3    Kuhne, R.4    Schulze-Osthoff, K.5    Schmitz, I.6
  • 121
    • 23744456144 scopus 로고    scopus 로고
    • An essential role for c-FLIP in the efficient development of mature T lymphocytes
    • DOI 10.1084/jem.20050117
    • Zhang N, He YW. An essential role for c-FLIP in the efficient development of mature T lymphocytes. J Exp Med 2005;202:395-404. (Pubitemid 41126957)
    • (2005) Journal of Experimental Medicine , vol.202 , Issue.3 , pp. 395-404
    • Zhang, N.1    He, Y.-W.2
  • 122
    • 0038373452 scopus 로고    scopus 로고
    • cFLIP-L inhibits p38 MAPK activation. An additional anti-apoptotic mechanism in bile acid-mediated apoptosis
    • DOI 10.1074/jbc.M303229200
    • Grambihler A, Higuchi H, Bronk SF, Gores GJ. cFLIP-L inhibits p38 MAPK activation: an additional anti-apoptotic mechanism in bile acid-mediated apoptosis. J Biol Chem 2003;278:26831-7. (Pubitemid 36876833)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26831-26837
    • Grambihler, A.1    Higuchi, H.2    Bronk, S.F.3    Gores, G.J.4
  • 125
    • 17844361968 scopus 로고    scopus 로고
    • + T cell activation through caspase-8-dependent NF-kappaB activation
    • Dohrman A, Kataoka T, Cuenin S, Russell JQ, Tschopp J, Budd RC. Cellular FLIP (long form) regulates CD8+ T cell activation through caspase-8-dependent NF-kappa B activation. J Immunol 2005;174:5270-8. (Pubitemid 40593165)
    • (2005) Journal of Immunology , vol.174 , Issue.9 , pp. 5270-5278
    • Dohrman, A.1    Kataoka, T.2    Cuenin, S.3    Russell, J.Q.4    Tschopp, J.5    Budd, R.C.6
  • 126
    • 77955465116 scopus 로고    scopus 로고
    • Model-based dissection of CD95 signaling dynamics reveals both a pro- And antiapoptotic role of c-FLIPL
    • Fricker N, Beaudouin J, Richter P, Eils R, Krammer PH, Lavrik IN. Model-based dissection of CD95 signaling dynamics reveals both a pro- and antiapoptotic role of c-FLIPL. J Cell Biol 2010;190:377-89.
    • (2010) J Cell Biol , vol.190 , pp. 377-389
    • Fricker, N.1    Beaudouin, J.2    Richter, P.3    Eils, R.4    Krammer, P.H.5    Lavrik, I.N.6
  • 128
    • 33144488766 scopus 로고    scopus 로고
    • Increased expression of cFLIP(L) in colonic adenocarcinoma
    • Ryu BK, Lee MG, Chi SG, Kim YW, Park JH. Increased expression of cFLIP(L) in colonic adenocarcinoma. J Pathol 2001;194:15-9.
    • (2001) J Pathol , vol.194 , pp. 15-19
    • Ryu, B.K.1    Lee, M.G.2    Chi, S.G.3    Kim, Y.W.4    Park, J.H.5
  • 129
    • 0038387494 scopus 로고    scopus 로고
    • 5-Fluorouracil: Mechanisms of action and clinical strategies
    • DOI 10.1038/nrc1074
    • Longley DB, Harkin DP, Johnston PG. 5-fluorouracil: mechanisms of action and clinical strategies. Nat Rev Cancer 2003;3:330-8. (Pubitemid 37328853)
    • (2003) Nature Reviews Cancer , vol.3 , Issue.5 , pp. 330-338
    • Longley, D.B.1    Harkin, D.P.2    Johnston, P.G.3
  • 132
    • 65649089859 scopus 로고    scopus 로고
    • 5-Fluorouracil and its active metabolite FdUMP cause DNA damage in human SW620 colon adenocarcinoma cell line
    • Matuo R, Sousa FG, Escargueil AE, Grivicich I, Garcia-Santos D, Chies JA, et al. 5-Fluorouracil and its active metabolite FdUMP cause DNA damage in human SW620 colon adenocarcinoma cell line. J Appl Toxicol 2009;29:308-16.
    • (2009) J Appl Toxicol , vol.29 , pp. 308-316
    • Matuo, R.1    Sousa, F.G.2    Escargueil, A.E.3    Grivicich, I.4    Garcia-Santos, D.5    Chies, J.A.6
  • 136
    • 4644299291 scopus 로고    scopus 로고
    • Alternative splicing of Bcl-2-related genes: Functional consequences and potential therapeutic applications
    • DOI 10.1007/s00018-004-4001-7
    • Akgul C, Moulding DA, Edwards SW. Alternative splicing of Bcl-2-related genes: functional consequences and potential therapeutic applications. Cell Mol Life Sci 2004;61:2189-99. (Pubitemid 39280118)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.17 , pp. 2189-2199
    • Akgul, C.1    Moulding, D.A.2    Edwards, S.W.3
  • 138
    • 0034682837 scopus 로고    scopus 로고
    • MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain
    • Bae J, Leo CP, Hsu SY, Hsueh AJ. MCL-1S, a splicing variant of the antiapoptotic BCL-2 family member MCL-1, encodes a proapoptotic protein possessing only the BH3 domain. J Biol Chem 2000;275:25255-61.
    • (2000) J Biol Chem , vol.275 , pp. 25255-25261
    • Bae, J.1    Leo, C.P.2    Hsu, S.Y.3    Hsueh, A.J.4
  • 139
    • 79960282729 scopus 로고    scopus 로고
    • Modulation of RNA splicing as a potential treatment for cancer
    • Bauman JA, Kole R. Modulation of RNA splicing as a potential treatment for cancer. Bioeng Bugs 2011;2:125-8.
    • (2011) Bioeng Bugs , vol.2 , pp. 125-128
    • Bauman, J.A.1    Kole, R.2
  • 140
    • 78049416081 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing regulation in cancer: Pathways and programs unhinged
    • David CJ, Manley JL. Alternative pre-mRNA splicing regulation in cancer: pathways and programs unhinged. Genes Dev 2010;24:2343-64.
    • (2010) Genes Dev , vol.24 , pp. 2343-2364
    • David, C.J.1    Manley, J.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.