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Volumn 32, Issue 7, 2012, Pages 1271-1283

A quantitative high-throughput in vitro splicing assay identifies inhibitors of spliceosome catalysis

Author keywords

[No Author keywords available]

Indexed keywords

1,4 HETEROCYCLIC QUINONE; 1,4 NAPHTHOQUINONE; 2 [(2 HYDROXYETHYL)THIOL] 3 METHYL 1,4 NAPTHOQUINONE; 2 CHLOROMETHYL, 3 METHYL 1,4 NAPTHOQUINONE; 2,3 BIS(METHYLTHIO) 1,4 NAPTHOQUINONE; 3 BENZOYLNAPTHO[1,2 B]FURAN 4,5 DIONE; ANTIBODY; BENZOTHIAZOLE 4,7 DIONE; BIOTIN; BN 82685; CELL EXTRACT; INITIATION FACTOR; INITIATION FACTOR 4AIII; MENADIONE; MESSENGER RNA; N (4 BIPHENYL) 3,4 BIS(2 HYDROXY ETHYLSULPHANYL)MALEIMIDE; NSC 95397; QUINONE DERIVATIVE; RNA; UNCLASSIFIED DRUG; 1,4-NAPHTHOQUINONE; BENZOQUINONE DERIVATIVE; NAPHTHOQUINONE; RNA PRECURSOR; THIAZOLE DERIVATIVE;

EID: 84859984478     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.05788-11     Document Type: Article
Times cited : (37)

References (65)
  • 1
    • 0031741144 scopus 로고    scopus 로고
    • The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein
    • Achsel T, Ahrens K, Brahms H, Teigelkamp S, Luhrmann R. 1998. The human U5-220kD protein (hPrp8) forms a stable RNA-free complex with several U5-specific proteins, including an RNA unwindase, a homologue of ribosomal elongation factor EF-2, and a novel WD-40 protein. Mol. Cell. Biol. 18:6756-6766.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6756-6766
    • Achsel, T.1    Ahrens, K.2    Brahms, H.3    Teigelkamp, S.4    Luhrmann, R.5
  • 2
    • 68849084041 scopus 로고    scopus 로고
    • Meayamycin inhibits pre-messenger RNA splicing and exhibits picomolar activity against multidrug-resistant cells
    • Albert BJ, et al. 2009. Meayamycin inhibits pre-messenger RNA splicing and exhibits picomolar activity against multidrug-resistant cells. Mol. Cancer Ther. 8:2308-2318.
    • (2009) Mol. Cancer Ther. , vol.8 , pp. 2308-2318
    • Albert, B.J.1
  • 3
    • 0030671163 scopus 로고    scopus 로고
    • Prp43: an RNA helicase-like factor involved in spliceosome disassembly
    • Arenas JE, Abelson JN. 1997. Prp43: an RNA helicase-like factor involved in spliceosome disassembly. Proc. Natl. Acad. Sci. U. S. A. 94:11798-11802.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 11798-11802
    • Arenas, J.E.1    Abelson, J.N.2
  • 4
    • 27144445082 scopus 로고    scopus 로고
    • The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity
    • Ballut L, et al. 2005. The exon junction core complex is locked onto RNA by inhibition of eIF4AIII ATPase activity. Nat. Struct. Mol. Biol. 12:861-869.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 861-869
    • Ballut, L.1
  • 5
    • 78649656777 scopus 로고    scopus 로고
    • Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis
    • Bessonov S, et al. 2010. Characterization of purified human Bact spliceosomal complexes reveals compositional and morphological changes during spliceosome activation and first step catalysis. RNA 16:2384-2403.
    • (2010) RNA , vol.16 , pp. 2384-2403
    • Bessonov, S.1
  • 6
    • 42249093677 scopus 로고    scopus 로고
    • Isolation of an active step I spliceosome and composition of its RNP core
    • Bessonov S, Anokhina M, Will CL, Urlaub H, Luhrmann R. 2008. Isolation of an active step I spliceosome and composition of its RNP core. Nature 452:846-850.
    • (2008) Nature , vol.452 , pp. 846-850
    • Bessonov, S.1    Anokhina, M.2    Will, C.L.3    Urlaub, H.4    Luhrmann, R.5
  • 7
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: new insights from global analyses
    • Blencowe BJ. 2006. Alternative splicing: new insights from global analyses. Cell 126:37-47.
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 8
    • 27644478392 scopus 로고    scopus 로고
    • Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1 and Prp4 kinase suggest a function in the control of the activation of spliceosomes in Schizosaccharomyces pombe
    • Bottner CA, Schmidt H, Vogel S, Michele M, Kaufer NF. 2005. Multiple genetic and biochemical interactions of Brr2, Prp8, Prp31, Prp1 and Prp4 kinase suggest a function in the control of the activation of spliceosomes in Schizosaccharomyces pombe. Curr. Genet. 48:151-161.
    • (2005) Curr. Genet. , vol.48 , pp. 151-161
    • Bottner, C.A.1    Schmidt, H.2    Vogel, S.3    Michele, M.4    Kaufer, N.F.5
  • 9
    • 27744539982 scopus 로고    scopus 로고
    • Inhibition of human tumor cell growth in vivo by an orally bioavailable inhibitor of CDC25 phosphatases
    • Brezak MC, et al. 2005. Inhibition of human tumor cell growth in vivo by an orally bioavailable inhibitor of CDC25 phosphatases. Mol. Cancer Ther. 4:1378-1387.
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1378-1387
    • Brezak, M.C.1
  • 10
    • 4344594832 scopus 로고    scopus 로고
    • Discovery and characterization of novel small molecule inhibitors of human Cdc25B dual specificity phosphatase
    • Brisson M, et al. 2004. Discovery and characterization of novel small molecule inhibitors of human Cdc25B dual specificity phosphatase. Mol. Pharmacol. 66:824-833.
    • (2004) Mol. Pharmacol. , vol.66 , pp. 824-833
    • Brisson, M.1
  • 11
    • 1542361776 scopus 로고    scopus 로고
    • eIF4A3 is a novel component of the exon junction complex
    • Chan CC, et al. 2004. eIF4A3 is a novel component of the exon junction complex. RNA 10:200-209.
    • (2004) RNA , vol.10 , pp. 200-209
    • Chan, C.C.1
  • 12
    • 0141924550 scopus 로고    scopus 로고
    • The Prp19p-associated complex in spliceosome activation
    • Chan SP, Kao DI, Tsai WY, Cheng SC. 2003. The Prp19p-associated complex in spliceosome activation. Science 302:279-282.
    • (2003) Science , vol.302 , pp. 279-282
    • Chan, S.P.1    Kao, D.I.2    Tsai, W.Y.3    Cheng, S.C.4
  • 15
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss G, Kim VN, Kataoka N. 2002. Messenger-RNA-binding proteins and the messages they carry. Nat. Rev. Mol. Cell Biol. 3:195-205.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 16
    • 33746606369 scopus 로고    scopus 로고
    • Utilization of host SR protein kinases and RNAsplicing machinery during viral replication
    • Fukuhara T, et al. 2006. Utilization of host SR protein kinases and RNAsplicing machinery during viral replication. Proc. Natl. Acad. Sci. U. S. A. 103:11329-11333.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11329-11333
    • Fukuhara, T.1
  • 17
    • 0027238743 scopus 로고
    • The biochemical defects of prp4-1 and prp6-1 yeast splicing mutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP
    • Galisson F, Legrain P. 1993. The biochemical defects of prp4-1 and prp6-1 yeast splicing mutants reveal that the PRP6 protein is required for the accumulation of the [U4/U6.U5] tri-snRNP. Nucleic Acids Res. 21: 1555-1562.
    • (1993) Nucleic Acids Res , vol.21 , pp. 1555-1562
    • Galisson, F.1    Legrain, P.2
  • 18
    • 29144463738 scopus 로고    scopus 로고
    • Alternative splicing: a new drug target of the postgenome era
    • Hagiwara M. 2005. Alternative splicing: a new drug target of the postgenome era. Biochim. Biophys. Acta 1754:324-331.
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 324-331
    • Hagiwara, M.1
  • 19
  • 20
    • 0042671357 scopus 로고    scopus 로고
    • Pre-mRNA splicing: awash in a sea of proteins
    • Jurica MS, Moore MJ. 2003. Pre-mRNA splicing: awash in a sea of proteins. Mol. Cell 12:5-14.
    • (2003) Mol. Cell , vol.12 , pp. 5-14
    • Jurica, M.S.1    Moore, M.J.2
  • 21
    • 34548095157 scopus 로고    scopus 로고
    • Spliceostatin A targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA
    • Kaida D, et al. 2007. Spliceostatin A targets SF3b and inhibits both splicing and nuclear retention of pre-mRNA. Nat. Chem. Biol. 3:576-583.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 576-583
    • Kaida, D.1
  • 22
    • 33746075605 scopus 로고    scopus 로고
    • PM-20, a novel inhibitor of Cdc25A, induces extracellular signal-regulated kinase 1/2 phosphorylation and inhibits hepatocellular carcinoma growth in vitro and in vivo
    • Kar S, Wang M, Yao W, Michejda CJ, Carr BI. 2006. PM-20, a novel inhibitor of Cdc25A, induces extracellular signal-regulated kinase 1/2 phosphorylation and inhibits hepatocellular carcinoma growth in vitro and in vivo. Mol. Cancer Ther. 5:1511-1519.
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1511-1519
    • Kar, S.1    Wang, M.2    Yao, W.3    Michejda, C.J.4    Carr, B.I.5
  • 23
    • 84934444843 scopus 로고    scopus 로고
    • Preparation of efficient splicing extracts from whole cells, nuclei, and cytoplasmic fractions
    • Kataoka N, Dreyfuss G. 2008. Preparation of efficient splicing extracts from whole cells, nuclei, and cytoplasmic fractions. Methods Mol. Biol. 488:357-365.
    • (2008) Methods Mol. Biol. , vol.488 , pp. 357-365
    • Kataoka, N.1    Dreyfuss, G.2
  • 24
    • 1342325392 scopus 로고    scopus 로고
    • A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex
    • Kataoka N, Dreyfuss G. 2004. A simple whole cell lysate system for in vitro splicing reveals a stepwise assembly of the exon-exon junction complex. J. Biol. Chem. 279:7009-7013.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7009-7013
    • Kataoka, N.1    Dreyfuss, G.2
  • 25
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • Kataoka N, et al. 2000. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol. Cell 6:673-682.
    • (2000) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1
  • 26
    • 0029965552 scopus 로고    scopus 로고
    • Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing
    • Kim SH, Lin RJ. 1996. Spliceosome activation by PRP2 ATPase prior to the first transesterification reaction of pre-mRNA splicing. Mol. Cell. Biol. 16:6810-6819.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6810-6819
    • Kim, S.H.1    Lin, R.J.2
  • 27
    • 0035901565 scopus 로고    scopus 로고
    • The Y14 protein communicates to the cytoplasm the position of exon-exon junctions
    • Kim VN, et al. 2001. The Y14 protein communicates to the cytoplasm the position of exon-exon junctions. EMBO J. 20:2062-2068.
    • (2001) EMBO J , vol.20 , pp. 2062-2068
    • Kim, V.N.1
  • 28
    • 0022549635 scopus 로고
    • Electrophoretic separation of complexes involved in the splicing of precursors to mRNAs
    • Konarska MM, Sharp PA. 1986. Electrophoretic separation of complexes involved in the splicing of precursors to mRNAs. Cell 46:845-855.
    • (1986) Cell , vol.46 , pp. 845-855
    • Konarska, M.M.1    Sharp, P.A.2
  • 29
    • 34548104659 scopus 로고    scopus 로고
    • Splicing factor SF3b as a target of the antitumor natural product pladienolide
    • Kotake Y, et al. 2007. Splicing factor SF3b as a target of the antitumor natural product pladienolide. Nat. Chem. Biol. 3:570-575.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 570-575
    • Kotake, Y.1
  • 30
    • 0026794668 scopus 로고
    • The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences
    • Krawczak M, Reiss J, Cooper DN. 1992. The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: causes and consequences. Hum. Genet. 90:41-54.
    • (1992) Hum. Genet. , vol.90 , pp. 41-54
    • Krawczak, M.1    Reiss, J.2    Cooper, D.N.3
  • 31
    • 58149092362 scopus 로고    scopus 로고
    • Stalling of spliceosome assembly at distinct stages by small-molecule inhibitors of protein acetylation and deacetylation
    • Kuhn AN, van Santen MA, Schwienhorst A, Urlaub H, Luhrmann R. 2009. Stalling of spliceosome assembly at distinct stages by small-molecule inhibitors of protein acetylation and deacetylation. RNA 15:153-175.
    • (2009) RNA , vol.15 , pp. 153-175
    • Kuhn, A.N.1    van Santen, M.A.2    Schwienhorst, A.3    Urlaub, H.4    Luhrmann, R.5
  • 32
    • 0035935711 scopus 로고    scopus 로고
    • Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25
    • Lazo JS, et al. 2001. Discovery and biological evaluation of a new family of potent inhibitors of the dual specificity protein phosphatase Cdc25. J. Med. Chem. 44:4042-4049.
    • (2001) J. Med. Chem. , vol.44 , pp. 4042-4049
    • Lazo, J.S.1
  • 33
    • 18344375627 scopus 로고    scopus 로고
    • Identification of a potent and selective pharmacophore for Cdc25 dual specificity phosphatase inhibitors
    • Lazo JS, et al. 2002. Identification of a potent and selective pharmacophore for Cdc25 dual specificity phosphatase inhibitors. Mol. Pharmacol. 61:720-728.
    • (2002) Mol. Pharmacol. , vol.61 , pp. 720-728
    • Lazo, J.S.1
  • 34
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exonexon junctions
    • Le Hir H, Izaurralde E, Maquat LE, Moore MJ. 2000. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exonexon junctions. EMBO J. 19:6860-6869.
    • (2000) EMBO J , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 35
    • 0037398519 scopus 로고    scopus 로고
    • How introns influence and enhance eukaryotic gene expression
    • Le Hir H, Nott A, Moore MJ. 2003. How introns influence and enhance eukaryotic gene expression. Trends Biochem. Sci. 28:215-220.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 215-220
    • Le Hir, H.1    Nott, A.2    Moore, M.J.3
  • 36
    • 0027096275 scopus 로고
    • Cantharidin-binding protein: identification as protein phosphatase 2A
    • Li YM, Casida JE. 1992. Cantharidin-binding protein: identification as protein phosphatase 2A. Proc. Natl. Acad. Sci. U. S. A. 89:11867-11870.
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 11867-11870
    • Li, Y.M.1    Casida, J.E.2
  • 37
    • 77950485320 scopus 로고    scopus 로고
    • The N terminus of Prp1 (Prp6/U5-102 K) is essential for spliceosome activation in vivo
    • Lutzelberger M, et al. 2010. The N terminus of Prp1 (Prp6/U5-102 K) is essential for spliceosome activation in vivo. Nucleic Acids Res. 38:1610-1622.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1610-1622
    • Lutzelberger, M.1
  • 38
    • 0037073946 scopus 로고    scopus 로고
    • Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome
    • Makarov EM, et al. 2002. Small nuclear ribonucleoprotein remodeling during catalytic activation of the spliceosome. Science 298:2205-2208.
    • (2002) Science , vol.298 , pp. 2205-2208
    • Makarov, E.M.1
  • 39
    • 0036500141 scopus 로고    scopus 로고
    • Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant retinitis pigmentosa, is required for U4/U6*U5 tri-snRNP formation and pre-mRNA splicing
    • Makarova OV, Makarov EM, Liu S, Vornlocher HP, Luhrmann R. 2002. Protein 61K, encoded by a gene (PRPF31) linked to autosomal dominant retinitis pigmentosa, is required for U4/U6*U5 tri-snRNP formation and pre-mRNA splicing. EMBO J. 21:1148-1157.
    • (2002) EMBO J , vol.21 , pp. 1148-1157
    • Makarova, O.V.1    Makarov, E.M.2    Liu, S.3    Vornlocher, H.P.4    Luhrmann, R.5
  • 40
    • 0742323558 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics
    • Maquat LE. 2004. Nonsense-mediated mRNA decay: splicing, translation and mRNP dynamics. Nat. Rev. Mol. Cell Biol. 5:89-99.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 89-99
    • Maquat, L.E.1
  • 41
    • 0026731973 scopus 로고
    • Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing
    • Mermoud JE, Cohen P, Lamond AI. 1992. Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucleic Acids Res. 20:5263-5269.
    • (1992) Nucleic Acids Res , vol.20 , pp. 5263-5269
    • Mermoud, J.E.1    Cohen, P.2    Lamond, A.I.3
  • 42
    • 2342655502 scopus 로고    scopus 로고
    • Manipulation of alternative splicing by a newly developed inhibitor of Clks
    • Muraki M, et al. 2004. Manipulation of alternative splicing by a newly developed inhibitor of Clks. J. Biol. Chem. 279:24246-24254.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24246-24254
    • Muraki, M.1
  • 43
    • 34250860714 scopus 로고    scopus 로고
    • Enzymes catalyzing protein folding and their cellular functions
    • Nagradova N. 2007. Enzymes catalyzing protein folding and their cellular functions. Curr. Protein Pept. Sci. 8:273-282.
    • (2007) Curr. Protein Pept. Sci. , vol.8 , pp. 273-282
    • Nagradova, N.1
  • 44
    • 0030466895 scopus 로고    scopus 로고
    • New antitumor substances, FR901463, FR901464 and FR901465. II. Activities against experimental tumors in mice and mechanism of action
    • Nakajima H, et al. 1996. New antitumor substances, FR901463, FR901464 and FR901465. II. Activities against experimental tumors in mice and mechanism of action. J. Antibiot. (Tokyo) 49:1204-1211.
    • (1996) J. Antibiot. (Tokyo) , vol.49 , pp. 1204-1211
    • Nakajima, H.1
  • 45
    • 57749093482 scopus 로고    scopus 로고
    • The biflavonoid isoginkgetin is a general inhibitor of Pre-mRNA splicing
    • O'Brien K, Matlin AJ, Lowell AM, Moore MJ. 2008. The biflavonoid isoginkgetin is a general inhibitor of Pre-mRNA splicing. J. Biol. Chem. 283:33147-33154.
    • (2008) J. Biol. Chem. , vol.283 , pp. 33147-33154
    • O'Brien, K.1    Matlin, A.J.2    Lowell, A.M.3    Moore, M.J.4
  • 46
    • 0035884180 scopus 로고    scopus 로고
    • Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506
    • Pilch B, et al. 2001. Specific inhibition of serine- and arginine-rich splicing factors phosphorylation, spliceosome assembly, and splicing by the antitumor drug NB-506. Cancer Res. 61:6876-6884.
    • (2001) Cancer Res , vol.61 , pp. 6876-6884
    • Pilch, B.1
  • 47
    • 4143124637 scopus 로고    scopus 로고
    • RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 disnRNPs in Cajal bodies
    • Schaffert N, Hossbach M, Heintzmann R, Achsel T, Luhrmann R. 2004. RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 disnRNPs in Cajal bodies. EMBO J. 23:3000-3009.
    • (2004) EMBO J , vol.23 , pp. 3000-3009
    • Schaffert, N.1    Hossbach, M.2    Heintzmann, R.3    Achsel, T.4    Luhrmann, R.5
  • 49
    • 76349122915 scopus 로고    scopus 로고
    • Human PRP4 kinase is required for stable tri-snRNP association during spliceosomal B complex formation
    • Schneider M, et al. 2010. Human PRP4 kinase is required for stable tri-snRNP association during spliceosomal B complex formation. Nat. Struct. Mol. Biol. 17:216-221.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 216-221
    • Schneider, M.1
  • 50
    • 33748415171 scopus 로고    scopus 로고
    • PP1/PP2A phosphatases are required for the second step of Pre-mRNA splicing and target specific snRNP proteins
    • Shi Y, Reddy B, Manley JL. 2006. PP1/PP2A phosphatases are required for the second step of Pre-mRNA splicing and target specific snRNP proteins. Mol. Cell 23:819-829.
    • (2006) Mol. Cell , vol.23 , pp. 819-829
    • Shi, Y.1    Reddy, B.2    Manley, J.L.3
  • 51
    • 1842577707 scopus 로고    scopus 로고
    • eIF4AIII binds splicedmRNAin the exon junction complex and is essential for nonsensemediated decay
    • Shibuya T, Tange TO, Sonenberg N, Moore MJ. 2004. eIF4AIII binds splicedmRNAin the exon junction complex and is essential for nonsensemediated decay. Nat. Struct. Mol. Biol. 11:346-351.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 346-351
    • Shibuya, T.1    Tange, T.O.2    Sonenberg, N.3    Moore, M.J.4
  • 52
    • 20844442133 scopus 로고    scopus 로고
    • Selective modification of alternative splicing by indole derivatives that target serine-arginine-rich protein splicing factors
    • Soret J, et al. 2005. Selective modification of alternative splicing by indole derivatives that target serine-arginine-rich protein splicing factors. Proc. Natl. Acad. Sci. U. S. A. 102:8764-8769.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8764-8769
    • Soret, J.1
  • 53
    • 0032489021 scopus 로고    scopus 로고
    • Mechanical devices of the spliceosome: motors, clocks, springs, and things
    • Staley JP, Guthrie C. 1998. Mechanical devices of the spliceosome: motors, clocks, springs, and things. Cell 92:315-326.
    • (1998) Cell , vol.92 , pp. 315-326
    • Staley, J.P.1    Guthrie, C.2
  • 54
    • 49649108878 scopus 로고    scopus 로고
    • A highthroughput screening strategy identifies cardiotonic steroids as alternative splicing modulators
    • Stoilov P, Lin CH, Damoiseaux R, Nikolic J, Black DL. 2008. A highthroughput screening strategy identifies cardiotonic steroids as alternative splicing modulators. Proc. Natl. Acad. Sci. U. S. A. 105:11218-11223.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11218-11223
    • Stoilov, P.1    Lin, C.H.2    Damoiseaux, R.3    Nikolic, J.4    Black, D.L.5
  • 55
    • 0024117031 scopus 로고
    • RNA binding specificity of hnRNP proteins: a subset bind to the 3′ end of introns
    • Swanson MS, Dreyfuss G. 1988. RNA binding specificity of hnRNP proteins: a subset bind to the 3′ end of introns. EMBO J. 7:3519-3529.
    • (1988) EMBO J , vol.7 , pp. 3519-3529
    • Swanson, M.S.1    Dreyfuss, G.2
  • 56
    • 0034163387 scopus 로고    scopus 로고
    • Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue
    • Tamura K, et al. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Res. 60:1317-1325.
    • (2000) Cancer Res , vol.60 , pp. 1317-1325
    • Tamura, K.1
  • 57
    • 15744375510 scopus 로고    scopus 로고
    • Selective inhibition of topoisomerase I and various steps of spliceosome assembly by diospyrin derivatives
    • Tazi J, et al. 2005. Selective inhibition of topoisomerase I and various steps of spliceosome assembly by diospyrin derivatives. Mol. Pharmacol. 67:1186-1194.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1186-1194
    • Tazi, J.1
  • 59
    • 22744449772 scopus 로고    scopus 로고
    • The spliceosome: a novel multifaceted target for therapy
    • Tazi J, Durand S, Jeanteur P. 2005. The spliceosome: a novel multifaceted target for therapy. Trends Biochem. Sci. 30:469-478.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 469-478
    • Tazi, J.1    Durand, S.2    Jeanteur, P.3
  • 60
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: design principles of a dynamic RNP machine
    • Wahl MC, Will CL, Luhrmann R. 2009. The spliceosome: design principles of a dynamic RNP machine. Cell 136:701-718.
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 61
    • 20744455958 scopus 로고    scopus 로고
    • The survival of motor neurons protein determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy
    • Wan L, et al. 2005. The survival of motor neurons protein determines the capacity for snRNP assembly: biochemical deficiency in spinal muscular atrophy. Mol. Cell. Biol. 25:5543-5551.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5543-5551
    • Wan, L.1
  • 62
    • 47349113209 scopus 로고    scopus 로고
    • Inactivation of the SMN complex by oxidative stress
    • Wan L, Ottinger E, Cho S, Dreyfuss G. 2008. Inactivation of the SMN complex by oxidative stress. Mol. Cell 31:244-254.
    • (2008) Mol. Cell , vol.31 , pp. 244-254
    • Wan, L.1    Ottinger, E.2    Cho, S.3    Dreyfuss, G.4
  • 63
    • 56549101959 scopus 로고    scopus 로고
    • Alternative isoform regulation in human tissue transcriptomes
    • Wang ET, et al. 2008. Alternative isoform regulation in human tissue transcriptomes. Nature 456:470-476.
    • (2008) Nature , vol.456 , pp. 470-476
    • Wang, E.T.1
  • 65
    • 77949408107 scopus 로고    scopus 로고
    • Rapid-response splicing reporter screens identify differential regulators of constitutive and alternative splicing
    • Younis I, et al. 2010. Rapid-response splicing reporter screens identify differential regulators of constitutive and alternative splicing. Mol. Cell. Biol. 30:1718-1728.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1718-1728
    • Younis, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.