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Volumn 10, Issue 11, 2009, Pages 741-754

Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBONUCLEOPROTEIN; RNA POLYMERASE II;

EID: 70350569286     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2777     Document Type: Review
Times cited : (972)

References (166)
  • 1
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black, D. L. Mechanisms of alternative pre-messenger RNA splicing. Annu. Rev. Biochem. 72, 291-336 (2003).
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 291-336
    • Black, D.L.1
  • 2
    • 60349104299 scopus 로고    scopus 로고
    • The spliceosome: Design principles of a dynamic RNP machine
    • Wahl, M. C., Will, C. L. & Luhrmann, R. The spliceosome: design principles of a dynamic RNP machine. Cell 136, 701-718 (2009).
    • (2009) Cell , vol.136 , pp. 701-718
    • Wahl, M.C.1    Will, C.L.2    Luhrmann, R.3
  • 3
    • 0030696675 scopus 로고    scopus 로고
    • The splicing factor BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC
    • Berglund, J. A., Chua, K., Abovich, N., Reed, R. & Rosbash, M. The splicing factor BBP interacts specifically with the pre-mRNA branchpoint sequence UACUAAC. Cell 89, 781-787 (1997).
    • (1997) Cell , vol.89 , pp. 781-787
    • Berglund, J.A.1    Chua, K.2    Abovich, N.3    Reed, R.4    Rosbash, M.5
  • 4
    • 0024408832 scopus 로고
    • Identification purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor
    • Zamore, P. D. & Green, M. R. Identification, purification, and biochemical characterization of U2 small nuclear ribonucleoprotein auxiliary factor. Proc. Natl Acad. Sci. USA 86, 9243-9247 (1989).
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 9243-9247
    • Zamore, P.D.1    Green, M.R.2
  • 5
    • 0024747748 scopus 로고
    • Mammalian U2 snRNP has a sequence-specific RNA-binding activity
    • Nelson, K. K. & Green, M. R. Mammalian U2 snRNP has a sequence-specific RNA-binding activity. Genes D e v. 3, 1562-1571 (1989).
    • (1989) Genes D e V. , vol.3 , pp. 1562-1571
    • Nelson, K.K.1    Green, M.R.2
  • 6
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley, B. R. Sorting out the complexity of SR protein functions. RNA 6, 1197-1211 (2000).
    • (2000) RNA , vol.6 , pp. 1197-1211
    • Graveley, B.R.1
  • 7
    • 0033152209 scopus 로고    scopus 로고
    • Determinants of SR protein specificity
    • Tacke, R. & Manley, J. L. Determinants of SR protein specificity. Curr. Opin. Cell Biol. 11, 358-362 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 358-362
    • Tacke, R.1    Manley, J.L.2
  • 8
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: Master regulators of gene expression
    • Long, J. C. & Caceres, J. F. The SR protein family of splicing factors: master regulators of gene expression. Biochem. J. 417, 15-27 (2009).
    • (2009) Biochem. J. , vol.417 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 9
    • 0034256020 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing: The logic of combinatorial control
    • Smith, C. W. & Valcarcel, J. Alternative pre-mRNA splicing: the logic of combinatorial control. Trends Biochem. Sci. 25, 381-388 (2000).
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 381-388
    • Smith, C.W.1    Valcarcel, J.2
  • 10
    • 0036512117 scopus 로고    scopus 로고
    • Messenger-RNA-binding proteins and the messages they carry
    • Dreyfuss, G., Kim, V. N. & Kataoka, N. Messenger-RNA-binding proteins and the messages they carry. Nature Rev. Mol. Cell Biol. 3, 195-205 (2002).
    • (2002) Nature Rev. Mol. Cell Biol. , vol.3 , pp. 195-205
    • Dreyfuss, G.1    Kim, V.N.2    Kataoka, N.3
  • 11
    • 33749056769 scopus 로고    scopus 로고
    • An RNA map predicting Nova-dependent splicing regulation
    • Ule, J. et al. An RNA map predicting Nova-dependent splicing regulation. Nature 444, 580-586 (2006).
    • (2006) Nature , vol.444 , pp. 580-586
    • Ule, J.1
  • 12
    • 21244469877 scopus 로고
    • Intronic CA-repeat and CA-rich elements: A new class of regulators of mammalian alternative splicing
    • Hui, J. et al. Intronic CA-repeat and CA-rich elements: a new class of regulators of mammalian alternative splicing. EMBO J. 24, 1988-1998 (2005).
    • (1988) EMBO J. , vol.24 , pp. 2005
    • Hui, J.1
  • 13
    • 59649107040 scopus 로고    scopus 로고
    • An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells
    • Yeo, G. W. et al. An RNA code for the FOX2 splicing regulator revealed by mapping RNA-protein interactions in stem cells. Nature Struct. Mol. Biol. 16, 130-137 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 130-137
    • Yeo, G.W.1
  • 14
    • 50249176008 scopus 로고    scopus 로고
    • HnRNP H and hnRNP F complex with Fox2 to silence fibroblast growth factor receptor 2 exon IIIc
    • Mauger, D. M., Lin, C. & Garcia-Blanco, M. A. hnRNP H and hnRNP F complex with Fox2 to silence fibroblast growth factor receptor 2 exon IIIc. Mol. Cell. Biol. 28, 5403-5419 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5403-5419
    • Mauger, D.M.1    Lin, C.2    Garcia-Blanco, M.A.3
  • 15
    • 33749515475 scopus 로고    scopus 로고
    • An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition
    • House, A. E. & Lynch, K. W. An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition. Nature Struct. Mol. Biol. 13, 937-944 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 937-944
    • House, A.E.1    Lynch, K.W.2
  • 16
    • 38849187162 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
    • Sharma, S., Kohlstaedt, L. A., Damianov, A., Rio, D. C. & Black, D. L. Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nature Struct. Mol. Biol. 15, 183-191 (2008)
    • (2008) Nature Struct. Mol. Biol. , vol.15 , pp. 183-191
    • Sharma, S.1    Kohlstaedt, L.A.2    Damianov, A.3    Rio, D.C.4    Black, D.L.5
  • 17
    • 70350569859 scopus 로고    scopus 로고
    • note
    • This study shows that PTB inhibits Src exon N1 inclusion by preventing the transition from an exon-definition to an intron-definition complex and analyses the protein composition of different complexes.
  • 18
    • 0037013146 scopus 로고    scopus 로고
    • Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45
    • Lallena, M. J., Chalmers, K. J., Llamazares, S., Lamond, A. I. & Valcarcel, J. Splicing regulation at the second catalytic step by Sex-lethal involves 3′ splice site recognition by SPF45. Cell 109, 285-296 (2002).
    • (2002) Cell , vol.109 , pp. 285-296
    • Lallena, M.J.1    Chalmers, K.J.2    Llamazares, S.3    Lamond, A.I.4    Valcarcel, J.5
  • 19
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/SNF subunit Brm is a regulator of alternative splicing
    • Batsche, E., Yaniv, M. & Muchardt, C. The human SWI/SNF subunit Brm is a regulator of alternative splicing. Nature Struct. Mol. Biol. 13, 22-29 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 22-29
    • Batsche, E.1    Yaniv, M.2    Muchardt, C.3
  • 20
    • 33750596100 scopus 로고    scopus 로고
    • RNA polymerase II C-terminal domain mediates regulation of alternative splicing by SRp20
    • de la Mata, M. & Kornblihtt, A. R. RNA polymerase II C-terminal domain mediates regulation of alternative splicing by SRp20. Nature Struct. Mol. Biol. 13, 973-980 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 973-980
    • De La Mata, M.1    Kornblihtt, A.R.2
  • 21
    • 36249027156 scopus 로고    scopus 로고
    • Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing
    • Sims, R. J. 3rd et al. Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing. Mol. Cell 28, 665-676 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 665-676
    • Sims Iii, R.J.1
  • 23
    • 54049093628 scopus 로고    scopus 로고
    • Promoter-driven splicing regulation in fission yeast
    • Moldon, A. et al. Promoter-driven splicing regulation in fission yeast. Nature 455, 997-1000 (2008).
    • (2008) Nature , vol.455 , pp. 997-1000
    • Moldon, A.1
  • 24
    • 0035252410 scopus 로고    scopus 로고
    • Alternative splicing: Increasing diversity in the proteomic world
    • Graveley, B. R. Alternative splicing: increasing diversity in the proteomic world. Trends Genet. 17, 100-107 (2001)
    • (2001) Trends Genet , vol.17 , pp. 100-107
    • Graveley, B.R.1
  • 25
    • 70350568699 scopus 로고    scopus 로고
    • Blencowe, B. J. & Graveley, B. R. (eds) Springer, the Netherlands
    • Blencowe, B. J. & Graveley, B. R. (eds) Alternative Splicing in the Postgenomic Era. (Springer, the Netherlands, 2007).
    • (2007) Alternative Splicing in the Postgenomic Era
  • 26
    • 0034906754 scopus 로고    scopus 로고
    • Alternative RNA splicing in the nervous system
    • Grabowski, P. J. & Black, D. L. Alternative RNA splicing in the nervous system. Prog. Neurobiol. 65, 289-308 (2001).
    • (2001) Prog. Neurobiol , vol.65 , pp. 289-308
    • Grabowski, P.J.1    Black, D.L.2
  • 27
    • 8644278829 scopus 로고    scopus 로고
    • Identification of alternative splicing regulators by RNA interference in Drosophila
    • Park, J. W., Parisky, K., Celotto, A. M., Reenan, R. A. & Graveley, B. R. Identification of alternative splicing regulators by RNA interference in Drosophila. Proc. Natl Acad. Sci. USA 101, 15974-15979 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 15974-15979
    • Park, J.W.1    Parisky, K.2    Celotto, A.M.3    Reenan, R.A.4    Graveley, B.R.5
  • 28
    • 43049168361 scopus 로고    scopus 로고
    • SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing
    • Zhang, Z. et al. SMN deficiency causes tissue-specific perturbations in the repertoire of snRNAs and widespread defects in splicing. Cell 133, 585-600 (2008).
    • (2008) Cell , vol.133 , pp. 585-600
    • Zhang, Z.1
  • 29
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: New insights from global analyses
    • Blencowe, B. J. Alternative splicing: new insights from global analyses. Cell 126, 37-47 (2006).
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 30
    • 56549101959 scopus 로고    scopus 로고
    • Alternative isoform regulation in human tissue transcriptomes
    • Wang, E. T. et al. Alternative isoform regulation in human tissue transcriptomes. Nature 456, 470-476 (2008).
    • (2008) Nature , vol.456 , pp. 470-476
    • Wang, E.T.1
  • 31
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan, Q., Shai, O., Lee, L. J., Frey, B. J. & Blencowe, B. J. Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nature Genet. 40, 1413-1415 (2008).
    • (2008) Nature Genet. , vol.40 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 32
    • 56749164864 scopus 로고    scopus 로고
    • Expression of 24,426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines
    • Castle, J. C. et al. Expression of 24,426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines. Nature Genet. 40, 1416-1425 (2008).
    • (2008) Nature Genet. , vol.40 , pp. 1416-1425
    • Castle, J.C.1
  • 33
    • 47649124124 scopus 로고    scopus 로고
    • A global view of gene activity and alternative splicing by deep sequencing of the human transcriptome
    • Sultan, M. et al. A global view of gene activity and alternative splicing by deep sequencing of the human transcriptome. Science 321, 956-960 (2008).
    • (2008) Science , vol.321 , pp. 956-960
    • Sultan, M.1
  • 35
    • 0028895417 scopus 로고
    • Exon recognition in vertebrate splicing
    • Berget, S. M. Exon recognition in vertebrate splicing. J. Biol. Chem. 270, 2411-2414 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 2411-2414
    • Berget, S.M.1
  • 36
    • 4143078172 scopus 로고    scopus 로고
    • Commitment to splice site pairing coincides with A complex formation
    • Lim, S. R. & Hertel, K. J. Commitment to splice site pairing coincides with A complex formation. Mol. Cell 15, 477-483 (2004).
    • (2004) Mol. Cell , vol.15 , pp. 477-483
    • Lim, S.R.1    Hertel, K.J.2
  • 37
    • 59449100357 scopus 로고    scopus 로고
    • Spliceosome assembly pathways for different types of alternative splicing converge during commitment to splice site pairing in the A complex
    • Kotlajich, M. V., Crabb, T. L. & Hertel, K. J. Spliceosome assembly pathways for different types of alternative splicing converge during commitment to splice site pairing in the A complex. Mol. Cell. Biol. 29, 1072-1082 (2009).
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1072-1082
    • Kotlajich, M.V.1    Crabb, T.L.2    Hertel, K.J.3
  • 38
    • 0032740121 scopus 로고    scopus 로고
    • Identification of a bidirectional splicing enhancer: Differential involvement of SR proteins in 5′ or 3′ splice site activation
    • Bourgeois, C. F., Popielarz, M., Hildwein, G. & Stevenin, J. Identification of a bidirectional splicing enhancer: differential involvement of SR proteins in 5′ or 3′ splice site activation. Mol. Cell. Biol. 19, 7347-7356 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7347-7356
    • Bourgeois, C.F.1    Popielarz, M.2    Hildwein, G.3    Stevenin, J.4
  • 39
    • 0029665533 scopus 로고    scopus 로고
    • The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing
    • Zuo, P. & Maniatis, T. The splicing factor U2AF35 mediates critical protein-protein interactions in constitutive and enhancer-dependent splicing. Genes Dev. 10, 1356-1368 (1996).
    • (1996) Genes Dev. , vol.10 , pp. 1356-1368
    • Zuo, P.1    Maniatis, T.2
  • 40
    • 53549089314 scopus 로고    scopus 로고
    • Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator
    • Feng, Y., Chen, M. & Manley, J. L. Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator. Nature Struct. Mol. Biol. 15, 1040-1048 (2008).
    • (2008) Nature Struct. Mol. Biol. , vol.15 , pp. 1040-1048
    • Feng, Y.1    Chen, M.2    Manley, J.L.3
  • 41
    • 0034743627 scopus 로고    scopus 로고
    • The role of U2AF35 and U2AF65 in enhancer-dependent splicing
    • Graveley, B. R., Hertel, K. J. & Maniatis, T. The role of U2AF35 and U2AF65 in enhancer-dependent splicing. RNA 7, 806-818 (2001).
    • (2001) RNA , vol.7 , pp. 806-818
    • Graveley, B.R.1    Hertel, K.J.2    Maniatis, T.3
  • 42
    • 0028289188 scopus 로고
    • Protein-protein interactions and 5′-splice-site recognition in mammalian mRNA precursors
    • Kohtz, J. D. et al. Protein-protein interactions and 5′-splice-site recognition in mammalian mRNA precursors. Nature 368, 119-124 (1994).
    • (1994) Nature , vol.368 , pp. 119-124
    • Kohtz, J.D.1
  • 43
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu, J. Y. & Maniatis, T. Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75, 1061-1070 (1993).
    • (1993) Cell , vol.75 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 44
    • 0031042396 scopus 로고    scopus 로고
    • Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing
    • Xiao, S. H. & Manley, J. L. Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing. Genes Dev. 11, 334-344 (1997).
    • (1997) Genes Dev. , vol.11 , pp. 334-344
    • Xiao, S.H.1    Manley, J.L.2
  • 45
    • 33750053338 scopus 로고    scopus 로고
    • In vivo requirement of the small subunit of U2AF for recognition of a weak 3′ splice site
    • Pacheco, T. R., Coelho, M. B., Desterro, J. M., Mollet, I. & Carmo-Fonseca, M. In vivo requirement of the small subunit of U2AF for recognition of a weak 3′ splice site. Mol. Cell. Biol. 26, 8183-8190 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8183-8190
    • Pacheco, T.R.1    Coelho, M.B.2    Desterro, J.M.3    Mollet, I.4    Carmo-Fonseca, M.5
  • 46
    • 0035846545 scopus 로고    scopus 로고
    • Multiple interactions between SRm160 and SR family proteins in enhancer-dependent splicing and development of C. elegans
    • Longman, D. et al. Multiple interactions between SRm160 and SR family proteins in enhancer-dependent splicing and development of C. elegans. Curr. Biol. 11, 1923-1933 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1923-1933
    • Longman, D.1
  • 47
    • 0033984807 scopus 로고    scopus 로고
    • The SRm160/300 splicing coactivator subunits
    • Blencowe, B. J. et al. The SRm160/300 splicing coactivator subunits. RNA 6, 111-120 (2000).
    • (2000) RNA , vol.6 , pp. 111-120
    • Blencowe, B.J.1
  • 48
    • 0032914520 scopus 로고    scopus 로고
    • Functions of SR and Tra2 proteins in pre-mRNA splicing regulation
    • Tacke, R. & Manley, J. L. Functions of SR and Tra2 proteins in pre-mRNA splicing regulation. Proc. Soc. Exp. Biol. Med. 220, 59-63 (1999).
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.220 , pp. 59-63
    • Tacke, R.1    Manley, J.L.2
  • 49
    • 23744492690 scopus 로고    scopus 로고
    • Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition
    • Izquierdo, J. M. et al. Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol. Cell 19, 475-484 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 475-484
    • Izquierdo, J.M.1
  • 50
    • 0037121924 scopus 로고    scopus 로고
    • The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites
    • Forch, P., Puig, O., Martinez, C., Seraphin, B. & Valcarcel, J. The splicing regulator TIA-1 interacts with U1-C to promote U1 snRNP recruitment to 5′ splice sites. EMBO J. 21, 6882-6892 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6882-6892
    • Forch, P.1    Puig, O.2    Martinez, C.3    Seraphin, B.4    Valcarcel, J.5
  • 51
    • 38949098164 scopus 로고    scopus 로고
    • Signal-regulated pre-mRNA occupancy by the general splicing factor U2AF
    • Tisserant, A. & Konig, H. Signal-regulated pre-mRNA occupancy by the general splicing factor U2AF. PLoS ONE 3, e1418 (2008).
    • (2008) PLoS ONE , vol.3
    • Tisserant, A.1    Konig, H.2
  • 52
    • 0032561190 scopus 로고    scopus 로고
    • Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing
    • DOI 10.1074/jbc.273.43.27761
    • Yang, L., Embree, L. J., Tsai, S. & Hickstein, D. D. Oncoprotein TLS interacts with serine-arginine proteins involved in RNA splicing. J. Biol. Chem. 273, 27761-27764 (1998). (Pubitemid 28496059)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.43 , pp. 27761-27764
    • Yang, L.1    Embree, L.J.2    Tsai, S.3    Hickstein, D.D.4
  • 53
    • 0032713422 scopus 로고    scopus 로고
    • And characterization of two neural-salient serine/arginine-rich (NSSR) proteins involved in the regulation of alternative splicing in neurones
    • Komatsu, M., Kominami, E., Arahata, K. & Tsukahara, T. Cloning and characterization of two neural-salient serine/arginine-rich (NSSR) proteins involved in the regulation of alternative splicing in neurones. Genes Cells 4, 593-606 (1999).
    • (1999) Genes Cells , vol.4 , pp. 593-606
    • Komatsu, M.1    Kominami, E.2    Arahata, K.3    Cloning, T.T.4
  • 54
    • 0035966063 scopus 로고    scopus 로고
    • Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing
    • Cowper, A. E., Caceres, J. F., Mayeda, A. & Screaton, G. R. Serine-arginine (SR) protein-like factors that antagonize authentic SR proteins and regulate alternative splicing. J. Biol. Chem. 276, 48908-48914 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48908-48914
    • Cowper, A.E.1    Caceres, J.F.2    Mayeda, A.3    Screaton, G.R.4
  • 55
    • 0036848091 scopus 로고    scopus 로고
    • The SR protein SRp38 represses splicing in M phase cells
    • Shin, C. & Manley, J. L. The SR protein SRp38 represses splicing in M phase cells. Cell 111, 407-417 (2002).
    • (2002) Cell , vol.111 , pp. 407-417
    • Shin, C.1    Manley, J.L.2
  • 56
    • 1142310938 scopus 로고    scopus 로고
    • Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock
    • Shin, C., Feng, Y. & Manley, J. L. Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock. Nature 427, 553-558 (2004).
    • (2004) Nature , vol.427 , pp. 553-558
    • Shin, C.1    Feng, Y.2    Manley, J.L.3
  • 57
    • 0025346111 scopus 로고
    • Purification and characterization of pre-mRNA splicing factor SF2 from HeLa cells
    • Krainer, A. R., Conway, G. C. & Kozak, D. Purification and characterization of pre-mRNA splicing factor SF2 from HeLa cells. Genes Dev. 4, 1158-1171 (1990).
    • (1990) Genes Dev. , vol.4 , pp. 1158-1171
    • Krainer, A.R.1    Conway, G.C.2    Kozak, D.3
  • 58
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh, R., Valcarcel, J. & Green, M. R. Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science 268, 1173-1176 (1995).
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcarcel, J.2    Green, M.R.3
  • 59
    • 32344437827 scopus 로고    scopus 로고
    • Novel modes of splicing repression by PTB
    • Spellman, R. & Smith, C. W. Novel modes of splicing repression by PTB. Trends Biochem. Sci. 31, 73-76 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 73-76
    • Spellman, R.1    Smith, C.W.2
  • 60
    • 33845225902 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein (PTB) represses splicing of exon 6B from the β-tropomyosin pre-mRNA by directly interfering with the binding of the U2AF65 subunit
    • Sauliere, J., Sureau, A., Expert-Bezancon, A. & Marie, J. The polypyrimidine tract binding protein (PTB) represses splicing of exon 6B from the β-tropomyosin pre-mRNA by directly interfering with the binding of the U2AF65 subunit. Mol. Cell. Biol. 26, 8755-8769 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8755-8769
    • Sauliere, J.1    Sureau, A.2    Expert-Bezancon, A.3    Marie, J.4
  • 61
    • 0035886048 scopus 로고    scopus 로고
    • The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element
    • Tange, T. O., Damgaard, C. K., Guth, S., Valcarcel, J. & Kjems, J. The hnRNP A1 protein regulates HIV-1 tat splicing via a novel intron silencer element. EMBO J. 20, 5748-5758 (2001).
    • (2001) EMBO J. , vol.20 , pp. 5748-5758
    • Tange, T.O.1    Damgaard, C.K.2    Guth, S.3    Valcarcel, J.4    Kjems, J.5
  • 62
    • 50249117753 scopus 로고    scopus 로고
    • Repression of prespliceosome complex formation at two distinct steps by Fox-1/ Fox-2 proteins
    • Zhou, H. L. & Lou, H. Repression of prespliceosome complex formation at two distinct steps by Fox-1/ Fox-2 proteins. Mol. Cell. Biol. 28, 5507-5516 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5507-5516
    • Zhou, H.L.1    Lou, H.2
  • 63
    • 38949098620 scopus 로고    scopus 로고
    • Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA
    • Zhu, H., Hinman, M. N., Hasman, R. A., Mehta, P. & Lou, H. Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA. Mol. Cell. Biol. 28, 1240-1251 (2008).
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 1240-1251
    • Zhu, H.1    Hinman, M.N.2    Hasman, R.A.3    Mehta, P.4    Lou, H.5
  • 64
    • 0041665176 scopus 로고    scopus 로고
    • A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy
    • Kashima, T. & Manley, J. L. A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy. Nature Genet. 34, 460-463 (2003).
    • (2003) Nature Genet. , vol.34 , pp. 460-463
    • Kashima, T.1    Manley, J.L.2
  • 65
    • 62549087007 scopus 로고    scopus 로고
    • Differential 3′ splice site recognition of SMN1 and SMN2 transcripts by U2AF and U2 snRNP
    • Martins de Araujo, M., Bonnal, S., Hastings, M. L., Krainer, A. R. & Valcarcel, J. Differential 3′ splice site recognition of SMN1 and SMN2 transcripts by U2AF and U2 snRNP. RNA 15, 515-523 (2009).
    • (2009) RNA , vol.15 , pp. 515-523
    • Martins De Araujo, M.1    Bonnal, S.2    Hastings, M.L.3    Krainer, A.R.4    Valcarcel, J.5
  • 66
    • 23744484618 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein blocks the 5′ splice site-dependent assembly of U2AF and the prespliceosomal e complex
    • Sharma, S., Falick, A. M. & Black, D. L. Polypyrimidine tract binding protein blocks the 5′ splice site-dependent assembly of U2AF and the prespliceosomal E complex. Mol. Cell 19, 485-496 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 485-496
    • Sharma, S.1    Falick, A.M.2    Black, D.L.3
  • 67
    • 0036849108 scopus 로고    scopus 로고
    • HnRNP A1 controls HIV-1 mRNA splicing through cooperative binding to intron and exon splicing silencers in the context of a conserved secondary structure
    • Damgaard, C. K., Tange, T. O. & Kjems, J. hnRNP A1 controls HIV-1 mRNA splicing through cooperative binding to intron and exon splicing silencers in the context of a conserved secondary structure. RNA 8, 1401-1415 (2002).
    • (2002) RNA , vol.8 , pp. 1401-1415
    • Damgaard, C.K.1    Tange, T.O.2    Kjems, J.3
  • 68
    • 0036674179 scopus 로고    scopus 로고
    • High-affinity hnRNP A1 binding sites and duplex-forming inverted repeats have similar effects on 5′ splice site selection in support of a common looping out and repression mechanism
    • Nasim, F. U., Hutchison, S., Cordeau, M. & Chabot, B. High-affinity hnRNP A1 binding sites and duplex-forming inverted repeats have similar effects on 5′ splice site selection in support of a common looping out and repression mechanism. RNA 8, 1078-1089 (2002).
    • (2002) RNA , vol.8 , pp. 1078-1089
    • Nasim, F.U.1    Hutchison, S.2    Cordeau, M.3    Chabot, B.4
  • 69
    • 0037119437 scopus 로고    scopus 로고
    • Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor
    • Hutchison, S., LeBel, C., Blanchette, M. & Chabot, B. Distinct sets of adjacent heterogeneous nuclear ribonucleoprotein (hnRNP) A1/A2 binding sites control 5′ splice site selection in the hnRNP A1 mRNA precursor. J. Biol. Chem. 277, 29745-29752 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 29745-29752
    • Hutchison, S.1    Lebel, C.2    Blanchette, M.3    Chabot, B.4
  • 70
    • 36248987806 scopus 로고    scopus 로고
    • HnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing
    • Kashima, T., Rao, N., David, C. J. & Manley, J. L. hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing. Hum. Mol. Genet. 16, 3149-3159 (2007).
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3149-3159
    • Kashima, T.1    Rao, N.2    David, C.J.3    Manley, J.L.4
  • 71
    • 33847665554 scopus 로고    scopus 로고
    • An intronic element contributes to splicing repression in spinal muscular atrophy
    • Kashima, T., Rao, N. & Manley, J. L. An intronic element contributes to splicing repression in spinal muscular atrophy. Proc. Natl Acad. Sci. USA 104, 3426-3431 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 3426-3431
    • Kashima, T.1    Rao, N.2    Manley, J.L.3
  • 72
    • 0033634948 scopus 로고    scopus 로고
    • Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing
    • Chou, M. Y., Underwood, J. G., Nikolic, J., Luu, M. H. & Black, D. L. Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing. Mol. Cell 5, 949-957 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 949-957
    • Chou, M.Y.1    Underwood, J.G.2    Nikolic, J.3    Luu, M.H.4    Black, D.L.5
  • 73
    • 0027151934 scopus 로고
    • Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF
    • Mayeda, A., Helfman, D. M. & Krainer, A. R. Modulation of exon skipping and inclusion by heterogeneous nuclear ribonucleoprotein A1 and pre-mRNA splicing factor SF2/ASF. Mol. Cell. Biol. 13, 2993-3001 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2993-3001
    • Mayeda, A.1    Helfman, D.M.2    Krainer, A.R.3
  • 74
    • 1642372088 scopus 로고    scopus 로고
    • SC35 and heterogeneous nuclear ribonucleoprotein A/B proteins bind to a juxtaposed exonic splicing enhancer/exonic splicing silencer element to regulate HIV-1 tat exon 2 splicing
    • Zahler, A. M., Damgaard, C. K., Kjems, J. & Caputi, M. SC35 and heterogeneous nuclear ribonucleoprotein A/B proteins bind to a juxtaposed exonic splicing enhancer/exonic splicing silencer element to regulate HIV-1 tat exon 2 splicing. J. Biol. Chem. 279, 10077-10084 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 10077-10084
    • Zahler, A.M.1    Damgaard, C.K.2    Kjems, J.3    Caputi, M.4
  • 75
    • 0034671932 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the absence of an SR protein RS domain
    • Zhu, J. & Krainer, A. R. Pre-mRNA splicing in the absence of an SR protein RS domain. Genes Dev. 14, 3166-3178 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 3166-3178
    • Zhu, J.1    Krainer, A.R.2
  • 76
    • 33845213293 scopus 로고    scopus 로고
    • Activation of α-tropomyosin exon 2 is regulated by the SR protein 9G8 and heterogeneous nuclear ribonucleoproteins H and F.
    • Crawford, J. B. & Patton, J. G. Activation of α-tropomyosin exon 2 is regulated by the SR protein 9G8 and heterogeneous nuclear ribonucleoproteins H and F. Mol. Cell. Biol. 26, 8791-8802 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 8791-8802
    • Crawford, J.B.1    Patton, J.G.2
  • 77
    • 4644256654 scopus 로고    scopus 로고
    • HnRNP A1 and the SR proteins ASF/SF2 and SC35 have antagonistic functions in splicing of β-tropomyosin exon 6B
    • Expert-Bezancon, A. et al. hnRNP A1 and the SR proteins ASF/SF2 and SC35 have antagonistic functions in splicing of β-tropomyosin exon 6B. J. Biol. Chem. 279, 38249-38259 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38249-38259
    • Expert-Bezancon, A.1
  • 78
    • 0036203307 scopus 로고    scopus 로고
    • Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing
    • Charlet, B. N., Logan, P., Singh, G. & Cooper, T. A. Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing. Mol. Cell 9, 649-658 (2002).
    • (2002) Mol. Cell , vol.9 , pp. 649-658
    • Charlet, B.N.1    Logan, P.2    Singh, G.3    Cooper, T.A.4
  • 79
    • 60549097502 scopus 로고    scopus 로고
    • Genome-wide analysis of alternative pre-mRNA splicing and RNA-binding specificities of the Drosophila hnRNP A/B family members
    • Blanchette, M. et al. Genome-wide analysis of alternative pre-mRNA splicing and RNA-binding specificities of the Drosophila hnRNP A/B family members. Mol. Cell 33, 438-449 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 438-449
    • Blanchette, M.1
  • 80
    • 38649129366 scopus 로고    scopus 로고
    • Diverse roles of hnRNP L in mammalian mRNA processing: A combined microarray and RNAi analysis
    • Hung, L. H. et al. Diverse roles of hnRNP L in mammalian mRNA processing: a combined microarray and RNAi analysis. RNA 14, 284-296 (2008).
    • (2008) RNA , vol.14 , pp. 284-296
    • Hung, L.H.1
  • 81
    • 56549105330 scopus 로고    scopus 로고
    • HITS-CLIP yields genome-wide insights into brain alternative RNA processing
    • Licatalosi, D. D. et al. HITS-CLIP yields genome-wide insights into brain alternative RNA processing. Nature 456, 464-469 (2008).
    • (2008) Nature , vol.456 , pp. 464-469
    • Licatalosi, D.D.1
  • 82
    • 18444362088 scopus 로고    scopus 로고
    • Nova autoregulation reveals dual functions in neuronal splicing
    • Dredge, B. K., Stefani, G., Engelhard, C. C. & Darnell, R. B. Nova autoregulation reveals dual functions in neuronal splicing. EMBO J. 24, 1608-1620 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1608-1620
    • Dredge, B.K.1    Stefani, G.2    Engelhard, C.C.3    Darnell, R.B.4
  • 83
    • 33244483620 scopus 로고    scopus 로고
    • Intronic binding sites for hnRNP A/B and hnRNP F/H proteins stimulate pre-mRNA splicing
    • Martinez-Contreras, R. et al. Intronic binding sites for hnRNP A/B and hnRNP F/H proteins stimulate pre-mRNA splicing. PLoS Biol. 4, e21 (2006).
    • (2006) PLoS Biol. , vol.4
    • Martinez-Contreras, R.1
  • 84
    • 42449098125 scopus 로고    scopus 로고
    • Splicing regulation: From a parts list of regulatory elements to an integrated splicing code
    • Wang, Z. & Burge, C. B. Splicing regulation: from a parts list of regulatory elements to an integrated splicing code. RNA 14, 802-813 (2008).
    • (2008) RNA , vol.14 , pp. 802-813
    • Wang, Z.1    Burge, C.B.2
  • 85
    • 0038382977 scopus 로고    scopus 로고
    • Nova regulates GABAA receptor y2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer
    • Dredge, B. K. & Darnell, R. B. Nova regulates GABAA receptor y2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer. Mol. Cell. Biol. 23, 4687-4700 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4687-4700
    • Dredge, B.K.1    Darnell, R.B.2
  • 86
    • 34250313662 scopus 로고    scopus 로고
    • Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes
    • Schaub, M. C, Lopez, S. R. & Caputi, M. Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes. J. Biol. Chem. 282, 13617-13626 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 13617-13626
    • Schaub, M.C.1    Lopez, S.R.2    Caputi, M.3
  • 87
    • 0035941211 scopus 로고    scopus 로고
    • Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H/F/2H9 family
    • Caputi, M. & Zahler, A. M. Determination of the RNA binding specificity of the heterogeneous nuclear ribonucleoprotein (hnRNP) H/H/F/2H9 family. J. Biol. Chem. 276, 43850-43859 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43850-43859
    • Caputi, M.1    Zahler, A.M.2
  • 88
    • 54849438715 scopus 로고    scopus 로고
    • Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF
    • Sanford, J. R. et al. Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF. PLoS ONE 3, e3369 (2008).
    • (2008) PLoS ONE , vol.3
    • Sanford, J.R.1
  • 89
    • 61849139645 scopus 로고    scopus 로고
    • Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts
    • Sanford, J. R. et al. Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts. Genome Res. 19, 381-394 (2009).
    • (2009) Genome Res. , vol.19 , pp. 381-394
    • Sanford, J.R.1
  • 90
    • 26244435561 scopus 로고    scopus 로고
    • Mutually exclusive splicing of the insect Dscam pre-mRNA directed by competing intronic RNA secondary structures
    • Graveley, B. R. Mutually exclusive splicing of the insect Dscam pre-mRNA directed by competing intronic RNA secondary structures. Cell 123, 65-73 (2005).
    • (2005) Cell , vol.123 , pp. 65-73
    • Graveley, B.R.1
  • 91
    • 36849015934 scopus 로고    scopus 로고
    • A regulator of Dscam mutually exclusive splicing fidelity. Nature Struct
    • Olson, S. et al. A regulator of Dscam mutually exclusive splicing fidelity. Nature Struct. Mol. Biol. 14, 1134-1140 (2007).
    • (2007) Mol. Biol. , vol.14 , pp. 1134-1140
    • Olson, S.1
  • 92
    • 0033591225 scopus 로고    scopus 로고
    • 5' splice site mutations in tau associated with the inherited dementia FTDP-17 affect a stem-loop structure that regulates alternative splicing of exon 10
    • Grover, A. et al. 5' splice site mutations in tau associated with the inherited dementia FTDP-17 affect a stem-loop structure that regulates alternative splicing of exon 10. J. Biol. Chem. 274, 15134-15143 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 15134-15143
    • Grover, A.1
  • 93
    • 37349056702 scopus 로고    scopus 로고
    • Pre-mRNA secondary structures influence exon recognition
    • Hiller, M., Zhang, Z., Backofen, R. & Stamm, S. Pre-mRNA secondary structures influence exon recognition. PLoS Genet. 3, e204 (2007).
    • (2007) PLoS Genet. , vol.3
    • Hiller, M.1    Zhang, Z.2    Backofen, R.3    Stamm, S.4
  • 94
    • 51449107580 scopus 로고    scopus 로고
    • P68 RNA helicase (DDX5) alters activity of cis-and trans-acting factors of the alternative splicing of H-Ras
    • Camats, M., Guil, S., Kokolo, M. & Bach-Elias, M. P68 RNA helicase (DDX5) alters activity of cis-and trans-acting factors of the alternative splicing of H-Ras. PLoS ONE 3, e2926 (2008).
    • (2008) PLoS ONE , vol.3
    • Camats, M.1    Guil, S.2    Kokolo, M.3    Bach-Elias, M.4
  • 95
    • 0026770679 scopus 로고
    • In vivo splicing of the beta tropomyosin pre-mRNA: A role for branch point and donor site competition
    • Libri, D., Balvay, L. & Fiszman, M. Y. In vivo splicing of the beta tropomyosin pre-mRNA: a role for branch point and donor site competition. Mol. Cell. Biol. 12, 3204-32 15 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3204-3215
    • Libri, D.1    Balvay, L.2    Fiszman, M.Y.3
  • 96
    • 58049217240 scopus 로고    scopus 로고
    • Riboswitch RNAs: Using RNA to sense cellular metabolism
    • Henkin, T. M. Riboswitch RNAs: using RNA to sense cellular metabolism. Genes Dev. 22, 3383-3390 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 3383-3390
    • Henkin . T, M.1
  • 97
    • 34249278470 scopus 로고    scopus 로고
    • Control of alternative RNA splicing and gene expression by eukaryotic riboswitches
    • Cheah, M. T., Wachter, A., Sudarsan, N. & Breaker, R. R. Control of alternative RNA splicing and gene expression by eukaryotic riboswitches. Nature 447, 497-500 (2007).
    • (2007) Nature , vol.447 , pp. 497-500
    • Cheah, M.T.1    Wachter, A.2    Sudarsan, N.3    Breaker, R.R.4
  • 99
    • 30844442607 scopus 로고    scopus 로고
    • The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C
    • Kishore, S. & Stamm, S. The snoRNA HBII-52 regulates alternative splicing of the serotonin receptor 2C. Science 311, 230-232 (2006).
    • (2006) Science , vol.311 , pp. 230-232
    • Kishore, S.1    Stamm, S.2
  • 100
    • 57649231776 scopus 로고    scopus 로고
    • Dynamic regulation of alternative splicing by silencers that modulate 5' splice site competition
    • Yu, Y et al. Dynamic regulation of alternative splicing by silencers that modulate 5' splice site competition. Cell 135, 1224-1236 (2008).
    • (2008) Cell , vol.135 , pp. 1224-1236
    • Yu, Y.1
  • 101
    • 34547212309 scopus 로고    scopus 로고
    • The microRNA miR-124 promotes neuronal differentiation by triggering brain-specific alternative pre-mRNA splicing
    • Makeyev, E. V., Zhang, J., Carrasco, M. A. & Maniatis, T. The microRNA miR-124 promotes neuronal differentiation by triggering brain-specific alternative pre-mRNA splicing. Mol. Cell 27, 435-448 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 435-448
    • Makeyev, E.V.1    Zhang, J.2    Carrasco, M.A.3    Maniatis, T.4
  • 102
    • 34347384211 scopus 로고    scopus 로고
    • A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons
    • Boutz, P. L. et al. A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons. Genes Dev. 21, 1636-1652 (2007)
    • (2007) Genes Dev. , vol.21 , pp. 1636-1652
    • Boutz, P.L.1
  • 103
    • 70350569858 scopus 로고    scopus 로고
    • note
    • Using sirNA and microarray analysis, the authors show that the PTB-to-nPTB switch provides a post-transcriptional mechanism that is important for programming neuronal differentiation.
  • 104
    • 34347378276 scopus 로고    scopus 로고
    • PTB/nPTB switch: A post-transcriptional mechanism for programming neuronal differentiation
    • Coutinho-Mansfield, G. C., Xue, Y., Zhang, Y. & Fu, X. D. PTB/nPTB switch: a post-transcriptional mechanism for programming neuronal differentiation. Genes Dev. 21, 1573-1577 (2007).
    • (2007) Genes Dev. , vol.21 , pp. 1573-1577
    • Coutinho-Mansfield, G.C.1    Xue, Y.2    Zhang, Y.3    Fu, X.D.4
  • 105
    • 34547205013 scopus 로고    scopus 로고
    • Crossregulation and functional redundancy between the splicing regulator PTB and its paralogs nPTB and ROD1
    • Spellman, R., Llorian, M. & Smith, C. W. Crossregulation and functional redundancy between the splicing regulator PTB and its paralogs nPTB and ROD1. Mol. Cell 27, 420-434 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 420-434
    • Spellman, R.1    Llorian, M.2    Smith, C.W.3
  • 106
    • 11144320747 scopus 로고    scopus 로고
    • Structural and functional analysis of essential pre-mRNA splicing factor Prp19p
    • Ohi, M. D. et al. Structural and functional analysis of essential pre-mRNA splicing factor Prp19p. Mol. Cell. Biol. 25, 451-460 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 451-460
    • Ohi, M.D.1
  • 107
    • 42249093677 scopus 로고    scopus 로고
    • Isolation of an active step i spliceosome and composition of its RNP core
    • Bessonov, S., Anokhina, M., Will, C. L., Urlaub, H. & Luhrmann, R. Isolation of an active step I spliceosome and composition of its RNP core. Nature 452, 846-850 (2008).
    • (2008) Nature , vol.452 , pp. 846-850
    • Bessonov, S.1    Anokhina, M.2    Will, C.L.3    Urlaub, H.4    Luhrmann, R.5
  • 108
    • 0033022124 scopus 로고    scopus 로고
    • The SRm160/300 splicing coactivator is required for exon-enhancer function
    • Eldridge, A. G., Li, Y., Sharp, P. A. & Blencowe, B. J. The SRm160/300 splicing coactivator is required for exon-enhancer function. Proc. Natl Acad. Sci. USA 96, 6125-6130 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6125-6130
    • Eldridge, A.G.1    Li, Y.2    Sharp, P.A.3    Blencowe, B.J.4
  • 109
    • 0033755837 scopus 로고    scopus 로고
    • LUCA15, a putative tumour suppressor gene encoding an RNA-binding nuclear protein, is down-regulated in ras-transformed Rat-1 cells
    • Edamatsu, H., Kaziro, Y. & Itoh, H. LUCA15, a putative tumour suppressor gene encoding an RNA-binding nuclear protein, is down-regulated in ras-transformed Rat-1 cells. Genes Cells 5, 849-858 (2000).
    • (2000) Genes Cells , vol.5 , pp. 849-858
    • Edamatsu, H.1    Kaziro, Y.2    Itoh, H.3
  • 110
    • 0036792645 scopus 로고    scopus 로고
    • Candidate tumour suppressor LUCA-15 can regulate multiple apoptotic pathways
    • Mourtada-Maarabouni, M., Sutherland, L. C. & Williams, G. T. Candidate tumour suppressor LUCA-15 can regulate multiple apoptotic pathways. Apoptosis 7, 421-432 (2002).
    • (2002) Apoptosis , vol.7 , pp. 421-432
    • Mourtada-Maarabouni, M.1    Sutherland, L.C.2    Williams, G.T.3
  • 111
    • 53149145051 scopus 로고    scopus 로고
    • RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition
    • Bonnal, S. et al. RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition. Mol. Cell 32, 81-95 (2008).
    • (2008) Mol. Cell , vol.32 , pp. 81-95
    • Bonnal, S.1
  • 112
    • 30044440197 scopus 로고    scopus 로고
    • Chromatin transcript elongation and alternative splicing
    • Kornblihtt, A. R. Chromatin, transcript elongation and alternative splicing. Nature Struct. Mol. Biol. 13, 5-7 (2006).
    • (2006) Nature Struct. Mol. Biol. , vol.13 , pp. 5-7
    • Kornblihtt, A.R.1
  • 113
    • 34250363024 scopus 로고    scopus 로고
    • SR proteins function in coupling RNAP II transcription to pre-mRNA splicing
    • Das, R. et al. SR proteins function in coupling RNAP II transcription to pre-mRNA splicing. Mol. Cell 26, 867-881 (2007).
    • (2007) Mol. Cell , vol.26 , pp. 867-881
    • Das, R.1
  • 114
    • 1442281514 scopus 로고    scopus 로고
    • Differential recruitment of nuclear receptor coactivators may determine alternative RNA splice site choice in target genes
    • Auboeuf, D. et al. Differential recruitment of nuclear receptor coactivators may determine alternative RNA splice site choice in target genes. Proc. Natl Acad. Sci. USA 101, 2270-2274 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2270-2274
    • Auboeuf, D.1
  • 115
    • 0033180615 scopus 로고    scopus 로고
    • Coupling of transcription with alternative splicing: RNA pol II promoters modulate SF2/ASF and 9G8 effects on an exonic splicing enhancer
    • Cramer, P. et al. Coupling of transcription with alternative splicing: RNA pol II promoters modulate SF2/ASF and 9G8 effects on an exonic splicing enhancer. Mol. Cell 4, 251-258 (1999).
    • (1999) Mol. Cell , vol.4 , pp. 251-258
    • Cramer, P.1
  • 116
    • 0033638283 scopus 로고    scopus 로고
    • Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1
    • Monsalve, M. et al. Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1. Mol. Cell 6, 307-316 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 307-316
    • Monsalve, M.1
  • 117
    • 0141888375 scopus 로고    scopus 로고
    • A slow RNA polymerase II affects alternative splicing in vivo
    • de la Mata, M. et al. A slow RNA polymerase II affects alternative splicing in vivo. Mol. Cell 12, 525-532 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 525-532
    • De La Mata, M.1
  • 118
    • 65549147264 scopus 로고    scopus 로고
    • DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation
    • Munoz, M. J. et al. DNA damage regulates alternative splicing through inhibition of RNA polymerase II elongation. Cell 137, 708-720 (2009).
    • (2009) Cell , vol.137 , pp. 708-720
    • Munoz, M.J.1
  • 119
    • 33751090746 scopus 로고    scopus 로고
    • Phosphorylation and functions of the RNA polymerase II CTD
    • Phatnani, H. P. & Greenleaf, A. L. Phosphorylation and functions of the RNA polymerase II CTD. Genes Dev. 20, 2922-2936 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 2922-2936
    • Phatnani, H.P.1    Greenleaf, A.L.2
  • 120
    • 0036052014 scopus 로고    scopus 로고
    • CTD phosphatase: Role in RNA polymerase II cycling and the regulation of transcript elongation. Prog. Nucleic Acid Res
    • Lin, P. S., Marshall, N. F. & Dahmus, M. E. CTD phosphatase: role in RNA polymerase II cycling and the regulation of transcript elongation. Prog. Nucleic Acid Res. Mol. Biol. 72, 333-365 (2002).
    • (2002) Mol. Biol. , vol.72 , pp. 333-365
    • Lin, P.S.1    Marshall, N.F.2    Dahmus, M.E.3
  • 121
    • 38949133822 scopus 로고    scopus 로고
    • The search for alternative splicing regulators: New approaches offer a path to a splicing code
    • David, C. J. & Manley, J. L. The search for alternative splicing regulators: new approaches offer a path to a splicing code. Genes Dev. 22, 279-285 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 279-285
    • David, C.J.1    Manley, J.L.2
  • 122
    • 38949110702 scopus 로고    scopus 로고
    • STAR family RNA-binding protein ASD-2 regulates developmental switching of mutually exclusive alternative splicing in vivo
    • Ohno, G., Hagiwara, M. & Kuroyanagi, H. STAR family RNA-binding protein ASD-2 regulates developmental switching of mutually exclusive alternative splicing in vivo. Genes Dev. 22, 360-374 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 360-374
    • Ohno, G.1    Hagiwara, M.2    Kuroyanagi, H.3
  • 123
    • 35548940665 scopus 로고    scopus 로고
    • Neuronal regulation of alternative pre-mRNA splicing
    • Li, Q., Lee, J. A. & Black, D. L. Neuronal regulation of alternative pre-mRNA splicing. Nature Rev. Neurosci. 8, 819-831 (2007).
    • (2007) Nature Rev. Neurosci. , vol.8 , pp. 819-831
    • Li, Q.1    Lee, J.A.2    Black, D.L.3
  • 124
    • 23044431574 scopus 로고    scopus 로고
    • Nova regulates brain-specific splicing to shape the synapse
    • Ule, J. et al. Nova regulates brain-specific splicing to shape the synapse. Nature Genet. 37, 844-852 (2005).
    • (2005) Nature Genet. , vol.37 , pp. 844-852
    • Ule, J.1
  • 125
    • 0036212521 scopus 로고    scopus 로고
    • Role of HuD and other RNA-binding proteins in neural development and plasticity
    • Perrone-Bizzozero, N. & Bolognani, F. Role of HuD and other RNA-binding proteins in neural development and plasticity. J. Neurosci. Res. 68, 121-126 (2002).
    • (2002) J. Neurosci. Res. , vol.68 , pp. 121-126
    • Perrone-Bizzozero, N.1    Bolognani, F.2
  • 126
    • 33845380816 scopus 로고    scopus 로고
    • A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators
    • Zhu, H., Hasman, R. A., Barron, V. A., Luo, G. & Lou, H. A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators. Mol. Biol. Cell 17, 5105-5114 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 5105-5114
    • Zhu, H.1    Hasman, R.A.2    Barron, V.A.3    Luo, G.4    Lou, H.5
  • 127
    • 45249093014 scopus 로고    scopus 로고
    • Regulation of the ELAV target ewg: Insights from an evolutionary perspective
    • Soller, M., Li, M. & Haussmann, I. U. Regulation of the ELAV target ewg: insights from an evolutionary perspective. Biochem. Soc. Trans. 36, 502-504 (2008).
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 502-504
    • Soller, M.1    Li, M.2    Haussmann, I.U.3
  • 128
    • 24344452361 scopus 로고    scopus 로고
    • A genome-wide in situ hybridization map of RNA-binding proteins reveals anatomically restricted expression in the developing mouse brain
    • McKee, A. E. et al. A genome-wide in situ hybridization map of RNA-binding proteins reveals anatomically restricted expression in the developing mouse brain. BMC Dev. Biol. 5, 14 (2005).
    • (2005) BMC Dev. Biol. , vol.5 , pp. 14
    • McKee, A.E.1
  • 129
    • 13144293035 scopus 로고    scopus 로고
    • The neuronal RNA-binding protein Nova-2 is implicated as the autoantigen targeted in POMA patients with dementia
    • Yang, Y. Y., Yin, G. L. & Darnell, R. B. The neuronal RNA-binding protein Nova-2 is implicated as the autoantigen targeted in POMA patients with dementia. Proc. Natl Acad. Sci. USA 95, 13254-13259 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13254-13259
    • Yang, Y.Y.1    Yin, G.L.2    Darnell, R.B.3
  • 130
    • 61649087689 scopus 로고    scopus 로고
    • ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2 splicing
    • Warzecha, C. C., Sato, T. K., Nabet, B., Hogenesch, J. B. & Carstens, R. P. ESRP1 and ESRP2 are epithelial cell-type-specific regulators of FGFR2 splicing. Mol. Cell 33, 591-601 (2009).
    • (2009) Mol. Cell , vol.33 , pp. 591-601
    • Warzecha, C.C.1    Sato, T.K.2    Nabet, B.3    Hogenesch, J.B.4    Carstens, R.P.5
  • 131
    • 12144285753 scopus 로고    scopus 로고
    • Dilated cardiomyopathy caused by tissue-specific ablation of SC35 in the heart
    • Ding, J. H. et al. Dilated cardiomyopathy caused by tissue-specific ablation of SC35 in the heart. EMBO J. 23, 885-896 (2004).
    • (2004) EMBO J. , vol.23 , pp. 885-896
    • Ding, J.H.1
  • 132
    • 19944427655 scopus 로고    scopus 로고
    • ASF/SF2-regulated CaMKIIδ alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle
    • Xu, X. et al. ASF/SF2-regulated CaMKIIδ alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle. Cell 120, 59-72 (2005).
    • (2005) Cell , vol.120 , pp. 59-72
    • Xu, X.1
  • 133
    • 64549159302 scopus 로고    scopus 로고
    • 2+ handling in the embryonic heart
    • Feng, Y. et al. SRp38 regulates alternative splicing and is required for Ca2+ handling in the embryonic heart. Dev. Cell 16, 528-538 (2009).
    • (2009) Dev. Cell , vol.16 , pp. 528-538
    • Feng, Y.1
  • 134
    • 50849145126 scopus 로고    scopus 로고
    • Tissue-specific splicing factor gene expression signatures
    • Grosso, A. R. et al. Tissue-specific splicing factor gene expression signatures. Nucleic Acids Res. 36, 4823-4832 (2008).
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4823-4832
    • Grosso, A.R.1
  • 135
    • 33845715579 scopus 로고    scopus 로고
    • SAP155 binds to ceramide-responsive RNA cis-element 1 and regulates the alternative 5′ splice site selection of Bcl-x pre-mRNA
    • Massiello, A., Roesser, J. R. & Chalfant, C. E. SAP155 binds to ceramide-responsive RNA cis-element 1 and regulates the alternative 5′ splice site selection of Bcl-x pre-mRNA. FASEB J. 20, 1680-1682 (2006).
    • (2006) FASEB J. , vol.20 , pp. 1680-1682
    • Massiello, A.1    Roesser, J.R.2    Chalfant, C.E.3
  • 136
    • 33749471110 scopus 로고    scopus 로고
    • 35 impairs cell cycle progression and modulates alternative splicing of Cdc25 transcripts
    • Pacheco, T. R., Moita, L. F., Gomes, A. Q., Hacohen, N. & Carmo-Fonseca, M. RNA interference knockdown of hU2AF35 impairs cell cycle progression and modulates alternative splicing of Cdc25 transcripts. Mol. Biol. Cell 17, 4187-4199 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4187-4199
    • Pacheco, T.R.1    Moita, L.F.2    Gomes, A.Q.3    Hacohen, N.4    Carmo-Fonseca, M.5
  • 137
    • 34748855702 scopus 로고    scopus 로고
    • Rapid transcript-specific changes in splicing in response to environmental stress
    • Pleiss, J. A., Whitworth, G. B., Bergkessel, M. & Guthrie, C. Rapid, transcript-specific changes in splicing in response to environmental stress. Mol. Cell 27, 928-937 (2007).
    • (2007) Mol. Cell , vol.27 , pp. 928-937
    • Pleiss, J.A.1    Whitworth, G.B.2    Bergkessel, M.3    Guthrie, C.4
  • 138
    • 29144463310 scopus 로고    scopus 로고
    • Spinal muscular atrophy: A deficiency in a ubiquitous protein; A motor neuron-specific disease
    • Monani, U. R. Spinal muscular atrophy: a deficiency in a ubiquitous protein; a motor neuron-specific disease. Neuron 48, 885-896 (2005).
    • (2005) Neuron , vol.48 , pp. 885-896
    • Monani, U.R.1
  • 139
    • 41549119007 scopus 로고    scopus 로고
    • Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs
    • Gabanella, F. et al. Ribonucleoprotein assembly defects correlate with spinal muscular atrophy severity and preferentially affect a subset of spliceosomal snRNPs. PLoS ONE 2, e921 (2007).
    • (2007) PLoS ONE , vol.2
    • Gabanella, F.1
  • 140
    • 4444272979 scopus 로고    scopus 로고
    • Cell signalling and the control of pre-mRNA splicing
    • Shin, C. & Manley, J. L. Cell signalling and the control of pre-mRNA splicing. Nature Rev. Mol. Cell Biol. 5, 727-738 (2004).
    • (2004) Nature Rev. Mol. Cell Biol. , vol.5 , pp. 727-738
    • Shin, C.1    Manley, J.L.2
  • 141
    • 34447297332 scopus 로고    scopus 로고
    • Cellular signals modulate alternative splicing
    • Tarn, W. Y. Cellular signals modulate alternative splicing. J. Biomed. Sci. 14, 517-522 (2007).
    • (2007) J. Biomed. Sci. , vol.14 , pp. 517-522
    • Tarn, W.Y.1
  • 142
    • 3042836378 scopus 로고    scopus 로고
    • A molecular link between SR protein dephosphorylation and mRNA export
    • Huang, Y., Yario, T. A. & Steitz, J. A. A molecular link between SR protein dephosphorylation and mRNA export. Proc. Natl Acad. Sci. USA 101, 9666-9670 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 9666-9670
    • Huang, Y.1    Yario, T.A.2    Steitz, J.A.3
  • 143
    • 0007570010 scopus 로고    scopus 로고
    • The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation
    • van der Houven van Oordt, W. et al. The MKK(3/6)-p38-signaling cascade alters the subcellular distribution of hnRNP A1 and modulates alternative splicing regulation. J. Cell Biol. 149, 307-316 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 307-316
    • Van Der Houven1    Van Oordt, W.2
  • 144
    • 0035095885 scopus 로고    scopus 로고
    • ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation
    • Habelhah, H. et al. ERK phosphorylation drives cytoplasmic accumulation of hnRNP-K and inhibition of mRNA translation. Nature Cell Biol. 3, 325-330 (2001).
    • (2001) Nature Cell Biol. , vol.3 , pp. 325-330
    • Habelhah, H.1
  • 145
    • 0037101633 scopus 로고    scopus 로고
    • Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain
    • Daoud, R. et al. Ischemia induces a translocation of the splicing factor tra2-beta 1 and changes alternative splicing patterns in the brain. J. Neurosci. 22, 5889-5899 (2002).
    • (2002) J. Neurosci. , vol.22 , pp. 5889-5899
    • Daoud, R.1
  • 146
    • 33746516731 scopus 로고    scopus 로고
    • F. hnRNP A1 relocalization to the stress granules reflects a role in the stress response
    • Guil, S., Long, J. C. & Caceres, J. F. hnRNP A1 relocalization to the stress granules reflects a role in the stress response. Mol. Cell. Biol. 26, 5744-5758 (2006).
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 5744-5758
    • Guil, S.1    Long, J.C.2    Caceres, J.3
  • 147
    • 33846268431 scopus 로고    scopus 로고
    • Phosphorylation by SR kinases regulates the binding of PTB-associated splicing factor (PSF) to the pre-mRNA polypyrimidine tract
    • Huang, C. J., Tang, Z., Lin, R. J. & Tucker, P. W. Phosphorylation by SR kinases regulates the binding of PTB-associated splicing factor (PSF) to the pre-mRNA polypyrimidine tract. FEBS Lett. 581, 223-232 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 223-232
    • Huang, C.J.1    Tang, Z.2    Lin, R.J.3    Tucker, P.W.4
  • 148
    • 0031037690 scopus 로고    scopus 로고
    • Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: Creation of an SRp40-specific splicing enhancer
    • Tacke, R., Chen, Y. & Manley, J. L. Sequence-specific RNA binding by an SR protein requires RS domain phosphorylation: creation of an SRp40-specific splicing enhancer. Proc. Natl Acad. Sci. USA 94, 1148-1153 (1997).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1148-1153
    • Tacke, R.1    Chen, Y.2    Manley, J.L.3
  • 149
    • 33847308702 scopus 로고    scopus 로고
    • Fas-activated serine/ threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing
    • Izquierdo, J. M. & Valcarcel, J. Fas-activated serine/ threonine kinase (FAST K) synergizes with TIA-1/TIAR proteins to regulate Fas alternative splicing. J. Biol. Chem. 282, 1539-1543 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 1539-1543
    • Izquierdo, J.M.1    Valcarcel, J.2
  • 150
    • 33947712084 scopus 로고    scopus 로고
    • The RNA-binding protein Sam68 odulates the alternative splicing of Bcl-x
    • Paronetto, M. P., Achsel, T., Massiello, A., Chalfant, C. E. & Sette, C. The RNA-binding protein Sam68 odulates the alternative splicing of Bcl-x. J. Cell Biol. 176, 929-939 (2007).
    • (2007) J. Cell Biol. , vol.176 , pp. 929-939
    • Paronetto, M.P.1    Achsel, T.2    Massiello, A.3    Chalfant, C.E.4    Sette, C.5
  • 151
    • 34249654182 scopus 로고    scopus 로고
    • Relocalization of the polypyrimidine tract-binding protein during PKA-induced neurite growth
    • Ma, S., Liu, G., Sun, Y. & Xie, J. Relocalization of the polypyrimidine tract-binding protein during PKA-induced neurite growth. Biochim. Biophys. Acta 1773, 912-923 (2007).
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 912-923
    • Ma, S.1    Liu, G.2    Sun, Y.3    Xie, J.4
  • 152
    • 0041806593 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein
    • Xie, J., Lee, J. A., Kress, T. L., Mowry, K. L. & Black, D. L. Protein kinase A phosphorylation modulates transport of the polypyrimidine tract-binding protein. Proc. Natl Acad. Sci. USA 100, 8776-8781 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8776-8781
    • Xie, J.1    Lee, J.A.2    Kress, T.L.3    Mowry, K.L.4    Black, D.L.5
  • 153
    • 34948892099 scopus 로고    scopus 로고
    • A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock
    • Shi, Y. & Manley, J. L. A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock. Mol. Cell 28, 79-90 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 79-90
    • Shi, Y.1    Manley, J.L.2
  • 154
    • 0028825490 scopus 로고
    • Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing
    • Van Eynde, A. et al. Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. J. Biol. Chem. 270, 28068-28074 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28068-28074
    • Van Eynde, A.1
  • 155
    • 0037081563 scopus 로고    scopus 로고
    • Protein phosphatase 1 targeted in many directions
    • Cohen, P. T. Protein phosphatase 1 targeted in many directions. J. Cell Sci. 11 5, 241-256 (2002).
    • (2002) J. Cell Sci. , vol.11 , Issue.5 , pp. 241-256
    • Cohen, P.T.1
  • 156
    • 38049061206 scopus 로고    scopus 로고
    • Alternative splicing: Current perspectives
    • Kim, E., Goren, A. & Ast, G. Alternative splicing: current perspectives. Bioessays 30, 38-47 (2008).
    • (2008) Bioessays , vol.30 , pp. 38-47
    • Kim, E.1    Goren, A.2    Ast, G.3
  • 157
    • 30344439849 scopus 로고    scopus 로고
    • Genome-wide prediction of mammalian enhancers based on analysis of transcription-factor binding affinity
    • Hallikas, O. et al. Genome-wide prediction of mammalian enhancers based on analysis of transcription-factor binding affinity. Cell 124, 47-59 (2006).
    • (2006) Cell , vol.124 , pp. 47-59
    • Hallikas, O.1
  • 159
    • 0029064220 scopus 로고
    • The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
    • Tacke, R. & Manley, J. L. The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities. EMBO J. 14, 3540-3551 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3540-3551
    • Tacke, R.1    Manley, J.L.2
  • 160
    • 11144331491 scopus 로고    scopus 로고
    • Characterization of a U2AF-independent commitment complex (E′) in the mammalian spliceosome assembly pathway
    • Kent, O. A., Ritchie, D. B. & Macmillan, A. M. Characterization of a U2AF-independent commitment complex (E′) in the mammalian spliceosome assembly pathway. Mol. Cell. Biol. 25, 233-240 (2005).
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 233-240
    • Kent, O.A.1    Ritchie, D.B.2    MacMillan, A.M.3
  • 161
    • 33745609509 scopus 로고    scopus 로고
    • RS domains contact splicing signals and promote splicing by a common mechanism in yeast through humans
    • Shen, H. & Green, M. R. RS domains contact splicing signals and promote splicing by a common mechanism in yeast through humans. Genes Dev. 20, 1755-1765 (2006).
    • (2006) Genes Dev. , vol.20 , pp. 1755-1765
    • Shen, H.1    Green, M.R.2
  • 162
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang, Y., Gattoni, R., Stevenin, J. & Steitz, J. A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 11, 837-843 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 163
    • 8844219677 scopus 로고    scopus 로고
    • Involvement of SR proteins in mRNA surveillance
    • Zhang, Z. & Krainer, A. R. Involvement of SR proteins in mRNA surveillance. Mol. Cell 16, 597-607 (2004).
    • (2004) Mol. Cell , vol.16 , pp. 597-607
    • Zhang, Z.1    Krainer, A.R.2
  • 164
    • 1842632326 scopus 로고    scopus 로고
    • A novel role for shuttling SR proteins in mRNA translation
    • Sanford, J. R., Gray, N. K., Beckmann, K. & Caceres, J. F. A novel role for shuttling SR proteins in mRNA translation. Genes Dev. 18, 755-768 (2004).
    • (2004) Genes Dev. , vol.18 , pp. 755-768
    • Sanford, J.R.1    Gray, N.K.2    Beckmann, K.3    Caceres, J.F.4
  • 165
    • 0036544654 scopus 로고    scopus 로고
    • Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1
    • Cartegni, L. & Krainer, A. R. Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1. Nature Genet. 30, 377-384 (2002).
    • (2002) Nature Genet. , vol.30 , pp. 377-384
    • Cartegni, L.1    Krainer, A.R.2


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