메뉴 건너뛰기




Volumn 15, Issue 10, 2014, Pages 689-701

Context-dependent control of alternative splicing by RNA-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

RNA BINDING PROTEIN; PROTEIN BINDING;

EID: 84922255144     PISSN: 14710056     EISSN: 14710064     Source Type: Journal    
DOI: 10.1038/nrg3778     Document Type: Review
Times cited : (756)

References (176)
  • 2
    • 5044222204 scopus 로고    scopus 로고
    • How did alternative splicing evolve?. Nature Rev
    • Ast, G. How did alternative splicing evolve?. Nature Rev. Genet. 5, 773-782 (2004
    • (2004) Genet , vol.5 , pp. 773-782
    • Ast, G.1
  • 3
    • 77951120000 scopus 로고    scopus 로고
    • Alternative splicing and evolution: Diversification, exon definition and function
    • Keren, H., Lev-Maor, G. & Ast, G. Alternative splicing and evolution: diversification, exon definition and function. Nature Rev. Genet. 11, 345-355 (2010
    • (2010) Nature Rev. Genet , vol.11 , pp. 345-355
    • Keren, H.1    Lev-Maor, G.2    Ast, G.3
  • 5
    • 84871410405 scopus 로고    scopus 로고
    • The evolutionary landscape of alternative splicing in vertebrate species
    • Barbosa-Morais, N. L. et al. The evolutionary landscape of alternative splicing in vertebrate species. Science 338, 1587-1593 (2012
    • (2012) Science , vol.338 , pp. 1587-1593
    • Barbosa-Morais, N.L.1
  • 6
    • 84871436996 scopus 로고    scopus 로고
    • Evolutionary dynamics of gene and isoform regulation in mammalian tissues
    • Merkin, J., Russell, C., Chen, P. & Burge, C. B. Evolutionary dynamics of gene and isoform regulation in mammalian tissues. Science 338, 1593-1599 (2012
    • (2012) Science , vol.338 , pp. 1593-1599
    • Merkin, J.1    Russell, C.2    Chen, P.3    Burge, C.B.4
  • 7
    • 84894318075 scopus 로고    scopus 로고
    • Coupling mRNA processing with transcription in time and space
    • Bentley, D. L. Coupling mRNA processing with transcription in time and space. Nature Rev. Genet. 15, 163-175 (2014
    • (2014) Nature Rev. Genet , vol.15 , pp. 163-175
    • Bentley, D.L.1
  • 9
    • 84875444381 scopus 로고    scopus 로고
    • Alternative splicing: A pivotal step between eukaryotic transcription and translation
    • Kornblihtt, A. R. et al. Alternative splicing: a pivotal step between eukaryotic transcription and translation. Nature Rev. Mol. Cell Biol. 14, 153-165 (2013
    • (2013) Nature Rev. Mol. Cell Biol , vol.14 , pp. 153-165
    • Kornblihtt, A.R.1
  • 10
    • 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
  • 11
    • 75849145292 scopus 로고    scopus 로고
    • Expansion of the eukaryotic proteome by alternative splicing
    • Nilsen, T. W. & Graveley, B. R. Expansion of the eukaryotic proteome by alternative splicing. Nature 463, 457-463 (2010
    • (2010) Nature , vol.463 , pp. 457-463
    • Nilsen, T.W.1    Graveley, B.R.2
  • 12
    • 10944220623 scopus 로고    scopus 로고
    • Towards a splicing code
    • Fu, X. D. Towards a splicing code. Cell 119, 736-738 (2004
    • (2004) Cell , vol.119 , pp. 736-738
    • Fu, X.D.1
  • 13
    • 77952029221 scopus 로고    scopus 로고
    • Deciphering the splicing code
    • Barash, Y. et al. Deciphering the splicing code. Nature 465, 53-59 (2010
    • (2010) Nature , vol.465 , pp. 53-59
    • Barash, Y.1
  • 14
    • 49849086337 scopus 로고    scopus 로고
    • An intronic signal for alternative splicing in the human genome
    • Havlioglu, N. et al. An intronic signal for alternative splicing in the human genome. PLoS ONE 2, e1246 (2007
    • (2007) PLoS ONE , vol.2 , pp. e1246
    • Havlioglu, N.1
  • 15
    • 60149093432 scopus 로고    scopus 로고
    • And disease
    • Cooper, T. A., Wan, L. & Dreyfuss, G. RNA and disease. Cell 136, 777-793 (2009
    • (2009) Cell , vol.136 , pp. 777-793
    • Cooper, T.A.1    Wan, L.2    Rna, D.G.3
  • 16
    • 78049416081 scopus 로고    scopus 로고
    • Alternative pre-mRNA splicing regulation in cancer: Pathways and programs unhinged
    • David, C. J. & Manley, J. L. Alternative pre-mRNA splicing regulation in cancer: pathways and programs unhinged. Genes Dev. 24, 2343-2364 (2010
    • (2010) Genes Dev , vol.24 , pp. 2343-2364
    • David, C.J.1    Manley, J.L.2
  • 17
    • 80053027909 scopus 로고    scopus 로고
    • Functional consequences of developmentally regulated alternative splicing
    • Kalsotra, A. & Cooper, T. A. Functional consequences of developmentally regulated alternative splicing. Nature Rev. Genet. 12, 715-729 (2011
    • (2011) Nature Rev. Genet , vol.12 , pp. 715-729
    • Kalsotra, A.1    Cooper, T.A.2
  • 19
    • 0025098474 scopus 로고
    • Exon definition may facilitate splice site selection in RNAs with multiple exons
    • Robberson, B. L., Cote, G. J. & Berget, S. M. Exon definition may facilitate splice site selection in RNAs with multiple exons. Mol. Cell. Biol. 10, 84-94 (1990
    • (1990) Mol. Cell. Biol , vol.10 , pp. 84-94
    • Robberson, B.L.1    Cote, G.J.2    Berget, S.M.3
  • 20
    • 0025760145 scopus 로고
    • Control of alternative splicing by the differential binding of U1 small nuclear ribonucleoprotein particle
    • Kuo, H. C., Nasim, F. H. & Grabowski, P. J. Control of alternative splicing by the differential binding of U1 small nuclear ribonucleoprotein particle. Science 251, 1045-1050 (1991
    • (1991) Science , vol.251 , pp. 1045-1050
    • Kuo, H.C.1    Nasim, F.H.2    Grabowski, P.J.3
  • 21
    • 79960918747 scopus 로고    scopus 로고
    • RNA structure and the mechanisms of alternative splicing
    • McManus, C. J. & Graveley, B. R. RNA structure and the mechanisms of alternative splicing. Curr. Opin. Genet. Dev. 21, 373-379 (2011
    • (2011) Curr. Opin. Genet. Dev , vol.21 , pp. 373-379
    • McManus, C.J.1    Graveley, B.R.2
  • 22
    • 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
  • 23
    • 84893427735 scopus 로고    scopus 로고
    • In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features
    • Ding, Y. et al. In vivo genome-wide profiling of RNA secondary structure reveals novel regulatory features. Nature 505, 696-700 (2014
    • (2014) Nature 505 , pp. 696-700
    • Ding, Y.1
  • 24
    • 84893351549 scopus 로고    scopus 로고
    • Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo
    • Rouskin, S., Zubradt, M., Washietl, S., Kellis, M. & Weissman, J. S. Genome-wide probing of RNA structure reveals active unfolding of mRNA structures in vivo. Nature 505, 701-705 (2014
    • (2014) Nature , vol.505 , pp. 701-705
    • Rouskin, S.1    Zubradt, M.2    Washietl, S.3    Kellis, M.4    Weissman, J.S.5
  • 25
    • 84893358533 scopus 로고    scopus 로고
    • Landscape and variation of RNA secondary structure across the human transcriptome
    • Wan, Y. et al. Landscape and variation of RNA secondary structure across the human transcriptome. Nature 505, 706-709 (2014
    • (2014) Nature , vol.505 , pp. 706-709
    • Wan, Y.1
  • 26
    • 22344439658 scopus 로고    scopus 로고
    • Dichotomous splicing signals in exon flanks
    • Zhang, X. H., Leslie, C. S. & Chasin, L. A. Dichotomous splicing signals in exon flanks. Genome Res. 15, 768-779 (2005
    • (2005) Genome Res , vol.15 , pp. 768-779
    • Zhang, X.H.1    Leslie, C.S.2    Chasin, L.A.3
  • 27
    • 84890132388 scopus 로고    scopus 로고
    • Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges
    • Lovci, M. T. et al. Rbfox proteins regulate alternative mRNA splicing through evolutionarily conserved RNA bridges. Nature Struct. Mol. Biol. 20, 1434-1442 (2013
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 1434-1442
    • Lovci, M.T.1
  • 28
    • 84884856342 scopus 로고    scopus 로고
    • Cas9 as a versatile tool for engineering biology
    • Mali, P., Esvelt, K. M. & Church, G. M. Cas9 as a versatile tool for engineering biology. Nature Methods 10, 957-963 (2013
    • (2013) Nature Methods , vol.10 , pp. 957-963
    • Mali, P.1    Esvelt, K.M.2    Church, G.M.3
  • 29
    • 84902096048 scopus 로고    scopus 로고
    • And applications of CRISPR-Cas9 for genome engineering
    • Hsu, P. D., Lander, E. S. & Zhang, F. Development and applications of CRISPR-Cas9 for genome engineering. Cell 157, 1262-1278 (2014
    • (2014) Cell , vol.157 , pp. 1262-1278
    • Hsu, P.D.1    Lander, E.S.2    Development, Z.F.3
  • 30
    • 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
  • 31
    • 84885842840 scopus 로고    scopus 로고
    • Hidden specificity in an apparently nonspecific RNA-binding protein
    • Guenther, U. P. et al. Hidden specificity in an apparently nonspecific RNA-binding protein. Nature 502, 385-388 (2013
    • (2013) Nature , vol.502 , pp. 385-388
    • Guenther, U.P.1
  • 32
    • 0037047644 scopus 로고    scopus 로고
    • Predictive identification of exonic splicing enhancers in human genes
    • Fairbrother, W. G., Yeh, R. F., Sharp, P. A. & Burge, C. B. Predictive identification of exonic splicing enhancers in human genes. Science 297, 1007-1013 (2002
    • (2002) Science , vol.297 , pp. 1007-1013
    • Fairbrother, W.G.1    Yeh, R.F.2    Sharp, P.A.3    Burge, C.B.4
  • 33
    • 36749057933 scopus 로고    scopus 로고
    • Coevolutionary networks of splicing cis-regulatory elements
    • Xiao, X., Wang, Z., Jang, M. & Burge, C. B. Coevolutionary networks of splicing cis-regulatory elements. Proc. Natl Acad. Sci. USA 104, 18583-18588 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 18583-18588
    • Xiao, X.1    Wang, Z.2    Jang, M.3    Burge, C.B.4
  • 34
    • 2642525438 scopus 로고    scopus 로고
    • Computational definition of sequence motifs governing constitutive exon splicing
    • Zhang, X. H. & Chasin, L. A. Computational definition of sequence motifs governing constitutive exon splicing. Genes Dev. 18, 1241-1250 (2004
    • (2004) Genes Dev , vol.18 , pp. 1241-1250
    • Zhang, X.H.1    Chasin, L.A.2
  • 35
    • 27944440915 scopus 로고    scopus 로고
    • Computational searches for splicing signals
    • Zhang, X. H., Leslie, C. S. & Chasin, L. A. Computational searches for splicing signals. Methods 37, 292-305 (2005
    • (2005) Methods , vol.37 , pp. 292-305
    • Zhang, X.H.1    Leslie, C.S.2    Chasin, L.A.3
  • 36
    • 33745207758 scopus 로고    scopus 로고
    • Comparative analysis identifies exonic splicing regulatory sequences - The complex definition of enhancers and silencers
    • Goren, A. et al. Comparative analysis identifies exonic splicing regulatory sequences - the complex definition of enhancers and silencers. Mol. Cell 22, 769-781 (2006
    • (2006) Mol. Cell , vol.22 , pp. 769-781
    • Goren, A.1
  • 37
    • 0028805223 scopus 로고
    • Selection of novel exon recognition elements from a pool of
    • random sequences
    • Tian, H. & Kole, R. Selection of novel exon recognition elements from a pool of random sequences. Mol. Cell. Biol. 15, 6291-6298 (1995
    • (1995) Mol. Cell. Biol , vol.15 , pp. 6291-6298
    • Tian, H.1    Kole, R.2
  • 38
    • 0030988942 scopus 로고    scopus 로고
    • Identification of a new class of exonic splicing enhancers by in vivo selection
    • Coulter, L. R., Landree, M. A. & Cooper, T. A. Identification of a new class of exonic splicing enhancers by in vivo selection. Mol. Cell. Biol. 17, 2143-2150 (1997
    • (1997) Mol. Cell. Biol , vol.17 , pp. 2143-2150
    • Coulter, L.R.1    Landree, M.A.2    Cooper, T.A.3
  • 39
    • 10944256767 scopus 로고    scopus 로고
    • Systematic identification and analysis of exonic splicing silencers
    • Wang, Z. et al. Systematic identification and analysis of exonic splicing silencers. Cell 119, 831-845 (2004
    • (2004) Cell , vol.119 , pp. 831-845
    • Wang, Z.1
  • 40
    • 84867234474 scopus 로고    scopus 로고
    • Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules
    • Wang, Y., Ma, M., Xiao, X. & Wang, Z. Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules. Nature Struct. Mol. Biol. 19, 1044-1052 (2012
    • (2012) Nature Struct. Mol. Biol , vol.19 , pp. 1044-1052
    • Wang, Y.1    Ma, M.2    Xiao, X.3    Wang, Z.4
  • 41
    • 84872017252 scopus 로고    scopus 로고
    • A complex network of factors with overlapping affinities represses splicing through intronic elements
    • Wang, Y. et al. A complex network of factors with overlapping affinities represses splicing through intronic elements. Nature Struct. Mol. Biol. 20, 36-45 (2013
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 36-45
    • Wang, Y.1
  • 42
    • 80051562607 scopus 로고    scopus 로고
    • Quantitative evaluation of all hexamers as exonic splicing elements
    • Ke, S. et al. Quantitative evaluation of all hexamers as exonic splicing elements. Genome Res. 21, 1360-1374 (2011
    • (2011) Genome Res , vol.21 , pp. 1360-1374
    • Ke, S.1
  • 43
    • 84861969926 scopus 로고    scopus 로고
    • Insights into RNA biology from an atlas of mammalian mRNA-binding proteins
    • Castello, A. et al. Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149, 1393-1406 (2012
    • (2012) Cell , vol.149 , pp. 1393-1406
    • Castello, A.1
  • 44
    • 84883741725 scopus 로고    scopus 로고
    • The RNA-binding protein repertoire of embryonic stem cells
    • Kwon, S. C. et al. The RNA-binding protein repertoire of embryonic stem cells. Nature Struct. Mol. Biol. 20, 1122-1130 (2013
    • (2013) Nature Struct. Mol. Biol , vol.20 , pp. 1122-1130
    • Kwon, S.C.1
  • 45
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • Lunde, B. M., Moore, C. & Varani, G. RNA-binding proteins: modular design for efficient function. Nature Rev. Mol. Cell Biol. 8, 479-490 (2007
    • (2007) Nature Rev. Mol. Cell Biol , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 46
    • 84880427394 scopus 로고    scopus 로고
    • A compendium of RNA-binding motifs for decoding gene regulation
    • Ray, D. et al. A compendium of RNA-binding motifs for decoding gene regulation. Nature 499, 172-177 (2013
    • (2013) Nature , vol.499 , pp. 172-177
    • Ray, D.1
  • 47
    • 77955662560 scopus 로고    scopus 로고
    • An alternative splicing network links cell-cycle control to apoptosis
    • Moore, M. J., Wang, Q., Kennedy, C. J. & Silver, P. A. An alternative splicing network links cell-cycle control to apoptosis. Cell 142, 625-636 (2010
    • (2010) Cell , vol.142 , pp. 625-636
    • Moore, M.J.1    Wang, Q.2    Kennedy, C.J.3    Silver, P.A.4
  • 48
    • 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
  • 49
    • 0025740935 scopus 로고
    • Crosslinking proteins to nucleic acids by ultraviolet laser irradiation
    • Pashev, I. G., Dimitrov, S. I. & Angelov, D. Crosslinking proteins to nucleic acids by ultraviolet laser irradiation. Trends Biochem. Sci. 16, 323-326 (1991
    • (1991) Trends Biochem. Sci , vol.16 , pp. 323-326
    • Pashev, I.G.1    Dimitrov, S.I.2    Angelov, D.3
  • 50
    • 0242497663 scopus 로고    scopus 로고
    • CLIP identifies Nova-regulated RNA networks in the brain
    • Ule, J. et al. CLIP identifies Nova-regulated RNA networks in the brain. Science 302, 1212-1215 (2003
    • (2003) Science , vol.302 , pp. 1212-1215
    • Ule, J.1
  • 51
    • 77950920903 scopus 로고    scopus 로고
    • Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP
    • Hafner, M. et al. Transcriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP. Cell 141, 129-141 (2010
    • (2010) Cell , vol.141 , pp. 129-141
    • Hafner, M.1
  • 52
    • 77954387023 scopus 로고    scopus 로고
    • ICLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution
    • Konig, J. et al. iCLIP reveals the function of hnRNP particles in splicing at individual nucleotide resolution. Nature Struct. Mol. Biol. 17, 909-915 (2010
    • (2010) Nature Struct. Mol. Biol , vol.17 , pp. 909-915
    • Konig, J.1
  • 53
    • 84901913783 scopus 로고    scopus 로고
    • RNA Bind n Seq: Quantitative assessment of the sequence and structural binding specificity of RNA binding proteins
    • Lambert, N. et al. RNA Bind n Seq: quantitative assessment of the sequence and structural binding specificity of RNA binding proteins. Mol. Cell 54, 887-900 (2014
    • (2014) Mol. Cell , vol.54 , pp. 887-900
    • Lambert, N.1
  • 54
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors
    • Wiley Interdiscip
    • Busch, A. & Hertel, K. J. Evolution of SR protein and hnRNP splicing regulatory factors. Wiley Interdiscip. Rev. RNA 3, 1-12 (2012
    • (2012) Rev. RNA , vol.3 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 55
    • 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
  • 56
    • 0029372979 scopus 로고
    • The superfamily of arginine/serine-rich splicing factors
    • Fu, X. D. The superfamily of arginine/serine-rich splicing factors. RNA 1, 663-680 (1995
    • (1995) RNA , vol.1 , pp. 663-680
    • Fu, X.D.1
  • 57
    • 84878582352 scopus 로고    scopus 로고
    • Regulation of splicing by SR proteins and SR protein-specific kinases
    • Zhou, Z. & Fu, X. D. Regulation of splicing by SR proteins and SR protein-specific kinases. Chromosoma 122, 191-207 (2013
    • (2013) Chromosoma , vol.122 , pp. 191-207
    • Zhou, Z.1    Fu, X.D.2
  • 58
    • 84860268701 scopus 로고    scopus 로고
    • The RNA-binding landscapes of two SR proteins reveal unique functions and binding to diverse RNA classes
    • Anko, M. L. et al. The RNA-binding landscapes of two SR proteins reveal unique functions and binding to diverse RNA classes. Genome Biol. 13, R17 (2012
    • (2012) Genome Biol , vol.13 , pp. R17
    • Anko, M.L.1
  • 59
    • 84876839218 scopus 로고    scopus 로고
    • Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing
    • Pandit, S. et al. Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing. Mol. Cell 50, 223-235 (2013
    • (2013) Mol. Cell , vol.50 , pp. 223-235
    • Pandit, S.1
  • 60
    • 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
  • 61
    • 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
  • 62
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda, A. & Krainer, A. R. Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68, 365-375 (1992
    • (1992) Cell , vol.68 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 63
    • 0028061367 scopus 로고
    • Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins
    • Mayeda, A., Munroe, S. H., Caceres, J. F. & Krainer, A. R. Function of conserved domains of hnRNP A1 and other hnRNP A/B proteins. EMBO J. 13, 5483-5495 (1994
    • (1994) EMBO J. , vol.13 , pp. 5483-5495
    • Mayeda, A.1    Munroe, S.H.2    Caceres, J.F.3    Krainer, A.R.4
  • 64
    • 0035691667 scopus 로고    scopus 로고
    • Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins
    • Zhu, J., Mayeda, A. & Krainer, A. R. Exon identity established through differential antagonism between exonic splicing silencer-bound hnRNP A1 and enhancer-bound SR proteins. Mol. Cell 8, 1351-1361 (2001
    • (2001) Mol. Cell , vol.8 , pp. 1351-1361
    • Zhu, J.1    Mayeda, A.2    Krainer, A.R.3
  • 66
    • 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
  • 67
    • 77956342570 scopus 로고    scopus 로고
    • Position-dependent alternative splicing activity revealed by global profiling of alternative splicing events regulated by PTB
    • Llorian, M. et al. Position-dependent alternative splicing activity revealed by global profiling of alternative splicing events regulated by PTB. Nature Struct. Mol. Biol. 17, 1114-1123 (2010
    • (2010) Nature Struct. Mol. Biol , vol.17 , pp. 1114-1123
    • Llorian, M.1
  • 68
    • 72149117411 scopus 로고    scopus 로고
    • Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping
    • Xue, Y. et al. Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping. Mol. Cell 36, 996-1006 (2009
    • (2009) Mol. Cell , vol.36 , pp. 996-1006
    • Xue, Y.1
  • 69
    • 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
  • 70
    • 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
  • 71
    • 79951996054 scopus 로고    scopus 로고
    • U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression
    • Sharma, S., Maris, C., Allain, F. H. & Black, D. L. U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression. Mol. Cell 41, 579-588 (2011
    • (2011) Mol. Cell , vol.41 , pp. 579-588
    • Sharma, S.1    Maris, C.2    Allain, F.H.3    Black, D.L.4
  • 72
    • 84876820281 scopus 로고    scopus 로고
    • Hnrnp L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly
    • Chiou, N. T., Shankarling, G. & Lynch, K. W. hnRNP L and hnRNP A1 induce extended U1 snRNA interactions with an exon to repress spliceosome assembly. Mol. Cell 49, 972-982 (2013
    • (2013) Mol. Cell , vol.49 , pp. 972-982
    • Chiou, N.T.1    Shankarling, G.2    Lynch, K.W.3
  • 73
    • 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
  • 74
    • 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
  • 75
    • 52949090808 scopus 로고    scopus 로고
    • A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4
    • Topp, J. D., Jackson, J., Melton, A. A. & Lynch, K. W. A cell-based screen for splicing regulators identifies hnRNP LL as a distinct signal-induced repressor of CD45 variable exon 4. RNA 14, 2038-2049 (2008
    • (2008) RNA , vol.14 , pp. 2038-2049
    • Topp, J.D.1    Jackson, J.2    Melton, A.A.3    Lynch, K.W.4
  • 76
    • 48749100692 scopus 로고    scopus 로고
    • Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL
    • Oberdoerffer, S. et al. Regulation of CD45 alternative splicing by heterogeneous ribonucleoprotein, hnRNPLL. Science 321, 686-691 (2008
    • (2008) Science , vol.321 , pp. 686-691
    • Oberdoerffer, S.1
  • 77
    • 69449093703 scopus 로고    scopus 로고
    • Regulation of vertebrate nervous system alternative splicing and development by an SR related protein
    • Calarco, J. A. et al. Regulation of vertebrate nervous system alternative splicing and development by an SR related protein. Cell 138, 898-910 (2009
    • (2009) Cell , vol.138 , pp. 898-910
    • Calarco, J.A.1
  • 78
    • 84861161751 scopus 로고    scopus 로고
    • Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins
    • Huelga, S. C. et al. Integrative genome-wide analysis reveals cooperative regulation of alternative splicing by hnRNP proteins. Cell Rep. 1, 167-178 (2012
    • (2012) Cell Rep , vol.1 , pp. 167-178
    • Huelga, S.C.1
  • 79
    • 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
  • 80
    • 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
  • 81
    • 61449176062 scopus 로고    scopus 로고
    • Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones
    • Zhong, X. Y., Ding, J. H., Adams, J. A., Ghosh, G. & Fu, X. D. Regulation of SR protein phosphorylation and alternative splicing by modulating kinetic interactions of SRPK1 with molecular chaperones. Genes Dev. 23, 482-495 (2009
    • (2009) Genes Dev , vol.23 , pp. 482-495
    • Zhong, X.Y.1    Ding, J.H.2    Adams, J.A.3    Ghosh, G.4    Fu, X.D.5
  • 82
    • 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
  • 83
    • 84865201988 scopus 로고    scopus 로고
    • Transcriptome-wide regulation of pre-mRNA splicing and mRNA localization by muscleblind proteins
    • Wang, E. T. et al. Transcriptome-wide regulation of pre-mRNA splicing and mRNA localization by muscleblind proteins. Cell 150, 710-724 (2012
    • (2012) Cell , vol.150 , pp. 710-724
    • Wang, E.T.1
  • 84
    • 76249102027 scopus 로고    scopus 로고
    • Aberrant alternative splicing and extracellular matrix gene expression in mouse models of myotonic dystrophy
    • Du, H. et al. Aberrant alternative splicing and extracellular matrix gene expression in mouse models of myotonic dystrophy. Nature Struct. Mol. Biol. 17, 187-193 (2010
    • (2010) Nature Struct. Mol. Biol , vol.17 , pp. 187-193
    • Du, H.1
  • 85
    • 84876512920 scopus 로고    scopus 로고
    • Quaking and PTB control overlapping splicing regulatory networks during muscle cell differentiation
    • Hall, M. P. et al. Quaking and PTB control overlapping splicing regulatory networks during muscle cell differentiation. RNA 19, 627-638 (2013
    • (2013) RNA , vol.19 , pp. 627-638
    • Hall, M.P.1
  • 86
    • 77950552549 scopus 로고    scopus 로고
    • The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events
    • Warzecha, C. C., Shen, S., Xing, Y. & Carstens, R. P. The epithelial splicing factors ESRP1 and ESRP2 positively and negatively regulate diverse types of alternative splicing events. RNA Biol. 6, 546-562 (2009
    • (2009) RNA Biol , vol.6 , pp. 546-562
    • Warzecha, C.C.1    Shen, S.2    Xing, Y.3    Carstens, R.P.4
  • 87
    • 84861302942 scopus 로고    scopus 로고
    • Genome-wide determination of a broad ESRP-regulated posttranscriptional network by high-Throughput sequencing
    • Dittmar, K. A. et al. Genome-wide determination of a broad ESRP-regulated posttranscriptional network by high-Throughput sequencing. Mol. Cell. Biol. 32, 1468-1482 (2012
    • (2012) Mol. Cell. Biol , vol.32 , pp. 1468-1482
    • Dittmar, K.A.1
  • 88
    • 2442694425 scopus 로고    scopus 로고
    • And Genome Conservation of Alternative Splicing Events in Humans and Mice
    • Sugnet, C. W., Kent, W. J., Ares, M. Jr & Haussler, D. Transcriptome and genome conservation of alternative splicing events in humans and mice. Pac. Symp. Biocomput. 2004, 66-77 (2004
    • (2004) Pac. Symp. Biocomput , vol.2004 , pp. 66-77
    • Sugnet, C.W.1    Kent, W.J.2    Ares, M.3    Transcriptome, H.D.4
  • 89
    • 79951715071 scopus 로고    scopus 로고
    • Regulation of alternative splicing by the core spliceosomal machinery
    • Saltzman, A. L., Pan, Q. & Blencowe, B. J. Regulation of alternative splicing by the core spliceosomal machinery. Genes Dev. 25, 373-384 (2011
    • (2011) Genes Dev , vol.25 , pp. 373-384
    • Saltzman, A.L.1    Pan, Q.2    Blencowe, B.J.3
  • 90
    • 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
  • 91
    • 0034853047 scopus 로고    scopus 로고
    • Modulation of P element pre-mRNA splicing by a direct interaction between PSI and U1 snRNP 70K protein
    • Labourier, E., Adams, M. D. & Rio, D. C. Modulation of P element pre-mRNA splicing by a direct interaction between PSI and U1 snRNP 70K protein. Mol. Cell 8, 363-373 (2001
    • (2001) Mol. Cell , vol.8 , pp. 363-373
    • Labourier, E.1    Adams, M.D.2    Rio, D.C.3
  • 92
    • 84862807502 scopus 로고    scopus 로고
    • Nuclear matrix factor hnRNP U/SAF A exerts a global control of alternative splicing by regulating U2 snRNP maturation
    • Xiao, R. et al. Nuclear matrix factor hnRNP U/SAF A exerts a global control of alternative splicing by regulating U2 snRNP maturation. Mol. Cell 45, 656-668 (2012
    • (2012) Mol. Cell , vol.45 , pp. 656-668
    • Xiao, R.1
  • 93
    • 84881494632 scopus 로고    scopus 로고
    • Competition between pre-mRNAs for the splicing machinery drives global regulation of splicing
    • Munding, E. M., Shiue, L., Katzman, S., Donohue, J. P. & Ares, Jr. M. Competition between pre-mRNAs for the splicing machinery drives global regulation of splicing. Mol. Cell 51, 338-348 (2013
    • (2013) Mol. Cell , vol.51 , pp. 338-348
    • Munding, E.M.1    Shiue, L.2    Katzman, S.3    Donohue, J.P.4    Ares, M.5
  • 94
    • 35848950003 scopus 로고    scopus 로고
    • Prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast
    • Boon, K. L. et al. prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast. Nature Struct. Mol. Biol. 14, 1077-1083 (2007
    • (2007) Nature Struct. Mol. Biol , vol.14 , pp. 1077-1083
    • Boon, K.L.1
  • 95
    • 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
  • 96
    • 80053900941 scopus 로고    scopus 로고
    • Frequent pathway mutations of splicing machinery in myelodysplasia
    • Yoshida, K. et al. Frequent pathway mutations of splicing machinery in myelodysplasia. Nature 478, 64-69 (2011
    • (2011) Nature , vol.478 , pp. 64-69
    • Yoshida, K.1
  • 97
    • 34748892292 scopus 로고    scopus 로고
    • Combinatorial control of signal-induced exon repression by hnRNP L and PSF
    • Melton, A. A., Jackson, J., Wang, J. & Lynch, K. W. Combinatorial control of signal-induced exon repression by hnRNP L and PSF. Mol. Cell. Biol. 27, 6972-6984 (2007
    • (2007) Mol. Cell. Biol , vol.27 , pp. 6972-6984
    • Melton, A.A.1    Jackson, J.2    Wang, J.3    Lynch, K.W.4
  • 98
    • 23844471326 scopus 로고    scopus 로고
    • Hnrnp L represses exon splicing via a regulated exonic splicing silencer
    • Rothrock, C. R., House, A. E. & Lynch, K. W. hnRNP L represses exon splicing via a regulated exonic splicing silencer. EMBO J. 24, 2792-2802 (2005
    • (2005) EMBO J. , vol.24 , pp. 2792-2802
    • Rothrock, C.R.1    House, A.E.2    Lynch, K.W.3
  • 99
    • 21244469877 scopus 로고    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
    • (2005) EMBO J. , vol.24 , pp. 1988-1998
    • Hui, J.1
  • 100
    • 0037217365 scopus 로고    scopus 로고
    • HnRNP L stimulates splicing of the eNOS gene by binding to variable-length CA repeats
    • Hui, J., Stangl, K., Lane, W. S. & Bindereif, A. hnRNP L stimulates splicing of the eNOS gene by binding to variable-length CA repeats. Nature Struct. Biol. 10, 33-37 (2003
    • (2003) Nature Struct. Biol , vol.10 , pp. 33-37
    • Hui, J.1    Stangl, K.2    Lane, W.S.3    Bindereif, A.4
  • 101
    • 70349843229 scopus 로고    scopus 로고
    • Splice site strength-dependent activity and genetic buffering by poly G runs
    • Xiao, X. et al. Splice site strength-dependent activity and genetic buffering by poly G runs. Nature Struct. Mol. Biol. 16, 1094-1100 (2009
    • (2009) Nature Struct. Mol. Biol , vol.16 , pp. 1094-1100
    • Xiao, X.1
  • 102
    • 0032953308 scopus 로고    scopus 로고
    • HnRNP H is a component of a splicing enhancer complex that activates A C src alternative exon in neuronal cells
    • Chou, M. Y., Rooke, N., Turck, C. W. & Black, D. L. hnRNP H is a component of a splicing enhancer complex that activates a c src alternative exon in neuronal cells. Mol. Cell. Biol. 19, 69-77 (1999
    • (1999) Mol. Cell. Biol , vol.19 , pp. 69-77
    • Chou, M.Y.1    Rooke, N.2    Turck, C.W.3    Black, D.L.4
  • 103
    • 0033105787 scopus 로고    scopus 로고
    • Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-Tropomyosin gene
    • Chen, C. D., Kobayashi, R. & Helfman, D. M. Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta-Tropomyosin gene. Genes Dev. 13, 593-606 (1999
    • (1999) Genes Dev , vol.13 , pp. 593-606
    • Chen, C.D.1    Kobayashi, R.2    Helfman, D.M.3
  • 104
    • 33845213293 scopus 로고    scopus 로고
    • Activation of alpha-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 alpha-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
  • 105
    • 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
  • 106
    • 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 , pp. e21
    • Martinez-Contreras, R.1
  • 107
    • 20744450092 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl x
    • Garneau, D., Revil, T., Fisette, J. F. & Chabot, B. Heterogeneous nuclear ribonucleoprotein F/H proteins modulate the alternative splicing of the apoptotic mediator Bcl x. J. Biol. Chem. 280, 22641-22650 (2005
    • (2005) J. Biol. Chem , vol.280 , pp. 22641-22650
    • Garneau, D.1    Revil, T.2    Fisette, J.F.3    Chabot, B.4
  • 108
    • 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
  • 109
    • 84871401549 scopus 로고    scopus 로고
    • Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms
    • Erkelenz, S. et al. Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms. RNA 19, 96-102 (2013
    • (2013) RNA , vol.19 , pp. 96-102
    • Erkelenz, S.1
  • 110
    • 34547830368 scopus 로고    scopus 로고
    • SR protein-mediated inhibition of CFTR exon 9 inclusion: Molecular characterization of the intronic splicing silencer
    • Buratti, E., Stuani, C., De Prato, G. & Baralle, F. E. SR protein-mediated inhibition of CFTR exon 9 inclusion: molecular characterization of the intronic splicing silencer. Nucleic Acids Res. 35, 4359-4368 (2007
    • (2007) Nucleic Acids Res , vol.35 , pp. 4359-4368
    • Buratti, E.1    Stuani, C.2    De Prato, G.3    Baralle, F.E.4
  • 111
    • 0032482968 scopus 로고    scopus 로고
    • Regulation of Ich 1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors
    • Jiang, Z. H., Zhang, W. J., Rao, Y. & Wu, J. Y. Regulation of Ich 1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors. Proc. Natl Acad. Sci. USA 95, 9155-9160 (1998
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 9155-9160
    • Jiang, Z.H.1    Zhang, W.J.2    Rao, Y.3    Wu, J.Y.4
  • 112
    • 74749089043 scopus 로고    scopus 로고
    • Context-dependent regulatory mechanism of the splicing factor hnRNP L
    • Motta-Mena, L. B., Heyd, F. & Lynch, K. W. Context-dependent regulatory mechanism of the splicing factor hnRNP L. Mol. Cell 37, 223-234 (2010
    • (2010) Mol Cell , vol.37 , pp. 223-234
    • Motta-Mena, L.B.1    Heyd, F.2    Lynch, K.W.3
  • 113
    • 84862950521 scopus 로고    scopus 로고
    • Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2
    • Sun, S., Zhang, Z., Fregoso, O. & Krainer, A. R. Mechanisms of activation and repression by the alternative splicing factors RBFOX1/2. RNA 18, 274-283 (2012
    • (2012) RNA , vol.18 , pp. 274-283
    • Sun, S.1    Zhang, Z.2    Fregoso, O.3    Krainer, A.R.4
  • 114
    • 75149194407 scopus 로고    scopus 로고
    • Autoregulation of Fox protein expression to produce dominant negative splicing factors
    • Damianov, A. & Black, D. L. Autoregulation of Fox protein expression to produce dominant negative splicing factors. RNA 16, 405-416 (2010
    • (2010) RNA , vol.16 , pp. 405-416
    • Damianov, A.1    Black, D.L.2
  • 115
    • 84878995293 scopus 로고    scopus 로고
    • MBNL proteins repress ES cell-specific alternative splicing and reprogramming
    • Han, H. et al. MBNL proteins repress ES cell-specific alternative splicing and reprogramming. Nature 498, 241-245 (2013
    • (2013) Nature , vol.498 , pp. 241-245
    • Han, H.1
  • 116
    • 79251584960 scopus 로고    scopus 로고
    • SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons
    • Han, J. et al. SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons. Mol. Cell. Biol. 31, 793-802 (2011
    • (2011) Mol. Cell. Biol , vol.31 , pp. 793-802
    • Han, J.1
  • 117
    • 79957865299 scopus 로고    scopus 로고
    • Pre-mRNA splicing: Where and when in the nucleus
    • Han, J., Xiong, J., Wang, D. & Fu, X. D. Pre-mRNA splicing: where and when in the nucleus. Trends Cell Biol. 21, 336-343 (2011
    • (2011) Trends Cell Biol , vol.21 , pp. 336-343
    • Han, J.1    Xiong, J.2    Wang, D.3    Fu, X.D.4
  • 118
    • 84890192305 scopus 로고    scopus 로고
    • RBM5, 6, and 10 differentially regulate NUMB alternative splicing to control cancer cell proliferation
    • Bechara, E. G., Sebestyen, E., Bernardis, I., Eyras, E. & Valcarcel, J. RBM5, 6, and 10 differentially regulate NUMB alternative splicing to control cancer cell proliferation. Mol. Cell 52, 720-733 (2013
    • (2013) Mol. Cell , vol.52 , pp. 720-733
    • Bechara, E.G.1    Sebestyen, E.2    Bernardis, I.3    Eyras, E.4    Valcarcel, J.5
  • 119
    • 70350569286 scopus 로고    scopus 로고
    • Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches
    • Chen, M. & Manley, J. L. Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches. Nature Rev. Mol. Cell Biol. 10, 741-754 (2009
    • (2009) Nature Rev. Mol. Cell Biol , vol.10 , pp. 741-754
    • Chen, M.1    Manley, J.L.2
  • 120
    • 19944427655 scopus 로고    scopus 로고
    • ASF/SF2 regulated CaMKII? Alternative splicing temporally reprograms excitation-contraction coupling in cardiac muscle
    • Xu, X. et al. ASF/SF2 regulated CaMKII? 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
  • 121
    • 64549159302 scopus 로고    scopus 로고
    • SRp38 regulates alternative splicing and is required for Ca2+ 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
  • 122
    • 84898747945 scopus 로고    scopus 로고
    • The splicing regulator PTBP2 controls a program of embryonic splicing required for neuronal maturation
    • Li, Q. et al. The splicing regulator PTBP2 controls a program of embryonic splicing required for neuronal maturation. Elife 3, e01201 (2014
    • (2014) Elife , vol.3 , pp. e01201
    • Li, Q.1
  • 123
    • 84864020005 scopus 로고    scopus 로고
    • Ptbp2 represses adult-specific splicing to regulate the generation of neuronal precursors in the embryonic brain
    • Licatalosi, D. D. et al. Ptbp2 represses adult-specific splicing to regulate the generation of neuronal precursors in the embryonic brain. Genes Dev. 26, 1626-1642 (2012
    • (2012) Genes Dev , vol.26 , pp. 1626-1642
    • Licatalosi, D.D.1
  • 124
    • 37549047982 scopus 로고    scopus 로고
    • The Fox 1 family and SUP 12 coordinately regulate tissue-specific alternative splicing in vivo
    • Kuroyanagi, H., Ohno, G., Mitani, S. & Hagiwara, M. The Fox 1 family and SUP 12 coordinately regulate tissue-specific alternative splicing in vivo. Mol. Cell. Biol. 27, 8612-8621 (2007
    • (2007) Mol. Cell. Biol , vol.27 , pp. 8612-8621
    • Kuroyanagi, H.1    Ohno, G.2    Mitani, S.3    Hagiwara, M.4
  • 125
    • 77954838957 scopus 로고    scopus 로고
    • Integrative modeling defines the Nova splicing-regulatory network and its combinatorial controls
    • Zhang, C. et al. Integrative modeling defines the Nova splicing-regulatory network and its combinatorial controls. Science 329, 439-443 (2010
    • (2010) Science , vol.329 , pp. 439-443
    • Zhang, C.1
  • 126
    • 84868110958 scopus 로고    scopus 로고
    • Muscle-specific splicing factors ASD 2 and SUP 12 cooperatively switch alternative pre-mRNA processing patterns of the ADF/cofilin gene in Caenorhabditis elegans
    • Ohno, G. et al. Muscle-specific splicing factors ASD 2 and SUP 12 cooperatively switch alternative pre-mRNA processing patterns of the ADF/cofilin gene in Caenorhabditis elegans. PLoS Genet. 8, e1002991 (2012
    • (2012) PLoS Genet , vol.8 , pp. e1002991
    • Ohno, G.1
  • 127
    • 84866076924 scopus 로고    scopus 로고
    • Intrinsic disorder in the human spliceosomal proteome
    • Korneta, I. & Bujnicki, J. M. Intrinsic disorder in the human spliceosomal proteome. PLoS Comput. Biol. 8, e1002641 (2012
    • (2012) PLoS Comput. Biol , vol.8 , pp. e1002641
    • Korneta, I.1    Bujnicki, J.M.2
  • 128
    • 84860863700 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Bound RNAs identify features and components of cellular assemblies
    • Han, T. W. et al. Cell-free formation of RNA granules: bound RNAs identify features and components of cellular assemblies. Cell 149, 768-779 (2012
    • (2012) Cell , vol.149 , pp. 768-779
    • Han, T.W.1
  • 129
    • 84860872161 scopus 로고    scopus 로고
    • Cell-free formation of RNA granules: Low complexity sequence domains form dynamic fibers within hydrogels
    • Kato, M. et al. Cell-free formation of RNA granules: low complexity sequence domains form dynamic fibers within hydrogels. Cell 149, 753-767 (2012
    • (2012) Cell , vol.149 , pp. 753-767
    • Kato, M.1
  • 130
    • 84875605133 scopus 로고    scopus 로고
    • Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS
    • Kim, H. J. et al. Mutations in prion-like domains in hnRNPA2B1 and hnRNPA1 cause multisystem proteinopathy and ALS. Nature 495, 467-473 (2013
    • (2013) Nature , vol.495 , pp. 467-473
    • Kim, H.J.1
  • 131
    • 84878661360 scopus 로고    scopus 로고
    • Stress granules as crucibles of ALS pathogenesis
    • Li, Y. R., King, O. D., Shorter, J. & Gitler, A. D. Stress granules as crucibles of ALS pathogenesis. J. Cell Biol. 201, 361-372 (2013
    • (2013) J. Cell Biol , vol.201 , pp. 361-372
    • Li, Y.R.1    King, O.D.2    Shorter, J.3    Gitler, A.D.4
  • 133
    • 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
  • 134
    • 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
  • 135
    • 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
  • 136
    • 84872601985 scopus 로고    scopus 로고
    • Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits
    • Xue, Y. et al. Direct conversion of fibroblasts to neurons by reprogramming PTB-regulated microRNA circuits. Cell 152, 82-96 (2013
    • (2013) Cell , vol.152 , pp. 82-96
    • Xue, Y.1
  • 137
    • 84857653757 scopus 로고    scopus 로고
    • PSD 95 is post-Transcriptionally repressed during early neural development by PTBP1 and PTBP2
    • Zheng, S. et al. PSD 95 is post-Transcriptionally repressed during early neural development by PTBP1 and PTBP2. Nature Neurosci. 15, 381-388 (2012
    • (2012) Nature Neurosci , vol.15 , pp. 381-388
    • Zheng, S.1
  • 138
    • 0032916285 scopus 로고    scopus 로고
    • Combinatorial control of a neuron-specific exon
    • Modafferi, E. F. & Black, D. L. Combinatorial control of a neuron-specific exon. RNA 5, 687-706 (1999
    • (1999) RNA , vol.5 , pp. 687-706
    • Modafferi, E.F.1    Black, D.L.2
  • 139
    • 84873323035 scopus 로고    scopus 로고
    • Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements
    • Zarnack, K. et al. Direct competition between hnRNP C and U2AF65 protects the transcriptome from the exonization of Alu elements. Cell 152, 453-466 (2013
    • (2013) Cell , vol.152 , pp. 453-466
    • Zarnack, K.1
  • 140
    • 84868160135 scopus 로고    scopus 로고
    • LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance
    • Wilbert, M. L. et al. LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance. Mol. Cell 48, 195-206 (2012
    • (2012) Mol. Cell , vol.48 , pp. 195-206
    • Wilbert, M.L.1
  • 141
    • 84864624361 scopus 로고    scopus 로고
    • An integrated regulatory network reveals pervasive cross-regulation among transcription and splicing factors
    • Kosti, I., Radivojac, P. & Mandel-Gutfreund, Y. An integrated regulatory network reveals pervasive cross-regulation among transcription and splicing factors. PLoS Comput. Biol. 8, e1002603 (2012
    • (2012) PLoS Comput. Biol , vol.8 , pp. e1002603
    • Kosti, I.1    Radivojac, P.2    Mandel-Gutfreund, Y.3
  • 142
    • 84863003268 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing remodels protein-protein interaction networks
    • Ellis, J. D. et al. Tissue-specific alternative splicing remodels protein-protein interaction networks. Mol. Cell 46, 884-892 (2012
    • (2012) Mol. Cell , vol.46 , pp. 884-892
    • Ellis, J.D.1
  • 143
    • 33947305594 scopus 로고    scopus 로고
    • Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay
    • Ni, J. Z. et al. Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay. Genes Dev. 21, 708-718 (2007
    • (2007) Genes Dev , vol.21 , pp. 708-718
    • Ni, J.Z.1
  • 144
    • 34247330971 scopus 로고    scopus 로고
    • Unproductive splicing of SR genes associated with highly conserved and ultraconserved DNA elements
    • Lareau, L. F., Inada, M., Green, R. E., Wengrod, J. C. & Brenner, S. E. Unproductive splicing of SR genes associated with highly conserved and ultraconserved DNA elements. Nature 446, 926-929 (2007
    • (2007) Nature , vol.446 , pp. 926-929
    • Lareau, L.F.1    Inada, M.2    Green, R.E.3    Wengrod, J.C.4    Brenner, S.E.5
  • 145
    • 0035794679 scopus 로고    scopus 로고
    • SC35 autoregulates its expression by promoting splicing events that destabilize its mRNAs
    • Sureau, A., Gattoni, R., Dooghe, Y., Stevenin, J. & Soret, J. SC35 autoregulates its expression by promoting splicing events that destabilize its mRNAs. EMBO J. 20, 1785-1796 (2001
    • (2001) EMBO J. , vol.20 , pp. 1785-1796
    • Sureau, A.1    Gattoni, R.2    Dooghe, Y.3    Stevenin, J.4    Soret, J.5
  • 146
    • 84874262984 scopus 로고    scopus 로고
    • ALS-linked TDP 43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP 43
    • Arnold, E. S. et al. ALS-linked TDP 43 mutations produce aberrant RNA splicing and adult-onset motor neuron disease without aggregation or loss of nuclear TDP 43. Proc. Natl Acad. Sci. USA 110, E736-E745 (2013
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E736-E745
    • Arnold, E.S.1
  • 147
    • 84868152371 scopus 로고    scopus 로고
    • Divergent roles of ALS-linked proteins FUS/TLS and TDP 43 intersect in processing long pre-mRNAs
    • Lagier-Tourenne, C. et al. Divergent roles of ALS-linked proteins FUS/TLS and TDP 43 intersect in processing long pre-mRNAs. Nature Neurosci. 15, 1488-1497 (2012
    • (2012) Nature Neurosci , vol.15 , pp. 1488-1497
    • Lagier-Tourenne, C.1
  • 148
    • 84877721757 scopus 로고    scopus 로고
    • SR proteins collaborate with 7SK and promoter-Associated nascent RNA to release paused polymerase
    • Ji, X. et al. SR proteins collaborate with 7SK and promoter-Associated nascent RNA to release paused polymerase. Cell 153, 855-868 (2013
    • (2013) Cell , vol.153 , pp. 855-868
    • Ji, X.1
  • 150
    • 0035912224 scopus 로고    scopus 로고
    • A CaMK IV responsive RNA element mediates depolarization-induced alternative splicing of ion channels
    • Xie, J. & Black, D. L. A CaMK IV responsive RNA element mediates depolarization-induced alternative splicing of ion channels. Nature 410, 936-939 (2001
    • (2001) Nature , vol.410 , pp. 936-939
    • Xie, J.1    Black, D.L.2
  • 151
    • 59449098699 scopus 로고    scopus 로고
    • The heterogeneous nuclear ribonucleoprotein L is an essential component in the Ca2+/calmodulin-dependent protein kinase IV regulated alternative splicing through cytidine-Adenosine repeats
    • Yu, J. et al. The heterogeneous nuclear ribonucleoprotein L is an essential component in the Ca2+/calmodulin-dependent protein kinase IV regulated alternative splicing through cytidine-Adenosine repeats. J. Biol. Chem. 284, 1505-1513 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 1505-1513
    • Yu, J.1
  • 153
    • 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
  • 154
    • 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 Houven Van Oordt, W.1
  • 155
    • 79960925229 scopus 로고    scopus 로고
    • The Ewing sarcoma protein regulates DNA damage-induced alternative splicing
    • Paronetto, M. P., Minana, B. & Valcarcel, J. The Ewing sarcoma protein regulates DNA damage-induced alternative splicing. Mol. Cell 43, 353-368 (2011
    • (2011) Mol. Cell , vol.43 , pp. 353-368
    • Paronetto, M.P.1    Minana, B.2    Valcarcel, J.3
  • 156
    • 0037069651 scopus 로고    scopus 로고
    • Signal-dependent regulation of splicing via phosphorylation of Sam68
    • Matter, N., Herrlich, P. & Konig, H. Signal-dependent regulation of splicing via phosphorylation of Sam68. Nature 420, 691-695 (2002
    • (2002) Nature , vol.420 , pp. 691-695
    • Matter, N.1    Herrlich, P.2    Konig, H.3
  • 157
    • 84455200617 scopus 로고    scopus 로고
    • SAM68 regulates neuronal activity-dependent alternative splicing of neurexin 1
    • Iijima, T. et al. SAM68 regulates neuronal activity-dependent alternative splicing of neurexin 1. Cell 147, 1601-1614 (2011
    • (2011) Cell , vol.147 , pp. 1601-1614
    • Iijima, T.1
  • 158
    • 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
  • 159
    • 77957377260 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing
    • Heyd, F. & Lynch, K. W. Phosphorylation-dependent regulation of PSF by GSK3 controls CD45 alternative splicing. Mol. Cell 40, 126-137 (2010
    • (2010) Mol. Cell , vol.40 , pp. 126-137
    • Heyd, F.1    Lynch, K.W.2
  • 160
    • 79957784833 scopus 로고    scopus 로고
    • Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1 70K snRNP protein determines early spliceosome assembly
    • Cho, S. et al. Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1 70K snRNP protein determines early spliceosome assembly. Proc. Natl Acad. Sci. USA 108, 8233-8238 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 8233-8238
    • Cho, S.1
  • 161
    • 69949167523 scopus 로고    scopus 로고
    • Interaction of Akt-phosphorylated SRPK2 with 14
    • Jang, S. W. et al. Interaction of Akt-phosphorylated SRPK2 with 14 3 3 mediates cell cycle and cell death in neurons. J. Biol. Chem. 284, 24512-24525 (2009
    • (2009) J. Biol. Chem , vol.3 , Issue.284 , pp. 24512-24525
    • Jang, S.W.1
  • 162
    • 84864910082 scopus 로고    scopus 로고
    • The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus
    • Zhou, Z. et al. The Akt-SRPK-SR axis constitutes a major pathway in transducing EGF signaling to regulate alternative splicing in the nucleus. Mol. Cell 47, 422-433 (2012
    • (2012) Mol. Cell , vol.47 , pp. 422-433
    • Zhou, Z.1
  • 163
    • 84899821715 scopus 로고    scopus 로고
    • Both decreased and increased SRPK1 levels promote cancer by interfering with PHLPP-mediated dephosphorylation of Akt
    • Wang, P. et al. Both decreased and increased SRPK1 levels promote cancer by interfering with PHLPP-mediated dephosphorylation of Akt. Mol. Cell 54, 378-391 (2014
    • (2014) Mol. Cell , vol.54 , pp. 378-391
    • Wang, P.1
  • 164
    • 80053932983 scopus 로고    scopus 로고
    • Stress-responsive maturation of Clk1/4 pre-mRNAs promotes phosphorylation of SR splicing factor
    • Ninomiya, K., Kataoka, N. & Hagiwara, M. Stress-responsive maturation of Clk1/4 pre-mRNAs promotes phosphorylation of SR splicing factor. J. Cell Biol. 195, 27-40 (2011
    • (2011) J. Cell Biol , vol.195 , pp. 27-40
    • Ninomiya, K.1    Kataoka, N.2    Hagiwara, M.3
  • 165
    • 0026034658 scopus 로고
    • Mechanisms of alternative pre-mRNA splicing
    • Maniatis, T. Mechanisms of alternative pre-mRNA splicing. Science 251, 33-34 (1991
    • (1991) Science , vol.251 , pp. 33-34
    • Maniatis, T.1
  • 166
    • 70149112363 scopus 로고    scopus 로고
    • RNA gain of function in spinocerebellar ataxia type 8
    • Daughters, R. S. et al. RNA gain of function in spinocerebellar ataxia type 8. PLoS Genet. 5, e1000600 (2009
    • (2009) PLoS Genet , vol.5 , pp. e1000600
    • Daughters, R.S.1
  • 167
    • 84864912095 scopus 로고    scopus 로고
    • Muscleblind-like 2 mediated alternative splicing in the developing brain and dysregulation in myotonic dystrophy
    • Charizanis, K. et al. Muscleblind-like 2 mediated alternative splicing in the developing brain and dysregulation in myotonic dystrophy. Neuron 75, 437-450 (2012
    • (2012) Neuron , vol.75 , pp. 437-450
    • Charizanis, K.1
  • 168
    • 84897051164 scopus 로고    scopus 로고
    • HITS-CLIP and integrative modeling define the Rbfox splicing-regulatory network linked to brain development and autism
    • Weyn-Vanhentenryck, S. M. et al. HITS-CLIP and integrative modeling define the Rbfox splicing-regulatory network linked to brain development and autism. Cell Rep. 6, 1139-1152 (2014
    • (2014) Cell Rep , vol.6 , pp. 1139-1152
    • Weyn-Vanhentenryck, S.M.1
  • 169
    • 78149393552 scopus 로고    scopus 로고
    • ICLIP predicts the dual splicing effects of TIA-RNA interactions
    • Wang, Z. et al. iCLIP predicts the dual splicing effects of TIA-RNA interactions. PLoS Biol. 8, e1000530 (2010
    • (2010) PLoS Biol , vol.8 , pp. e1000530
    • Wang, Z.1
  • 170
    • 84861944874 scopus 로고    scopus 로고
    • An oxygen-regulated switch in the protein synthesis machinery
    • Uniacke, J. et al. An oxygen-regulated switch in the protein synthesis machinery. Nature 486, 126-129 (2012
    • (2012) Nature , vol.486 , pp. 126-129
    • Uniacke, J.1
  • 171
    • 79960929333 scopus 로고    scopus 로고
    • Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR
    • Lebedeva, S. et al. Transcriptome-wide analysis of regulatory interactions of the RNA-binding protein HuR. Mol. Cell 43, 340-352 (2011
    • (2011) Mol. Cell , vol.43 , pp. 340-352
    • Lebedeva, S.1
  • 172
    • 79960918737 scopus 로고    scopus 로고
    • Integrative regulatory mapping indicates that the RNA-binding protein HuR couples pre-mRNA processing and mRNA stability
    • Mukherjee, N. et al. Integrative regulatory mapping indicates that the RNA-binding protein HuR couples pre-mRNA processing and mRNA stability. Mol. Cell 43, 327-339 (2011
    • (2011) Mol. Cell , vol.43 , pp. 327-339
    • Mukherjee, N.1
  • 173
    • 84866505114 scopus 로고    scopus 로고
    • Neuronal Elav-like (Hu) proteins regulate RNA splicing and abundance to control glutamate levels and neuronal excitability
    • Ince-Dunn, G. et al. Neuronal Elav-like (Hu) proteins regulate RNA splicing and abundance to control glutamate levels and neuronal excitability. Neuron 75, 1067-1080 (2012
    • (2012) Neuron , vol.75 , pp. 1067-1080
    • Ince-Dunn, G.1
  • 174
    • 79953157487 scopus 로고    scopus 로고
    • Analysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicing
    • Corioni, M., Antih, N., Tanackovic, G., Zavolan, M. & Kramer, A. Analysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicing. Nucleic Acids Res. 39, 1868-1879 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. 1868-1879
    • Corioni, M.1    Antih, N.2    Tanackovic, G.3    Zavolan, M.4    Kramer, A.5
  • 175
    • 84896885113 scopus 로고    scopus 로고
    • Crosslinking-immunoprecipitation (iCLIP) analysis reveals global regulatory roles of hnRNP L.
    • Rossbach, O Et Al. Crosslinking-immunoprecipitation (ICLIP) Analysis Reveals Global Regulatory Roles of HnRNP L. RNA Biol. 11, 146-155 (2014
    • (2014) RNA Biol , vol.11 , pp. 146-155
    • Rossbach, O.1
  • 176
    • 84891387068 scopus 로고    scopus 로고
    • Transcriptome-wide RNA interaction profiling reveals physical and functional targets of hnRNP L in human T cells
    • Shankarling, G., Cole, B. S., Mallory, M. J. & Lynch, K. W. Transcriptome-wide RNA interaction profiling reveals physical and functional targets of hnRNP L in human T cells. Mol. Cell. Biol. 34, 71-83 (2014
    • (2014) Mol. Cell. Biol , vol.34 , pp. 71-83
    • Shankarling, G.1    Cole, B.S.2    Mallory, M.J.3    Lynch, K.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.