메뉴 건너뛰기




Volumn 110, Issue 30, 2013, Pages

Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition

Author keywords

NMR; Protein RNA complex; Splicing factor

Indexed keywords

SERINE ARGININE RICH PROTEIN;

EID: 84880676352     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1303445110     Document Type: Article
Times cited : (102)

References (78)
  • 1
    • 0033835333 scopus 로고    scopus 로고
    • Sorting out the complexity of SR protein functions
    • Graveley BR (2000) Sorting out the complexity of SR protein functions. RNA 6(9): 1197-1211.
    • (2000) RNA , vol.6 , Issue.9 , pp. 1197-1211
    • Graveley, B.R.1
  • 2
    • 70350569286 scopus 로고    scopus 로고
    • Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches
    • Chen M, Manley JL (2009) Mechanisms of alternative splicing regulation: Insights from molecular and genomics approaches. Nat Rev Mol Cell Biol 10(11):741-754.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , Issue.11 , pp. 741-754
    • Chen, M.1    Manley, J.L.2
  • 3
    • 14644445227 scopus 로고    scopus 로고
    • SRprises along a messenger's journey
    • Huang Y, Steitz JA (2005) SRprises along a messenger's journey. Mol Cell 17(5): 613-615.
    • (2005) Mol Cell , vol.17 , Issue.5 , pp. 613-615
    • Huang, Y.1    Steitz, J.A.2
  • 4
    • 58249093940 scopus 로고    scopus 로고
    • The SR protein family of splicing factors: Master regulators of gene expression
    • Long JC, Caceres JF (2009) The SR protein family of splicing factors: Master regulators of gene expression. Biochem J 417(1):15-27.
    • (2009) Biochem J , vol.417 , Issue.1 , pp. 15-27
    • Long, J.C.1    Caceres, J.F.2
  • 5
    • 67649671966 scopus 로고    scopus 로고
    • SR proteins in vertical integration of gene expression from transcription to RNA processing to translation
    • Zhong XY, Wang P, Han J, Rosenfeld MG, Fu XD (2009) SR proteins in vertical integration of gene expression from transcription to RNA processing to translation. Mol Cell 35(1):1-10.
    • (2009) Mol Cell , vol.35 , Issue.1 , pp. 1-10
    • Zhong, X.Y.1    Wang, P.2    Han, J.3    Rosenfeld, M.G.4    Fu, X.D.5
  • 7
    • 34547852903 scopus 로고    scopus 로고
    • SR proteins as potential targets for therapy
    • Soret J, Gabut M, Tazi J (2006) SR proteins as potential targets for therapy. Prog Mol Subcell Biol 44:65-87.
    • (2006) Prog Mol Subcell Biol , vol.44 , pp. 65-87
    • Soret, J.1    Gabut, M.2    Tazi, J.3
  • 8
    • 56749098074 scopus 로고    scopus 로고
    • Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
    • Pan Q, Shai O, Lee LJ, Frey BJ, Blencowe BJ (2008) Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing. Nat Genet 40(12):1413-1415.
    • (2008) Nat Genet , vol.40 , Issue.12 , pp. 1413-1415
    • Pan, Q.1    Shai, O.2    Lee, L.J.3    Frey, B.J.4    Blencowe, B.J.5
  • 9
    • 56549101959 scopus 로고    scopus 로고
    • Alternative isoform regulation in human tissue transcriptomes
    • Wang ET, et al. (2008) Alternative isoform regulation in human tissue transcriptomes. Nature 456(7221):470-476.
    • (2008) Nature , vol.456 , Issue.7221 , pp. 470-476
    • Wang, E.T.1
  • 10
    • 34548758543 scopus 로고    scopus 로고
    • Splicing in disease: Disruption of the splicing code and the decoding machinery
    • Wang GS, Cooper TA (2007) Splicing in disease: Disruption of the splicing code and the decoding machinery. Nat Rev Genet 8(10):749-761.
    • (2007) Nat Rev Genet , vol.8 , Issue.10 , pp. 749-761
    • Wang, G.S.1    Cooper, T.A.2
  • 11
    • 84861961269 scopus 로고    scopus 로고
    • Alternative splicing: Decoding an expansive regulatory layer
    • Irimia M, Blencowe BJ (2012) Alternative splicing: Decoding an expansive regulatory layer. Curr Opin Cell Biol 24(3):323-332.
    • (2012) Curr Opin Cell Biol , vol.24 , Issue.3 , pp. 323-332
    • Irimia, M.1    Blencowe, B.J.2
  • 12
    • 21244439380 scopus 로고    scopus 로고
    • Regulation of apoptosis by alternative premRNA splicing
    • Schwerk C, Schulze-Osthoff K (2005) Regulation of apoptosis by alternative premRNA splicing. Mol Cell 19(1):1-13.
    • (2005) Mol Cell , vol.19 , Issue.1 , pp. 1-13
    • Schwerk, C.1    Schulze-Osthoff, K.2
  • 13
    • 53149145051 scopus 로고    scopus 로고
    • RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition
    • Bonnal S, et al. (2008) RBM5/Luca-15/H37 regulates Fas alternative splice site pairing after exon definition. Mol Cell 32(1):81-95.
    • (2008) Mol Cell , vol.32 , Issue.1 , pp. 81-95
    • Bonnal, S.1
  • 14
    • 34548600067 scopus 로고    scopus 로고
    • U2AF-homology motif interactions are required for alternative splicing regulation by SPF45
    • Corsini L, et al. (2007) U2AF-homology motif interactions are required for alternative splicing regulation by SPF45. Nat Struct Mol Biol 14(7):620-629.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.7 , pp. 620-629
    • Corsini, L.1
  • 15
    • 0033636996 scopus 로고    scopus 로고
    • The apoptosis-promoting factor TIA-1 is a regulator of alternative pre-mRNA splicing
    • Förch P, et al. (2000) The apoptosis-promoting factor TIA-1 is a regulator of alternative pre-mRNA splicing. Mol Cell 6(5):1089-1098.
    • (2000) Mol Cell , vol.6 , Issue.5 , pp. 1089-1098
    • Förch, P.1
  • 16
    • 23744492690 scopus 로고    scopus 로고
    • Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition
    • Izquierdo JM, et al. (2005) Regulation of Fas alternative splicing by antagonistic effects of TIA-1 and PTB on exon definition. Mol Cell 19(4):475-484.
    • (2005) Mol Cell , vol.19 , Issue.4 , pp. 475-484
    • Izquierdo, J.M.1
  • 17
    • 0028274042 scopus 로고
    • Protection from Fas-mediated apoptosis by a soluble form of the Fas molecule
    • Cheng J, et al. (1994) Protection from Fas-mediated apoptosis by a soluble form of the Fas molecule. Science 263(5154):1759-1762.
    • (1994) Science , vol.263 , Issue.5154 , pp. 1759-1762
    • Cheng, J.1
  • 18
    • 14644431487 scopus 로고    scopus 로고
    • Broad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA
    • Bourgeois CF, Lejeune F, Stévenin J (2004) Broad specificity of SR (serine/arginine) proteins in the regulation of alternative splicing of pre-messenger RNA. Prog Nucleic Acid Res Mol Biol 78:37-88.
    • (2004) Prog Nucleic Acid Res Mol Biol , vol.78 , pp. 37-88
    • Bourgeois, C.F.1    Lejeune, F.2    Stévenin, J.3
  • 19
    • 0030850812 scopus 로고    scopus 로고
    • The splicing factor SRp20 modifies splicing of its own mRNA and ASF/SF2 antagonizes this regulation
    • Jumaa H, Nielsen PJ (1997) The splicing factor SRp20 modifies splicing of its own mRNA and ASF/SF2 antagonizes this regulation. EMBO J 16(16):5077-5085.
    • (1997) EMBO J , vol.16 , Issue.16 , pp. 5077-5085
    • Jumaa, H.1    Nielsen, P.J.2
  • 20
    • 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 FE (2007) SR protein-mediated inhibition of CFTR exon 9 inclusion: Molecular characterization of the intronic splicing silencer. Nucleic Acids Res 35(13):4359-4368.
    • (2007) Nucleic Acids Res , vol.35 , Issue.13 , pp. 4359-4368
    • Buratti, E.1    Stuani, C.2    De Prato, G.3    Baralle, F.E.4
  • 21
    • 0030998715 scopus 로고    scopus 로고
    • The SR splicing factors ASF/SF2 and SC35 have antagonistic effects on intronic enhancer-dependent splicing of the beta-tropomyosin alternative exon 6A
    • Gallego ME, Gattoni R, Stévenin J, Marie J, Expert-Bezançon A (1997) The SR splicing factors ASF/SF2 and SC35 have antagonistic effects on intronic enhancer-dependent splicing of the beta-tropomyosin alternative exon 6A. EMBO J 16(7):1772-1784.
    • (1997) EMBO J , vol.16 , Issue.7 , pp. 1772-1784
    • Gallego, M.E.1    Gattoni, R.2    Stévenin, J.3    Marie, J.4    Expert- Bezançon, A.5
  • 22
    • 79251584960 scopus 로고    scopus 로고
    • SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons
    • Han J, et al. (2011) SR proteins induce alternative exon skipping through their activities on the flanking constitutive exons. Mol Cell Biol 31(4):793-802.
    • (2011) Mol Cell Biol , vol.31 , Issue.4 , pp. 793-802
    • Han, J.1
  • 23
    • 0032482968 scopus 로고    scopus 로고
    • Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors
    • Jiang ZH, Zhang WJ, Rao Y, Wu JY (1998) Regulation of Ich-1 pre-mRNA alternative splicing and apoptosis by mammalian splicing factors. Proc Natl Acad Sci USA 95(16): 9155-9160.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.16 , pp. 9155-9160
    • Jiang, Z.H.1    Zhang, W.J.2    Rao, Y.3    Wu, J.Y.4
  • 24
    • 0033053790 scopus 로고    scopus 로고
    • SF2 and SRp55 regulation of CD45 exon 4 skipping during T cell activation
    • Lemaire R, Winne A, Sarkissian M, Lafyatis R (1999) SF2 and SRp55 regulation of CD45 exon 4 skipping during T cell activation. Eur J Immunol 29(3):823-837.
    • (1999) Eur J Immunol , vol.29 , Issue.3 , pp. 823-837
    • Lemaire, R.1    Winne, A.2    Sarkissian, M.3    Lafyatis, R.4
  • 25
    • 53049092777 scopus 로고    scopus 로고
    • Growth hormone deficiency and splicing fidelity: Two serine/arginine-rich proteins, ASF/SF2 and SC35, act antagonistically
    • Solis AS, Peng R, Crawford JB, Phillips JA, 3rd, Patton JG (2008) Growth hormone deficiency and splicing fidelity: Two serine/arginine-rich proteins, ASF/SF2 and SC35, act antagonistically. J Biol Chem 283(35):23619-23626.
    • (2008) J Biol Chem , vol.283 , Issue.35 , pp. 23619-23626
    • Solis, A.S.1    Peng, R.2    Crawford, J.B.3    Phillips III, J.A.4    Patton, J.G.5
  • 26
    • 0034658619 scopus 로고    scopus 로고
    • Regulation of alternative splicing of CD45 by antagonistic effects of SR protein splicing factors
    • ten Dam GB, et al. (2000) Regulation of alternative splicing of CD45 by antagonistic effects of SR protein splicing factors. J Immunol 164(10):5287-5295.
    • (2000) J Immunol , vol.164 , Issue.10 , pp. 5287-5295
    • Ten Dam, G.B.1
  • 27
    • 8644268780 scopus 로고    scopus 로고
    • A pathway of sequential arginine-serine-rich domainsplicing signal interactions during mammalian spliceosome assembly
    • Shen H, Green MR (2004) A pathway of sequential arginine-serine-rich domainsplicing signal interactions during mammalian spliceosome assembly. Mol Cell 16(3): 363-373.
    • (2004) Mol Cell , vol.16 , Issue.3 , pp. 363-373
    • Shen, H.1    Green, M.R.2
  • 28
    • 0028289188 scopus 로고
    • Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors
    • Kohtz JD, et al. (1994) Protein-protein interactions and 5'-splice-site recognition in mammalian mRNA precursors. Nature 368(6467):119-124.
    • (1994) Nature , vol.368 , Issue.6467 , pp. 119-124
    • Kohtz, J.D.1
  • 29
    • 0027137934 scopus 로고
    • Specific interactions between proteins implicated in splice site selection and regulated alternative splicing
    • Wu JY, Maniatis T (1993) Specific interactions between proteins implicated in splice site selection and regulated alternative splicing. Cell 75(6):1061-1070.
    • (1993) Cell , vol.75 , Issue.6 , pp. 1061-1070
    • Wu, J.Y.1    Maniatis, T.2
  • 30
    • 0028324929 scopus 로고
    • The role of specific protein-RNA and proteinprotein interactions in positive and negative control of pre-mRNA splicing by Transformer 2
    • Amrein H, Hedley ML, Maniatis T (1994) The role of specific protein-RNA and proteinprotein interactions in positive and negative control of pre-mRNA splicing by Transformer 2. Cell 76(4):735-746.
    • (1994) Cell , vol.76 , Issue.4 , pp. 735-746
    • Amrein, H.1    Hedley, M.L.2    Maniatis, T.3
  • 31
    • 0034671932 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the absence of an SR protein RS domain
    • Zhu J, Krainer AR (2000) Pre-mRNA splicing in the absence of an SR protein RS domain. Genes Dev 14(24):3166-3178.
    • (2000) Genes Dev , vol.14 , Issue.24 , pp. 3166-3178
    • Zhu, J.1    Krainer, A.R.2
  • 32
    • 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. (2011) 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(20):8233-8238.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.20 , pp. 8233-8238
    • Cho, S.1
  • 33
    • 77953030317 scopus 로고    scopus 로고
    • A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins)
    • Manley JL, Krainer AR (2010) A rational nomenclature for serine/arginine-rich protein splicing factors (SR proteins). Genes Dev 24(11):1073-1074.
    • (2010) Genes Dev , vol.24 , Issue.11 , pp. 1073-1074
    • Manley, J.L.1    Krainer, A.R.2
  • 34
    • 0025324948 scopus 로고
    • A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro
    • Ge H, Manley JL (1990) A protein factor, ASF, controls cell-specific alternative splicing of SV40 early pre-mRNA in vitro. Cell 62(1):25-34.
    • (1990) Cell , vol.62 , Issue.1 , pp. 25-34
    • Ge, H.1    Manley, J.L.2
  • 35
    • 0025367075 scopus 로고
    • The essential pre-mRNA splicing factor SF2 influences 5' splice site selection by activating proximal sites
    • Krainer AR, Conway GC, Kozak D (1990) The essential pre-mRNA splicing factor SF2 influences 5' splice site selection by activating proximal sites. Cell 62(1):35-42.
    • (1990) Cell , vol.62 , Issue.1 , pp. 35-42
    • Krainer, A.R.1    Conway, G.C.2    Kozak, D.3
  • 36
    • 33847630730 scopus 로고    scopus 로고
    • The gene encoding the splicing factor SF2/ASF is a protooncogene
    • Karni R, et al. (2007) The gene encoding the splicing factor SF2/ASF is a protooncogene. Nat Struct Mol Biol 14(3):185-193.
    • (2007) Nat Struct Mol Biol , vol.14 , Issue.3 , pp. 185-193
    • Karni, R.1
  • 37
    • 0029859659 scopus 로고    scopus 로고
    • Targeted disruption of an essential vertebrate gene: ASF/SF2 is required for cell viability
    • Wang J, Takagaki Y, Manley JL (1996) Targeted disruption of an essential vertebrate gene: ASF/SF2 is required for cell viability. Genes Dev 10(20):2588-2599.
    • (1996) Genes Dev , vol.10 , Issue.20 , pp. 2588-2599
    • Wang, J.1    Takagaki, Y.2    Manley, J.L.3
  • 38
    • 0034599949 scopus 로고    scopus 로고
    • Functional characterization of SR and SRrelated genes in Caenorhabditis elegans
    • Longman D, Johnstone IL, Cáceres JF (2000) Functional characterization of SR and SRrelated genes in Caenorhabditis elegans. EMBO J 19(7):1625-1637.
    • (2000) EMBO J , vol.19 , Issue.7 , pp. 1625-1637
    • Longman, D.1    Johnstone, I.L.2    Cáceres, J.F.3
  • 39
    • 0030891302 scopus 로고    scopus 로고
    • RNA splicing specificity determined by the coordinated action of RNA recognition motifs in SR proteins
    • Chandler SD, Mayeda A, Yeakley JM, Krainer AR, Fu XD (1997) RNA splicing specificity determined by the coordinated action of RNA recognition motifs in SR proteins. Proc Natl Acad Sci USA 94(8):3596-3601.
    • (1997) Proc Natl Acad Sci USA , vol.94 , Issue.8 , pp. 3596-3601
    • Chandler, S.D.1    Mayeda, A.2    Yeakley, J.M.3    Krainer, A.R.4    Fu, X.D.5
  • 40
    • 4043072200 scopus 로고    scopus 로고
    • RNA recognition motif 2 directs the recruitment of SF2/ASF to nuclear stress bodies
    • Chiodi I, et al. (2004) RNA recognition motif 2 directs the recruitment of SF2/ASF to nuclear stress bodies. Nucleic Acids Res 32(14):4127-4136.
    • (2004) Nucleic Acids Res , vol.32 , Issue.14 , pp. 4127-4136
    • Chiodi, I.1
  • 41
    • 3242783149 scopus 로고    scopus 로고
    • The second RNA-binding domain of the human splicing factor ASF/SF2 is the critical domain controlling adenovirus E1A alternative 5'-splice site selection
    • Dauksaite V, Akusjärvi G (2004) The second RNA-binding domain of the human splicing factor ASF/SF2 is the critical domain controlling adenovirus E1A alternative 5'-splice site selection. Biochem J 381(Pt 2):343-350.
    • (2004) Biochem J , vol.381 , Issue.PART 2 , pp. 343-350
    • Dauksaite, V.1    Akusjärvi, G.2
  • 42
    • 42949109848 scopus 로고    scopus 로고
    • The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1
    • Michlewski G, Sanford JR, Cáceres JF (2008) The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1. Mol Cell 30(2): 179-189.
    • (2008) Mol Cell , vol.30 , Issue.2 , pp. 179-189
    • Michlewski, G.1    Sanford, J.R.2    Cáceres, J.F.3
  • 43
    • 0027753933 scopus 로고
    • Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors
    • Birney E, Kumar S, Krainer AR (1993) Analysis of the RNA-recognition motif and RS and RGG domains: Conservation in metazoan pre-mRNA splicing factors. Nucleic Acids Res 21(25):5803-5816.
    • (1993) Nucleic Acids Res , vol.21 , Issue.25 , pp. 5803-5816
    • Birney, E.1    Kumar, S.2    Krainer, A.R.3
  • 45
    • 0029064220 scopus 로고
    • The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities
    • Tacke R, Manley JL (1995) The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities. EMBO J 14(14):3540-3551.
    • (1995) EMBO J , vol.14 , Issue.14 , pp. 3540-3551
    • Tacke, R.1    Manley, J.L.2
  • 46
    • 54849438715 scopus 로고    scopus 로고
    • Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF
    • Sanford JR, et al. (2008) Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF. PLoS ONE 3(10):e3369.
    • (2008) PLoS ONE , vol.3 , Issue.10
    • Sanford, J.R.1
  • 47
    • 34547643766 scopus 로고    scopus 로고
    • Structural and functional analysis of RNA and TAP binding to SF2/ASF
    • Tintaru AM, et al. (2007) Structural and functional analysis of RNA and TAP binding to SF2/ASF. EMBO Rep 8(8):756-762.
    • (2007) EMBO Rep , vol.8 , Issue.8 , pp. 756-762
    • Tintaru, A.M.1
  • 48
    • 0036142662 scopus 로고    scopus 로고
    • An exonic splicing enhancer in human IGF-I pre-mRNA mediates recognition of alternative exon 5 by the serine-arginine protein splicing factor-2/alternative splicing factor
    • Smith PJ, et al. (2002) An exonic splicing enhancer in human IGF-I pre-mRNA mediates recognition of alternative exon 5 by the serine-arginine protein splicing factor-2/alternative splicing factor. Endocrinology 143(1):146-154.
    • (2002) Endocrinology , vol.143 , Issue.1 , pp. 146-154
    • Smith, P.J.1
  • 49
    • 70350782482 scopus 로고    scopus 로고
    • Antagonistic SR proteins regulate alternative splicing of tumor-related Rac1b downstream of the PI3-kinase and Wnt pathways
    • Gonçalves V, Matos P, Jordan P (2009) Antagonistic SR proteins regulate alternative splicing of tumor-related Rac1b downstream of the PI3-kinase and Wnt pathways. Hum Mol Genet 18(19):3696-3707.
    • (2009) Hum Mol Genet , vol.18 , Issue.19 , pp. 3696-3707
    • Gonçalves, V.1    Matos, P.2    Jordan, P.3
  • 50
    • 0033762534 scopus 로고    scopus 로고
    • Selection of alternative 5' splice sites: Role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1
    • Eperon IC, et al. (2000) Selection of alternative 5' splice sites: Role of U1 snRNP and models for the antagonistic effects of SF2/ASF and hnRNP A1. Mol Cell Biol 20(22): 8303-8318.
    • (2000) Mol Cell Biol , vol.20 , Issue.22 , pp. 8303-8318
    • Eperon, I.C.1
  • 51
    • 0026543785 scopus 로고
    • Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2
    • Mayeda A, Krainer AR (1992) Regulation of alternative pre-mRNA splicing by hnRNP A1 and splicing factor SF2. Cell 68(2):365-375.
    • (1992) Cell , vol.68 , Issue.2 , pp. 365-375
    • Mayeda, A.1    Krainer, A.R.2
  • 52
    • 0033134777 scopus 로고    scopus 로고
    • Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA
    • Ding J, et al. (1999) Crystal structure of the two-RRM domain of hnRNP A1 (UP1) complexed with single-stranded telomeric DNA. Genes Dev 13(9):1102-1115.
    • (1999) Genes Dev , vol.13 , Issue.9 , pp. 1102-1115
    • Ding, J.1
  • 53
    • 36348937901 scopus 로고    scopus 로고
    • Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals
    • Deka P, Bucheli ME, Moore C, Buratowski S, Varani G (2008) Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end processing signals. J Mol Biol 375(1): 136-150.
    • (2008) J Mol Biol , vol.375 , Issue.1 , pp. 136-150
    • Deka, P.1    Bucheli, M.E.2    Moore, C.3    Buratowski, S.4    Varani, G.5
  • 54
    • 40649092847 scopus 로고    scopus 로고
    • A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1
    • Ngo JC, et al. (2008) A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1. Mol Cell 29(5):563-576.
    • (2008) Mol Cell , vol.29 , Issue.5 , pp. 563-576
    • Ngo, J.C.1
  • 55
    • 77954384049 scopus 로고    scopus 로고
    • Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs
    • Dominguez C, Fisette JF, Chabot B, Allain FH (2010) Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs. Nat Struct Mol Biol 17(7):853-861.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.7 , pp. 853-861
    • Dominguez, C.1    Fisette, J.F.2    Chabot, B.3    Allain, F.H.4
  • 56
    • 77956715760 scopus 로고    scopus 로고
    • Structure of the RNA binding domain of a DEADbox helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif
    • Hardin JW, Hu YX, McKay DB (2010) Structure of the RNA binding domain of a DEADbox helicase bound to its ribosomal RNA target reveals a novel mode of recognition by an RNA recognition motif. J Mol Biol 402(2):412-427.
    • (2010) J Mol Biol , vol.402 , Issue.2 , pp. 412-427
    • Hardin, J.W.1    Hu, Y.X.2    McKay, D.B.3
  • 57
    • 84876839218 scopus 로고    scopus 로고
    • Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing
    • Pandit S, et al. (2013) Genome-wide analysis reveals SR protein cooperation and competition in regulated splicing. Mol Cell 50(2):223-235.
    • (2013) Mol Cell , vol.50 , Issue.2 , pp. 223-235
    • Pandit, S.1
  • 58
    • 84878582352 scopus 로고    scopus 로고
    • Regulation of splicing by SR proteins and SR protein-specific kinases
    • Zhou Z, Fu XD (2013) Regulation of splicing by SR proteins and SR protein-specific kinases. Chromosoma 122(3):191-207.
    • (2013) Chromosoma , vol.122 , Issue.3 , pp. 191-207
    • Zhou, Z.1    Fu, X.D.2
  • 59
    • 61849139645 scopus 로고    scopus 로고
    • Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts
    • Sanford JR, et al. (2009) Splicing factor SFRS1 recognizes a functionally diverse landscape of RNA transcripts. Genome Res 19(3):381-394.
    • (2009) Genome Res , vol.19 , Issue.3 , pp. 381-394
    • Sanford, J.R.1
  • 60
    • 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 betatropomyosin gene
    • Chen CD, Kobayashi R, Helfman DM (1999) Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat betatropomyosin gene. Genes Dev 13(5):593-606.
    • (1999) Genes Dev , vol.13 , Issue.5 , pp. 593-606
    • Chen, C.D.1    Kobayashi, R.2    Helfman, D.M.3
  • 61
    • 0035798607 scopus 로고    scopus 로고
    • A second exon splicing silencer within human immunodeficiency virus type 1 tat exon 2 represses splicing of Tat mRNA and binds protein hnRNP H
    • Jacquenet S, et al. (2001) A second exon splicing silencer within human immunodeficiency virus type 1 tat exon 2 represses splicing of Tat mRNA and binds protein hnRNP H. J Biol Chem 276(44):40464-40475.
    • (2001) J Biol Chem , vol.276 , Issue.44 , pp. 40464-40475
    • Jacquenet, S.1
  • 62
    • 23844471326 scopus 로고    scopus 로고
    • HnRNP L represses exon splicing via a regulated exonic splicing silencer
    • Rothrock CR, House AE, Lynch KW (2005) HnRNP L represses exon splicing via a regulated exonic splicing silencer. EMBO J 24(15):2792-2802.
    • (2005) EMBO J , vol.24 , Issue.15 , pp. 2792-2802
    • Rothrock, C.R.1    House, A.E.2    Lynch, K.W.3
  • 63
    • 84878720961 scopus 로고    scopus 로고
    • HnRNP A1 contacts exon 5 to promote exon 6 inclusion of apoptotic Fas gene
    • Oh HK, et al. (2013) hnRNP A1 contacts exon 5 to promote exon 6 inclusion of apoptotic Fas gene. Apoptosis 18(7):825-835.
    • (2013) Apoptosis , vol.18 , Issue.7 , pp. 825-835
    • Oh, H.K.1
  • 65
    • 84871401549 scopus 로고    scopus 로고
    • Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms
    • Erkelenz S, et al. (2013) Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms. RNA 19(1):96-102.
    • (2013) RNA , vol.19 , Issue.1 , pp. 96-102
    • Erkelenz, S.1
  • 66
    • 79953805056 scopus 로고    scopus 로고
    • Molecular basis of purine-rich RNA recognition by the human SRlike protein Tra2-β1
    • Cl?ry A, et al. (2011) Molecular basis of purine-rich RNA recognition by the human SRlike protein Tra2-β1. Nat Struct Mol Biol 18(4):443-450.
    • (2011) Nat Struct Mol Biol , vol.18 , Issue.4 , pp. 443-450
    • Cléry, A.1
  • 67
    • 0347722841 scopus 로고    scopus 로고
    • Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients
    • Sattler M, Schleucher J, Griesinger C (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients. Prog NMR Spec 34:93-158.
    • (1999) Prog NMR Spec , vol.34 , pp. 93-158
    • Sattler, M.1    Schleucher, J.2    Griesinger, C.3
  • 68
    • 1242340502 scopus 로고    scopus 로고
    • New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes
    • Peterson RD, Theimer CA, Wu H, Feigon J (2004) New applications of 2D filtered/edited NOESY for assignment and structure elucidation of RNA and RNA-protein complexes. J Biomol NMR 28(1):59-67.
    • (2004) J Biomol NMR , vol.28 , Issue.1 , pp. 59-67
    • Peterson, R.D.1    Theimer, C.A.2    Wu, H.3    Feigon, J.4
  • 69
    • 0028022578 scopus 로고
    • A pulsed field gradient isotopefiltered 3D 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes
    • Lee W, Revington MJ, Arrowsmith C, Kay LE (1994) A pulsed field gradient isotopefiltered 3D 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes. FEBS Lett 350(1):87-90.
    • (1994) FEBS Lett , vol.350 , Issue.1 , pp. 87-90
    • Lee, W.1    Revington, M.J.2    Arrowsmith, C.3    Kay, L.E.4
  • 70
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol 319(1):209-227.
    • (2002) J Mol Biol , vol.319 , Issue.1 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 71
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann T, Güntert P, Wüthrich K (2002) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS. J Biomol NMR 24(3):171-189.
    • (2002) J Biomol NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 72
    • 23444454552 scopus 로고    scopus 로고
    • The Amber biomolecular simulation programs
    • Case DA, et al. (2005) The Amber biomolecular simulation programs. J Comput Chem 26(16):1668-1688.
    • (2005) J Comput Chem , vol.26 , Issue.16 , pp. 1668-1688
    • Case, D.A.1
  • 73
    • 0001398008 scopus 로고    scopus 로고
    • How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules?
    • Wang JM, Cieplak P, Kollman PA (2000) How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? J Comput Chem 21(12):1049-1074.
    • (2000) J Comput Chem , vol.21 , Issue.12 , pp. 1049-1074
    • Wang, J.M.1    Cieplak, P.2    Kollman, P.A.3
  • 74
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8(4):477-486.
    • (1996) J Biomol NMR , vol.8 , Issue.4 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 75
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graph 14(1):51-55, 29-32.
    • (1996) J Mol Graph , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 76
    • 0038401969 scopus 로고    scopus 로고
    • Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity
    • Cáceres JF, Misteli T, Screaton GR, Spector DL, Krainer AR (1997) Role of the modular domains of SR proteins in subnuclear localization and alternative splicing specificity. J Cell Biol 138(2):225-238.
    • (1997) J Cell Biol , vol.138 , Issue.2 , pp. 225-238
    • Cáceres, J.F.1    Misteli, T.2    Screaton, G.R.3    Spector, D.L.4    Krainer, A.R.5
  • 77
    • 34247388843 scopus 로고    scopus 로고
    • Enhancement of SMN2 exon 7 inclusion by antisense oligonucleotides targeting the exon
    • Hua Y, Vickers TA, Baker BF, Bennett CF, Krainer AR (2007) Enhancement of SMN2 exon 7 inclusion by antisense oligonucleotides targeting the exon. PLoS Biol 5(4):e73.
    • (2007) PLoS Biol , vol.5 , Issue.4
    • Hua, Y.1    Vickers, T.A.2    Baker, B.F.3    Bennett, C.F.4    Krainer, A.R.5
  • 78
    • 79951528344 scopus 로고    scopus 로고
    • Strict 3' splice site sequence requirements for U2 snRNP recruitment after U2AF binding underlie a genetic defect leading to autoimmune disease
    • Corrionero A, Raker VA, Izquierdo JM, Valcárcel J (2011) Strict 3' splice site sequence requirements for U2 snRNP recruitment after U2AF binding underlie a genetic defect leading to autoimmune disease. RNA 17(3):401-411.
    • (2011) RNA , vol.17 , Issue.3 , pp. 401-411
    • Corrionero, A.1    Raker, V.A.2    Izquierdo, J.M.3    Valcárcel, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.