메뉴 건너뛰기




Volumn 41, Issue 14, 2013, Pages 7153-7166

Structural insights into the targeting of mRNA GU-rich elements by the three RRMs of CELF1

Author keywords

[No Author keywords available]

Indexed keywords

CUG BP ELAV LIKE FAMILY 1 PROTEIN; CYTOSINE; MESSENGER RNA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; URACIL;

EID: 84881503204     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt470     Document Type: Article
Times cited : (27)

References (86)
  • 1
    • 33744980908 scopus 로고    scopus 로고
    • Mammalian CELF/Bruno-like RNA-binding proteins: Molecular characteristics and biological functions
    • Barreau C., Paillard L., Mereau A. and Osborne H.B. (2006) Mammalian CELF/Bruno-like RNA-binding proteins: Molecular characteristics and biological functions. Biochimie., 88, 515-525
    • (2006) Biochimie , vol.88 , pp. 515-525
    • Barreau, C.1    Paillard, L.2    Mereau, A.3    Osborne, H.B.4
  • 2
    • 57349138816 scopus 로고    scopus 로고
    • Posttranscriptional regulation of gene networks by GU-rich elements and CELF proteins
    • Vlasova I.A. and Bohjanen P.R. (2008) Posttranscriptional regulation of gene networks by GU-rich elements and CELF proteins. RNA Biol., 5, 201-207
    • (2008) RNA Biol , vol.5 , pp. 201-207
    • Vlasova, I.A.1    Bohjanen, P.R.2
  • 4
    • 0038377392 scopus 로고    scopus 로고
    • A functional deadenylation assay identifies human CUG-BP as a deadenylation factor
    • Paillard L., Legagneux V. and Osborne H.B. (2003) A functional deadenylation assay identifies human CUG-BP as a deadenylation factor. Biol. Cell, 95, 107-113
    • (2003) Biol. Cell , vol.95 , pp. 107-113
    • Paillard, L.1    Legagneux, V.2    Osborne, H.B.3
  • 5
  • 6
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis
    • Nakamura A., Sato K. and Hanyu-Nakamura K. (2004) Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev. Cell, 6, 69-78
    • (2004) Dev. Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 7
    • 0032472377 scopus 로고    scopus 로고
    • EDEN and EDEN-BP, a cis element and an associated factor that mediate sequence-specific mRNA deadenylation in Xenopus embryos
    • Paillard L., Omilli F., Legagneux V., Bassez T., Maniey D. and Osborne H.B. (1998) EDEN and EDEN-BP, a cis element and an associated factor that mediate sequence-specific mRNA deadenylation in Xenopus embryos. EMBO J., 17, 278-287
    • (1998) EMBO J. , vol.17 , pp. 278-287
    • Paillard, L.1    Omilli, F.2    Legagneux, V.3    Bassez, T.4    Maniey, D.5    Osborne, H.B.6
  • 9
    • 33746214640 scopus 로고    scopus 로고
    • Protein expression is increased by a class III AU-rich element and tethered CUG-BP1
    • Barreau C., Watrin T., Beverley O.H. and Paillard L. (2006) Protein expression is increased by a class III AU-rich element and tethered CUG-BP1. Biochem. Biophys. Res. Commun., 347, 723-730
    • (2006) Biochem. Biophys. Res. Commun , vol.347 , pp. 723-730
    • Barreau, C.1    Watrin, T.2    Beverley, O.H.3    Paillard, L.4
  • 10
    • 0037245474 scopus 로고    scopus 로고
    • Coupled mRNA stabilization and translational silencing of cyclooxygenase-2 by a novel RNA binding protein
    • Mukhopadhyay D., Houchen C.W., Kennedy S., Dieckgraefe B.K. and Anant S. (2003) Coupled mRNA stabilization and translational silencing of cyclooxygenase-2 by a novel RNA binding protein, CUGBP2. Mol. Cell, 11, 113-126
    • (2003) CUGBP2. Mol. Cell , vol.11 , pp. 113-126
    • Mukhopadhyay, D.1    Houchen, C.W.2    Kennedy, S.3    Dieckgraefe, B.K.4    Anant, S.5
  • 13
    • 33646875518 scopus 로고    scopus 로고
    • CUG-BP binds to RNA substrates and recruits PARN deadenylase
    • Moraes K.C.M., Wilusz C.J. and Wilusz J. (2006) CUG-BP binds to RNA substrates and recruits PARN deadenylase. RNA, 12, 1810-1816
    • (2006) RNA , vol.12 , pp. 1810-1816
    • Moraes, K.C.M.1    Wilusz, C.J.2    Wilusz, J.3
  • 14
    • 77956108781 scopus 로고    scopus 로고
    • CUG-BP1 overexpression in mouse skeletal muscle reproduces features of myotonic dystrophy type 1
    • Ward A.J., Rimer M., Killian J.M., Dowling J.J. and Cooper T.A. (2010) CUG-BP1 overexpression in mouse skeletal muscle reproduces features of myotonic dystrophy type 1. Hum. Mol. Genet., 19, 3614-3622
    • (2010) Hum. Mol. Genet , vol.19 , pp. 3614-3622
    • Ward, A.J.1    Rimer, M.2    Killian, J.M.3    Dowling, J.J.4    Cooper, T.A.5
  • 15
    • 77950658740 scopus 로고    scopus 로고
    • Heart-specific overexpression of CUGBP1 reproduces functional and molecular abnormalities of myotonic dystrophy type 1
    • Koshelev M., Sarma S., Price R.E., Wehrens X.H. and Cooper T.A. (2010) Heart-specific overexpression of CUGBP1 reproduces functional and molecular abnormalities of myotonic dystrophy type 1. Hum. Mol. Genet., 19, 1066-1075
    • (2010) Hum. Mol. Genet , vol.19 , pp. 1066-1075
    • Koshelev, M.1    Sarma, S.2    Price, R.E.3    Wehrens, X.H.4    Cooper, T.A.5
  • 16
    • 70450203364 scopus 로고    scopus 로고
    • Pathogenic mechanisms of myotonic dystrophy
    • Lee J.E. and Cooper T.A. (2009) Pathogenic mechanisms of myotonic dystrophy. Biochem. Soc. Trans., 37, 1281-1286
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 1281-1286
    • Lee, J.E.1    Cooper, T.A.2
  • 17
    • 33846639660 scopus 로고    scopus 로고
    • Inactivation of CUG-BP1/CELF1 causes growth viability, and spermatogenesis defects in mice
    • Kress C., Gautier-Courteille C., Osborne H.B., Babinet C. and Paillard L. (2007) Inactivation of CUG-BP1/CELF1 causes growth, viability, and spermatogenesis defects in mice. Mol. Cell. Biol., 27, 1146-1157
    • (2007) Mol. Cell. Biol , vol.27 , pp. 1146-1157
    • Kress, C.1    Gautier-Courteille, C.2    Osborne, H.B.3    Babinet, C.4    Paillard, L.5
  • 18
    • 84858440814 scopus 로고    scopus 로고
    • The importance of celf control: Molecular and biological roles of the cug-bp, elav-like family of rna-binding proteins
    • Dasgupta T. and Ladd A.N. (2012) The importance of CELF control: Molecular and biological roles of the CUG-BP, Elav-like family of RNA-binding proteins. Wiley Interdicip. Rev. RNA, 3, 104-121
    • (2012) Wiley Interdicip Rev. RNA , vol.3 , pp. 104-121
    • Dasgupta, T.1    Ladd, A.N.2
  • 20
    • 0029448033 scopus 로고
    • Substratespecific regulation of RNA deadenylation in Xenopus embryo and activated egg extracts
    • Legagneux V., Omilli F. and Osborne H.B. (1995) Substratespecific regulation of RNA deadenylation in Xenopus embryo and activated egg extracts. RNA, 1, 1001-1008
    • (1995) RNA , vol.1 , pp. 1001-1008
    • Legagneux, V.1    Omilli, F.2    Osborne, H.B.3
  • 21
    • 53049095405 scopus 로고    scopus 로고
    • The rnabinding protein cugbp1 regulates stability of tumor necrosis factor mrna in muscle cells: Implications for myotonic dystrophy
    • Zhang L., Lee J.E., Wilusz J. and Wilusz C.J. (2008) The RNAbinding protein CUGBP1 regulates stability of tumor necrosis factor mRNA in muscle cells: Implications for myotonic dystrophy. J. Biol. Chem., 283, 22457-22463
    • (2008) J. Biol. Chem , vol.283 , pp. 22457-22463
    • Zhang, L.1    Lee, J.E.2    Wilusz, J.3    Wilusz, C.J.4
  • 22
    • 1942422305 scopus 로고    scopus 로고
    • Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary epithelial cells
    • Baldwin B.R., Timchenko N.A. and Zahnow C.A. (2004) Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary epithelial cells. Mol. Cell. Biol., 24, 3682-3691
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3682-3691
    • Baldwin, B.R.1    Timchenko, N.A.2    Zahnow, C.A.3
  • 23
    • 34250645370 scopus 로고    scopus 로고
    • Regulation of the promoter of CUG triplet repeat binding protein, Cugbp1, during myogenesis
    • Huichalaf C.H., Sakai K., Wang G.L., Timchenko N.A. and Timchenko L. (2007) Regulation of the promoter of CUG triplet repeat binding protein, Cugbp1, during myogenesis. Gene, 396, 391-402
    • (2007) Gene , vol.396 , pp. 391-402
    • Huichalaf, C.H.1    Sakai, K.2    Wang, G.L.3    Timchenko, N.A.4    Timchenko, L.5
  • 25
    • 1842529234 scopus 로고    scopus 로고
    • Overexpression of CUG triplet repeatbinding protein, CUGBP1, in mice inhibits myogenesis
    • Timchenko N.A., Patel R., Iakova P., Cai Z.J., Quan L. and Timchenko L.T. (2004) Overexpression of CUG triplet repeatbinding protein, CUGBP1, in mice inhibits myogenesis. J. Biol. Chem., 279, 13129-13139
    • (2004) J. Biol. Chem , vol.279 , pp. 13129-13139
    • Timchenko, N.A.1    Patel, R.2    Iakova, P.3    Cai, Z.J.4    Quan, L.5    Timchenko, L.T.6
  • 26
    • 75649151225 scopus 로고    scopus 로고
    • A strategy to analyze the phenotypic consequences of inhibiting the association of an RNA-binding protein with a specific RNA
    • Cibois M., Gautier-Courteille C., Vallee A. and Paillard L. (2010) A strategy to analyze the phenotypic consequences of inhibiting the association of an RNA-binding protein with a specific RNA. RNA, 16, 10-15
    • (2010) RNA , vol.16 , pp. 10-15
    • Cibois, M.1    Gautier-Courteille, C.2    Vallee, A.3    Paillard, L.4
  • 28
    • 0030869091 scopus 로고    scopus 로고
    • The Mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes
    • De Moor C.H. and Richter J.D. (1997) The Mos pathway regulates cytoplasmic polyadenylation in Xenopus oocytes. Mol.Cell.Biol., 17, 6419-6426
    • (1997) Mol.Cell.Biol , vol.17 , pp. 6419-6426
    • De Moor, C.H.1    Richter, J.D.2
  • 29
    • 0033560759 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA
    • De Moor C.H. and Richter J.D. (1999) Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA. EMBO J., 18, 2294-2303
    • (1999) EMBO J. , vol.18 , pp. 2294-2303
    • De Moor, C.H.1    Richter, J.D.2
  • 30
    • 84887626009 scopus 로고    scopus 로고
    • CUG-BP and 30UTR sequences influence PARN-mediated deadenylation in mammalian cell extracts
    • Moraes K.C.M., Wilusz C.J. and Wilusz J. (2007) CUG-BP and 30UTR sequences influence PARN-mediated deadenylation in mammalian cell extracts. Genetics Mol. Biol., 30, 646-655
    • (2007) Genetics Mol. Biol , vol.30 , pp. 646-655
    • Moraes, K.C.M.1    Wilusz, C.J.2    Wilusz, J.3
  • 32
    • 40549141419 scopus 로고    scopus 로고
    • Quantitative analysis of CUG-BP1 binding to RNA repeats
    • Mori D., Sasagawa N., Kino Y. and Ishiura S. (2008) Quantitative analysis of CUG-BP1 binding to RNA repeats. J. Biochem., 143, 377-383
    • (2008) J. Biochem , vol.143 , pp. 377-383
    • Mori, D.1    Sasagawa, N.2    Kino, Y.3    Ishiura, S.4
  • 34
    • 56749164864 scopus 로고    scopus 로고
    • Expression of 24 426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines
    • Castle J.C., Zhang C., Shah J.K., Kulkarni A.V., Kalsotra A., Cooper T.A. and Johnson J.M. (2008) Expression of 24,426 human alternative splicing events and predicted cis regulation in 48 tissues and cell lines. Nat. Genet., 40, 1416-25
    • (2008) Nat. Genet , vol.40 , pp. 1416-1425
    • Castle, J.C.1    Zhang, C.2    Shah, J.K.3    Kulkarni, A.V.4    Kalsotra, A.5    Cooper, T.A.6    Johnson, J.M.7
  • 35
    • 12844278103 scopus 로고    scopus 로고
    • Identification of putative new splicing targets for ETR-3 using sequences identified by systematic evolution of ligands by exponential enrichment
    • Faustino N.A. and Cooper T.A. (2005) Identification of putative new splicing targets for ETR-3 using sequences identified by systematic evolution of ligands by exponential enrichment. Mol. Cell Biol., 25, 879-887
    • (2005) Mol. Cell Biol , vol.25 , pp. 879-887
    • Faustino, N.A.1    Cooper, T.A.2
  • 36
    • 70149109214 scopus 로고    scopus 로고
    • The CUGBP2 splicing factor regulates an ensemble of branchpoints from perimeter binding sites with implications for autoregulation
    • Dembowski J.A. and Grabowski P.J. (2009) The CUGBP2 splicing factor regulates an ensemble of branchpoints from perimeter binding sites with implications for autoregulation. PLoS Genet., 5, e1000595
    • (2009) PLoS Genet , vol.5
    • Dembowski, J.A.1    Grabowski, P.J.2
  • 37
    • 67949097422 scopus 로고    scopus 로고
    • CUGBP2 directly interacts with U2 17S snRNP components and promotes U2 snRNA binding to cardiac troponin T pre-mRNA
    • Goo Y.H. and Cooper T.A. (2009) CUGBP2 directly interacts with U2 17S snRNP components and promotes U2 snRNA binding to cardiac troponin T pre-mRNA. Nucleic Acids Res., 37, 4275-4286
    • (2009) Nucleic Acids Res , vol.37 , pp. 4275-4286
    • Goo, Y.H.1    Cooper, T.A.2
  • 40
    • 77957796477 scopus 로고    scopus 로고
    • Structural insights into RNA recognition by the alternate-splicing regulator CUG-Binding Protein 1
    • Teplova M., Song J., Gaw H.Y., Teplov A. and Patel D.J. (2010) Structural insights into RNA recognition by the alternate-splicing regulator CUG-Binding Protein 1. Structure, 18, 1364-1377
    • (2010) Structure , vol.18 , pp. 1364-1377
    • Teplova, M.1    Song, J.2    Gaw, H.Y.3    Teplov, A.4    Patel, D.J.5
  • 41
    • 80455168356 scopus 로고    scopus 로고
    • Sequence determinants for the tandem recognition of UGU and CUG rich RNA elements by the two N-Terminal RRMs of CELF1
    • Edwards J., Malaurie E., Kondrashnov A., Long J., de Moor C.H., Searle M.S. and Emsley J. (2011) Sequence determinants for the tandem recognition of UGU and CUG rich RNA elements by the two N-Terminal RRMs of CELF1. Nucleic Acids Res., 39, 8638-8650
    • (2011) Nucleic Acids Res , vol.39 , pp. 8638-8650
    • Edwards, J.1    Malaurie, E.2    Kondrashnov, A.3    Long, J.4    De Moor, C.H.5    Searle, M.S.6    Emsley, J.7
  • 43
    • 0036850732 scopus 로고    scopus 로고
    • An analysis of the sequence requirements of EDEN-BP for specific RNA binding
    • Bonnet-Corven S., Audic Y., Omilli F. and Osborne H.B. (2002) An analysis of the sequence requirements of EDEN-BP for specific RNA binding. Nucleic Acids Res., 30, 4667-4674
    • (2002) Nucleic Acids Res , vol.30 , pp. 4667-4674
    • Bonnet-Corven, S.1    Audic, Y.2    Omilli, F.3    Osborne, H.B.4
  • 44
    • 0033570899 scopus 로고    scopus 로고
    • CUG repeat binding protein (CUGBP1) interacts with the 50 region of C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms
    • Timchenko N.A., Welm A.L., Lu X. and Timchenko L.T. (1999) CUG repeat binding protein (CUGBP1) interacts with the 50 region of C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms. Nucleic Acids Res., 27, 4517-4525
    • (1999) Nucleic Acids Res , vol.27 , pp. 4517-4525
    • Timchenko, N.A.1    Welm, A.L.2    Lu, X.3    Timchenko, L.T.4
  • 47
    • 0036479108 scopus 로고    scopus 로고
    • C-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation element-binding protein)-dependent pathway
    • Paillard L., Legagneux V., Maniey D. and Osborne H.B. (2002) c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation element-binding protein)-dependent pathway. J. Biol. Chem., 277, 3232-3235
    • (2002) J. Biol. Chem , vol.277 , pp. 3232-3235
    • Paillard, L.1    Legagneux, V.2    Maniey, D.3    Osborne, H.B.4
  • 48
    • 70450203364 scopus 로고    scopus 로고
    • Pathogenic mechanisms of myotonic dystrophy
    • Lee J.E. and Cooper T.A. (2009) Pathogenic mechanisms of myotonic dystrophy. Biochem. Soc. Trans., 37, 1281-1286
    • (2009) Biochem. Soc. Trans , vol.37 , pp. 1281-1286
    • Lee, J.E.1    Cooper, T.A.2
  • 50
    • 57149097433 scopus 로고    scopus 로고
    • Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1
    • Teplova M. and Patel D.J. (2008) Structural insights into RNA recognition by the alternative-splicing regulator muscleblind-like MBNL1. Nat. Struct. Mol. Biol., 15, 1343-1351
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 1343-1351
    • Teplova, M.1    Patel, D.J.2
  • 52
    • 0033198739 scopus 로고    scopus 로고
    • Visualisation of doublestranded RNAs from the myotonic dystrophy protein kinase gene and interactions with CUG-binding protein
    • Michalowski S., Miller J.W., Urbinati C.R., Paliouras M., Swanson M.S. and Griffith J. (1999) Visualisation of doublestranded RNAs from the myotonic dystrophy protein kinase gene and interactions with CUG-binding protein. Nucleic Acids Res., 27, 3534-3542
    • (1999) Nucleic Acids Res , vol.27 , pp. 3534-3542
    • Michalowski, S.1    Miller, J.W.2    Urbinati, C.R.3    Paliouras, M.4    Swanson, M.S.5    Griffith, J.6
  • 53
    • 0037984764 scopus 로고    scopus 로고
    • Motions of the substrate recognition duplex in a group I intron assessed by site-directed spin labeling
    • Qin P.Z., Hideg K., Feigon J. and Hubbell W.L. (2003) Motions of the substrate recognition duplex in a group I intron assessed by site-directed spin labeling. Biochemistry, 42, 6772-6783
    • (2003) Biochemistry , vol.42 , pp. 6772-6783
    • Qin, P.Z.1    Hideg, K.2    Feigon, J.3    Hubbell, W.L.4
  • 56
    • 77149180105 scopus 로고    scopus 로고
    • Chemical rna modifications for studies of rna structure and dynamics
    • Wachowius F. and Hobartner C. (2010) Chemical RNA Modifications for studies of RNA structure and dynamics. Chembiochem, 11, 469-480
    • (2010) Chembiochem , vol.11 , pp. 469-480
    • Wachowius, F.1    Hobartner, C.2
  • 58
    • 39649120317 scopus 로고    scopus 로고
    • Affinity makes the difference: Nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains
    • Zhang D., Raasi S. and Fushman D. (2008) Affinity makes the difference: Nonselective interaction of the UBA domain of Ubiquilin-1 with monomeric ubiquitin and polyubiquitin chains. J. Mol. Biol., 377, 162-180
    • (2008) J. Mol. Biol , vol.377 , pp. 162-180
    • Zhang, D.1    Raasi, S.2    Fushman, D.3
  • 60
    • 0035153840 scopus 로고    scopus 로고
    • Structural basis for recognition of AU-rich element RNA by the HuD protein
    • Wang X. and Tanaka Hall T.M. (2001) Structural basis for recognition of AU-rich element RNA by the HuD protein. Nat. Struct. Biol., 8, 141-145
    • (2001) Nat. Struct. Biol , vol.8 , pp. 141-145
    • Wang, X.1    Tanaka Hall, T.M.2
  • 61
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo R.C., Bonanno J.B., Sonenberg N. and Burley S.K. (1999) Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell, 98, 835-845
    • (1999) Cell , vol.98 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 62
    • 33746296753 scopus 로고    scopus 로고
    • Grabbing the message: Structural basis of mRNA 30UTR recognition by Hrp1
    • Perez-Canadillas J.M. (2006) Grabbing the message: Structural basis of mRNA 30UTR recognition by Hrp1. EMBO J., 25, 3167-3178
    • (2006) EMBO J. , vol.25 , pp. 3167-3178
    • Perez-Canadillas, J.M.1
  • 63
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker M. (2003) Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res., 31, 3406-3415
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 64
    • 0031724103 scopus 로고    scopus 로고
    • Embryo deadenylation element-dependent deadenylation is enhanced by a cis element containing AUU repeats
    • Audic Y., Omilli F. and Osborne H.B. (1998) Embryo deadenylation element-dependent deadenylation is enhanced by a cis element containing AUU repeats. Mol. Cell. Biol., 18, 6879-6884
    • (1998) Mol. Cell. Biol , vol.18 , pp. 6879-6884
    • Audic, Y.1    Omilli, F.2    Osborne, H.B.3
  • 66
    • 72149117411 scopus 로고    scopus 로고
    • Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon exclusion or skipping
    • Xue Y., Zhou Y., Wu T., Zhu T., Ji X., Kwon Y.S., Zhang C., Yeo G., Black D.L., Sun H. et al. (2009) Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon exclusion or skipping. Mol. Cell, 36, 996-1006
    • (2009) Mol. Cell , vol.36 , pp. 996-1006
    • Xue, Y.1    Zhou, Y.2    Wu, T.3    Zhu, T.4    Ji, X.5    Kwon, Y.S.6    Zhang, C.7    Yeo, G.8    Black, D.L.9    Sun, H.10
  • 68
    • 34948834723 scopus 로고    scopus 로고
    • Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKC-mediated hyperphosphorylation
    • Kuyumcu-Martinez N.M., Wang G.S. and Cooper T.A. (2007) Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKC-mediated hyperphosphorylation. Mol. Cell, 28, 68-78
    • (2007) Mol. Cell , vol.28 , pp. 68-78
    • Kuyumcu-Martinez, N.M.1    Wang, G.S.2    Cooper, T.A.3
  • 69
    • 0342927495 scopus 로고    scopus 로고
    • Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold
    • Conte M.R., Grüne T., Ghuman J., Kelly G., Ladas A., Matthews S. and Curry S. (2000) Structure of tandem RNA recognition motifs from polypyrimidine tract binding protein reveals novel features of the RRM fold. EMBO J., 19, 3132-3141
    • (2000) EMBO J. , vol.19 , pp. 3132-3141
    • Conte, M.R.1    Grüne, T.2    Ghuman, J.3    Kelly, G.4    Ladas, A.5    Matthews, S.6    Curry, S.7
  • 72
    • 0030878682 scopus 로고    scopus 로고
    • Mutation of PTB binding sites causes misregulation of alternative 30 splice site selection in vivo
    • Pérez I., Lin C.H., McAfee J.G. and Patton J.G. (1997) Mutation of PTB binding sites causes misregulation of alternative 30 splice site selection in vivo. RNA, 3, 764-778
    • (1997) RNA , vol.3 , pp. 764-778
    • Pérez, I.1    Lin, C.H.2    McAfee, J.G.3    Patton, J.G.4
  • 74
    • 64349124740 scopus 로고    scopus 로고
    • The domains of polypyrimidine tract binding protein have distinct RNA structural preferences
    • Clerte C. and Hall K. (2009) The domains of polypyrimidine tract binding protein have distinct RNA structural preferences. Biochemistry, 48, 2063-2074
    • (2009) Biochemistry , vol.48 , pp. 2063-2074
    • Clerte, C.1    Hall, K.2
  • 75
    • 66449130983 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation
    • Kafasla P., Morgner N., Pöyry T.A.A., Curry S., Robinson C.V. and Jackson R.J. (2009) Polypyrimidine tract binding protein stabilizes the encephalomyocarditis virus IRES structure via binding multiple sites in a unique orientation. Mol. Cell, 34, 556-568
    • (2009) Mol. Cell , vol.34 , pp. 556-568
    • Kafasla, P.1    Morgner, N.2    Pöyry, T.A.A.3    Curry, S.4    Robinson, C.V.5    Jackson, R.J.6
  • 76
    • 0029295295 scopus 로고
    • Regulation of alternative 30 splice site selection by constitutive splicing factors
    • Lin C.H. and Patton J.G. (1995) Regulation of alternative 30 splice site selection by constitutive splicing factors. RNA, 1, 234-245
    • (1995) RNA , vol.1 , pp. 234-245
    • Lin, C.H.1    Patton, J.G.2
  • 77
    • 0029055472 scopus 로고
    • Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins
    • Singh R., Valcárcel J. and Green M.R. (1995) Distinct binding specificities and functions of higher eukaryotic polypyrimidine tract-binding proteins. Science, 268, 1173-1176
    • (1995) Science , vol.268 , pp. 1173-1176
    • Singh, R.1    Valcárcel, J.2    Green, M.R.3
  • 78
    • 0035038207 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein antagonizes exon definition
    • Wagner E.J. and Garcia-Blanco M.A. (2001) Polypyrimidine tract binding protein antagonizes exon definition. Mol. Cell. Biol., 21, 3281-3288
    • (2001) Mol. Cell. Biol , vol.21 , pp. 3281-3288
    • Wagner, E.J.1    Garcia-Blanco, M.A.2
  • 80
    • 0033634948 scopus 로고    scopus 로고
    • Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing
    • Chou M.Y., Underwood J.G., Nikolic J., Luu M.H. and Black D.L. (2000) Multisite RNA binding and release of polypyrimidine tract binding protein during the regulation of c-src neural-specific splicing. Mol. Cell, 5, 949-957
    • (2000) Mol. Cell , vol.5 , pp. 949-957
    • Chou, M.Y.1    Underwood, J.G.2    Nikolic, J.3    Luu, M.H.4    Black, D.L.5
  • 82
    • 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. and Black D.L. (2008) Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nat. Struct. Mol. Biol., 15, 183-191
    • (2008) Nat. 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
  • 83
    • 79951996054 scopus 로고    scopus 로고
    • U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression
    • Sharma S., Maris C., Allain F.H-T. and Black D.L. (2011) U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression. Mol. Cell, 41, 579-588
    • (2011) Mol. Cell , vol.41 , pp. 579-588
    • Sharma, S.1    Maris, C.2    Allain, F.H.-T.3    Black, D.L.4
  • 84
    • 82955205878 scopus 로고    scopus 로고
    • Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing
    • Joshi A., Coelho M.B., Kotik-Kogan O., Simpson P.J., Matthews S.J., Smith C.W. and Curry S. (2011) Crystallographic analysis of polypyrimidine tract-binding protein-Raver1 interactions involved in regulation of alternative splicing. Structure, 19, 1816-1825
    • (2011) Structure , vol.19 , pp. 1816-1825
    • Joshi, A.1    Coelho, M.B.2    Kotik-Kogan, O.3    Simpson, P.J.4    Matthews, S.J.5    Smith, C.W.6    Curry, S.7
  • 85
    • 0031985529 scopus 로고    scopus 로고
    • Role of an inhibitory pyrimidine element and polypyrimidine tract binding protein in repression of a regulated alpha-Tropomyosin exon
    • Gooding C., Roberts G.C. and Smith C.W. (1998) Role of an inhibitory pyrimidine element and polypyrimidine tract binding protein in repression of a regulated alpha-Tropomyosin exon. RNA, 4, 85-100
    • (1998) RNA , vol.4 , pp. 85-100
    • Gooding, C.1    Roberts, G.C.2    Smith, C.W.3
  • 86
    • 84855490669 scopus 로고    scopus 로고
    • Regulation of CUG-binding Protein 1 (CUGBP1) binding to target transcripts upon T cell activation
    • Beisang D., Rattenbacher B., Vlasova-St. Louis I.A. and Bohjanen P.R. (2012) Regulation of CUG-binding Protein 1 (CUGBP1) binding to target transcripts upon T cell activation. J. Biol. Chem., 287, 950-960
    • (2012) J. Biol. Chem , vol.287 , pp. 950-960
    • Beisang, D.1    Rattenbacher, B.2    Vlasova-St. Louis, I.A.3    Bohjanen, P.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.