메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Human Tra2 proteins jointly control a CHEK1 splicing switch among alternative and constitutive target exons

Author keywords

[No Author keywords available]

Indexed keywords

CHECKPOINT KINASE 1; HISTONE H2AX; PROTEIN; RNA BINDING PROTEIN; TRA2 ALPHA PROTEIN; TRA2 BETA PROTEIN; TRA2 PROTEIN; UNCLASSIFIED DRUG; MESSENGER RNA; NERVE PROTEIN; PROTEIN KINASE; TRA2B PROTEIN, HUMAN; TRANSFORMER2 ALPHA PROTEIN, HUMAN;

EID: 84923365697     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5760     Document Type: Article
Times cited : (44)

References (74)
  • 1
    • 60549104588 scopus 로고    scopus 로고
    • Splice-site pairing is an intrinsically high fidelity process
    • Fox-Walsh, K. L. & Hertel, K. J. Splice-site pairing is an intrinsically high fidelity process. Proc. Natl Acad. Sci. USA 106, 1766-1771 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1766-1771
    • Fox-Walsh, K.L.1    Hertel, K.J.2
  • 2
    • 84871435525 scopus 로고    scopus 로고
    • Function of alternative splicing
    • Kelemen, O. et al. Function of alternative splicing. Gene 514, 1-30 (2013).
    • (2013) Gene , vol.514 , pp. 1-30
    • Kelemen, O.1
  • 3
    • 84865757142 scopus 로고    scopus 로고
    • Landscape of transcription in human cells
    • Djebali, S. et al. Landscape of transcription in human cells. Nature 489, 101-108 (2012).
    • (2012) Nature , vol.489 , pp. 101-108
    • Djebali, S.1
  • 4
    • 84876854542 scopus 로고    scopus 로고
    • The tissue-specific RNA binding protein T-STAR controls regional splicing patterns of neurexin pre-mRNAs in the brain
    • Ehrmann, I. et al. The tissue-specific RNA binding protein T-STAR controls regional splicing patterns of neurexin pre-mRNAs in the brain. PLoS Genet 9, e1003474 (2013).
    • (2013) PLoS Genet , vol.9 , pp. e1003474
    • Ehrmann, I.1
  • 5
    • 84871857826 scopus 로고    scopus 로고
    • RBFOX2 is an important regulator of mesenchymal tissue-specific splicing in both normal and cancer tissues
    • Venables, J. P. et al. RBFOX2 is an important regulator of mesenchymal tissue-specific splicing in both normal and cancer tissues. Mol. Cell Biol. 33, 396-405 (2013).
    • (2013) Mol. Cell Biol. , vol.33 , pp. 396-405
    • Venables, J.P.1
  • 6
    • 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. Nat. Genet. 37, 844-852 (2005).
    • (2005) Nat. Genet. , vol.37 , pp. 844-852
    • Ule, J.1
  • 7
    • 51949111100 scopus 로고    scopus 로고
    • Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2
    • Zhang, C. et al. Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2. Genes Dev. 22, 2550-2563 (2008).
    • (2008) Genes Dev. , vol.22 , pp. 2550-2563
    • Zhang, C.1
  • 8
    • 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. Nat. Struct. Mol. Biol. 17, 1114-1123 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1114-1123
    • Llorian, M.1
  • 9
    • 79952324952 scopus 로고    scopus 로고
    • Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM
    • Tsuda, K. et al. Structural basis for the dual RNA-recognition modes of human Tra2-beta RRM. Nucleic Acids Res. 39, 1538-1553 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1538-1553
    • Tsuda, K.1
  • 11
    • 0024328766 scopus 로고
    • Sex in flies: The splice of life
    • Baker, B. S. Sex in flies: the splice of life. Nature 340, 521-524 (1989).
    • (1989) Nature , vol.340 , pp. 521-524
    • Baker, B.S.1
  • 12
    • 1842865939 scopus 로고    scopus 로고
    • Splicing regulation in Drosophila sex determination
    • Forch, P. & Valcarcel, J. Splicing regulation in Drosophila sex determination. Prog. Mol. Subcell. Biol. 31, 127-151 (2003).
    • (2003) Prog. Mol. Subcell. Biol. , vol.31 , pp. 127-151
    • Forch, P.1    Valcarcel, J.2
  • 13
    • 0029831071 scopus 로고    scopus 로고
    • A human homologue of the Drosophila sex determination factor transformer-2 has conserved splicing regulatory functions
    • Dauwalder, B., Amaya-Manzanares, F. & Mattox, W. A human homologue of the Drosophila sex determination factor transformer-2 has conserved splicing regulatory functions. Proc. Natl Acad. Sci. USA 93, 9004-9009 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9004-9009
    • Dauwalder, B.1    Amaya-Manzanares, F.2    Mattox, W.3
  • 14
    • 0031010564 scopus 로고    scopus 로고
    • Molecular cloning of htra2-beta-1 and htra2-beta-2, two human homologs of tra-2 generated by alternative splicing
    • Beil, B., Screaton, G. & Stamm, S. Molecular cloning of htra2-beta-1 and htra2-beta-2, two human homologs of tra-2 generated by alternative splicing. DNA Cell Biol. 16, 679-690 (1997).
    • (1997) DNA Cell Biol. , vol.16 , pp. 679-690
    • Beil, B.1    Screaton, G.2    Stamm, S.3
  • 15
    • 77953519937 scopus 로고    scopus 로고
    • Deficiency of the splicing factor Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn splicing
    • Mende, Y. et al. Deficiency of the splicing factor Sfrs10 results in early embryonic lethality in mice and has no impact on full-length SMN/Smn splicing. Hum. Mol. Genet. 19, 2154-2167 (2010).
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 2154-2167
    • Mende, Y.1
  • 16
    • 84889667906 scopus 로고    scopus 로고
    • Splicing factor TRA2B is required for neural progenitor survival
    • Roberts, J. M. et al. Splicing factor TRA2B is required for neural progenitor survival. J. Comp. Neurol. 522, 372-392 (2014).
    • (2014) J. Comp. Neurol. , vol.522 , pp. 372-392
    • Roberts, J.M.1
  • 17
    • 84896771891 scopus 로고    scopus 로고
    • Neuronal-specific deficiency of the splicing factor tra2b causes apoptosis in neurogenic areas of the developing mouse brain
    • Storbeck, M. et al. Neuronal-specific deficiency of the splicing factor tra2b causes apoptosis in neurogenic areas of the developing mouse brain. PLoS ONE 9, e89020 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e89020
    • Storbeck, M.1
  • 18
    • 84855281890 scopus 로고    scopus 로고
    • Identification of evolutionarily conserved exons as regulated targets for the splicing activator tra2beta in development
    • Grellscheid, S. et al. Identification of evolutionarily conserved exons as regulated targets for the splicing activator tra2beta in development. PLoS Genet. 7, e1002390 (2011).
    • (2011) PLoS Genet. , vol.7 , pp. e1002390
    • Grellscheid, S.1
  • 19
    • 84880904913 scopus 로고    scopus 로고
    • Expression of Tra2 beta in cancer cells as a potential contributory factor to neoplasia and metastasis
    • Best, A. et al. Expression of Tra2 beta in cancer cells as a potential contributory factor to neoplasia and metastasis. Int. J. Cell Biol. 2013, 843781 (2013).
    • (2013) Int. J. Cell Biol. , vol.2013 , pp. 843781
    • Best, A.1
  • 20
    • 0034662922 scopus 로고    scopus 로고
    • Htra2-beta 1 stimulates an exonic splicing enhancer and can restore full-length SMN expression to survival motor neuron 2 (SMN2)
    • Hofmann, Y., Lorson, C. L., Stamm, S., Androphy, E. J. & Wirth, B. Htra2-beta 1 stimulates an exonic splicing enhancer and can restore full-length SMN expression to survival motor neuron 2 (SMN2). Proc. Natl Acad. Sci. USA 97, 9618-9623 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 9618-9623
    • Hofmann, Y.1    Lorson, C.L.2    Stamm, S.3    Androphy, E.J.4    Wirth, B.5
  • 21
    • 33645107783 scopus 로고    scopus 로고
    • The alternative splicing of tau exon 10 and its regulatory proteins CLK2 and TRA2-BETA1 changes in sporadic Alzheimer's disease
    • Glatz, D. C. et al. The alternative splicing of tau exon 10 and its regulatory proteins CLK2 and TRA2-BETA1 changes in sporadic Alzheimer's disease. J. Neurochem. 96, 635-644 (2006).
    • (2006) J. Neurochem. , vol.96 , pp. 635-644
    • Glatz, D.C.1
  • 22
    • 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
  • 23
    • 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
  • 24
    • 26444575502 scopus 로고    scopus 로고
    • Up-regulation of the ubiquitous alternative splicing factor Tra2beta causes inclusion of a germ cell-specific exon
    • Venables, J. P. et al. Up-regulation of the ubiquitous alternative splicing factor Tra2beta causes inclusion of a germ cell-specific exon. Hum. Mol. Genet. 14, 2289-2303 (2005).
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2289-2303
    • Venables, J.P.1
  • 25
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors
    • Busch, A. & Hertel, K. J. Evolution of SR protein and hnRNP splicing regulatory factors. Wiley Interdiscip. Rev. RNA 3, 1-12 (2012).
    • (2012) Wiley Interdiscip. Rev. RNA , vol.3 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 26
    • 0032478506 scopus 로고    scopus 로고
    • Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing
    • Tacke, R., Tohyama, M., Ogawa, S. & Manley, J. L. Human Tra2 proteins are sequence-specific activators of pre-mRNA splicing. Cell 93, 139-148 (1998).
    • (1998) Cell , vol.93 , pp. 139-148
    • Tacke, R.1    Tohyama, M.2    Ogawa, S.3    Manley, J.L.4
  • 27
    • 79953805056 scopus 로고    scopus 로고
    • Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1
    • Clery, A. et al. Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-beta1. Nat. Struct. Mol. Biol. 18, 443-450 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 443-450
    • Clery, A.1
  • 28
    • 84870471564 scopus 로고    scopus 로고
    • Site identification in high-throughput RNA-protein interaction data
    • Uren, P. J. et al. Site identification in high-throughput RNA-protein interaction data. Bioinformatics 28, 3013-3020 (2012).
    • (2012) Bioinformatics , vol.28 , pp. 3013-3020
    • Uren, P.J.1
  • 29
    • 84859971554 scopus 로고    scopus 로고
    • The cardiotonic steroid digitoxin regulates alternative splicing through depletion of the splicing factors SRSF3 and TRA2B
    • Anderson, E. S. et al. The cardiotonic steroid digitoxin regulates alternative splicing through depletion of the splicing factors SRSF3 and TRA2B. RNA 18, 1041-1049 (2012).
    • (2012) RNA , vol.18 , pp. 1041-1049
    • Anderson, E.S.1
  • 30
    • 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
  • 31
    • 1542359466 scopus 로고    scopus 로고
    • Human tra2-beta1 autoregulates its protein concentration by influencing alternative splicing of its pre-mRNA
    • Stoilov, P., Daoud, R., Nayler, O. & Stamm, S. Human tra2-beta1 autoregulates its protein concentration by influencing alternative splicing of its pre-mRNA. Hum. Mol. Genet. 13, 509-524 (2004).
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 509-524
    • Stoilov, P.1    Daoud, R.2    Nayler, O.3    Stamm, S.4
  • 32
    • 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, 373-84 (2011).
    • (2011) Genes Dev , vol.25 , pp. 373-384
    • Saltzman, A.L.1    Pan, Q.2    Blencowe, B.J.3
  • 33
    • 80455179726 scopus 로고    scopus 로고
    • ICLIP-transcriptome-wide mapping of protein-RNA interactions with individual nucleotide resolution
    • 2638
    • Konig, J. et al. iCLIP-transcriptome-wide mapping of protein-RNA interactions with individual nucleotide resolution. J. Vis. Exp. 50: pii 2638 (2011).
    • (2011) J. Vis. Exp. , vol.50
    • Konig, J.1
  • 34
    • 84859865967 scopus 로고    scopus 로고
    • The UCSC Genome Browser database: Extensions and updates 2011
    • Dreszer, T. R. et al. The UCSC Genome Browser database: extensions and updates 2011. Nucleic Acids Res. 40, D918-D923 (2012).
    • (2012) Nucleic Acids Res. , vol.40 , pp. D918-D923
    • Dreszer, T.R.1
  • 35
    • 84875404794 scopus 로고    scopus 로고
    • The UCSC Genome Browser database: Extensions and updates 2013
    • Meyer, L. R. et al. The UCSC Genome Browser database: extensions and updates 2013. Nucleic Acids Res. 41, D64-D69 (2013).
    • (2013) Nucleic Acids Res. , vol.41 , pp. D64-D69
    • Meyer, L.R.1
  • 36
    • 33644873184 scopus 로고    scopus 로고
    • BioGRID: A general repository for interaction datasets
    • Stark, C. et al. BioGRID: a general repository for interaction datasets. Nucleic Acids Res. 34, D535-D539 (2006).
    • (2006) Nucleic Acids Res. , vol.34 , pp. D535-D539
    • Stark, C.1
  • 37
    • 84856015337 scopus 로고    scopus 로고
    • Checkpoint kinase 1 (Chk1)-short is a splice variant and endogenous inhibitor of Chk1 that regulates cell cycle and DNA damage checkpoints
    • Pabla, N., Bhatt, K. & Dong, Z. Checkpoint kinase 1 (Chk1)-short is a splice variant and endogenous inhibitor of Chk1 that regulates cell cycle and DNA damage checkpoints. Proc. Natl Acad. Sci. USA 109, 197-202 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 197-202
    • Pabla, N.1    Bhatt, K.2    Dong, Z.3
  • 38
    • 77649083117 scopus 로고    scopus 로고
    • Enhanced H2AX phosphorylation, DNA replication fork arrest, and cell death in the absence of Chk1
    • Gagou, M. E., Zuazua-Villar, P. & Meuth, M. Enhanced H2AX phosphorylation, DNA replication fork arrest, and cell death in the absence of Chk1. Mol. Biol. Cell 21, 739-752 (2010).
    • (2010) Mol. Biol. Cell , vol.21 , pp. 739-752
    • Gagou, M.E.1    Zuazua-Villar, P.2    Meuth, M.3
  • 39
    • 20244388673 scopus 로고    scopus 로고
    • Inhibition of human Chk1 causes increased initiation of DNA replication, phosphorylation of ATR targets, and DNA breakage
    • Syljuasen, R. G. et al. Inhibition of human Chk1 causes increased initiation of DNA replication, phosphorylation of ATR targets, and DNA breakage. Mol. Cell Biol. 25, 3553-3562 (2005).
    • (2005) Mol. Cell Biol. , vol.25 , pp. 3553-3562
    • Syljuasen, R.G.1
  • 40
    • 69049116283 scopus 로고    scopus 로고
    • Stochastic noise in splicing machinery
    • Melamud, E. & Moult, J. Stochastic noise in splicing machinery. Nucleic Acids Res. 37, 4873-4886 (2009).
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4873-4886
    • Melamud, E.1    Moult, J.2
  • 41
    • 0042092002 scopus 로고    scopus 로고
    • Direct repression of splicing by transformer-2
    • Chandler, D. S., Qi, J. L. & Mattox, W. Direct repression of splicing by transformer-2. Mol. Cell Biol. 23, 5174-5185 (2003).
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5174-5185
    • Chandler, D.S.1    Qi, J.L.2    Mattox, W.3
  • 42
    • 84863693531 scopus 로고    scopus 로고
    • Quality of computationally inferred gene ontology annotations
    • Skunca, N., Altenhoff, A. & Dessimoz, C. Quality of computationally inferred gene ontology annotations. PLoS Comput. Biol. 8, e1002533 (2012).
    • (2012) PLoS Comput. Biol. , vol.8 , pp. e1002533
    • Skunca, N.1    Altenhoff, A.2    Dessimoz, C.3
  • 43
    • 27144546434 scopus 로고    scopus 로고
    • A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16
    • Smith, E.R. et al. A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16. Mol Cell Biol 25, 9175-88 (2005).
    • (2005) Mol Cell Biol , vol.25 , pp. 9175-9188
    • Smith, E.R.1
  • 44
    • 84883727456 scopus 로고    scopus 로고
    • Ribosomal RNA gene transcription mediated by the master genome regulator protein CCCTC-binding factor (CTCF) is negatively regulated by the condensin complex
    • Huang, K. et al. Ribosomal RNA gene transcription mediated by the master genome regulator protein CCCTC-binding factor (CTCF) is negatively regulated by the condensin complex. J Biol Chem 288, 26067-77 (2013).
    • (2013) J Biol Chem , vol.288 , pp. 26067-26077
    • Huang, K.1
  • 45
    • 0036079123 scopus 로고    scopus 로고
    • Cardiac ankyrin repeat protein, a negative regulator of cardiac gene expression, is augmented in human heart failure
    • Zolk, O. et al. Cardiac ankyrin repeat protein, a negative regulator of cardiac gene expression, is augmented in human heart failure. Biochem Biophys Res Commun 293, 1377-1382 (2002).
    • (2002) Biochem Biophys Res Commun , vol.293 , pp. 1377-1382
    • Zolk, O.1
  • 46
    • 84873420044 scopus 로고    scopus 로고
    • LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation
    • Fang, R. et al. LSD2/KDM1B and its cofactor NPAC/GLYR1 endow a structural and molecular model for regulation of H3K4 demethylation. Mol. Cell 49, 558-570 (2013).
    • (2013) Mol. Cell , vol.49 , pp. 558-570
    • Fang, R.1
  • 47
    • 78650446573 scopus 로고    scopus 로고
    • The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation
    • Schmidt, M. J., West, S. & Norbury, C. J. The human cytoplasmic RNA terminal U-transferase ZCCHC11 targets histone mRNAs for degradation. RNA 17, 39-44 (2011).
    • (2011) RNA , vol.17 , pp. 39-44
    • Schmidt, M.J.1    West, S.2    Norbury, C.J.3
  • 48
    • 80054811443 scopus 로고    scopus 로고
    • Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex
    • Fasken, M. B. et al. Air1 zinc knuckles 4 and 5 and a conserved IWRXY motif are critical for the function and integrity of the Trf4/5-Air1/2-Mtr4 polyadenylation (TRAMP) RNA quality control complex. J. Biol. Chem. 286, 37429-37445 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 37429-37445
    • Fasken, M.B.1
  • 49
    • 70349820140 scopus 로고    scopus 로고
    • Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells
    • Hagan, J. P., Piskounova, E. & Gregory, R. I. Lin28 recruits the TUTase Zcchc11 to inhibit let-7 maturation in mouse embryonic stem cells. Nat. Struct. Mol. Biol. 16, 1021-1025 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 1021-1025
    • Hagan, J.P.1    Piskounova, E.2    Gregory, R.I.3
  • 50
    • 0031905587 scopus 로고    scopus 로고
    • M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component
    • Westendorf, J.M. et al. M phase phosphoprotein 10 is a human U3 small nucleolar ribonucleoprotein component. Mol Biol Cell 9, 437-49 (1998).
    • (1998) Mol Biol Cell , vol.9 , pp. 437-449
    • Westendorf, J.M.1
  • 51
    • 79960063257 scopus 로고    scopus 로고
    • Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin
    • Eustermann, S. et al. Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin. Nat. Struct. Mol. Biol. 18, 777-782 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 777-782
    • Eustermann, S.1
  • 52
    • 33749056769 scopus 로고    scopus 로고
    • An RNA map predicting Nova-dependent splicing regulation
    • Ule, J. et al. An RNA map predicting Nova-dependent splicing regulation. Nature 444, 580-586 (2006).
    • (2006) Nature , vol.444 , pp. 580-586
    • Ule, J.1
  • 53
    • 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
  • 54
    • 84855464193 scopus 로고    scopus 로고
    • Thresholds of replication stress signaling in cancer development and treatment
    • Bartek, J., Mistrik, M. & Bartkova, J. Thresholds of replication stress signaling in cancer development and treatment. Nat. Struct. Mol. Biol. 19, 5-7 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 5-7
    • Bartek, J.1    Mistrik, M.2    Bartkova, J.3
  • 55
    • 82955203422 scopus 로고    scopus 로고
    • Exploiting oncogene-induced replicative stress for the selective killing of Myc-driven tumors
    • Murga, M. et al. Exploiting oncogene-induced replicative stress for the selective killing of Myc-driven tumors. Nat. Struct. Mol. Biol. 18, 1331-1335 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1331-1335
    • Murga, M.1
  • 56
    • 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. Nat Struct Mol Biol 17, 909-15 (2010).
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 909-915
    • Konig, J.1
  • 58
    • 84923327529 scopus 로고    scopus 로고
    • Li, H. seqtk. Available at https://github.com/lh3/seqtk.
    • Seqtk
    • Li, H.1
  • 59
    • 84871741936 scopus 로고    scopus 로고
    • Krueger, F. Trim Galore! Available at http://www.bioinformatics.babraham. ac.uk/projects/trim-galore/.
    • Trim Galore!
    • Krueger, F.1
  • 60
    • 84876996918 scopus 로고    scopus 로고
    • TopHat2: Accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions
    • Kim, D. et al. TopHat2: accurate alignment of transcriptomes in the presence of insertions, deletions and gene fusions. Genome Biology 14, R36 (2013).
    • (2013) Genome Biology , vol.14 , pp. R36
    • Kim, D.1
  • 61
    • 77951770756 scopus 로고    scopus 로고
    • BEDTools: A flexible suite of utilities for comparing genomic features
    • Quinlan, A.R. & Hall, I.M. BEDTools: a flexible suite of utilities for comparing genomic features. Bioinformatics 26, 841-842 (2010).
    • (2010) Bioinformatics , vol.26 , pp. 841-842
    • Quinlan, A.R.1    Hall, I.M.2
  • 62
    • 77958471357 scopus 로고    scopus 로고
    • Differential expression analysis for sequence count data
    • Anders, S. & Huber, W. Differential expression analysis for sequence count data. Genome Biology 11, R106 (2010).
    • (2010) Genome Biology , vol.11 , pp. R106
    • Anders, S.1    Huber, W.2
  • 63
    • 84865527768 scopus 로고    scopus 로고
    • Detecting differential usage of exons from RNA-seq data
    • Anders, S. et al. Detecting differential usage of exons from RNA-seq data. Genome Research 22, 2008-2017 (2012).
    • (2012) Genome Research , vol.22 , pp. 2008-2017
    • Anders, S.1
  • 64
    • 0032740121 scopus 로고    scopus 로고
    • Identification of a bidirectional splicing enhancer: Differential involvement of SR proteins in 5' or 3' splice site activation
    • Bourgeois, C. F., Popielarz, M., Hildwein, G. & Stevenin, J. Identification of a bidirectional splicing enhancer: differential involvement of SR proteins in 5' or 3' splice site activation. Mol. Cell. Biol. 19, 7347-7356 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7347-7356
    • Bourgeois, C.F.1    Popielarz, M.2    Hildwein, G.3    Stevenin, J.4
  • 65
    • 80054087689 scopus 로고    scopus 로고
    • Molecular design of a splicing switch responsive to the RNA binding protein Tra2beta
    • Grellscheid, S. N. et al. Molecular design of a splicing switch responsive to the RNA binding protein Tra2beta. Nucleic Acids Res. 39, 8092-8104 (2011).
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8092-8104
    • Grellscheid, S.N.1
  • 66
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology. The gene ontology consortium
    • Ashburner, M. et al. Gene ontology: tool for the unification of biology. The Gene Ontology Consortium. Nat. Genet. 25, 25-29 (2000).
    • (2000) Nat. Genet. , vol.25 , pp. 25-29
    • Ashburner, M.1
  • 67
    • 33846689706 scopus 로고    scopus 로고
    • Using GOstats to test gene lists for GO term association
    • Falcon, S. & Gentleman, R. Using GOstats to test gene lists for GO term association. Bioinformatics 23, 257-258 (2007).
    • (2007) Bioinformatics , vol.23 , pp. 257-258
    • Falcon, S.1    Gentleman, R.2
  • 68
    • 28744458859 scopus 로고    scopus 로고
    • Bioconductor: Open software development for computational biology and bioinformatics
    • Gentleman, R. C. et al. Bioconductor: open software development for computational biology and bioinformatics. Genome Biol. 5, R80 (2004).
    • (2004) Genome Biol. , vol.5 , pp. R80
    • Gentleman, R.C.1
  • 69
    • 84995546277 scopus 로고    scopus 로고
    • Org. Hs.eg.db: Genome wide annotation for Human
    • Carlson, M. org. Hs.eg.db: Genome wide annotation for Human. R package version 2.8.0. (2012).
    • (2012) R Package Version 2.8.0
    • Carlson, M.1
  • 71
    • 0242490780 scopus 로고    scopus 로고
    • Cytoscape: A software environment for integrated models of biomolecular interaction networks
    • Shannon, P. et al. Cytoscape: a software environment for integrated models of biomolecular interaction networks. Genome Res. 13, 2498-2504 (2003).
    • (2003) Genome Res. , vol.13 , pp. 2498-2504
    • Shannon, P.1
  • 72
    • 84898761557 scopus 로고    scopus 로고
    • A proteomic chronology of gene expression through the cell cycle in human myeloid leukemia cells
    • Ly, T. et al. A proteomic chronology of gene expression through the cell cycle in human myeloid leukemia cells. Elife 3, e01630 (2014).
    • (2014) Elife , vol.3 , pp. e01630
    • Ly, T.1
  • 73
    • 0029096822 scopus 로고
    • CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis
    • Liao, H., Winkfein, R. J., Mack, G., Rattner, J. B. & Yen, T. J. CENP-F is a protein of the nuclear matrix that assembles onto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130, 507-518 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 507-518
    • Liao, H.1    Winkfein, R.J.2    MacK, G.3    Rattner, J.B.4    Yen, T.J.5
  • 74
    • 0030828073 scopus 로고    scopus 로고
    • Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation
    • Hendzel, M. J. et al. Mitosis-specific phosphorylation of histone H3 initiates primarily within pericentromeric heterochromatin during G2 and spreads in an ordered fashion coincident with mitotic chromosome condensation. Chromosoma 106, 348-360 (1997).
    • (1997) Chromosoma , vol.106 , pp. 348-360
    • Hendzel, M.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.