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Volumn 15, Issue 6, 2014, Pages 492-502

Post-transcriptional coordination of immunological responses by RNA-binding proteins

Author keywords

[No Author keywords available]

Indexed keywords

RNA BINDING PROTEIN;

EID: 84901032555     PISSN: 15292908     EISSN: 15292916     Source Type: Journal    
DOI: 10.1038/ni.2884     Document Type: Review
Times cited : (169)

References (111)
  • 1
    • 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
  • 2
    • 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. Nat. Rev. Mol. Cell Biol. 8, 479-490 (2007
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 3
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-Transcriptional gene regulation
    • Glisovic, T., Bachorik, J.L., Yong, J. & Dreyfuss, G. RNA-binding proteins and post-Transcriptional gene regulation. FEBS Lett. 582, 1977-1986 (2008
    • (2008) FEBS Lett. , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 4
    • 84855916545 scopus 로고    scopus 로고
    • Protein-RNA interactions: New genomic technologies and perspectives
    • König, J., Zarnack, K., Luscombe, N.M. & Ule, J. Protein-RNA interactions: New genomic technologies and perspectives. Nat. Rev. Genet. 13, 77-83 (2012
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 77-83
    • König, J.1    Zarnack, K.2    Luscombe, N.M.3    Ule, J.4
  • 5
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: Coordination of post-Transcriptional events
    • Keene, J.D. RNA regulons: Coordination of post-Transcriptional events. Nat. Rev. Genet. 8, 533-543 (2007
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 533-543
    • Keene, J.D.1
  • 6
    • 84864251757 scopus 로고    scopus 로고
    • Transcript dynamics of proinflammatory genes revealed by sequence analysis of subcellular RNA fractions
    • Bhatt, D.M. et al. Transcript dynamics of proinflammatory genes revealed by sequence analysis of subcellular RNA fractions. Cell 20, 279-290 (2012
    • (2012) Cell , vol.20 , pp. 279-290
    • Bhatt, D.M.1
  • 7
    • 84878513440 scopus 로고    scopus 로고
    • Distinct translational control in CD4+ T cell subsets
    • Bjur, E. et al. Distinct translational control in CD4+ T cell subsets. PLoS Genet. 9, e1003494 (2013
    • (2013) PLoS Genet , vol.9
    • Bjur, E.1
  • 8
    • 60749124122 scopus 로고    scopus 로고
    • The stability of mRNA influences the temporal order of the induction of genes encoding inflammatory molecules
    • Hao, S. & Baltimore, D. The stability of mRNA influences the temporal order of the induction of genes encoding inflammatory molecules. Nat. Immunol. 10, 281-288 (2009
    • (2009) Nat. Immunol. , vol.10 , pp. 281-288
    • Hao, S.1    Baltimore, D.2
  • 9
    • 84880361099 scopus 로고    scopus 로고
    • RNA splicing regulates the temporal order of TNF-induced gene expression
    • Hao, S. & Baltimore, D. RNA splicing regulates the temporal order of TNF-induced gene expression. Proc. Natl. Acad. Sci. USA 110, 11934-11939 (2013
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 11934-11939
    • Hao, S.1    Baltimore, D.2
  • 10
    • 84887617987 scopus 로고    scopus 로고
    • ADAR regulates RNA editing, transcript stability, and gene expression
    • Wang, I.X. et al. ADAR regulates RNA editing, transcript stability, and gene expression. Cell Rep. 5, 849-860 (2013
    • (2013) Cell Rep. , vol.5 , pp. 849-860
    • Wang, I.X.1
  • 11
    • 84866167339 scopus 로고    scopus 로고
    • Genetics and regulatory impact of alternative polyadenylation in human B-lymphoblastoid cells
    • Yoon, O.K., Hsu, T.Y., Im, J.H. & Brem, R.B. Genetics and regulatory impact of alternative polyadenylation in human B-lymphoblastoid cells. PLoS Genet. 8, e1002882 (2012
    • (2012) PLoS Genet , vol.8
    • Yoon, O.K.1    Hsu, T.Y.2    Im, J.H.3    Brem, R.B.4
  • 12
    • 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. Nat. Rev. Mol. Cell Biol. 14, 153-165 (2013
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 153-165
    • Kornblihtt, A.R.1
  • 14
    • 77956687928 scopus 로고    scopus 로고
    • Functional diversity of the hnRNPs: Past, present and perspectives
    • Han, S.P., Tang, Y.H. & Smith, R. Functional diversity of the hnRNPs: Past, present and perspectives. Biochem. J. 430, 379-392 (2010
    • (2010) Biochem. J. , vol.430 , pp. 379-392
    • Han, S.P.1    Tang, Y.H.2    Smith, R.3
  • 15
    • 84858446718 scopus 로고    scopus 로고
    • Regulation of cytoplasmic mRNA decay
    • Schoenberg, D.R. & Maquat, L.E. Regulation of cytoplasmic mRNA decay. Nat. Rev. Genet. 13, 246-259 (2012
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 246-259
    • Schoenberg, D.R.1    Maquat, L.E.2
  • 16
    • 84871681585 scopus 로고    scopus 로고
    • MicroRNAs mediate gene silencing via multiple different pathways in Drosophila
    • Fukaya, T. & Tomari, Y. MicroRNAs mediate gene silencing via multiple different pathways in Drosophila. Mol. Cell 48, 825-836 (2012
    • (2012) Mol. Cell , vol.48 , pp. 825-836
    • Fukaya, T.1    Tomari, Y.2
  • 17
    • 84873810502 scopus 로고    scopus 로고
    • Eukaryotic elongation factor 2 controls TNF-α translation in LPS-induced hepatitis
    • González-Terán, B. et al. Eukaryotic elongation factor 2 controls TNF-α translation in LPS-induced hepatitis. J. Clin. Invest. 123, 164-178 (2013
    • (2013) J. Clin. Invest. , vol.123 , pp. 164-178
    • González-Terán, B.1
  • 18
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay, N. & Sonenberg, N. Upstream and downstream of mTOR. Genes Dev. 18, 1926-1945 (2004
    • (2004) Genes Dev. , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 19
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-Transcriptional and epigenetic modulators of gene expression
    • Anderson, P. & Kedersha, N. RNA granules: Post-Transcriptional and epigenetic modulators of gene expression. Nat. Rev. Mol. Cell Biol. 10, 430-436 (2009
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 20
    • 56749174940 scopus 로고    scopus 로고
    • Exploring the full spectrum of macrophage activation
    • Mosser, D.M. & Edwards, J.P. Exploring the full spectrum of macrophage activation. Nat. Rev. Immunol. 8, 958-969 (2008
    • (2008) Nat. Rev. Immunol. , vol.8 , pp. 958-969
    • Mosser, D.M.1    Edwards, J.P.2
  • 21
    • 84871681585 scopus 로고    scopus 로고
    • MicroRNAs mediate gene silencing via multiple different pathways in Drosophila
    • Fukaya, T. & Tomari, Y. MicroRNAs mediate gene silencing via multiple different pathways in Drosophila. Mol. Cell 48, 825-836 (2012
    • (2012) Mol. Cell , vol.48 , pp. 825-836
    • Fukaya, T.1    Tomari, Y.2
  • 22
    • 77950362382 scopus 로고    scopus 로고
    • The inflammasomes
    • Schroder, K. & Tschopp, J. The inflammasomes. Cell 19, 821-832 (2010
    • (2010) Cell , vol.19 , pp. 821-832
    • Schroder, K.1    Tschopp, J.2
  • 23
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O. & Akira, S. Pattern recognition receptors and inflammation. Cell 19, 805-820 (2010
    • (2010) Cell , vol.19 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 24
    • 0037454946 scopus 로고    scopus 로고
    • Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4
    • Burns, K. et al. Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4. J. Exp. Med. 197, 263-268 (2003
    • (2003) J. Exp. Med. , vol.197 , pp. 263-268
    • Burns, K.1
  • 25
    • 84887281296 scopus 로고    scopus 로고
    • Limiting of the innate immune response by SF3A-dependent control of MyD88 alternative mRNA splicing
    • De Arras, L. & Alper, S. Limiting of the innate immune response by SF3A-dependent control of MyD88 alternative mRNA splicing. PLoS Genet. 9, e1003855 (2013
    • (2013) PLoS Genet , vol.9
    • De Arras, L.1    Alper, S.2
  • 26
    • 79251545169 scopus 로고    scopus 로고
    • RNA-binding protein AUF1 regulates lipopolysaccharide-induced IL10 expression by activating IκB kinase complex in monocytes
    • Sarkar, S. et al. RNA-binding protein AUF1 regulates lipopolysaccharide- induced IL10 expression by activating IκB kinase complex in monocytes. Mol. Cell. Biol. 31, 602-615 (2011
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 602-615
    • Sarkar, S.1
  • 27
    • 84887442268 scopus 로고    scopus 로고
    • Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis
    • Qiang, X. et al. Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis. Nat. Med. 19, 1489-1495 (2013
    • (2013) Nat. Med. , vol.19 , pp. 1489-1495
    • Qiang, X.1
  • 28
    • 84891391037 scopus 로고    scopus 로고
    • Cold-inducible RNA-binding protein is an important mediator of alcohol-induced brain inflammation
    • Rajayer, S.R. et al. Cold-inducible RNA-binding protein is an important mediator of alcohol-induced brain inflammation. PLoS ONE 8, e79430 (2013
    • (2013) PLoS ONE , vol.8
    • Rajayer, S.R.1
  • 29
    • 84880745984 scopus 로고    scopus 로고
    • The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome
    • Mitoma, H. et al. The DHX33 RNA helicase senses cytosolic RNA and activates the NLRP3 inflammasome. Immunity 39, 123-135 (2013
    • (2013) Immunity , vol.39 , pp. 123-135
    • Mitoma, H.1
  • 30
    • 77954674891 scopus 로고    scopus 로고
    • Role of PKR and Type I IFNs in viral control during primary and secondary infection
    • Nakayama, Y. et al. Role of PKR and Type I IFNs in viral control during primary and secondary infection. PLoS Pathog. 6, e1000966 (2010
    • (2010) PLoS Pathog. , vol.6
    • Nakayama, Y.1
  • 31
    • 79961182322 scopus 로고    scopus 로고
    • Host response to polyomavirus infection is modulated by RNA adenosine deaminase ADAR1 but not by ADAR2
    • George, C.X. & Samuel, C.E. Host response to polyomavirus infection is modulated by RNA adenosine deaminase ADAR1 but not by ADAR2. J. Virol. 85, 8338-8347 (2011
    • (2011) J. Virol. , vol.85 , pp. 8338-8347
    • George, C.X.1    Samuel, C.E.2
  • 32
    • 84876453384 scopus 로고    scopus 로고
    • Regulation of stress granules and P-bodies during RNA virus infection
    • Lloyd, R.E. Regulation of stress granules and P-bodies during RNA virus infection. Wiley. Interdiscip. Rev. RNA. 4, 317-331 (2013
    • (2013) Wiley Interdiscip. Rev. RNA. , vol.4 , pp. 317-331
    • Lloyd, R.E.1
  • 33
    • 84888438314 scopus 로고    scopus 로고
    • Changes in cellular mRNA stability, splicing, and polyadenylation through HuR protein sequestration by a cytoplasmic RNA virus
    • Barnhart, M.D., Moon, S.L., Emch, A.W., Wilusz, C.J. & Wilusz, J. Changes in cellular mRNA stability, splicing, and polyadenylation through HuR protein sequestration by a cytoplasmic RNA virus. Cell Rep. 5, 909-917 (2013
    • (2013) Cell Rep. , vol.5 , pp. 909-917
    • Barnhart, M.D.1    Moon, S.L.2    Emch, A.W.3    Wilusz, C.J.4    Wilusz, J.5
  • 34
    • 81255154489 scopus 로고    scopus 로고
    • The IκB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1
    • Iwasaki, H. et al. The IκB kinase complex regulates the stability of cytokine-encoding mRNA induced by TLR-IL-1R by controlling degradation of regnase-1. Nat. Immunol. 12, 1167-1175 (2011
    • (2011) Nat. Immunol. , vol.12 , pp. 1167-1175
    • Iwasaki, H.1
  • 35
    • 84878696872 scopus 로고    scopus 로고
    • Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo
    • Masuda, K. et al. Arid5a controls IL-6 mRNA stability, which contributes to elevation of IL-6 level in vivo. Proc. Natl. Acad. Sci. USA 110, 9409-9414 (2013
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 9409-9414
    • Masuda, K.1
  • 36
    • 84877793134 scopus 로고    scopus 로고
    • Tristetraprolin (TTP interactions with mRNA and proteins, and current thoughts on mechanisms of action
    • Brooks, S.A. & Blackshear, P.J. Tristetraprolin (TTP): Interactions with mRNA and proteins, and current thoughts on mechanisms of action. Biochim. Biophys. Acta 1829, 666-679 (2013
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 666-679
    • Brooks, S.A.1    Blackshear, P.J.2
  • 37
    • 0344305405 scopus 로고    scopus 로고
    • IL-4-Stat6 signaling induces tristetraprolin expression and inhibits TNF-Alpha production in mast cells
    • Suzuki, K. et al. IL-4-Stat6 signaling induces tristetraprolin expression and inhibits TNF-Alpha production in mast cells. J. Exp. Med. 198, 1717-1727 (2003
    • (2003) J. Exp. Med. , vol.198 , pp. 1717-1727
    • Suzuki, K.1
  • 38
    • 70249145543 scopus 로고    scopus 로고
    • Tristetraprolin is required for full anti-inflammatory response of murine macrophages to IL-10
    • Schaljo, B. et al. Tristetraprolin is required for full anti-inflammatory response of murine macrophages to IL-10. J. Immunol. 183, 1197-1206 (2009
    • (2009) J. Immunol. , vol.183 , pp. 1197-1206
    • Schaljo, B.1
  • 39
    • 84891445643 scopus 로고    scopus 로고
    • Transforming growth factor β regulates P-body formation through induction of the mRNA decay factor tristetraprolin
    • Blanco, F.F., Sanduja, S., Deane, N.G., Blackshear, P.J. & Dixon, D.A. Transforming growth factor β regulates P-body formation through induction of the mRNA decay factor tristetraprolin. Mol. Cell. Biol. 34, 180-195 (2014
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 180-195
    • Blanco, F.F.1    Sanduja, S.2    Deane, N.G.3    Blackshear, P.J.4    Dixon, D.A.5
  • 40
    • 80052648818 scopus 로고    scopus 로고
    • Zinc finger protein tristetraprolin interacts with CCL3 mRNA and regulates tissue inflammation
    • Kang, J.G. et al. Zinc finger protein tristetraprolin interacts with CCL3 mRNA and regulates tissue inflammation. J. Immunol. 187, 2696-2701 (2011
    • (2011) J. Immunol. , vol.187 , pp. 2696-2701
    • Kang, J.G.1
  • 41
    • 84865179916 scopus 로고    scopus 로고
    • Tristetraprolin-driven regulatory circuit controls quality and timing of mRNA decay in inflammation
    • Kratochvill, F. et al. Tristetraprolin-driven regulatory circuit controls quality and timing of mRNA decay in inflammation. Mol. Syst. Biol. 7, 560 (2011
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 560
    • Kratochvill, F.1
  • 42
    • 84884250248 scopus 로고    scopus 로고
    • Tristetraprolin regulation of interleukin 23 mRNA stability prevents a spontaneous inflammatory disease
    • Molle, C. et al. Tristetraprolin regulation of interleukin 23 mRNA stability prevents a spontaneous inflammatory disease. J. Exp. Med. 210, 1675-1684 (2013
    • (2013) J. Exp. Med. , vol.210 , pp. 1675-1684
    • Molle, C.1
  • 43
    • 84861135683 scopus 로고    scopus 로고
    • Myeloid-specific tristetraprolin deficiency in mice results in extreme lipopolysaccharide sensitivity in an otherwise minimal phenotype
    • Qiu, L.Q., Stumpo, D.J. & Blackshear, P.J. Myeloid-specific tristetraprolin deficiency in mice results in extreme lipopolysaccharide sensitivity in an otherwise minimal phenotype. J. Immunol. 188, 5150-5159 (2012
    • (2012) J. Immunol. , vol.188 , pp. 5150-5159
    • Qiu, L.Q.1    Stumpo, D.J.2    Blackshear, P.J.3
  • 44
    • 16044369031 scopus 로고    scopus 로고
    • A pathogenetic role for TNF α in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency
    • Taylor, G.A. et al. A pathogenetic role for TNF α in the syndrome of cachexia, arthritis, and autoimmunity resulting from tristetraprolin (TTP) deficiency. Immunity 4, 445-454 (1996
    • (1996) Immunity , vol.4 , pp. 445-454
    • Taylor, G.A.1
  • 45
    • 84877708543 scopus 로고    scopus 로고
    • Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs
    • Leppek, K. et al. Roquin promotes constitutive mRNA decay via a conserved class of stem-loop recognition motifs. Cell Identification of CDEs as the RNA element of Roquins. 153, 869-881 (2013
    • (2013) Cell Identification of CDEs as the RNA element of Roquins. , vol.153 , pp. 869-881
    • Leppek, K.1
  • 46
    • 84893134469 scopus 로고    scopus 로고
    • Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate stress responses
    • Maruyama, T. et al. Roquin-2 promotes ubiquitin-mediated degradation of ASK1 to regulate stress responses. Sci. Signal. 7, ra8 (2014
    • (2014) Sci. Signal. , vol.7
    • Maruyama, T.1
  • 47
    • 21144438325 scopus 로고    scopus 로고
    • A RING-Type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity
    • Vinuesa, C.G. et al. A RING-Type ubiquitin ligase family member required to repress follicular helper T cells and autoimmunity. Nature 435, 452-458 (2005
    • (2005) Nature , vol.435 , pp. 452-458
    • Vinuesa, C.G.1
  • 48
    • 77954959530 scopus 로고    scopus 로고
    • Roquin binds inducible costimulator mRNA and effectors of mRNA decay to induce microRNA-independent post-Transcriptional repression
    • Glasmacher, E. et al. Roquin binds inducible costimulator mRNA and effectors of mRNA decay to induce microRNA-independent post-Transcriptional repression. Nat. Immunol. 11, 725-733 (2010
    • (2010) Nat. Immunol. , vol.11 , pp. 725-733
    • Glasmacher, E.1
  • 49
    • 84876775237 scopus 로고    scopus 로고
    • Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation
    • Pratama, A. et al. Roquin-2 shares functions with its paralog Roquin-1 in the repression of mRNAs controlling T follicular helper cells and systemic inflammation. Immunity 38, 669-680 (2013
    • (2013) Immunity , vol.38 , pp. 669-680
    • Pratama, A.1
  • 50
    • 78650434686 scopus 로고    scopus 로고
    • Heterogeneous ribonucleoprotein C displays a repressor activity mediated by T-cell intracellular antigen-1-related/like protein to modulate Fas exon 6 splicing through a mechanism involving Hu antigen R
    • Izquierdo, J.M Heterogeneous ribonucleoprotein C displays a repressor activity mediated by T-cell intracellular antigen-1-related/like protein to modulate Fas exon 6 splicing through a mechanism involving Hu antigen R. Nucleic Acids Res. 38, 8001-8014 (2010
    • (2010) Nucleic Acids Res. , vol.38 , pp. 8001-8014
    • Izquierdo, J.M.1
  • 51
    • 0034254553 scopus 로고    scopus 로고
    • TIA-1 is a translational silencer that selectively regulates the expression of TNF-Alpha
    • Piecyk, M. et al. TIA-1 is a translational silencer that selectively regulates the expression of TNF-Alpha. EMBO J. 19, 4154-4163 (2000
    • (2000) EMBO J. , vol.19 , pp. 4154-4163
    • Piecyk, M.1
  • 52
    • 1242341962 scopus 로고    scopus 로고
    • Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor α, cyclooxygenase 2, and inflammatory arthritis
    • Phillips, K., Kedersha, N., Shen, L., Blackshear, P.J. & Anderson, P. Arthritis suppressor genes TIA-1 and TTP dampen the expression of tumor necrosis factor α, cyclooxygenase 2, and inflammatory arthritis. Proc. Natl. Acad. Sci. USA 101, 2011-2016 (2004
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2011-2016
    • Phillips, K.1    Kedersha, N.2    Shen, L.3    Blackshear, P.J.4    Anderson, P.5
  • 53
    • 84864120321 scopus 로고    scopus 로고
    • The translational repressor T-cell intracellular antigen-1 (TIA-1) is a key modulator of Th2 and Th17 responses driving pulmonary inflammation induced by exposure to house dust mite
    • Simarro, M. et al. The translational repressor T-cell intracellular antigen-1 (TIA-1) is a key modulator of Th2 and Th17 responses driving pulmonary inflammation induced by exposure to house dust mite. Immunol. Lett. 146, 8-14 (2012
    • (2012) Immunol. Lett. , vol.146 , pp. 8-14
    • Simarro, M.1
  • 54
    • 84863842721 scopus 로고    scopus 로고
    • Mrna decay factor auf1 maintains normal aging telomere maintenance and suppression of senescence by activation of telomerase transcription
    • Pont, A.R., Sadri, N., Hsiao, S.J., Smith, S. & Schneider, R.J. mRNA decay factor AUF1 maintains normal aging, telomere maintenance, and suppression of senescence by activation of telomerase transcription. Mol. Cell 47, 5-15 (2012
    • (2012) Mol. Cell , vol.47 , pp. 5-15
    • Pont, A.R.1    Sadri, N.2    Hsiao, S.J.3    Smith, S.4    Schneider, R.J.5
  • 55
    • 84877826875 scopus 로고    scopus 로고
    • Post-Transcriptional control of gene expression by AUF1: Mechanisms, physiological targets, and regulation
    • White, E.J., Brewer, G. & Wilson, G.M. Post-Transcriptional control of gene expression by AUF1: Mechanisms, physiological targets, and regulation. Biochim. Biophys. Acta 1829, 680-688 (2013
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 680-688
    • White, E.J.1    Brewer, G.2    Wilson, G.M.3
  • 56
    • 33751257755 scopus 로고    scopus 로고
    • Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs
    • Lu, J.Y., Sadri, N. & Schneider, R.J. Endotoxic shock in AUF1 knockout mice mediated by failure to degrade proinflammatory cytokine mRNAs. Genes Dev. 20, 3174-3184 (2006
    • (2006) Genes Dev. , vol.20 , pp. 3174-3184
    • Lu, J.Y.1    Sadri, N.2    Schneider, R.J.3
  • 57
    • 59949094888 scopus 로고    scopus 로고
    • Auf1/Hnrnpd-deficient mice develop pruritic inflammatory skin disease
    • Sadri, N. & Schneider, R.J. Auf1/Hnrnpd-deficient mice develop pruritic inflammatory skin disease. J. Invest. Dermatol. 129, 657-670 (2009
    • (2009) J. Invest. Dermatol. , vol.129 , pp. 657-670
    • Sadri, N.1    Schneider, R.J.2
  • 58
    • 79961159449 scopus 로고    scopus 로고
    • Posttranscriptional control of type I interferon genes by KSRP in the innate immune response against viral infection
    • Lin, W.J. et al. Posttranscriptional control of type I interferon genes by KSRP in the innate immune response against viral infection. Mol. Cell. Biol. 31, 3196-3207 (2011
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3196-3207
    • Lin, W.J.1
  • 60
    • 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
  • 61
    • 84855465218 scopus 로고    scopus 로고
    • Myeloid cell expression of the RNA-binding protein HuR protects mice from pathologic inflammation and colorectal carcinogenesis
    • Yiakouvaki, A. et al. Myeloid cell expression of the RNA-binding protein HuR protects mice from pathologic inflammation and colorectal carcinogenesis. J. Clin. Invest. 122, 48-61 (2012
    • (2012) J. Clin. Invest. , vol.122 , pp. 48-61
    • Yiakouvaki, A.1
  • 62
    • 84863927610 scopus 로고    scopus 로고
    • Functional interplay between RNA-binding protein HuR and microRNAs
    • Srikantan, S., Tominaga, K. & Gorospe, M. Functional interplay between RNA-binding protein HuR and microRNAs. Curr. Protein Pept. Sci. 13, 372-379 (2012
    • (2012) Curr. Protein Pept. Sci. , vol.13 , pp. 372-379
    • Srikantan, S.1    Tominaga, K.2    Gorospe, M.3
  • 63
    • 84859363017 scopus 로고    scopus 로고
    • Sequence requirements for RNA binding by HuR and AUF1
    • Barker, A. et al. Sequence requirements for RNA binding by HuR and AUF1. J. Biochem. 151, 423-437 (2012
    • (2012) J. Biochem. , vol.151 , pp. 423-437
    • Barker, A.1
  • 64
    • 84859055291 scopus 로고    scopus 로고
    • Macrophage β2 integrin-mediated HuR-dependent stabilization of angiogenic factor-encoding mRNAs in inflammatory angiogenesis
    • Zhang, J. et al. Macrophage β2 integrin-mediated, HuR-dependent stabilization of angiogenic factor-encoding mRNAs in inflammatory angiogenesis. Am. J. Pathol. 180, 1751-1760 (2012
    • (2012) Am. J. Pathol. , vol.180 , pp. 1751-1760
    • Zhang, J.1
  • 65
    • 24944468765 scopus 로고    scopus 로고
    • HuR as a negative posttranscriptional modulator in inflammation
    • Katsanou, V. et al. HuR as a negative posttranscriptional modulator in inflammation. Mol. Cell 19, 777-789 (2005
    • (2005) Mol. Cell , vol.19 , pp. 777-789
    • Katsanou, V.1
  • 66
    • 84874027192 scopus 로고    scopus 로고
    • Antagonistic function of the RNA-binding protein HuR and miR-200b in post-Transcriptional regulation of vascular endothelial growth factor-A expression and angiogenesis
    • Chang, S.H. et al. Antagonistic function of the RNA-binding protein HuR and miR-200b in post-Transcriptional regulation of vascular endothelial growth factor-A expression and angiogenesis. J. Biol. Chem. 288, 4908-4921 (2013
    • (2013) J. Biol. Chem. , vol.288 , pp. 4908-4921
    • Chang, S.H.1
  • 68
    • 84871870204 scopus 로고    scopus 로고
    • Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages
    • Arif, A., Chatterjee, P., Moodt, R.A. & Fox, P.L. Heterotrimeric GAIT complex drives transcript-selective translation inhibition in murine macrophages. Mol. Cell. Biol. 32, 5046-5055 (2012
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 5046-5055
    • Arif, A.1    Chatterjee, P.2    Moodt, R.A.3    Fox, P.L.4
  • 69
    • 84875431089 scopus 로고    scopus 로고
    • An extraribosomal function of ribosomal protein L13a in macrophages resolves inflammation
    • Poddar, D. et al. An extraribosomal function of ribosomal protein L13a in macrophages resolves inflammation. J. Immunol. 190, 3600-3612 (2013
    • (2013) J. Immunol. , vol.190 , pp. 3600-3612
    • Poddar, D.1
  • 70
    • 54949109311 scopus 로고    scopus 로고
    • The TSC-mTOR signaling pathway regulates the innate inflammatory response
    • Weichhart, T. et al. The TSC-mTOR signaling pathway regulates the innate inflammatory response. Immunity 29, 565-577 (2008
    • (2008) Immunity , vol.29 , pp. 565-577
    • Weichhart, T.1
  • 71
    • 84887917428 scopus 로고    scopus 로고
    • Pathogen signatures activate a ubiquitination pathway that modulates the function of the metabolic checkpoint kinase mTOR
    • Ivanov, S.S. & Roy, C.R. Pathogen signatures activate a ubiquitination pathway that modulates the function of the metabolic checkpoint kinase mTOR. Nat. Immunol. 14, 1219-1228 (2013
    • (2013) Nat. Immunol. , vol.14 , pp. 1219-1228
    • Ivanov, S.S.1    Roy, C.R.2
  • 72
    • 84862187485 scopus 로고    scopus 로고
    • Akt1 and Akt2 protein kinases differentially contribute to macrophage polarization
    • Arranz, A. et al. Akt1 and Akt2 protein kinases differentially contribute to macrophage polarization. Proc. Natl. Acad. Sci. USA 109, 9517-9522 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9517-9522
    • Arranz, A.1
  • 73
    • 84889249320 scopus 로고    scopus 로고
    • The TSC-mTOR pathway regulates macrophage polarization
    • Byles, V. et al. The TSC-mTOR pathway regulates macrophage polarization. Nat. Commun. 4, 2834 (2013
    • (2013) Nat. Commun. , vol.4 , Issue.2834
    • Byles, V.1
  • 74
    • 0036238675 scopus 로고    scopus 로고
    • AMP-Activated kinase regulates cytoplasmic HuR
    • Wang, W. et al. AMP-Activated kinase regulates cytoplasmic HuR. Mol. Cell. Biol. 22, 3425-3436 (2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3425-3436
    • Wang, W.1
  • 75
    • 25444524850 scopus 로고    scopus 로고
    • Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity
    • Hahn-Windgassen, A. et al. Akt activates the mammalian target of rapamycin by regulating cellular ATP level and AMPK activity. J. Biol. Chem. 280, 32081-32089 (2005
    • (2005) J. Biol. Chem. , vol.280 , pp. 32081-32089
    • Hahn-Windgassen, A.1
  • 76
    • 80053625750 scopus 로고    scopus 로고
    • Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR
    • Damgaard, C.K. & Lykke-Andersen, J. Translational coregulation of 5′TOP mRNAs by TIA-1 and TIAR. Genes Dev. 25, 2057-2068 (2011
    • (2011) Genes Dev. , vol.25 , pp. 2057-2068
    • Damgaard, C.K.1    Lykke-Andersen, J.2
  • 77
    • 77954939922 scopus 로고    scopus 로고
    • Deletion of the RNA-binding proteins ZFP36L1 and ZFP36L2 leads to perturbed thymic development and T lymphoblastic leukemia
    • Hodson, D.J. et al. Deletion of the RNA-binding proteins ZFP36L1 and ZFP36L2 leads to perturbed thymic development and T lymphoblastic leukemia. Nat. Immunol. 11, 717-724 (2010
    • (2010) Nat. Immunol. , vol.11 , pp. 717-724
    • Hodson, D.J.1
  • 78
    • 33845436674 scopus 로고    scopus 로고
    • BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites
    • Benjamin, D., Schmidlin, M., Min, L., Gross, B. & Moroni, C. BRF1 protein turnover and mRNA decay activity are regulated by protein kinase B at the same phosphorylation sites. Mol. Cell. Biol. 26, 9497-9507 (2006
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 9497-9507
    • Benjamin, D.1    Schmidlin, M.2    Min, L.3    Gross, B.4    Moroni, C.5
  • 79
    • 33947584399 scopus 로고    scopus 로고
    • Notch3 and the Notch3-upregulated RNA-binding protein HuD regulate Ikaros alternative splicing
    • Bellavia, D. et al. Notch3 and the Notch3-upregulated RNA-binding protein HuD regulate Ikaros alternative splicing. EMBO J. 26, 1670-1680 (2007
    • (2007) EMBO J. , vol.26 , pp. 1670-1680
    • Bellavia, D.1
  • 80
    • 79960612825 scopus 로고    scopus 로고
    • Perturbation of thymocyte development in nonsense-mediated decay (NMD)-deficient mice
    • Frischmeyer-Guerrerio, P.A. et al. Perturbation of thymocyte development in nonsense-mediated decay (NMD)-deficient mice. Proc. Natl. Acad. Sci. USA 108, 10638-10643 (2011
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 10638-10643
    • Frischmeyer-Guerrerio, P.A.1
  • 81
    • 44149104364 scopus 로고    scopus 로고
    • NMD is essential for hematopoietic stem and progenitor cells and for eliminating by-products of programmed DNA rearrangements
    • Weischenfeldt, J. et al. NMD is essential for hematopoietic stem and progenitor cells and for eliminating by-products of programmed DNA rearrangements. Genes Dev. 22, 1381-1396 (2008
    • (2008) Genes Dev. , vol.22 , pp. 1381-1396
    • Weischenfeldt, J.1
  • 82
    • 29144438951 scopus 로고    scopus 로고
    • Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response
    • Sulic, S. et al. Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response. Genes Dev. 19, 3070-3082 (2005
    • (2005) Genes Dev. , vol.19 , pp. 3070-3082
    • Sulic, S.1
  • 83
    • 34250205545 scopus 로고    scopus 로고
    • Ablation of ribosomal protein L22 selectively impairs alphabeta T cell development by activation of a p53-dependent checkpoint
    • Anderson, S.J. et al. Ablation of ribosomal protein L22 selectively impairs alphabeta T cell development by activation of a p53-dependent checkpoint. Immunity 26, 759-772 (2007
    • (2007) Immunity , vol.26 , pp. 759-772
    • Anderson, S.J.1
  • 84
    • 79952142751 scopus 로고    scopus 로고
    • ATM regulates a DNA damage response posttranscriptional RNA operon in lymphocytes
    • Mazan-Mamczarz, K. et al. ATM regulates a DNA damage response posttranscriptional RNA operon in lymphocytes. Blood 117, 2441-2450 (2011
    • (2011) Blood , vol.117 , pp. 2441-2450
    • Mazan-Mamczarz, K.1
  • 85
    • 67449149662 scopus 로고    scopus 로고
    • Control of thymic T cell maturation, deletion and egress by the RNA-binding protein HuR
    • Papadaki, O. et al. Control of thymic T cell maturation, deletion and egress by the RNA-binding protein HuR. J. Immunol. 182, 6779-6788 (2009
    • (2009) J. Immunol. , vol.182 , pp. 6779-6788
    • Papadaki, O.1
  • 86
    • 79958050339 scopus 로고    scopus 로고
    • Signal-And development-dependent alternative splicing of LEF1 in T cells is controlled by CELF2
    • Mallory, M.J. et al. Signal-And development-dependent alternative splicing of LEF1 in T cells is controlled by CELF2. Mol. Cell. Biol. 31, 2184-2195 (2011
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 2184-2195
    • Mallory, M.J.1
  • 87
    • 50649124254 scopus 로고    scopus 로고
    • The RNA-stabilizing protein HuR regulates the expression of ζ chain of the human T cell receptor-Associated CD3 complex
    • Moulton, V.R., Kyttaris, V.C., Juang, Y.T., Chowdhury, B. & Tsokos, G.C. The RNA-stabilizing protein HuR regulates the expression of ζ chain of the human T cell receptor-Associated CD3 complex. J. Biol. Chem. 283, 20037-20044 (2008
    • (2008) J. Biol. Chem. , vol.283 , pp. 20037-20044
    • Moulton, V.R.1    Kyttaris, V.C.2    Juang, Y.T.3    Chowdhury, B.4    Tsokos, G.C.5
  • 88
    • 84873176790 scopus 로고
    • Splicing factor SF2/ASF rescues IL-2 production in T cells from systemic lupus erythematosus patients by activating IL-2 transcription
    • Moulton, V.R., Grammatikos, A.P., Fitzgerald, L.M. & Tsokos, G.C. Splicing factor SF2/ASF rescues IL-2 production in T cells from systemic lupus erythematosus patients by activating IL-2 transcription. Proc. Natl. Acad. Sci. USA 110, 1845-1850 (2013
    • (1845) Proc. Natl. Acad. Sci. USA 110 , vol.2013
    • Moulton, V.R.1    Grammatikos, A.P.2    Fitzgerald, L.M.3    Tsokos, G.C.4
  • 89
    • 0035106072 scopus 로고    scopus 로고
    • SC35 plays a role in T cell development and alternative splicing of CD45
    • Wang, H.Y., Xu, X., Ding, J.H., Bermingham, J.R. Jr. & Fu, X.D. SC35 plays a role in T cell development and alternative splicing of CD45. Mol. Cell 7, 331-342 (2001
    • (2001) Mol. Cell , vol.7 , pp. 331-342
    • Wang, H.Y.1    Xu, X.2    Ding, J.H.3    Bermingham Jr., J.R.4    Fu, X.D.5
  • 90
    • 84862002189 scopus 로고    scopus 로고
    • Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein L regulates development, proliferation, and migration of thymic pre-T cells
    • Gaudreau, M.C., Heyd, F., Bastien, R., Wilhelm, B. & Moroy, T. Alternative splicing controlled by heterogeneous nuclear ribonucleoprotein L regulates development, proliferation, and migration of thymic pre-T cells. J. Immunol. 188, 5377-5388 (2012
    • (2012) J. Immunol. , vol.188 , pp. 5377-5388
    • Gaudreau, M.C.1    Heyd, F.2    Bastien, R.3    Wilhelm, B.4    Moroy, T.5
  • 92
    • 70149110269 scopus 로고    scopus 로고
    • Dicer-dependent microRNA pathway controls invariant NKT cell development
    • Fedeli, M. et al. Dicer-dependent microRNA pathway controls invariant NKT cell development. J. Immunol. 183, 2506-2512 (2009
    • (2009) J. Immunol. , vol.183 , pp. 2506-2512
    • Fedeli, M.1
  • 93
    • 51049110261 scopus 로고    scopus 로고
    • Dicer-dependent microRNA pathway safeguards regulatory T cell function
    • Liston, A., Lu, L.F., O'Carroll, D., Tarakhovsky, A. & Rudensky, A.Y. Dicer-dependent microRNA pathway safeguards regulatory T cell function. J. Exp. Med. 205, 1993-2004 (2008
    • (2008) J. Exp. Med. , vol.205 , pp. 1993-2004
    • Liston, A.1    Lu, L.F.2    O'Carroll, D.3    Tarakhovsky, A.4    Rudensky, A.Y.5
  • 94
    • 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
  • 95
    • 57449113390 scopus 로고    scopus 로고
    • Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL
    • Wu, Z. et al. Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL. Immunity 19, 863-875 (2008
    • (2008) Immunity , vol.19 , pp. 863-875
    • Wu, Z.1
  • 96
    • 84878315256 scopus 로고    scopus 로고
    • Malt1-induced cleavage of regnase-1 in CD4+ helper T cells regulates immune activation
    • Uehata, T. et al. Malt1-induced cleavage of regnase-1 in CD4+ helper T cells regulates immune activation. Cell 153, 1036-1049 (2013
    • (2013) Cell , vol.153 , pp. 1036-1049
    • Uehata, T.1
  • 97
    • 84876781274 scopus 로고    scopus 로고
    • Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40 costimulator mRNAs and control follicular helper T cell differentiation
    • Vogel, K.U. et al. Roquin paralogs 1 and 2 redundantly repress the Icos and Ox40 costimulator mRNAs and control follicular helper T cell differentiation. Immunity 38, 655-668 (2013
    • (2013) Immunity , vol.38 , pp. 655-668
    • Vogel, K.U.1
  • 98
    • 67650529584 scopus 로고    scopus 로고
    • Post-Transcriptional regulation in lymphocytes: The case of CD154
    • Vavassori, S. & Covey, L.R. Post-Transcriptional regulation in lymphocytes: The case of CD154. RNA Biol. 6, 259-265 (2009
    • (2009) RNA Biol. , vol.6 , pp. 259-265
    • Vavassori, S.1    Covey, L.R.2
  • 99
    • 84869821367 scopus 로고    scopus 로고
    • MCPIP1 down-regulates IL-2 expression through an ARE-independent pathway
    • Li, M. et al. MCPIP1 down-regulates IL-2 expression through an ARE-independent pathway. PLoS ONE 7, e49841 (2012
    • (2012) PLoS ONE , vol.7
    • Li, M.1
  • 100
    • 34249063242 scopus 로고    scopus 로고
    • NF90 regulates inducible IL-2 gene expression in T cells
    • Shi, L., Godfrey, W.R., Lin, J., Zhao, G. & Kao, P.N. NF90 regulates inducible IL-2 gene expression in T cells. J. Exp. Med. 204, 971-977 (2007
    • (2007) J. Exp. Med. , vol.204 , pp. 971-977
    • Shi, L.1    Godfrey, W.R.2    Lin, J.3    Zhao, G.4    Kao, P.N.5
  • 101
    • 84888391819 scopus 로고    scopus 로고
    • Posttranscriptional gene regulation of IL-17 by the RNA-binding protein HuR is required for initiation of experimental autoimmune encephalomyelitis
    • Chen, J. et al. Posttranscriptional gene regulation of IL-17 by the RNA-binding protein HuR is required for initiation of experimental autoimmune encephalomyelitis. J. Immunol. 191, 5441-5450 (2013
    • (2013) J. Immunol. , vol.191 , pp. 5441-5450
    • Chen, J.1
  • 102
    • 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, V.A., Izquierdo, J.M. & Valcarcel, J. Strict 3′ splice site sequence requirements for U2 snRNP recruitment after U2AF binding underlie a genetic defect leading to autoimmune disease. RNA 17, 401-411 (2011
    • (2011) RNA , vol.17 , pp. 401-411
    • Corrionero, A.1    Raker, V.A.2    Izquierdo, J.M.3    Valcarcel, J.4
  • 103
    • 84878720961 scopus 로고    scopus 로고
    • Hnrnp A1 contacts exon 5 to promote exon 6 inclusion of apoptotic Fas gene
    • Oh, H. et al. hnRNP A1 contacts exon 5 to promote exon 6 inclusion of apoptotic Fas gene. Apoptosis 18, 825-835 (2013
    • (2013) Apoptosis , vol.18 , pp. 825-835
    • Oh, H.1
  • 104
    • 84871014558 scopus 로고    scopus 로고
    • Apoptotic-induced cleavage shifts HuR from being a promoter of survival to an activator of caspase-mediated apoptosis
    • von Roretz, C. et al. Apoptotic-induced cleavage shifts HuR from being a promoter of survival to an activator of caspase-mediated apoptosis. Cell Death Differ. 20, 154-168 (2013
    • (2013) Cell Death Differ. , vol.20 , pp. 154-168
    • Von Roretz, C.1
  • 105
    • 54249164720 scopus 로고    scopus 로고
    • Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65
    • Izquierdo, J.M. Fas splicing regulation during early apoptosis is linked to caspase-mediated cleavage of U2AF65. Mol. Biol. Cell 19, 3299-3307 (2008
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3299-3307
    • Izquierdo, J.M.1
  • 107
    • 78751705190 scopus 로고    scopus 로고
    • Posttranscriptional silencing of effector cytokine mRNA underlies the anergic phenotype of self-reactive T cells
    • Villarino, A.V. et al. Posttranscriptional silencing of effector cytokine mRNA underlies the anergic phenotype of self-reactive T cells. Immunity 34, 50-60 (2011
    • (2011) Immunity , vol.34 , pp. 50-60
    • Villarino, A.V.1
  • 108
    • 34447532192 scopus 로고    scopus 로고
    • Identification and mechanistic characterization of low-molecular-weight inhibitors for HuR
    • Meisner, N.C. et al. Identification and mechanistic characterization of low-molecular-weight inhibitors for HuR. Nat. Chem. Biol. 3, 508-515 (2007
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 508-515
    • Meisner, N.C.1
  • 109
    • 81255210981 scopus 로고    scopus 로고
    • Designer RNA-binding proteins: New tools for manipulating the transcriptome
    • Filipovska, A. & Rackham, O. Designer RNA-binding proteins: New tools for manipulating the transcriptome. RNA Biol. 8, 978-983 (2011
    • (2011) RNA Biol. , vol.8 , pp. 978-983
    • Filipovska, A.1    Rackham, O.2
  • 111


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