메뉴 건너뛰기




Volumn 57, Issue 4, 2014, Pages 432-444

RNA-binding proteins in neurological diseases

Author keywords

neurological diseases; post transcriptional regulation; RNA binding proteins

Indexed keywords

DNA BINDING PROTEIN; FRAGILE X MENTAL RETARDATION PROTEIN; HU ANTIGEN; MESSENGER RNA; NERVE PROTEIN; NOVA ANTIGEN; PROTEIN TDP-43; QKI PROTEIN, HUMAN; RBFOX1 PROTEIN, HUMAN; RNA BINDING PROTEIN; TUMOR ANTIGEN;

EID: 84899945638     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-014-4647-9     Document Type: Review
Times cited : (70)

References (170)
  • 1
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: coordination of post-transcriptional events
    • Keene JD. RNA regulons: coordination of post-transcriptional events. Nat Rev Genet, 2007, 8: 533-543.
    • (2007) Nat Rev Genet , vol.8 , pp. 533-543
    • Keene, J.D.1
  • 2
    • 24644502657 scopus 로고    scopus 로고
    • From birth to death: the complex lives of eukaryotic mrnas
    • Moore MJ. From birth to death: the complex lives of eukaryotic mrnas. Science, 2005, 309: 1514-1518.
    • (2005) Science , vol.309 , pp. 1514-1518
    • Moore, M.J.1
  • 3
    • 40449138572 scopus 로고    scopus 로고
    • Post-transcriptional gene regulation: from genome-wide studies to principles
    • Halbeisen RE, Galgano A, Scherrer T, Gerber AP. Post-transcriptional gene regulation: from genome-wide studies to principles. Cell Mol Life Sci, 2008, 65: 798-813.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 798-813
    • Halbeisen, R.E.1    Galgano, A.2    Scherrer, T.3    Gerber, A.P.4
  • 4
    • 80053618714 scopus 로고    scopus 로고
    • Construction, structure and dynamics of post-transcriptional regulatory network directed by RNA-binding proteins
    • Janga SC, Mittal N. Construction, structure and dynamics of post-transcriptional regulatory network directed by RNA-binding proteins. Adv Exp Med Biol, 2011, 722: 103-117.
    • (2011) Adv Exp Med Biol , vol.722 , pp. 103-117
    • Janga, S.C.1    Mittal, N.2
  • 5
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: modular design for efficient function
    • Lunde BM, Moore C, Varani G. RNA-binding proteins: modular design for efficient function. Nat Rev Mol Cell Biol, 2007, 8: 479-490.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 6
    • 0037678415 scopus 로고    scopus 로고
    • Cell-specific RNA-binding proteins in human disease
    • Musunuru K. Cell-specific RNA-binding proteins in human disease. Trends Cardiovasc Med, 2003, 13: 188-195.
    • (2003) Trends Cardiovasc Med , vol.13 , pp. 188-195
    • Musunuru, K.1
  • 8
    • 84875429298 scopus 로고    scopus 로고
    • Reflections on the history of pre-mRNA processing and highlights of current knowledge: a unified picture
    • Darnell JE Jr. Reflections on the history of pre-mRNA processing and highlights of current knowledge: a unified picture. RNA, 2013, 19: 443-460.
    • (2013) Rna , vol.19 , pp. 443-460
    • Darnell Jr., J.E.1
  • 9
    • 84863255704 scopus 로고    scopus 로고
    • Evolution of SR protein and hnRNP splicing regulatory factors
    • Busch A, Hertel KJ. Evolution of SR protein and hnRNP splicing regulatory factors. Wiley Interdiscip Rev RNA, 2012, 3: 1-12.
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , pp. 1-12
    • Busch, A.1    Hertel, K.J.2
  • 10
    • 84880604441 scopus 로고    scopus 로고
    • Take the (RN)A-train: localization of mRNA to the endoplasmic reticulum
    • Hermesh O, Jansen RP. Take the (RN)A-train: localization of mRNA to the endoplasmic reticulum. Biochim Biophys Acta, 2013, 1833: 2519-2525.
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 2519-2525
    • Hermesh, O.1    Jansen, R.P.2
  • 13
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: the ins and outs of translation
    • Buchan JR, Parker R. Eukaryotic stress granules: the ins and outs of translation. Mol Cell, 2009, 36: 932-941.
    • (2009) Mol Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 14
    • 33847417585 scopus 로고    scopus 로고
    • P bodies and the control of mRNA translation and degradation
    • Parker R, Sheth U. P bodies and the control of mRNA translation and degradation. Mol Cell, 2007, 25: 635-646.
    • (2007) Mol Cell , vol.25 , pp. 635-646
    • Parker, R.1    Sheth, U.2
  • 15
    • 84869192353 scopus 로고    scopus 로고
    • Regulated protein aggregation: stress granules and neurodegeneration
    • Wolozin B. Regulated protein aggregation: stress granules and neurodegeneration. Mol Neurodeg, 2012, 7: 56.
    • (2012) Mol Neurodeg , vol.7 , pp. 56
    • Wolozin, B.1
  • 16
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: possible roles in the control of translation and mRNA degradation
    • Decker CJ, Parker R. P-bodies and stress granules: possible roles in the control of translation and mRNA degradation. Cold Spring Harbor Perspect Biol, 2012, 4: a012286.
    • (2012) Cold Spring Harbor Perspect Biol , vol.4
    • Decker, C.J.1    Parker, R.2
  • 18
    • 84880312659 scopus 로고    scopus 로고
    • RNA protein interaction in neurons
    • Darnell RB. RNA protein interaction in neurons. Annu Rev Neurosci, 2013, 36: 243-270.
    • (2013) Annu Rev Neurosci , vol.36 , pp. 243-270
    • Darnell, R.B.1
  • 19
    • 35548940665 scopus 로고    scopus 로고
    • Neuronal regulation of alternative pre-mrna splicing
    • Li Q, Lee JA, Black DL. Neuronal regulation of alternative pre-mrna splicing. Nat Rev Neurosci, 2007, 8: 819-831.
    • (2007) Nat Rev Neurosci , vol.8 , pp. 819-831
    • Li, Q.1    Lee, J.A.2    Black, D.L.3
  • 20
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: new insights from global analyses
    • Blencowe BJ. Alternative splicing: new insights from global analyses. Cell, 2006, 126: 37-47.
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 21
    • 10944229314 scopus 로고    scopus 로고
    • Variation in alternative splicing across human tissues
    • Yeo G, Holste D, Kreiman G, Burge CB. Variation in alternative splicing across human tissues. Genome Biol, 2004, 5: R74.
    • (2004) Genome Biol , vol.5
    • Yeo, G.1    Holste, D.2    Kreiman, G.3    Burge, C.B.4
  • 22
  • 23
    • 84882822335 scopus 로고    scopus 로고
    • Alternative splicing in the nervous system. In: Squire LR, ed. New Encyclopedia of Neuroscience
    • Wu JY, Postashkin J. Alternative splicing in the nervous system. In: Squire LR, ed. New Encyclopedia of Neuroscience. Elsevier, 2009, 1: 245-251.
    • (2009) Elsevier , vol.1 , pp. 245-251
    • Wu, J.Y.1    Postashkin, J.2
  • 24
    • 79953183632 scopus 로고    scopus 로고
    • Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy
    • Fushimi K, Long C, Jayaram N, Chen X, Li L, Wu JY. Expression of human FUS/TLS in yeast leads to protein aggregation and cytotoxicity, recapitulating key features of FUS proteinopathy. Protein Cell, 2011, 2: 141-149.
    • (2011) Protein Cell , vol.2 , pp. 141-149
    • Fushimi, K.1    Long, C.2    Jayaram, N.3    Chen, X.4    Li, L.5    Wu, J.Y.6
  • 25
    • 70849088746 scopus 로고    scopus 로고
    • Subcellular mRNA localization in animal cells and why it matters
    • Holt CE, Bullock SL. Subcellular mRNA localization in animal cells and why it matters. Science, 2009, 326: 1212-1216.
    • (2009) Science , vol.326 , pp. 1212-1216
    • Holt, C.E.1    Bullock, S.L.2
  • 26
    • 0346728801 scopus 로고    scopus 로고
    • Long-term potentiation and memory
    • Lynch MA. Long-term potentiation and memory. Physiol Rev, 2004, 84: 87-136.
    • (2004) Physiol Rev , vol.84 , pp. 87-136
    • Lynch, M.A.1
  • 27
    • 0037079094 scopus 로고    scopus 로고
    • Localized synaptic potentiation by BDNF requires local protein synthesis in the developing axon
    • Zhang X, Poo MM. Localized synaptic potentiation by BDNF requires local protein synthesis in the developing axon. Neuron, 2002, 36: 675-688.
    • (2002) Neuron , vol.36 , pp. 675-688
    • Zhang, X.1    Poo, M.M.2
  • 29
    • 80054696673 scopus 로고    scopus 로고
    • RNA regulation in neurologic disease and cancer
    • Darnell RB. RNA regulation in neurologic disease and cancer. Cancer Res Treat, 2010, 42: 125-129.
    • (2010) Cancer Res Treat , vol.42 , pp. 125-129
    • Darnell, R.B.1
  • 30
    • 0037443035 scopus 로고    scopus 로고
    • Pre-mRNA splicing and human disease
    • Faustino NA, Cooper TA. Pre-mRNA splicing and human disease. Genes Dev, 2003, 17: 419-437.
    • (2003) Genes Dev , vol.17 , pp. 419-437
    • Faustino, N.A.1    Cooper, T.A.2
  • 31
    • 84863527997 scopus 로고    scopus 로고
    • RNA-binding proteins in neurodegenerative disease: Tdp-43 and beyond
    • Hanson KA, Kim SH, Tibbetts RS. RNA-binding proteins in neurodegenerative disease: Tdp-43 and beyond. Wiley Interdiscip Rev RNA, 2012, 3: 265-285.
    • (2012) Wiley Interdiscip Rev RNA , vol.3 , pp. 265-285
    • Hanson, K.A.1    Kim, S.H.2    Tibbetts, R.S.3
  • 32
    • 33749054403 scopus 로고    scopus 로고
    • Splicing regulation in neurologic disease
    • Licatalosi DD, Darnell RB. Splicing regulation in neurologic disease. Neuron, 2006, 52: 93-101.
    • (2006) Neuron , vol.52 , pp. 93-101
    • Licatalosi, D.D.1    Darnell, R.B.2
  • 33
    • 0027374048 scopus 로고
    • Nova, the paraneoplastic Ri antigen, is homologous to an rna-binding protein and is specifically expressed in the developing motor system
    • Buckanovich RJ, Posner JB, Darnell RB. Nova, the paraneoplastic Ri antigen, is homologous to an rna-binding protein and is specifically expressed in the developing motor system. Neuron, 1993, 11: 657-672.
    • (1993) Neuron , vol.11 , pp. 657-672
    • Buckanovich, R.J.1    Posner, J.B.2    Darnell, R.B.3
  • 35
    • 13144293035 scopus 로고    scopus 로고
    • The neuronal RNA-binding protein Nova-2 is implicated as the autoantigen targeted in POMA patients with dementia
    • Yang YY, Yin GL, Darnell RB. The neuronal RNA-binding protein Nova-2 is implicated as the autoantigen targeted in POMA patients with dementia. Proc Natl Acad Sci USA, 1998, 95: 13254-13259.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13254-13259
    • Yang, Y.Y.1    Yin, G.L.2    Darnell, R.B.3
  • 37
    • 0034705034 scopus 로고    scopus 로고
    • The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain
    • Jensen KB, Musunuru K, Lewis HA, Burley SK, Darnell RB. The tetranucleotide UCAY directs the specific recognition of RNA by the Nova K-homology 3 domain. Proc Natl Acad Sci USA, 2000, 97: 5740-5745.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5740-5745
    • Jensen, K.B.1    Musunuru, K.2    Lewis, H.A.3    Burley, S.K.4    Darnell, R.B.5
  • 39
    • 0030992812 scopus 로고    scopus 로고
    • The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo
    • Buckanovich RJ, Darnell RB. The neuronal RNA binding protein Nova-1 recognizes specific RNA targets in vitro and in vivo. Mol Cell Biol, 1997, 17: 3194-3201.
    • (1997) Mol Cell Biol , vol.17 , pp. 3194-3201
    • Buckanovich, R.J.1    Darnell, R.B.2
  • 40
    • 0038382977 scopus 로고    scopus 로고
    • Nova regulates GABA(A) receptor gamma2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer
    • Dredge BK, Darnell RB. Nova regulates GABA(A) receptor gamma2 alternative splicing via a distal downstream UCAU-rich intronic splicing enhancer. Mol Cell Biol, 2003, 23: 4687-4700.
    • (2003) Mol Cell Biol , vol.23 , pp. 4687-4700
    • Dredge, B.K.1    Darnell, R.B.2
  • 45
    • 0026094583 scopus 로고
    • HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal
    • Szabo A, Dalmau J, Manley G, Rosenfeld M, Wong E, Henson J, Posner JB, Furneaux HM. HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal. Cell, 1991, 67: 325-333.
    • (1991) Cell , vol.67 , pp. 325-333
    • Szabo, A.1    Dalmau, J.2    Manley, G.3    Rosenfeld, M.4    Wong, E.5    Henson, J.6    Posner, J.B.7    Furneaux, H.M.8
  • 46
    • 0026712949 scopus 로고
    • The expression of the Hu (paraneoplastic encephalomyelitis/sensory neuronopathy) antigen in human normal and tumor tissues
    • Dalmau J, Furneaux HM, Cordon-Cardo C, Posner JB. The expression of the Hu (paraneoplastic encephalomyelitis/sensory neuronopathy) antigen in human normal and tumor tissues. Am J Pathol, 1992, 141: 881-886.
    • (1992) Am J Pathol , vol.141 , pp. 881-886
    • Dalmau, J.1    Furneaux, H.M.2    Cordon-Cardo, C.3    Posner, J.B.4
  • 47
    • 0030909816 scopus 로고    scopus 로고
    • A hierarchy of Hu RNA binding proteins in developing and adult neurons
    • Okano HJ, Darnell RB. A hierarchy of Hu RNA binding proteins in developing and adult neurons. J Neurosci, 1997, 17: 3024-3037.
    • (1997) J Neurosci , vol.17 , pp. 3024-3037
    • Okano, H.J.1    Darnell, R.B.2
  • 49
    • 0033836348 scopus 로고    scopus 로고
    • Overexpression of HuD, but not of its truncated form HuD I+II, promotes GAP-43 gene expression and neurite outgrowth in PC12 cells in the absence of nerve growth factor
    • Anderson KD, Morin MA, Beckel-Mitchener A, Mobarak CD, Neve RL, Furneaux HM, Burry R, Perrone-Bizzozero NI. Overexpression of HuD, but not of its truncated form HuD I+II, promotes GAP-43 gene expression and neurite outgrowth in PC12 cells in the absence of nerve growth factor. J Neurochem, 2000, 75: 1103-1114.
    • (2000) J Neurochem , vol.75 , pp. 1103-1114
    • Anderson, K.D.1    Morin, M.A.2    Beckel-Mitchener, A.3    Mobarak, C.D.4    Neve, R.L.5    Furneaux, H.M.6    Burry, R.7    Perrone-Bizzozero, N.I.8
  • 50
    • 0035949678 scopus 로고    scopus 로고
    • Posttranscriptional regulation of gene expression in learning by the neuronal ELAV-like mRNA-stabilizing proteins
    • Quattrone A, Pascale A, Nogues X, Zhao W, Gusev P, Pacini A, Alkon DL. Posttranscriptional regulation of gene expression in learning by the neuronal ELAV-like mRNA-stabilizing proteins. Proc Natl Acad Sci USA, 2001, 98: 11668-11673.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11668-11673
    • Quattrone, A.1    Pascale, A.2    Nogues, X.3    Zhao, W.4    Gusev, P.5    Pacini, A.6    Alkon, D.L.7
  • 51
    • 38849117246 scopus 로고    scopus 로고
    • RNA-protein interactions and control of mRNA stability in neurons
    • Bolognani F, Perrone-Bizzozero NI. RNA-protein interactions and control of mRNA stability in neurons. J Neurosci Res, 2008, 86: 481-489.
    • (2008) J Neurosci Res , vol.86 , pp. 481-489
    • Bolognani, F.1    Perrone-Bizzozero, N.I.2
  • 53
    • 53849124668 scopus 로고    scopus 로고
    • Diverse molecular functions of Hu proteins
    • Hinman MN, Lou H. Diverse molecular functions of Hu proteins. Cell Mol Life Sci, 2008, 65: 3168-3181.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 3168-3181
    • Hinman, M.N.1    Lou, H.2
  • 54
    • 0037008694 scopus 로고    scopus 로고
    • Poly(A) tail length-dependent stabilization of GAP-43 mRNA by the RNA-binding protein HuD
    • Beckel-Mitchener AC, Miera A, Keller R, Perrone-Bizzozero NI. Poly(A) tail length-dependent stabilization of GAP-43 mRNA by the RNA-binding protein HuD. J Biol Chem, 2002, 277: 27996-28002.
    • (2002) J Biol Chem , vol.277 , pp. 27996-28002
    • Beckel-Mitchener, A.C.1    Miera, A.2    Keller, R.3    Perrone-Bizzozero, N.I.4
  • 55
    • 0031038858 scopus 로고    scopus 로고
    • Ectopic expression of Hel-N1, an RNA-binding protein, increases glucose transporter (GLUT1) expression in 3T3-L1 adipocytes
    • Jain RG, Andrews LG, McGowan KM, Pekala PH, Keene JD. Ectopic expression of Hel-N1, an RNA-binding protein, increases glucose transporter (GLUT1) expression in 3T3-L1 adipocytes. Mol Cell Biol, 1997, 17: 954-962.
    • (1997) Mol Cell Biol , vol.17 , pp. 954-962
    • Jain, R.G.1    Andrews, L.G.2    McGowan, K.M.3    Pekala, P.H.4    Keene, J.D.5
  • 56
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy NS, Chung S, Furneaux H, Levy AP. Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J Biol Chem, 1998, 273: 6417-6423.
    • (1998) J Biol Chem , vol.273 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 57
    • 0030933006 scopus 로고    scopus 로고
    • Identification of HuR as a protein implicated in AUUUA-mediated mRNA decay
    • Myer VE, Fan XC, Steitz JA. Identification of HuR as a protein implicated in AUUUA-mediated mRNA decay. EMBO J, 1997, 16: 2130-2139.
    • (1997) EMBO J , vol.16 , pp. 2130-2139
    • Myer, V.E.1    Fan, X.C.2    Steitz, J.A.3
  • 58
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng SS, Chen CY, Xu N, Shyu AB. RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J, 1998, 17: 3461-3470.
    • (1998) EMBO J , vol.17 , pp. 3461-3470
    • Peng, S.S.1    Chen, C.Y.2    Xu, N.3    Shyu, A.B.4
  • 59
    • 0035162672 scopus 로고    scopus 로고
    • ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins
    • Bakheet T, Frevel M, Williams BR, Greer W, Khabar KS. ARED: human AU-rich element-containing mRNA database reveals an unexpectedly diverse functional repertoire of encoded proteins. Nucleic Acids Res, 2001, 29: 246-254.
    • (2001) Nucleic Acids Res , vol.29 , pp. 246-254
    • Bakheet, T.1    Frevel, M.2    Williams, B.R.3    Greer, W.4    Khabar, K.S.5
  • 60
    • 0033557936 scopus 로고    scopus 로고
    • ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in human teratocarcinoma cells
    • Antic D, Lu N, Keene JD. ELAV tumor antigen, Hel-N1, increases translation of neurofilament M mRNA and induces formation of neurites in human teratocarcinoma cells. Genes Dev, 1999, 13: 449-461.
    • (1999) Genes Dev , vol.13 , pp. 449-461
    • Antic, D.1    Lu, N.2    Keene, J.D.3
  • 62
    • 33847076533 scopus 로고    scopus 로고
    • Hu proteins regulate polyadenylation by blocking sites containing U-rich sequences
    • Zhu H, Zhou HL, Hasman RA, Lou H. Hu proteins regulate polyadenylation by blocking sites containing U-rich sequences. J Biol Chem, 2007, 282: 2203-2210.
    • (2007) J Biol Chem , vol.282 , pp. 2203-2210
    • Zhu, H.1    Zhou, H.L.2    Hasman, R.A.3    Lou, H.4
  • 63
    • 49649128843 scopus 로고    scopus 로고
    • Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of fas apoptosis-promoting receptor on exon definition
    • Izquierdo JM. Hu antigen R (HuR) functions as an alternative pre-mRNA splicing regulator of fas apoptosis-promoting receptor on exon definition. J Biol Chem, 2008, 283: 19077-19084.
    • (2008) J Biol Chem , vol.283 , pp. 19077-19084
    • Izquierdo, J.M.1
  • 64
    • 77954366986 scopus 로고    scopus 로고
    • Promotion of exon 6 inclusion in HuD pre-mRNA by Hu protein family members
    • Wang H, Molfenter J, Zhu H, Lou H. Promotion of exon 6 inclusion in HuD pre-mRNA by Hu protein family members. Nucleic Acids Res, 2010, 38: 3760-3770.
    • (2010) Nucleic Acids Res , vol.38 , pp. 3760-3770
    • Wang, H.1    Molfenter, J.2    Zhu, H.3    Lou, H.4
  • 66
    • 33845380816 scopus 로고    scopus 로고
    • A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators
    • Zhu H, Hasman RA, Barron VA, Luo G, Lou H. A nuclear function of Hu proteins as neuron-specific alternative RNA processing regulators. Mol Biol Cell, 2006, 17: 5105-5114.
    • (2006) Mol Biol Cell , vol.17 , pp. 5105-5114
    • Zhu, H.1    Hasman, R.A.2    Barron, V.A.3    Luo, G.4    Lou, H.5
  • 67
    • 38949098620 scopus 로고    scopus 로고
    • Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA
    • Zhu H, Hinman MN, Hasman RA, Mehta P, Lou H. Regulation of neuron-specific alternative splicing of neurofibromatosis type 1 pre-mRNA. Mol Cell Biol, 2008, 28: 1240-1251.
    • (2008) Mol Cell Biol , vol.28 , pp. 1240-1251
    • Zhu, H.1    Hinman, M.N.2    Hasman, R.A.3    Mehta, P.4    Lou, H.5
  • 68
    • 0037450704 scopus 로고    scopus 로고
    • A vertebrate RNA-binding protein Fox-1 regulates tissue-specific splicing via the pentanucleotide GCAUG
    • Jin Y, Suzuki H, Maegawa S, Endo H, Sugano S, Hashimoto K, Yasuda K, Inoue K. A vertebrate RNA-binding protein Fox-1 regulates tissue-specific splicing via the pentanucleotide GCAUG. EMBO J, 2003, 22: 905-912.
    • (2003) EMBO J , vol.22 , pp. 905-912
    • Jin, Y.1    Suzuki, H.2    Maegawa, S.3    Endo, H.4    Sugano, S.5    Hashimoto, K.6    Yasuda, K.7    Inoue, K.8
  • 69
    • 27644455141 scopus 로고    scopus 로고
    • Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals
    • Underwood JG, Boutz PL, Dougherty JD, Stoilov P, Black DL. Homologues of the Caenorhabditis elegans Fox-1 protein are neuronal splicing regulators in mammals. Mol Cell Biol, 2005, 25: 10005-10016.
    • (2005) Mol Cell Biol , vol.25 , pp. 10005-10016
    • Underwood, J.G.1    Boutz, P.L.2    Dougherty, J.D.3    Stoilov, P.4    Black, D.L.5
  • 70
    • 79959679062 scopus 로고    scopus 로고
    • NeuN/Rbfox3 nuclear and cytoplasmic isoforms differentially regulate alternative splicing and nonsense-mediated decay of Rbfox2
    • Dredge BK, Jensen KB. NeuN/Rbfox3 nuclear and cytoplasmic isoforms differentially regulate alternative splicing and nonsense-mediated decay of Rbfox2. PLoS ONE, 2011, 6: e21585.
    • (2011) PLoS ONE , vol.6
    • Dredge, B.K.1    Jensen, K.B.2
  • 71
    • 0034701797 scopus 로고    scopus 로고
    • A novel protein with RNA-binding motifs interacts with ataxin-2
    • Shibata H, Huynh DP, Pulst SM. A novel protein with RNA-binding motifs interacts with ataxin-2. Hum Mol Genet, 2000, 9: 1303-1313.
    • (2000) Hum Mol Genet , vol.9 , pp. 1303-1313
    • Shibata, H.1    Huynh, D.P.2    Pulst, S.M.3
  • 72
    • 18944370955 scopus 로고    scopus 로고
    • Candidate-gene screening and association analysis at the autism-susceptibility locus on chromosome 16p: evidence of association at GRIN2A and ABAT
    • International Molecular Genetics Study of Autism Consortium
    • Barnby G, Abbott A, Sykes N, Morris A, Weeks DE, Mott R, Lamb J, Bailey AJ, Monaco AP; International Molecular Genetics Study of Autism Consortium. Candidate-gene screening and association analysis at the autism-susceptibility locus on chromosome 16p: evidence of association at GRIN2A and ABAT. Am J Hum Genet, 2005, 76: 950-966.
    • (2005) Am J Hum Genet , vol.76 , pp. 950-966
    • Barnby, G.1    Abbott, A.2    Sykes, N.3    Morris, A.4    Weeks, D.E.5    Mott, R.6    Lamb, J.7    Bailey, A.J.8    Monaco, A.P.9
  • 77
    • 59649107040 scopus 로고    scopus 로고
    • An RNA code for the Fox2 splicing regulator revealed by mapping RNA-protein interactions in stem cells
    • Yeo GW, Coufal NG, Liang TY, Peng GE, Fu XD, Gage FH. An RNA code for the Fox2 splicing regulator revealed by mapping RNA-protein interactions in stem cells. Nat Struct Mol Biol, 2009, 16: 130-137.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 130-137
    • Yeo, G.W.1    Coufal, N.G.2    Liang, T.Y.3    Peng, G.E.4    Fu, X.D.5    Gage, F.H.6
  • 78
    • 51949111100 scopus 로고    scopus 로고
    • Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2
    • Zhang C, Zhang Z, Castle J, Sun S, Johnson J, Krainer AR, Zhang MQ. Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2. Genes Dev, 2008, 22: 2550-2563.
    • (2008) Genes Dev , vol.22 , pp. 2550-2563
    • Zhang, C.1    Zhang, Z.2    Castle, J.3    Sun, S.4    Johnson, J.5    Krainer, A.R.6    Zhang, M.Q.7
  • 79
    • 25444437768 scopus 로고    scopus 로고
    • QUAKING KH domain proteins as regulators of glial cell fate and myelination
    • Larocque D, Richard S. QUAKING KH domain proteins as regulators of glial cell fate and myelination. RNA Biol, 2005, 2: 37-40.
    • (2005) RNA Biol , vol.2 , pp. 37-40
    • Larocque, D.1    Richard, S.2
  • 80
    • 0032189955 scopus 로고    scopus 로고
    • QKI expression is regulated during neuron-glial cell fate decisions
    • Hardy RJ. QKI expression is regulated during neuron-glial cell fate decisions. J Neurosci Res, 1998, 54: 46-57.
    • (1998) J Neurosci Res , vol.54 , pp. 46-57
    • Hardy, R.J.1
  • 81
    • 38849206330 scopus 로고    scopus 로고
    • New implications for the quaking RNA binding protein in human disease
    • Chenard CA, Richard S. New implications for the quaking RNA binding protein in human disease. J Neurosci Res, 2008, 86: 233-242.
    • (2008) J Neurosci Res , vol.86 , pp. 233-242
    • Chenard, C.A.1    Richard, S.2
  • 82
    • 40549106161 scopus 로고    scopus 로고
    • Developmental expression profile of quaking, a candidate gene for schizophrenia, and its target genes in human prefrontal cortex and hippocampus shows regional specificity
    • Lauriat TL, Shiue L, Haroutunian V, Verbitsky M, Ares M Jr, Ospina L, McInnes LA. Developmental expression profile of quaking, a candidate gene for schizophrenia, and its target genes in human prefrontal cortex and hippocampus shows regional specificity. J Neurosci Res, 2008, 86: 785-796.
    • (2008) J Neurosci Res , vol.86 , pp. 785-796
    • Lauriat, T.L.1    Shiue, L.2    Haroutunian, V.3    Verbitsky, M.4    Ares Jr., M.5    Ospina, L.6    McInnes, L.A.7
  • 83
    • 0032519750 scopus 로고    scopus 로고
    • Molecular defects in the dysmyelinating mutant quaking
    • Hardy RJ. Molecular defects in the dysmyelinating mutant quaking. J Neurosci Res, 1998, 51: 417-422.
    • (1998) J Neurosci Res , vol.51 , pp. 417-422
    • Hardy, R.J.1
  • 84
    • 77953708144 scopus 로고    scopus 로고
    • High-affinity consensus binding of target RNAs by the STAR/GSG proteins GLD-1, STAR-2 and Quaking
    • Carmel AB, Wu J, Lehmann-Blount KA, Williamson JR. High-affinity consensus binding of target RNAs by the STAR/GSG proteins GLD-1, STAR-2 and Quaking. BMC Mol Biol, 2010, 11: 48.
    • (2010) BMC Mol Biol , vol.11 , pp. 48
    • Carmel, A.B.1    Wu, J.2    Lehmann-Blount, K.A.3    Williamson, J.R.4
  • 85
    • 0031858861 scopus 로고    scopus 로고
    • Structure-function analysis of Qk1: a lethal point mutation in mouse quaking prevents homodimerization
    • Chen T, Richard S. Structure-function analysis of Qk1: a lethal point mutation in mouse quaking prevents homodimerization. Mol Cell Biol, 1998, 18: 4863-4871.
    • (1998) Mol Cell Biol , vol.18 , pp. 4863-4871
    • Chen, T.1    Richard, S.2
  • 88
    • 0034235156 scopus 로고    scopus 로고
    • Destabilization and mislocalization of myelin basic protein mRNAs in quaking dysmyelination lacking the QKI RNA-binding proteins
    • Li Z, Zhang Y, Li D, Feng Y. Destabilization and mislocalization of myelin basic protein mRNAs in quaking dysmyelination lacking the QKI RNA-binding proteins. J Neurosci, 2000, 20: 4944-4953.
    • (2000) J Neurosci , vol.20 , pp. 4944-4953
    • Li, Z.1    Zhang, Y.2    Li, D.3    Feng, Y.4
  • 90
    • 0037007093 scopus 로고    scopus 로고
    • Function of quaking in myelination: regulation of alternative splicing
    • Wu JI, Reed RB, Grabowski PJ, Artzt K. Function of quaking in myelination: regulation of alternative splicing. Proc Natl Acad Sci USA, 2002, 99: 4233-4238.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 4233-4238
    • Wu, J.I.1    Reed, R.B.2    Grabowski, P.J.3    Artzt, K.4
  • 92
    • 84868100738 scopus 로고    scopus 로고
    • Quantitative mass spectrometry and PAR-CLIP to identify RNA-protein interactions
    • Scheibe M, Butter F, Hafner M, Tuschl T, Mann M. Quantitative mass spectrometry and PAR-CLIP to identify RNA-protein interactions. Nucleic Acids Res, 2012, 40: 9897-9902.
    • (2012) Nucleic Acids Res , vol.40 , pp. 9897-9902
    • Scheibe, M.1    Butter, F.2    Hafner, M.3    Tuschl, T.4    Mann, M.5
  • 93
    • 33645993912 scopus 로고    scopus 로고
    • The fragile X syndrome: exploring its molecular basis and seeking a treatment
    • Bardoni B, Davidovic L, Bensaid M, Khandjian EW. The fragile X syndrome: exploring its molecular basis and seeking a treatment. Expert Rev Mol Med, 2006, 8: 1-16.
    • (2006) Expert Rev Mol Med , vol.8 , pp. 1-16
    • Bardoni, B.1    Davidovic, L.2    Bensaid, M.3    Khandjian, E.W.4
  • 94
    • 84886953546 scopus 로고    scopus 로고
    • The translation of translational control by FMRP: therapeutic targets for FXS
    • Darnell JC, Klann E. The translation of translational control by FMRP: therapeutic targets for FXS. Nat Neurosci, 2013, 16: 1530-1536.
    • (2013) Nat Neurosci , vol.16 , pp. 1530-1536
    • Darnell, J.C.1    Klann, E.2
  • 96
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome
    • Verkerk AJ, Pieretti M, Sutcliffe JS, Fu YH, Kuhl DP, Pizzuti A, Reiner O, Richards S, Victoria MF, Zhang FP. Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome. Cell, 1991, 65: 905-914.
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.1    Pieretti, M.2    Sutcliffe, J.S.3    Fu, Y.H.4    Kuhl, D.P.5    Pizzuti, A.6    Reiner, O.7    Richards, S.8    Victoria, M.F.9    Zhang, F.P.10
  • 98
    • 0037084852 scopus 로고    scopus 로고
    • Premutation and intermediate-size FMR 1 alleles in 10572 males from the general population: loss of an AGG interruption is a late event in the generation of fragile X syndrome alleles
    • Dombrowski C, Levesque S, Morel ML, Rouillard P, Morgan K, Rousseau F. Premutation and intermediate-size FMR 1 alleles in 10572 males from the general population: loss of an AGG interruption is a late event in the generation of fragile X syndrome alleles. Hum Mol Genet, 2002, 11: 371-378.
    • (2002) Hum Mol Genet , vol.11 , pp. 371-378
    • Dombrowski, C.1    Levesque, S.2    Morel, M.L.3    Rouillard, P.4    Morgan, K.5    Rousseau, F.6
  • 99
    • 0036591683 scopus 로고    scopus 로고
    • The fragile X premutation: into the phenotypic fold
    • Hagerman RJ, Hagerman PJ. The fragile X premutation: into the phenotypic fold. Curr Opin Genet Dev, 2002, 12: 278-283.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 278-283
    • Hagerman, R.J.1    Hagerman, P.J.2
  • 100
    • 2342635196 scopus 로고    scopus 로고
    • The fragile-X premutation: a maturing perspective
    • Hagerman PJ, Hagerman RJ. The fragile-X premutation: a maturing perspective. Am J Hum Genet, 2004, 74: 805-816.
    • (2004) Am J Hum Genet , vol.74 , pp. 805-816
    • Hagerman, P.J.1    Hagerman, R.J.2
  • 102
    • 0141994818 scopus 로고    scopus 로고
    • A fragile balance: FMR1 expression levels
    • Oostra BA, Willemsen R. A fragile balance: FMR1 expression levels. Hum Mol Genet, 2003, 12: R249-257.
    • (2003) Hum Mol Genet , vol.12
    • Oostra, B.A.1    Willemsen, R.2
  • 103
    • 59649126241 scopus 로고    scopus 로고
    • The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits
    • Christie SB, Akins MR, Schwob JE, Fallon JR. The FXG: a presynaptic fragile X granule expressed in a subset of developing brain circuits. J Neurosci, 2009, 29: 1514-1524.
    • (2009) J Neurosci , vol.29 , pp. 1514-1524
    • Christie, S.B.1    Akins, M.R.2    Schwob, J.E.3    Fallon, J.R.4
  • 104
    • 77953267727 scopus 로고    scopus 로고
    • The developmental roles of FMRP
    • Till SM. The developmental roles of FMRP. Biochem Soc Trans, 2010, 38: 507-510.
    • (2010) Biochem Soc Trans , vol.38 , pp. 507-510
    • Till, S.M.1
  • 105
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell JC, Jensen KB, Jin P, Brown V, Warren ST, Darnell RB. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell, 2001, 107: 489-499.
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5    Darnell, R.B.6
  • 106
    • 77954657503 scopus 로고    scopus 로고
    • The role of G-quadruplex in RNA metabolism: involvement of FMRP and FMR2P
    • Melko M, Bardoni B. The role of G-quadruplex in RNA metabolism: involvement of FMRP and FMR2P. Biochimie, 2010, 92: 919-926.
    • (2010) Biochimie , vol.92 , pp. 919-926
    • Melko, M.1    Bardoni, B.2
  • 107
    • 47649101029 scopus 로고    scopus 로고
    • Hunting G-quadruplexes
    • Huppert JL. Hunting G-quadruplexes. Biochimie, 2008, 90: 1140-1148.
    • (2008) Biochimie , vol.90 , pp. 1140-1148
    • Huppert, J.L.1
  • 109
    • 53849110899 scopus 로고    scopus 로고
    • Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function
    • Bassell GJ, Warren ST. Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function. Neuron, 2008, 60: 201-214.
    • (2008) Neuron , vol.60 , pp. 201-214
    • Bassell, G.J.1    Warren, S.T.2
  • 112
    • 23944511133 scopus 로고    scopus 로고
    • Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons
    • Antar LN, Dictenberg JB, Plociniak M, Afroz R, Bassell GJ. Localization of FMRP-associated mRNA granules and requirement of microtubules for activity-dependent trafficking in hippocampal neurons. Genes Brain Behav, 2005, 4: 350-359.
    • (2005) Genes Brain Behav , vol.4 , pp. 350-359
    • Antar, L.N.1    Dictenberg, J.B.2    Plociniak, M.3    Afroz, R.4    Bassell, G.J.5
  • 116
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou SH, Wu F, Harrich D, García-Martínez LF, Gaynor RB. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol, 1995, 69: 3584-3596.
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3    García-Martínez, L.F.4    Gaynor, R.B.5
  • 124
    • 80052936462 scopus 로고    scopus 로고
    • Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments
    • Swarup V, Phaneuf D, Bareil C, Robertson J, Rouleau GA, Kriz J, Julien JP. Pathological hallmarks of amyotrophic lateral sclerosis/frontotemporal lobar degeneration in transgenic mice produced with TDP-43 genomic fragments. Brain, 2011, 134: 2610-2626.
    • (2011) Brain , vol.134 , pp. 2610-2626
    • Swarup, V.1    Phaneuf, D.2    Bareil, C.3    Robertson, J.4    Rouleau, G.A.5    Kriz, J.6    Julien, J.P.7
  • 126
    • 77956850818 scopus 로고    scopus 로고
    • TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
    • Mackenzie IR, Rademakers R, Neumann M. TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia. Lancet Neurol, 2010, 9: 995-1007.
    • (2010) Lancet Neurol , vol.9 , pp. 995-1007
    • Mackenzie, I.R.1    Rademakers, R.2    Neumann, M.3
  • 128
    • 64549100193 scopus 로고    scopus 로고
    • Structural insights into TDP-43 in nucleic-acid binding and domain interactions
    • Kuo PH, Doudeva LG, Wang YT, Shen CK, Yuan HS. Structural insights into TDP-43 in nucleic-acid binding and domain interactions. Nucleic Acids Res, 2009, 37: 1799-1808.
    • (2009) Nucleic Acids Res , vol.37 , pp. 1799-1808
    • Kuo, P.H.1    Doudeva, L.G.2    Wang, Y.T.3    Shen, C.K.4    Yuan, H.S.5
  • 131
    • 77953890823 scopus 로고    scopus 로고
    • TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
    • Lagier-Tourenne C, Polymenidou M, Cleveland DW. TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration. Hum Mol Genet, 2010, 19: R46-64.
    • (2010) Hum Mol Genet , vol.19
    • Lagier-Tourenne, C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 132
    • 57649174592 scopus 로고    scopus 로고
    • TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing
    • Bose JK, Wang IF, Hung L, Tarn WY, Shen CK. TDP-43 overexpression enhances exon 7 inclusion during the survival of motor neuron pre-mRNA splicing. J Biol Chem, 2008, 283: 28852-28859.
    • (2008) J Biol Chem , vol.283 , pp. 28852-28859
    • Bose, J.K.1    Wang, I.F.2    Hung, L.3    Tarn, W.Y.4    Shen, C.K.5
  • 133
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle FE. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem, 2001, 276: 36337-36343.
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 134
    • 27744554553 scopus 로고    scopus 로고
    • Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
    • Mercado PA, Ayala YM, Romano M, Buratti E, Baralle FE. Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene. Nucleic Acids Res, 2005, 33: 6000-6010.
    • (2005) Nucleic Acids Res , vol.33 , pp. 6000-6010
    • Mercado, P.A.1    Ayala, Y.M.2    Romano, M.3    Buratti, E.4    Baralle, F.E.5
  • 135
    • 77958604956 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA
    • Kim SH, Shanware NP, Bowler MJ, Tibbetts RS. Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. J Biol Chem, 2010, 285: 34097-34105.
    • (2010) J Biol Chem , vol.285 , pp. 34097-34105
    • Kim, S.H.1    Shanware, N.P.2    Bowler, M.J.3    Tibbetts, R.S.4
  • 136
    • 73949134014 scopus 로고    scopus 로고
    • Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS)
    • Volkening K, Leystra-Lantz C, Yang W, Jaffee H, Strong MJ. Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS). Brain Res, 2009, 1305: 168-182.
    • (2009) Brain Res , vol.1305 , pp. 168-182
    • Volkening, K.1    Leystra-Lantz, C.2    Yang, W.3    Jaffee, H.4    Strong, M.J.5
  • 138
    • 84860863883 scopus 로고    scopus 로고
    • TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells
    • Colombrita C, Onesto E, Megiorni F, Pizzuti A, Baralle FE, Buratti E, Silani V, Ratti A. TDP-43 and FUS RNA-binding proteins bind distinct sets of cytoplasmic messenger RNAs and differently regulate their post-transcriptional fate in motoneuron-like cells. J Biol Chem, 2012, 287: 15635-15647.
    • (2012) J Biol Chem , vol.287 , pp. 15635-15647
    • Colombrita, C.1    Onesto, E.2    Megiorni, F.3    Pizzuti, A.4    Baralle, F.E.5    Buratti, E.6    Silani, V.7    Ratti, A.8
  • 144
    • 77949878273 scopus 로고    scopus 로고
    • TDP-43 is a developmentally regulated protein essential for early embryonic development
    • Sephton CF, Good SK, Atkin S, Dewey CM, Mayer P 3rd, Herz J, Yu G. TDP-43 is a developmentally regulated protein essential for early embryonic development. J Biol Chem, 2010, 285: 6826-6834.
    • (2010) J Biol Chem , vol.285 , pp. 6826-6834
    • Sephton, C.F.1    Good, S.K.2    Atkin, S.3    Dewey, C.M.4    Mayer 3rd, P.5    Herz, J.6    Yu, G.7
  • 146
    • 84155167265 scopus 로고    scopus 로고
    • Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration
    • Lee EB, Lee VM, Trojanowski JQ. Gains or losses: molecular mechanisms of TDP43-mediated neurodegeneration. Nat Rev Neurosci, 2012, 13: 38-50.
    • (2012) Nat Rev Neurosci , vol.13 , pp. 38-50
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 147
    • 84884777626 scopus 로고    scopus 로고
    • Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders
    • Janssens J, van Broeckhoven C. Pathological mechanisms underlying TDP-43 driven neurodegeneration in FTLD-ALS spectrum disorders. Hum Mol Genet, 2013, 22: R77-87.
    • (2013) Hum Mol Genet , vol.22
    • Janssens, J.1    van Broeckhoven, C.2
  • 152
    • 30544448358 scopus 로고    scopus 로고
    • TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines
    • Fujii R, Takumi T. TLS facilitates transport of mRNA encoding an actin-stabilizing protein to dendritic spines. J Cell Sci, 2005, 118: 5755-5765.
    • (2005) J Cell Sci , vol.118 , pp. 5755-5765
    • Fujii, R.1    Takumi, T.2
  • 162
    • 0028961902 scopus 로고
    • Glutamate receptor RNA editing in vitro by enzymatic conversion of adenosine to inosine
    • Rueter SM, Burns CM, Coode SA, Mookherjee P, Emeson RB. Glutamate receptor RNA editing in vitro by enzymatic conversion of adenosine to inosine. Science, 1995, 267: 1491-1494.
    • (1995) Science , vol.267 , pp. 1491-1494
    • Rueter, S.M.1    Burns, C.M.2    Coode, S.A.3    Mookherjee, P.4    Emeson, R.B.5
  • 163
    • 0032077722 scopus 로고    scopus 로고
    • RNA editing of brain glutamate receptor channels: mechanism and physiology
    • Seeburg PH, Higuchi M, Sprengel R. RNA editing of brain glutamate receptor channels: mechanism and physiology. Brain Res Brain Res Rev, 1998, 26: 217-229.
    • (1998) Brain Res Brain Res Rev , vol.26 , pp. 217-229
    • Seeburg, P.H.1    Higuchi, M.2    Sprengel, R.3
  • 166
    • 79959345878 scopus 로고    scopus 로고
    • Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination
    • Skourti-Stathaki K, Proudfoot NJ, Gromak N. Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination. Mol Cell, 2011, 42: 794-805.
    • (2011) Mol Cell , vol.42 , pp. 794-805
    • Skourti-Stathaki, K.1    Proudfoot, N.J.2    Gromak, N.3
  • 167
    • 33747884761 scopus 로고    scopus 로고
    • Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes
    • Satterfield TF, Pallanck LJ. Ataxin-2 and its Drosophila homolog, ATX2, physically assemble with polyribosomes. Hum Mol Genet, 2006, 15: 2523-2532.
    • (2006) Hum Mol Genet , vol.15 , pp. 2523-2532
    • Satterfield, T.F.1    Pallanck, L.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.