메뉴 건너뛰기




Volumn 19, Issue 5, 2013, Pages 627-638

Quaking and PTB control overlapping splicing regulatory networks during muscle cell differentiation

Author keywords

Alternative splicing; Myogenesis; Splicing enhancer; Splicing silencer

Indexed keywords

POLYPYRIMIDINE TRACT BINDING PROTEIN;

EID: 84876512920     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.038422.113     Document Type: Article
Times cited : (131)

References (82)
  • 1
    • 0029949698 scopus 로고    scopus 로고
    • Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA
    • Arning S, Gruter P, Bilbe G, Kramer A. 1996. Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA. RNA 2:794-810. (Pubitemid 26374210)
    • (1996) RNA , vol.2 , Issue.8 , pp. 794-810
    • Arning, S.1    Gruter, P.2    Bilbe, G.3    Kramer, A.4
  • 2
    • 0030970264 scopus 로고    scopus 로고
    • Who encodes a KH RNA binding protein that functions in muscle development
    • Baehrecke EH. 1997. who encodes a KH RNA binding protein that functions in muscle development. Development 124: 1323-1332. (Pubitemid 27190105)
    • (1997) Development , vol.124 , Issue.7 , pp. 1323-1332
    • Baehrecke, E.H.1
  • 3
    • 84867573652 scopus 로고    scopus 로고
    • Structural analysis of the Quaking homodimerization interface
    • Beuck C, Qu S, Fagg WS, Ares M Jr, Williamson JR. 2012. Structural Analysis of the Quaking Homodimerization Interface. J Mol Biol 423: 766-781.
    • (2012) J Mol Biol , vol.423 , pp. 766-781
    • Beuck, C.1    Qu, S.2    Fagg, W.S.3    Ares Jr., M.4    Williamson, J.R.5
  • 4
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • DOI 10.1146/annurev.biochem.72.121801.161720
    • Black DL. 2003. Mechanisms of alternative pre-messenger RNA splicing. Annu Rev Biochem 72: 291-336. (Pubitemid 36930448)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 291-336
    • Black, D.L.1
  • 6
    • 33846135109 scopus 로고    scopus 로고
    • MicroRNAs regulate the expression of the alternative splicing factor nPTB during muscle development
    • DOI 10.1101/gad.1500707
    • Boutz PL, Chawla G, Stoilov P, Black DL. 2007a. MicroRNAs regulate the expression of the alternative splicing factor nPTB during muscle development. Genes Dev 21: 71-84. (Pubitemid 46089709)
    • (2007) Genes and Development , vol.21 , Issue.1 , pp. 71-84
    • Boutz, P.L.1    Chawla, G.2    Stoilov, P.3    Black, D.L.4
  • 7
    • 34347384211 scopus 로고    scopus 로고
    • A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons
    • DOI 10.1101/gad.1558107
    • Boutz PL, Stoilov P, Li Q, Lin CH, Chawla G, Ostrow K, Shiue L, Ares M Jr, Black DL. 2007b. A post-transcriptional regulatory switch in pol-ypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons. Genes Dev 21: 1636-1652. (Pubitemid 47026368)
    • (2007) Genes and Development , vol.21 , Issue.13 , pp. 1636-1652
    • Boutz, P.L.1    Stoilov, P.2    Li, Q.3    Lin, C.-H.4    Chawla, G.5    Ostrow, K.6    Shiue, L.7    Ares Jr., M.8    Black, D.L.9
  • 8
    • 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. 2010. High-affinity consensus binding of target RNAs by the STAR/GSG proteins GLD-1, STAR-2 and Quaking. BMC Mol Biol 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
  • 9
    • 0030872401 scopus 로고    scopus 로고
    • The polypyrimidine tract binding protein binds upstream of neural cell- specific c-src exert N1 to repress the splicing of the intron downstream
    • Chan RC, Black DL. 1997. The polypyrimidine tract binding protein binds upstream of neural cell-specific c-src exon N1 to repress the splicing of the intron downstream. Mol Cell Biol 17: 4667-4676. (Pubitemid 27318142)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.8 , pp. 4667-4676
    • Chan, R.C.1    Black, D.L.2
  • 11
    • 0036203307 scopus 로고    scopus 로고
    • Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing
    • DOI 10.1016/S1097-2765(02)00479-3
    • Charlet-B N, Logan P, Singh G, Cooper TA. 2002. Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing. Mol Cell 9: 649-658. (Pubitemid 34273794)
    • (2002) Molecular Cell , vol.9 , Issue.3 , pp. 649-658
    • Charlet-B, N.1    Logan, P.2    Singh, G.3    Cooper, T.A.4
  • 12
    • 0031858861 scopus 로고    scopus 로고
    • Structure-function analysis of Qk1: A lethal point mutation in mouse quaking prevents homodimerization
    • Chen T, Richard S. 1998. Structure-function analysis of Qk1: A lethal point mutation in mouse quaking prevents homodimerization. Mol Cell Biol 18: 4863-4871. (Pubitemid 28343070)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.8 , pp. 4863-4871
    • Chen, T.1    Richard, S.2
  • 14
    • 38849206330 scopus 로고    scopus 로고
    • New implications for the QUAKING RNA binding protein in human disease
    • DOI 10.1002/jnr.21485
    • Chénard CA, Richard S. 2008. New implications for the QUAKING RNA binding protein in human disease. J Neurosci Res 86: 233-242. (Pubitemid 351196729)
    • (2008) Journal of Neuroscience Research , vol.86 , Issue.2 , pp. 233-242
    • Chenard, C.A.1    Richard, S.2
  • 15
    • 79953157487 scopus 로고    scopus 로고
    • Analysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicing
    • Corioni M, Antih N, Tanackovic G, Zavolan M, Kramer A. 2011. Analysis of in situ pre-mRNA targets of human splicing factor SF1 reveals a function in alternative splicing. Nucleic Acids Res 39: 1868-1879.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1868-1879
    • Corioni, M.1    Antih, N.2    Tanackovic, G.3    Zavolan, M.4    Kramer, A.5
  • 16
    • 33845213293 scopus 로고    scopus 로고
    • Activation of α-tropomyosin exon 2 is regulated by the SR protein 9G8 and heterogeneous nuclear ribonucleoproteins H and F
    • DOI 10.1128/MCB.01677-06
    • Crawford JB, Patton JG. 2006. Activation of α-tropomyosin exon 2 is regulated by the SR protein 9G8 and heterogeneous nuclear ribonu-cleoproteins H and F. Mol Cell Biol 26: 8791-8802. (Pubitemid 44851939)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.23 , pp. 8791-8802
    • Crawford, J.B.1    Patton, J.G.2
  • 19
    • 0026039804 scopus 로고
    • Selection of splice sites in pre-mRNAs with short internal exons
    • Dominski Z, Kole R. 1991. Selection of splice sites in pre-mRNAs with short internal exons. Mol Cell Biol 11: 6075-6083. (Pubitemid 21895379)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.12 , pp. 6075-6083
    • Dominski, Z.1    Kole, R.2
  • 21
    • 0029944722 scopus 로고    scopus 로고
    • The quaking gene product necessary in embryogenesis and myelination combines features of RNA binding and signal transduction proteins
    • DOI 10.1038/ng0396-260
    • Ebersole TA, Chen Q, Justice MJ, Artzt K. 1996. The quaking gene product necessary in embryogenesis and myelination combines features of RNA binding and signal transduction proteins. Nat Genet 12: 260-265. (Pubitemid 26080084)
    • (1996) Nature Genetics , vol.12 , Issue.3 , pp. 260-265
    • Ebersole, T.A.1    Chen, Q.2    Justice, M.J.3    Artzt, K.4
  • 23
    • 24044513966 scopus 로고    scopus 로고
    • Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations
    • DOI 10.1038/nmeth785
    • Elias JE, Haas W, Faherty BK, Gygi SP. 2005. Comparative evaluation of mass spectrometry platforms used in large-scale proteomics investigations. Nat Methods 2: 667-675. (Pubitemid 41223093)
    • (2005) Nature Methods , vol.2 , Issue.9 , pp. 667-675
    • Elias, J.E.1    Haas, W.2    Faherty, B.K.3    Gygi, S.P.4
  • 24
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng J, McCormack AL, Yates JR. 1994. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. Am Soc Mass Spectrom 5: 976-989.
    • (1994) Am Soc Mass Spectrom , vol.5 , pp. 976-989
    • Eng, J.1    McCormack, A.L.2    Yates, J.R.3
  • 25
    • 0028796703 scopus 로고
    • Gld-1, a tumor suppressor gene required for oocyte development in Caenorhabditis elegans
    • Francis R, Barton MK, Kimble J, Schedl T. 1995. gld-1, a tumor suppressor gene required for oocyte development in Caenorhabditis elegans. Genetics 139: 579-606.
    • (1995) Genetics , vol.139 , pp. 579-606
    • Francis, R.1    Barton, M.K.2    Kimble, J.3    Schedl, T.4
  • 26
    • 0030822068 scopus 로고    scopus 로고
    • A Drosophila muscle-specific gene related to the mouse quaking locus
    • DOI 10.1016/S0378-1119(97)00278-3, PII S0378111997002783
    • Fyrberg C, Becker J, Barthmaier P, Mahaffey J, Fyrberg E. 1997. A Drosophila muscle-specific gene related to the mouse quaking locus. Gene 197: 315-323. (Pubitemid 27399907)
    • (1997) Gene , vol.197 , Issue.1-2 , pp. 315-323
    • Fyrberg, C.1    Becker, J.2    Barthmaier, P.3    Mahaffey, J.4    Fyrberg, E.5
  • 27
    • 26944489263 scopus 로고    scopus 로고
    • Target RNA motif and target mRNAs of the Quaking STAR protein
    • DOI 10.1038/nsmb963, PII NSMB963
    • Galarneau A, Richard S. 2005. Target RNA motif and target mRNAs of the Quaking STAR protein. Nat Struct Mol Biol 12: 691-698. (Pubitemid 43086275)
    • (2005) Nature Structural and Molecular Biology , vol.12 , Issue.8 , pp. 691-698
    • Galarneau, A.1    Richard, S.2
  • 28
    • 67949097422 scopus 로고    scopus 로고
    • CUGBP2 directly interacts with U2 17S snRNP components and promotes U2 snRNA binding to cardiac troponin T pre-mRNA
    • Goo Y-H, Cooper TA. 2009. CUGBP2 directly interacts with U2 17S snRNP components and promotes U2 snRNA binding to cardiac troponin T pre-mRNA. Nucleic Acids Res 37: 4275-4286.
    • (2009) Nucleic Acids Res , vol.37 , pp. 4275-4286
    • Goo, Y.-H.1    Cooper, T.A.2
  • 29
    • 0031985529 scopus 로고    scopus 로고
    • Role of an inhibitory pyrimidine element and polypyrimidine tract binding protein in repression of a regulated α-tropomyosin exon
    • Gooding C, Roberts GC, Smith CW. 1998. Role of an inhibitory pyrim-idine element and polypyrimidine tract binding protein in repression of a regulated α-tropomyosin exon. RNA 4: 85-100. (Pubitemid 28060287)
    • (1998) RNA , vol.4 , Issue.1 , pp. 85-100
    • Gooding, C.1    Roberts, G.C.2    Smith, C.W.J.3
  • 30
    • 0037377379 scopus 로고    scopus 로고
    • Antagonistic regulation of α-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein
    • DOI 10.1261/rna.2191903
    • Gromak N, Matlin AJ, Cooper TA, Smith CWJ. 2003. Antagonistic regulation of α-actinin alternative splicing by CELF proteins and poly-pyrimidine tract binding protein. RNA 9: 443-456. (Pubitemid 36356731)
    • (2003) RNA , vol.9 , Issue.4 , pp. 443-456
    • Gromak, N.1    Matlin, A.J.2    Cooper, T.A.3    Smith, C.W.J.4
  • 32
    • 0028308631 scopus 로고
    • Regulation of alternative pre-mRNA splicing by a novel repeated hexanucleotide element
    • Huh GS, Hynes RO. 1994. Regulation of alternative pre-mRNA splicing by a novel repeated hexanucleotide element. Genes Dev8: 1561-1574. (Pubitemid 24218290)
    • (1994) Genes and Development , vol.8 , Issue.13 , pp. 1561-1574
    • Huh, G.S.1    Hynes, R.O.2
  • 33
    • 84875857459 scopus 로고    scopus 로고
    • MiR-574-5p negatively regulates Qki6/7 to impact β-catenin/Wnt signalling and the development of colorectal cancer
    • doi: 10.1136/gutjnl-2011-301083
    • Ji S, Ye G, Zhang J, Wang L, Wang T, Wang Z, Zhang T, Wang G, Guo Z, Luo Y, et al. 2012. miR-574-5p negatively regulates Qki6/7 to impact β-catenin/Wnt signalling and the development of colorectal cancer. Gut doi: 10.1136/gutjnl-2011-301083.
    • (2012) Gut
    • Ji, S.1    Ye, G.2    Zhang, J.3    Wang, L.4    Wang, T.5    Wang, Z.6    Zhang, T.7    Wang, G.8    Guo, Z.9    Luo, Y.10
  • 34
    • 0037450704 scopus 로고    scopus 로고
    • A vertebrate RNA-binding protein Fox-1 regulates tissue-specific splicing via the pentanucleotide GCAUG
    • DOI 10.1093/emboj/cdg089
    • Jin Y, Suzuki H, Maegawa S, Endo H, Sugano S, Hashimoto K, Yasuda K, Inoue K. 2003. A vertebrate RNA-binding protein Fox-1 regulates tissue-specific splicing via the pentanucleotide GCAUG. EMBO J 22: 905-912. (Pubitemid 36227792)
    • (2003) EMBO Journal , vol.22 , Issue.4 , 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
  • 35
    • 80053027909 scopus 로고    scopus 로고
    • Functional consequences of developmen-tally regulated alternative splicing
    • Kalsotra A, Cooper TA. 2011. Functional consequences of developmen-tally regulated alternative splicing. Nat Rev Genet 12: 715-729.
    • (2011) Nat Rev Genet , vol.12 , pp. 715-729
    • Kalsotra, A.1    Cooper, T.A.2
  • 36
    • 0026668641 scopus 로고
    • Purification of splicing factor SF1, a heat-stable protein that functions in the assembly of a presplicing complex
    • Kramer A. 1992. Purification of splicing factor SF1, a heat-stable protein that functions in the assembly of a presplicing complex. Mol Cell Biol 12: 4545-4552.
    • (1992) Mol Cell Biol , vol.12 , pp. 4545-4552
    • Kramer, A.1
  • 37
    • 27744505660 scopus 로고    scopus 로고
    • STAR proteins quaking-6 and GLD-1 regulate translation of the homologues GLI1 and tra-1 through a conserved RNA 3′UTR-based mechanism
    • DOI 10.1016/j.ydbio.2005.08.038, PII S0012160605005658
    • Lakiza O, Frater L, Yoo Y, Villavicencio E, Walterhouse D, Goodwin EB, Iannaccone P. 2005. STAR proteins quaking-6 and GLD-1 regulate translation of the homologues GLI1 and tra-1 through a conserved RNA 3′UTR-based mechanism. Dev Biol 287: 98-110. (Pubitemid 41587481)
    • (2005) Developmental Biology , vol.287 , Issue.1 , pp. 98-110
    • Lakiza, O.1    Frater, L.2    Yoo, Y.3    Villavicencio, E.4    Walterhouse, D.5    Goodwin, E.B.6    Iannaccone, P.7
  • 38
    • 19344366251 scopus 로고    scopus 로고
    • Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells
    • DOI 10.1016/j.ceb.2005.03.002, PII S0955067405000426, Nucleus and Gene Expression
    • Lejeune F, Maquat LE. 2005. Mechanistic links between nonsense-mediated mRNA decay and pre-mRNA splicing in mammalian cells. Curr Opin Cell Biol 17: 309-315. (Pubitemid 40719922)
    • (2005) Current Opinion in Cell Biology , vol.17 , Issue.3 , pp. 309-315
    • Lejeune, F.1    Maquat, L.E.2
  • 40
    • 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. 2000. Destabilization and mislocalization of myelin basic protein mRNAs in quaking dysmyelination lacking the QKI RNA-binding proteins. J Neurosci 20: 4944-4953. (Pubitemid 30421698)
    • (2000) Journal of Neuroscience , vol.20 , Issue.13 , pp. 4944-4953
    • Li, Z.1    Zhang, Y.2    Li, D.3    Feng, Y.4
  • 41
    • 0031806710 scopus 로고    scopus 로고
    • Alternative splicing of the fibronectin EIIIB exon depends on specific TGCATG repeats
    • Lim LP, Sharp PA 1998. Alternative splicing of the fibronectin EIIIB exon depends on specific TGCATG repeats. Mol Cell Biol 18: 3900-3906. (Pubitemid 28287913)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.7 , pp. 3900-3906
    • Lim, L.P.1    Sharp, P.A.2
  • 44
    • 79955391375 scopus 로고    scopus 로고
    • Fine-tuning of Hh signaling by the RNA-binding protein Quaking to control muscle development
    • Lobbardi R, Lambert G, Zhao J, Geisler R, Kim HR, Rosa FM. 2011. Fine-tuning of Hh signaling by the RNA-binding protein Quaking to control muscle development. Development 138: 1783-1794.
    • (2011) Development , vol.138 , pp. 1783-1794
    • Lobbardi, R.1    Lambert, G.2    Zhao, J.3    Geisler, R.4    Kim, H.R.5    Rosa, F.M.6
  • 45
    • 0030061773 scopus 로고    scopus 로고
    • The human p62 cDNA encodes Sam68 and not the RasGAP-associated p62 protein
    • DOI 10.1016/S0092-8674(00)80989-7
    • Lock P, Fumagalli S, Polakis P, McCormick F, Courtneidge SA. 1996. The human p62 cDNA encodes Sam68 and not the RasGAP-associ-ated p62 protein. Cell 84: 23-24. (Pubitemid 26031457)
    • (1996) Cell , vol.84 , Issue.1 , pp. 23-24
    • Lock, P.1    Fumagalli, S.2    Polakis, P.3    McCormick, F.4    Courtneidge, S.A.5
  • 47
    • 0030832044 scopus 로고    scopus 로고
    • A complex intronic splicing enhancer from the c-src pre-mRNA activates inclusion of a heterologous exon
    • Modafferi EF, Black DL. 1997. A complex intronic splicing enhancer from the c-src pre-mRNA activates inclusion of a heterologous exon. Mol Cell Biol 17: 6537-6545. (Pubitemid 27451200)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.11 , pp. 6537-6545
    • Modafferi, E.F.1    Black, D.L.2
  • 48
    • 33947305594 scopus 로고    scopus 로고
    • Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay
    • DOI 10.1101/gad.1525507
    • Ni JZ, Grate L, Donohue JP, Preston C, Nobida N, O'Brien G, Shiue L, Clark TA, Blume JE, Ares M. 2007. Ultraconserved elements are associated with homeostatic control of splicing regulators by alternative splicing and nonsense-mediated decay. Genes Dev 21: 708-718. (Pubitemid 46440292)
    • (2007) Genes and Development , vol.21 , Issue.6 , pp. 708-718
    • Ni, J.Z.1    Grate, L.2    Donohue, J.P.3    Preston, C.4    Nobida, N.5    O'Brien, G.6    Shiue, L.7    Clark, T.A.8    Blume, J.E.9    Ares Jr., M.10
  • 49
    • 75849145292 scopus 로고    scopus 로고
    • Expansion of the eukaryotic proteome by alternative splicing
    • Nilsen TW, Graveley BR. 2010. Expansion of the eukaryotic proteome by alternative splicing. Nature 463: 457-463.
    • (2010) Nature , vol.463 , pp. 457-463
    • Nilsen, T.W.1    Graveley, B.R.2
  • 50
    • 38949110702 scopus 로고    scopus 로고
    • STAR family RNA-binding protein ASD-2 regulates developmental switching of mutually exclusive alternative splicing in vivo
    • DOI 10.1101/gad.1620608
    • Ohno G, Hagiwara M, Kuroyanagi H. 2008. STAR family RNA-binding protein ASD-2 regulates developmental switching of mutually exclusive alternative splicing in vivo. Genes Dev 22: 360-374. (Pubitemid 351214277)
    • (2008) Genes and Development , vol.22 , Issue.3 , pp. 360-374
    • Ohno, G.1    Hagiwara, M.2    Kuroyanagi, H.3
  • 51
    • 84859876858 scopus 로고    scopus 로고
    • The regulation of glial-specific splicing of Neurexin IV requires HOW and Cdk12 activity
    • Rodrigues F, Thuma L, Klambt C. 2012. The regulation of glial-specific splicing of Neurexin IV requires HOW and Cdk12 activity. Development 139: 1765-1776.
    • (2012) Development , vol.139 , pp. 1765-1776
    • Rodrigues, F.1    Thuma, L.2    Klambt, C.3
  • 52
    • 4344672685 scopus 로고    scopus 로고
    • Specificity of the STAR/GSG domain protein Qk1: Implications for the regulation of myelination
    • DOI 10.1261/rna.7780504
    • Ryder SP, Williamson JR. 2004. Specificity of the STAR/GSG domain protein Qk1: Implications for the regulation of myelination. RNA 10: 1449-1458. (Pubitemid 39122115)
    • (2004) RNA , vol.10 , Issue.9 , pp. 1449-1458
    • Ryder, S.P.1    Williamson, J.R.2
  • 55
    • 9444225935 scopus 로고    scopus 로고
    • Java Treeview - Extensible visualization of microarray data
    • DOI 10.1093/bioinformatics/bth349
    • Saldanha AJ. 2004. Java Treeview-extensible visualization of microar-ray data. Bioinformatics 20: 3246-3248. (Pubitemid 39619217)
    • (2004) Bioinformatics , vol.20 , Issue.17 , pp. 3246-3248
    • Saldanha, A.J.1
  • 56
    • 21044438900 scopus 로고    scopus 로고
    • Multiple roles of arginine/serine-rich splicing factors in RNA processing
    • DOI 10.1042/BST0330443
    • Sanford JR, Ellis J, Caceres JF. 2005. Multiple roles of arginine/serine-rich splicing factors in RNA processing. Biochem Soc Trans 33: 443-446. (Pubitemid 40873861)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.3 , pp. 443-446
    • Sanford, J.R.1    Ellis, J.2    Caceres, J.F.3
  • 57
    • 0027959864 scopus 로고
    • Differential localization and sequence analysis of capping protein [3-subunit iso-forms of vertebrates
    • Schafer DA, Korshunova YO, Schroer TA, Cooper JA. 1994. Differential localization and sequence analysis of capping protein [3-subunit iso-forms of vertebrates. J Cell Biol 127: 453-465.
    • (1994) J Cell Biol , vol.127 , pp. 453-465
    • Schafer, D.A.1    Korshunova, Y.O.2    Schroer, T.A.3    Cooper, J.A.4
  • 58
    • 38849187162 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome
    • DOI 10.1038/nsmb.1375, PII NSMB1375
    • Sharma S, Kohlstaedt LA, Damianov A, Rio DC, Black DL. 2008. Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome. Nat Struct Mol Biol 15: 183-191. (Pubitemid 351207512)
    • (2008) Nature Structural and Molecular Biology , vol.15 , Issue.2 , pp. 183-191
    • Sharma, S.1    Kohlstaedt, L.A.2    Damianov, A.3    Rio, D.C.4    Black, D.L.5
  • 59
    • 0000672995 scopus 로고
    • Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system
    • Sidman R, Dickie M, Appel S. 1964. Mutant mice (quaking and jimpy) with deficient myelination in the central nervous system. Science 144: 309-311.
    • (1964) Science , vol.144 , pp. 309-311
    • Sidman, R.1    Dickie, M.2    Appel, S.3
  • 60
    • 0032962639 scopus 로고    scopus 로고
    • Polypyrimidine tract binding protein functions as a repressor to regulate alternative splicing of a-actinin mutally exclusive exons
    • Southby J, Gooding C, Smith CWJ. 1999. Polypyrimidine tract binding protein functions as a repressor to regulate alternative splicing of a-actinin mutally exclusive exons. Mol Cell Biol 19: 2699-2711. (Pubitemid 29144514)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.4 , pp. 2699-2711
    • Southby, J.1    Gooding, C.2    Smith, C.W.J.3
  • 62
    • 0036393898 scopus 로고    scopus 로고
    • DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics
    • Tabb D, McDonald W, Yates JR. 2002. DTASelect and Contrast: Tools for assembling and comparing protein identifications from shotgun proteomics. J Proteome Res 1: 21-26.
    • (2002) J Proteome Res , vol.1 , pp. 21-26
    • Tabb, D.1    McDonald, W.2    Yates, J.R.3
  • 63
    • 0031431129 scopus 로고    scopus 로고
    • Cloning and expressionof the quaking gene in the zebrafish embryo
    • CH. 1997.
    • Tanaka H, Abe K, Kim CH. 1997. Cloning and expressionof the quaking gene in the zebrafish embryo. Mech Dev 69: 209-213.
    • Mech Dev , vol.69 , pp. 209-213
    • Tanaka, H.1    Kim, A.K.2
  • 64
    • 68849112458 scopus 로고    scopus 로고
    • Developmental control of CaV1.2 L-type calcium channel splicing by Fox proteins
    • Tang ZZ, Zheng S, Nikolic J, Black DL. 2009. Developmental control of CaV1.2 L-type calcium channel splicing by Fox proteins. Mol Cell Biol 29: 4757-4765.
    • (2009) Mol Cell Biol , vol.29 , pp. 4757-4765
    • Tang, Z.Z.1    Zheng, S.2    Nikolic, J.3    Black, D.L.4
  • 68
    • 0031451912 scopus 로고    scopus 로고
    • STAR, a gene family involved in signal transduction and activation of RNA
    • DOI 10.1016/S0168-9525(97)01269-9
    • Vernet C, Artzt K. 1997. STAR, a gene family involved in signal trans-duction and activation of RNA. Trends Genet 13: 479-484. (Pubitemid 28004921)
    • (1997) Trends in Genetics , vol.13 , Issue.12 , pp. 479-484
    • Vernet, C.1    Artzt, K.2
  • 69
    • 34347379534 scopus 로고    scopus 로고
    • A comprehensive computational characterization of conserved mammalian intronic sequences reveals conserved motifs associated with constitutive and alternative splicing
    • DOI 10.1101/gr.6017807
    • Voelker RB, Berglund JA. 2007. A comprehensive computational characterization of conserved mammalian intronic sequences reveals conserved motifs associated with constitutive and alternative splicing. Genome Res 17: 1023-1033. (Pubitemid 47026349)
    • (2007) Genome Research , vol.17 , Issue.7 , pp. 1023-1033
    • Voelker, R.B.1    Berglund, J.A.2
  • 71
    • 67249165478 scopus 로고    scopus 로고
    • The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing
    • Warf MB, Diegel JV, von Hippel PH, Berglund JA. 2009. The protein factors MBNL1 and U2AF65 bind alternative RNA structures to regulate splicing. Proc Natl Acad Sci 106: 9203-9208.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 9203-9208
    • Warf, M.B.1    Diegel, J.V.2    Von Hippel, P.H.3    Berglund, J.A.4
  • 72
    • 0035106351 scopus 로고    scopus 로고
    • Large-scale analysis of the yeast proteome by multidimensional protein identification technology
    • DOI 10.1038/85686
    • Washburn MP, Wolters D, Yates JR. 2001. Large-scale analysis of the yeast proteome by multidimensional protein identification technology. Nat Biotechnol 19: 242-247. (Pubitemid 32220565)
    • (2001) Nature Biotechnology , vol.19 , Issue.3 , pp. 242-247
    • Washburn, M.P.1    Wolters, D.2    Yates, J.R.3
  • 73
    • 0032856992 scopus 로고    scopus 로고
    • The quaking I-5 protein (QKI-5) has a novel nuclear localization signal and shuttles between the nucleus and the cytoplasm
    • Wu J, Zhou L, Tonissen K, Tee R, Artzt K. 1999. The quaking I-5 protein (QKI-5) has a novel nuclear localization signal and shuttles between the nucleus and the cytoplasm. J Biol Chem 274: 29202-29210.
    • (1999) J Biol Chem , vol.274 , pp. 29202-29210
    • Wu, J.1    Zhou, L.2    Tonissen, K.3    Tee, R.4    Artzt, K.5
  • 74
    • 72149117411 scopus 로고    scopus 로고
    • Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping
    • Xue Y, Zhou Y, Wu T, Zhu T, Ji X, Kwon YS, Zhang C, Yeo G, Black DL, Sun H, et al. 2009. Genome-wide analysis of PTB-RNA interactions reveals a strategy used by the general splicing repressor to modulate exon inclusion or skipping. Mol Cell 36: 996-1006.
    • (2009) Mol Cell , vol.36 , pp. 996-1006
    • Xue, Y.1    Zhou, Y.2    Wu, T.3    Zhu, T.4    Ji, X.5    Kwon, Y.S.6    Zhang, C.7    Yeo, G.8    Black, D.L.9    Sun, H.10
  • 75
    • 67651173106 scopus 로고    scopus 로고
    • Proteomics by mass spectrom-etry: Approaches, advances, and applications
    • Yates J, Ruse CI, Nakorchevsky A. 2009. Proteomics by mass spectrom-etry: Approaches, advances, and applications. Annu Rev Biomed Eng 11: 49-79.
    • (2009) Annu Rev Biomed Eng , vol.11 , pp. 49-79
    • Yates, J.1    Ruse, C.I.2    Nakorchevsky, A.3
  • 76
    • 34249696543 scopus 로고    scopus 로고
    • Discovery and analysis of evolutionarily conserved intronic splicing regulatory elements
    • Yeo GW, Nostrand ELV, Liang TY. 2007. Discovery and analysis of evolutionarily conserved intronic splicing regulatory elements. PLoS Genet 3: e85.
    • (2007) PLoS Genet , vol.3
    • Yeo, G.W.1    Nostrand, E.L.V.2    Liang, T.Y.3
  • 77
    • 59649107040 scopus 로고    scopus 로고
    • AnRNA code for the FOX2 splicing regulator revealed by mapping RNA-pro-tein interactions in stem cells
    • Yeo GW, Coufal NG, Liang TY, Peng GE, Fu XD, Gage FH. 2009. AnRNA code for the FOX2 splicing regulator revealed by mapping RNA-pro-tein interactions in stem cells. Nat Struct Mol Biol 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
    • 0030959948 scopus 로고    scopus 로고
    • The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity
    • Zaffran S, Astier M, Gratecos D, Semeriva M. 1997. The held out wings (how) Drosophila gene encodes a putative RNA-binding protein involved in the control of muscular and cardiac activity. Development 124: 2087-2098. (Pubitemid 27270276)
    • (1997) Development , vol.124 , Issue.10 , pp. 2087-2098
    • Zaffran, S.1    Astier, M.2    Gratecos, D.3    Semeriva, M.4
  • 80
    • 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. 2008. Defining the regulatory network of the tissue-specific splicing factors Fox-1 and Fox-2. Genes Dev 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
  • 81
    • 78650495026 scopus 로고    scopus 로고
    • Quaking i controls a unique cytoplasmic pathway that regulates alternative splicing of myelin-as-sociated glycoprotein
    • Zhao L, Mandler MD, Yi H, Feng Y. 2010. Quaking I controls a unique cytoplasmic pathway that regulates alternative splicing of myelin-as-sociated glycoprotein. Proc Natl Acad Sci 107: 19061-19066.
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 19061-19066
    • Zhao, L.1    Mandler, M.D.2    Yi, H.3    Feng, Y.4
  • 82
    • 0030961189 scopus 로고    scopus 로고
    • The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos
    • Zorn AM, Krieg PA. 1997. The KH domain protein encoded by quaking functions as a dimer and is essential for notochord development in Xenopus embryos. Genes Dev 11: 2176-2190. (Pubitemid 27387969)
    • (1997) Genes and Development , vol.11 , Issue.17 , pp. 2176-2190
    • Zorn, A.M.1    Krieg, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.