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Volumn 5, Issue 2, 2004, Pages 89-99

Nonsense-mediated mRNA decay: Splicing, translation and mRNP dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CYTIDINE DEAMINASE; MESSENGER RNA; MESSENGER RNA PRECURSOR; RIBONUCLEOPROTEIN; RNA BINDING PROTEIN; SELENOPROTEIN;

EID: 0742323558     PISSN: 14710072     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrm1310     Document Type: Review
Times cited : (991)

References (162)
  • 1
    • 0035951432 scopus 로고    scopus 로고
    • Quality control of mRNA function
    • Maquat, L. E. & Carmichael, G. G. Quality control of mRNA function. Cell 104, 173-176 (2001).
    • (2001) Cell , vol.104 , pp. 173-176
    • Maquat, L.E.1    Carmichael, G.G.2
  • 2
    • 0029330286 scopus 로고
    • When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells
    • Maquat, L. E. When cells stop making sense: effects of nonsense codons on RNA metabolism in vertebrate cells. RNA 1, 453-466 (1995).
    • (1995) RNA , vol.1 , pp. 453-466
    • Maquat, L.E.1
  • 3
    • 0002650836 scopus 로고    scopus 로고
    • (eds. Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) (Cold Spring Harbor Press, New York)
    • Maquat, L. E. in Translational Control of Gene Expression (eds. Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) 849-868 (Cold Spring Harbor Press, New York, 2000).
    • (2000) Translational Control of Gene Expression , pp. 849-868
    • Maquat, L.E.1
  • 4
    • 0037708992 scopus 로고    scopus 로고
    • Post-transcriptional control of gene expression: Effectors of mRNA decay
    • Arraiano, C. M. & Maquat, L. E. Post-transcriptional control of gene expression: effectors of mRNA decay. Mol. Microbiol. 49, 267-276 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 267-276
    • Arraiano, C.M.1    Maquat, L.E.2
  • 5
    • 0001211084 scopus 로고    scopus 로고
    • (eds. Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) (Cold Spring Harbor Press, New York)
    • Peltz, S. W. & Jacobson, A. in Translational Control of Gene Expression (eds. Sonenberg, N., Hershey, J. W. B. & Mathews, M. B.) 827-847 (Cold Spring Harbor Press, New York, 2000).
    • (2000) Translational Control of Gene Expression , pp. 827-847
    • Peltz, S.W.1    Jacobson, A.2
  • 6
    • 0032006979 scopus 로고    scopus 로고
    • Nonsense surveillance in lymphocytes?
    • Li, S. & Wilkinson, M. F. Nonsense surveillance in lymphocytes? Immunity 8, 135-141 (1998).
    • (1998) Immunity , vol.8 , pp. 135-141
    • Li, S.1    Wilkinson, M.F.2
  • 7
    • 0032837376 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in health and disease
    • Frischmeyer, P. A. & Dietz, H. C. Nonsense-mediated mRNA decay in health and disease. Hum. Mol. Genet. 8, 1893-1900 (1999).
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1893-1900
    • Frischmeyer, P.A.1    Dietz, H.C.2
  • 8
    • 0033525169 scopus 로고    scopus 로고
    • A perfect message: RNA surveillance and nonsense-mediated decay
    • Hentze, M. W. & Kulozik, A. E. A perfect message: RNA surveillance and nonsense-mediated decay. Cell 96, 307-310 (1999).
    • (1999) Cell , vol.96 , pp. 307-310
    • Hentze, M.W.1    Kulozik, A.E.2
  • 9
    • 0033375911 scopus 로고    scopus 로고
    • Mechanisms of mRNA surveillance in eukaryotes
    • Hilleren, P. & Parker, R. Mechanisms of mRNA surveillance in eukaryotes. Annu. Rev. Genet. 33, 229-260 (1999).
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 229-260
    • Hilleren, P.1    Parker, R.2
  • 10
    • 0036677083 scopus 로고    scopus 로고
    • mRNA surveillance: The perfect persist
    • Wagner, E. & Lykke-Andersen, J. mRNA surveillance: the perfect persist. J. Cell. Sci. 115, 3033-3038 (2002).
    • (2002) J. Cell. Sci. , vol.115 , pp. 3033-3038
    • Wagner, E.1    Lykke-Andersen, J.2
  • 11
    • 0037382643 scopus 로고    scopus 로고
    • Looking at mRNA decay pathways through the window of molecular evolution
    • Culbertson, M. R. & Leeds, P. F. Looking at mRNA decay pathways through the window of molecular evolution. Curr. Opin. Genet. Dev 13, 207-214 (2003).
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 207-214
    • Culbertson, M.R.1    Leeds, P.F.2
  • 12
    • 0019733025 scopus 로고
    • Unstable β-globin mRNA in mRNA-defident β°-thalassemia
    • Maquat, L. E., Kinniburgh, A. J., Rachmilewitz, E. A. & Ross, J. Unstable β-globin mRNA in mRNA-defident β°-thalassemia. Cell 27, 543-553 (1981).
    • (1981) Cell , vol.27 , pp. 543-553
    • Maquat, L.E.1    Kinniburgh, A.J.2    Rachmilewitz, E.A.3    Ross, J.4
  • 14
    • 0035036534 scopus 로고    scopus 로고
    • Gene structure prediction and alternative splicing analysis using genomically aligned ESTs
    • Kan, Z., Rouchka, E. C., Gish, W. R. & States, D. J. Gene structure prediction and alternative splicing analysis using genomically aligned ESTs. Genome Res. 11, 889-900 (2001).
    • (2001) Genome Res. , vol.11 , pp. 889-900
    • Kan, Z.1    Rouchka, E.C.2    Gish, W.R.3    States, D.J.4
  • 15
    • 0030931561 scopus 로고    scopus 로고
    • smg mutants affect the expression of alternatively spliced SR protein mRNAs in Caenorhabditis elegans
    • Morrison, M., Harris, K. S. & Roth, M. B. smg mutants affect the expression of alternatively spliced SR protein mRNAs in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 94, 9782-9785 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9782-9785
    • Morrison, M.1    Harris, K.S.2    Roth, M.B.3
  • 16
    • 0031896755 scopus 로고    scopus 로고
    • Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likely to be nonsense codon-mediated decay of cytoplasmic mRNA
    • Moriarty, P. M., Reddy, C. C. & Maquat, L. E. Selenium deficiency reduces the abundance of mRNA for Se-dependent glutathione peroxidase 1 by a UGA-dependent mechanism likely to be nonsense codon-mediated decay of cytoplasmic mRNA. Mol. Cell. Biol. 18, 2932-2939 (1998). Describes a natural target for cytoplasmic NMD.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2932-2939
    • Moriarty, P.M.1    Reddy, C.C.2    Maquat, L.E.3
  • 17
    • 0035164664 scopus 로고    scopus 로고
    • Nonsense-mediated decay of mRNA for the selenoprotein phospholipid hydroperoxide glutathione peroxidase is detectable in cultured cells but masked or inhibited in rat tissues
    • Sun, X. et al. Nonsense-mediated decay of mRNA for the selenoprotein phospholipid hydroperoxide glutathione peroxidase is detectable in cultured cells but masked or inhibited in rat tissues. Mol. Biol. Cell 12, 1009-1017 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1009-1017
    • Sun, X.1
  • 18
    • 0037422575 scopus 로고    scopus 로고
    • Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans
    • Lewis, B. P., Green, R. E. & Brenner, S. E. Evidence for the widespread coupling of alternative splicing and nonsense-mediated mRNA decay in humans. Proc. Natl Acad. Sci. USA 100, 189-192 (2003). Provides evidence for widespread use of NMD as a means of regulating gene expression.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 189-192
    • Lewis, B.P.1    Green, R.E.2    Brenner, S.E.3
  • 19
    • 0035862813 scopus 로고    scopus 로고
    • Rent1, a trans-effector of nonsense-mediated mRNA decay, is essential for mammalian embryonic viability
    • Medghalchi, S. M. et al. Rent1, a trans-effector of nonsense-mediated mRNA decay, is essential for mammalian embryonic viability. Hum. Mol. Genet. 10, 99-105 (2001).
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 99-105
    • Medghalchi, S.M.1
  • 20
    • 0027410487 scopus 로고
    • T cell receptor-β mRNA splicing: Regulation of unusual splicing intermediates
    • Qian, L. et al. T cell receptor-β mRNA splicing: regulation of unusual splicing intermediates. Mol. Cell. Biol. 13, 1686-1696 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1686-1696
    • Qian, L.1
  • 21
    • 0028540401 scopus 로고
    • Evidence for degradation of mRNA encoding α-L-iduronidase in Hurler fibroblasts with premature termination alleles
    • Menon, K. P. & Neufeld, E. F. Evidence for degradation of mRNA encoding α-L-iduronidase in Hurler fibroblasts with premature termination alleles. Cell. Mol. Biol. 40, 999-1005 (1994).
    • (1994) Cell. Mol. Biol. , vol.40 , pp. 999-1005
    • Menon, K.P.1    Neufeld, E.F.2
  • 22
    • 0028884942 scopus 로고
    • A regulatory mechanism that detects premature nonsense codons in T-cell receptor transcripts in vivo is reversed by protein synthesis inhibitors in vitro
    • Carter, M. S. et al. A regulatory mechanism that detects premature nonsense codons in T-cell receptor transcripts in vivo is reversed by protein synthesis inhibitors in vitro. J. Biol. Chem. 270, 28995-29003 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 28995-29003
    • Carter, M.S.1
  • 23
    • 0032530480 scopus 로고    scopus 로고
    • Proteolysis of human eukaryotic translation initiation factor elF4GII, but not elF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection
    • Gradi, A., Svitkin, Y. V. Imataka, H. & Sonenberg, N. Proteolysis of human eukaryotic translation initiation factor elF4GII, but not elF4GI, coincides with the shutoff of host protein synthesis after poliovirus infection. Proc. Natl Acad. Sci. USA 95, 11089-11094 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11089-11094
    • Gradi, A.1    Svitkin, Y.V.2    Imataka, H.3    Sonenberg, N.4
  • 24
    • 0036171240 scopus 로고    scopus 로고
    • Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease
    • Kuyumcu-Martinez, N. M., Joachims, M. & Lloyd, R. E. Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease. J. Virol. 76, 2062-2074 (2002).
    • (2002) J. Virol. , vol.76 , pp. 2062-2074
    • Kuyumcu-Martinez, N.M.1    Joachims, M.2    Lloyd, R.E.3
  • 25
    • 0027388887 scopus 로고
    • Evidence to implicate translation by ribosomes in the mechanism by which nonsense codons reduce the nuclear level of human triosephosphate isomerase mRNA
    • Belgrader, P., Cheng, J. & Maquat, L. E. Evidence to implicate translation by ribosomes in the mechanism by which nonsense codons reduce the nuclear level of human triosephosphate isomerase mRNA. Proc. Natl Acad. Sci. USA 90, 482-486 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 482-486
    • Belgrader, P.1    Cheng, J.2    Maquat, L.E.3
  • 26
    • 0032526946 scopus 로고    scopus 로고
    • Binary specification of nonsense codons by splicing and cytoplasmic translation
    • Thermann, R. et al. Binary specification of nonsense codons by splicing and cytoplasmic translation. EMBO J. 17, 3484-3494 (1998).
    • (1998) EMBO J. , vol.17 , pp. 3484-3494
    • Thermann, R.1
  • 27
    • 0031004756 scopus 로고    scopus 로고
    • T cell receptor (TCR) mini-gene mRNA expression regulated by nonsense codons: A nuclear-associated translation-like mechanism
    • Li, S., Leonard, D. & Wilkinson, M. F. T cell receptor (TCR) mini-gene mRNA expression regulated by nonsense codons: a nuclear-associated translation-like mechanism. J. Exp. Med. 185, 985-992 (1997).
    • (1997) J. Exp. Med. , vol.185 , pp. 985-992
    • Li, S.1    Leonard, D.2    Wilkinson, M.F.3
  • 28
    • 0031046735 scopus 로고    scopus 로고
    • Evidence that translation reinitiation abrogates nonsense-mediated mRNA decay in mammalian cells
    • Zhang, J. & Maquat, L. E. Evidence that translation reinitiation abrogates nonsense-mediated mRNA decay in mammalian cells. EMBO J. 16, 826-833 (1997).
    • (1997) EMBO J. , vol.16 , pp. 826-833
    • Zhang, J.1    Maquat, L.E.2
  • 29
    • 0027993583 scopus 로고
    • Introns are cis effectors of the nonsense-codon-mediated reduction in nuclear mRNA abundance
    • Cheng, J., Belgreder, P., Zhou, X. & Maquat, L. E. Introns are cis effectors of the nonsense-codon-mediated reduction in nuclear mRNA abundance. Mol. Cell. Biol. 14, 6317-6325 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6317-6325
    • Cheng, J.1    Belgreder, P.2    Zhou, X.3    Maquat, L.E.4
  • 30
    • 0029908912 scopus 로고    scopus 로고
    • A splicing-dependent regulatory mechanism that detects translation signals
    • Carter, M. S., Li, S. & Wilkinson, M. F. A splicing-dependent regulatory mechanism that detects translation signals. EMBO J. 15, 5965-5975 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5965-5975
    • Carter, M.S.1    Li, S.2    Wilkinson, M.F.3
  • 31
    • 0031840487 scopus 로고    scopus 로고
    • At least one intron is required for the nonsense-mediated decay of triosephosphate isomerase mRNA: A possible link between nuclear splicing and cytoplasmic translation
    • Zhang, J., Sun, X., Qian, Y., LaDuca, J. P. & Maquat, L. E. At least one intron is required for the nonsense-mediated decay of triosephosphate isomerase mRNA: a possible link between nuclear splicing and cytoplasmic translation. Mol. Cell. Biol. 18, 5272-5283 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5272-5283
    • Zhang, J.1    Sun, X.2    Qian, Y.3    LaDuca, J.P.4    Maquat, L.E.5
  • 32
    • 0031870169 scopus 로고    scopus 로고
    • Intron function in the nonsense-mediated decay of β-globin mRNA: Indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm
    • Zhang, J., Sun, X., Qian, Y. & Maquat, L. E. Intron function in the nonsense-mediated decay of β-globin mRNA: indications that pre-mRNA splicing in the nucleus can influence mRNA translation in the cytoplasm. RNA 4, 801-815 (1998).
    • (1998) RNA , vol.4 , pp. 801-815
    • Zhang, J.1    Sun, X.2    Qian, Y.3    Maquat, L.E.4
  • 33
    • 0034282528 scopus 로고    scopus 로고
    • Nonsense-mediated decay of glutathione peroxidase 1 mRNA in the cytoplasm depends on intron position
    • Sun, X., Monarty, P. M. & Maquat, L. E. Nonsense-mediated decay of glutathione peroxidase 1 mRNA in the cytoplasm depends on intron position. EMBO J. 19, 4734-4744 (2000).
    • (2000) EMBO J. , vol.19 , pp. 4734-4744
    • Sun, X.1    Monarty, P.M.2    Maquat, L.E.3
  • 34
    • 0027536976 scopus 로고
    • Nonsense codons can reduce the abundance of nuclear mRNA without affecting the abundance of pre-mRNA or the half-life of cytoplasmic mRNA
    • Cheng, J. & Maquat, L. E. Nonsense codons can reduce the abundance of nuclear mRNA without affecting the abundance of pre-mRNA or the half-life of cytoplasmic mRNA. Mol. Cell. Biol, 13, 1892-1902 (1993).
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1892-1902
    • Cheng, J.1    Maquat, L.E.2
  • 35
    • 0028125262 scopus 로고
    • Mammalian nonsense codons can be cis effectors of nuclear mRNA half-life
    • Belgrader, P., Cheng, J., Zhou, X., Stephenson, L. S. & Maquat, L. E. Mammalian nonsense codons can be cis effectors of nuclear mRNA half-life. Mol. Cell. Biol. 14, 8219-8228(1994). Shows that nucleus-associated NMD targets newly synthesized mRNA.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8219-8228
    • Belgrader, P.1    Cheng, J.2    Zhou, X.3    Stephenson, L.S.4    Maquat, L.E.5
  • 36
    • 0036645697 scopus 로고    scopus 로고
    • The exon junction complex is detected on CBP80-bound but not elF4E-bound mRNA in mammalian cells: Dynamics of mRNP remodeling
    • Lejeune, F., Ishigaki, Y., Li, X. & Maquat, L. E. The exon junction complex is detected on CBP80-bound but not elF4E-bound mRNA in mammalian cells: dynamics of mRNP remodeling. EMBO J. 21, 3536-3545 (2002). Characterizes the exon junction complex that is formed in vivo.
    • (2002) EMBO J. , vol.21 , pp. 3536-3545
    • Lejeune, F.1    Ishigaki, Y.2    Li, X.3    Maquat, L.E.4
  • 37
    • 0032104190 scopus 로고    scopus 로고
    • A rule for termination-codon position within intron-containing genes: When nonsense affects RNA abundance
    • Nagy, E. & Maquat, L. E. A rule for termination-codon position within intron-containing genes: when nonsense affects RNA abundance. Trends Biochem. Sci. 23, 198-199 (1998). Establishes a rule for which PTCs elicit NMD.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 198-199
    • Nagy, E.1    Maquat, L.E.2
  • 38
    • 0035028094 scopus 로고    scopus 로고
    • Mammalian heat shock p70 and histone H4 transcripts, which derive from naturally intronless genes, are immune to nonsense-mediated decay
    • Maquat, L. E. & Li, X. Mammalian heat shock p70 and histone H4 transcripts, which derive from naturally intronless genes, are immune to nonsense-mediated decay. RNA 7, 445-456 (2001).
    • (2001) RNA , vol.7 , pp. 445-456
    • Maquat, L.E.1    Li, X.2
  • 40
    • 0036205348 scopus 로고    scopus 로고
    • Boundary-independent polar nonsense-mediated decay
    • Wang, J., Gudikote, J. P., Olivas, O. R. & Wilkinson, M. F. Boundary-independent polar nonsense-mediated decay. EMBO Rep. 3, 274-279 (2002). Illustrates an example of an mRNA that breaks the 50-55-nt rule.
    • (2002) EMBO Rep. , vol.3 , pp. 274-279
    • Wang, J.1    Gudikote, J.P.2    Olivas, O.R.3    Wilkinson, M.F.4
  • 41
    • 0038402506 scopus 로고    scopus 로고
    • Computational modeling and experimental analysis of nonsense-mediated decay in yeast
    • Cao, D. & Parker, R. Computational modeling and experimental analysis of nonsense-mediated decay in yeast. Cell 113, 533-545 (2003).
    • (2003) Cell , vol.113 , pp. 533-545
    • Cao, D.1    Parker, R.2
  • 42
    • 0034667531 scopus 로고    scopus 로고
    • Nonsense mutations in the human β-globin gene lead to unexpected levels of cytoplasmic mRNA accumulation
    • Romao, L. et al. Nonsense mutations in the human β-globin gene lead to unexpected levels of cytoplasmic mRNA accumulation. Blood 96, 2895-2901 (2000).
    • (2000) Blood , vol.96 , pp. 2895-2901
    • Romao, L.1
  • 43
    • 0034705289 scopus 로고    scopus 로고
    • The RNA binding protein Publ modulates the stability of transcripts containing upstream open reading frames
    • Ruiz-Echevarria, M. J. & Peltz, S. W. The RNA binding protein Publ modulates the stability of transcripts containing upstream open reading frames. Cell 101, 741-751 (2000).
    • (2000) Cell , vol.101 , pp. 741-751
    • Ruiz-Echevarria, M.J.1    Peltz, S.W.2
  • 44
    • 0036493774 scopus 로고    scopus 로고
    • Abnormally spliced β-globin mRNAs: A single point mutation generates transcripts sensitive and insensitive to nonsense-mediated mRNA decay
    • Danckwardt, S. et al. Abnormally spliced β-globin mRNAs: a single point mutation generates transcripts sensitive and insensitive to nonsense-mediated mRNA decay. Blood 99, 1811-1816 (2002).
    • (2002) Blood , vol.99 , pp. 1811-1816
    • Danckwardt, S.1
  • 45
    • 0035254681 scopus 로고    scopus 로고
    • Splicing and 3′ end formation in the definition of nonsense-mediated decay-competent human β-globin mRNPs
    • Neu-Yilik, G. et al. Splicing and 3′ end formation in the definition of nonsense-mediated decay-competent human β-globin mRNPs. EMBO J. 20, 532-540 (2001).
    • (2001) EMBO J. , vol.20 , pp. 532-540
    • Neu-Yilik, G.1
  • 46
    • 0041524056 scopus 로고    scopus 로고
    • The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay
    • Chester, A. et al. The apolipoprotein B mRNA editing complex performs a multifunctional cycle and suppresses nonsense-mediated decay. EMBO J. 22, 3971-3982 (2003). Describes the mechanism by which edited apoB mRNA is immune to NMD.
    • (2003) EMBO J. , vol.22 , pp. 3971-3982
    • Chester, A.1
  • 47
    • 0027478167 scopus 로고
    • Targeted modification of the apolipoprotein B gene results in hypobetalipoproteinemia and developmental abnormalities in mice
    • Homanics, G. E. et al. Targeted modification of the apolipoprotein B gene results in hypobetalipoproteinemia and developmental abnormalities in mice. Proc. Natl Acad. Sci. USA 90, 2389-2393 (1993).
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2389-2393
    • Homanics, G.E.1
  • 48
    • 0032545280 scopus 로고    scopus 로고
    • A gene-targeted mouse model for familial hypobetalipoproteinemia. Low levels of apolipoprotein B mRNA in association with a nonsense mutation in exon 26 of the apolipoprotein B gene
    • Kim, E., Ambroziak, P., Veniant, M. M., Hamilton, R. L. & Young, S. G. A gene-targeted mouse model for familial hypobetalipoproteinemia. Low levels of apolipoprotein B mRNA in association with a nonsense mutation in exon 26 of the apolipoprotein B gene. J. Biol. Chem. 273, 33977-33984 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 33977-33984
    • Kim, E.1    Ambroziak, P.2    Veniant, M.M.3    Hamilton, R.L.4    Young, S.G.5
  • 49
    • 0034672093 scopus 로고    scopus 로고
    • The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions
    • Le Hir, H., Izaurralde, E., Maquat, L. E. & Moore, M. J. The spliceosome deposits multiple proteins 20-24 nucleotides upstream of mRNA exon-exon junctions. EMBO J. 19, 6860-6869 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6860-6869
    • Le Hir, H.1    Izaurralde, E.2    Maquat, L.E.3    Moore, M.J.4
  • 51
    • 0033575702 scopus 로고    scopus 로고
    • Purification and characterization of human RNPS1: A general activator of pre-mRNA splicing
    • Mayeda, A. et al. Purification and characterization of human RNPS1: a general activator of pre-mRNA splicing. EMBO J. 10, 4560-4570 (1999).
    • (1999) EMBO J. , vol.10 , pp. 4560-4570
    • Mayeda, A.1
  • 52
    • 0033634824 scopus 로고    scopus 로고
    • Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm
    • Kataoka, N. et al. Pre-mRNA splicing imprints mRNA in the nucleus with a novel RNA-binding protein that persists in the cytoplasm. Mol. Cell 6, 673-682 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 673-682
    • Kataoka, N.1
  • 53
    • 0035890258 scopus 로고    scopus 로고
    • Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex
    • Kataoka, N., Diem, M. D., Kim, V. N., Yong, J. & Dreyfuss, G. Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex. EMBO J. 20, 6424-6433 (2001).
    • (2001) EMBO J. , vol.20 , pp. 6424-6433
    • Kataoka, N.1    Diem, M.D.2    Kim, V.N.3    Yong, J.4    Dreyfuss, G.5
  • 54
    • 0034193569 scopus 로고    scopus 로고
    • Pre-mRNA splicing afters mRNP composition: Evidence for stable association of proteins at exon-exon junctions
    • Le Hir, H., Moore, M. J. & Maquat, L. E. Pre-mRNA splicing afters mRNP composition: evidence for stable association of proteins at exon-exon junctions. Genes Dev. 14, 1098-1108 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 1098-1108
    • Le Hir, H.1    Moore, M.J.2    Maquat, L.E.3
  • 55
    • 0035687504 scopus 로고    scopus 로고
    • The protein Mago provides a link between splicing and mRNA localization
    • Le Hir, H., Gatfield, D., Braun, I. C., Forler, D. & Izaurralde, E. The protein Mago provides a link between splicing and mRNA localization. EMBO Rep. 2, 1119-1124 (2001). Provides an initial characterization of components of the exon junction complex formed in vitro.
    • (2001) EMBO Rep. , vol.2 , pp. 1119-1124
    • Le Hir, H.1    Gatfield, D.2    Braun, I.C.3    Forler, D.4    Izaurralde, E.5
  • 56
    • 0034710286 scopus 로고    scopus 로고
    • The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes
    • McGarvey, T. et al. The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes. J. Cell Biol. 150, 309-320 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 309-320
    • McGarvey, T.1
  • 57
    • 0034699472 scopus 로고    scopus 로고
    • The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
    • Zhou, Z. et al. The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 407, 401-405 (2000).
    • (2000) Nature , vol.407 , pp. 401-405
    • Zhou, Z.1
  • 58
    • 0035975942 scopus 로고    scopus 로고
    • The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila
    • Gatfield, D. et al. The DExH/D box protein HEL/UAP56 is essential for mRNA nuclear export in Drosophila. Curr. Biol. 11, 1716-1721 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1716-1721
    • Gatfield, D.1
  • 59
    • 0035846138 scopus 로고    scopus 로고
    • Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly
    • Luo, M. L. et al. Pre-mRNA splicing and mRNA export linked by direct interactions between UAP56 and Aly. Nature 413, 644-647 (2001).
    • (2001) Nature , vol.413 , pp. 644-647
    • Luo, M.L.1
  • 60
    • 0036826885 scopus 로고    scopus 로고
    • 5′ exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly
    • Reichert, V. L., Le Hir, H., Jurica, M. S. & Moore, M. J. 5′ exon interactions within the human spliceosome establish a framework for exon junction complex structure and assembly. Genes Dev. 16, 2778-2791 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 2778-2791
    • Reichert, V.L.1    Le Hir, H.2    Jurica, M.S.3    Moore, M.J.4
  • 61
    • 0035901565 scopus 로고    scopus 로고
    • The Y14 protein communicates to the cytoplasm the position of exon-exon junctions
    • Kim, V. N. et al. The Y14 protein communicates to the cytoplasm the position of exon-exon junctions. EMBO J. 20, 2062-2068 (2001).
    • (2001) EMBO J. , vol.20 , pp. 2062-2068
    • Kim, V.N.1
  • 62
    • 0035823036 scopus 로고    scopus 로고
    • Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20
    • Ishigaki, Y., Li, X., Serin, G. & Maquat, L. E. Evidence for a pioneer round of mRNA translation: mRNAs subject to nonsense-mediated decay in mammalian cells are bound by CBP80 and CBP20. Cell 106, 607-617 (2001). Shows that NMD targets CBP80-bound mRNA during a pioneer round of translation.
    • (2001) Cell , vol.106 , pp. 607-617
    • Ishigaki, Y.1    Li, X.2    Serin, G.3    Maquat, L.E.4
  • 63
    • 0035823247 scopus 로고    scopus 로고
    • Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS 1
    • Lykke-Andersen, J., Shu, M. D. & Steitz, J. A. Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1. Science 293, 1836-1839 (2001).
    • (2001) Science , vol.293 , pp. 1836-1839
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 64
    • 0037046798 scopus 로고    scopus 로고
    • Translation is required to remove Y14 from mRNAs in the cytoplasm
    • Dostie, J. & Dreyfuss, G. Translation is required to remove Y14 from mRNAs in the cytoplasm. Curr. Biol. 12, 1060-1067 (2002). Provides evidence that translating ribosomes remove a component of the exon junction complex.
    • (2002) Curr. Biol. , vol.12 , pp. 1060-1067
    • Dostie, J.1    Dreyfuss, G.2
  • 65
    • 0033592896 scopus 로고    scopus 로고
    • Splicing is required for rapid and efficient mRNA export in metazoans
    • Luo, M. J. & Reed, R. Splicing is required for rapid and efficient mRNA export in metazoans. Proc. Natl Acad. Sci. USA 96, 14937-14942 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14937-14942
    • Luo, M.J.1    Reed, R.2
  • 66
    • 0345643313 scopus 로고    scopus 로고
    • The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human
    • Katahira, J. et al. The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18, 2593-2609 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2593-2609
    • Katahira, J.1
  • 67
    • 17044441683 scopus 로고    scopus 로고
    • The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates
    • Bachi, A. et al. The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. RNA 6, 136-158 (2000).
    • (2000) RNA , vol.6 , pp. 136-158
    • Bachi, A.1
  • 68
    • 0035801373 scopus 로고    scopus 로고
    • The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay
    • Le Hir, H., Gatfield, D., Izaurralde, E. & Moore, M. J. The exon-exon junction complex provides a binding platform for factors involved in mRNA export and nonsense-mediated mRNA decay. EMBO J. 20, 4987-4997 (2001).
    • (2001) EMBO J. , vol.20 , pp. 4987-4997
    • Le Hir, H.1    Gatfield, D.2    Izaurralde, E.3    Moore, M.J.4
  • 69
    • 0035970063 scopus 로고    scopus 로고
    • REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus
    • Rodrigues, J. P. et al. REF proteins mediate the export of spliced and unspliced mRNAs from the nucleus. Proc. Natl Acad. Sci. USA 98, 1030-1035 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1030-1035
    • Rodrigues, J.P.1
  • 70
    • 0141469976 scopus 로고    scopus 로고
    • Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex 67p and is required for mRNA export
    • Strasser, K. & Hurt, E. Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19, 410-420 (2000).
    • (2000) EMBO J. , vol.19 , pp. 410-420
    • Strasser, K.1    Hurt, E.2
  • 71
    • 0037850982 scopus 로고    scopus 로고
    • Structure of the y14-magoh core of the exon junction complex
    • Lau, C. K., Diem, M. D., Dreyfuss, G. & Van Duyne, G. D. Structure of the y14-magoh core of the exon junction complex. Curr. Biol. 13, 933-941 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 933-941
    • Lau, C.K.1    Diem, M.D.2    Dreyfuss, G.3    Van Duyne, G.D.4
  • 72
    • 0037447151 scopus 로고    scopus 로고
    • Crystal structure of the Drosophila Mago nashi-Y14 complex
    • Shi, H. & Xu, R. M. Crystal structure of the Drosophila Mago nashi-Y14 complex. Genes Dev. 17, 971-976 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 971-976
    • Shi, H.1    Xu, R.M.2
  • 74
    • 0035975970 scopus 로고    scopus 로고
    • Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport
    • Hachet, O. & Ephrussi, A. Drosophila Y14 shuttles to the posterior of the oocyte and is required for oskar mRNA transport. Curr. Biol. 11, 1666-1674 (2001).
    • (2001) Curr. Biol. , vol.11 , pp. 1666-1674
    • Hachet, O.1    Ephrussi, A.2
  • 75
    • 0035498967 scopus 로고    scopus 로고
    • The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis
    • Mohr, S. E., Dillon, S. T. & Boswell, R. E. The RNA-binding protein Tsunagi interacts with Mago Nashi to establish polarity and localize oskar mRNA during Drosophila oogenesis. Genes Dev. 15, 2886-2899 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2886-2899
    • Mohr, S.E.1    Dillon, S.T.2    Boswell, R.E.3
  • 76
    • 0037154964 scopus 로고    scopus 로고
    • A conserved mRNA export machinery coupled to pre-mRNA splicing
    • Reed, R. & Hurt, E. A conserved mRNA export machinery coupled to pre-mRNA splicing. Cell 108, 523-531 (2002).
    • (2002) Cell , vol.108 , pp. 523-531
    • Reed, R.1    Hurt, E.2
  • 77
    • 0037175374 scopus 로고    scopus 로고
    • REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export
    • Gatfield, D. & Izaurralde, E. REF1/Aly and the additional exon junction complex proteins are dispensable for nuclear mRNA export. J. Cell Biol. 159, 579-588 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 579-588
    • Gatfield, D.1    Izaurralde, E.2
  • 78
    • 0037406116 scopus 로고    scopus 로고
    • A quantitative analysis of intron effects on mammalian gene expression
    • Nott, A., Meislin, S. H. & Moore, M. J. A quantitative analysis of intron effects on mammalian gene expression. RNA 9, 607-617 (2003).
    • (2003) RNA , vol.9 , pp. 607-617
    • Nott, A.1    Meislin, S.H.2    Moore, M.J.3
  • 79
    • 0141706348 scopus 로고    scopus 로고
    • Exon junction complexes mediate the enhancing effect of splicing on mRNA expression
    • Wiegand, H. L., Lu, S. & Cullen, B. R. Exon junction complexes mediate the enhancing effect of splicing on mRNA expression. Proc. Natl Acad. Sci. USA 100, 11327-11332 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11327-11332
    • Wiegand, H.L.1    Lu, S.2    Cullen, B.R.3
  • 80
    • 0035025061 scopus 로고    scopus 로고
    • Splicing factors SRp 20 and 9G8 promote the nucleocytoplasmic export of mRNA
    • Huang, Y. & Steitz, J. A. Splicing factors SRp20 and 9G8 promote the nucleocytoplasmic export of mRNA. Mol. Cell 7, 899-905 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 899-905
    • Huang, Y.1    Steitz, J.A.2
  • 81
    • 0344211508 scopus 로고    scopus 로고
    • SR splicing factors serve as adapter proteins for TAP-dependent mRNA export
    • Huang, Y., Gattoni, R., Stevenin, J. & Steitz, J. A. SR splicing factors serve as adapter proteins for TAP-dependent mRNA export. Mol. Cell 11, 837-843 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 837-843
    • Huang, Y.1    Gattoni, R.2    Stevenin, J.3    Steitz, J.A.4
  • 82
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen, J., Shu, M. D. & Steitz, J. A. Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell 103, 1121-1131 (2000). Demonstrates that tethering any one of the UPF proteins downstream of a normal termination codon is sufficient to elicit NMD.
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 83
    • 0038814325 scopus 로고    scopus 로고
    • Y14 and hUpf3b form an NMD-activating complex
    • Gehring, N. H., Neu-Yilik, G., Schell, T., Hentze, M. W. & Kulozik, A. E. Y14 and hUpf3b form an NMD-activating complex. Mol. Cell 11, 939-949 (2003). Illustrates a functional difference between UPF3 (UPF3A) and UPF3X (UPF3B) as well as the importance of Y14 to NMD.
    • (2003) Mol. Cell , vol.11 , pp. 939-949
    • Gehring, N.H.1    Neu-Yilik, G.2    Schell, T.3    Hentze, M.W.4    Kulozik, A.E.5
  • 84
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune, F., Li, X. & Maquat, L. E. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12, 675-687 (2003). Provides an initial characterization of the enzymology of NMD in mammalian cells.
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.E.3
  • 85
    • 0027969151 scopus 로고
    • A nuclear cap binding protein complex involved in pre-mRNA splicing
    • Izaurralde, E. et al. A nuclear cap binding protein complex involved in pre-mRNA splicing. Cell 78, 657-668 (1994).
    • (1994) Cell , vol.78 , pp. 657-668
    • Izaurralde, E.1
  • 86
    • 0030753073 scopus 로고    scopus 로고
    • The role of the cap structure in RNA processing and nuclear export
    • Lewis, J. D. & Izaurralde, E. The role of the cap structure in RNA processing and nuclear export. Eur. J. Biochem. 247, 461-469 (1997).
    • (1997) Eur. J. Biochem. , vol.247 , pp. 461-469
    • Lewis, J.D.1    Izaurralde, E.2
  • 87
    • 0029870388 scopus 로고    scopus 로고
    • A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionaly and accompanies the ribonucleoprotein particle during nuclear export
    • Visa, N., Izaurralde, E., Ferreira, J., Daneholt, B. & Mattaj, I. W. A nuclear cap-binding complex binds Balbiani ring pre-mRNA cotranscriptionaly and accompanies the ribonucleoprotein particle during nuclear export. J. Cell Biol. 133, 5-14 (1996).
    • (1996) J. Cell Biol. , vol.133 , pp. 5-14
    • Visa, N.1    Izaurralde, E.2    Ferreira, J.3    Daneholt, B.4    Mattaj, I.W.5
  • 88
    • 0034604712 scopus 로고    scopus 로고
    • The yeast mRNA-binding protein Npl3p interacts with the cap-binding complex
    • Shen, E. C., Stage-Zimmermann, T, Chui, P. & Silver, P. A. The yeast mRNA-binding protein Npl3p interacts with the cap-binding complex. J. Biol. Chem. 275, 23718-23724 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 23718-23724
    • Shen, E.C.1    Stage-Zimmermann, T.2    Chui, P.3    Silver, P.A.4
  • 89
    • 0026705268 scopus 로고
    • A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus
    • Lejbkowicz, F. et al. A fraction of the mRNA 5′ cap-binding protein, eukaryotic initiation factor 4E, localizes to the nucleus. Proc. Natl Acad. Sci. USA 89, 9612-9616 (1992).
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 9612-9616
    • Lejbkowicz, F.1
  • 90
    • 0032834055 scopus 로고    scopus 로고
    • elF4 initiation factors: Effectors of mRNA recruitment to dbosomes and regulators of translation
    • Gingras, A. C., Raught, B. & Sonenberg, N. elF4 initiation factors: effectors of mRNA recruitment to dbosomes and regulators of translation. Annu. Rev. Biochem. 68, 913-963 (1999).
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913-963
    • Gingras, A.C.1    Raught, B.2    Sonenberg, N.3
  • 91
    • 0034707668 scopus 로고    scopus 로고
    • Nuclear eukaryotic initiation factor 4E (elF4E) calocalizes with splicing factors in speckles
    • Dostie, J., Lejbkowicz, F. & Sonenberg, N. Nuclear eukaryotic initiation factor 4E (elF4E) calocalizes with splicing factors in speckles. J. Cell Biol. 148, 239-247 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 239-247
    • Dostie, J.1    Lejbkowicz, F.2    Sonenberg, N.3
  • 92
    • 0037099212 scopus 로고    scopus 로고
    • NASty effects on fibrillin pre-mRNA splicing: Another case of ESE does it, but proposals for translation-dependent splice site choice live on
    • Maquat, L. E. NASty effects on fibrillin pre-mRNA splicing: another case of ESE does it, but proposals for translation-dependent splice site choice live on. Genes Dev. 16, 1743-1753 (2002).
    • (2002) Genes Dev. , vol.16 , pp. 1743-1753
    • Maquat, L.E.1
  • 93
    • 0036809882 scopus 로고    scopus 로고
    • Nonsense-associated altered splicing: A frame-dependent response distinct from nonsense-mediated decay
    • Wang, J., Chang, Y. F., Hamilton, J. I. & Wilkinson, M. F. Nonsense-associated altered splicing: a frame-dependent response distinct from nonsense-mediated decay. Mol. Cell 10, 951-957 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 951-957
    • Wang, J.1    Chang, Y.F.2    Hamilton, J.I.3    Wilkinson, M.F.4
  • 94
    • 0037275978 scopus 로고    scopus 로고
    • Nuclear translation: What is the evidence?
    • Dahlberg, J. E., Lund, E. & Goodwin, E. B. Nuclear translation: what is the evidence? RNA 9, 1-8 (2003). Evaluates the possibility of translation within nuclei, which was re-established with the discovery of NMD.
    • (2003) RNA , vol.9 , pp. 1-8
    • Dahlberg, J.E.1    Lund, E.2    Goodwin, E.B.3
  • 95
    • 0035839002 scopus 로고    scopus 로고
    • Coupled transcription and translation within nuclei of mammalian cells
    • Iborra, F. J., Jackson, D. A. & Cook, P. R. Coupled transcription and translation within nuclei of mammalian cells. Science 293, 1139-1142 (2001).
    • (2001) Science , vol.293 , pp. 1139-1142
    • Iborra, F.J.1    Jackson, D.A.2    Cook, P.R.3
  • 96
    • 0034886974 scopus 로고    scopus 로고
    • Precursor RNAs harboring nonsense codons accumulate near the site of transcription
    • Muhlemann, O. et al. Precursor RNAs harboring nonsense codons accumulate near the site of transcription. Mol. Cell 8, 33-43 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 33-43
    • Muhlemann, O.1
  • 97
    • 0036023947 scopus 로고    scopus 로고
    • Intranuclear degradation of nonsense codon-containing mRNA
    • Buhler, M., Wilkinson, M. F. & Muhlemann, O. Intranuclear degradation of nonsense codon-containing mRNA. EMBO Rep. 3, 646-651 (2002).
    • (2002) EMBO Rep. , vol.3 , pp. 646-651
    • Buhler, M.1    Wilkinson, M.F.2    Muhlemann, O.3
  • 98
    • 0036781068 scopus 로고    scopus 로고
    • Ribosome components are associated with sites of transcription
    • Brogna, S., Sato, T. A. & Rosbash, M. Ribosome components are associated with sites of transcription. Mol. Cell 10, 93-104 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 93-104
    • Brogna, S.1    Sato, T.A.2    Rosbash, M.3
  • 99
    • 0037112790 scopus 로고    scopus 로고
    • Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    • Bohnsack, M. T. et al. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J. 21, 6205-6215 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6205-6215
    • Bohnsack, M.T.1
  • 100
    • 0037112842 scopus 로고    scopus 로고
    • Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
    • Calado, A., Treichel, N., Muller, E. C., Otto, A. & Kutay, U. Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J. 21, 6216-6224 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6216-6224
    • Calado, A.1    Treichel, N.2    Muller, E.C.3    Otto, A.4    Kutay, U.5
  • 101
    • 0037025175 scopus 로고    scopus 로고
    • Alternatively spliced TCR mRNA induced by disruption of reading frame
    • Wang, J., Hamilton, J. I., Carter, M. S., Li, S. & Wilkinson, M. F. Alternatively spliced TCR mRNA induced by disruption of reading frame. Science 297, 108-110 (2002).
    • (2002) Science , vol.297 , pp. 108-110
    • Wang, J.1    Hamilton, J.I.2    Carter, M.S.3    Li, S.4    Wilkinson, M.F.5
  • 102
    • 0037278925 scopus 로고    scopus 로고
    • Nuclear protein synthesis: A re-evaluation
    • Nathanson, L, Xia, T. & Deutscher, M. P. Nuclear protein synthesis: a re-evaluation. RNA 9, 9-13 (2003).
    • (2003) RNA , vol.9 , pp. 9-13
    • Nathanson, L.1    Xia, T.2    Deutscher, M.P.3
  • 103
    • 0042830818 scopus 로고    scopus 로고
    • Looking for nuclear translation using Xenopus oocytes
    • Cosson, B. & Philippe, M. Looking for nuclear translation using Xenopus oocytes. Biol. Cell 95, 321-325 (2003).
    • (2003) Biol. Cell , vol.95 , pp. 321-325
    • Cosson, B.1    Philippe, M.2
  • 104
    • 0037844806 scopus 로고    scopus 로고
    • Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates
    • Trotta, C. R., Lund, E., Kahan, L., Johnson, A. W. & Dahlberg, J. E. Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates. EMBO J. 22, 2841-2851 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2841-2851
    • Trotta, C.R.1    Lund, E.2    Kahan, L.3    Johnson, A.W.4    Dahlberg, J.E.5
  • 105
    • 0030034421 scopus 로고    scopus 로고
    • A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes
    • Visa, N. et al. A pre-mRNA-binding protein accompanies the RNA from the gene through the nuclear pores and into polysomes. Cell 84, 253-264 (1996).
    • (1996) Cell , vol.84 , pp. 253-264
    • Visa, N.1
  • 106
    • 0037064145 scopus 로고    scopus 로고
    • Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts
    • Mendell, J. T., Ap Rhys, C. M. & Dietz, H. C. Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts. Science 298, 419-422 (2002).
    • (2002) Science , vol.298 , pp. 419-422
    • Mendell, J.T.1    Ap Rhys, C.M.2    Dietz, H.C.3
  • 107
    • 0032544062 scopus 로고    scopus 로고
    • A mutated human homologue to yeast Upf1 protein has a dominant-negative effect on the decay of nonsense-containing mRNAs in mammalian cells
    • Sun, X., Pedick, H. A., Dietz, H. C. & Maquat, L. E. A mutated human homologue to yeast Upf1 protein has a dominant-negative effect on the decay of nonsense-containing mRNAs in mammalian cells. Proc. Natl Acad. Sci. USA 95, 10009-10014 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 10009-10014
    • Sun, X.1    Pedick, H.A.2    Dietz, H.C.3    Maquat, L.E.4
  • 108
    • 0033835231 scopus 로고    scopus 로고
    • Characterization of the biochemical properties of the human Upf1 gene product that is involved in nonsense-mediated mRNA decay
    • Bhattacharya, A. et al. Characterization of the biochemical properties of the human Upf1 gene product that is involved in nonsense-mediated mRNA decay. RNA 6, 1226-1235 (2000).
    • (2000) RNA , vol.6 , pp. 1226-1235
    • Bhattacharya, A.1
  • 109
    • 0035038083 scopus 로고    scopus 로고
    • Evidence that phosphorylation of human Upf1 protein varies with intracellular location and is mediated by a wortmannin-sensitive and rapamycin-sensitive PI3-kinase-related kinase signaling pathway
    • Pal, M., Ishigaki, Y., Nagy, E. & Maquat, L. E. Evidence that phosphorylation of human Upf1 protein varies with intracellular location and is mediated by a wortmannin-sensitive and rapamycin-sensitive PI3-kinase-related kinase signaling pathway. RNA 7, 5-15 (2001).
    • (2001) RNA , vol.7 , pp. 5-15
    • Pal, M.1    Ishigaki, Y.2    Nagy, E.3    Maquat, L.E.4
  • 110
    • 0030745114 scopus 로고    scopus 로고
    • Cloning and characterization of HUPF1, a human homolog of the Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein
    • Applequist, S. E., Selg, M., Raman, C. & Jack, H. M. Cloning and characterization of HUPF1, a human homolog of the Saccharomyces cerevisiae nonsense mRNA-reducing UPF1 protein. Nucleic Acids Res. 25, 814-821 (1997).
    • (1997) Nucleic Acids Res. , vol.25 , pp. 814-821
    • Applequist, S.E.1    Selg, M.2    Raman, C.3    Jack, H.M.4
  • 111
    • 0034751160 scopus 로고    scopus 로고
    • Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabdtis elegans SMG-4)
    • Serin, G., Gersappe, A., Black, J. D., Aronoff, R. & Maquat, L. E. Identification and characterization of human orthologues to Saccharomyces cerevisiae Upf2 protein and Upf3 protein (Caenorhabdtis elegans SMG-4). Mol. Cell. Biol. 21, 209-223 (2001).
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 209-223
    • Serin, G.1    Gersappe, A.2    Black, J.D.3    Aronoff, R.4    Maquat, L.E.5
  • 112
    • 0037279012 scopus 로고    scopus 로고
    • Characterization of human Smg5/7a: A protein with similarities to C. elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1
    • Chiu, S.-Y., Senn, G. Ohara, O. and Maquat, L. E. Characterization of human Smg5/7a: a protein with similarities to C. elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1. RNA 9, 77-87 (2003).
    • (2003) RNA , vol.9 , pp. 77-87
    • Chiu, S.-Y.1    Senn, G.2    Ohara, O.3    Maquat, L.E.4
  • 113
    • 0034460323 scopus 로고    scopus 로고
    • Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes
    • Mendell, J. T., Medghalchi, S. M., Lake, R. G., Noensie, E. N. & Dietz, H. C. Novel Upf2p orthologues suggest a functional link between translation initiation and nonsense surveillance complexes. Mol. Cell. Biol. 20, 8944-8957 (2000).
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8944-8957
    • Mendell, J.T.1    Medghalchi, S.M.2    Lake, R.G.3    Noensie, E.N.4    Dietz, H.C.5
  • 114
    • 0032771414 scopus 로고    scopus 로고
    • SMG-2 is a phosphorylated protein required for mRNA surveillance in Caenorhabditis elegans and related to Upf1 p of yeast
    • Page, M. F., Carr, B., Anders, K. R., Grimson, A. & Anderson, P. SMG-2 is a phosphorylated protein required for mRNA surveillance in Caenorhabditis elegans and related to Upf1 p of yeast. Mol. Cell. Biol. 19, 5943-5951 (1999). Characterizes the function of SMG in NMD.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5943-5951
    • Page, M.F.1    Carr, B.2    Anders, K.R.3    Grimson, A.4    Anderson, P.5
  • 115
    • 0035933889 scopus 로고    scopus 로고
    • Cloning of a novel phosphatidylinositol kinase-related kinase: Characterization of the human SMG-1 RNA surveillance protein
    • Denning, G., Jamieson, L., Maquat, L. E., Thompson, E. A. & Fields, A. P. Cloning of a novel phosphatidylinositol kinase-related kinase: characterization of the human SMG-1 RNA surveillance protein. J. Biol. Chem. 276, 22709-22714 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 22709-22714
    • Denning, G.1    Jamieson, L.2    Maquat, L.E.3    Thompson, E.A.4    Fields, A.P.5
  • 116
    • 0035449691 scopus 로고    scopus 로고
    • Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay
    • Yamashita, A., Ohnishi, T., Kashima, I., Taya, Y. & Ohno, S. Human SMG-1, a novel phosphatidylinositol 3-kinase-related protein kinase, associates with components of the mRNA surveillance complex and is involved in the regulation of nonsense-mediated mRNA decay. Genes Dev. 15, 2215-2228 (2001).
    • (2001) Genes Dev. , vol.15 , pp. 2215-2228
    • Yamashita, A.1    Ohnishi, T.2    Kashima, I.3    Taya, Y.4    Ohno, S.5
  • 117
    • 0037415691 scopus 로고    scopus 로고
    • SMG-5, required for C. elegans nonsense-mediated mRNA decay, associates with SMG-2 and protein phosphatase 2A
    • Anders, K. R., Grimson, A. & Anderson, P. SMG-5, required for C. elegans nonsense-mediated mRNA decay, associates with SMG-2 and protein phosphatase 2A. EMBO J. 22, 641-650 (2003).
    • (2003) EMBO J. , vol.22 , pp. 641-650
    • Anders, K.R.1    Grimson, A.2    Anderson, P.3
  • 118
    • 0042025014 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in Drosophila: At the intersection of the yeast and mammalian pathways
    • Gatfield, D., Unterholzner, L., Ciccarelli, F. D., Bork, P. & Izaurralde, E. Nonsense-mediated mRNA decay in Drosophila: at the intersection of the yeast and mammalian pathways. EMBO J. 22, 3960-3970 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3960-3970
    • Gatfield, D.1    Unterholzner, L.2    Ciccarelli, F.D.3    Bork, P.4    Izaurralde, E.5
  • 119
    • 2642656314 scopus 로고    scopus 로고
    • The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs
    • Czaplinski, K. et al. The surveillance complex interacts with the translation release factors to enhance termination and degrade aberrant mRNAs. Genes Dev. 12, 1665-1677 (1998).
    • (1998) Genes Dev. , vol.12 , pp. 1665-1677
    • Czaplinski, K.1
  • 120
    • 0035865408 scopus 로고    scopus 로고
    • The role of Upf proteins in modulating the translation read-through of nonsense-containing transcripts
    • Wang, W., Czaplinski, K., Rao, Y. & Peltz, S. W. The role of Upf proteins in modulating the translation read-through of nonsense-containing transcripts. EMBO J. 20, 880-890 (2001).
    • (2001) EMBO J. , vol.20 , pp. 880-890
    • Wang, W.1    Czaplinski, K.2    Rao, Y.3    Peltz, S.W.4
  • 121
    • 0033942924 scopus 로고    scopus 로고
    • Nonsense-mediated decay mutants do not affect programmed-1 frameshifting
    • Bidou, L. et al. Nonsense-mediated decay mutants do not affect programmed-1 frameshifting. RNA 6, 952-961 (2000).
    • (2000) RNA , vol.6 , pp. 952-961
    • Bidou, L.1
  • 122
    • 0042068262 scopus 로고    scopus 로고
    • Complexes between the nonsense-mediated mRNA decay pathway factor human upf1 (up-frameshift protein 1) and essential nonsense-mediated mRNA decay factors in HeLa cells
    • Schell, T. et al. Complexes between the nonsense-mediated mRNA decay pathway factor human upf1 (up-frameshift protein 1) and essential nonsense-mediated mRNA decay factors in HeLa cells. Biochem. J. 373, 775-783 (2003).
    • (2003) Biochem. J. , vol.373 , pp. 775-783
    • Schell, T.1
  • 123
    • 0035787913 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: Insights into mechanism from the cellular abundance of human Upf1, Upf2, Upf3, and Upf3X proteins
    • Maquat, L. E. & Serin, G. Nonsense-mediated mRNA decay: insights into mechanism from the cellular abundance of human Upf1, Upf2, Upf3, and Upf3X proteins. Cold Spring Harb. Symp. Quant. Biol. 66, 313-320 (2001).
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 313-320
    • Maquat, L.E.1    Serin, G.2
  • 124
    • 0037080771 scopus 로고    scopus 로고
    • T-cell receptor sequences that elicit strong down-regulation of premature termination codon-bearing transcripts
    • Gudikote, J. P. & Wilkinson, M. F. T-cell receptor sequences that elicit strong down-regulation of premature termination codon-bearing transcripts. EMBO J. 21, 125-134 (2002).
    • (2002) EMBO J. , vol.21 , pp. 125-134
    • Gudikote, J.P.1    Wilkinson, M.F.2
  • 125
    • 0037052949 scopus 로고    scopus 로고
    • Identification of δ-helicase as the bovine homolog of HUPF1: Demonstration of an interaction with the third subunit of DNA polymerase &
    • Carastro, L. M. et al. Identification of δ-helicase as the bovine homolog of HUPF1: demonstration of an interaction with the third subunit of DNA polymerase & Nucleic Acids Res. 30, 2232-2243 (2002).
    • (2002) Nucleic Acids Res. , vol.30 , pp. 2232-2243
    • Carastro, L.M.1
  • 126
    • 0026536395 scopus 로고
    • Purification and characterization of δ-helicase from fetal calf thymus
    • Li, X., Tan, C. K., So, A. G. & Downey, K. M. Purification and characterization of δ-helicase from fetal calf thymus. Biochemistry 31, 3507-3513 (1992).
    • (1992) Biochemistry , vol.31 , pp. 3507-3513
    • Li, X.1    Tan, C.K.2    So, A.G.3    Downey, K.M.4
  • 127
    • 0034665818 scopus 로고    scopus 로고
    • A link between RNA interference and nonsense-mediated decay in Caenorhabditis elegans
    • Domeier, M. E. et al. A link between RNA interference and nonsense-mediated decay in Caenorhabditis elegans. Science 289, 1928-1931 (2000).
    • (2000) Science , vol.289 , pp. 1928-1931
    • Domeier, M.E.1
  • 128
    • 0037381155 scopus 로고    scopus 로고
    • A human homolog of yeast est1 associates with telomerase and uncaps chromosome ends when overexpressed
    • Reichenbach, P. et al. A human homolog of yeast est1 associates with telomerase and uncaps chromosome ends when overexpressed. Curr. Biol. 13, 568-574 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 568-574
    • Reichenbach, P.1
  • 129
    • 0003245690 scopus 로고    scopus 로고
    • mRNAs encoding telomerase components and regulators are controlled by UPF genes in Saccharomyces cerevisiae
    • Dahlseid, J. N. et al. mRNAs encoding telomerase components and regulators are controlled by UPF genes in Saccharomyces cerevisiae. Eukaryot. Cell 2, 134-142 (2003).
    • (2003) Eukaryot. Cell , vol.2 , pp. 134-142
    • Dahlseid, J.N.1
  • 130
    • 0028861358 scopus 로고
    • Characterization of cis-acting sequences and decay intermediates involved in nonsense-mediated mRNA turnover
    • Hagan, K. W., Ruiz-Echevama, M. J., Quan, Y. & Peltz, S. W. Characterization of cis-acting sequences and decay intermediates involved in nonsense-mediated mRNA turnover. Mol. Cell. Biol. 15, 809-823 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 809-823
    • Hagan, K.W.1    Ruiz-Echevama, M.J.2    Quan, Y.3    Peltz, S.W.4
  • 131
    • 0027932513 scopus 로고
    • Premature translational termination triggers mRNA decapping
    • Muhlrad, D. & Parker, R. Premature translational termination triggers mRNA decapping. Nature 370, 578-581 (1994).
    • (1994) Nature , vol.370 , pp. 578-581
    • Muhlrad, D.1    Parker, R.2
  • 132
    • 0032880399 scopus 로고    scopus 로고
    • Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance
    • Muhlrad, D. & Parker, R. Aberrant mRNAs with extended 3′ UTRs are substrates for rapid degradation by mRNA surveillance. RNA 5, 1299-1307 (1999).
    • (1999) RNA , vol.5 , pp. 1299-1307
    • Muhlrad, D.1    Parker, R.2
  • 133
    • 0037762554 scopus 로고    scopus 로고
    • An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′→5′ degradation
    • Mitchell, P. & Tollervey, D. An NMD pathway in yeast involving accelerated deadenylation and exosome-mediated 3′→5′ degradation. Mol. Cell 11, 1405-1413 (2003).
    • (2003) Mol. Cell , vol.11 , pp. 1405-1413
    • Mitchell, P.1    Tollervey, D.2
  • 134
    • 0036888905 scopus 로고    scopus 로고
    • Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
    • Lykke-Andersen, J. Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol. Cell. Biol. 22, 8114-8121 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8114-8121
    • Lykke-Andersen, J.1
  • 135
    • 0036909093 scopus 로고    scopus 로고
    • The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci
    • Ingelfinger, D., Arndt-Jovin, D. J., Luhrmann, R. & Achsel, T. The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci. RNA 8, 1489-1501 (2002).
    • (2002) RNA , vol.8 , pp. 1489-1501
    • Ingelfinger, D.1    Arndt-Jovin, D.J.2    Luhrmann, R.3    Achsel, T.4
  • 136
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • Van Dijk, E. et al. Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J. 21, 6915-6924 (2002).
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1
  • 137
    • 0038112021 scopus 로고    scopus 로고
    • Rapid deadenylation triggered by a nonsense codon precedes decay of the RNA body in a mammalian cytoplasmic nonsense-mediated decay pathway
    • Chen, C. Y. & Shyu, A. B. Rapid deadenylation triggered by a nonsense codon precedes decay of the RNA body in a mammalian cytoplasmic nonsense-mediated decay pathway. Mol. Cell. Biol. 23, 4805-4813 (2003).
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4805-4813
    • Chen, C.Y.1    Shyu, A.B.2
  • 138
    • 0024443107 scopus 로고
    • Novel metabolism of several β°-thalassemic β-globin mRNAs in the erythroid tissues of transgenic mice
    • Lim, S., Mullins, J. J., Chen, C. M., Gross, K. W. & Maquat, L. E. Novel metabolism of several β°-thalassemic β-globin mRNAs in the erythroid tissues of transgenic mice. EMBO J. 8, 2613-2619 (1989).
    • (1989) EMBO J. , vol.8 , pp. 2613-2619
    • Lim, S.1    Mullins, J.J.2    Chen, C.M.3    Gross, K.W.4    Maquat, L.E.5
  • 139
    • 0026641165 scopus 로고
    • Human β-globin mRNAs that harbor a nonsense codon are degraded in murine erythroid tissues to intermediates lacking regions of exon I or exons I and II that have a cap-like structure at the 5′ termini
    • Lim, S. K. & Maquat, L. E. Human β-globin mRNAs that harbor a nonsense codon are degraded in murine erythroid tissues to intermediates lacking regions of exon I or exons I and II that have a cap-like structure at the 5′ termini. EMBO J. 11, 3271-3278 (1992).
    • (1992) EMBO J. , vol.11 , pp. 3271-3278
    • Lim, S.K.1    Maquat, L.E.2
  • 140
    • 0026583873 scopus 로고
    • Nonsense codons in human β-globin mRNA result in the production of mRNA degradation products
    • Lim, S. K., Sigmund, C. D., Gross, K. W. & Maquat, L. E. Nonsense codons in human β-globin mRNA result in the production of mRNA degradation products. Mol. Cell. Biol. 12, 1149-1161 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1149-1161
    • Lim, S.K.1    Sigmund, C.D.2    Gross, K.W.3    Maquat, L.E.4
  • 141
    • 0036790995 scopus 로고    scopus 로고
    • β-globin mRNA decay in erythroid cells: UG site-preferred endonucleotytic cleavage that is augmented by a premature termination codon
    • Stevens, A. et al. β-globin mRNA decay in erythroid cells: UG site-preferred endonucleotytic cleavage that is augmented by a premature termination codon. Proc. Natl Acad. Sci. USA 99, 12741-12746 (2002). Characterizes an endonuclease that degrades β-globin mRNA with a PTC in erythroid cells.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12741-12746
    • Stevens, A.1
  • 142
    • 0041832086 scopus 로고    scopus 로고
    • An endonuclease activity similar toXenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells
    • Bremer, K. A., Stevens, A. & Schoenberg, D. R. An endonuclease activity similar toXenopus PMR1 catalyzes the degradation of normal and nonsense-containing human β-globin mRNA in erythroid cells. RNA 9, 1157-1167 (2003).
    • (2003) RNA , vol.9 , pp. 1157-1167
    • Bremer, K.A.1    Stevens, A.2    Schoenberg, D.R.3
  • 143
    • 0032696240 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4AIII (elF4AIII) is functionally distinct from elF 4AI and elF4AII
    • Li, Q. et al. Eukaryotic translation initiation factor 4AIII (elF4AIII) is functionally distinct from elF4AI and elF4AII. Mol. Cell. Biol. 19, 7336-7346 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7336-7346
    • Li, Q.1
  • 144
    • 0025786141 scopus 로고
    • The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon
    • Leeds, R, Peltz, S. W., Jacobson, A. & Culbertson, M. R. The product of the yeast UPF1 gene is required for rapid turnover of mRNAs containing a premature translational termination codon. Genes Dev. 5, 2303-2314 (1991). Provides initial characterization of a factor that is required for NMD.
    • (1991) Genes Dev. , vol.5 , pp. 2303-2314
    • Leeds, R.1    Peltz, S.W.2    Jacobson, A.3    Culbertson, M.R.4
  • 145
    • 0026773782 scopus 로고
    • Gene products that promote mRNA turnover in Saccharomyces cerevisiae
    • Leeds, R, Wood, J. M., Lee, B. S. & Culbertson, M. R. Gene products that promote mRNA turnover in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 2165-2177 (1992).
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2165-2177
    • Leeds, R.1    Wood, J.M.2    Lee, B.S.3    Culbertson, M.R.4
  • 146
    • 0024444026 scopus 로고
    • A new kind of informational suppression in the nematode Caenorhabditis elegans
    • Hodgkin, J., Papp, A., Pulak, R., Ambros, V. & Anderson, P. A new kind of informational suppression in the nematode Caenorhabditis elegans. Genetics 123, 301-313 (1989).
    • (1989) Genetics , vol.123 , pp. 301-313
    • Hodgkin, J.1    Papp, A.2    Pulak, R.3    Ambros, V.4    Anderson, P.5
  • 147
    • 0027382460 scopus 로고
    • mRNA surveillance by the Caenorhabditis elegans smg genes
    • Pulak, R. & Anderson, P. mRNA surveillance by the Caenorhabditis elegans smg genes. Genes Dev. 7, 1885-1897 (1993).
    • (1993) Genes Dev. , vol.7 , pp. 1885-1897
    • Pulak, R.1    Anderson, P.2
  • 148
    • 0032940802 scopus 로고    scopus 로고
    • smg-7 is required for mRNA surveillance in Caenorhabditis elegans
    • Cali, B. M., Kuchma, S. L., Latham, J. & Anderson, P. smg-7 is required for mRNA surveillance in Caenorhabditis elegans. Genetics 151, 605-616 (1999).
    • (1999) Genetics , vol.151 , pp. 605-616
    • Cali, B.M.1    Kuchma, S.L.2    Latham, J.3    Anderson, P.4
  • 149
    • 0036792078 scopus 로고    scopus 로고
    • From the cover: The hDcp2 protein is a mammalian mRNA decapping enzyme
    • Wang, Z., Jiao, X., Carr Schmid, A. & Kiledjian, M. From the cover: the hDcp2 protein is a mammalian mRNA decapping enzyme. Proc. Natl Acad. Sci. USA 99, 12663-12668 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12663-12668
    • Wang, Z.1    Jiao, X.2    Carr Schmid, A.3    Kiledjian, M.4
  • 150
    • 0041832085 scopus 로고    scopus 로고
    • Functional characterization of the mammalian mRNA decapping enzyme hDcp2
    • Piccirillo, C., Khanna, R. & Kiledjian, M. Functional characterization of the mammalian mRNA decapping enzyme hDcp2. RNA 9, 1138-1147 (2003).
    • (2003) RNA , vol.9 , pp. 1138-1147
    • Piccirillo, C.1    Khanna, R.2    Kiledjian, M.3
  • 151
    • 0036792048 scopus 로고    scopus 로고
    • mRNA decay enzymes: Decappers conserved between yeast and mammals
    • Decker, C. J. & Parker, R. mRNA decay enzymes: decappers conserved between yeast and mammals. Proc. NatlAcad. Sci, USA 99, 12512-12514 (2002).
    • (2002) Proc. NatlAcad. Sci. USA , vol.99 , pp. 12512-12514
    • Decker, C.J.1    Parker, R.2
  • 152
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • Bashkirov, V. I., Scherthan, H., Solinger, J. A., Buerstedde, J. M. & Heyer, W. D. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 136, 761-773 (1997).
    • (1997) J. Cell Biol. , vol.136 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.M.4    Heyer, W.D.5
  • 153
    • 0033566223 scopus 로고    scopus 로고
    • Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2
    • Zhang, M. et al. Cloning and mapping of the XRN2 gene to human chromosome 20p11.1-p11.2. Genomics 59, 252-254 (1999).
    • (1999) Genomics , vol.59 , pp. 252-254
    • Zhang, M.1
  • 155
    • 0039535081 scopus 로고    scopus 로고
    • Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease
    • Korner, C. G. & Wahle, E. Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease. J. Biol. Chem. 272, 10448-10456 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 10448-10456
    • Korner, C.G.1    Wahle, E.2
  • 156
    • 0033567131 scopus 로고    scopus 로고
    • The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases
    • Allmang, C. et al. The yeast exosome and human PM-Scl are related complexes of 3′→5′ exonucleases. Genes Dev. 13, 2148-2158 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 2148-2158
    • Allmang, C.1
  • 157
    • 18044371822 scopus 로고    scopus 로고
    • AU binding proteins recruit the exosome to degrade ARE-containing mRNAs
    • Chen, C. Y. et al. AU binding proteins recruit the exosome to degrade ARE-containing mRNAs. Cell 107, 451-464 (2001).
    • (2001) Cell , vol.107 , pp. 451-464
    • Chen, C.Y.1
  • 158
    • 0035853691 scopus 로고    scopus 로고
    • Identification of in vivo mRNA decay intermediates corresponding to sites of in vitro cleavage by polysomal ribonuclease 1
    • Hanson, M. N. & Schoenberg, D. R. Identification of in vivo mRNA decay intermediates corresponding to sites of in vitro cleavage by polysomal ribonuclease 1. J. Biol. Chem. 276, 12331-12337 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 12331-12337
    • Hanson, M.N.1    Schoenberg, D.R.2
  • 159
    • 2042437650 scopus 로고    scopus 로고
    • Initial sequencing and analysis of the human genome
    • Lander, E. S. et al. Initial sequencing and analysis of the human genome. Nature 409, 860-921 (2001).
    • (2001) Nature , vol.409 , pp. 860-921
    • Lander, E.S.1
  • 160
    • 0035895505 scopus 로고    scopus 로고
    • The sequence of the human genome
    • Venter, J. C. et al. The sequence of the human genome. Science 291, 1304-1351 (2001).
    • (2001) Science , vol.291 , pp. 1304-1351
    • Venter, J.C.1
  • 161
    • 0035823150 scopus 로고    scopus 로고
    • Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex
    • Kim, V. N., Kataoka, N. & Dreyfuss, G. Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex. Science 293, 1832-1836 (2001).
    • (2001) Science , vol.293 , pp. 1832-1836
    • Kim, V.N.1    Kataoka, N.2    Dreyfuss, G.3
  • 162
    • 1842689543 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay: A comporative analysis of different species
    • in the press
    • Maquat, L. E. Nonsense-mediated mRNA decay: a comporative analysis of different species. Curr. Genomics (in the press).
    • Curr. Genomics
    • Maquat, L.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.