메뉴 건너뛰기




Volumn 18, Issue 16, 2004, Pages 2010-2023

UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant

Author keywords

CCR4; MRNA turnover; PABP; Poly(A)nuclease; Translational control; UNR

Indexed keywords

CHEMOKINE RECEPTOR CCR4; MESSENGER RNA; NUCLEASE; POLYADENYLIC ACID BINDING PROTEIN; POLYADENYLIC ACID NUCLEASE; UNCLASSIFIED DRUG;

EID: 4043062382     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.1219104     Document Type: Article
Times cited : (130)

References (57)
  • 2
    • 0037316406 scopus 로고    scopus 로고
    • Nocturnin, a deadenylase in Xenopus laevis retina: A mechanism for posttranscriptional control of circadian-related mRNA
    • Baggs, J.E. and Green, C.B. 2003. Nocturnin, a deadenylase in Xenopus laevis retina: A mechanism for posttranscriptional control of circadian-related mRNA. Curr. Biol. 13: 189-198.
    • (2003) Curr. Biol. , vol.13 , pp. 189-198
    • Baggs, J.E.1    Green, C.B.2
  • 3
    • 0029053016 scopus 로고
    • Degradation of mRNA in eukaryotes
    • Beelman, C.A. and Parker, R. 1995. Degradation of mRNA in eukaryotes. Cell 81: 179-183.
    • (1995) Cell , vol.81 , pp. 179-183
    • Beelman, C.A.1    Parker, R.2
  • 4
    • 0037334142 scopus 로고    scopus 로고
    • Unr is required in vivo for efficient initiation of translation from the internal ribosome entry sites of both rhinovirus and poliovirus
    • Boussadia, O., Niepmann, M., Creancier, L., Prats, A.-C., Dautry, F., and Jacquemin-Sablon, H. 2003. Unr is required in vivo for efficient initiation of translation from the internal ribosome entry sites of both rhinovirus and poliovirus. J. Virol. 77: 3353-3359.
    • (2003) J. Virol. , vol.77 , pp. 3353-3359
    • Boussadia, O.1    Niepmann, M.2    Creancier, L.3    Prats, A.-C.4    Dautry, F.5    Jacquemin-Sablon, H.6
  • 5
    • 0028131915 scopus 로고
    • Selective degradation of early-response-gene mRNAs: Functional analyses of sequence features of the AU-rich elements
    • Chen, C.Y. and Shyu, A.B. 1994. Selective degradation of early-response-gene mRNAs: Functional analyses of sequence features of the AU-rich elements. Mol. Cell. Biol. 14: 8471-8482.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8471-8482
    • Chen, C.Y.1    Shyu, A.B.2
  • 6
    • 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
    • -. 2003. 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) Mol. Cell. Biol. , vol.23 , pp. 4805-4813
  • 7
    • 0026459943 scopus 로고
    • Two cellular proteins bind specifically to a purine-rich sequence necessary for the destabilization function of a c-fos protein-coding region determinant of mRNA instability
    • Chen, C.Y., You, Y., and Shyu, A.B. 1992. Two cellular proteins bind specifically to a purine-rich sequence necessary for the destabilization function of a c-fos protein-coding region determinant of mRNA instability. Mol. Cell. Biol. 12: 5748-5757.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5748-5757
    • Chen, C.Y.1    You, Y.2    Shyu, A.B.3
  • 8
    • 0029126879 scopus 로고
    • mRNA decay mediated by two distinct AU-rich elements from c-fos and granulocyte-macrophage colony-stimulating factor transcripts: Different deadenylation kinetics and uncoupling from translation
    • Chen, C.Y., Xu, N., and Shyu, A.B. 1995. mRNA decay mediated by two distinct AU-rich elements from c-fos and granulocyte-macrophage colony-stimulating factor transcripts: Different deadenylation kinetics and uncoupling from translation. Mol. Cell. Biol. 15: 5777-5788.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5777-5788
    • Chen, C.Y.1    Xu, N.2    Shyu, A.B.3
  • 9
    • 0037086701 scopus 로고    scopus 로고
    • CCR4, a 3′-5′ poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase
    • Chen, J., Chiang, Y.-C., and Denis, C.L. 2002. CCR4, a 3′-5′ poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase. EMBO J. 21: 1414-1426.
    • (2002) EMBO J. , vol.21 , pp. 1414-1426
    • Chen, J.1    Chiang, Y.-C.2    Denis, C.L.3
  • 10
    • 0032473972 scopus 로고    scopus 로고
    • Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation
    • Craig, A.W., Haghighat, A., Yu, A.T., and Sonenberg, N. 1998. Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation. Nature 392: 520-523.
    • (1998) Nature , vol.392 , pp. 520-523
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 11
    • 0031591391 scopus 로고    scopus 로고
    • Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast Poly(A)-binding protein1
    • Deardorff, J.A. and Sachs, A.B. 1997. Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast Poly(A)-binding protein1. J. Mol. Biol. 269: 67-81.
    • (1997) J. Mol. Biol. , vol.269 , pp. 67-81
    • Deardorff, J.A.1    Sachs, A.B.2
  • 13
    • 0141888419 scopus 로고    scopus 로고
    • A 3′ exonuclease that specifically interacts with the 3′ end of histone mRNA
    • Dominski, Z., Yang, X.C., Kaygun, H., Dadlez, M., and Marzluff, W.F. 2003. A 3′ exonuclease that specifically interacts with the 3′ end of histone mRNA. Mol. Cell 12: 295-305.
    • (2003) Mol. Cell , vol.12 , pp. 295-305
    • Dominski, Z.1    Yang, X.C.2    Kaygun, H.3    Dadlez, M.4    Marzluff, W.F.5
  • 14
    • 9144252209 scopus 로고    scopus 로고
    • Identification of four families of yCCR4- and Mg2+-dependent endonuclease-related proteins in higher eukaryotes, and characterization of orthologs of yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2 binding
    • Dupressoir, A., Morel, A.-P., Barbot, W., Loireau, M.-P., Corbo, L., and Heidmann, T. 2001. Identification of four families of yCCR4- and Mg2+-dependent endonuclease-related proteins in higher eukaryotes, and characterization of orthologs of yCCR4 with a conserved leucine-rich repeat essential for hCAF1/hPOP2 binding. BMC Genomics 2: 9.
    • (2001) BMC Genomics , vol.2 , pp. 9
    • Dupressoir, A.1    Morel, A.-P.2    Barbot, W.3    Loireau, M.-P.4    Corbo, L.5    Heidmann, T.6
  • 15
    • 0037155592 scopus 로고    scopus 로고
    • An mRNA surveillance mechanism that eliminates transcripts lacking termination codons
    • Frischmeyer, P.A., van Hoof, A., O'Donnell, K., Guerrerio, A.L., Parker, R., and Dietz, H.C. 2002. An mRNA surveillance mechanism that eliminates transcripts lacking termination codons. Science 295: 2258-2261.
    • (2002) Science , vol.295 , pp. 2258-2261
    • Frischmeyer, P.A.1    Van Hoof, A.2    O'Donnell, K.3    Guerrerio, A.L.4    Parker, R.5    Dietz, H.C.6
  • 16
    • 0033680082 scopus 로고    scopus 로고
    • Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro
    • Gao, M., Fritz, D.T., Ford, L.P., and Wilusz, J. 2000. Interaction between a poly(A)-specific ribonuclease and the 5′ cap influences mRNA deadenylation rates in vitro. Mol. Cell 5: 479-488.
    • (2000) Mol. Cell , vol.5 , pp. 479-488
    • Gao, M.1    Fritz, D.T.2    Ford, L.P.3    Wilusz, J.4
  • 17
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann, P.L. and Marahiel, M.A. 1998. A superfamily of proteins that contain the cold-shock domain. Trends Biochem. Sci. 23: 286-290.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 18
    • 0034730324 scopus 로고    scopus 로고
    • A mechanism for translationally coupled mRNA turnover: Interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex
    • Grosset, C., Chen, C.-Y.A., Xu, N., Sonenberg, N., Jacquemin-Sablon, H., and Shyu, A.-B. 2000. A mechanism for translationally coupled mRNA turnover: Interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex. Cell 103: 29-40.
    • (2000) Cell , vol.103 , pp. 29-40
    • Grosset, C.1    Chen, C.-Y.A.2    Xu, N.3    Sonenberg, N.4    Jacquemin-Sablon, H.5    Shyu, A.-B.6
  • 19
    • 0032889252 scopus 로고    scopus 로고
    • A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice
    • Harris, C.E., Boden, R.A., and Astell, C.R. 1999. A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice. J. Virol. 73: 72-80.
    • (1999) J. Virol. , vol.73 , pp. 72-80
    • Harris, C.E.1    Boden, R.A.2    Astell, C.R.3
  • 20
    • 0025769412 scopus 로고
    • Primary response genes induced by growth factors and tumor promoters
    • Herschman, H.R. 1991. Primary response genes induced by growth factors and tumor promoters. Annu. Rev. Biochem. 60: 281-319.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 281-319
    • Herschman, H.R.1
  • 21
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA: Direct association of erf3/GSPT with polyadenylate-binding protein
    • Hoshino, S., Imai, M., Kobayashi, T., Uchida, N., and Katada, T. 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3′-poly(A) tail of mRNA: Direct association of erf3/GSPT with polyadenylate-binding protein. J. Biol. Chem. 274: 16677-16680.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 22
    • 0033557935 scopus 로고    scopus 로고
    • unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA
    • Hunt, S.L., Hsuan, J.J., Totty, N., and Jackson, R.J. 1999. unr, a cellular cytoplasmic RNA-binding protein with five cold-shock domains, is required for internal initiation of translation of human rhinovirus RNA. Genes & Dev. 15: 437-438.
    • (1999) Genes & Dev. , vol.15 , pp. 437-438
    • Hunt, S.L.1    Hsuan, J.J.2    Totty, N.3    Jackson, R.J.4
  • 23
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation
    • Imataka, H., Gradi, A., and Sonenberg, N. 1998. A newly identified N-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17: 7480-7489.
    • (1998) EMBO J. , vol.17 , pp. 7480-7489
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 24
    • 0029973094 scopus 로고    scopus 로고
    • Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells
    • Jacobson, A. and Peltz, S.W. 1996. Interrelationships of the pathways of mRNA decay and translation in eukaryotic cells. Ann. Rev. Biochem. 65: 693-739.
    • (1996) Ann. Rev. Biochem. , vol.65 , pp. 693-739
    • Jacobson, A.1    Peltz, S.W.2
  • 26
    • 0035787721 scopus 로고    scopus 로고
    • The mRNA closed-loop model: The function of PABP and PABP-interacting proteins in mRNA translation
    • Kahvejian, A., Roy, G., and Sonenberg, N. 2001. The mRNA closed-loop model: The function of PABP and PABP-interacting proteins in mRNA translation. Cold Spring Harb. Symp. Quant. Biol. 66: 293-300.
    • (2001) Cold Spring Harb. Symp. Quant. Biol. , vol.66 , pp. 293-300
    • Kahvejian, A.1    Roy, G.2    Sonenberg, N.3
  • 28
    • 0039535081 scopus 로고    scopus 로고
    • Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease
    • Korner, C.G. and Wahle, E. 1997. Poly(A) tail shortening by a mammalian poly(A)-specific 3′-exoribonuclease. J. Biol. Chem. 272: 10448-10456.
    • (1997) J. Biol. Chem. , vol.272 , pp. 10448-10456
    • Korner, C.G.1    Wahle, E.2
  • 29
    • 0038063499 scopus 로고    scopus 로고
    • Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction
    • Kuhn, U. and Pieler, T. 1996. Xenopus poly(A) binding protein: Functional domains in RNA binding and protein-protein interaction. J. Mol. Biol. 256: 20-30.
    • (1996) J. Mol. Biol. , vol.256 , pp. 20-30
    • Kuhn, U.1    Pieler, T.2
  • 30
    • 0141819096 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities
    • Lejeune, F., Li, X., and Maquat, L. 2003. Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities. Mol. Cell 12: 675-687.
    • (2003) Mol. Cell , vol.12 , pp. 675-687
    • Lejeune, F.1    Li, X.2    Maquat, L.3
  • 31
    • 0036261716 scopus 로고    scopus 로고
    • Regulation of c-myc mRNA decay by translational pausing in a coding region instability determinant
    • Lemm, I. and Ross, J. 2002. Regulation of c-myc mRNA decay by translational pausing in a coding region instability determinant. Mol. Cell. Biol. 22: 3959-3969.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3959-3969
    • Lemm, I.1    Ross, J.2
  • 33
    • 0033565383 scopus 로고    scopus 로고
    • Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element
    • Loflin, P.A., Chen, C.-Y.A., and Shyu, A.-B. 1999a. Unraveling a cytoplasmic role for hnRNP D in the in vivo mRNA destabilization directed by the AU-rich element. Genes & Dev. 13: 1884-1897.
    • (1999) Genes & Dev. , vol.13 , pp. 1884-1897
    • Loflin, P.A.1    Chen, C.-Y.A.2    Shyu, A.-B.3
  • 34
    • 0032847422 scopus 로고    scopus 로고
    • Transcriptional pulsing approaches for analysis of mRNA turnover in mammalian cells
    • Loflin, T.L., Chen, C.-Y.A., Xu, N., and Shyu, A.-B. 1999b. Transcriptional pulsing approaches for analysis of mRNA turnover in mammalian cells. Methods 17: 11-20.
    • (1999) Methods , vol.17 , pp. 11-20
    • Loflin, T.L.1    Chen, C.-Y.A.2    Xu, N.3    Shyu, A.-B.4
  • 35
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus, D.A., Evans, M.C., and Jacobson, A. 2003. Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4: 223.
    • (2003) Genome Biol. , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 36
    • 0034604553 scopus 로고    scopus 로고
    • A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease
    • Martinez, J., Ren, Y., Thuresson, A., Hellman, U., Astrom, J., and Virtanen, A. 2000. A 54-kDa fragment of the poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting poly(A)-specific 3′ exonuclease. J. Biol. Chem. 275: 24222-24230.
    • (2000) J. Biol. Chem. , vol.275 , pp. 24222-24230
    • Martinez, J.1    Ren, Y.2    Thuresson, A.3    Hellman, U.4    Astrom, J.5    Virtanen, A.6
  • 37
    • 0037349339 scopus 로고    scopus 로고
    • The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr
    • Mitchell, S.A., Spriggs, K.A., Cloldwell, M.J., Jackson, R.J., and Willis, A.E. 2003. The Apaf-1 internal ribosome entry segment attains the correct structural conformation for function via interactions with PTB and unr. Mol. Cell 11: 757-771.
    • (2003) Mol. Cell , vol.11 , pp. 757-771
    • Mitchell, S.A.1    Spriggs, K.A.2    Cloldwell, M.J.3    Jackson, R.J.4    Willis, A.E.5
  • 38
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos, Z., Abel, L., Yong, J., Kataoka, N., and Dreyfuss, G. 2001. SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J. 20: 5443-5452.
    • (2001) EMBO J. , vol.20 , pp. 5443-5452
    • Mourelatos, Z.1    Abel, L.2    Yong, J.3    Kataoka, N.4    Dreyfuss, G.5
  • 39
    • 0742288008 scopus 로고    scopus 로고
    • The enzymes and control of eukaryotic mRNa turnover
    • Parker, R. and Song, H. 2004. The enzymes and control of eukaryotic mRNa turnover. Nat. Strut. Mol. Biol. 11: 121-127.
    • (2004) Nat. Strut. Mol. Biol. , vol.11 , pp. 121-127
    • Parker, R.1    Song, H.2
  • 40
    • 0032526417 scopus 로고    scopus 로고
    • RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein
    • Peng, S.-P., Chen, C.-Y., Xu, N., and Shyu, A.-B. 1998. RNA stabilization by the AU-rich element binding protein, HuR, an ELAV protein. EMBO J. 17: 3461-3470.
    • (1998) EMBO J. , vol.17 , pp. 3461-3470
    • Peng, S.-P.1    Chen, C.-Y.2    Xu, N.3    Shyu, A.-B.4
  • 41
    • 0037155135 scopus 로고    scopus 로고
    • Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe2+-mediated cleavage
    • Ren, Y.-G., Martinez, J., and Virtanen, A. 2002. Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe2+-mediated cleavage. J. Biol. Chem. 277: 5982-5987.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5982-5987
    • Ren, Y.-G.1    Martinez, J.2    Virtanen, A.3
  • 43
    • 0028111481 scopus 로고
    • Multiple elements in the c-fos protein-coding region facilitate mRNA deadenylation and decay by a mechanism coupled to translation
    • Schiavi, S.C., Wellington, C.L., Shyu, A.B., Chen, C.Y., Greenberg, M.E., and Belasco, J.G. 1994. Multiple elements in the c-fos protein-coding region facilitate mRNA deadenylation and decay by a mechanism coupled to translation. J. Biol. Chem. 269: 3441-3448.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3441-3448
    • Schiavi, S.C.1    Wellington, C.L.2    Shyu, A.B.3    Chen, C.Y.4    Greenberg, M.E.5    Belasco, J.G.6
  • 44
    • 0034697972 scopus 로고    scopus 로고
    • The double lives of shuttling mRNA binding proteins
    • Shyu, A.B. and Wilkinson, M.F. 2000. The double lives of shuttling mRNA binding proteins. Cell 102: 135-138.
    • (2000) Cell , vol.102 , pp. 135-138
    • Shyu, A.B.1    Wilkinson, M.F.2
  • 45
    • 0024488977 scopus 로고
    • The c-fos mRNA is targeted for rapid decay by two distinct mRNA degradation pathways
    • Shyu, A.B., Greenberg, M.E., and Belasco, J.G. 1989. The c-fos mRNA is targeted for rapid decay by two distinct mRNA degradation pathways. Genes & Dev. 3: 60-72.
    • (1989) Genes & Dev. , vol.3 , pp. 60-72
    • Shyu, A.B.1    Greenberg, M.E.2    Belasco, J.G.3
  • 46
    • 0026027749 scopus 로고
    • Two distinct destabilizing elements in the c-fos message trigger deadenylation as a first step in rapid mRNA decay
    • Shyu, A.-B., Belasco, J.G., and Greenberg, M.G. 1991. Two distinct destabilizing elements in the c-fos message trigger deadenylation as a first step in rapid mRNA decay. Genes & Dev. 5: 221-232.
    • (1991) Genes & Dev. , vol.5 , pp. 221-232
    • Shyu, A.-B.1    Belasco, J.G.2    Greenberg, M.G.3
  • 47
    • 0038785142 scopus 로고    scopus 로고
    • Analysis of mRNA decay in mammalian cells
    • (ed., I. Lefkovits). Academic Press, London
    • Shyu, A.B., Garcia-Sanz, J.A., and Mullner, E. 1996. Analysis of mRNA decay in mammalian cells. In: The immunology methods manual (ed., I. Lefkovits), pp. 450-462. Academic Press, London.
    • (1996) The Immunology Methods Manual , pp. 450-462
    • Shyu, A.B.1    Garcia-Sanz, J.A.2    Mullner, E.3
  • 49
    • 0035830508 scopus 로고    scopus 로고
    • The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae
    • Tucker, M., Valencia-Sanchez, M.A., Staples, R.R., Chen, J., Denis, C.L., and Parker, R. 2001. The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae. Cell 104: 377-386.
    • (2001) Cell , vol.104 , pp. 377-386
    • Tucker, M.1    Valencia-Sanchez, M.A.2    Staples, R.R.3    Chen, J.4    Denis, C.L.5    Parker, R.6
  • 50
    • 0037086657 scopus 로고    scopus 로고
    • Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae
    • Tucker, M., Staples, R.R., Valencia-Sanchez, M.A., Muhlrad, D., and Parker, R. 2002. Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae. EMBO J. 21: 1427-1436.
    • (2002) EMBO J. , vol.21 , pp. 1427-1436
    • Tucker, M.1    Staples, R.R.2    Valencia-Sanchez, M.A.3    Muhlrad, D.4    Parker, R.5
  • 51
    • 0347093310 scopus 로고    scopus 로고
    • Identification of a human cytoplasmic Poly(A) nuclease complex stimulated by Poly(A)-binding protein
    • Uchida, N., Hoshino, S.-i., and Katada, T. 2004. Identification of a human cytoplasmic Poly(A) nuclease complex stimulated by Poly(A)-binding protein. J. Biol. Chem. 279: 1383-1391.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1383-1391
    • Uchida, N.1    Hoshino, S.-I.2    Katada, T.3
  • 52
    • 0037155584 scopus 로고    scopus 로고
    • Exosome-mediated recognition and degradation of mRNAs lacking a termination codon
    • van Hoof, A., Frischmeyer, P.A., Dietz, H.C., and Parker, R. 2002. Exosome-mediated recognition and degradation of mRNAs lacking a termination codon. Science 295: 2262-2264.
    • (2002) Science , vol.295 , pp. 2262-2264
    • Van Hoof, A.1    Frischmeyer, P.A.2    Dietz, H.C.3    Parker, R.4
  • 53
    • 0027182796 scopus 로고
    • The destabilizing elements in the coding region of c-fos mRNA are recognized as RNA
    • Wellington, C.L., Greenberg, M.E., and Belasco, J.G. 1993. The destabilizing elements in the coding region of c-fos mRNA are recognized as RNA. Mol. Cell. Biol. 13: 5034-5042.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5034-5042
    • Wellington, C.L.1    Greenberg, M.E.2    Belasco, J.G.3
  • 55
    • 0034806974 scopus 로고    scopus 로고
    • Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover
    • Xu, N., Chen, C., and Shyu, A. 2001. Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol. Cell. Biol. 21: 6960-6971.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6960-6971
    • Xu, N.1    Chen, C.2    Shyu, A.3
  • 56
    • 0024291284 scopus 로고
    • Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin
    • Yen, T.J., Machlin, P.S., and Cleveland, D.W. 1988. Autoregulated instability of β-tubulin mRNAs by recognition of the nascent amino terminus of β-tubulin. Nature 334: 580-585.
    • (1988) Nature , vol.334 , pp. 580-585
    • Yen, T.J.1    Machlin, P.S.2    Cleveland, D.W.3
  • 57
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y. and Deutscher, M.P. 2001. Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution. Nucl. Acids Res. 29: 1017-1026.
    • (2001) Nucl. Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.