메뉴 건너뛰기




Volumn 71, Issue , 2006, Pages 537-543

Regulation of poly(A)-binding protein through PABP-interacting proteins

Author keywords

[No Author keywords available]

Indexed keywords

INITIATION FACTOR 3; INITIATION FACTOR 4A; PABP INTERACTING PROTEIN; POLYADENYLIC ACID BINDING PROTEIN; UNCLASSIFIED DRUG; CAPPED RNA; INITIATION FACTOR; MESSENGER RNA; REPRESSOR PROTEIN; RNA BINDING PROTEIN;

EID: 34250674933     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.2006.71.061     Document Type: Conference Paper
Times cited : (101)

References (68)
  • 1
    • 0022766180 scopus 로고
    • mRNA polyadenylate-binding protein: Gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence
    • Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., and Dreyfuss G. 1986. mRNA polyadenylate-binding protein: Gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol. Cell. Biol. 6: 2932.
    • (1986) Mol. Cell. Biol , vol.6 , pp. 2932
    • Adam, S.A.1    Nakagawa, T.2    Swanson, M.S.3    Woodruff, T.K.4    Dreyfuss, G.5
  • 3
    • 33746577884 scopus 로고    scopus 로고
    • Regulation of poly(A) binding protein function in translation: Characterization of the Paip2 homolog, Paip2B
    • Berlanga J.J., Baass A., and Sonenberg N. 2006. Regulation of poly(A) binding protein function in translation: Characterization of the Paip2 homolog, Paip2B. RNA 12: 1556.
    • (2006) RNA , vol.12 , pp. 1556
    • Berlanga, J.J.1    Baass, A.2    Sonenberg, N.3
  • 4
    • 0024323801 scopus 로고
    • Poly(A), poly(A) binding protein and the regulation of mRNA stability
    • Bernstein P. and Ross J. 1989. Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem. Sci. 14: 373.
    • (1989) Trends Biochem. Sci , vol.14 , pp. 373
    • Bernstein, P.1    Ross, J.2
  • 5
    • 0025762042 scopus 로고
    • The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities
    • Burd C.G., Matunis E.L., and Dreyfuss G. 1991. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11: 3419.
    • (1991) Mol. Cell. Biol , vol.11 , pp. 3419
    • Burd, C.G.1    Matunis, E.L.2    Dreyfuss, G.3
  • 6
    • 21444446061 scopus 로고    scopus 로고
    • Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection
    • Byrd M.P., Zamora M., and Lloyd R.E. 2005. Translation of eukaryotic translation initiation factor 4GI (eIF4GI) proceeds from multiple mRNAs containing a novel cap-dependent internal ribosome entry site (IRES) that is active during poliovirus infection. J. Biol. Chem. 280: 18610.
    • (2005) J. Biol. Chem , vol.280 , pp. 18610
    • Byrd, M.P.1    Zamora, M.2    Lloyd, R.E.3
  • 7
    • 0032585636 scopus 로고    scopus 로고
    • Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs
    • Callaghan M.J., Russell A.J., Woollatt E., Sutherland G.R., Sutherland R.L., and Watts C.K. 1998. Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs. Oncogene 17: 3479.
    • (1998) Oncogene , vol.17 , pp. 3479
    • Callaghan, M.J.1    Russell, A.J.2    Woollatt, E.3    Sutherland, G.R.4    Sutherland, R.L.5    Watts, C.K.6
  • 8
    • 0028788194 scopus 로고
    • AU-rich elements: Characterization and importance in mRNA degradation
    • Chen C.Y. and Shyu A.B. 1995. AU-rich elements: Characterization and importance in mRNA degradation. Trends Biochem. Sci. 20: 465.
    • (1995) Trends Biochem. Sci , vol.20 , pp. 465
    • Chen, C.Y.1    Shyu, A.B.2
  • 9
    • 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.
    • (1992) Mol. Cell. Biol , vol.12 , pp. 5748
    • Chen, C.Y.1    You, Y.2    Shyu, A.B.3
  • 10
    • 23044468281 scopus 로고    scopus 로고
    • The DAZL family proteins are PABP-binding proteins that regulate translation in germ cells
    • Collier B., Gorgoni B., Loveridge C., Cooke H.J., and Gray N.K. 2005. The DAZL family proteins are PABP-binding proteins that regulate translation in germ cells. EMBO J. 24: 2656.
    • (2005) EMBO J , vol.24 , pp. 2656
    • Collier, B.1    Gorgoni, B.2    Loveridge, C.3    Cooke, H.J.4    Gray, N.K.5
  • 11
    • 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.
    • (1998) Nature , vol.392 , pp. 520
    • Craig, A.W.1    Haghighat, A.2    Yu, A.T.3    Sonenberg, N.4
  • 12
    • 0035836636 scopus 로고    scopus 로고
    • X-ray structure of the human hyperplastic discs protein: An ortholog of the carboxyl terminus domain of poly(A)-binding protein
    • Deo R.C., Sonenberg N., and Burley S.K. 2001. X-ray structure of the human hyperplastic discs protein: An ortholog of the carboxyl terminus domain of poly(A)-binding protein. Proc. Natl. Acad. Sci. 98: 4414.
    • (2001) Proc. Natl. Acad. Sci , vol.98 , pp. 4414
    • Deo, R.C.1    Sonenberg, N.2    Burley, S.K.3
  • 13
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • Deo R.C., Bonanno J.B., Sonenberg N., and Burley S.K. 1999. Recognition of polyadenylate RNA by the poly(A)-binding protein. Cell 98: 835.
    • (1999) Cell , vol.98 , pp. 835
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 14
    • 0017143935 scopus 로고
    • The translational capacity of deadenylated ovalbumin messenger RNA
    • Doel M.T. and Carey N.H. 1976. The translational capacity of deadenylated ovalbumin messenger RNA. Cell 8: 51.
    • (1976) Cell , vol.8 , pp. 51
    • Doel, M.T.1    Carey, N.H.2
  • 15
    • 0026038913 scopus 로고
    • The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie D.R. 1991. The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency. Genes Dev. 5: 2108.
    • (1991) Genes Dev , vol.5 , pp. 2108
    • Gallie, D.R.1
  • 17
    • 0028340737 scopus 로고
    • The mRNA poly(A)-binding protein: Localization, abundance, and RNA-binding specificity
    • Görlach M., Burd C.G., and Dreyfuss G. 1994. The mRNA poly(A)-binding protein: Localization, abundance, and RNA-binding specificity. Exp. Cell Res. 211: 400.
    • (1994) Exp. Cell Res , vol.211 , pp. 400
    • Görlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 18
    • 0141953690 scopus 로고    scopus 로고
    • Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: Role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2
    • Gouyon F., Onesto C., Dalet V., Pages G., Leturque A., and Brot-Laroche E. 2003. Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: Role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2. Biochem J. 375: 167.
    • (2003) Biochem J , vol.375 , pp. 167
    • Gouyon, F.1    Onesto, C.2    Dalet, V.3    Pages, G.4    Leturque, A.5    Brot-Laroche, E.6
  • 19
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray N.K., Coller J.M., Dickson K.S., and Wickens M. 2000. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19: 4723.
    • (2000) EMBO J , vol.19 , pp. 4723
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 20
    • 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., 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.
    • (2000) Cell , vol.103 , pp. 29
    • Grosset, C.1    Chen, C.Y.2    Xu, N.3    Sonenberg, N.4    Jacquemin-Sablon, H.5    Shyu, A.B.6
  • 22
    • 0034103227 scopus 로고    scopus 로고
    • Functions of Lsm proteins in mRNA degradation and splicing
    • He W. and Parker R. 2000. Functions of Lsm proteins in mRNA degradation and splicing. Curr. Opin. Cell Biol. 12: 346.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 346
    • He, W.1    Parker, R.2
  • 23
    • 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.
    • (1999) J. Biol. Chem , vol.274 , pp. 16677
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 24
  • 25
    • 0028907874 scopus 로고
    • A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase
    • Huibregtse J.M., Scheffner M., Beaudenon S., and Howley P.M. 1995. A family of proteins structurally and functionally related to the E6-AP ubiquitin-protein ligase. Proc. Natl. Acad. Sci. 92: 2563.
    • (1995) Proc. Natl. Acad. Sci , vol.92 , pp. 2563
    • Huibregtse, J.M.1    Scheffner, M.2    Beaudenon, S.3    Howley, P.M.4
  • 26
    • 0028034493 scopus 로고
    • Capdependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae
    • Iizuka N., Najita L., Franzusoff A., and Sarnow P. 1994. Capdependent and cap-independent translation by internal initiation of mRNAs in cell extracts prepared from Saccharomyces cerevisiae. Mol. Cell. Biol. 14: 7322.
    • (1994) Mol. Cell. Biol , vol.14 , pp. 7322
    • Iizuka, N.1    Najita, L.2    Franzusoff, A.3    Sarnow, P.4
  • 27
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H. and Sonenberg N. 1997. Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A. Mol. Cell. Biol. 17: 6940.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 6940
    • Imataka, H.1    Sonenberg, N.2
  • 28
    • 0032535452 scopus 로고    scopus 로고
    • A newly identified amino-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 amino-terminal amino acid sequence of human eIF4G binds poly(A)-binding protein and functions in poly(A)-dependent translation. EMBO J. 17: 7480.
    • (1998) EMBO J , vol.17 , pp. 7480
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 29
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation: The closed-loop model
    • ed. J.W.B. Hershey et al, p, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Jacobson A. 1996. Poly(A) metabolism and translation: The closed-loop model. In Translational control (ed. J.W.B. Hershey et al.), p. 451. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (1996) Translational control , pp. 451
    • Jacobson, A.1
  • 30
    • 0021111301 scopus 로고
    • Possible involvement of poly(A) in protein synthesis
    • Jacobson A. and Favreau M. 1983. Possible involvement of poly(A) in protein synthesis. Nucleic Acids Res. 11: 6353.
    • (1983) Nucleic Acids Res , vol.11 , pp. 6353
    • Jacobson, A.1    Favreau, M.2
  • 31
    • 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 Harbor Symp. Quant. Biol. 66: 293.
    • (2001) Cold Spring Harbor Symp. Quant. Biol , vol.66 , pp. 293
    • Kahvejian, A.1    Roy, G.2    Sonenberg, N.3
  • 32
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • Kahvejian A., Svitkin Y.V., Sukarieh R., M'Boutchou M.N., and Sonenberg N. 2005. Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms. Genes Dev. 19: 104.
    • (2005) Genes Dev , vol.19 , pp. 104
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.N.4    Sonenberg, N.5
  • 36
    • 0034457113 scopus 로고    scopus 로고
    • The ortholog of human ataxin-2 is essential for early embryonic patterning in C. elegans
    • Kiehl T.R., Shibata H., and Pulst S.M. 2000. The ortholog of human ataxin-2 is essential for early embryonic patterning in C. elegans. J. Mol. Neurosci. 15: 231.
    • (2000) J. Mol. Neurosci , vol.15 , pp. 231
    • Kiehl, T.R.1    Shibata, H.2    Pulst, S.M.3
  • 38
    • 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.
    • (1996) J. Mol. Biol , vol.256 , pp. 20
    • Kuhn, U.1    Pieler, T.2
  • 39
    • 0030952218 scopus 로고    scopus 로고
    • Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity
    • Le H., Tanguay R.L., Balasta M.L., Wei C.C., Browning K.S., Metz A.M., Goss D.J., and Gallie D.R. 1997. Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity. J. Biol. Chem. 272: 16247.
    • (1997) J. Biol. Chem , vol.272 , pp. 16247
    • Le, H.1    Tanguay, R.L.2    Balasta, M.L.3    Wei, C.C.4    Browning, K.S.5    Metz, A.M.6    Goss, D.J.7    Gallie, D.R.8
  • 40
    • 0031724595 scopus 로고    scopus 로고
    • Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation
    • Mangus D.A., Amrani N., and Jacobson A. 1998. Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation. Mol. Cell. Biol. 18: 7383.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 7383
    • Mangus, D.A.1    Amrani, N.2    Jacobson, A.3
  • 41
    • 36348996412 scopus 로고    scopus 로고
    • Origins and principles of translational control
    • ed. M.B. Mathews et al, p, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Mathews M.B., Sonenberg N., and Hershey J.W.B. 2007. Origins and principles of translational control. In Translational control in biology and medicine (ed. M.B. Mathews et al.), p. 1. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2007) Translational control in biology and medicine , pp. 1
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.B.3
  • 42
    • 0033957406 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the carboxyl terminus one-third functions as a modulatory region
    • Morino S., Imataka H., Svitkin Y.V., Pestova T.V., and Sonenberg N. 2000. Eukaryotic translation initiation factor 4E (eIF4E) binding site and the middle one-third of eIF4GI constitute the core domain for cap-dependent translation, and the carboxyl terminus one-third functions as a modulatory region. Mol. Cell. Biol. 20: 468.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 468
    • Morino, S.1    Imataka, H.2    Svitkin, Y.V.3    Pestova, T.V.4    Sonenberg, N.5
  • 43
    • 0025310854 scopus 로고
    • mRNA poly(A) tail, a 3? enhancer of translational initiation
    • Munroe D. and Jacobson A. 1990a. mRNA poly(A) tail, a 3? enhancer of translational initiation. Mol. Cell. Biol. 10: 3441.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 3441
    • Munroe, D.1    Jacobson, A.2
  • 44
    • 0025112854 scopus 로고
    • Tales of poly(A): A review
    • - . 1990b. Tales of poly(A): A review. Gene 91: 151.
    • (1990) Gene , vol.91 , pp. 151
    • Munroe, D.1    Jacobson, A.2
  • 45
    • 14244256765 scopus 로고    scopus 로고
    • Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: Implication of Tob in translational control
    • Okochi K., Suzuki T., Inoue J., Matsuda S., and Yamamoto T. 2005. Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: Implication of Tob in translational control. Genes Cells 10: 151.
    • (2005) Genes Cells , vol.10 , pp. 151
    • Okochi, K.1    Suzuki, T.2    Inoue, J.3    Matsuda, S.4    Yamamoto, T.5
  • 46
    • 4544245080 scopus 로고    scopus 로고
    • Poly(A)-binding protein-interacting protein 2, a strong regulator of vascular endothelial growth factor mRNA
    • Onesto C., Berra E., Grepin R., and Pages G. 2004. Poly(A)-binding protein-interacting protein 2, a strong regulator of vascular endothelial growth factor mRNA. J. Biol. Chem. 279: 34217.
    • (2004) J. Biol. Chem , vol.279 , pp. 34217
    • Onesto, C.1    Berra, E.2    Grepin, R.3    Pages, G.4
  • 47
    • 0033153302 scopus 로고    scopus 로고
    • The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms
    • Otero L.J., Ashe M.P., and Sachs A.B. 1999. The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms. EMBO J. 18: 3153.
    • (1999) EMBO J , vol.18 , pp. 3153
    • Otero, L.J.1    Ashe, M.P.2    Sachs, A.B.3
  • 48
    • 0036773058 scopus 로고    scopus 로고
    • Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase induced in germ cells of the rat testis and similar to the Drosophila hyperplastic discs gene
    • Oughtred R., Bedard N., Adegoke O.A., Morales C.R., Trasler J., Rajapurohitam V., and Wing S.S. 2002. Characterization of rat100, a 300-kilodalton ubiquitin-protein ligase induced in germ cells of the rat testis and similar to the Drosophila hyperplastic discs gene. Endocrinology 143: 3740.
    • (2002) Endocrinology , vol.143 , pp. 3740
    • Oughtred, R.1    Bedard, N.2    Adegoke, O.A.3    Morales, C.R.4    Trasler, J.5    Rajapurohitam, V.6    Wing, S.S.7
  • 49
    • 0021139622 scopus 로고
    • Translational control during early Dictyostelium development: Possible involvement of poly(A) sequences
    • Palatnik C.M., Wilkins C., and Jacobson A. 1984. Translational control during early Dictyostelium development: Possible involvement of poly(A) sequences. Cell 36: 1017.
    • (1984) Cell , vol.36 , pp. 1017
    • Palatnik, C.M.1    Wilkins, C.2    Jacobson, A.3
  • 50
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in eukaryotes
    • ed. M.B. Mathews et al, p, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Pestova T.V., Lorsch J.R., and Hellen C.U. 2007. The mechanism of translation initiation in eukaryotes. In Translational control in biology and medicine (ed. M.B. Mathews et al.), p. 87. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2007) Translational control in biology and medicine , pp. 87
    • Pestova, T.V.1    Lorsch, J.R.2    Hellen, C.U.3
  • 51
    • 0033521535 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E
    • Pyronnet S., Imataka H., Gingras A.-C., Fukunaga R., Hunter T., and Sonenberg N. 1999. Human eukaryotic translation initiation factor 4G (eIF4G) recruits Mnk1 to phosphorylate eIF4E. EMBO J. 18: 270.
    • (1999) EMBO J , vol.18 , pp. 270
    • Pyronnet, S.1    Imataka, H.2    Gingras, A.-C.3    Fukunaga, R.4    Hunter, T.5    Sonenberg, N.6
  • 52
    • 1642499397 scopus 로고    scopus 로고
    • The Drosophila poly(A) binding protein-interacting protein, dPaip2, is a novel effector of cell growth
    • Roy G., Miron M., Khaleghpour K., Lasko P., and Sonenberg N. 2004. The Drosophila poly(A) binding protein-interacting protein, dPaip2, is a novel effector of cell growth. Mol. Cell. Biol. 24: 1143.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 1143
    • Roy, G.1    Miron, M.2    Khaleghpour, K.3    Lasko, P.4    Sonenberg, N.5
  • 54
    • 0002411516 scopus 로고    scopus 로고
    • Physical and functional interactions between the mRNA cap structure and the poly(A) tail
    • ed. N. Sonenberg et al, p, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Sachs A. 2000. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. In Translational control of gene expression (ed. N. Sonenberg et al.), p. 447. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2000) Translational control of gene expression , pp. 447
    • Sachs, A.1
  • 55
    • 0024416021 scopus 로고
    • The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunitdependent translation initiation
    • Sachs A.B. and Davis R.W. 1989. The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunitdependent translation initiation. Cell 58: 857.
    • (1989) Cell , vol.58 , pp. 857
    • Sachs, A.B.1    Davis, R.W.2
  • 56
    • 0025271804 scopus 로고
    • Translation initiation and ribosomal biogenesis: Involvement of a putative rRNA helicase and RPL46
    • - . 1990. Translation initiation and ribosomal biogenesis: Involvement of a putative rRNA helicase and RPL46. Science 247: 1077.
    • (1990) Science , vol.247 , pp. 1077
    • Sachs, A.B.1    Davis, R.W.2
  • 57
    • 0023405161 scopus 로고
    • A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability
    • Sachs A.B., Davis R.W., and Kornberg R.D. 1987. A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability. Mol. Cell. Biol. 7: 3268.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 3268
    • Sachs, A.B.1    Davis, R.W.2    Kornberg, R.D.3
  • 58
    • 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.
    • (1994) J. Biol. Chem , vol.269 , pp. 3441
    • Schiavi, S.C.1    Wellington, C.L.2    Shyu, A.B.3    Chen, C.Y.4    Greenberg, M.E.5    Belasco, J.G.6
  • 59
    • 0024488977 scopus 로고
    • The c-fos transcript 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 transcript is targeted for rapid decay by two distinct mRNA degradation pathways. Genes Dev. 3: 60.
    • (1989) Genes Dev , vol.3 , pp. 60
    • Shyu, A.B.1    Greenberg, M.E.2    Belasco, J.G.3
  • 60
    • 2142826526 scopus 로고    scopus 로고
    • An efficient system for cap- and poly(A)-dependent translation in vitro
    • Svitkin Y.V. and Sonenberg N. 2004. An efficient system for cap- and poly(A)-dependent translation in vitro. Methods Mol. Biol. 257: 155.
    • (2004) Methods Mol. Biol , vol.257 , pp. 155
    • Svitkin, Y.V.1    Sonenberg, N.2
  • 61
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun S.Z. and Sachs A.B. 1995. A common function for mRNA 5′ and 3′ ends in translation initiation in yeast. Genes Dev. 9: 2997.
    • (1995) Genes Dev , vol.9 , pp. 2997
    • Tarun, S.Z.1    Sachs, A.B.2
  • 62
    • 12644303224 scopus 로고    scopus 로고
    • Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G
    • - . 1996. Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G. EMBO J. 15: 7168.
    • (1996) EMBO J , vol.15 , pp. 7168
    • Tarun, S.Z.1    Sachs, A.B.2
  • 63
    • 0037184899 scopus 로고    scopus 로고
    • The interaction between the eukaryotic releasing factor eRF3/GSPT and poly adenylate-binding protein is important for translation initiation
    • Uchida N., Hoshino S., Imataka H., Sonenberg N., and Katada T. 2002a. The interaction between the eukaryotic releasing factor eRF3/GSPT and poly adenylate-binding protein is important for translation initiation. J. Biol. Chem. 277: 50286.
    • (2002) J. Biol. Chem , vol.277 , pp. 50286
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 64
    • 0037184899 scopus 로고    scopus 로고
    • A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation
    • - . 2002b. A novel role of the mammalian GSPT/eRF3 associating with poly(A)-binding protein in Cap/Poly(A)-dependent translation. J. Biol. Chem. 277: 50286.
    • (2002) J. Biol. Chem , vol.277 , pp. 50286
    • Uchida, N.1    Hoshino, S.2    Imataka, H.3    Sonenberg, N.4    Katada, T.5
  • 65
    • 0034699248 scopus 로고    scopus 로고
    • Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation
    • Wakiyama M., Imataka H., and Sonenberg N. 2000. Interaction of eIF4G with poly(A)-binding protein stimulates translation and is critical for Xenopus oocyte maturation. Curr. Biol. 10: 1147.
    • (2000) Curr. Biol , vol.10 , pp. 1147
    • Wakiyama, M.1    Imataka, H.2    Sonenberg, N.3
  • 66
    • 0002068909 scopus 로고    scopus 로고
    • Translational control of developmental decisions
    • ed. N. Sonenberg et al, p, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wickens M., Goodwin E.B., Kimble J., Strickland S., and Hentze M.W. 2000. Translational control of developmental decisions. In Translational control of gene expression (ed. N. Sonenberg et al.), p. 295. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2000) Translational control of gene expression , pp. 295
    • Wickens, M.1    Goodwin, E.B.2    Kimble, J.3    Strickland, S.4    Hentze, M.W.5
  • 67
    • 0026026139 scopus 로고
    • The protein-coding region of cmyc mRNA contains a sequence that specifies rapid mRNA turnover and induction by protein synthesis inhibitors
    • Wisdom R. and Lee W. 1991. The protein-coding region of cmyc mRNA contains a sequence that specifies rapid mRNA turnover and induction by protein synthesis inhibitors. Genes Dev. 5: 232.
    • (1991) Genes Dev , vol.5 , pp. 232
    • Wisdom, R.1    Lee, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.