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Volumn 66, Issue , 2001, Pages 329-336

Translational control of 15-lipoxygenase and msl-2 mRNAs: Single regulators or corepressor assemblies?

Author keywords

[No Author keywords available]

Indexed keywords

ARACHIDONATE 15 LIPOXYGENASE; GENE PRODUCT; MESSENGER RNA; PROTEIN MSL 2; REPRESSOR PROTEIN; UNCLASSIFIED DRUG; COREPRESSOR PROTEIN; MESSENGER RNA MSL 2;

EID: 0035787702     PISSN: 00917451     EISSN: None     Source Type: Book Series    
DOI: 10.1101/sqb.2001.66.329     Document Type: Conference Paper
Times cited : (8)

References (65)
  • 1
    • 0025963078 scopus 로고
    • Control of the sperm-oocyte switch in Caenorhabditis elegans hermaphrodites by the fem-3 3′ untranslated region
    • Ahringer J. and Kimble J. 1991. Control of the sperm-oocyte switch in Caenorhabditis elegans hermaphrodites by the fem-3 3′ untranslated region, Nature 349: 346.
    • (1991) Nature , vol.349 , pp. 346
    • Ahringer, J.1    Kimble, J.2
  • 2
    • 0034176145 scopus 로고    scopus 로고
    • Translational control of cyclin B1 mRNA during meiotic maturation: Coordinated repression and cytoplasmic polyadenylation
    • Barkoff A., Dickson K., Gray N., and Wickens M. 2000. Translational control of cyclin B1 mRNA during meiotic maturation: Coordinated repression and cytoplasmic polyadenylation. Dev. Biol. 220: 97.
    • (2000) Dev. Biol. , vol.220 , pp. 97
    • Barkoff, A.1    Dickson, K.2    Gray, N.3    Wickens, M.4
  • 3
    • 0030678550 scopus 로고    scopus 로고
    • The regulation of the Drosophila msl-2 gene reveals a function for Sex-lethal in translational control
    • Bashaw G. and Baker B. 1997. The regulation of the Drosophila msl-2 gene reveals a function for Sex-lethal in translational control. Cell 89: 789.
    • (1997) Cell , vol.89 , pp. 789
    • Bashaw, G.1    Baker, B.2
  • 4
    • 0024819020 scopus 로고
    • Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA
    • Casey J., Koeller D., Ramin V., Klausner R., and Harford J. 1989. Iron regulation of transferrin receptor mRNA levels requires iron-responsive elements and a rapid turnover determinant in the 3′ untranslated region of the mRNA. EMBO J. 8: 3693.
    • (1989) EMBO J. , vol.8 , pp. 3693
    • Casey, J.1    Koeller, D.2    Ramin, V.3    Klausner, R.4    Harford, J.5
  • 5
    • 0034105305 scopus 로고    scopus 로고
    • Control of oskar mRNA translation by Bruno in a novel cell-free system from Drosophila ovaries
    • Castagnetti S., Hentze M., Ephrussi A., and Gebauer F. 2000. Control of oskar mRNA translation by Bruno in a novel cell-free system from Drosophila ovaries. Development 127: 1063.
    • (2000) Development , vol.127 , pp. 1063
    • Castagnetti, S.1    Hentze, M.2    Ephrussi, A.3    Gebauer, F.4
  • 6
    • 0035949575 scopus 로고    scopus 로고
    • Poly(A)-independent regulation of maternal hunchback translation in the Drosophila embryo
    • Chagnovich D. and Lehmann R. 2001. Poly(A)-independent regulation of maternal hunchback translation in the Drosophila embryo. Proc. Natl. Acad. Sci. 98: 11359.
    • (2001) Proc. Natl. Acad. Sci. , vol.98 , pp. 11359
    • Chagnovich, D.1    Lehmann, R.2
  • 7
    • 0031046736 scopus 로고    scopus 로고
    • A CCHC metal-binding domain in Nanos is essential for translational regulation
    • Curtis D., Treiber D., Tao F., Zamore P., Williamson J., and Lehmann R. 1997. A CCHC metal-binding domain in Nanos is essential for translational regulation. EMBO J. 16: 834.
    • (1997) EMBO J. , vol.16 , pp. 834
    • Curtis, D.1    Treiber, D.2    Tao, F.3    Zamore, P.4    Williamson, J.5    Lehmann, R.6
  • 8
    • 0033560759 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA
    • de Moor C. and Richter J. 1999. Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA. EMBO J. 18: 2294.
    • (1999) EMBO J. , vol.18 , pp. 2294
    • De Moor, C.1    Richter, J.2
  • 9
    • 0035210646 scopus 로고    scopus 로고
    • Translational control in vertebrate development
    • -. 2001. Translational control in vertebrate development. Int. Rev. Cytol. 203: 567.
    • (2001) Int. Rev. Cytol. , vol.203 , pp. 567
  • 10
    • 0026038913 scopus 로고
    • The cap and poly(A) tail function synergistically to regulate mRNA translational efficiency
    • Gallie D. 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.1
  • 11
    • 0031894413 scopus 로고    scopus 로고
    • The Drosophila splicing regulator sex-lethal directly inhibits translation of male-specific-lethal-2 mRNA
    • Gebauer F., Merendino L., Hentze M., and Valcárcel J. 1998. The Drosophila splicing regulator sex-lethal directly inhibits translation of male-specific-lethal-2 mRNA. RNA 4: 142.
    • (1998) RNA , vol.4 , pp. 142
    • Gebauer, F.1    Merendino, L.2    Hentze, M.3    Valcárcel, J.4
  • 12
    • 0033229825 scopus 로고    scopus 로고
    • Translational control of dosage compensation in Drosophila by Sex-lethal: Cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail
    • Gebauer F., Corona D., Preiss T., Becker P., and Hentze M. 1999. Translational control of dosage compensation in Drosophila by Sex-lethal: Cooperative silencing via the 5′ and 3′ UTRs of msl-2 mRNA is independent of the poly(A) tail. EMBO J. 18: 6146.
    • (1999) EMBO J. , vol.18 , pp. 6146
    • Gebauer, F.1    Corona, D.2    Preiss, T.3    Becker, P.4    Hentze, M.5
  • 13
    • 0032834055 scopus 로고    scopus 로고
    • eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • Gingras A., Raught B., and Sonenberg N. 1999. eIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation. Annu. Rev. Biochem. 68: 913.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 913
    • Gingras, A.1    Raught, B.2    Sonenberg, N.3
  • 14
    • 0028059555 scopus 로고
    • Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs
    • Gray N. and Hentze M. 1994. Iron regulatory protein prevents binding of the 43S translation pre-initiation complex to ferritin and eALAS mRNAs. EMBO J. 13: 3882.
    • (1994) EMBO J. , vol.13 , pp. 3882
    • Gray, N.1    Hentze, M.2
  • 15
    • 0034721667 scopus 로고    scopus 로고
    • CPEB, maskin and cyclin B1 mRNA at the mitotic apparatus: Implications for local translational control of cell division
    • Groisman I., Huang Y.-S., Mendez R., Cao Q., Theurkauf W., and Richter J. 2000. CPEB, maskin and cyclin B1 mRNA at the mitotic apparatus: Implications for local translational control of cell division. Cell 103: 435.
    • (2000) Cell , vol.103 , pp. 435
    • Groisman, I.1    Huang, Y.-S.2    Mendez, R.3    Cao, Q.4    Theurkauf, W.5    Richter, J.6
  • 16
    • 2642633741 scopus 로고    scopus 로고
    • Localization-dependent translation requires a functional interaction between the 5′ and 3′ ends of oskar mRNA
    • Gunkel N., Yano T., Markussen F.-H., Olsen L., and Ephrussi A. 1998. Localization-dependent translation requires a functional interaction between the 5′ and 3′ ends of oskar mRNA. Genes Dev. 12: 1652.
    • (1998) Genes Dev. , vol.12 , pp. 1652
    • Gunkel, N.1    Yano, T.2    Markussen, F.-H.3    Olsen, L.4    Ephrussi, A.5
  • 17
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze M. and Kühn L. 1996. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. 93: 8175.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 8175
    • Hentze, M.1    Kühn, L.2
  • 18
    • 0023797880 scopus 로고
    • Activation of translationally inactive lipoxygenase mRNP particles from rabbit reticulocytes
    • Höhne M., Thiele B., Prehn S., Giessmann E., Nack B., and Rapoport S. 1988. Activation of translationally inactive lipoxygenase mRNP particles from rabbit reticulocytes. Biomed. Biochim. Acta 47: 75.
    • (1988) Biomed. Biochim. Acta , vol.47 , pp. 75
    • Höhne, M.1    Thiele, B.2    Prehn, S.3    Giessmann, E.4    Nack, B.5    Rapoport, S.6
  • 19
    • 0028034493 scopus 로고
    • Cap-dependent 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. Cap-dependent 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
  • 20
    • 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.
    • (1998) EMBO J. , vol.17 , pp. 7480
    • Imataka, H.1    Gradi, A.2    Sonenberg, N.3
  • 21
    • 0035320036 scopus 로고    scopus 로고
    • mRNA localization: Message on the move
    • Jansen R. 2001. mRNA localization: Message on the move. Nat. Rev. Mol. Cell Biol. 2: 247.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 247
    • Jansen, R.1
  • 22
    • 0030913367 scopus 로고    scopus 로고
    • Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism
    • Kelley R., Wang J., Bell L., and Kuroda M. 1997. Sex lethal controls dosage compensation in Drosophila by a non-splicing mechanism. Nature 387: 195.
    • (1997) Nature , vol.387 , pp. 195
    • Kelley, R.1    Wang, J.2    Bell, L.3    Kuroda, M.4
  • 23
    • 0029063585 scopus 로고
    • Expression of Msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila
    • Kelley R., Solovyeva I., Lyman L., Richman R., Solovyev V., and Kuroda M. 1995. Expression of Msl-2 causes assembly of dosage compensation regulators on the X chromosomes and female lethality in Drosophila. Cell 81: 867.
    • (1995) Cell , vol.81 , pp. 867
    • Kelley, R.1    Solovyeva, I.2    Lyman, L.3    Richman, R.4    Solovyev, V.5    Kuroda, M.6
  • 24
    • 0033598198 scopus 로고    scopus 로고
    • Nanos-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans
    • Kraemer B., Crittenden S., Gallegos M., Moulder G., Barstead R., Kimble J., and Wickens M. 1999. Nanos-3 and FBF proteins physically interact to control the sperm-oocyte switch in Caenorhabditis elegans. Curr. Biol. 9: 1009.
    • (1999) Curr. Biol. , vol.9 , pp. 1009
    • Kraemer, B.1    Crittenden, S.2    Gallegos, M.3    Moulder, G.4    Barstead, R.5    Kimble, J.6    Wickens, M.7
  • 25
    • 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., Balasta M., Wei C., Browning K., Metz A., Gross D., and Gallie D. 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.2    Balasta, M.3    Wei, C.4    Browning, K.5    Metz, A.6    Gross, D.7    Gallie, D.8
  • 26
    • 0032938811 scopus 로고    scopus 로고
    • Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation
    • Lie Y. and Macdonald P. 1999a. Apontic binds the translational repressor Bruno and is implicated in regulation of oskar mRNA translation. Development 126: 1129.
    • (1999) Development , vol.126 , pp. 1129
    • Lie, Y.1    Macdonald, P.2
  • 27
    • 0033452314 scopus 로고    scopus 로고
    • Translational regulation of oskar mRNA occurs independent of the cap and poly(A) tail in Drosophila ovarian extracts
    • -. 1999b. Translational regulation of oskar mRNA occurs independent of the cap and poly(A) tail in Drosophila ovarian extracts. Development 126: 4989.
    • (1999) Development , vol.126 , pp. 4989
  • 28
    • 0033860615 scopus 로고    scopus 로고
    • Mechanisms of RNA localization and translational regulation
    • Lipshitz H. and Smibert C. 2000. Mechanisms of RNA localization and translational regulation. Curr. Opin. Genet. Dev. 10: 476.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 476
    • Lipshitz, H.1    Smibert, C.2
  • 29
    • 0035371080 scopus 로고    scopus 로고
    • Diversity in translational regulation
    • Macdonald P. 2001. Diversity in translational regulation. Curr. Opin. Cell Biol. 13: 326.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 326
    • Macdonald, P.1
  • 30
    • 0035404265 scopus 로고    scopus 로고
    • Translational control by CPEB: A means to the end
    • Mendez R. and Richter J. 2001. Translational control by CPEB: A means to the end. Nat. Rev. Mol. Cell Biol. 2: 521.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 521
    • Mendez, R.1    Richter, J.2
  • 31
    • 0032160381 scopus 로고    scopus 로고
    • IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F
    • Muckenthaler M., Gray N., and Hentze M. 1998. IRP-1 binding to ferritin mRNA prevents the recruitment of the small ribosomal subunit by the cap-binding complex eIF4F. Mol. Cell 2: 383.
    • (1998) Mol. Cell , vol.2 , pp. 383
    • Muckenthaler, M.1    Gray, N.2    Hentze, M.3
  • 32
    • 0028987223 scopus 로고
    • Binding of Pumilio to maternal hunchback mRNA is required for posterior patterning in Drosophila embryos
    • Murata Y. and Wharton R. 1995. Binding of Pumilio to maternal hunchback mRNA is required for posterior patterning in Drosophila embryos. Cell 80: 747.
    • (1995) Cell , vol.80 , pp. 747
    • Murata, Y.1    Wharton, R.2
  • 33
    • 0035951373 scopus 로고    scopus 로고
    • Lipoxygenase mRNA silencing in erythroid differentiation: The 3′ UTR regulatory complex controls 60S ribosomal subunit joining
    • Ostareck D., Ostareck-Lederer A., Shatsky I., and Hentze M. 2001. Lipoxygenase mRNA silencing in erythroid differentiation: The 3′ UTR regulatory complex controls 60S ribosomal subunit joining. Cell 104: 281.
    • (2001) Cell , vol.104 , pp. 281
    • Ostareck, D.1    Ostareck-Lederer, A.2    Shatsky, I.3    Hentze, M.4
  • 34
    • 0030772963 scopus 로고    scopus 로고
    • mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end
    • Ostareck D., Ostareck-Lederer A., Wilm M., Thiele B., Mann M., and Hentze M. 1997. mRNA silencing in erythroid differentiation: hnRNP K and hnRNP E1 regulate 15-lipoxygenase translation from the 3′ end. Cell 89: 597.
    • (1997) Cell , vol.89 , pp. 597
    • Ostareck, D.1    Ostareck-Lederer, A.2    Wilm, M.3    Thiele, B.4    Mann, M.5    Hentze, M.6
  • 35
    • 0031795447 scopus 로고    scopus 로고
    • Cytoplasmic regulatory functions of the KH-domain proteins hn-RNPs K and E1/E2
    • Ostareck-Lederer A., Ostareck D., and Hentze M. 1998. Cytoplasmic regulatory functions of the KH-domain proteins hn-RNPs K and E1/E2. Trends Biochem. Sci. 275: 409.
    • (1998) Trends Biochem. Sci. , vol.275 , pp. 409
    • Ostareck-Lederer, A.1    Ostareck, D.2    Hentze, M.3
  • 36
    • 0028201735 scopus 로고
    • Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region
    • Ostareck-Lederer A., Ostareck D., Standart N., and Thiele B. 1994. Translation of 15-lipoxygenase mRNA is inhibited by a protein that binds to a repeated sequence in the 3′ untranslated region. EMBO J. 13: 1476.
    • (1994) EMBO J. , vol.13 , pp. 1476
    • Ostareck-Lederer, A.1    Ostareck, D.2    Standart, N.3    Thiele, B.4
  • 37
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause A. and Sonenberg N. 1992. Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A. EMBO J. 11: 2643.
    • (1992) EMBO J. , vol.11 , pp. 2643
    • Pause, A.1    Sonenberg, N.2
  • 38
    • 0032473954 scopus 로고    scopus 로고
    • Dual function of the messenger cap structure in poly(A)-tail-promoted translation in yeast
    • Preiss T. and Hentze M. 1998. Dual function of the messenger cap structure in poly(A)-tail-promoted translation in yeast. Nature 392: 516.
    • (1998) Nature , vol.392 , pp. 516
    • Preiss, T.1    Hentze, M.2
  • 39
    • 0032811271 scopus 로고    scopus 로고
    • Translational control of nuclear lamin B1 mRNA during oogenesis and early development of Xenopus
    • Ralle T., Gremmels D., and Stick R. 1999. Translational control of nuclear lamin B1 mRNA during oogenesis and early development of Xenopus. Mech. Dev. 84: 89.
    • (1999) Mech. Dev. , vol.84 , pp. 89
    • Ralle, T.1    Gremmels, D.2    Stick, R.3
  • 40
    • 0022861651 scopus 로고
    • The maturational breakdown of mitochondria in reticulocytes
    • Rapoport S. and Schewe T. 1986. The maturational breakdown of mitochondria in reticulocytes. Biochim. Biophys. Acta 864: 471.
    • (1986) Biochim. Biophys. Acta , vol.864 , pp. 471
    • Rapoport, S.1    Schewe, T.2
  • 41
    • 0033052063 scopus 로고    scopus 로고
    • Cytoplasmic polyadenylation in development and beyond
    • Richter J. 1999. Cytoplasmic polyadenylation in development and beyond. Microbiol. Mol. Biol. Rev. 63: 446.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 446
    • Richter, J.1
  • 42
    • 0001364237 scopus 로고    scopus 로고
    • Influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function
    • ed. N. Sonenberg et al. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • -. Influence of polyadenylation-induced translation on metazoan development and neuronal synaptic function. In Translational control of gene expression (ed. N. Sonenberg et al.), p. 785. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • Translational Control of Gene Expression , pp. 785
  • 43
    • 0002463490 scopus 로고    scopus 로고
    • Translational control of ferritin synthesis
    • ed. N. Sonenberg et al. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Rouault T. 2000. Translational control of ferritin synthesis. In Translational control of gene expression (ed. N. Sonenberg et al.), p. 655. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York.
    • (2000) Translational Control of Gene Expression , pp. 655
    • Rouault, T.1
  • 44
    • 0031877789 scopus 로고    scopus 로고
    • Premature translation of oskar in oocytes lacking the RNA-binding protein bicaudal-C
    • Saffman E., Styhler S., Rother K., Li W., Richard S., and Lasko P. 1998. Premature translation of oskar in oocytes lacking the RNA-binding protein bicaudal-C. Mol. Cell. Biol. 18: 4855.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4855
    • Saffman, E.1    Styhler, S.2    Rother, K.3    Li, W.4    Richard, S.5    Lasko, P.6
  • 45
    • 0027075193 scopus 로고
    • Translational control by poly(A) elongation during Xenopus development: Differential repression and enhancement by a novel cytoplasmic polyadenylation element
    • Simon R., Tassan J.-P., and Richter J. 1992. Translational control by poly(A) elongation during Xenopus development: Differential repression and enhancement by a novel cytoplasmic polyadenylation element. Genes Dev. 6: 2580.
    • (1992) Genes Dev. , vol.6 , pp. 2580
    • Simon, R.1    Tassan, J.-P.2    Richter, J.3
  • 46
    • 0033634943 scopus 로고    scopus 로고
    • The LIN-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-49 transcription factor
    • Slack F.J., Basson M., Liu Z., Ambros V., Horvitz H.R., and Ruvkun G. 2000. The LIN-41 RBCC gene acts in the C. elegans heterochronic pathway between the let-7 regulatory RNA and the LIN-49 transcription factor. Mol. Cell 5: 659.
    • (2000) Mol. Cell , vol.5 , pp. 659
    • Slack, F.J.1    Basson, M.2    Liu, Z.3    Ambros, V.4    Horvitz, H.R.5    Ruvkun, G.6
  • 47
    • 0033569404 scopus 로고    scopus 로고
    • Recruitment of Nanos to hunchback mRNA by Pumilio
    • Sonoda J. and Wharton R. 1999. Recruitment of Nanos to hunchback mRNA by Pumilio. Genes Dev. 13: 2704.
    • (1999) Genes Dev. , vol.13 , pp. 2704
    • Sonoda, J.1    Wharton, R.2
  • 48
    • 0035868645 scopus 로고    scopus 로고
    • Drosophila Brain Tumor is a translational repressor
    • -. 2001. Drosophila Brain Tumor is a translational repressor. Genes Dev. 15: 762.
    • (2001) Genes Dev. , vol.15 , pp. 762
  • 49
    • 0033394199 scopus 로고    scopus 로고
    • Maskin is a CPEB-associated factor that transiently interacts with eIF-4E
    • Stebbins-Boaz B., Cao Q., de Moor C., Mendez R., and Richter J. 1999. Maskin is a CPEB-associated factor that transiently interacts with eIF-4E. Mol. Cell 4: 1017.
    • (1999) Mol. Cell , vol.4 , pp. 1017
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.3    Mendez, R.4    Richter, J.5
  • 50
    • 0032529190 scopus 로고    scopus 로고
    • Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes
    • Stutz A., Conne B., Huarte J., Gubler P., Völkel V., Flandin P., and Vassalli J.-D. 1998. Masking, unmasking, and regulated polyadenylation cooperate in the translational control of a dormant mRNA in mouse oocytes. Genes Dev. 12: 2535.
    • (1998) Genes Dev. , vol.12 , pp. 2535
    • Stutz, A.1    Conne, B.2    Huarte, J.3    Gubler, P.4    Völkel, V.5    Flandin, P.6    Vassalli, J.-D.7
  • 51
    • 0028884380 scopus 로고
    • A common function for mRNA 5′ and 3′ ends in translation initiation in yeast
    • Tarun S. and Sachs A. 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.1    Sachs, A.2
  • 52
    • 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
  • 53
    • 0030797564 scopus 로고    scopus 로고
    • Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
    • Tarun S., Wells S., Deardorff J., and Sachs A. 1997. Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation. Proc. Natl. Acad. Sci. 94: 9046.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 9046
    • Tarun, S.1    Wells, S.2    Deardorff, J.3    Sachs, A.4
  • 54
    • 0033993581 scopus 로고    scopus 로고
    • Rapid deadenylation and poly(A)-dependent translational repression mediated by the Caenorhabditis elegans tra-2 3′untranslated region in Xenopus embryos
    • Thompson S.R., Goodwin E.B., and Wickens M. 2000. Rapid deadenylation and poly(A)-dependent translational repression mediated by the Caenorhabditis elegans tra-2 3′untranslated region in Xenopus embryos. Mol. Cell. Biol. 20: 2129.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2129
    • Thompson, S.R.1    Goodwin, E.B.2    Wickens, M.3
  • 55
    • 0033957069 scopus 로고    scopus 로고
    • Molecular mechanisms for activity-regulated protein synthesis in the synapto-dendritic compartment
    • Wells D., Richter J., and Fallon J. 2000. Molecular mechanisms for activity-regulated protein synthesis in the synapto-dendritic compartment. Curr. Opin. Neurobiol. 10: 132.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 132
    • Wells, D.1    Richter, J.2    Fallon, J.3
  • 56
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells S.E., Hillner P.E., Vale R.D., and Sachs A.B. 1998. Circularization of mRNA by eukaryotic translation initiation factors. Mol. Cell 2: 135.
    • (1998) Mol. Cell , vol.2 , pp. 135
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 57
    • 0025748167 scopus 로고
    • RNA regulatory elements mediate control of Drosophila body pattern by the posterior morphogen nanos
    • Wharton R. and Struhl G. 1991. RNA regulatory elements mediate control of Drosophila body pattern by the posterior morphogen nanos. Cell 67: 955.
    • (1991) Cell , vol.67 , pp. 955
    • Wharton, R.1    Struhl, G.2
  • 58
    • 0032059805 scopus 로고    scopus 로고
    • The pumilio RNA-binding domain is also a translational regulator
    • Wharton R., Sonoda J., Lee T., Patterson M., and Murata Y. 1998. The pumilio RNA-binding domain is also a translational regulator. Mol. Cell 1: 863.
    • (1998) Mol. Cell , vol.1 , pp. 863
    • Wharton, R.1    Sonoda, J.2    Lee, T.3    Patterson, M.4    Murata, Y.5
  • 59
    • 0002068909 scopus 로고    scopus 로고
    • Translational control of developmental decisions
    • ed. N. Sonenberg et al. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York
    • Wickens M., Goodwin E., Kimble J., Strickland S., and Hentze M. 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.2    Kimble, J.3    Strickland, S.4    Hentze, M.5
  • 60
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the A site of the ribosome
    • Wilson J., Pestova T., Hellen C., and Samow P. 2000a. Initiation of protein synthesis from the A site of the ribosome. Cell 102: 511.
    • (2000) Cell , vol.102 , pp. 511
    • Wilson, J.1    Pestova, T.2    Hellen, C.3    Samow, P.4
  • 61
    • 0033920258 scopus 로고    scopus 로고
    • Naturally occuring dicistronic cricket paralysis virus RNA is regulated by two internal ribosome entry sites
    • Wilson J., Powell M., Hoover S., and Samow P. 2000b. Naturally occuring dicistronic cricket paralysis virus RNA is regulated by two internal ribosome entry sites. Mol. Cell. Biol. 20: 4990.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4990
    • Wilson, J.1    Powell, M.2    Hoover, S.3    Samow, P.4
  • 63
    • 0030757678 scopus 로고    scopus 로고
    • Nanos and pumilio establish embryonic polarity in Drosophila by promoting posterior deadenylation of hunchback mRNA
    • Wreden C., Verroti A., Schisa J., Lieberfarb M., and Strickland S. 1997. Nanos and pumilio establish embryonic polarity in Drosophila by promoting posterior deadenylation of hunchback mRNA. Development 124: 3015.
    • (1997) Development , vol.124 , pp. 3015
    • Wreden, C.1    Verroti, A.2    Schisa, J.3    Lieberfarb, M.4    Strickland, S.5
  • 64
    • 0030799124 scopus 로고    scopus 로고
    • The 36-kilodalton embryonic-type cytoplasmic polyadenylation element-binding protein in Xenopus laevis is ElrA, a member of the ELAV family of RNA-binding proteins
    • Wu L., Good P., and Richter J. 1997. The 36-kilodalton embryonic-type cytoplasmic polyadenylation element-binding protein in Xenopus laevis is ElrA, a member of the ELAV family of RNA-binding proteins. Mol. Cell. Biol. 17: 6402.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6402
    • Wu, L.1    Good, P.2    Richter, J.3
  • 65
    • 0031452082 scopus 로고    scopus 로고
    • A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germ line
    • Zhang B., Gallegos M., Puoti A., Durkin E., Fields S., Kimble J., and Wickens M. 1997. A conserved RNA-binding protein that regulates sexual fates in the C. elegans hermaphrodite germ line. Nature 390: 477.
    • (1997) Nature , vol.390 , pp. 477
    • Zhang, B.1    Gallegos, M.2    Puoti, A.3    Durkin, E.4    Fields, S.5    Kimble, J.6    Wickens, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.