메뉴 건너뛰기




Volumn 38, Issue 22, 2010, Pages 8039-8050

Identifying eIF4E-binding protein translationally-controlled transcripts reveals links to mRNAs bound by specific PUF proteins

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; INITIATION FACTOR 4E BINDING PROTEIN; MESSENGER RNA; PROTEIN PUF1P; PROTEIN PUF2P; PROTEIN PUF4P; PROTEIN PUF5P; UNCLASSIFIED DRUG;

EID: 78650424915     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkq686     Document Type: Article
Times cited : (42)

References (49)
  • 1
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R.J., Hellen, C.U. and Pestova, T.V. (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat. Rev. Mol. Cell Biol., 11, 113-127.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.2    Pestova, T.V.3
  • 2
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • Richter, J.D. and Sonenberg, N. (2005) Regulation of cap-dependent translation by eIF4E inhibitory proteins. Nature, 433, 477-480.
    • (2005) Nature , vol.433 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 3
    • 0034057277 scopus 로고    scopus 로고
    • Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression
    • Mothe-Satney, I., Yang, D., Fadden, P., Haystead, T.A. and Lawrence, J.C. Jr. (2000) Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression. Mol. Cell. Biol., 20, 3558-3567.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3558-3567
    • Mothe-Satney, I.1    Yang, D.2    Fadden, P.3    Haystead, T.A.4    Lawrence Jr., J.C.5
  • 5
    • 34249886604 scopus 로고    scopus 로고
    • Translational control in development
    • Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds) CHSL Press, Cold Spring Harbor
    • Thompson, B., Wickens, M. and Kimble, J. (2007) Translational control in development. In: Mathews, M.B., Sonenberg, N. and Hershey, J.W.B. (eds), Translational Control in Biology and Medicine. CHSL Press, Cold Spring Harbor, pp. 507-544.
    • (2007) Translational Control in Biology and Medicine , pp. 507-544
    • Thompson, B.1    Wickens, M.2    Kimble, J.3
  • 6
    • 0031041015 scopus 로고    scopus 로고
    • A novel inhibitor of cap-dependent translation initiation in yeast: P20 competes with eIF4G for binding to eIF4E
    • Altmann, M., Schmitz, N., Berset, C. and Trachsel, H. (1997) A novel inhibitor of cap-dependent translation initiation in yeast: p20 competes with eIF4G for binding to eIF4E. EMBO J., 16, 1114-1121.
    • (1997) EMBO J. , vol.16 , pp. 1114-1121
    • Altmann, M.1    Schmitz, N.2    Berset, C.3    Trachsel, H.4
  • 7
    • 0034044544 scopus 로고    scopus 로고
    • Eap1p, a novel eukaryotic translation initiation factor 4E-associated protein in Saccharomyces cerevisiae
    • Cosentino, G.P., Schmelzle, T., Haghighat, A., Helliwell, S.B., Hall, M.N. and Sonenberg, N. (2000) Eap1p, a novel eukaryotic translation initiation factor 4E-associated protein in Saccharomyces cerevisiae. Mol. Cell. Biol., 20, 4604-4613.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4604-4613
    • Cosentino, G.P.1    Schmelzle, T.2    Haghighat, A.3    Helliwell, S.B.4    Hall, M.N.5    Sonenberg, N.6
  • 8
    • 0031000205 scopus 로고    scopus 로고
    • The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae
    • De la Cruz, J., Iost, I., Kressler, D. and Linder, P. (1997) The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent translation in Saccharomyces cerevisiae. Proc. Natl Acad. Sci. USA, 94, 5201-5206.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5201-5206
    • De La Cruz, J.1    Iost, I.2    Kressler, D.3    Linder, P.4
  • 9
    • 51349111701 scopus 로고    scopus 로고
    • Gcn4 Is Required for the Response to Peroxide Stress in the Yeast Saccharomyces cerevisiae
    • Mascarenhas, C., Edwards-Ingram, L.C., Zeef, L., Shenton, D., Ashe, M.P. and Grant, C.M. (2008) Gcn4 Is Required for the Response to Peroxide Stress in the Yeast Saccharomyces cerevisiae. Mol. Biol. Cell, 19, 2995-3007.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2995-3007
    • Mascarenhas, C.1    Edwards-Ingram, L.C.2    Zeef, L.3    Shenton, D.4    Ashe, M.P.5    Grant, C.M.6
  • 10
    • 33751571405 scopus 로고    scopus 로고
    • Regulation of translation initiation by the yeast eIF4E binding proteins is required for the pseudohyphal response
    • Ibrahimo, S., Holmes, L.E. and Ashe, M.P. (2006) Regulation of translation initiation by the yeast eIF4E binding proteins is required for the pseudohyphal response. Yeast, 23, 1075-1088.
    • (2006) Yeast , vol.23 , pp. 1075-1088
    • Ibrahimo, S.1    Holmes, L.E.2    Ashe, M.P.3
  • 11
    • 33644851220 scopus 로고    scopus 로고
    • Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae
    • DOI 10.1091/mbc.E05-11-1039
    • Meier, K.D., Deloche, O., Kajiwara, K., Funato, K. and Riezman, H. (2006) Sphingoid base is required for translation initiation during heat stress in Saccharomyces cerevisiae. Mol. Biol. Cell, 17, 1164-1175. (Pubitemid 43376538)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.3 , pp. 1164-1175
    • Meier, K.D.1    Deloche, O.2    Kajiwara, K.3    Funato, K.4    Riezman, H.5
  • 12
    • 1242316948 scopus 로고    scopus 로고
    • A membrane transport defect leads to a rapid attenuation of translation initiation in Saccharomyces cerevisiae
    • Deloche, O., de la Cruz, J., Kressler, D., Doere, M. and Linder, P. (2004) A membrane transport defect leads to a rapid attenuation of translation initiation in Saccharomyces cerevisiae. Mol. Cell, 13, 357-366.
    • (2004) Mol. Cell , vol.13 , pp. 357-366
    • Deloche, O.1    De La Cruz, J.2    Kressler, D.3    Doere, M.4    Linder, P.5
  • 13
    • 0030855972 scopus 로고    scopus 로고
    • Coupling of cell division to cell growth by translational control of the G1 cyclin CLN3 in yeast
    • Polymenis, M. and Schmidt, E.V. (1997) Coupling of cell division to cell growth by translational control of the G1 cyclin CLN3 in yeast. Genes Dev., 11, 2522-2531.
    • (1997) Genes Dev. , vol.11 , pp. 2522-2531
    • Polymenis, M.1    Schmidt, E.V.2
  • 14
    • 0033563235 scopus 로고    scopus 로고
    • CLN3 expression is sufficient to restore G1-to-S-phase progression in Saccharomyces cerevisiae mutants defective in translation initiation factor eIF4E
    • Danaie, P., Altmann, M., Hall, M.N., Trachsel, H. and Helliwell, S.B. (1999) CLN3 expression is sufficient to restore G1-to-S-phase progression in Saccharomyces cerevisiae mutants defective in translation initiation factor eIF4E. Biochem. J., 340, 135-141.
    • (1999) Biochem. J. , vol.340 , pp. 135-141
    • Danaie, P.1    Altmann, M.2    Hall, M.N.3    Trachsel, H.4    Helliwell, S.B.5
  • 15
    • 67649639495 scopus 로고    scopus 로고
    • The SESA network links duplication of the yeast centrosome with the protein translation machinery
    • Sezen, B., Seedorf, M. and Schiebel, E. (2009) The SESA network links duplication of the yeast centrosome with the protein translation machinery. Genes Dev., 23, 1559-1570.
    • (2009) Genes Dev. , vol.23 , pp. 1559-1570
    • Sezen, B.1    Seedorf, M.2    Schiebel, E.3
  • 16
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R.S. and Hieter, P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 18
    • 0037438569 scopus 로고    scopus 로고
    • Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae
    • Warringer, J. and Blomberg, A. (2003) Automated screening in environmental arrays allows analysis of quantitative phenotypic profiles in Saccharomyces cerevisiae. Yeast, 20, 53-67.
    • (2003) Yeast , vol.20 , pp. 53-67
    • Warringer, J.1    Blomberg, A.2
  • 19
    • 19344365947 scopus 로고    scopus 로고
    • Extensive association of functionally and cytotopically related mRNAs with Puf family RNA-binding proteins in yeast
    • Gerber, A.P., Herschlag, D. and Brown, P.O. (2004) Extensive association of functionally and cytotopically related mRNAs with Puf family RNA-binding proteins in yeast. PLoS Biol., 2, E79.
    • (2004) PLoS Biol. , vol.2
    • Gerber, A.P.1    Herschlag, D.2    Brown, P.O.3
  • 20
  • 21
    • 27144465421 scopus 로고    scopus 로고
    • Global gene expression profiling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways
    • Smirnova, J.B., Selley, J.N., Sanchez-Cabo, F., Carroll, K., Eddy, A.A., McCarthy, J.E., Hubbard, S.J., Pavitt, G.D., Grant, C.M. and Ashe, M.P. (2005) Global gene expression profiling reveals widespread yet distinctive translational responses to different eukaryotic translation initiation factor 2B-targeting stress pathways. Mol. Cell. Biol., 25, 9340-9349.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9340-9349
    • Smirnova, J.B.1    Selley, J.N.2    Sanchez-Cabo, F.3    Carroll, K.4    Eddy, A.A.5    McCarthy, J.E.6    Hubbard, S.J.7    Pavitt, G.D.8    Grant, C.M.9    Ashe, M.P.10
  • 23
    • 34447514386 scopus 로고    scopus 로고
    • Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange
    • Mohammad-Qureshi, S.S., Haddad, R., Hemingway, E.J., Richardson, J.P. and Pavitt, G.D. (2007) Critical contacts between the eukaryotic initiation factor 2B (eIF2B) catalytic domain and both eIF2beta and -2gamma mediate guanine nucleotide exchange. Mol. Cell. Biol., 27, 5225-5234.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5225-5234
    • Mohammad-Qureshi, S.S.1    Haddad, R.2    Hemingway, E.J.3    Richardson, J.P.4    Pavitt, G.D.5
  • 24
    • 0035882157 scopus 로고    scopus 로고
    • Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4
    • Jager, S., Strayle, J., Heinemeyer, W. and Wolf, D.H. (2001) Cic1, an adaptor protein specifically linking the 26S proteasome to its substrate, the SCF component Cdc4. EMBO J., 20, 4423-4431.
    • (2001) EMBO J. , vol.20 , pp. 4423-4431
    • Jager, S.1    Strayle, J.2    Heinemeyer, W.3    Wolf, D.H.4
  • 25
    • 0035022015 scopus 로고    scopus 로고
    • Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast la protein
    • Pannone, B.K., Kim, S.D., Noe, D.A. and Wolin, S.L. (2001) Multiple functional interactions between components of the Lsm2-Lsm8 complex, U6 snRNA, and the yeast La protein. Genetics, 158, 187-196.
    • (2001) Genetics , vol.158 , pp. 187-196
    • Pannone, B.K.1    Kim, S.D.2    Noe, D.A.3    Wolin, S.L.4
  • 26
    • 1842505511 scopus 로고    scopus 로고
    • Autonomous function of the amino-terminal inhibitory domain of TAF1 in transcriptional regulation
    • Takahata, S., Kasahara, K., Kawaichi, M. and Kokubo, T. (2004) Autonomous function of the amino-terminal inhibitory domain of TAF1 in transcriptional regulation. Mol. Cell. Biol., 24, 3089-3099.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 3089-3099
    • Takahata, S.1    Kasahara, K.2    Kawaichi, M.3    Kokubo, T.4
  • 27
    • 30944465453 scopus 로고    scopus 로고
    • An intramolecular t-SNARE complex functions in vivo without the syntaxin NH2-terminal regulatory domain
    • Van Komen, J.S., Bai, X., Scott, B.L. and McNew, J.A. (2006) An intramolecular t-SNARE complex functions in vivo without the syntaxin NH2-terminal regulatory domain. J. Cell Biol., 172, 295-307.
    • (2006) J. Cell Biol. , vol.172 , pp. 295-307
    • Van Komen, J.S.1    Bai, X.2    Scott, B.L.3    McNew, J.A.4
  • 28
    • 0027486013 scopus 로고
    • PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae
    • Anderson, J.T., Paddy, M.R. and Swanson, M.S. (1993) PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae. Mol. Cell. Biol., 13, 6102-6113.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6102-6113
    • Anderson, J.T.1    Paddy, M.R.2    Swanson, M.S.3
  • 29
    • 0345602742 scopus 로고    scopus 로고
    • Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock
    • Preiss, T., Baron-Benhamou, J., Ansorge, W. and Hentze, M.W. (2003) Homodirectional changes in transcriptome composition and mRNA translation induced by rapamycin and heat shock. Nat. Struct. Biol., 10, 1039-1047.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 1039-1047
    • Preiss, T.1    Baron-Benhamou, J.2    Ansorge, W.3    Hentze, M.W.4
  • 30
    • 0346503888 scopus 로고    scopus 로고
    • Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis
    • Nakamura, A., Sato, K. and Hanyu-Nakamura, K. (2004) Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis. Dev. Cell, 6, 69-78.
    • (2004) Dev. Cell , vol.6 , pp. 69-78
    • Nakamura, A.1    Sato, K.2    Hanyu-Nakamura, K.3
  • 32
    • 34250313519 scopus 로고    scopus 로고
    • Local activation of yeast ASH1 mRNA translation through phosphorylation of Khd1p by the casein kinase Yck1p
    • Paquin, N., Menade, M., Poirier, G., Donato, D., Drouet, E. and Chartrand, P. (2007) Local activation of yeast ASH1 mRNA translation through phosphorylation of Khd1p by the casein kinase Yck1p. Mol. Cell, 26, 795-809.
    • (2007) Mol. Cell , vol.26 , pp. 795-809
    • Paquin, N.1    Menade, M.2    Poirier, G.3    Donato, D.4    Drouet, E.5    Chartrand, P.6
  • 33
    • 42149091071 scopus 로고    scopus 로고
    • Translation of ASH1 mRNA is repressed by Puf6p-Fun12p/eIF5B interaction and released by CK2 phosphorylation
    • Deng, Y., Singer, R.H. and Gu, W. (2008) Translation of ASH1 mRNA is repressed by Puf6p-Fun12p/eIF5B interaction and released by CK2 phosphorylation. Genes Dev., 22, 1037-1050.
    • (2008) Genes Dev. , vol.22 , pp. 1037-1050
    • Deng, Y.1    Singer, R.H.2    Gu, W.3
  • 34
    • 33845659611 scopus 로고    scopus 로고
    • Identification of translational regulation target genes during filamentous growth in Saccharomyces cerevisiae: Regulatory role of Caf20 and Dhh1
    • Park, Y.U., Hur, H., Ka, M. and Kim, J. (2006) Identification of translational regulation target genes during filamentous growth in Saccharomyces cerevisiae: regulatory role of Caf20 and Dhh1. Eukaryot. Cell, 5, 2120-2127.
    • (2006) Eukaryot. Cell , vol.5 , pp. 2120-2127
    • Park, Y.U.1    Hur, H.2    Ka, M.3    Kim, J.4
  • 35
    • 0029914164 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae S288C has a mutation in FLO8, a gene required for filamentous growth
    • Liu, H., Styles, C.A. and Fink, G.R. (1996) Saccharomyces cerevisiae S288C has a mutation in FLO8, a gene required for filamentous growth. Genetics, 144, 967-978.
    • (1996) Genetics , vol.144 , pp. 967-978
    • Liu, H.1    Styles, C.A.2    Fink, G.R.3
  • 36
    • 0031971444 scopus 로고    scopus 로고
    • Dip5p mediates high-affinity and high-capacity transport of L-glutamate and L-aspartate in Saccharomyces cerevisiae
    • Regenberg, B., Holmberg, S., Olsen, L.D. and Kielland-Brandt, M.C. (1998) Dip5p mediates high-affinity and high-capacity transport of L-glutamate and L-aspartate in Saccharomyces cerevisiae. Curr. Genet., 33, 171-177.
    • (1998) Curr. Genet. , vol.33 , pp. 171-177
    • Regenberg, B.1    Holmberg, S.2    Olsen, L.D.3    Kielland-Brandt, M.C.4
  • 37
    • 20744452172 scopus 로고    scopus 로고
    • Global analysis of Pub1p targets reveals a coordinate control of gene expression through modulation of binding and stability
    • Duttagupta, R., Tian, B., Wilusz, C.J., Khounh, D.T., Soteropoulos, P., Ouyang, M., Dougherty, J.P. and Peltz, S.W. (2005) Global analysis of Pub1p targets reveals a coordinate control of gene expression through modulation of binding and stability. Mol. Cell. Biol., 25, 5499-5513.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5499-5513
    • Duttagupta, R.1    Tian, B.2    Wilusz, C.J.3    Khounh, D.T.4    Soteropoulos, P.5    Ouyang, M.6    Dougherty, J.P.7    Peltz, S.W.8
  • 38
    • 0347717583 scopus 로고    scopus 로고
    • Identification of Lhp1p-associated RNAs by microarray analysis in Saccharomyces cerevisiae reveals association with coding and noncoding RNAs
    • Inada, M. and Guthrie, C. (2004) Identification of Lhp1p-associated RNAs by microarray analysis in Saccharomyces cerevisiae reveals association with coding and noncoding RNAs. Proc. Natl Acad. Sci. USA, 101, 434-439.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 434-439
    • Inada, M.1    Guthrie, C.2
  • 39
    • 54949148332 scopus 로고    scopus 로고
    • Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system
    • Hogan, D.J., Riordan, D.P., Gerber, A.P., Herschlag, D. and Brown, P.O. (2008) Diverse RNA-binding proteins interact with functionally related sets of RNAs, suggesting an extensive regulatory system. PLoS Biol., 6, e255.
    • (2008) PLoS Biol. , vol.6
    • Hogan, D.J.1    Riordan, D.P.2    Gerber, A.P.3    Herschlag, D.4    Brown, P.O.5
  • 41
    • 5444249309 scopus 로고    scopus 로고
    • Regulation of neuronal excitability through pumilio-dependent control of a sodium channel gene
    • Mee, C.J., Pym, E.C., Moffat, K.G. and Baines, R.A. (2004) Regulation of neuronal excitability through pumilio-dependent control of a sodium channel gene. J. Neurosci., 24, 8695-8703.
    • (2004) J. Neurosci. , vol.24 , pp. 8695-8703
    • Mee, C.J.1    Pym, E.C.2    Moffat, K.G.3    Baines, R.A.4
  • 42
    • 0035917508 scopus 로고    scopus 로고
    • Structure of Pumilio reveals similarity between RNA and peptide binding motifs
    • Edwards, T.A., Pyle, S.E., Wharton, R.P. and Aggarwal, A.K. (2001) Structure of Pumilio reveals similarity between RNA and peptide binding motifs. Cell, 105, 281-289.
    • (2001) Cell , vol.105 , pp. 281-289
    • Edwards, T.A.1    Pyle, S.E.2    Wharton, R.P.3    Aggarwal, A.K.4
  • 43
    • 0142123289 scopus 로고    scopus 로고
    • Model of the brain tumor-Pumilio translation repressor complex
    • Edwards, T.A., Wilkinson, B.D., Wharton, R.P. and Aggarwal, A.K. (2003) Model of the brain tumor-Pumilio translation repressor complex. Genes Dev., 17, 2508-2513.
    • (2003) Genes Dev. , vol.17 , pp. 2508-2513
    • Edwards, T.A.1    Wilkinson, B.D.2    Wharton, R.P.3    Aggarwal, A.K.4
  • 44
    • 2942692177 scopus 로고    scopus 로고
    • A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization
    • Gu, W., Deng, Y., Zenklusen, D. and Singer, R.H. (2004) A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization. Genes Dev., 18, 1452-1465.
    • (2004) Genes Dev. , vol.18 , pp. 1452-1465
    • Gu, W.1    Deng, Y.2    Zenklusen, D.3    Singer, R.H.4
  • 45
    • 4644284749 scopus 로고    scopus 로고
    • Recruitment of the Puf3 protein to its mRNA target for regulation of mRNA decay in yeast
    • Jackson, J.S. Jr., Houshmandi, S.S., Lopez Leban, F. and Olivas, W.M. (2004) Recruitment of the Puf3 protein to its mRNA target for regulation of mRNA decay in yeast. RNA, 10, 1625-1636.
    • (2004) RNA , vol.10 , pp. 1625-1636
    • Jackson Jr., J.S.1    Houshmandi, S.S.2    Lopez Leban, F.3    Olivas, W.M.4
  • 46
    • 27144544947 scopus 로고    scopus 로고
    • Yeast Puf3 mutants reveal the complexity of Puf-RNA binding and identify a loop required for regulation of mRNA decay
    • Houshmandi, S.S. and Olivas, W.M. (2005) Yeast Puf3 mutants reveal the complexity of Puf-RNA binding and identify a loop required for regulation of mRNA decay. RNA, 11, 1655-1666.
    • (2005) RNA , vol.11 , pp. 1655-1666
    • Houshmandi, S.S.1    Olivas, W.M.2
  • 47
    • 38649087012 scopus 로고    scopus 로고
    • Puf1p acts in combination with other yeast Puf proteins to control mRNA stability
    • Ulbricht, R.J. and Olivas, W.M. (2008) Puf1p acts in combination with other yeast Puf proteins to control mRNA stability. RNA, 14, 246-262.
    • (2008) RNA , vol.14 , pp. 246-262
    • Ulbricht, R.J.1    Olivas, W.M.2
  • 48
    • 34447503943 scopus 로고    scopus 로고
    • Two yeast PUF proteins negatively regulate a single mRNA
    • Hook, B.A., Goldstrohm, A.C., Seay, D.J. and Wickens, M. (2007) Two yeast PUF proteins negatively regulate a single mRNA. J. Biol. Chem., 282, 15430-15438.
    • (2007) J. Biol. Chem. , vol.282 , pp. 15430-15438
    • Hook, B.A.1    Goldstrohm, A.C.2    Seay, D.J.3    Wickens, M.4
  • 49
    • 77952703757 scopus 로고    scopus 로고
    • Translational repression by PUF proteins in vitro
    • Chritton, J.J. and Wickens, M. (2010) Translational repression by PUF proteins in vitro. RNA, 16, 1217-1225.
    • (2010) RNA , vol.16 , pp. 1217-1225
    • Chritton, J.J.1    Wickens, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.