메뉴 건너뛰기




Volumn 42, Issue 4, 2014, Pages 1238-1245

EIF4E-binding proteins: New factors, new locations, new roles

Author keywords

Cap binding; MRNA decay; RNA binding protein; Translation initiation; Translational repression

Indexed keywords

FUNGAL PROTEIN; INITIATION FACTOR 4E BINDING PROTEIN; INITIATION FACTOR 4G; INITIATION FACTOR 4E; RNA BINDING PROTEIN;

EID: 84905816368     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20140063     Document Type: Conference Paper
Times cited : (28)

References (67)
  • 2
    • 67650543838 scopus 로고    scopus 로고
    • EIF4E: New family members, new binding partners, new roles
    • Rhoads, R. (2009) eIF4E: new family members, new binding partners, new roles. J. Biol. Chem. 284, 16711-16715
    • (2009) J. Biol. Chem. , vol.284 , pp. 16711-16715
    • Rhoads, R.1
  • 3
    • 0028786952 scopus 로고
    • Repression of cap-dependent translation by 4E-binding protein 1: Competition with p220 for binding to eukaryotic initiation factor-4E
    • Haghighat, A., Mader, S., Pause, A. and Sonenberg, N. (1995) Repression of cap-dependent translation by 4E-binding protein 1: competition with p220 for binding to eukaryotic initiation factor-4E. EMBO J. 14, 5701-5709
    • (1995) EMBO J. , vol.14 , pp. 5701-5709
    • Haghighat, A.1    Mader, S.2    Pause, A.3    Sonenberg, N.4
  • 4
    • 0032541425 scopus 로고    scopus 로고
    • Cooperative modulation by eIF4G of eIF4E-binding to the mRNA 5 cap in yeast involves a site partially shared by p20
    • Ptushkina, M., von der Haar, T., Vasilescu, S., Frank, R., Birkenhager, R. and McCarthy, J.E. (1998) Cooperative modulation by eIF4G of eIF4E-binding to the mRNA 5 cap in yeast involves a site partially shared by p20. EMBO J. 17, 4798-4808
    • (1998) EMBO J. , vol.17 , pp. 4798-4808
    • Ptushkina, M.1    Von Der Haar, T.2    Vasilescu, S.3    Frank, R.4    Birkenhager, R.5    McCarthy, J.E.6
  • 5
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson, R.J., Hellen, C. and Pestova, T. (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.2    Pestova, T.3
  • 6
    • 84861231813 scopus 로고    scopus 로고
    • Translational control in cellular and developmental processes
    • Kong, J. and Lasko, P. (2012) Translational control in cellular and developmental processes. Nat. Rev. Genet. 13, 383-394
    • (2012) Nat. Rev. Genet. , vol.13 , pp. 383-394
    • Kong, J.1    Lasko, P.2
  • 7
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: New insights and challenges
    • Hinnebusch, A.G. and Lorsch, J.R. (2012) The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol. 4, a011544
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 8
    • 84882291342 scopus 로고    scopus 로고
    • Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity
    • Feoktistova, K., Tuvshintogs, E., Do, A. and Fraser, C.S. (2013) Human eIF4E promotes mRNA restructuring by stimulating eIF4A helicase activity. Proc. Natl. Acad. Sci. U.S.A. 110, 13339-13344
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 13339-13344
    • Feoktistova, K.1    Tuvshintogs, E.2    Do, A.3    Fraser, C.S.4
  • 9
    • 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, 104-113
    • (2005) Genes Dev. , vol.19 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'boutchou, M.N.4    Sonenberg, N.5
  • 10
    • 0025314596 scopus 로고
    • Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5 cap
    • Lazaris-Karatzas, A., Montine, K. and Sonenberg, N. (1990) Malignant transformation by a eukaryotic initiation factor subunit that binds to mRNA 5 cap. Nature 345, 544-547
    • (1990) Nature , vol.345 , pp. 544-547
    • Lazaris-Karatzas, A.1    Montine, K.2    Sonenberg, N.3
  • 11
    • 0026723117 scopus 로고
    • MRNAs containing extensive secondary structure in their 5 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E
    • Koromilas, A.E., Lazaris-Karatzas, A. and Sonenberg, N. (1992) mRNAs containing extensive secondary structure in their 5 non-coding region translate efficiently in cells overexpressing initiation factor eIF-4E. EMBO J. 11, 4153-4158
    • (1992) EMBO J. , vol.11 , pp. 4153-4158
    • Koromilas, A.E.1    Lazaris-Karatzas, A.2    Sonenberg, N.3
  • 13
    • 77956271160 scopus 로고    scopus 로고
    • Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development
    • Ueda, T., Sasaki, M., Elia, A.J., Chio, I.I., Hamada, K., Fukunaga, R. and Mak, T.W. (2010) Combined deficiency for MAP kinase-interacting kinase 1 and 2 (Mnk1 and Mnk2) delays tumor development. Proc. Natl. Acad. Sci. U.S.A. 107, 13984-13990
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 13984-13990
    • Ueda, T.1    Sasaki, M.2    Elia, A.J.3    Chio, I.I.4    Hamada, K.5    Fukunaga, R.6    Mak, T.W.7
  • 14
    • 84873739231 scopus 로고    scopus 로고
    • Anti-oncogenic potential of the eIF4E-binding proteins
    • Martineau, Y., Azar, R., Bousquet, C. and Pyronnet, S. (2013) Anti-oncogenic potential of the eIF4E-binding proteins. Oncogene 32, 671-677
    • (2013) Oncogene , vol.32 , pp. 671-677
    • Martineau, Y.1    Azar, R.2    Bousquet, C.3    Pyronnet, S.4
  • 20
  • 21
    • 0034660062 scopus 로고    scopus 로고
    • A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5 cap-binding protein, eIF4E
    • Dostie, J., Ferraiuolo, M., Pause, A., Adam, S.A. and Sonenberg, N. (2000) A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5 cap-binding protein, eIF4E. EMBO J. 19, 3142-3156
    • (2000) EMBO J. , vol.19 , pp. 3142-3156
    • Dostie, J.1    Ferraiuolo, M.2    Pause, A.3    Adam, S.A.4    Sonenberg, N.5
  • 22
    • 84855394456 scopus 로고    scopus 로고
    • RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor
    • Marnef, A., Weil, D. and Standart, N. (2012) RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor. Mol. Biol. Cell 23, 213-224
    • (2012) Mol. Biol. Cell , vol.23 , pp. 213-224
    • Marnef, A.1    Weil, D.2    Standart, N.3
  • 24
    • 38049134877 scopus 로고    scopus 로고
    • CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes
    • Minshall, N., Reiter, M.-H., Weil, D. and Standart, N. (2007) CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes. J. Biol. Chem. 282, 37389-37401
    • (2007) J. Biol. Chem. , vol.282 , pp. 37389-37401
    • Minshall, N.1    Reiter, M.-H.2    Weil, D.3    Standart, N.4
  • 26
    • 49349088194 scopus 로고    scopus 로고
    • Translational control in early development: CPEB, P-bodies and germinal granules
    • Standart, N. and Minshall, N. (2008) Translational control in early development: CPEB, P-bodies and germinal granules. Biochem. Soc. Trans. 36, 671-676
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 671-676
    • Standart, N.1    Minshall, N.2
  • 27
    • 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.H., Mendez, R. and Richter, J.D. (1999) Maskin is a CPEB-associated factor that transiently interacts with eIF-4E. Mol. Cell 4, 1017-1027
    • (1999) Mol. Cell , vol.4 , pp. 1017-1027
    • Stebbins-Boaz, B.1    Cao, Q.2    De Moor, C.H.3    Mendez, R.4    Richter, J.D.5
  • 28
    • 41549097210 scopus 로고    scopus 로고
    • Translational control by cytoplasmic polyadenylation in Xenopus oocytes
    • Radford, H.E., Meijer, H.A. and de Moor, C.H. (2008) Translational control by cytoplasmic polyadenylation in Xenopus oocytes. Biochim. Biophys. Acta 1779, 217-229
    • (2008) Biochim. Biophys. Acta , vol.1779 , pp. 217-229
    • Radford, H.E.1    Meijer, H.A.2    De Moor, C.H.3
  • 29
    • 85192419842 scopus 로고    scopus 로고
    • From oocyte to fertilizable egg: Regulated mRNA expression and the control of maternal mRNA translation
    • (Kloc, M. and Kubiak, J.Z., eds), John Wiley and Sons, Oxford
    • Cragle, C.E. and MacNicol, A.M. (2014) From oocyte to fertilizable egg: regulated mRNA expression and the control of maternal mRNA translation. In Xenopus Development (Kloc, M. and Kubiak, J.Z., eds), John Wiley and Sons, Oxford
    • (2014) Xenopus Development
    • Cragle, C.E.1    Macnicol, A.M.2
  • 30
    • 18844397041 scopus 로고    scopus 로고
    • A new paradigm for translational control: Inhibition via 5-3 mRNA tethering by bicoid and the eIF4E cognate 4EHP
    • Cho, P.F., Poulin, F., Cho-Park, Y.A., Cho-Park, I.B., Chicoine, J.D., Lasko, P. and Sonenberg, N. (2005) A new paradigm for translational control: inhibition via 5-3 mRNA tethering by bicoid and the eIF4E cognate 4EHP. Cell 121, 411-423
    • (2005) Cell , vol.121 , pp. 411-423
    • Cho, P.F.1    Poulin, F.2    Cho-Park, Y.A.3    Cho-Park, I.B.4    Chicoine, J.D.5    Lasko, P.6    Sonenberg, N.7
  • 31
    • 84882645365 scopus 로고    scopus 로고
    • Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-transporter on its cellular distribution in HeLa cells
    • Kubacka, D., Kamenska, A., Broomhead, H., Minshall, N., Darzynkiewicz, E. and Standart, N. (2013) Investigating the consequences of eIF4E2 (4EHP) interaction with 4E-transporter on its cellular distribution in HeLa cells. PLoS ONE 8, e72761
    • (2013) PLoS ONE , vol.8
    • Kubacka, D.1    Kamenska, A.2    Broomhead, H.3    Minshall, N.4    Darzynkiewicz, E.5    Standart, N.6
  • 33
    • 84865658810 scopus 로고    scopus 로고
    • P-bodies and stress granules: Possible roles in the control of translation and mRNA degradation
    • Decker, C.J. and Parker, R. (2012) P-bodies and stress granules: possible roles in the control of translation and mRNA degradation. Cold Spring Harb. Perspect. Biol. 4, a012286
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Decker, C.J.1    Parker, R.2
  • 34
    • 17844371700 scopus 로고    scopus 로고
    • A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies
    • Andrei, M.A., Ingelfinger, D., Heintzmann, R., Achsel, T., Rivera-Pomar, R. and Lührmann, R. (2005) A role for eIF4E and eIF4E-transporter in targeting mRNPs to mammalian processing bodies. RNA 11, 717-727
    • (2005) RNA , vol.11 , pp. 717-727
    • Andrei, M.A.1    Ingelfinger, D.2    Heintzmann, R.3    Achsel, T.4    Rivera-Pomar, R.5    Lührmann, R.6
  • 36
    • 41149176379 scopus 로고    scopus 로고
    • Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation
    • Lee, H.C., Cho, H. and Kim, Y.K. (2008) Ectopic expression of eIF4E-transporter triggers the movement of eIF4E into P-bodies, inhibiting steady-state translation but not the pioneer round of translation. Biochem. Biophys. Res. Commun. 369, 1160-1165
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 1160-1165
    • Lee, H.C.1    Cho, H.2    Kim, Y.K.3
  • 38
    • 0842328579 scopus 로고    scopus 로고
    • Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression
    • Nelson, M.R., Leidal, A.M. and Smibert, C.A. (2004) Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression. EMBO J. 23, 150-159
    • (2004) EMBO J. , vol.23 , pp. 150-159
    • Nelson, M.R.1    Leidal, A.M.2    Smibert, C.A.3
  • 39
    • 80052972576 scopus 로고    scopus 로고
    • CUP promotes deadenylation and inhibits decapping of mRNA targets
    • Igreja, C. and Izaurralde, E. (2011) CUP promotes deadenylation and inhibits decapping of mRNA targets. Genes Dev. 25, 1955-1967
    • (2011) Genes Dev. , vol.25 , pp. 1955-1967
    • Igreja, C.1    Izaurralde, E.2
  • 40
    • 84865118901 scopus 로고    scopus 로고
    • Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression
    • Kinkelin, K., Veith, K., Grünwald, M. and Bono, F. (2012) Crystal structure of a minimal eIF4E-Cup complex reveals a general mechanism of eIF4E regulation in translational repression. RNA 18, 1624-1634
    • (2012) RNA , vol.18 , pp. 1624-1634
    • Kinkelin, K.1    Veith, K.2    Grünwald, M.3    Bono, F.4
  • 41
  • 42
    • 0029958353 scopus 로고    scopus 로고
    • Smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo
    • Smibert, C.A., Wilson, J.E., Kerr, K. and Macdonald, P.M. (1996) Smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo. Genes Dev. 10, 2600-2609
    • (1996) Genes Dev. , vol.10 , pp. 2600-2609
    • Smibert, C.A.1    Wilson, J.E.2    Kerr, K.3    Macdonald, P.M.4
  • 43
    • 0346554981 scopus 로고    scopus 로고
    • Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz
    • Wilhelm, J.E., Hilton, M., Amos, Q. and Henzel, W. (2003) Cup is an eIF4E binding protein required for both the translational repression of oskar and the recruitment of Barentsz. J. Cell Biol. 163, 1197-1204
    • (2003) J. Cell Biol. , vol.163 , pp. 1197-1204
    • Wilhelm, J.E.1    Hilton, M.2    Amos, Q.3    Henzel, W.4
  • 44
    • 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
  • 45
    • 32044471522 scopus 로고    scopus 로고
    • Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles
    • Chekulaeva, M., Hentze, M.W. and Ephrussi, A. (2006) Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles. Cell 124, 521-533
    • (2006) Cell , vol.124 , pp. 521-533
    • Chekulaeva, M.1    Hentze, M.W.2    Ephrussi, A.3
  • 46
    • 78650894705 scopus 로고    scopus 로고
    • Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels
    • Jeske, M., Moritz, B., Anders, A. and Wahle, E. (2011) Smaug assembles an ATP-dependent stable complex repressing nanos mRNA translation at multiple levels. EMBO J. 30, 90-103
    • (2011) EMBO J. , vol.30 , pp. 90-103
    • Jeske, M.1    Moritz, B.2    Anders, A.3    Wahle, E.4
  • 49
    • 77957661302 scopus 로고    scopus 로고
    • Zif-1 translational repression defines a second, mutually exclusive OMA function in germline transcriptional repression
    • Guven-Ozkan, T., Robertson, S.M., Nishi, Y. and Lin, R. (2010) zif-1 translational repression defines a second, mutually exclusive OMA function in germline transcriptional repression. Development 137, 3373-3382
    • (2010) Development , vol.137 , pp. 3373-3382
    • Guven-Ozkan, T.1    Robertson, S.M.2    Nishi, Y.3    Lin, R.4
  • 51
    • 84893912480 scopus 로고    scopus 로고
    • Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5-TOP mRNA translation
    • Tcherkezian, J., Cargnello, M., Romeo, Y., Huttlin, E.L., Lavoie, G., Gygi, S.P. and Roux, P.P. (2014) Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5-TOP mRNA translation. Genes Dev. 28, 357-371
    • (2014) Genes Dev. , vol.28 , pp. 357-371
    • Tcherkezian, J.1    Cargnello, M.2    Romeo, Y.3    Huttlin, E.L.4    Lavoie, G.5    Gygi, S.P.6    Roux, P.P.7
  • 52
    • 84879132779 scopus 로고    scopus 로고
    • The role of the DEAD-box RNA helicase DDX3 in mRNA metabolism
    • Soto-Rifo, R. and Ohlmann, T. (2013) The role of the DEAD-box RNA helicase DDX3 in mRNA metabolism. Wiley Interdiscip. Rev. RNA 4, 369-385
    • (2013) Wiley Interdiscip. Rev. RNA , vol.4 , pp. 369-385
    • Soto-Rifo, R.1    Ohlmann, T.2
  • 54
    • 70349193390 scopus 로고    scopus 로고
    • Identification of gemin5 as a novel 7-methylguanosine cap-binding protein
    • Bradrick, S.S. and Gromeier, M. (2009) Identification of gemin5 as a novel 7-methylguanosine cap-binding protein. PLoS ONE 4, e7030
    • (2009) PLoS ONE , vol.4
    • Bradrick, S.S.1    Gromeier, M.2
  • 58
    • 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
  • 59
    • 0028825724 scopus 로고
    • Characterization of the in vivo phosphorylation sites of the mRNA cap-binding complex proteins eukaryotic initiation factor-4E and p20 in Saccharomyces cerevisiae
    • Zanchin, N.I. and McCarthy, J.E.G. (1995) Characterization of the in vivo phosphorylation sites of the mRNA cap-binding complex proteins eukaryotic initiation factor-4E and p20 in Saccharomyces cerevisiae. J. Biol. Chem. 270, 26505-26510
    • (1995) J. Biol. Chem. , vol.270 , pp. 26505-26510
    • Zanchin, N.I.1    McCarthy, J.E.G.2
  • 60
    • 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.A. 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.A.2    Ashe, M.P.3
  • 62
    • 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
  • 63
    • 84903369142 scopus 로고    scopus 로고
    • MRNA localization to P-bodies in yeast is bi-phasic with many mRNAs captured in a late Bfr1p-dependent wave
    • Simpson, C.E., Lui, J., Kershaw, C.J., Sims, P.F. and Ashe, M.P. (2014) mRNA localization to P-bodies in yeast is bi-phasic with many mRNAs captured in a late Bfr1p-dependent wave. J. Cell Sci. 127, 1254-1262
    • (2014) J. Cell Sci. , vol.127 , pp. 1254-1262
    • Simpson, C.E.1    Lui, J.2    Kershaw, C.J.3    Sims, P.F.4    Ashe, M.P.5
  • 65
    • 84868699644 scopus 로고    scopus 로고
    • A eukaryotic translation initiation factor 4E-binding protein promotes mRNA decapping and is required for PUF repression
    • Blewett, N.H. and Goldstrohm, A.C. (2012) A eukaryotic translation initiation factor 4E-binding protein promotes mRNA decapping and is required for PUF repression. Mol. Cell. Biol. 32, 4181-4194
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4181-4194
    • Blewett, N.H.1    Goldstrohm, A.C.2
  • 66
    • 84867374203 scopus 로고    scopus 로고
    • The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay
    • Rendl, L.M., Bieman, M.A., Vari, H.K. and Smibert, C.A. (2012) The eIF4E-binding protein Eap1p functions in Vts1p-mediated transcript decay. PLoS ONE 7, e47121
    • (2012) PLoS ONE , vol.7
    • Rendl, L.M.1    Bieman, M.A.2    Vari, H.K.3    Smibert, C.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.