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Volumn 2012, Issue , 2012, Pages

Evolutionary conservation and diversification of the translation initiation apparatus in trypanosomatids

Author keywords

[No Author keywords available]

Indexed keywords

CAP BINDING PROTEIN; INITIATION FACTOR 4F; MESSENGER RNA; POLYADENYLIC ACID BINDING PROTEIN; SPLICED LEADER RNA;

EID: 84864953147     PISSN: 15316912     EISSN: 15326268     Source Type: Journal    
DOI: 10.1155/2012/813718     Document Type: Review
Times cited : (31)

References (90)
  • 1
    • 0032834055 scopus 로고    scopus 로고
    • EIF4 initiation factors: Effectors of mRNA recruitment to ribosomes and regulators of translation
    • DOI 10.1146/annurev.biochem.68.1.913
    • Gingras A. C., Raught B., Sonenberg N., eIF4 initiation factors: effectors of mRNA recruitment to ribosomes and regulators of translation Annual Review of Biochemistry 1999 68 913 963 (Pubitemid 29449212)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 913-963
    • Gingras, A.-C.1    Raught, B.2    Sonenberg, N.3
  • 2
    • 33846991130 scopus 로고    scopus 로고
    • The mechanism of translation initiation in Eukaryotes
    • Mathews M. B. Sonenberg N. Hershey J. W. B. Cold Spring Harbor Cold Spring Harbor, NY, USA
    • Pestova T. V., Lorch J. R., Hellen C. H. T., Mathews M. B., Sonenberg N., Hershey J. W. B., The mechanism of translation initiation in Eukaryotes Translation Control in Biology and Medicine 2007 Cold Spring Harbor Cold Spring Harbor, NY, USA 87 128
    • (2007) Translation Control in Biology and Medicine , pp. 87-128
    • Pestova, T.V.1    Lorch, J.R.2    Hellen, C.H.T.3
  • 3
    • 0347281686 scopus 로고    scopus 로고
    • Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E
    • DOI 10.1016/S0092-8674(03)00975-9
    • Gross J. D., Moerke N. J., Von Der Haar T., Lugovskoy A. A., Sachs A. B., McCarthy J. E. G., Wagner G., Ribosome loading onto the mRNA cap is driven by conformational coupling between eIF4G and eIF4E Cell 2003 115 6 739 750 (Pubitemid 38030302)
    • (2003) Cell , vol.115 , Issue.6 , pp. 739-750
    • Gross, J.D.1    Moerke, N.J.2    Von Der Haar, T.3    Lugovskoy, A.A.4    Sachs, A.B.5    McCarthy, J.E.G.6    Wagner, G.7
  • 5
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • DOI 10.1038/nature06974, PII NATURE06974
    • Amrani N., Ghosh S., Mangus D. A., Jacobson A., Translation factors promote the formation of two states of the closed-loop mRNP Nature 2008 453 7199 1276 1280 (Pubitemid 351913593)
    • (2008) Nature , vol.453 , Issue.7199 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 6
    • 34548509679 scopus 로고    scopus 로고
    • EIF4G, eIFiso4G, and eIF4B bind the poly(A)-binding protein through overlapping sites within the RNA recognition motif domains
    • DOI 10.1074/jbc.M702193200
    • Cheng S., Gallie D. R., eIF4G, eIFiso4G, and eIF4B bind the poly(A)-binding protein through overlapping sites within the RNA recognition motif domains Journal of Biological Chemistry 2007 282 35 25247 25258 (Pubitemid 47372779)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.35 , pp. 25247-25258
    • Cheng, S.1    Gallie, D.R.2
  • 7
    • 34447302886 scopus 로고    scopus 로고
    • Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
    • DOI 10.1038/sj.emboj.7601751, PII 7601751
    • Unbehaun A., Marintchev A., Lomakin I. B., Didenko T., Wagner G., Hellen C. U. T., Pestova T. V., Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing EMBO Journal 2007 26 13 3109 3123 (Pubitemid 47057491)
    • (2007) EMBO Journal , vol.26 , Issue.13 , pp. 3109-3123
    • Unbehaun, A.1    Marintchev, A.2    Lomakin, I.B.3    Didenko, T.4    Wagner, G.5    Hellen, C.U.T.6    Pestova, T.V.7
  • 8
    • 53349147033 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 6 is rate-limiting in translation, growth and transformation
    • Gandin V., Miluzio A., Barbieri A. M., Beugnet A., Kiyokawa H., Marchisio P. C., Biffo S., Eukaryotic initiation factor 6 is rate-limiting in translation, growth and transformation Nature 2008 455 7213 684 688
    • (2008) Nature , vol.455 , Issue.7213 , pp. 684-688
    • Gandin, V.1    Miluzio, A.2    Barbieri, A.M.3    Beugnet, A.4    Kiyokawa, H.5    Marchisio, P.C.6    Biffo, S.7
  • 9
    • 24944469031 scopus 로고    scopus 로고
    • Structural basis for the enhancement of eIF4A helicase activity by eIF4G
    • DOI 10.1101/gad.1335305
    • Oberer M., Marintchev A., Wagner G., Structural basis for the enhancement of eIF4A helicase activity by eIF4G Genes and Development 2005 19 18 2212 2223 (Pubitemid 41330322)
    • (2005) Genes and Development , vol.19 , Issue.18 , pp. 2212-2223
    • Oberer, M.1    Marintchev, A.2    Wagner, G.3
  • 10
    • 0030666625 scopus 로고    scopus 로고
    • Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A
    • Imataka H., Sonenberg N., Human eukaryotic translation initiation factor 4G (eIF4G) possesses two separate and independent binding sites for eIF4A Molecular and Cellular Biology 1997 17 12 6940 6947 (Pubitemid 27505924)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.12 , pp. 6940-6947
    • Imataka, H.1    Sonenberg, N.2
  • 11
    • 0028331455 scopus 로고
    • The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence
    • Methot N., Pause A., Hershey J. W. B., Sonenberg N., The translation initiation factor eIF-4B contains an RNA-binding region that is distinct and independent from its ribonucleoprotein consensus sequence Molecular and Cellular Biology 1994 14 4 2307 2316 (Pubitemid 24108212)
    • (1994) Molecular and Cellular Biology , vol.14 , Issue.4 , pp. 2307-2316
    • Methot, N.1    Pause, A.2    Hershey, J.W.B.3    Sonenberg, N.4
  • 12
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • DOI 10.1101/gad.891101
    • Hellen C. U. T., Sarnow P., Internal ribosome entry sites in eukaryotic mRNA molecules Genes and Development 2001 15 13 1593 1612 (Pubitemid 32702581)
    • (2001) Genes and Development , vol.15 , Issue.13 , pp. 1593-1612
    • Hellen, C.U.T.1    Sarnow, P.2
  • 14
    • 33646884832 scopus 로고    scopus 로고
    • Assessing IRES activity in the HIF-1α and other cellular 5′ UTRs
    • DOI 10.1261/rna.2320506
    • Bert A. G., Grépin R., Vadas M. A., Goodall G. J., Assessing IRES activity in the HIF-1 and other cellular 5′ UTRs RNA 2006 12 6 1074 1083 (Pubitemid 43788125)
    • (2006) RNA , vol.12 , Issue.6 , pp. 1074-1083
    • Bert, A.G.1    Grepin, R.2    Vadas, M.A.3    Goodall, G.J.4
  • 15
    • 0034307483 scopus 로고    scopus 로고
    • Internal ribosome initiation of translation and the control of cell death
    • Holcik M., Sonenberg N., Korneluk R. G., Internal ribosome initiation of translation and the control of cell death Trends in Genetics 2000 16 10 469 473
    • (2000) Trends in Genetics , vol.16 , Issue.10 , pp. 469-473
    • Holcik, M.1    Sonenberg, N.2    Korneluk, R.G.3
  • 16
    • 17144424622 scopus 로고    scopus 로고
    • Translational control in stress and apoptosis
    • DOI 10.1038/nrm1618
    • Holcik M., Sonenberg N., Translational control in stress and apoptosis Nature Reviews Molecular Cell Biology 2005 6 4 318 327 (Pubitemid 40516898)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.4 , pp. 318-327
    • Holcik, M.1    Sonenberg, N.2
  • 17
    • 70350696063 scopus 로고    scopus 로고
    • Differential contribution of the m 7 G-cap to the 5 ′ end-dependent translation initiation of mammalian mRNAs
    • Andreev D. E., Dmitriev S. E., Terenin I. M., Prassolov V. S., Merrick W. C., Shatsky I. N., Differential contribution of the m 7 G-cap to the 5 ′ end-dependent translation initiation of mammalian mRNAs Nucleic Acids Research 2009 37 18 6135 6147
    • (2009) Nucleic Acids Research , vol.37 , Issue.18 , pp. 6135-6147
    • Andreev, D.E.1    Dmitriev, S.E.2    Terenin, I.M.3    Prassolov, V.S.4    Merrick, W.C.5    Shatsky, I.N.6
  • 18
    • 77956940474 scopus 로고    scopus 로고
    • The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway
    • Mitchell S. F., Walker S. E., Algire M. A., Park E. H., Hinnebusch A. G., Lorsch J. R., The 5'-7-methylguanosine cap on eukaryotic mRNAs serves both to stimulate canonical translation initiation and to block an alternative pathway Molecular Cell 2010 39 6 950 962
    • (2010) Molecular Cell , vol.39 , Issue.6 , pp. 950-962
    • Mitchell, S.F.1    Walker, S.E.2    Algire, M.A.3    Park, E.H.4    Hinnebusch, A.G.5    Lorsch, J.R.6
  • 19
    • 0028034233 scopus 로고
    • Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function
    • Pause A., Belsham G. J., Gingras A. C., Donze O., Lin T. A., Lawrence J. C., Sonenberg N., Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5'-cap function Nature 1994 371 6500 762 767
    • (1994) Nature , vol.371 , Issue.6500 , pp. 762-767
    • Pause, A.1    Belsham, G.J.2    Gingras, A.C.3    Donze, O.4    Lin, T.A.5    Lawrence, J.C.6    Sonenberg, N.7
  • 20
    • 0028126506 scopus 로고
    • PHAS-I as a link between mitogen-activated protein kinase and translation initiation
    • Lin T. A., Kong X., Haystead T. A. J., Pause A., Belsham G., Sonenberg N., Lawrence J. C., PHAS-I as a link between mitogen-activated protein kinase and translation initiation Science 1994 266 5185 653 656 (Pubitemid 24363524)
    • (1994) Science , vol.266 , Issue.5185 , pp. 653-656
    • Lin, T.-A.1    Kong, X.2    Haystead, T.A.J.3    Pause, A.4    Belsham, G.5    Sonenberg, N.6    Lawrence Jr., J.C.7
  • 21
    • 13444259647 scopus 로고    scopus 로고
    • Regulation of cap-dependent translation by eIF4E inhibitory proteins
    • DOI 10.1038/nature03205
    • Richter J. D., Sonenberg N., Regulation of cap-dependent translation by eIF4E inhibitory proteins Nature 2005 433 7025 477 480 (Pubitemid 40204297)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 477-480
    • Richter, J.D.1    Sonenberg, N.2
  • 22
    • 0030883848 scopus 로고    scopus 로고
    • PHAS/4E-BPs as regulators of mRNA translation and cell proliferation
    • Lawrence J. C., Abraham R. T., PHAS/4E-BPs as regulators of mRNA translation and cell proliferation Trends in Biochemical Sciences 1997 22 9 345 349
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.9 , pp. 345-349
    • Lawrence, J.C.1    Abraham, R.T.2
  • 25
    • 70450204007 scopus 로고    scopus 로고
    • An emerging role of mTOR in lipid biosynthesis
    • Laplante M., Sabatini D. M., An emerging role of mTOR in lipid biosynthesis Current Biology 2009 19 22 R1046 R1052
    • (2009) Current Biology , vol.19 , Issue.22
    • Laplante, M.1    Sabatini, D.M.2
  • 27
    • 0037154965 scopus 로고    scopus 로고
    • Gene-specific regulation by general translation factors
    • DOI 10.1016/S0092-8674(02)00642-6
    • Dever T. E., Gene-specific regulation by general translation factors Cell 2002 108 4 545 556 (Pubitemid 34260879)
    • (2002) Cell , vol.108 , Issue.4 , pp. 545-556
    • Dever, T.E.1
  • 28
    • 0022133046 scopus 로고
    • The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader
    • McGarry T. J., Lindquist S., The preferential translation of Drosophila hsp70 mRNA requires sequences in the untranslated leader Cell 1985 42 3 903 911
    • (1985) Cell , vol.42 , Issue.3 , pp. 903-911
    • McGarry, T.J.1    Lindquist, S.2
  • 29
    • 0022109611 scopus 로고
    • Selective translation of heat shock mRNA in Drosophila melanogaster depends on sequence information in the leader
    • Klemenz R., Hultmark D., Gehring W. J., Selective translation of heat shock mRNA in Drosophila melanogaster depends on sequence information in the leader EMBO Journal 1985 4 8 2053 2060
    • (1985) EMBO Journal , vol.4 , Issue.8 , pp. 2053-2060
    • Klemenz, R.1    Hultmark, D.2    Gehring, W.J.3
  • 30
    • 9644275414 scopus 로고    scopus 로고
    • Translational regulation of Hsp90 mRNA: Aug-proximal 5́- untranslated region elements essential for preferential heat shock translation
    • DOI 10.1074/jbc.M404681200
    • Ahmed R., Duncan R. F., Translational regulation of Hsp90 mRNA: AUG-proximal 5 ′ -untranslated region elements essential for preferential heat shock translation Journal of Biological Chemistry 2004 279 48 49919 49930 (Pubitemid 39577800)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.48 , pp. 49919-49930
    • Ahmed, R.1    Duncan, R.F.2
  • 31
    • 0021320759 scopus 로고
    • Identification of an infective stage of Leishmania promastigotes
    • Sacks D. L., Perkins P. V., Identification of an infective stage of Leishmania promastigotes Science 1984 223 4643 1417 1419 (Pubitemid 14161006)
    • (1984) Science , vol.223 , Issue.4643 , pp. 1417-1419
    • Sacks, D.L.1    Perkins, P.V.2
  • 33
    • 0017311847 scopus 로고
    • Multiplication of a human parasite (Leishmania donovani) in phagolysosomes of hamster macrophages in vitro
    • Chang K. P., Dwyer D. M., Multiplication of a human parasite (Leishmania donovani) in phagolysosomes of hamster macrophages in vitro Science 1976 193 4254 678 680
    • (1976) Science , vol.193 , Issue.4254 , pp. 678-680
    • Chang, K.P.1    Dwyer, D.M.2
  • 34
    • 0002549642 scopus 로고
    • Biology of Leishmania and leishmaniasis
    • Chang K. P. Bray R. S. Amsterdam, The Netherlands Elsevier
    • Chang K. P., Fong D., Bray R. S., Chang K. P., Bray R. S., Biology of Leishmania and leishmaniasis Leishmaniasis 1985 Amsterdam, The Netherlands Elsevier 1 30
    • (1985) Leishmaniasis , pp. 1-30
    • Chang, K.P.1    Fong, D.2    Bray, R.S.3
  • 35
    • 0027138234 scopus 로고
    • Evolution of nuclear ribosomal RNAs in kinetoplastid protozoa: Perspectives on the age and origins of parasitism
    • DOI 10.1073/pnas.90.24.11608
    • Fernandes A. P., Nelson K., Beverley S. M., Evolution of nuclear ribosomal RNAs in kinetoplastid protozoa: perspectives on the age and origins of parasitism Proceedings of the National Academy of Sciences of the United States of America 1993 90 24 11608 11612 (Pubitemid 24008688)
    • (1993) Proceedings of the National Academy of Sciences of the United States of America , vol.90 , Issue.24 , pp. 11608-11612
    • Fernandes, A.P.1    Nelson, K.2    Beverley, S.M.3
  • 36
    • 0037090528 scopus 로고    scopus 로고
    • Life without transcriptional control? From fly to man and back again
    • DOI 10.1093/emboj/21.8.1881
    • Clayton C. E., Life without transcriptional control? From fly to man and back again EMBO Journal 2002 21 8 1881 1888 (Pubitemid 34437185)
    • (2002) EMBO Journal , vol.21 , Issue.8 , pp. 1881-1888
    • Clayton, C.E.1
  • 37
    • 79955619183 scopus 로고    scopus 로고
    • Trans-splicing in trypanosomes: Machinery and its impact on the parasite transcriptome
    • Michaeli S., Trans-splicing in trypanosomes: machinery and its impact on the parasite transcriptome Future Microbiology 2011 6 4 459 474
    • (2011) Future Microbiology , vol.6 , Issue.4 , pp. 459-474
    • Michaeli, S.1
  • 38
    • 35349012982 scopus 로고    scopus 로고
    • Post-transcriptional regulation of gene expression in trypanosomes and leishmanias
    • DOI 10.1016/j.molbiopara.2007.07.007, PII S0166685107002101
    • Clayton C., Shapira M., Post-transcriptional regulation of gene expression in trypanosomes and leishmanias Molecular and Biochemical Parasitology 2007 156 2 93 101 (Pubitemid 47600362)
    • (2007) Molecular and Biochemical Parasitology , vol.156 , Issue.2 , pp. 93-101
    • Clayton, C.1    Shapira, M.2
  • 39
    • 0142247085 scopus 로고    scopus 로고
    • Trans and cis splicing in trypanosomatids: Mechanism, factors, and regulation
    • DOI 10.1128/EC.2.5.830-840.2003
    • Liang X. H., Haritan A., Uliel S., Michaeli S., trans and cis splicing in trypanosomatids: mechanism, factors, and regulation Eukaryotic Cell 2003 2 5 830 840 (Pubitemid 37298696)
    • (2003) Eukaryotic Cell , vol.2 , Issue.5 , pp. 830-840
    • Liang, X.-H.1    Haritan, A.2    Uliel, S.3    Michaeli, S.4
  • 41
    • 0037144435 scopus 로고    scopus 로고
    • On the role of exon and intron sequences in trans-splicing utilization and cap 4 modification of the trypanosomatid Leptomonas collosoma SL RNA
    • Mandelboim M., Estrao C. L., Tschudi C., Ullu E., Michaeli S., On the role of exon and intron sequences in trans-splicing utilization and cap 4 modification of the trypanosomatid Leptomonas collosoma SL RNA Journal of Biological Chemistry 2002 277 38 35210 35218
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.38 , pp. 35210-35218
    • Mandelboim, M.1    Estrao, C.L.2    Tschudi, C.3    Ullu, E.4    Michaeli, S.5
  • 42
    • 34447250502 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma brucei cap hypermethylase Tgs1
    • DOI 10.1016/j.molbiopara.2007.05.008, PII S0166685107001454
    • Ruan J. P., Ullu E., Tschudi C., Characterization of the Trypanosoma brucei cap hypermethylase Tgs1 Molecular and Biochemical Parasitology 2007 155 1 66 69 (Pubitemid 47042216)
    • (2007) Molecular and Biochemical Parasitology , vol.155 , Issue.1 , pp. 66-69
    • Ruan, J.-p.1    Ullu, E.2    Tschudi, C.3
  • 43
    • 33645843623 scopus 로고    scopus 로고
    • 2 ′ -O-Methylation of position 2 of the trypanosome spliced leader cap 4 is mediated by a 48 kDa protein related to vaccinia virus VP39
    • Arhin G. K., Ullu E., Tschudi C., 2 ′ -O-Methylation of position 2 of the trypanosome spliced leader cap 4 is mediated by a 48 kDa protein related to vaccinia virus VP39 Molecular and Biochemical Parasitology 2006 147 1 137 139
    • (2006) Molecular and Biochemical Parasitology , vol.147 , Issue.1 , pp. 137-139
    • Arhin, G.K.1    Ullu, E.2    Tschudi, C.3
  • 44
  • 46
    • 33845622060 scopus 로고    scopus 로고
    • Binding specificities and potential roles of isoforms of eukaryotic initiation factor 4E in Leishmania
    • DOI 10.1128/EC.00230-06
    • Yoffe Y., Zuberek J., Lerer A., Lewdorowicz M., Stepinski J., Altmann M., Darzynkiewicz E., Shapira M., Binding specificities and potential roles of isoforms of eukaryotic initiation factor 4E in Leishmania Eukaryotic Cell 2006 5 12 1969 1979 (Pubitemid 44956809)
    • (2006) Eukaryotic Cell , vol.5 , Issue.12 , pp. 1969-1979
    • Yoffe, Y.1    Zuberek, J.2    Lerer, A.3    Lewdorowicz, M.4    Stepinski, J.5    Altmann, M.6    Darzynkiewicz, E.7    Shapira, M.8
  • 47
    • 0030728936 scopus 로고    scopus 로고
    • Cocrystal structure of the messenger RNA 5' cap-binding protein (elF4E) bound to 7-methyl-GDP
    • Marcotrigiano J., Gingras A. C., Sonenberg N., Burley S. K., Cocrystal structure of the messenger RNA 5' cap-binding protein (elF4E) bound to 7-methyl-GDP Cell 1997 89 6 951 961 (Pubitemid 27513521)
    • (1997) Cell , vol.89 , Issue.6 , pp. 951-961
    • Marcotrigiano, J.1    Gingras, A.-C.2    Sonenberg, N.3    Burley, S.K.4
  • 49
    • 0033597729 scopus 로고    scopus 로고
    • The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1
    • Hershey P. E. C., McWhirter S. M., Gross J. D., Wagner G., Alber T., Sachs A. B., The cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1 Journal of Biological Chemistry 1999 274 30 21297 21304
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.30 , pp. 21297-21304
    • Hershey, P.E.C.1    McWhirter, S.M.2    Gross, J.D.3    Wagner, G.4    Alber, T.5    Sachs, A.B.6
  • 51
    • 0024361258 scopus 로고
    • A mammalian translation initiation factor can substitute for its yeast homologue in vivo
    • Altmann M., Muller P. P., Pelletier J., Sonenberg N., Trachsel H., A mammalian translation initiation factor can substitute for its yeast homologue in vivo Journal of Biological Chemistry 1989 264 21 12145 12147 (Pubitemid 19191096)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.21 , pp. 12145-12147
    • Altmann, M.1    Muller, P.P.2    Pelletier, J.3    Sonenberg, N.4    Trachsel, H.5
  • 56
    • 80455178807 scopus 로고    scopus 로고
    • A novel 4E-interacting protein in Leishmania is involved in stage-specific translation pathways
    • Zinoviev A., Leger M., Wagner G., Shapira M., A novel 4E-interacting protein in Leishmania is involved in stage-specific translation pathways Nucleic Acids Research 2011 39 8404 8415
    • (2011) Nucleic Acids Research , vol.39 , pp. 8404-8415
    • Zinoviev, A.1    Leger, M.2    Wagner, G.3    Shapira, M.4
  • 57
    • 0024495356 scopus 로고
    • In vitro synthesis, phosphorylation, and localization on 48 S initiation complexes of human protein synthesis initiation factor 4E
    • Hiremath L. S., Hiremath S. T., Rychlik W., Joshi S., Domier L. L., Rhoads R. E., in vitro synthesis, phosphorylation, and localization on 48 S initiation complexes of human protein synthesis initiation factor 4E Journal of Biological Chemistry 1989 264 2 1132 1138 (Pubitemid 19038103)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.2 , pp. 1132-1138
    • Hiremath, L.S.1    Hiremath, S.T.2    Rychlik, W.3    Joshi, S.4    Domier, L.L.5    Rhoads, R.E.6
  • 58
    • 0030009739 scopus 로고    scopus 로고
    • A reevaluation of the Cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate
    • DOI 10.1074/jbc.271.15.8983
    • Rau M., Ohlmann T., Morley S. J., Pain V. M., A reevaluation of the Cap-binding protein, eIF4E, as a rate-limiting factor for initiation of translation in reticulocyte lysate Journal of Biological Chemistry 1996 271 15 8983 8990 (Pubitemid 26123327)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.15 , pp. 8983-8990
    • Rau, M.1    Ohlmann, T.2    Morley, S.J.3    Pain, V.M.4
  • 59
    • 55049098755 scopus 로고    scopus 로고
    • Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2 phosphorylation at Thr169
    • Kramer S., Queiroz R., Ellis L., Webb H., Hoheisel J. D., Clayton C., Carrington M., Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2 phosphorylation at Thr169 Journal of Cell Science 2008 121 18 3002 3014
    • (2008) Journal of Cell Science , vol.121 , Issue.18 , pp. 3002-3014
    • Kramer, S.1    Queiroz, R.2    Ellis, L.3    Webb, H.4    Hoheisel, J.D.5    Clayton, C.6    Carrington, M.7
  • 60
    • 34447572786 scopus 로고    scopus 로고
    • Recruitment of mRNAs to cytoplasmic ribonucleoprotein granules in trypanosomes
    • DOI 10.1111/j.1365-2958.2007.05833.x
    • Cassola A., De Gaudenzi J. G., Frasch A. C., Recruitment of mRNAs to cytoplasmic ribonucleoprotein granules in trypanosomes Molecular Microbiology 2007 65 3 655 670 (Pubitemid 47077240)
    • (2007) Molecular Microbiology , vol.65 , Issue.3 , pp. 655-670
    • Cassola, A.1    De Gaudenzi, J.G.2    Frasch, A.C.3
  • 61
    • 0035105502 scopus 로고    scopus 로고
    • A conserved HEAT domain within eIF4G Directs Assembly of the Translation Initiation Machinery
    • DOI 10.1016/S1097-2765(01)00167-8
    • Marcotrigiano J., Lomakin I. B., Sonenberg N., Pestova T. V., Hellen C. U. T., Burley S. K., A conserved HEAT domain within eIF4G directs assembly of the translation initiation machinery Molecular Cell 2001 7 1 193 203 (Pubitemid 32162912)
    • (2001) Molecular Cell , vol.7 , Issue.1 , pp. 193-203
    • Marcotrigiano, J.1    Lomakin, I.B.2    Sonenberg, N.3    Pestova, T.V.4    Hellen, C.U.T.5    Burley, S.K.6
  • 62
    • 24944572189 scopus 로고    scopus 로고
    • EIF4G and CBP80 share a common origin and similar domain organization: Implications for the structure and function of eIF4G
    • DOI 10.1021/bi051271v
    • Marintchev A., Wagner G., eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G Biochemistry 2005 44 37 12265 12272 (Pubitemid 41324319)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12265-12272
    • Marintchev, A.1    Wagner, G.2
  • 63
    • 0029166687 scopus 로고
    • The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 and the translational repressors 4E-binding proteins
    • Mader S., Lee H., Pause A., Sonenberg N., The translation initiation factor eIF-4E binds to a common motif shared by the translation factor eIF-4 and the translational repressors 4E-binding proteins Molecular and Cellular Biology 1995 15 9 4990 4997
    • (1995) Molecular and Cellular Biology , vol.15 , Issue.9 , pp. 4990-4997
    • Mader, S.1    Lee, H.2    Pause, A.3    Sonenberg, N.4
  • 66
    • 33749139723 scopus 로고    scopus 로고
    • Dead-box proteins: A family affair - Active and passive players in RNP-remodeling
    • DOI 10.1093/nar/gkl468
    • Linder P., Dead-box proteins: a family affairactive and passive players in RNP-remodeling Nucleic Acids Research 2006 34 15 4168 4180 (Pubitemid 44542196)
    • (2006) Nucleic Acids Research , vol.34 , Issue.15 , pp. 4168-4180
    • Linder, P.1
  • 68
    • 11844281461 scopus 로고    scopus 로고
    • Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
    • DOI 10.1101/gad.1262905
    • Kahvejian A., Svitkin Y. V., Sukarieh R., M'Boutchou M. N., Sonenberg N., Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms Genes and Development 2005 19 1 104 113 (Pubitemid 40095820)
    • (2005) Genes and Development , vol.19 , Issue.1 , pp. 104-113
    • Kahvejian, A.1    Svitkin, Y.V.2    Sukarieh, R.3    M'Boutchou, M.-N.4    Sonenberg, N.5
  • 69
    • 0033578927 scopus 로고    scopus 로고
    • Recognition of polyadenylate RNA by the poly(A)-binding protein
    • DOI 10.1016/S0092-8674(00)81517-2
    • Deo R. C., Bonanno J. B., Sonenberg N., Burley S. K., Recognition of polyadenylate RNA by the poly(A)-binding protein Cell 1999 98 6 835 845 (Pubitemid 29446900)
    • (1999) Cell , vol.98 , Issue.6 , pp. 835-845
    • Deo, R.C.1    Bonanno, J.B.2    Sonenberg, N.3    Burley, S.K.4
  • 70
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells S. E., Hillner P. E., Vale R. D., Sachs A. B., Circularization of mRNA by eukaryotic translation initiation factors Molecular Cell 1998 2 1 135 140 (Pubitemid 128378975)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 72
    • 28844476749 scopus 로고    scopus 로고
    • Alternative mechanisms of initiating translation of mammalian mRNAs
    • DOI 10.1042/BST20051231
    • Jackson R. J., Alternative mechanisms of initiating translation of mammalian mRNAs Biochemical Society Transactions 2005 33 6 1231 1241 (Pubitemid 41779656)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.6 , pp. 1231-1241
    • Jackson, R.J.1
  • 74
    • 0034159895 scopus 로고    scopus 로고
    • Poly(A)-binding protein I of Leishmania: Functional analysis and localisation in trypanosomatid parasites
    • Bates E. J., Knuepfer E., Smith D. F., Poly(A)-binding protein I of Leishmania: functional analysis and localisation in trypanosomatid parasites Nucleic Acids Research 2000 28 5 1211 1220 (Pubitemid 30107693)
    • (2000) Nucleic Acids Research , vol.28 , Issue.5 , pp. 1211-1220
    • Bates, E.J.1    Knuepfer, E.2    Smith, D.F.3
  • 75
    • 0033832476 scopus 로고    scopus 로고
    • Identification of a putative regulatory element in the 3'-untranslated region that controls expression of HSP70 in Leishmania infantum
    • Quijada L., Soto M., Alonso C., Requena J. M., Identification of a putative regulatory element in the 3'-untranslated region that controls expression of HSP70 in Leishmania infantum Molecular and Biochemical Parasitology 2000 110 1 79 91
    • (2000) Molecular and Biochemical Parasitology , vol.110 , Issue.1 , pp. 79-91
    • Quijada, L.1    Soto, M.2    Alonso, C.3    Requena, J.M.4
  • 76
    • 27444431869 scopus 로고    scopus 로고
    • The translational efficiencies of the two Leishmania infantum HSP70 mRNAs, differing in their 3′-untranslated regions, are affected by shifts in the temperature of growth through different mechanisms
    • DOI 10.1074/jbc.M505559200
    • Folgueira C., Quijada L., Soto M., Abanades D. R., Alonso C., Requena J. M., The translational efficiencies of the two Leishmania infantum HSP70 mRNAs, differing in their 3 ′ -untranslated regions, are affected by shifts in the temperature of growth through different mechanisms Journal of Biological Chemistry 2005 280 42 35172 35183 (Pubitemid 41532704)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35172-35183
    • Folgueira, C.1    Quijada, L.2    Soto, M.3    Abanades, D.R.4    Alonso, C.5    Requena, J.M.6
  • 77
    • 0035930556 scopus 로고    scopus 로고
    • Developmental regulation of heat shock protein 83 in Leishmania: 3′ processing and mRNA stability control transcript abundance, and translation is directed by a determinant in the 3′-untranslated region
    • Zilka A., Garlapati S., Dahan E., Yaolsky V., Shapira M., Developmental regulation of heat shock protein 83 in Leishmania: 3′ processing and mRNA stability control transcript abundance, and translation is directed by a determinant in the 3′-untranslated region Journal of Biological Chemistry 2001 276 51 47922 47929
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.51 , pp. 47922-47929
    • Zilka, A.1    Garlapati, S.2    Dahan, E.3    Yaolsky, V.4    Shapira, M.5
  • 78
    • 26444522312 scopus 로고    scopus 로고
    • The expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translation
    • Larreta R., Soto M., Quijada L., Folgueira C., Abanades D. R., Alonso C., Requena J. M., The expression of HSP83 genes in Leishmania infantum is affected by temperature and by stage-differentiation and is regulated at the levels of mRNA stability and translation BMC Molecular Biology 2004 5, article 3
    • (2004) BMC Molecular Biology , vol.53
    • Larreta, R.1    Soto, M.2    Quijada, L.3    Folgueira, C.4    Abanades, D.R.5    Alonso, C.6    Requena, J.M.7
  • 79
    • 75149175207 scopus 로고    scopus 로고
    • Preferential translation of Hsp83 in Leishmania requires a thermosensitive polypyrimidine-rich element in the 3 ′ UTR and involves scanning of the 5 ′ UTR
    • David M., Gabdank I., Ben-David M., Zilka A., Orr I., Barash D., Shapira M., Preferential translation of Hsp83 in Leishmania requires a thermosensitive polypyrimidine-rich element in the 3 ′ UTR and involves scanning of the 5 ′ UTR RNA 2010 16 2 364 374
    • (2010) RNA , vol.16 , Issue.2 , pp. 364-374
    • David, M.1    Gabdank, I.2    Ben-David, M.3    Zilka, A.4    Orr, I.5    Barash, D.6    Shapira, M.7
  • 80
    • 84934438960 scopus 로고    scopus 로고
    • UNAFold: Software for nucleic acid folding and hybridization
    • Markham N. R., Zuker M., UNAFold: software for nucleic acid folding and hybridization Methods in Molecular Biology 2008 453 3 31
    • (2008) Methods in Molecular Biology , vol.453 , pp. 3-31
    • Markham, N.R.1    Zuker, M.2
  • 81
    • 0037205486 scopus 로고    scopus 로고
    • A common mechanism of stage-regulated gene expression in Leishmania mediated by a conserved 3′-untranslated region element
    • DOI 10.1074/jbc.M200500200
    • Boucher N., Wu Y., Dumas C., Dubé M., Sereno D., Breton M., Papadopoulou B., A common mechanism of stage-regulated gene expression in Leishmania mediated by a conserved 3 ′ -untranslated region element Journal of Biological Chemistry 2002 277 22 19511 19520 (Pubitemid 34967463)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19511-19520
    • Boucher, N.1    Wu, Y.2    Dumas, C.3    Dube, M.4    Sereno, D.5    Breton, M.6    Papadopoulou, B.7
  • 82
    • 27444434267 scopus 로고    scopus 로고
    • Distinct 3′-untranslated region elements regulate stage-specific mRNA accumulation and translation in Leishmania
    • DOI 10.1074/jbc.M507511200
    • McNicoll F., Mller M., Cloutier S., Boilard N., Rochette A., Dubé M., Papadopoulou B., Distinct 3 ′ -untranslated region elements regulate stage-specific mRNA accumulation and translation in Leishmania Journal of Biological Chemistry 2005 280 42 35238 35246 (Pubitemid 41532711)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35238-35246
    • McNicoll, F.1    Muller, M.2    Cloutier, S.3    Boilard, N.4    Rochette, A.5    Dube, M.6    Papadopoulou, B.7
  • 85
    • 0028331192 scopus 로고
    • Expression of heat shock protein 83 in Leishmania is regulated post-transcriptionally
    • DOI 10.1016/0166-6851(94)90138-4
    • Argaman M., Aly R., Shapira M., Expression of heat shock protein 83 in Leishmania is regulated post-transcriptionally Molecular and Biochemical Parasitology 1994 64 1 95 110 (Pubitemid 24126845)
    • (1994) Molecular and Biochemical Parasitology , vol.64 , Issue.1 , pp. 95-110
    • Argaman, M.1    Aly, R.2    Shapira, M.3
  • 87
    • 36549005184 scopus 로고    scopus 로고
    • Developmental regulation of gene expression in trypanosomatid parasitic protozoa
    • DOI 10.1016/j.mib.2007.10.001, PII S1369527407001415, Growth and Development
    • Haile S., Papadopoulou B., Developmental regulation of gene expression in trypanosomatid parasitic protozoa Current Opinion in Microbiology 2007 10 6 569 577 (Pubitemid 350180594)
    • (2007) Current Opinion in Microbiology , vol.10 , Issue.6 , pp. 569-577
    • Haile, S.1    Papadopoulou, B.2
  • 88
    • 38949167477 scopus 로고    scopus 로고
    • Retooling Leishmania metabolism: From sand fly gut to human macrophage
    • DOI 10.1096/fj.07-9254com
    • Rosenzweig D., Smith D., Opperdoes F., Stern S., Olafson R. W., Zilberstein D., Retooling Leishmania metabolismml: from sand fly gut to human macrophage FASEB Journal 2008 22 2 590 602 (Pubitemid 351225595)
    • (2008) FASEB Journal , vol.22 , Issue.2 , pp. 590-602
    • Rosenzweig, D.1    Smith, D.2    Opperdoes, F.3    Stern, S.4    Olafson, R.W.5    Zilberstein, D.6
  • 89
    • 79955054747 scopus 로고    scopus 로고
    • Translational control of Leishmania infection throught mTORC1 signaling
    • Jaramillo M., Gomez M. A., Larson O., Translational control of Leishmania infection throught mTORC1 signaling Cell Host and Microbe 2011 9 331 341
    • (2011) Cell Host and Microbe , vol.9 , pp. 331-341
    • Jaramillo, M.1    Gomez, M.A.2    Larson, O.3


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