메뉴 건너뛰기




Volumn 13, Issue 5, 2014, Pages 664-674

Depletion of the trypanosome pumilio domain protein PUF2 or of some other essential proteins causes transcriptome changes related to coding region length

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; PROTOZOAL PROTEIN; PROTOZOAL RNA; RNA BINDING PROTEIN; TRANSCRIPTOME;

EID: 84899921635     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00018-14     Document Type: Article
Times cited : (21)

References (73)
  • 1
    • 77950931631 scopus 로고    scopus 로고
    • The Puf family of RNA-binding proteins in plants: Phylogeny, structural modeling, activity and subcellular localization
    • Tam PP, Barrette-Ng IH, Simon DM, Tam MW, Ang AL, Muench DG. 2010. The Puf family of RNA-binding proteins in plants: phylogeny, structural modeling, activity and subcellular localization. BMC Plant Biol. 10: 44. http://dx. doi. org/10. 1186/1471-2229-10-44.
    • (2010) BMC Plant Biol , vol.10 , pp. 44
    • Tam, P.P.1    Barrette-Ng, I.H.2    Simon, D.M.3    Tam, M.W.4    Ang, A.L.5    Muench, D.G.6
  • 2
    • 79956218301 scopus 로고    scopus 로고
    • Pumilio Puf domain RNA-binding proteins in Arabidopsis
    • Abbasi N, Park YI, Choi SB. 2011. Pumilio Puf domain RNA-binding proteins in Arabidopsis. Plant Signal. Behav. 6: 364-368. http://dx. doi. org/10. 4161/psb. 6. 3. 14380.
    • (2011) Plant Signal. Behav , vol.6 , pp. 364-368
    • Abbasi, N.1    Park, Y.I.2    Choi, S.B.3
  • 3
    • 79151471434 scopus 로고    scopus 로고
    • PUF proteins: Repression, activation and mRNA localization
    • Quenault T, Lithgow T, Traven A. 2011. PUF proteins: repression, activation and mRNA localization. Trends Cell Biol. 21: 104-112. http://dx. doi. org/10. 1016/j. tcb. 2010. 09. 013.
    • (2011) Trends Cell Biol , vol.21 , pp. 104-112
    • Quenault, T.1    Lithgow, T.2    Traven, A.3
  • 4
    • 79952460244 scopus 로고    scopus 로고
    • Alternate modes of cognate RNA recognition by human PUMILIO proteins
    • Lu G, Hall TM. 2011. Alternate modes of cognate RNA recognition by human PUMILIO proteins. Structure 19: 361-367. http://dx. doi. org/10. 1016/j. str. 2010. 12. 019.
    • (2011) Structure , vol.19 , pp. 361-367
    • Lu, G.1    Hall, T.M.2
  • 5
    • 79960922805 scopus 로고    scopus 로고
    • Roles of Puf proteins in mRNA degradation and translation
    • Miller MA, Olivas WM. 2011. Roles of Puf proteins in mRNA degradation and translation. Wiley Interdiscip. Rev. RNA 2: 471-492. http://dx. doi. org/10. 1002/wrna. 69.
    • (2011) Wiley Interdiscip. Rev. RNA , vol.2 , pp. 471-492
    • Miller, M.A.1    Olivas, W.M.2
  • 6
    • 36248953200 scopus 로고    scopus 로고
    • Nop9 is an RNA binding protein present in pre-40S ribosomes and required for 18S rRNA synthesis in yeast
    • Thomson E, Rappsilber J, Tollervey D. 2007. Nop9 is an RNA binding protein present in pre-40S ribosomes and required for 18S rRNA synthesis in yeast. RNA 13: 2165-2174. http://dx. doi. org/10. 1261/rna. 747607.
    • (2007) RNA , vol.13 , pp. 2165-2174
    • Thomson, E.1    Rappsilber, J.2    Tollervey, D.3
  • 7
    • 0034388021 scopus 로고    scopus 로고
    • The Puf3 protein is a transcript-specific regulator of mRNA degradation in yeast
    • Olivas W, Parker R. 2000. The Puf3 protein is a transcript-specific regulator of mRNA degradation in yeast. EMBO J. 19: 6602-6611. http://dx. doi. org/10. 1093/emboj/19. 23. 6602.
    • (2000) EMBO J , vol.19 , pp. 6602-6611
    • Olivas, W.1    Parker, R.2
  • 8
    • 34447503943 scopus 로고    scopus 로고
    • Two yeast PUF proteins negatively regulate a single mRNA
    • Hook BA, Goldstrohm AC, Seay DJ, Wickens M. 2007. Two yeast PUF proteins negatively regulate a single mRNA. J. Biol. Chem. 282: 15430-15438. http://dx. doi. org/10. 1074/jbc. M611253200.
    • (2007) J Biol. Chem , vol.282 , pp. 15430-15438
    • Hook, B.A.1    Goldstrohm, A.C.2    Seay, D.J.3    Wickens, M.4
  • 10
    • 38649087012 scopus 로고    scopus 로고
    • Puf1p acts in combination with other yeast Puf proteins to control mRNA stability
    • Ulbricht RJ, Olivas WM. 2008. Puf1p acts in combination with other yeast Puf proteins to control mRNA stability. RNA 14: 246-262. http://dx. doi. org/10. 1261/rna. 847408.
    • (2008) RNA , vol.14 , pp. 246-262
    • Ulbricht, R.J.1    Olivas, W.M.2
  • 12
    • 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, Singer RH. 2004. A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization. Genes Dev. 18: 1452-1465. http://dx. doi. org/10. 1101/gad. 1189004.
    • (2004) Genes Dev , vol.18 , pp. 1452-1465
    • Gu, W.1    Deng, Y.2    Zenklusen, D.3    Singer, R.H.4
  • 13
    • 79956202317 scopus 로고    scopus 로고
    • The Puf-family RNA-binding protein Puf2 controls sporozoite conversion to liver stages in the malaria parasite
    • Muller K, Matuschewski K, Silvie O. 2011. The Puf-family RNA-binding protein Puf2 controls sporozoite conversion to liver stages in the malaria parasite. PLoS One 6(5): e19860. http://dx. doi. org/10. 1371/journal. pone. 0019860.
    • (2011) PLoS One , vol.6 , Issue.5
    • Muller, K.1    Matuschewski, K.2    Silvie, O.3
  • 15
    • 58149218238 scopus 로고    scopus 로고
    • A 3=UTR pumilio-binding element directs translational activation in olfactory sensory neurons
    • Kaye JA, Rose NC, Goldsworthy B, Goga A, L'Etoile ND. 2009. A 3=UTR pumilio-binding element directs translational activation in olfactory sensory neurons. Neuron 61: 57-70. http://dx. doi. org/10. 1016/j. neuron. 2008. 11. 012.
    • (2009) Neuron , vol.61 , pp. 57-70
    • Kaye, J.A.1    Rose, N.C.2    Goldsworthy, B.3    Goga, A.4    L'Etoile, N.D.5
  • 16
    • 79955619183 scopus 로고    scopus 로고
    • Trans-Splicing in trypanosomes: Machinery and its impact on the parasite transcriptome
    • Michaeli S. 2011. trans-Splicing in trypanosomes: machinery and its impact on the parasite transcriptome. Future Microbiol. 6: 459-474. http://dx. doi. org/10. 2217/fmb. 11. 20.
    • (2011) Future Microbiol , vol.6 , pp. 459-474
    • Michaeli, S.1
  • 17
    • 80054730384 scopus 로고    scopus 로고
    • The role of the 5=-3= exoribonuclease XRNA in transcriptome-wide mRNA degradation
    • Manful T, Fadda A, Clayton C. 2011. The role of the 5=-3= exoribonuclease XRNA in transcriptome-wide mRNA degradation. RNA 17: 2039-2047. http://dx. doi. org/10. 1261/rna. 2837311.
    • (2011) RNA , vol.17 , pp. 2039-2047
    • Manful, T.1    Fadda, A.2    Clayton, C.3
  • 20
    • 62549158711 scopus 로고    scopus 로고
    • Multiple roles for polypyrimidine tract binding (PTB) proteins in trypanosome RNA metabolism
    • Stern M, Gupta S, Salmon-Divon M, Haham T, Barda O, Levi S, Wachtel C, Nilsen T, Michaeli S. 2009. Multiple roles for polypyrimidine tract binding (PTB) proteins in trypanosome RNA metabolism. RNA 15: 648-665. http://dx. doi. org/10. 1261/rna. 1230209.
    • (2009) RNA , vol.15 , pp. 648-665
    • Stern, M.1    Gupta, S.2    Salmon-Divon, M.3    Haham, T.4    Barda, O.5    Levi, S.6    Wachtel, C.7    Nilsen, T.8    Michaeli, S.9
  • 21
    • 84893694734 scopus 로고    scopus 로고
    • The CAF1-NOT complex of trypanosomes
    • Erben E, Chakraborty C, Clayton C. 2014. The CAF1-NOT complex of trypanosomes. Front. Genet. Res. Top. 4: 299. http://dx. doi. org/10. 3389/fgene. 2013. 00299.
    • (2014) Front. Genet. Res. Top , vol.4 , pp. 299
    • Erben, E.1    Chakraborty, C.2    Clayton, C.3
  • 22
    • 84879289671 scopus 로고    scopus 로고
    • The roles of 3=-exoribonucleases and the exosome in trypanosome mRNA degradation
    • Fadda A, Färber V, Droll D, Clayton C. 2013. The roles of 3=-exoribonucleases and the exosome in trypanosome mRNA degradation. RNA 19: 937-947. http://dx. doi. org/10. 1261/rna. 038430. 113.
    • (2013) RNA , vol.19 , pp. 937-947
    • Fadda, A.1    Färber, V.2    Droll, D.3    Clayton, C.4
  • 25
    • 0035898660 scopus 로고    scopus 로고
    • The exosome of Trypanosoma brucei
    • Estevez AM, Kempf T, Clayton C. 2001. The exosome of Trypanosoma brucei. EMBO J. 20: 3831-3839. http://dx. doi. org/10. 1093/emboj/20. 14. 3831.
    • (2001) EMBO J , vol.20 , pp. 3831-3839
    • Estevez, A.M.1    Kempf, T.2    Clayton, C.3
  • 26
    • 45249090233 scopus 로고    scopus 로고
    • A role for Caf1 in mRNA deadenylation and decay in trypanosomes and human cells
    • Schwede A, Ellis L, Luther J, Carrington M, Stoecklin G, Clayton C. 2008. A role for Caf1 in mRNA deadenylation and decay in trypanosomes and human cells. Nucleic Acids Res. 36: 3374-3388. http://dx. doi. org/10. 1093/nar/gkn108.
    • (2008) Nucleic Acids Res , vol.36 , pp. 3374-3388
    • Schwede, A.1    Ellis, L.2    Luther, J.3    Carrington, M.4    Stoecklin, G.5    Clayton, C.6
  • 27
    • 79953776282 scopus 로고    scopus 로고
    • Posttranscriptional control and the role of RNA-binding proteins in gene regulation in trypanosomatid protozoan parasites
    • Fernandez-Moya SM, Estevez AM. 2010. Posttranscriptional control and the role of RNA-binding proteins in gene regulation in trypanosomatid protozoan parasites. Wiley Interdiscip Rev. RNA 1: 34-46. http://dx. doi. org/10. 1002/wrna. 6.
    • (2010) Wiley Interdiscip Rev. RNA , vol.1 , pp. 34-46
    • Fernandez-Moya, S.M.1    Estevez, A.M.2
  • 28
    • 78650533544 scopus 로고    scopus 로고
    • Trans-Acting proteins regulating mRNA maturation, stability and translation in trypanosomatids
    • Kramer S, Carrington M. 2011. trans-Acting proteins regulating mRNA maturation, stability and translation in trypanosomatids. Trends Parasitol. 27: 23-30. http://dx. doi. org/10. 1016/j. pt. 2010. 06. 011.
    • (2011) Trends Parasitol , vol.27 , pp. 23-30
    • Kramer, S.1    Carrington, M.2
  • 29
    • 84888236056 scopus 로고    scopus 로고
    • The regulation of trypanosome gene expression by RNA-binding proteins
    • Clayton C. 2013. The regulation of trypanosome gene expression by RNA-binding proteins. PLoS Pathog. 9(11): e1003680. http://dx. doi. org/10. 1371/journal. ppat. 1003680.
    • (2013) PLoS Pathog , vol.9 , Issue.11
    • Clayton, C.1
  • 30
    • 77950368329 scopus 로고    scopus 로고
    • The trypanosome Pumilio-domain protein PUF7 associates with a nuclear cyclophilin and is involved in ribosomal RNA maturation
    • Droll D, Archer S, Fenn K, Delhi P, Matthews K, Clayton C. 2010. The trypanosome Pumilio-domain protein PUF7 associates with a nuclear cyclophilin and is involved in ribosomal RNA maturation. FEBS Lett. 584: 1156-1162. http://dx. doi. org/10. 1016/j. febslet. 2010. 02. 018.
    • (2010) FEBS Lett , vol.584 , pp. 1156-1162
    • Droll, D.1    Archer, S.2    Fenn, K.3    Delhi, P.4    Matthews, K.5    Clayton, C.6
  • 33
    • 84885963067 scopus 로고    scopus 로고
    • The trypanosome pumilio domain protein PUF5
    • Jha B, Archer S, Clayton C. 2013. The trypanosome pumilio domain protein PUF5. PLoS One 8(10): e77371. http://dx. doi. org/10. 1371/journal. pone. 0077371.
    • (2013) PLoS One , vol.8 , Issue.10
    • Jha, B.1    Archer, S.2    Clayton, C.3
  • 34
    • 70049084728 scopus 로고    scopus 로고
    • Trypanosoma brucei PUF9 regulates mRNAs for proteins involved in replicative processes over the cell cycle
    • Archer SK, Luu VD, de Queiroz RA, Brems S, Clayton C. 2009. Trypanosoma brucei PUF9 regulates mRNAs for proteins involved in replicative processes over the cell cycle. PLoS Pathog. 5(8): e1000565. http://dx. doi. org/10. 1371/journal. ppat. 1000565.
    • (2009) PLoS Pathog , vol.5 , Issue.8
    • Archer, S.K.1    Luu, V.D.2    de Queiroz, R.A.3    Brems, S.4    Clayton, C.5
  • 35
    • 11144327213 scopus 로고    scopus 로고
    • A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei
    • Alibu VP, Storm L, Haile S, Clayton C, Horn D. 2005. A doubly inducible system for RNA interference and rapid RNAi plasmid construction in Trypanosoma brucei. Mol. Biochem. Parasitol. 139: 75-82. http://dx. doi. org/10. 1016/j. molbiopara. 2004. 10. 002.
    • (2005) Mol. Biochem. Parasitol , vol.139 , pp. 75-82
    • Alibu, V.P.1    Storm, L.2    Haile, S.3    Clayton, C.4    Horn, D.5
  • 36
    • 25144447731 scopus 로고    scopus 로고
    • Down-regulating gene expression by RNA interference in Trypanosoma brucei
    • Clayton CE, Estevez AM, Hartmann C, Alibu VP, Field M, Horn D. 2005. Down-regulating gene expression by RNA interference in Trypanosoma brucei. Methods Mol. Biol. 309: 39-60. http://dx. doi. org/10. 1385/1-59259-935-4: 039.
    • (2005) Methods Mol. Biol , vol.309 , pp. 39-60
    • Clayton, C.E.1    Estevez, A.M.2    Hartmann, C.3    Alibu, V.P.4    Field, M.5    Horn, D.6
  • 37
    • 84898980225 scopus 로고    scopus 로고
    • Trypanosome MKT1 and the RNA-binding protein ZC3H11: Interactions and potential roles in post-transcriptional regulatory networks
    • 26 January
    • Singh A, Minia I, Droll D, Fadda A, Clayton C, Erben E. 26 January 2014. Trypanosome MKT1 and the RNA-binding protein ZC3H11: interactions and potential roles in post-transcriptional regulatory networks. Nucleic Acids Res. http://dx. doi. org/10. 1093/nar/gkt1416.
    • (2014) Nucleic Acids Res
    • Singh, A.1    Minia, I.2    Droll, D.3    Fadda, A.4    Clayton, C.5    Erben, E.6
  • 38
    • 0035089905 scopus 로고    scopus 로고
    • In vivo epitope tagging of Trypanosoma brucei genes using a one step PCR-based strategy
    • Shen S, Arhin GK, Ullu E, Tschudi C. 2001. In vivo epitope tagging of Trypanosoma brucei genes using a one step PCR-based strategy. Mol. Biochem. Parasitol. 113: 171-173. http://dx. doi. org/10. 1016/S0166-6851(00)00383-2.
    • (2001) Mol. Biochem. Parasitol , vol.113 , pp. 171-173
    • Shen, S.1    Arhin, G.K.2    Ullu, E.3    Tschudi, C.4
  • 39
    • 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 JD, Clayton C, Carrington M. 2008. Heat shock causes a decrease in polysomes and the appearance of stress granules in trypanosomes independently of eIF2 phosphorylation at Thr169. J. Cell Sci. 121: 3002-3014. http://dx. doi. org/10. 1242/jcs. 031823.
    • (2008) J. Cell Sci , vol.121 , 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
  • 40
    • 80053047597 scopus 로고    scopus 로고
    • Is there a classical nonsense-mediated decay pathway in trypanosomes?
    • Delhi P, Queiroz R, Inchaustegui D, Carrington M, Clayton C. 2011. Is there a classical nonsense-mediated decay pathway in trypanosomes? PLoS One 6(9): e25112. http://dx. doi. org/10. 1371/journal. pone. 0025112.
    • (2011) PLoS One , vol.6 , Issue.9
    • Delhi, P.1    Queiroz, R.2    Inchaustegui, D.3    Carrington, M.4    Clayton, C.5
  • 41
    • 0033198238 scopus 로고    scopus 로고
    • Genetic manipulation of kinetoplastida
    • Clayton CE. 1999. Genetic manipulation of kinetoplastida. Trends Parasitol. 15: 372-378. http://dx. doi. org/10. 1016/S0169-4758(99)01498-2.
    • (1999) Trends Parasitol , vol.15 , pp. 372-378
    • Clayton, C.E.1
  • 43
    • 36749076437 scopus 로고    scopus 로고
    • Trypanosome MTR4 is involved in rRNA processing
    • Cristodero M, Clayton CE. 2007. Trypanosome MTR4 is involved in rRNA processing. Nucleic Acids Res. 35: 7023-7030. http://dx. doi. org/10. 1093/nar/gkm736.
    • (2007) Nucleic Acids Res , vol.35 , pp. 7023-7030
    • Cristodero, M.1    Clayton, C.E.2
  • 44
    • 0023605611 scopus 로고
    • Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei
    • Clayton CE. 1987. Import of fructose bisphosphate aldolase into the glycosomes of Trypanosoma brucei. J. Cell Biol. 105: 2649-2653.
    • (1987) J Cell Biol , vol.105 , pp. 2649-2653
    • Clayton, C.E.1
  • 45
    • 33845342890 scopus 로고    scopus 로고
    • The subcellular localisation of trypanosome RRP6 and its association with the exosome
    • Haile S, Cristodero M, Clayton C, Estevez AM. 2007. The subcellular localisation of trypanosome RRP6 and its association with the exosome. Mol. Biochem. Parasitol. 151: 52-58. http://dx. doi. org/10. 1016/j. molbiopara. 2006. 10. 005.
    • (2007) Mol. Biochem. Parasitol , vol.151 , pp. 52-58
    • Haile, S.1    Cristodero, M.2    Clayton, C.3    Estevez, A.M.4
  • 46
    • 0038721055 scopus 로고    scopus 로고
    • An siRNA ribonucleoprotein is found associated with polyribosomes in Trypanosoma brucei
    • Djikeng A, Shi H, Tschudi C, Shen S, Ullu E. 2003. An siRNA ribonucleoprotein is found associated with polyribosomes in Trypanosoma brucei. RNA 9: 802-808. http://dx. doi. org/10. 1261/rna. 5270203.
    • (2003) RNA , vol.9 , pp. 802-808
    • Djikeng, A.1    Shi, H.2    Tschudi, C.3    Shen, S.4    Ullu, E.5
  • 47
    • 0042317221 scopus 로고    scopus 로고
    • The roles of intersubunit interactions in exosome stability
    • Estevez AM, Lehner B, Sanderson CM, Ruppert T, Clayton C. 2003. The roles of intersubunit interactions in exosome stability. J. Biol. Chem. 278: 34943-34951. http://dx. doi. org/10. 1074/jbc. M305333200.
    • (2003) J. Biol. Chem , vol.278 , pp. 34943-34951
    • Estevez, A.M.1    Lehner, B.2    Sanderson, C.M.3    Ruppert, T.4    Clayton, C.5
  • 48
    • 84859620899 scopus 로고    scopus 로고
    • The Trypanosoma brucei CCCH zinc finger proteins ZC3H12 and ZC3H13
    • Ouna BA, Stewart M, Helbig C, Clayton C. 2012. The Trypanosoma brucei CCCH zinc finger proteins ZC3H12 and ZC3H13. Mol. Biochem. Parasitol. 183: 184-188. http://dx. doi. org/10. 1016/j. molbiopara. 2012. 02. 006.
    • (2012) Mol. Biochem. Parasitol , vol.183 , pp. 184-188
    • Ouna, B.A.1    Stewart, M.2    Helbig, C.3    Clayton, C.4
  • 49
    • 67649840910 scopus 로고    scopus 로고
    • CLIP: Construction of cDNA libraries for high-throughput sequencing from RNAs crosslinked to proteins in vivo
    • Wang Z, Tollervey J, Briese M, Turner D, Ule J. 2009. CLIP: construction of cDNA libraries for high-throughput sequencing from RNAs crosslinked to proteins in vivo. Methods 48: 287-293. http://dx. doi. org/10. 1016/j. ymeth. 2009. 02. 021.
    • (2009) Methods , vol.48 , pp. 287-293
    • Wang, Z.1    Tollervey, J.2    Briese, M.3    Turner, D.4    Ule, J.5
  • 52
    • 84857355078 scopus 로고    scopus 로고
    • Expression of the RNA recognition motif protein RBP10 promotes a bloodstream-form transcript pattern in Trypanosoma brucei
    • Wurst M, Seliger B, Jha BA, Klein C, Queiroz R, Clayton C. 2012. Expression of the RNA recognition motif protein RBP10 promotes a bloodstream-form transcript pattern in Trypanosoma brucei. Mol. Microbiol. 83: 1048-1063. http://dx. doi. org/10. 1111/j. 1365-2958. 2012. 07988. x.
    • (2012) Mol. Microbiol , vol.83 , pp. 1048-1063
    • Wurst, M.1    Seliger, B.2    Jha, B.A.3    Klein, C.4    Queiroz, R.5    Clayton, C.6
  • 54
    • 84876860902 scopus 로고    scopus 로고
    • Post-transcriptional regulation of the trypanosome heat shock response by a zinc finger protein
    • Droll D, Minia I, Fadda A, Singh A, Stewart M, Queiroz R, Clayton C. 2013. Post-transcriptional regulation of the trypanosome heat shock response by a zinc finger protein. PLoS Pathog. 9: e1003286. http://dx. doi. org/10. 1371/journal. ppat. 1003286.
    • (2013) PLoS Pathog , vol.9
    • Droll, D.1    Minia, I.2    Fadda, A.3    Singh, A.4    Stewart, M.5    Queiroz, R.6    Clayton, C.7
  • 55
    • 41449099992 scopus 로고    scopus 로고
    • Control and regulation of gene expression: Quantitative analysis of the expression of phosphoglycerate kinase in bloodstream form Trypanosoma brucei
    • Haanstra JR, Stewart M, Luu VD, van Tuijl A, Westerhoff HV, Clayton C, Bakker BM. 2008. Control and regulation of gene expression: quantitative analysis of the expression of phosphoglycerate kinase in bloodstream form Trypanosoma brucei. J. Biol. Chem. 283: 2495-2507. http://dx. doi. org/10. 1074/jbc. M705782200.
    • (2008) J. Biol. Chem , vol.283 , pp. 2495-2507
    • Haanstra, J.R.1    Stewart, M.2    Luu, V.D.3    van Tuijl, A.4    Westerhoff, H.V.5    Clayton, C.6    Bakker, B.M.7
  • 56
    • 79955602637 scopus 로고    scopus 로고
    • High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome
    • Alsford S, Turner DJ, Obado SO, Sanchez-Flores A, Glover L, Berriman M, Hertz-Fowler C, Horn D. 2011. High-throughput phenotyping using parallel sequencing of RNA interference targets in the African trypanosome. Genome Res. 21: 915-924. http://dx. doi. org/10. 1101/gr. 115089. 110.
    • (2011) Genome Res , vol.21 , pp. 915-924
    • Alsford, S.1    Turner, D.J.2    Obado, S.O.3    Sanchez-Flores, A.4    Glover, L.5    Berriman, M.6    Hertz-Fowler, C.7    Horn, D.8
  • 57
    • 84859941632 scopus 로고    scopus 로고
    • Depletion of trypanosome CTR9 leads to gene expression defects
    • Ouna B, Nyambega B, Manful T, Helbig C, Males M, Fadda A, Clayton C. 2012. Depletion of trypanosome CTR9 leads to gene expression defects. PLoS One 7(4): e34256. http://dx. doi. org/10. 1371/journal. pone. 0034256.
    • (2012) PLoS One , vol.7 , Issue.4
    • Ouna, B.1    Nyambega, B.2    Manful, T.3    Helbig, C.4    Males, M.5    Fadda, A.6    Clayton, C.7
  • 58
    • 66449123334 scopus 로고    scopus 로고
    • Hydrolase regulates NAD+ metabolites and modulates cellular redox
    • Tong L, Lee S, Denu JM. 2009. Hydrolase regulates NAD+ metabolites and modulates cellular redox. J. Biol. Chem. 284: 11256-11266. http://dx. doi. org/10. 1074/jbc. M809790200.
    • (2009) J. Biol. Chem , vol.284 , pp. 11256-11266
    • Tong, L.1    Lee, S.2    Denu, J.M.3
  • 59
    • 78149426485 scopus 로고    scopus 로고
    • Multiple mRNA decapping enzymes in mammalian cells
    • Song M-G, Li Y, Kiledjian M. 2010. Multiple mRNA decapping enzymes in mammalian cells. Mol. Cell 40: 423-432. http://dx. doi. org/10. 1016/j. molcel. 2010. 10. 010.
    • (2010) Mol. Cell , vol.40 , pp. 423-432
    • Song, M.-G.1    Li, Y.2    Kiledjian, M.3
  • 60
    • 36349025234 scopus 로고    scopus 로고
    • Regulation of a transmembrane protein gene family by the small RNA-binding proteins TbUBP1 and TbUBP2
    • Hartmann C, Clayton C. 2008. Regulation of a transmembrane protein gene family by the small RNA-binding proteins TbUBP1 and TbUBP2. Mol. Biochem. Parasitol. 157: 112-115. http://dx. doi. org/10. 1016/j. molbiopara. 2007. 09. 009.
    • (2008) Mol. Biochem. Parasitol , vol.157 , pp. 112-115
    • Hartmann, C.1    Clayton, C.2
  • 61
    • 38949107432 scopus 로고    scopus 로고
    • Tethering of proteins to RNAs by bacteriophage proteins
    • Keryer-Bibens C, Barreau C, Osborne HB. 2008. Tethering of proteins to RNAs by bacteriophage proteins. Biol. Cell 100: 125-138. http://dx. doi. org/10. 1042/BC20070067.
    • (2008) Biol. Cell , vol.100 , pp. 125-138
    • Keryer-Bibens, C.1    Barreau, C.2    Osborne, H.B.3
  • 62
    • 0033200316 scopus 로고    scopus 로고
    • Translation driven by an eIF4G core domain in vivo
    • De Gregorio E, Preiss T, Hentze MW. 1999. Translation driven by an eIF4G core domain in vivo. EMBO J. 18: 4865-4874. http://dx. doi. org/10. 1093/emboj/18. 17. 4865.
    • (1999) EMBO J , vol.18 , pp. 4865-4874
    • De Gregorio, E.1    Preiss, T.2    Hentze, M.W.3
  • 63
    • 70450253253 scopus 로고    scopus 로고
    • Widespread variation in transcript abundance within and across developmental stages of Trypanosoma brucei
    • Jensen B, Sivam D, Kifer C, Myler P, Parsons M. 2009. Widespread variation in transcript abundance within and across developmental stages of Trypanosoma brucei. BMC Genomics 10: 482. http://dx. doi. org/10. 1186/1471-2164-10-482.
    • (2009) BMC Genomics , vol.10 , pp. 482
    • Jensen, B.1    Sivam, D.2    Kifer, C.3    Myler, P.4    Parsons, M.5
  • 64
    • 70549084861 scopus 로고    scopus 로고
    • Transcriptome analysis of differentiating trypanosomes reveals the existence of multiple post-transcriptional regulons
    • Queiroz R, Benz C, Fellenberg K, Hoheisel JD, Clayton C. 2009. Transcriptome analysis of differentiating trypanosomes reveals the existence of multiple post-transcriptional regulons. BMC Genomics 10: 495. http://dx. doi. org/10. 1186/1471-2164-10-495.
    • (2009) BMC Genomics , vol.10 , pp. 495
    • Queiroz, R.1    Benz, C.2    Fellenberg, K.3    Hoheisel, J.D.4    Clayton, C.5
  • 66
    • 48749090496 scopus 로고    scopus 로고
    • Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes
    • Goler-Baron V, Selitrennik M, Barkai O, Haimovich G, Lotan R, Choder M. 2008. Transcription in the nucleus and mRNA decay in the cytoplasm are coupled processes. Genes Dev. 22: 2022-2027. http://dx. doi. org/10. 1101/gad. 473608.
    • (2008) Genes Dev , vol.22 , pp. 2022-2027
    • Goler-Baron, V.1    Selitrennik, M.2    Barkai, O.3    Haimovich, G.4    Lotan, R.5    Choder, M.6
  • 67
    • 78149478886 scopus 로고    scopus 로고
    • RNA polymerase II subunits link transcription and mRNA decay to translation
    • Harel-Sharvit L, Eldad N, Haimovich G, Barkai O, Duek L, Choder M. 2010. RNA polymerase II subunits link transcription and mRNA decay to translation. Cell 143: 552-563. http://dx. doi. org/10. 1016/j. cell. 2010. 10. 033.
    • (2010) Cell , vol.143 , pp. 552-563
    • Harel-Sharvit, L.1    Eldad, N.2    Haimovich, G.3    Barkai, O.4    Duek, L.5    Choder, M.6
  • 68
    • 79952609007 scopus 로고    scopus 로고
    • The multifunctional Ccr4-Not complex directly promotes transcription elongation
    • Kruk JA, Dutta A, Fu J, Gilmour DS, Reese JC. 2011. The multifunctional Ccr4-Not complex directly promotes transcription elongation. Genes Dev. 25: 581-593. http://dx. doi. org/10. 1101/gad. 2020911.
    • (2011) Genes Dev , vol.25 , pp. 581-593
    • Kruk, J.A.1    Dutta, A.2    Fu, J.3    Gilmour, D.S.4    Reese, J.C.5
  • 69
    • 0032858414 scopus 로고    scopus 로고
    • From factors to mechanisms: Translation and translational control in eukaryotes
    • Preiss T, Hentze MW. 1999. From factors to mechanisms: translation and translational control in eukaryotes. Curr. Opin. Genet. Dev. 9: 515-521. http://dx. doi. org/10. 1016/S0959-437X(99)00005-2.
    • (1999) Curr. Opin. Genet. Dev , vol.9 , pp. 515-521
    • Preiss, T.1    Hentze, M.W.2
  • 70
    • 0023119755 scopus 로고
    • Circular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rat anterior pituitary
    • Christensen AK, Kahn LE, Bourne CM. 1987. Circular polysomes predominate on the rough endoplasmic reticulum of somatotropes and mammotropes in the rat anterior pituitary. Am. J. Anat. 178: 1-10.
    • (1987) Am. J. Anat , vol.178 , pp. 1-10
    • Christensen, A.K.1    Kahn, L.E.2    Bourne, C.M.3
  • 71
    • 43349102982 scopus 로고    scopus 로고
    • Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNA
    • Kopeina GS, Afonina ZA, Gromova KV, Shirokov VA, Vasiliev VD, Spirin AS. 2008. Step-wise formation of eukaryotic double-row polyribosomes and circular translation of polysomal mRNA. Nucleic Acids Res. 36: 2476-2488. http://dx. doi. org/10. 1093/nar/gkm1177.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2476-2488
    • Kopeina, G.S.1    Afonina, Z.A.2    Gromova, K.V.3    Shirokov, V.A.4    Vasiliev, V.D.5    Spirin, A.S.6
  • 73
    • 79251570260 scopus 로고    scopus 로고
    • Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide
    • Park EH, Zhang F, Warringer J, Sunnerhagen P, Hinnebusch AG. 2011. Depletion of eIF4G from yeast cells narrows the range of translational efficiencies genome-wide. BMC Genomics 12: 68. http://dx. doi. org/10. 1186/1471-2164-12-68.
    • (2011) BMC Genomics , vol.12 , pp. 68
    • Park, E.H.1    Zhang, F.2    Warringer, J.3    Sunnerhagen, P.4    Hinnebusch, A.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.