메뉴 건너뛰기




Volumn 722, Issue , 2011, Pages 137-155

Unexpected functions of tRNA and tRNA processing enzymes

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA; RIBONUCLEASE P; SYNTHETASE; TRANSFER RNA; TRANSFER RNA AMINOACYL SYNTHETASE; TRANSFER RNA PROCESSING ENZYME; UNCLASSIFIED DRUG;

EID: 80053592894     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4614-0332-6_9     Document Type: Article
Times cited : (26)

References (82)
  • 1
    • 71549169628 scopus 로고    scopus 로고
    • Filtering of deep sequencing data reveals the existence of abundant Dicer-dependent small RNAs derived from tRNAs
    • Cole C, Sobala A, Lu C et al. Filtering of deep sequencing data reveals the existence of abundant Dicer-dependent small RNAs derived from tRNAs. RNA 2009; 15(12):2147-2160.
    • (2009) RNA , vol.15 , Issue.12 , pp. 2147-2160
    • Cole, C.1    Sobala, A.2    Lu, C.3
  • 2
    • 72749089855 scopus 로고    scopus 로고
    • A novel class of small RNAs: TRNA-derived RNA fragments (tRFs)
    • Lee YS, Shibata Y, Malhotra A et al. A novel class of small RNAs: tRNA-derived RNA fragments (tRFs). Genes Dev 2009; 23(22):2639-2649.
    • (2009) Genes Dev , vol.23 , Issue.22 , pp. 2639-2649
    • Lee, Y.S.1    Shibata, Y.2    Malhotra, A.3
  • 3
    • 41349089950 scopus 로고    scopus 로고
    • Met Synthesis Can Drive Cell Proliferation and Oncogenic Transformation
    • DOI 10.1016/j.cell.2008.02.035, PII S0092867408002869
    • Marshall L, Kenneth NS, White RJ. ElevatedtRNA(iMet) synthesis can drive cell proliferation and oncogenic transformation. Cell 2008; 133(l):78-89. (Pubitemid 351447300)
    • (2008) Cell , vol.133 , Issue.1 , pp. 78-89
    • Marshall, L.1    Kenneth, N.S.2    White, R.J.3
  • 4
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • DOI 10.1038/290470a0
    • Ojala D, Montoya J, Attardi G. tRNA punctuation model of RNA processing in human mitochondria. Nature 1981; 290(5806):470-474. (Pubitemid 11159076)
    • (1981) Nature , vol.290 , Issue.5806 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 6
    • 0037439213 scopus 로고    scopus 로고
    • tRNA transfers to the limelight
    • DOI 10.1101/gad.1049103
    • Hopper AK, Phizicky EM. tRNA transfers to the limelight. Genes Dev 2003; 17(2):162-180. (Pubitemid 36105890)
    • (2003) Genes and Development , vol.17 , Issue.2 , pp. 162-180
    • Hopper, A.K.1    Phizicky, E.M.2
  • 7
    • 67650652985 scopus 로고    scopus 로고
    • Characterization of mature mitochondrial transcripts in Drosophila and the implications for the tRNA punctuation model in arthropods
    • Stewart JB, Beckenbach AT. Characterization of mature mitochondrial transcripts in Drosophila and the implications for the tRNA punctuation model in arthropods. Gene 2009; 445(l-2):49-57.
    • (2009) Gene , vol.445 , Issue.1-2 , pp. 49-57
    • Stewart, J.B.1    Beckenbach, A.T.2
  • 8
    • 67650100790 scopus 로고    scopus 로고
    • Processing of a dicistronic tRNA-snoRNA precursor: Combined analysis in vitro and in vivo reveals alternate pathways and coupling to assembly of snoRNP
    • Barbezier N, Canino G, Rodor J et al. Processing of a dicistronic tRNA-snoRNA precursor: combined analysis in vitro and in vivo reveals alternate pathways and coupling to assembly of snoRNP. Plant Physiol 2009; 150(3):1598-1610.
    • (2009) Plant Physiol , vol.150 , Issue.3 , pp. 1598-1610
    • Barbezier, N.1    Canino, G.2    Rodor, J.3
  • 9
    • 67649933366 scopus 로고    scopus 로고
    • Eukaryotic snoRNAs: A paradigm for gene expression flexibility
    • Dieci G, Preti M, MontaniniB. Eukaryotic snoRNAs: a paradigm for gene expression flexibility. Genomics 2009; 94(2):83-88.
    • (2009) Genomics , vol.94 , Issue.2 , pp. 83-88
    • Dieci, G.1    Preti, M.2    Montanini, B.3
  • 10
    • 66149091123 scopus 로고    scopus 로고
    • Mitochondrial fatty acid synthesis type II: More thanjust fatty acids
    • Hiltunen JK, Schonauer MS, Autio KJ et al. Mitochondrial fatty acid synthesis type II: more thanjust fatty acids. J. Biol. Chem 2009; 284(14):9011-9015.
    • (2009) J. Biol. Chem , vol.284 , Issue.14 , pp. 9011-9015
    • Hiltunen, J.K.1    Schonauer, M.S.2    Autio, K.J.3
  • 12
    • 0027490295 scopus 로고
    • Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2
    • DOI 10.1111/j.1365-2958.1993.tb01947.x
    • Hinnebusch AG. Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol Microbiol 1993; 10(2):215-223. (Pubitemid 23316731)
    • (1993) Molecular Microbiology , vol.10 , Issue.2 , pp. 215-223
    • Hinnebusch, A.G.1
  • 13
    • 72049124015 scopus 로고    scopus 로고
    • ATF4-dependent transcription mediates signaling of amino acid limitation
    • Kilberg MS, Shan J, Su N. ATF4-dependent transcription mediates signaling of amino acid limitation. Trends Endocrinol Metab 2009; 20(9):436-443.
    • (2009) Trends Endocrinol Metab , vol.20 , Issue.9 , pp. 436-443
    • Kilberg, M.S.1    Shan, J.2    Su, N.3
  • 15
    • 3242668172 scopus 로고    scopus 로고
    • The different roles of tryptophan transfer RNA in regulating trp operon expression in E. coli versus B. subtilis
    • DOI 10.1016/j.tig.2004.06.007, PII S016895250400157X
    • Yanofsky C. The different roles of tryptophan transfer RNA in regulating trp operon expression in E. coli versus B. subtilis. Trends Genet 2004; 20(8):367-374. (Pubitemid 38943027)
    • (2004) Trends in Genetics , vol.20 , Issue.8 , pp. 367-374
    • Yanofsky, C.1
  • 16
    • 71549138669 scopus 로고    scopus 로고
    • The T box mechanism: TRNA as a regulatory molecule
    • Green NJ, Grundy FJ, Henkin TM. The T box mechanism: tRNA as a regulatory molecule. FEBS Lett;584(2):318-324.
    • FEBS Lett , vol.584 , Issue.2 , pp. 318-324
    • Green, N.J.1    Grundy, F.J.2    Henkin, T.M.3
  • 17
    • 29944432120 scopus 로고    scopus 로고
    • Starvation-induced cleavage of the tRNA anticodon loop in Tetrahymena thermophila
    • DOI 10.1074/jbc.M510356200
    • Lee SR, Collins K. Starvation-induced cleavage of the tRNA anticodon loop in Tetrahymena thermophila. J Biol Chem 2005; 280(52):42744-42749. (Pubitemid 43049235)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.52 , pp. 42744-42749
    • Lee, S.R.1    Collins, K.2
  • 18
    • 52949145277 scopus 로고    scopus 로고
    • TRNA cleavage is a conserved response to oxidative stress in eukaryotes
    • Thompson DM, Lu C, Green PJ et al. tRNA cleavage is a conserved response to oxidative stress in eukaryotes. RNA 2008; 14(10):2095-2103.
    • (2008) RNA , vol.14 , Issue.10 , pp. 2095-2103
    • Thompson, D.M.1    Lu, C.2    Green, P.J.3
  • 21
  • 22
    • 66149125192 scopus 로고    scopus 로고
    • The phloem-delivered RNA pool contains small noncoding RNAs and interferes with translation
    • Zhang S, SunL, KraglerF. The phloem-delivered RNA pool contains small noncoding RNAs and interferes with translation. Plant Physiol 2009; 150(1):378-387.
    • (2009) Plant Physiol , vol.150 , Issue.1 , pp. 378-387
    • Zhang, S.1    Sun, L.2    Kragler, F.3
  • 23
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • Yamasaki S, Ivanov P, Hu GF et al. Angiogenin cleaves tRNA and promotes stress-induced translational repression. J Cell Biol 2009; 185(1):35-42.
    • (2009) J Cell Biol , vol.185 , Issue.1 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3
  • 24
    • 58149498297 scopus 로고    scopus 로고
    • Stress induces tRNA cleavage by angiogenin in mammalian cells
    • Fu H, Feng J, Liu Q et al. Stress induces tRNA cleavage by angiogenin in mammalian cells. FEBS Lett 2009; 583(2):437-442.
    • (2009) FEBS Lett , vol.583 , Issue.2 , pp. 437-442
    • Fu, H.1    Feng, J.2    Liu, Q.3
  • 25
    • 56049119367 scopus 로고    scopus 로고
    • Stress-induced tRNA-derived RNAs: A novel class of small RNAs in the primitive eukaryote Giardia lamblia
    • Li Y, Luo J, Zhou H et al. Stress-induced tRNA-derived RNAs: a novel class of small RNAs in the primitive eukaryote Giardia lamblia. Nucleic Acids Res 2008; 36(19):6048-6055.
    • (2008) Nucleic Acids Res , vol.36 , Issue.19 , pp. 6048-6055
    • Li, Y.1    Luo, J.2    Zhou, H.3
  • 26
    • 71049136041 scopus 로고    scopus 로고
    • Uncovering small RNA-mediated responses to phosphate deficiency in Arabidopsis by deep sequencing
    • Hsieh LC, Lin SI, Shih AC et al. Uncovering small RNA-mediated responses to phosphate deficiency in Arabidopsis by deep sequencing. Plant Physiol 2009; 151(4):2120-2132.
    • (2009) Plant Physiol , vol.151 , Issue.4 , pp. 2120-2132
    • Hsieh, L.C.1    Lin, S.I.2    Shih, A.C.3
  • 27
    • 39449095457 scopus 로고    scopus 로고
    • Developmentally regulated cleavage of tRNAs in the bacterium Streptomyces coelicolor
    • DOI 10.1093/nar/gkm1096
    • Haiser HJ, Karginov FV, Hannon GJ et al. Developmentally regulated cleavage of tRNAs in the bacterium Streptomyces coelicolor. Nucleic Acids Res 2008; 36(3):732-741. (Pubitemid 351267231)
    • (2008) Nucleic Acids Research , vol.36 , Issue.3 , pp. 732-741
    • Haiser, H.J.1    Karginov, F.V.2    Hannon, G.J.3    Elliot, M.A.4
  • 28
    • 54349104464 scopus 로고    scopus 로고
    • Mouse ES cells express endogenous shRNAs, siRNAs and other Microprocessor-independent, Dicer-dependent small RNAs
    • Babiarz JE, Ruby JG, Wang Y et al. Mouse ES cells express endogenous shRNAs, siRNAs and other Microprocessor-independent, Dicer-dependent small RNAs. Genes Dev 2008; 22(20):2773-2785.
    • (2008) Genes Dev , vol.22 , Issue.20 , pp. 2773-2785
    • Babiarz, J.E.1    Ruby, J.G.2    Wang, Y.3
  • 29
    • 32344447144 scopus 로고    scopus 로고
    • A story with a good ending: tRNA 3′-end maturation by CCA-adding enzymes
    • DOI 10.1016/j.sbi.2005.12.001, PII S0959440X05002204
    • Xiong Y, Steitz TA. A story with a good ending: tRNA 3'-end maturation by CCA-adding enzymes. Curr Opin Struct Biol 2006; 16(1):12-17. (Pubitemid 43221866)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.1 , pp. 12-17
    • Xiong, Y.1    Steitz, T.A.2
  • 30
    • 54449094641 scopus 로고    scopus 로고
    • Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs
    • Takaku H, Nashimoto M. Escherichia coli tRNase Z can shut down growth probably by removing amino acids from aminoacyl-tRNAs. Genes Cells 2008; 13(11):1087-1097.
    • (2008) Genes Cells , vol.13 , Issue.11 , pp. 1087-1097
    • Takaku, H.1    Nashimoto, M.2
  • 31
    • 33846269602 scopus 로고    scopus 로고
    • RNAs wobble decoding of the genome: 40 years of modification
    • DOI 10.1016/j.jmb.2006.11.046, PII S0022283606015865
    • Agris PF, Vendeix FA, Graham WD. tRNAs wobble decoding of the genome: 40 years of modification. J Mol Biol 2007; 366(1):1-13. (Pubitemid 46123342)
    • (2007) Journal of Molecular Biology , vol.366 , Issue.1 , pp. 1-13
    • Agris, P.F.1    Vendeix, F.A.P.2    Graham, W.D.3
  • 32
    • 65249152479 scopus 로고    scopus 로고
    • The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae
    • Thompson DM, Parker R. The RNase Rny1p cleaves tRNAs and promotes cell death during oxidative stress in Saccharomyces cerevisiae. J Cell Biol 2009; 185(1):43-50.
    • (2009) J Cell Biol , vol.185 , Issue.1 , pp. 43-50
    • Thompson, D.M.1    Parker, R.2
  • 33
    • 73649145197 scopus 로고    scopus 로고
    • Cellular and transcriptional responses of yeast to the cleavage of cytosolic tRNAs induced by colicin D
    • Shigematsu M, Ogawa T, Kido A et al. Cellular and transcriptional responses of yeast to the cleavage of cytosolic tRNAs induced by colicin D. Yeast 2009; 26(12):663-673.
    • (2009) Yeast , vol.26 , Issue.12 , pp. 663-673
    • Shigematsu, M.1    Ogawa, T.2    Kido, A.3
  • 34
    • 50949113265 scopus 로고    scopus 로고
    • Long-distance movement and differential targeting of microRNA399s
    • Lin SI, Chiou TJ. Long-distance movement and differential targeting of microRNA399s. Plant Signal Behav 2008; 3(9):730-732.
    • (2008) Plant Signal Behav , vol.3 , Issue.9 , pp. 730-732
    • Lin, S.I.1    Chiou, T.J.2
  • 35
    • 80053591906 scopus 로고    scopus 로고
    • Maintenance of a constitutive heterochromatin domain in vertebrates by a Dicer-dependent mechanism
    • sup pp 91-96
    • Giles KE, Ghirlando R, FelsenfeldG. Maintenance of a constitutive heterochromatin domain in vertebrates by a Dicer-dependent mechanism. Nat Cell Biol;12(1):94-99; sup pp 91-96.
    • Nat Cell Biol , vol.12 , Issue.1 , pp. 94-99
    • Giles, K.E.1    Ghirlando, R.2    Felsenfeld, G.3
  • 36
    • 53549105500 scopus 로고    scopus 로고
    • TRAMP-mediated RNA surveillance prevents spurious entry of RNAs into the Schizosaccharomyces pombe siRNA pathway
    • Buhler M, Spies N, Bartel DP et al. TRAMP-mediated RNA surveillance prevents spurious entry of RNAs into the Schizosaccharomyces pombe siRNA pathway. Nat Struct Mol Biol 2008; 15(10):1015-1023.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.10 , pp. 1015-1023
    • Buhler, M.1    Spies, N.2    Bartel, D.P.3
  • 37
    • 70249111171 scopus 로고    scopus 로고
    • Functional conservation of tRNase ZL among Saccharomyces cerevisiae, Schizosaccharomyces pombe and humans
    • Zhao Z, Su W, Yuan S et al. Functional conservation of tRNase ZL among Saccharomyces cerevisiae, Schizosaccharomyces pombe and humans. Biochem J 2009; 422(3):483-492.
    • (2009) Biochem J , vol.422 , Issue.3 , pp. 483-492
    • Zhao, Z.1    Su, W.2    Yuan, S.3
  • 39
    • 67650035279 scopus 로고    scopus 로고
    • Modulation of gene expression by human cytosolic tRNase Z(L) through 5'-half-tRNA
    • Elbarbary RA, Takaku H, Uchiumi N et al. Modulation of gene expression by human cytosolic tRNase Z(L) through 5'-half-tRNA. PLoS One 2009; 4(6):e5908.
    • (2009) PLoS One , vol.4 , Issue.6
    • Elbarbary, R.A.1    Takaku, H.2    Uchiumi, N.3
  • 40
    • 0029854010 scopus 로고    scopus 로고
    • Specific cleavage of target RNAs from HIV-1 with 5' half tRNA by mammalian tRNA 3' processing endoribonuclease
    • Nashimoto M. Specific cleavage of target RNAs from HIV-1 with 5' half tRNA by mammalian tRNA 3' processing endoribonuclease. RNA 1996; 2(6):523-524.
    • (1996) RNA , vol.2 , Issue.6 , pp. 523-524
    • Nashimoto, M.1
  • 41
    • 0034725035 scopus 로고    scopus 로고
    • Anomalous RNA substrates for mammalian tRNA 3' processing endoribonuclease
    • DOI 10.1016/S0014-5793(00)01462-9, PII S0014579300014629
    • Nashimoto M. Anomalous RNA substrates for mammalian tRNA 3' processing endoribonuclease. FEBS Lett 2000; 472(2-3):179-186. (Pubitemid 30224460)
    • (2000) FEBS Letters , vol.472 , Issue.2-3 , pp. 179-186
    • Nashimoto, M.1
  • 42
    • 58949103658 scopus 로고    scopus 로고
    • Inhibition of vascular endothelial growth factor expression by TRUE gene silencing
    • Elbarbary RA, Takaku H, Tamura M et al. Inhibition of vascular endothelial growth factor expression by TRUE gene silencing. Biochem Biophys Res Commun 2009; 379(4):924-927.
    • (2009) Biochem Biophys Res Commun , vol.379 , Issue.4 , pp. 924-927
    • Elbarbary, R.A.1    Takaku, H.2    Tamura, M.3
  • 43
    • 0038750928 scopus 로고    scopus 로고
    • A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease
    • DOI 10.1093/nar/gkg337
    • Takaku H, Minagawa A, Takagi M et al. A candidate prostate cancer susceptibility gene encodes tRNA 3' processing endoribonuclease. Nucleic Acids Res 2003; 31(9):2272-2278. (Pubitemid 37442094)
    • (2003) Nucleic Acids Research , vol.31 , Issue.9 , pp. 2272-2278
    • Takaku, H.1    Minagawa, A.2    Takagi, M.3    Nashimoto, M.4
  • 45
    • 33645826534 scopus 로고    scopus 로고
    • RNase Z in Escherichia coli plays a significant role in mRNA decay
    • Perwez T, Kushner SR. RNase Z in Escherichia coli plays a significant role in mRNA decay. Mol Microbiol 2006; 60(3):723-737.
    • (2006) Mol Microbiol , vol.60 , Issue.3 , pp. 723-737
    • Perwez, T.1    Kushner, S.R.2
  • 46
    • 51349111701 scopus 로고    scopus 로고
    • Gcn4 is required for the response to peroxide stress in the yeast Saccharomyces cerevisiae
    • Mascarenhas C, Edwards-Ingram LC, Zeef L et al. Gcn4 is required for the response to peroxide stress in the yeast Saccharomyces cerevisiae. Mol Biol Cell 2008; 19(7):2995-3007.
    • (2008) Mol Biol Cell , vol.19 , Issue.7 , pp. 2995-3007
    • Mascarenhas, C.1    Edwards-Ingram, L.C.2    Zeef, L.3
  • 48
    • 56749170666 scopus 로고    scopus 로고
    • Non-coding RNA production by RNA polymerase III is implicated in cancer
    • Marshall L, White RJ. Non-coding RNA production by RNA polymerase III is implicated in cancer. Nat Rev Cancer 2008; 8(12):911-914.
    • (2008) Nat Rev Cancer , vol.8 , Issue.12 , pp. 911-914
    • Marshall, L.1    White, R.J.2
  • 50
    • 40649101442 scopus 로고    scopus 로고
    • On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE
    • Sheppard K, Soil D. On the evolution of the tRNA-dependent amidotransferases, GatCAB and GatDE. J Mol Biol 2008; 377(3):831-844.
    • (2008) J Mol Biol , vol.377 , Issue.3 , pp. 831-844
    • Sheppard, K.1    Soil, D.2
  • 51
    • 39149083088 scopus 로고    scopus 로고
    • Cytoplasmic steps ofpeptidoglycanbiosynthesis
    • BarreteauH, Kovac A, Boniface Aet al. Cytoplasmic steps ofpeptidoglycanbiosynthesis. FEMS Microbiol Rev 2008; 32(2):168-207.
    • (2008) FEMS Microbiol Rev , vol.32 , Issue.2 , pp. 168-207
    • Barreteau, H.1    Kovac, A.2    Boniface, A.3
  • 52
    • 71549148798 scopus 로고    scopus 로고
    • Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol
    • Roy H. Tuning the properties of the bacterial membrane with aminoacylated phosphatidylglycerol. IUBMB Life 2009; 61(10):940-953.
    • (2009) IUBMB Life , vol.61 , Issue.10 , pp. 940-953
    • Roy, H.1
  • 53
    • 71549148346 scopus 로고    scopus 로고
    • TRNA as an active chemical scaffold for diverse chemical transformations
    • Francklyn CS, Minajigi A. tRNA as an active chemical scaffold for diverse chemical transformations. FEBS Lett 584(2):366-375.
    • FEBS Lett , vol.584 , Issue.2 , pp. 366-375
    • Francklyn, C.S.1    Minajigi, A.2
  • 54
    • 69449087350 scopus 로고    scopus 로고
    • The N-end rule pathway controls multiple functions during Arabidopsis shoot and leafdevelopment
    • Graciet E, Walter F, Maoileidigh DO et al. The N-end rule pathway controls multiple functions during Arabidopsis shoot and leafdevelopment. Proc Natl Acad Sci USA 2009; 106(32):13618-13623.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.32 , pp. 13618-13623
    • Graciet, E.1    Walter, F.2    Maoileidigh, D.O.3
  • 55
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • Holzmann J, Frank P, Loftier E et al. RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 2008; 135(3):462-474.
    • (2008) Cell , vol.135 , Issue.3 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Loftier, E.3
  • 56
    • 70349587050 scopus 로고    scopus 로고
    • The RNase P family
    • Ellis JC, Brown JW. The RNase P family. RNA Biol 2009; 6(4):362-369.
    • (2009) RNA Biol , vol.6 , Issue.4 , pp. 362-369
    • Ellis, J.C.1    Brown, J.W.2
  • 57
    • 67349162192 scopus 로고    scopus 로고
    • TRNA recognition, processing and disease: Hypotheses around an unorthodox type ofRNase P in human mitochondria
    • Holzmann J, Rossmanith W. tRNA recognition, processing and disease: hypotheses around an unorthodox type ofRNase P in human mitochondria. Mitochondrion 2009; 9(4):284-288.
    • (2009) Mitochondrion , vol.9 , Issue.4 , pp. 284-288
    • Holzmann, J.1    Rossmanith, W.2
  • 58
    • 70349270679 scopus 로고    scopus 로고
    • Mental retardation linked to mutations in the HSD17B10 gene interfering with neurosteroid and isoleucine metabolism
    • Yang SY, He XY, Olpin SE et al. Mental retardation linked to mutations in the HSD17B10 gene interfering with neurosteroid and isoleucine metabolism. Proc Natl Acad Sci USA 2009; 106(35):14820-14824.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.35 , pp. 14820-14824
    • Yang, S.Y.1    He, X.Y.2    Olpin, S.E.3
  • 59
    • 80053584143 scopus 로고    scopus 로고
    • An unexpected ending: Noncanonical 3' end processing mechanisms
    • Wilusz JE, Spector DL. An unexpected ending: Noncanonical 3' end processing mechanisms. RNA 2009.
    • (2009) RNA
    • Wilusz, J.E.1    Spector, D.L.2
  • 60
    • 50449087360 scopus 로고    scopus 로고
    • Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs
    • Coughlin DJ, Pleiss JA, Walker SC et al. Genome-wide search for yeast RNase P substrates reveals role in maturation of intron-encoded box C/D small nucleolar RNAs. Proc Natl Acad Sci USA 2008; 105(34):12218-12223.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.34 , pp. 12218-12223
    • Coughlin, D.J.1    Pleiss, J.A.2    Walker, S.C.3
  • 61
    • 0036238633 scopus 로고    scopus 로고
    • Essential roles of Bdp1, a subunit of RNA polymerase III initiation factor TFIIIB, in transcription and tRNA processing
    • DOI 10.1128/MCB.22.10.3264-3275.2002
    • Ishiguro A, Kassavetis GA, Geiduschek EP. Essential roles of Bdpl, a subunit of RNA polymerase III initiation factor TFIIIB, in transcription and tRNA processing. Mol Cell Biol 2002; 22(10):3264-3275. (Pubitemid 34453968)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.10 , pp. 3264-3275
    • Ishiguro, A.1    Kassavetis, G.A.2    Geiduschek, E.P.3
  • 62
    • 34547102278 scopus 로고    scopus 로고
    • Human RNase P: A tRNA-processing enzyme and transcription factor
    • DOI 10.1093/nar/gkm071
    • Jarrous N, Reiner R. Human RNase P: atRNA-processing enzyme and transcription factor. Nucleic Acids Res 2007; 35(11):3519-3524. (Pubitemid 47244648)
    • (2007) Nucleic Acids Research , vol.35 , Issue.11 , pp. 3519-3524
    • Jarrous, N.1    Reiner, R.2
  • 63
    • 2042479408 scopus 로고    scopus 로고
    • Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3′ end formation
    • DOI 10.1016/S0092-8674(04)00342-3, PII S0092867404003423
    • Paushkin SV, Patel M, Furia BS et al. Identification of a human endonuclease complex reveals a link between tRNA splicing and pre-mRNA 3' endformation. Cell 2004; 117(3):311-321. (Pubitemid 38534538)
    • (2004) Cell , vol.117 , Issue.3 , pp. 311-321
    • Paushkin, S.V.1    Patel, M.2    Furia, B.S.3    Peltz, S.W.4    Trotta, C.R.5
  • 64
    • 50449096432 scopus 로고    scopus 로고
    • TRNA splicing endonuclease mutations cause pontocerebellar hypoplasia
    • Budde BS, Namavar Y, Barth PG et al. tRNA splicing endonuclease mutations cause pontocerebellar hypoplasia. Nat Genet 2008; 40(9):1113-1118.
    • (2008) Nat Genet , vol.40 , Issue.9 , pp. 1113-1118
    • Budde, B.S.1    Namavar, Y.2    Barth, P.G.3
  • 65
    • 0025001288 scopus 로고
    • Involvement of aminoacyl-tRNA synthetases and other proteins in group i and group II intron splicing
    • Lambowitz AM, Perlman PS. Involvement of aminoacyl-tRNA synthetases and other proteins in group I and group II intron splicing. Trends Biochem Sci 1990; 15(11):440-444.
    • (1990) Trends Biochem Sci , vol.15 , Issue.11 , pp. 440-444
    • Lambowitz, A.M.1    Perlman, P.S.2
  • 66
    • 65749103424 scopus 로고    scopus 로고
    • Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase
    • Kapoor M, Otero FJ, Slike BM et al. Mutational separation of aminoacylation and cytokine activities of human tyrosyl-tRNA synthetase. Chem Biol 2009; 16(5):531-539.
    • (2009) Chem Biol , vol.16 , Issue.5 , pp. 531-539
    • Kapoor, M.1    Otero, F.J.2    Slike, B.M.3
  • 67
    • 66449115592 scopus 로고    scopus 로고
    • LysRS serves as a key signaling molecule in the immune response by regulating gene expression
    • Yannay-Cohen N, Carmi-Levy I, Kay G et al. LysRS serves as a key signaling molecule in the immune response by regulating gene expression. Mol Cell 2009; 34(5):603-611.
    • (2009) Mol Cell , vol.34 , Issue.5 , pp. 603-611
    • Yannay-Cohen, N.1    Carmi-Levy, I.2    Kay, G.3
  • 68
    • 67650677056 scopus 로고    scopus 로고
    • Mutant glycyl-tRNA synthetase (Gars) ameliorates SODl(G93A) motor neuron degeneration phenotype but has little affect on Loa dynein heavy chain mutant mice
    • Banks GT, Bros-Facer V, Williams HP et al. Mutant glycyl-tRNA synthetase (Gars) ameliorates SODl(G93A) motor neuron degeneration phenotype but has little affect on Loa dynein heavy chain mutant mice. PLoS One 2009; 4(7):e6218.
    • (2009) PLoS One , vol.4 , Issue.7
    • Banks, G.T.1    Bros-Facer, V.2    Williams, H.P.3
  • 69
    • 1542376205 scopus 로고    scopus 로고
    • Molecular Modeling Study of the Editing Active Site of Escherichia coli Leucyl-tRNA Synthetase: Two Amino Acid Binding Sites in the Editing Domain
    • DOI 10.1002/prot.10300
    • Lee KW, Briggs JM. Molecular modeling study of the editing active site ofEscherichia coli leucyl-tRNA synthetase: two amino acid binding sites in the editing domain. Proteins 2004; 54(4):693-704. (Pubitemid 38298788)
    • (2004) Proteins: Structure, Function and Genetics , vol.54 , Issue.4 , pp. 693-704
    • Lee, K.W.1    Briggs, J.M.2
  • 70
    • 52949118056 scopus 로고    scopus 로고
    • The role ofaminoacyl-tRNA synthetases in genetic diseases
    • Antonellis A, Green ED. The role ofaminoacyl-tRNA synthetases in genetic diseases. Annu Rev Genomics Hum Genet 2008; 9:87-107.
    • (2008) Annu Rev Genomics Hum Genet , vol.9 , pp. 87-107
    • Antonellis, A.1    Green, E.D.2
  • 72
    • 69949167078 scopus 로고    scopus 로고
    • Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p
    • Zaborske JM, Narasimhan J, Jiang L et al. Genome-wide analysis of tRNA charging and activation of the eIF2 kinase Gcn2p. J Biol Chem 2009; 284(37):25254-25267.
    • (2009) J Biol Chem , vol.284 , Issue.37 , pp. 25254-25267
    • Zaborske, J.M.1    Narasimhan, J.2    Jiang, L.3
  • 73
    • 25444436228 scopus 로고    scopus 로고
    • Human mitochondrial diseases associated with tRNA wobble modification deficiency
    • Kirino Y, Suzuki T. Human mitochondrial diseases associated with tRNA wobble modification deficiency. RNA Biol 2005; 2(2):41-44. (Pubitemid 41359797)
    • (2005) RNA Biology , vol.2 , Issue.2 , pp. 41-44
    • Kirino, Y.1    Suzuki, T.2
  • 74
    • 38349190048 scopus 로고    scopus 로고
    • Deletion of the selenocysteine tRNA gene in macrophages and liver results in compensatory gene induction of cytoprotective enzymes by Nrf2
    • Suzuki T, Kelly VP, Motohashi H et al. Deletion of the selenocysteine tRNA gene in macrophages and liver results in compensatory gene induction of cytoprotective enzymes by Nrf2. J Biol Chem 2008; 283(4):2021-2030.
    • (2008) J Biol Chem , vol.283 , Issue.4 , pp. 2021-2030
    • Suzuki, T.1    Kelly, V.P.2    Motohashi, H.3
  • 75
    • 41649102484 scopus 로고    scopus 로고
    • Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast
    • DOI 10.1261/rna.966208
    • Gustavsson M, Ronne H. Evidence that tRNA modifying enzymes are important in vivo targets for 5-fluorouracil in yeast. RNA 2008; 14(4):666-674. (Pubitemid 351480879)
    • (2008) RNA , vol.14 , Issue.4 , pp. 666-674
    • Gustavsson, M.1    Ronne, H.2
  • 76
    • 59649123170 scopus 로고    scopus 로고
    • Chapter 11. Identification and analysis of tRNAs that are degraded in Saccharomyces cerevisiae due to lackofmodifications
    • Chernyakov I, Baker MA, Grayhack EJ et al. Chapter 11. Identification and analysis of tRNAs that are degraded in Saccharomyces cerevisiae due to lackofmodifications. Methods Enzymol 2008; 449:221-237.
    • (2008) Methods Enzymol , vol.449 , pp. 221-237
    • Chernyakov, I.1    Baker, M.A.2    Grayhack, E.J.3
  • 77
    • 0032488657 scopus 로고    scopus 로고
    • A conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst
    • DOI 10.1021/bi971874+
    • Huang L, Pookanjanatavip M, Gu X et al. A conserved aspartate of tRNA pseudouridine synthase is essential for activity and aprobable nucleophilic catalyst. Biochemistry (Mosc) 1998; 37(1):344-351. (Pubitemid 28049138)
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 344-351
    • Huang, L.1    Pookanjanatavip, M.2    Gu, X.3    Santi, D.V.4
  • 78
    • 0019978251 scopus 로고
    • Loss of tRNA 5-methyluridine methylstransferase and pseudouridine synthetase activities in 5-fluorouracil and 1-(tetrahydro-2-furanyl)-5- fluorouracil (ftorafur)-treated Escherichia coli
    • Frendewey DA, Kladianos DM, Moore VG et al. Loss of tRNA 5-methyluridine methyltransferase and pseudouridine synthetase activities in 5-fluorouracil and l-(tetrahydro-2-furanyl)-5-fluorouracil (ftorafur)-treated Escherichia coli. Biochim Biophys Acta 1982; 697(l):31-40. (Pubitemid 12082056)
    • (1982) Biochimica et Biophysica Acta , vol.697 , Issue.1 , pp. 31-40
    • Frendewey, D.A.1    Kladianos, D.M.2    Moore, V.G.3    Kaiser, I.I.4
  • 80
    • 0027716283 scopus 로고
    • Tumor markers for breast cancer
    • Hayes DF. Tumor markers for breast cancer. Ann Oncol 1993; 4(10):807-819. (Pubitemid 24032086)
    • (1993) Annals of Oncology , vol.4 , Issue.10 , pp. 807-819
    • Hayes, D.F.1
  • 81
    • 62049085249 scopus 로고    scopus 로고
    • Inhibition of RNA polymerase III transcription by BRCA1
    • Veras I, Rosen EM, Schramm L. Inhibition of RNA polymerase III transcription by BRCA1. J Mol Biol 2009; 387(3):523-531.
    • (2009) J Mol Biol , vol.387 , Issue.3 , pp. 523-531
    • Veras, I.1    Rosen, E.M.2    Schramm, L.3
  • 82
    • 33646500809 scopus 로고    scopus 로고
    • BRCA1 regulation oftranscription
    • Rosen EM, Fan S, Ma Y. BRCA1 regulation oftranscription. Cancer Lett 2006; 236(2):175-185.
    • (2006) Cancer Lett , vol.236 , Issue.2 , pp. 175-185
    • Rosen, E.M.1    Fan, S.2    Ma, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.