메뉴 건너뛰기




Volumn 5, Issue 1, 2014, Pages 15-29

The emerging role of triple helices in RNA biology

Author keywords

[No Author keywords available]

Indexed keywords

MALAT1 PROTEIN; MEMBRANE PROTEIN; NUCLEAR RNA; POLYADENYLATED RNA; POLYADENYLIC ACID; RNA; S ADENOSYLMETHIONINE; TELOMERASE; TELOMERASE ASSOCIATED RNA; UNCLASSIFIED DRUG; UNTRANSLATED RNA; VIRUS RNA;

EID: 84890278241     PISSN: 17577004     EISSN: 17577012     Source Type: Journal    
DOI: 10.1002/wrna.1194     Document Type: Review
Times cited : (65)

References (83)
  • 1
    • 0034636956 scopus 로고    scopus 로고
    • Structural biology. The ribosome is a ribozyme
    • Cech TR. Structural biology. The ribosome is a ribozyme. Science 2000, 289:878-879.
    • (2000) Science , vol.289 , pp. 878-879
    • Cech, T.R.1
  • 2
    • 33947470407 scopus 로고
    • Formation of a threestranded polynucleotide molecule
    • Rich A, Felsenfeld G. Formation of a threestranded polynucleotide molecule. J Am Chem Soc 1957, 79:2023-2024.
    • (1957) J Am Chem Soc , vol.79 , pp. 2023-2024
    • Rich, A.1    Felsenfeld, G.2
  • 3
    • 0024368152 scopus 로고
    • Studies on the formation of two- and three-stranded polyribonucleotides
    • Felsenfeld G, Rich A. Studies on the formation of two- and three-stranded polyribonucleotides. Biochim Biophys Acta 1957, 1000:87-98.
    • (1957) Biochim Biophys Acta , vol.1000 , pp. 87-98
    • Felsenfeld, G.1    Rich, A.2
  • 4
    • 79956073017 scopus 로고    scopus 로고
    • Potential in vivo roles of nucleic acid triple-helices
    • doi: 10.4161/rna.8.3.14999.
    • Buske FA, Mattick JS, Bailey TL. Potential in vivo roles of nucleic acid triple-helices. RNA Biol 2011, 8:427-439. doi: 10.4161/rna.8.3.14999.
    • (2011) RNA Biol , vol.8 , pp. 427-439
    • Buske, F.A.1    Mattick, J.S.2    Bailey, T.L.3
  • 5
    • 33646362778 scopus 로고    scopus 로고
    • Discovery of the hybrid helix and the first DNA-RNA hybridization
    • doi: 10.1074/JBC.X600003200.
    • Rich A. Discovery of the hybrid helix and the first DNA-RNA hybridization. J Biol Chem 2006, 281:7693-7696. doi: 10.1074/JBC.X600003200.
    • (2006) J Biol Chem , vol.281 , pp. 7693-7696
    • Rich, A.1
  • 6
    • 70350004178 scopus 로고    scopus 로고
    • The era of RNA awakening: structural biology of RNA in the early years
    • doi: 10.1017/S0033583509004776.
    • Rich A. The era of RNA awakening: structural biology of RNA in the early years. Q Rev Biophys 2009, 42:117-137. doi: 10.1017/S0033583509004776.
    • (2009) Q Rev Biophys , vol.42 , pp. 117-137
    • Rich, A.1
  • 7
    • 0000403995 scopus 로고
    • The crystal and molecular structure of a hydrogen-bonded complex between 1-methylthymine and 9-methyladenine
    • doi: 10.1107/S0365110X63002437.
    • Hoogsteen K. The crystal and molecular structure of a hydrogen-bonded complex between 1-methylthymine and 9-methyladenine. Acta Cryst 1963, 16:907-916. doi: 10.1107/S0365110X63002437.
    • (1963) Acta Cryst , vol.16 , pp. 907-916
    • Hoogsteen, K.1
  • 8
    • 38849197858 scopus 로고    scopus 로고
    • Structure of the SAM-II riboswitch bound to S-adenosylmethionine
    • doi: 10.1038/nsmb.1371.
    • Gilbert SD, Rambo RP, Van Tyne D, Batey RT. Structure of the SAM-II riboswitch bound to S-adenosylmethionine. Nat Struct Mol Biol 2008, 15:177-182. doi: 10.1038/nsmb.1371.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 177-182
    • Gilbert, S.D.1    Rambo, R.P.2    Van Tyne, D.3    Batey, R.T.4
  • 9
    • 14644435818 scopus 로고    scopus 로고
    • Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function
    • doi: 10.1016/j.molcel.2005.01.017.
    • Theimer CA, Blois CA, Feigon J. Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function. Mol Cell 2005, 17:671-682. doi: 10.1016/j.molcel.2005.01.017.
    • (2005) Mol Cell , vol.17 , pp. 671-682
    • Theimer, C.A.1    Blois, C.A.2    Feigon, J.3
  • 10
    • 0027753985 scopus 로고
    • Nucleoside triples from the group I intron
    • Chastain M, Tinoco I. Nucleoside triples from the group I intron. Biochemistry 1993, 32:14220-14228.
    • (1993) Biochemistry , vol.32 , pp. 14220-14228
    • Chastain, M.1    Tinoco, I.2
  • 11
    • 0033010932 scopus 로고    scopus 로고
    • Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot
    • doi: 10.1038/6722.
    • Su L, Chen L, Egli M, Berger JM, Rich A. Minor groove RNA triplex in the crystal structure of a ribosomal frameshifting viral pseudoknot. Nat Struct Biol. 1999, 6:285-292. doi: 10.1038/6722.
    • (1999) Nat Struct Biol. , vol.6 , pp. 285-292
    • Su, L.1    Chen, L.2    Egli, M.3    Berger, J.M.4    Rich, A.5
  • 12
    • 78649422018 scopus 로고    scopus 로고
    • Poly(A) tail recognition by a viral RNA element through assembly of a triple helix
    • doi: 10.1126/science.1195858.
    • Mitton-Fry RM, DeGregorio SJ, Wang J, Steitz TA, Steitz JA. Poly(A) tail recognition by a viral RNA element through assembly of a triple helix. Science 2010, 330:1244-1247. doi: 10.1126/science.1195858.
    • (2010) Science , vol.330 , pp. 1244-1247
    • Mitton-Fry, R.M.1    DeGregorio, S.J.2    Wang, J.3    Steitz, T.A.4    Steitz, J.A.5
  • 13
    • 41749109563 scopus 로고    scopus 로고
    • Crystal structure of a self-spliced group II intron
    • doi: 10.1126/science.1153803.
    • Toor N, Keating KS, Taylor SD, Pyle AM. Crystal structure of a self-spliced group II intron. Science 2008, 320:77-82. doi: 10.1126/science.1153803.
    • (2008) Science , vol.320 , pp. 77-82
    • Toor, N.1    Keating, K.S.2    Taylor, S.D.3    Pyle, A.M.4
  • 14
    • 84868519473 scopus 로고    scopus 로고
    • A triple helix stabilizes the 3' ends of long noncoding RNAs that lack poly(A) tails
    • doi: 10.1101/gad.204438.112.
    • Wilusz JE, JnBaptiste CK, Lu LY, Kuhn CD, Joshua-Tor L, Sharp PA. A triple helix stabilizes the 3' ends of long noncoding RNAs that lack poly(A) tails. Genes Dev 2012, 26:2392-2407. doi: 10.1101/gad.204438.112.
    • (2012) Genes Dev , vol.26 , pp. 2392-2407
    • Wilusz, J.E.1    JnBaptiste, C.K.2    Lu, L.Y.3    Kuhn, C.D.4    Joshua-Tor, L.5    Sharp, P.A.6
  • 15
    • 0027081208 scopus 로고
    • A base-triple structural domain in RNA
    • Chastain M, Tinoco I. A base-triple structural domain in RNA. Biochemistry 1992, 31:12733-12741.
    • (1992) Biochemistry , vol.31 , pp. 12733-12741
    • Chastain, M.1    Tinoco, I.2
  • 16
    • 84872543206 scopus 로고    scopus 로고
    • A decade of riboswitches
    • doi: 10.1016/j.cell.2012.12.024.
    • Serganov A, Nudler E. A decade of riboswitches. Cell 2013, 152(1-2):17-24. doi: 10.1016/j.cell.2012.12.024.
    • (2013) Cell , vol.152 , Issue.1-2 , pp. 17-24
    • Serganov, A.1    Nudler, E.2
  • 17
    • 33747186460 scopus 로고    scopus 로고
    • S-Adenosyl-L-methionine: beyond the universal methyl group donor
    • doi: 10.1016/j.phytochem.2006.04.019.
    • Roje S. S-Adenosyl-L-methionine: beyond the universal methyl group donor. Phytochemistry 2006, 67:1686-1698. doi: 10.1016/j.phytochem.2006.04.019.
    • (2006) Phytochemistry , vol.67 , pp. 1686-1698
    • Roje, S.1
  • 18
    • 42149091618 scopus 로고    scopus 로고
    • Riboswitches that sense S-adenosylmethionine and S-adenosylhomocysteine
    • doi: 10.1139/O08-008.
    • Wang JX, Breaker RR. Riboswitches that sense S-adenosylmethionine and S-adenosylhomocysteine. Biochem Cell Biol 2008, 86:157-168. doi: 10.1139/O08-008.
    • (2008) Biochem Cell Biol , vol.86 , pp. 157-168
    • Wang, J.X.1    Breaker, R.R.2
  • 19
    • 70350111141 scopus 로고    scopus 로고
    • A variant riboswitch aptamer class for S-adenosylmethionine common in marine bacteria
    • doi: 10.1261/rna.1824209.
    • Poiata E, Meyer MM, Ames TD, Breaker RR. A variant riboswitch aptamer class for S-adenosylmethionine common in marine bacteria. RNA 2009, 15:2046-2056. doi: 10.1261/rna.1824209.
    • (2009) RNA , vol.15 , pp. 2046-2056
    • Poiata, E.1    Meyer, M.M.2    Ames, T.D.3    Breaker, R.R.4
  • 20
    • 40849104495 scopus 로고    scopus 로고
    • The aptamer core of SAM-IV riboswitches mimics the ligand-binding site of SAM-I riboswitches
    • doi: 10.1261/rna.988608.
    • Weinberg Z, Regulski EE, Hammond MC, Barrick JE, Yao Z, Ruzzo WL, Breaker RR. The aptamer core of SAM-IV riboswitches mimics the ligand-binding site of SAM-I riboswitches. RNA 2008, 14:822-828. doi: 10.1261/rna.988608.
    • (2008) RNA , vol.14 , pp. 822-828
    • Weinberg, Z.1    Regulski, E.E.2    Hammond, M.C.3    Barrick, J.E.4    Yao, Z.5    Ruzzo, W.L.6    Breaker, R.R.7
  • 21
    • 80054990557 scopus 로고    scopus 로고
    • New families of human regulatory RNA structures identified by comparative analysis of vertebrate genomes
    • doi: 10.1101/gr.112516.110.
    • Parker BJ, Moltke I, Roth A, Washietl S, Wen J, Kellis M, Breaker R, Pedersen JS. New families of human regulatory RNA structures identified by comparative analysis of vertebrate genomes. Genome Res 2011, 21:1929-1943. doi: 10.1101/gr.112516.110.
    • (2011) Genome Res , vol.21 , pp. 1929-1943
    • Parker, B.J.1    Moltke, I.2    Roth, A.3    Washietl, S.4    Wen, J.5    Kellis, M.6    Breaker, R.7    Pedersen, J.S.8
  • 22
    • 32044442926 scopus 로고    scopus 로고
    • Evidence for a second class of S-adenosylmethionine riboswitches and other regulatory RNA motifs in alpha-proteobacteria
    • doi: 10.1186/gb-2005-6-8-r70.
    • Corbino KA, Barrick JE, Lim J, Welz R, Tucker BJ, Puskarz I, Mandal M, Rudnick ND, Breaker RR. Evidence for a second class of S-adenosylmethionine riboswitches and other regulatory RNA motifs in alpha-proteobacteria. Genome Biol 2005, 6:R70. doi: 10.1186/gb-2005-6-8-r70.
    • (2005) Genome Biol , vol.6
    • Corbino, K.A.1    Barrick, J.E.2    Lim, J.3    Welz, R.4    Tucker, B.J.5    Puskarz, I.6    Mandal, M.7    Rudnick, N.D.8    Breaker, R.R.9
  • 23
    • 84855984817 scopus 로고    scopus 로고
    • Atomic-level insights into metabolite recognition and specificity of the SAM-II riboswitch
    • doi: 10.1261/rna.028779.111.
    • Doshi U, Kelley JM, Hamelberg D. Atomic-level insights into metabolite recognition and specificity of the SAM-II riboswitch. RNA 2012, 18:300-307. doi: 10.1261/rna.028779.111.
    • (2012) RNA , vol.18 , pp. 300-307
    • Doshi, U.1    Kelley, J.M.2    Hamelberg, D.3
  • 24
    • 79956072525 scopus 로고    scopus 로고
    • Conformational capture of the SAM-II riboswitch
    • doi: 10.1038/nchembio.562.
    • Haller A, Rieder U, Aigner M, Blanchard SC, Micura R. Conformational capture of the SAM-II riboswitch. Nat Chem Biol 2011, 7:393-400. doi: 10.1038/nchembio.562.
    • (2011) Nat Chem Biol , vol.7 , pp. 393-400
    • Haller, A.1    Rieder, U.2    Aigner, M.3    Blanchard, S.C.4    Micura, R.5
  • 25
    • 84860160810 scopus 로고    scopus 로고
    • Multiple conformations of SAM-II riboswitch detected with SAXS and NMR spectroscopy
    • doi: 10.1093/nar/gkr1154.
    • Chen B, Zuo X, Wang Y-X, Dayie TK. Multiple conformations of SAM-II riboswitch detected with SAXS and NMR spectroscopy. Nucleic Acids Res 2012, 40:3117-3130. doi: 10.1093/nar/gkr1154.
    • (2012) Nucleic Acids Res , vol.40 , pp. 3117-3130
    • Chen, B.1    Zuo, X.2    Wang, Y.-X.3    Dayie, T.K.4
  • 26
    • 77950350987 scopus 로고    scopus 로고
    • Atomistic basis for the on-off signaling mechanism in SAM-II riboswitch
    • doi: 10.1093/nar/gkp1106.
    • Kelley JM, Hamelberg D. Atomistic basis for the on-off signaling mechanism in SAM-II riboswitch. Nucleic Acids Res 2010, 38:1392-1400. doi: 10.1093/nar/gkp1106.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1392-1400
    • Kelley, J.M.1    Hamelberg, D.2
  • 27
    • 84860261471 scopus 로고    scopus 로고
    • Telomerase: an RNP enzyme synthesizes DNA
    • doi: 10.1101/cshperspect.a003558.
    • Blackburn EH, Collins K. Telomerase: an RNP enzyme synthesizes DNA. Cold Spring Harb Perspect Biol 2011, 3:a003558-a003558. doi: 10.1101/cshperspect.a003558.
    • (2011) Cold Spring Harb Perspect Biol , vol.3
    • Blackburn, E.H.1    Collins, K.2
  • 28
    • 82755192899 scopus 로고    scopus 로고
    • Role of telomeres and telomerase in cancer
    • doi: 10.1016/j.semcancer.2011.10.001.
    • Shay JW, Wright WE. Role of telomeres and telomerase in cancer. Semin Cancer Biol 2011, 21:349-353. doi: 10.1016/j.semcancer.2011.10.001.
    • (2011) Semin Cancer Biol , vol.21 , pp. 349-353
    • Shay, J.W.1    Wright, W.E.2
  • 29
    • 84873319024 scopus 로고    scopus 로고
    • The role of telomeres in stem cells and cancer
    • doi: 10.1016/j.cell.2013.01.010.
    • Günes C, Rudolph KL. The role of telomeres in stem cells and cancer. Cell 2013, 152:390-393. doi: 10.1016/j.cell.2013.01.010.
    • (2013) Cell , vol.152 , pp. 390-393
    • Günes, C.1    Rudolph, K.L.2
  • 30
    • 77957220075 scopus 로고    scopus 로고
    • InTERTpreting telomerase structure and function
    • doi: 10.1093/nar/gkq370.
    • Wyatt HDM, West SC, Beattie TL. InTERTpreting telomerase structure and function. Nucleic Acids Res 2010, 38:5609-5622. doi: 10.1093/nar/gkq370.
    • (2010) Nucleic Acids Res , vol.38 , pp. 5609-5622
    • Wyatt, H.D.M.1    West, S.C.2    Beattie, T.L.3
  • 31
    • 53349161932 scopus 로고    scopus 로고
    • Structure of the Tribolium castaneum telomerase catalytic subunit TERT
    • doi: 10.1038/nature07283.
    • Gillis AJ, Schuller AP, Skordalakes E. Structure of the Tribolium castaneum telomerase catalytic subunit TERT. Nature 2008, 455:633-637. doi: 10.1038/nature07283.
    • (2008) Nature , vol.455 , pp. 633-637
    • Gillis, A.J.1    Schuller, A.P.2    Skordalakes, E.3
  • 32
    • 56949105325 scopus 로고    scopus 로고
    • Solution structure and dynamics of the wild-type pseudoknot of human telomerase RNA
    • doi: 10.1016/j.jmb.2008.10.005.
    • Kim N-K, Zhang Q, Zhou J, Theimer CA, Peterson RD, Feigon J. Solution structure and dynamics of the wild-type pseudoknot of human telomerase RNA. J Mol Biol 2008, 384:1249-1261. doi: 10.1016/j.jmb.2008.10.005.
    • (2008) J Mol Biol , vol.384 , pp. 1249-1261
    • Kim, N.-K.1    Zhang, Q.2    Zhou, J.3    Theimer, C.A.4    Peterson, R.D.5    Feigon, J.6
  • 33
    • 84866611481 scopus 로고    scopus 로고
    • Biogenesis of telomerase ribonucleoproteins
    • doi: 10.1261/rna.034629.112.
    • Egan ED, Collins K. Biogenesis of telomerase ribonucleoproteins. RNA 2012, 18:1747-1759. doi: 10.1261/rna.034629.112.
    • (2012) RNA , vol.18 , pp. 1747-1759
    • Egan, E.D.1    Collins, K.2
  • 34
    • 0034598919 scopus 로고    scopus 로고
    • Secondary structure of vertebrate telomerase RNA
    • Chen JL, Blasco MA, Greider CW. Secondary structure of vertebrate telomerase RNA. Cell 2000, 100:503-514.
    • (2000) Cell , vol.100 , pp. 503-514
    • Chen, J.L.1    Blasco, M.A.2    Greider, C.W.3
  • 35
    • 6944256804 scopus 로고    scopus 로고
    • An emerging consensus for telomerase RNA structure
    • doi: 10.1073/pnas.0406204101.
    • Chen J-L, Greider CW. An emerging consensus for telomerase RNA structure. Proc Natl Acad Sci USA 2004, 101:14683-14684. doi: 10.1073/pnas.0406204101.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14683-14684
    • Chen, J.-L.1    Greider, C.W.2
  • 36
    • 33744799697 scopus 로고    scopus 로고
    • Structure and function of telomerase RNA
    • doi: 10.1016/j.sbi.2006.05.005.
    • Theimer CA, Feigon J. Structure and function of telomerase RNA. Curr Opin Struct Biol 2006, 16:307-318. doi: 10.1016/j.sbi.2006.05.005.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 307-318
    • Theimer, C.A.1    Feigon, J.2
  • 37
    • 44849094904 scopus 로고    scopus 로고
    • Triple-helix structure in telomerase RNA contributes to catalysis
    • doi: 10.1038/nsmb.1420.
    • Qiao F, Cech TR. Triple-helix structure in telomerase RNA contributes to catalysis. Nat Struct Mol Biol 2008, 15:634-640. doi: 10.1038/nsmb.1420.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 634-640
    • Qiao, F.1    Cech, T.R.2
  • 38
    • 33947277419 scopus 로고    scopus 로고
    • A triple helix within a pseudoknot is a conserved and essential element of telomerase RNA
    • doi: 10.1128/MCB.01826-06.
    • Shefer K, Brown Y, Gorkovoy V, Nussbaum T, Ulyanov NB, Tzfati Y. A triple helix within a pseudoknot is a conserved and essential element of telomerase RNA. Mol Cell Biol 2007, 27:2130-2143. doi: 10.1128/MCB.01826-06.
    • (2007) Mol Cell Biol , vol.27 , pp. 2130-2143
    • Shefer, K.1    Brown, Y.2    Gorkovoy, V.3    Nussbaum, T.4    Ulyanov, N.B.5    Tzfati, Y.6
  • 39
    • 77956682931 scopus 로고    scopus 로고
    • Targeted 2'-O methylation at a nucleotide within the pseudoknot of telomerase RNA reduces telomerase activity in vivo
    • doi: 10.1128/MCB.00384-10.
    • Huang C, Yu Y-T. Targeted 2'-O methylation at a nucleotide within the pseudoknot of telomerase RNA reduces telomerase activity in vivo. Mol Cell Biol 2010, 30:4368-4378. doi: 10.1128/MCB.00384-10.
    • (2010) Mol Cell Biol , vol.30 , pp. 4368-4378
    • Huang, C.1    Yu, Y.-T.2
  • 40
    • 84867583317 scopus 로고    scopus 로고
    • Telomerase activity is sensitive to subtle perturbations of the TLC1 pseudoknot 3' stem and tertiary structure
    • doi: 10.1016/j.jmb.2012.08.025.
    • Liu F, Theimer CA. Telomerase activity is sensitive to subtle perturbations of the TLC1 pseudoknot 3' stem and tertiary structure. J Mol Biol 2012, 423:719-735. doi: 10.1016/j.jmb.2012.08.025.
    • (2012) J Mol Biol , vol.423 , pp. 719-735
    • Liu, F.1    Theimer, C.A.2
  • 41
    • 77957121811 scopus 로고    scopus 로고
    • Kaposi's sarcoma and its associated herpesvirus
    • doi: 10.1038/nrc2888.
    • Mesri EA, Cesarman E, Boshoff C. Kaposi's sarcoma and its associated herpesvirus. Nat Rev Cancer 2010, 10:707-719. doi: 10.1038/nrc2888.
    • (2010) Nat Rev Cancer , vol.10 , pp. 707-719
    • Mesri, E.A.1    Cesarman, E.2    Boshoff, C.3
  • 42
    • 78049380583 scopus 로고    scopus 로고
    • Molecular biology of Kaposi's sarcoma-associated herpesvirus and related oncogenesis
    • doi: 10.1016/B978-0-12-385032-4.00003-3.
    • Cai Q, Verma SC, Lu J, Robertson ES. Molecular biology of Kaposi's sarcoma-associated herpesvirus and related oncogenesis. Adv Virus Res 2010, 78:87-142. doi: 10.1016/B978-0-12-385032-4.00003-3.
    • (2010) Adv Virus Res , vol.78 , pp. 87-142
    • Cai, Q.1    Verma, S.C.2    Lu, J.3    Robertson, E.S.4
  • 43
    • 76849087997 scopus 로고    scopus 로고
    • Kaposi sarcoma-associated herpesvirus (KSHV): molecular biology and oncogenesis
    • doi: 10.1016/j.canlet.2009.07.004.
    • Wen KW, Damania B. Kaposi sarcoma-associated herpesvirus (KSHV): molecular biology and oncogenesis. Cancer Lett 2010, 289:140-150. doi: 10.1016/j.canlet.2009.07.004.
    • (2010) Cancer Lett , vol.289 , pp. 140-150
    • Wen, K.W.1    Damania, B.2
  • 44
    • 0035108050 scopus 로고    scopus 로고
    • Transcription activation of polyadenylated nuclear RNA by RTA in human herpesvirus 8/Kaposi's sarcoma-associated herpesvirus
    • doi: 10.1128/JVI.75.7.3129-3140.2001.
    • Song MJ, Brown HJ, Wu TT, Sun R. Transcription activation of polyadenylated nuclear RNA by RTA in human herpesvirus 8/Kaposi's sarcoma-associated herpesvirus. J Virol 2001, 75:3129-3140. doi: 10.1128/JVI.75.7.3129-3140.2001.
    • (2001) J Virol , vol.75 , pp. 3129-3140
    • Song, M.J.1    Brown, H.J.2    Wu, T.T.3    Sun, R.4
  • 45
    • 0029966233 scopus 로고    scopus 로고
    • Polyadenylylated nuclear RNA encoded by Kaposi sarcoma-associated herpesvirus
    • Sun R, Lin SF, Gradoville L, Miller G. Polyadenylylated nuclear RNA encoded by Kaposi sarcoma-associated herpesvirus. Proc Natl Acad Sci USA 1996, 93:11883-11888.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11883-11888
    • Sun, R.1    Lin, S.F.2    Gradoville, L.3    Miller, G.4
  • 46
    • 0029957833 scopus 로고    scopus 로고
    • Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma
    • Zhong W, Wang H, Herndier B, Ganem D. Restricted expression of Kaposi sarcoma-associated herpesvirus (human herpesvirus 8) genes in Kaposi sarcoma. Proc Natl Acad Sci USA 1996, 93:6641-6646.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6641-6646
    • Zhong, W.1    Wang, H.2    Herndier, B.3    Ganem, D.4
  • 47
    • 84863703084 scopus 로고    scopus 로고
    • KSHV PAN RNA associates with demethylases UTX and JMJD3 to activate lytic replication through a physical interaction with the virus genome
    • doi: 10.1371/journal.ppat.1002680.t002.
    • Rossetto CC, Pari G. KSHV PAN RNA associates with demethylases UTX and JMJD3 to activate lytic replication through a physical interaction with the virus genome. PLoS Pathog 2012, 8:e1002680. doi: 10.1371/journal.ppat.1002680.t002.
    • (2012) PLoS Pathog , vol.8
    • Rossetto, C.C.1    Pari, G.2
  • 48
    • 80055064878 scopus 로고    scopus 로고
    • A viral nuclear noncoding rna binds re-localized poly(A) binding protein and is required for late KSHV gene expression
    • doi: 10.1371/journal.ppat.1002300.g009.
    • Borah S, Darricarrère N, Darnell A, Myoung J, Steitz JA. A viral nuclear noncoding rna binds re-localized poly(A) binding protein and is required for late KSHV gene expression. PLoS Pathog 2011, 7:e1002300. doi: 10.1371/journal.ppat.1002300.g009.
    • (2011) PLoS Pathog , vol.7
    • Borah, S.1    Darricarrère, N.2    Darnell, A.3    Myoung, J.4    Steitz, J.A.5
  • 49
    • 84855853263 scopus 로고    scopus 로고
    • KSHV noncoding PAN RNA interacts with virus and cellular-encoded proteins and suppresses expression of genes involved in immune modulation
    • doi: 10.1128/JVI.05886-11.
    • Rossetto CC, Pari GS. KSHV noncoding PAN RNA interacts with virus and cellular-encoded proteins and suppresses expression of genes involved in immune modulation. J Virol 2011. doi: 10.1128/JVI.05886-11.
    • (2011) J Virol
    • Rossetto, C.C.1    Pari, G.S.2
  • 50
    • 84877336707 scopus 로고    scopus 로고
    • Regulation of viral and cellular gene expression by Kaposi's sarcoma associated herpesvirus (KSHV) PAN RNA
    • doi: 10.1128/JVI.03111-12.
    • Rossetto CC, Tarrant-Elorza M, Verma S, Purushothaman P, Pari GS. Regulation of viral and cellular gene expression by Kaposi's sarcoma associated herpesvirus (KSHV) PAN RNA. J Virol 2013. doi: 10.1128/JVI.03111-12.
    • (2013) J Virol
    • Rossetto, C.C.1    Tarrant-Elorza, M.2    Verma, S.3    Purushothaman, P.4    Pari, G.S.5
  • 51
    • 33750689875 scopus 로고    scopus 로고
    • Gene control by large noncoding RNAs
    • doi: 10.1126/stke.3552006pe40.
    • Shamovsky I, Nudler E. Gene control by large noncoding RNAs. Sci STKE 2006, 2006:pe40. doi: 10.1126/stke.3552006pe40.
    • (2006) Sci STKE , vol.2006
    • Shamovsky, I.1    Nudler, E.2
  • 52
    • 84875200257 scopus 로고    scopus 로고
    • Long noncoding RNAs: cellular address codes in development and disease
    • doi: 10.1016/j.cell.2013.02.012.
    • Batista PJ, Chang HY. Long noncoding RNAs: cellular address codes in development and disease. Cell 2013, 152:1298-1307. doi: 10.1016/j.cell.2013.02.012.
    • (2013) Cell , vol.152 , pp. 1298-1307
    • Batista, P.J.1    Chang, H.Y.2
  • 53
    • 20044369601 scopus 로고    scopus 로고
    • A Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts
    • doi: 10.1038/sj.emboj.7600662.
    • Conrad NK, Steitz JA. A Kaposi's sarcoma virus RNA element that increases the nuclear abundance of intronless transcripts. EMBO J 2005, 24:1831-1841. doi: 10.1038/sj.emboj.7600662.
    • (2005) EMBO J , vol.24 , pp. 1831-1841
    • Conrad, N.K.1    Steitz, J.A.2
  • 54
    • 34547510230 scopus 로고    scopus 로고
    • Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail
    • doi: 10.1073/pnas.0704187104.
    • Conrad NK, Shu M-D, Uyhazi KE, Steitz JA. Mutational analysis of a viral RNA element that counteracts rapid RNA decay by interaction with the polyadenylate tail. Proc Natl Acad Sci USA 2007, 104:10412-10417. doi: 10.1073/pnas.0704187104.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 10412-10417
    • Conrad, N.K.1    Shu, M.-D.2    Uyhazi, K.E.3    Steitz, J.A.4
  • 55
    • 33845662140 scopus 로고    scopus 로고
    • Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element
    • doi: 10.1016/j.molcel.2006.10.029.
    • Conrad NK, Mili S, Marshall EL, Shu M-D, Steitz JA. Identification of a rapid mammalian deadenylation-dependent decay pathway and its inhibition by a viral RNA element. Mol Cell 2006, 24:943-953. doi: 10.1016/j.molcel.2006.10.029.
    • (2006) Mol Cell , vol.24 , pp. 943-953
    • Conrad, N.K.1    Mili, S.2    Marshall, E.L.3    Shu, M.-D.4    Steitz, J.A.5
  • 56
    • 51549111789 scopus 로고    scopus 로고
    • Quality control of mRNP in the nucleus
    • doi: 10.1007/s00412-008-0166-4.
    • Schmid M, Jensen TH. Quality control of mRNP in the nucleus. Chromosoma 2008, 117:419-429. doi: 10.1007/s00412-008-0166-4.
    • (2008) Chromosoma , vol.117 , pp. 419-429
    • Schmid, M.1    Jensen, T.H.2
  • 57
    • 67650492477 scopus 로고    scopus 로고
    • Mechanisms of nuclear mRNA quality control
    • Fasken MB, Corbett AH. Mechanisms of nuclear mRNA quality control. RNA Biol 2009, 6:237-241.
    • (2009) RNA Biol , vol.6 , pp. 237-241
    • Fasken, M.B.1    Corbett, A.H.2
  • 58
    • 36049041612 scopus 로고    scopus 로고
    • RNA quality control in eukaryotes
    • doi: 10.1016/j.cell.2007.10.041.
    • Doma MK, Parker R. RNA quality control in eukaryotes. Cell 2007, 131:660-668. doi: 10.1016/j.cell.2007.10.041.
    • (2007) Cell , vol.131 , pp. 660-668
    • Doma, M.K.1    Parker, R.2
  • 60
    • 0035942248 scopus 로고    scopus 로고
    • RNA tertiary interactions in the large ribosomal subunit: the A-minor motif
    • doi: 10.1073/pnas.081082398.
    • Nissen P, Ippolito JA, Ban N, Moore PB, Steitz TA. RNA tertiary interactions in the large ribosomal subunit: the A-minor motif. Proc Natl Acad Sci USA 2001, 98:4899-4903. doi: 10.1073/pnas.081082398.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4899-4903
    • Nissen, P.1    Ippolito, J.A.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 61
    • 84864295521 scopus 로고    scopus 로고
    • Conservation of a triple-helix-forming RNA stability element in noncoding and genomic RNAs of diverse viruses
    • doi: 10.1016/j.celrep.2012.05.020.
    • Tycowski KT, Shu M-D, Borah S, Shi M, Steitz JA. Conservation of a triple-helix-forming RNA stability element in noncoding and genomic RNAs of diverse viruses. CellReports 2012, 2:26-32. doi: 10.1016/j.celrep.2012.05.020.
    • (2012) CellReports , vol.2 , pp. 26-32
    • Tycowski, K.T.1    Shu, M.-D.2    Borah, S.3    Shi, M.4    Steitz, J.A.5
  • 63
    • 77449149944 scopus 로고    scopus 로고
    • Dicistroviruses
    • doi: 10.1146/annurev-ento-112408-085457.
    • Bonning BC, Miller WA. Dicistroviruses. Annu Rev Entomol 2010, 55:129-150. doi: 10.1146/annurev-ento-112408-085457.
    • (2010) Annu Rev Entomol , vol.55 , pp. 129-150
    • Bonning, B.C.1    Miller, W.A.2
  • 64
    • 84869846717 scopus 로고    scopus 로고
    • Formation of triple-helical structures by the 3'-end sequences of MALAT1 and MENβ noncoding RNAs
    • doi: 10.1073/pnas.1217338109.
    • Brown JA, Valenstein ML, Yario TA, Tycowski KT, Steitz JA. Formation of triple-helical structures by the 3'-end sequences of MALAT1 and MENβ noncoding RNAs. Proc Natl Acad Sci 2012. doi: 10.1073/pnas.1217338109.
    • (2012) Proc Natl Acad Sci
    • Brown, J.A.1    Valenstein, M.L.2    Yario, T.A.3    Tycowski, K.T.4    Steitz, J.A.5
  • 65
    • 0344429906 scopus 로고    scopus 로고
    • MALAT-1, a novel noncoding RNA, and thymosin beta4 predict metastasis and survival in early-stage non-small cell lung cancer
    • doi: 10.1038/sj.onc.1206928.
    • Ji P, Diederichs S, Wang W, Böing S, Metzger R, Schneider PM, Tidow N, Brandt B, Buerger H, Bulk E, et al. MALAT-1, a novel noncoding RNA, and thymosin beta4 predict metastasis and survival in early-stage non-small cell lung cancer. Oncogene 2003, 22:8031-8041. doi: 10.1038/sj.onc.1206928.
    • (2003) Oncogene , vol.22 , pp. 8031-8041
    • Ji, P.1    Diederichs, S.2    Wang, W.3    Böing, S.4    Metzger, R.5    Schneider, P.M.6    Tidow, N.7    Brandt, B.8    Buerger, H.9    Bulk, E.10
  • 66
    • 84879837310 scopus 로고    scopus 로고
    • MALAT1-a paradigm for long noncoding RNA function in cancer
    • doi: 10.1007/s00109-013-1028-y.
    • Gutschner T, Hämmerle M, Diederichs S. MALAT1-a paradigm for long noncoding RNA function in cancer. J Mol Med 2013. doi: 10.1007/s00109-013-1028-y.
    • (2013) J Mol Med
    • Gutschner, T.1    Hämmerle, M.2    Diederichs, S.3
  • 67
    • 77956927823 scopus 로고    scopus 로고
    • The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation
    • doi: 10.1016/j.molcel.2010.08.011.
    • Tripathi V, Ellis JD, Shen Z, Song DY, Pan Q, Watt AT, Freier SM, Bennett CF, Sharma A, Bubulya PA, et al. The nuclear-retained noncoding RNA MALAT1 regulates alternative splicing by modulating SR splicing factor phosphorylation. Mol Cell 2010, 39:1-14. doi: 10.1016/j.molcel.2010.08.011.
    • (2010) Mol Cell , vol.39 , pp. 1-14
    • Tripathi, V.1    Ellis, J.D.2    Shen, Z.3    Song, D.Y.4    Pan, Q.5    Watt, A.T.6    Freier, S.M.7    Bennett, C.F.8    Sharma, A.9    Bubulya, P.A.10
  • 68
    • 84876003231 scopus 로고    scopus 로고
    • Long noncoding RNA MALAT1 controls cell cycle progression by regulating the expression of oncogenic transcription factor B-MYB
    • doi: 10.1371/journal.pgen.1003368.
    • Tripathi V, Shen Z, Chakraborty A, Giri S, Freier SM, Wu X, Zhang Y, Gorospe M, Prasanth SG, Lal A, et al. Long noncoding RNA MALAT1 controls cell cycle progression by regulating the expression of oncogenic transcription factor B-MYB. PLoS Genet 2013, 9:e1003368. doi: 10.1371/journal.pgen.1003368.
    • (2013) PLoS Genet , vol.9
    • Tripathi, V.1    Shen, Z.2    Chakraborty, A.3    Giri, S.4    Freier, S.M.5    Wu, X.6    Zhang, Y.7    Gorospe, M.8    Prasanth, S.G.9    Lal, A.10
  • 69
    • 81055140863 scopus 로고    scopus 로고
    • ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs
    • doi: 10.1016/j.cell.2011.08.054.
    • Yang L, Lin C, Liu W, Zhang J, Ohgi KA, Grinstein JD, Dorrestein PC, Rosenfeld MG. ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs. Cell 2011, 147:773-788. doi: 10.1016/j.cell.2011.08.054.
    • (2011) Cell , vol.147 , pp. 773-788
    • Yang, L.1    Lin, C.2    Liu, W.3    Zhang, J.4    Ohgi, K.A.5    Grinstein, J.D.6    Dorrestein, P.C.7    Rosenfeld, M.G.8
  • 71
    • 84864315112 scopus 로고    scopus 로고
    • The lncRNA Malat1 is dispensable for mouse development but its transcription plays a cis-regulatory role in the adult
    • doi: 10.1016/j.celrep.2012.06.003.
    • Zhang B, Arun G, Mao YS, Lazar Z, Hung G, Bhattacharjee G, Xiao X, Booth CJ, Wu J, Zhang C, et al. The lncRNA Malat1 is dispensable for mouse development but its transcription plays a cis-regulatory role in the adult. CellReports 2012, 2:111-123. doi: 10.1016/j.celrep.2012.06.003.
    • (2012) CellReports , vol.2 , pp. 111-123
    • Zhang, B.1    Arun, G.2    Mao, Y.S.3    Lazar, Z.4    Hung, G.5    Bhattacharjee, G.6    Xiao, X.7    Booth, C.J.8    Wu, J.9    Zhang, C.10
  • 72
    • 84864033675 scopus 로고    scopus 로고
    • Malat1 is not an essential component of nuclear speckles in mice
    • doi: 10.1261/rna.033217.112.
    • Nakagawa S, Ip JY, Shioi G, Tripathi V, Zong X, Hirose T, Prasanth KV. Malat1 is not an essential component of nuclear speckles in mice. RNA 2012, 18:1487-1499. doi: 10.1261/rna.033217.112.
    • (2012) RNA , vol.18 , pp. 1487-1499
    • Nakagawa, S.1    Ip, J.Y.2    Shioi, G.3    Tripathi, V.4    Zong, X.5    Hirose, T.6    Prasanth, K.V.7
  • 73
    • 56349113455 scopus 로고    scopus 로고
    • 3' end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA
    • doi: 10.1016/j.cell.2008.10.012.
    • Wilusz JE, Freier SM, Spector DL. 3' end processing of a long nuclear-retained noncoding RNA yields a tRNA-like cytoplasmic RNA. Cell 2008, 135:919-932. doi: 10.1016/j.cell.2008.10.012.
    • (2008) Cell , vol.135 , pp. 919-932
    • Wilusz, J.E.1    Freier, S.M.2    Spector, D.L.3
  • 74
    • 75149119376 scopus 로고    scopus 로고
    • An unexpected ending: noncanonical 3' end processing mechanisms
    • doi: 10.1261/rna.1907510.
    • Wilusz JE, Spector DL. An unexpected ending: noncanonical 3' end processing mechanisms. RNA 2010, 16:259-266. doi: 10.1261/rna.1907510.
    • (2010) RNA , vol.16 , pp. 259-266
    • Wilusz, J.E.1    Spector, D.L.2
  • 76
    • 38149023239 scopus 로고    scopus 로고
    • Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'
    • doi: 10.1101/gad.1622708.
    • Mullen TE, Marzluff WF. Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'. Genes Dev 2008, 22:50-65. doi: 10.1101/gad.1622708.
    • (2008) Genes Dev , vol.22 , pp. 50-65
    • Mullen, T.E.1    Marzluff, W.F.2
  • 77
    • 84877823397 scopus 로고    scopus 로고
    • RNA decay via 3' uridylation
    • doi: 10.1016/j.bbagrm.2013.01.009.
    • Scott DD, Norbury CJ. RNA decay via 3' uridylation. Biochim Biophys Acta 2013. doi: 10.1016/j.bbagrm.2013.01.009.
    • (2013) Biochim Biophys Acta
    • Scott, D.D.1    Norbury, C.J.2
  • 78
    • 23944470910 scopus 로고    scopus 로고
    • RNA turnover: unexpected consequences of being tailed
    • doi: 10.1016/j.cub.2005.08.002.
    • Anderson JT. RNA turnover: unexpected consequences of being tailed. Curr Biol 2005, 15:R635-8. doi: 10.1016/j.cub.2005.08.002.
    • (2005) Curr Biol , vol.15
    • Anderson, J.T.1
  • 79
    • 2442482777 scopus 로고    scopus 로고
    • Structure and function of poly(A) binding proteins
    • doi: 10.1016/j.bbaexp.2004.03.008.
    • Kühn U, Wahle E. Structure and function of poly(A) binding proteins. Biochim Biophys Acta 2004, 1678(2-3):67-84. doi: 10.1016/j.bbaexp.2004.03.008.
    • (2004) Biochim Biophys Acta , vol.1678 , Issue.2-3 , pp. 67-84
    • Kühn, U.1    Wahle, E.2
  • 80
    • 34249021370 scopus 로고    scopus 로고
    • Peptides encoded by short ORFs control development and define a new eukaryotic gene family
    • doi: 10.1371/journal.pbio.0050106.
    • Galindo MI, Pueyo JI, Fouix S, Bishop SA, Couso JP. Peptides encoded by short ORFs control development and define a new eukaryotic gene family. PLoS Biol 2007, 5:e106. doi: 10.1371/journal.pbio.0050106.
    • (2007) PLoS Biol , vol.5
    • Galindo, M.I.1    Pueyo, J.I.2    Fouix, S.3    Bishop, S.A.4    Couso, J.P.5
  • 81
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • doi: 10.1016/j.cell.2011.10.002.
    • Ingolia NT, Lareau LF, Weissman JS. Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes. Cell 2011, 147:789-802. doi: 10.1016/j.cell.2011.10.002.
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 82
    • 77952003905 scopus 로고    scopus 로고
    • Making sense of antisense: seemingly noncoding RNAs antisense to the master regulator of Kaposi's sarcoma-associated herpesvirus lytic replication do not regulate that transcript but serve as mRNAs encoding small peptides
    • doi: 10.1128/JVI.02705-09.
    • Xu Y, Ganem D. Making sense of antisense: seemingly noncoding RNAs antisense to the master regulator of Kaposi's sarcoma-associated herpesvirus lytic replication do not regulate that transcript but serve as mRNAs encoding small peptides. J Virol 2010, 84:5465-5475. doi: 10.1128/JVI.02705-09.
    • (2010) J Virol , vol.84 , pp. 5465-5475
    • Xu, Y.1    Ganem, D.2
  • 83
    • 75649116868 scopus 로고    scopus 로고
    • A structural analysis of the group II intron active site and implications for the spliceosome
    • doi: 10.1261/rna.1791310.
    • Keating KS, Toor N, Perlman PS, Pyle AM. A structural analysis of the group II intron active site and implications for the spliceosome. RNA 2009, 16:1-9. doi: 10.1261/rna.1791310.
    • (2009) RNA , vol.16 , pp. 1-9
    • Keating, K.S.1    Toor, N.2    Perlman, P.S.3    Pyle, A.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.