메뉴 건너뛰기




Volumn 589, Issue 14, 2015, Pages 1653-1668

G-quadruplexes: Emerging roles in neurodegenerative diseases and the non-coding transcriptome

Author keywords

G quadruplex; Neurodegenerative diseases; Non coding RNA

Indexed keywords

BINDING PROTEIN; FMRP PROTEIN; GUANINE QUADRUPLEX; MESSENGER RNA; PIWI INTERACTING RNA; PROTEIN ANTIBODY; TRANSCRIPTOME; UNCLASSIFIED DRUG; UNTRANSLATED RNA;

EID: 84930271972     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2015.05.003     Document Type: Review
Times cited : (174)

References (180)
  • 3
    • 77955834769 scopus 로고    scopus 로고
    • Structure, location and interactions of G-quadruplexes
    • J.L. Huppert Structure, location and interactions of G-quadruplexes FEBS J. 277 2010 3452 3458
    • (2010) FEBS J. , vol.277 , pp. 3452-3458
    • Huppert, J.L.1
  • 5
    • 0016862691 scopus 로고
    • Letter: Self-assembled 5′-guanosine monophosphate. Nuclear magnetic resonance evidence for a regular, ordered structure and slow chemical exchange
    • T.J. Pinnavaia, H.T. Miles, and E.D. Becker Letter: self-assembled 5′-guanosine monophosphate. Nuclear magnetic resonance evidence for a regular, ordered structure and slow chemical exchange J. Am. Chem. Soc. 97 1975 7198 7200
    • (1975) J. Am. Chem. Soc. , vol.97 , pp. 7198-7200
    • Pinnavaia, T.J.1    Miles, H.T.2    Becker, E.D.3
  • 6
    • 0031972920 scopus 로고    scopus 로고
    • Helix-specific interactions induce condensation of guanosine four-stranded helices in concentrated salt solutions
    • L.M.P. Saturni Helix-specific interactions induce condensation of guanosine four-stranded helices in concentrated salt solutions Biophys. J. 74 1998 430 435
    • (1998) Biophys. J. , vol.74 , pp. 430-435
    • Saturni, L.M.P.1
  • 7
    • 0000334398 scopus 로고    scopus 로고
    • Comprehensive supramolecular chemistry
    • J.P. Sauvage, M.W. Hossieni, Elsevier
    • G. G., and A. Garbesi Comprehensive supramolecular chemistry J.P. Sauvage, M.W. Hossieni, Comprehensive Supramolecular Chemistry 1996 Elsevier 483
    • (1996) Comprehensive Supramolecular Chemistry , pp. 483
    • G, G.1    Garbesi, A.2
  • 8
    • 0023788886 scopus 로고
    • Formation of parallel four-stranded complexes by guanine-rich motifs in DNA and its implications for meiosis
    • D. Sen, and W. Gilbert Formation of parallel four-stranded complexes by guanine-rich motifs in DNA and its implications for meiosis Nature 334 1988 364 366
    • (1988) Nature , vol.334 , pp. 364-366
    • Sen, D.1    Gilbert, W.2
  • 9
    • 0024843757 scopus 로고
    • Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops
    • W.I. Sundquist, and A. Klug Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops Nature 342 1989 825 829
    • (1989) Nature , vol.342 , pp. 825-829
    • Sundquist, W.I.1    Klug, A.2
  • 10
    • 0026687030 scopus 로고
    • Guanine residues in d(T2AG3) and d(T2G4) form parallel-stranded potassium cation stabilized G-quadruplexes with anti glycosidic torsion angles in solution
    • Y. Wang, and D.J. Patel Guanine residues in d(T2AG3) and d(T2G4) form parallel-stranded potassium cation stabilized G-quadruplexes with anti glycosidic torsion angles in solution Biochemistry 31 1992 8112 8119
    • (1992) Biochemistry , vol.31 , pp. 8112-8119
    • Wang, Y.1    Patel, D.J.2
  • 11
    • 0036290781 scopus 로고    scopus 로고
    • Crystal structure of the potassium form of an Oxytricha nova G-quadruplex
    • S. Haider, G.N. Parkinson, and S. Neidle Crystal structure of the potassium form of an Oxytricha nova G-quadruplex J. Mol. Biol. 320 2002 189 200
    • (2002) J. Mol. Biol. , vol.320 , pp. 189-200
    • Haider, S.1    Parkinson, G.N.2    Neidle, S.3
  • 12
    • 0037142071 scopus 로고    scopus 로고
    • Crystal structure of parallel quadruplexes from human telomeric DNA
    • G.N. Parkinson, M.P.H. Lee, and S. Neidle Crystal structure of parallel quadruplexes from human telomeric DNA Nature 417 2002 876 880
    • (2002) Nature , vol.417 , pp. 876-880
    • Parkinson, G.N.1    Lee, M.P.H.2    Neidle, S.3
  • 13
    • 66549124907 scopus 로고    scopus 로고
    • The structures of quadruplex nucleic acids and their drug complexes
    • S. Neidle The structures of quadruplex nucleic acids and their drug complexes Curr. Opin. Struct. Biol. 19 2009 239 250
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 239-250
    • Neidle, S.1
  • 15
    • 0035923718 scopus 로고    scopus 로고
    • X-ray analysis of an RNA tetraplex (UGGGGU)(4) with divalent Sr(2+) ions at subatomic resolution (0.61 A)
    • J. Deng, Y. Xiong, and M. Sundaralingam X-ray analysis of an RNA tetraplex (UGGGGU)(4) with divalent Sr(2+) ions at subatomic resolution (0.61 A) Proc. Natl. Acad. Sci. U.S.A. 98 2001 13665 13670
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 13665-13670
    • Deng, J.1    Xiong, Y.2    Sundaralingam, M.3
  • 16
    • 77956539976 scopus 로고    scopus 로고
    • A crystallographic and modelling study of a human telomeric RNA (TERRA) quadruplex
    • G.W. Collie, S.M. Haider, S. Neidle, and G.N. Parkinson A crystallographic and modelling study of a human telomeric RNA (TERRA) quadruplex Nucleic Acids Res. 38 2010 5569 5580
    • (2010) Nucleic Acids Res. , vol.38 , pp. 5569-5580
    • Collie, G.W.1    Haider, S.M.2    Neidle, S.3    Parkinson, G.N.4
  • 17
    • 67749143935 scopus 로고    scopus 로고
    • Structure of propeller-type parallel-stranded RNA G-quadruplexes, formed by human telomeric RNA sequences in K+ solution
    • H. Martadinata, and A.T. Phan Structure of propeller-type parallel-stranded RNA G-quadruplexes, formed by human telomeric RNA sequences in K+ solution J. Am. Chem. Soc. 131 2009 2570 2578
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 2570-2578
    • Martadinata, H.1    Phan, A.T.2
  • 18
    • 0029585993 scopus 로고
    • Solution structure of a DNA quadruplex containing the fragile X syndrome triplet repeat
    • A. Kettani, R.A. Kumar, and D.J. Patel Solution structure of a DNA quadruplex containing the fragile X syndrome triplet repeat J. Mol. Biol. 254 1995 638 656
    • (1995) J. Mol. Biol. , vol.254 , pp. 638-656
    • Kettani, A.1    Kumar, R.A.2    Patel, D.J.3
  • 19
    • 84903795949 scopus 로고    scopus 로고
    • A double-edged sword: R loops as threats to genome integrity and powerful regulators of gene expression
    • K. Skourti-Stathaki, and N.J. Proudfoot A double-edged sword: R loops as threats to genome integrity and powerful regulators of gene expression Genes Dev. 28 2014 1384 1396
    • (2014) Genes Dev. , vol.28 , pp. 1384-1396
    • Skourti-Stathaki, K.1    Proudfoot, N.J.2
  • 20
    • 84890411617 scopus 로고    scopus 로고
    • Bioinformatic analysis reveals an evolutional selection for DNA:RNA hybrid G-quadruplex structures as putative transcription regulatory elements in warm-blooded animals
    • S. Xiao, J.-Y. Zhang, K.-W. Zheng, Y.-H. Hao, and Z. Tan Bioinformatic analysis reveals an evolutional selection for DNA:RNA hybrid G-quadruplex structures as putative transcription regulatory elements in warm-blooded animals Nucleic Acids Res. 41 2013 10379 10390
    • (2013) Nucleic Acids Res. , vol.41 , pp. 10379-10390
    • Xiao, S.1    Zhang, J.-Y.2    Zheng, K.-W.3    Hao, Y.-H.4    Tan, Z.5
  • 21
    • 84878526299 scopus 로고    scopus 로고
    • Co-transcriptional formation of DNA:RNA hybrid G-quadruplex and potential function as constitutional cis element for transcription control
    • K. Zheng, S. Xiao, J. Liu, J. Zhang, Y. Hao, and Z. Tan Co-transcriptional formation of DNA:RNA hybrid G-quadruplex and potential function as constitutional cis element for transcription control Nucleic Acids Res. 41 2013 5533 5541
    • (2013) Nucleic Acids Res. , vol.41 , pp. 5533-5541
    • Zheng, K.1    Xiao, S.2    Liu, J.3    Zhang, J.4    Hao, Y.5    Tan, Z.6
  • 22
    • 33645527783 scopus 로고    scopus 로고
    • Downstream boundary of chromosomal R-loops at murine switch regions: Implications for the mechanism of class switch recombination
    • F.-T. Huang, K. Yu, C.-L. Hsieh, and M.R. Lieber Downstream boundary of chromosomal R-loops at murine switch regions: implications for the mechanism of class switch recombination Proc. Natl. Acad. Sci. U.S.A. 103 2006 5030 5035
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5030-5035
    • Huang, F.-T.1    Yu, K.2    Hsieh, C.-L.3    Lieber, M.R.4
  • 23
    • 84869006723 scopus 로고    scopus 로고
    • A hybrid G-quadruplex structure formed between RNA and DNA explains the extraordinary stability of the mitochondrial R-loop
    • P.H. Wanrooij, J.P. Uhler, Y. Shi, F. Westerlund, M. Falkenberg, and C.M. Gustafsson A hybrid G-quadruplex structure formed between RNA and DNA explains the extraordinary stability of the mitochondrial R-loop Nucleic Acids Res. 40 2012 10334 10344
    • (2012) Nucleic Acids Res. , vol.40 , pp. 10334-10344
    • Wanrooij, P.H.1    Uhler, J.P.2    Shi, Y.3    Westerlund, F.4    Falkenberg, M.5    Gustafsson, C.M.6
  • 24
    • 84923546301 scopus 로고    scopus 로고
    • Emerging role of RNA·DNA hybrids in C9orf72-linked neurodegeneration
    • J. Wang, A.R. Haeusler, and E.A.J. Simko Emerging role of RNA·DNA hybrids in C9orf72-linked neurodegeneration Cell Cycle 14 2015 526 532
    • (2015) Cell Cycle , vol.14 , pp. 526-532
    • Wang, J.1    Haeusler, A.R.2    Simko, E.A.J.3
  • 26
    • 84901346090 scopus 로고    scopus 로고
    • Transcription-associated R-loop formation across the human FMR1 CGG-repeat region
    • E.W. Loomis, L.A. Sanz, F. Chédin, and P.J. Hagerman Transcription-associated R-loop formation across the human FMR1 CGG-repeat region PLoS Genet. 10 2014 e1004294
    • (2014) PLoS Genet. , vol.10 , pp. e1004294
    • Loomis, E.W.1    Sanz, L.A.2    Chédin, F.3    Hagerman, P.J.4
  • 27
    • 84901626668 scopus 로고    scopus 로고
    • R-loops associated with triplet repeat expansions promote gene silencing in Friedreich ataxia and fragile X syndrome
    • M. Groh, M.M.P. Lufino, R. Wade-Martins, and N. Gromak R-loops associated with triplet repeat expansions promote gene silencing in Friedreich ataxia and fragile X syndrome PLoS Genet. 10 2014 e1004318
    • (2014) PLoS Genet. , vol.10 , pp. e1004318
    • Groh, M.1    Lufino, M.M.P.2    Wade-Martins, R.3    Gromak, N.4
  • 28
    • 0036699095 scopus 로고    scopus 로고
    • Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA
    • I. Cheung, M. Schertzer, A. Rose, and P.M. Lansdorp Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA Nat. Genet. 31 2002 405 409
    • (2002) Nat. Genet. , vol.31 , pp. 405-409
    • Cheung, I.1    Schertzer, M.2    Rose, A.3    Lansdorp, P.M.4
  • 30
    • 79957556530 scopus 로고    scopus 로고
    • DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase
    • K. Paeschke, J.A. Capra, and V.A. Zakian DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase Cell 145 2011 678 691
    • (2011) Cell , vol.145 , pp. 678-691
    • Paeschke, K.1    Capra, J.A.2    Zakian, V.A.3
  • 32
    • 84899887504 scopus 로고    scopus 로고
    • Periodic DNA patrolling underlies diverse functions of Pif1 on R-loops and G-rich DNA
    • R. Zhou, J. Zhang, M.L. Bochman, V.A. Zakian, and T. Ha Periodic DNA patrolling underlies diverse functions of Pif1 on R-loops and G-rich DNA Elife 3 2014 e02190
    • (2014) Elife , vol.3 , pp. e02190
    • Zhou, R.1    Zhang, J.2    Bochman, M.L.3    Zakian, V.A.4    Ha, T.5
  • 33
    • 33644664075 scopus 로고    scopus 로고
    • The DEXH protein product of the DHX36 gene is the major source of tetramolecular quadruplex G4-DNA resolving activity in HeLa cell lysates
    • J.P. Vaughn, S.D. Creacy, E.D. Routh, C. Joyner-Butt, G.S. Jenkins, S. Pauli, Y. Nagamine, and S.A. Akman The DEXH protein product of the DHX36 gene is the major source of tetramolecular quadruplex G4-DNA resolving activity in HeLa cell lysates J. Biol. Chem. 280 2005 38117 38120
    • (2005) J. Biol. Chem. , vol.280 , pp. 38117-38120
    • Vaughn, J.P.1    Creacy, S.D.2    Routh, E.D.3    Joyner-Butt, C.4    Jenkins, G.S.5    Pauli, S.6    Nagamine, Y.7    Akman, S.A.8
  • 34
    • 58049200140 scopus 로고    scopus 로고
    • G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high affinity and is the major source of tetramolecular quadruplex G4-DNA and G4-RNA resolving activity in HeLa cell lysates
    • S.D. Creacy, E.D. Routh, F. Iwamoto, Y. Nagamine, S.A. Akman, and J.P. Vaughn G4 resolvase 1 binds both DNA and RNA tetramolecular quadruplex with high affinity and is the major source of tetramolecular quadruplex G4-DNA and G4-RNA resolving activity in HeLa cell lysates J. Biol. Chem. 283 2008 34626 34634
    • (2008) J. Biol. Chem. , vol.283 , pp. 34626-34634
    • Creacy, S.D.1    Routh, E.D.2    Iwamoto, F.3    Nagamine, Y.4    Akman, S.A.5    Vaughn, J.P.6
  • 36
    • 84897029094 scopus 로고    scopus 로고
    • G quadruplexes are genomewide targets of transcriptional helicases XPB and XPD
    • L.T. Gray, A.C. Vallur, J. Eddy, and N. Maizels G quadruplexes are genomewide targets of transcriptional helicases XPB and XPD Nat. Chem. Biol. 10 2014 313 318
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 313-318
    • Gray, L.T.1    Vallur, A.C.2    Eddy, J.3    Maizels, N.4
  • 37
    • 79957813857 scopus 로고    scopus 로고
    • Human DHX9 helicase preferentially unwinds RNA-containing displacement loops (R-loops) and G-quadruplexes
    • P. Chakraborty, and F. Grosse Human DHX9 helicase preferentially unwinds RNA-containing displacement loops (R-loops) and G-quadruplexes DNA Repair (Amst.) 10 2011 654 665
    • (2011) DNA Repair (Amst.) , vol.10 , pp. 654-665
    • Chakraborty, P.1    Grosse, F.2
  • 39
  • 40
    • 0035902465 scopus 로고    scopus 로고
    • In vitro generated antibodies specific for telomeric guanine-quadruplex DNA react with Stylonychia lemnae macronuclei
    • C. Schaffitzel, I. Berger, J. Postberg, J. Hanes, H.J. Lipps, and A. Plückthun In vitro generated antibodies specific for telomeric guanine-quadruplex DNA react with Stylonychia lemnae macronuclei Proc. Natl. Acad. Sci. U.S.A. 98 2001 8572 8577
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8572-8577
    • Schaffitzel, C.1    Berger, I.2    Postberg, J.3    Hanes, J.4    Lipps, H.J.5    Plückthun, A.6
  • 41
    • 77449156015 scopus 로고    scopus 로고
    • Probing telomeric G-quadruplex DNA structures in cells with in vitro generated single-chain antibody fragments
    • C. Schaffitzel, J. Postberg, K. Paeschke, and H.J. Lipps Probing telomeric G-quadruplex DNA structures in cells with in vitro generated single-chain antibody fragments Methods Mol. Biol. 608 2010 159 181
    • (2010) Methods Mol. Biol. , vol.608 , pp. 159-181
    • Schaffitzel, C.1    Postberg, J.2    Paeschke, K.3    Lipps, H.J.4
  • 43
    • 84875464903 scopus 로고    scopus 로고
    • Quantitative visualization of DNA G-quadruplex structures in human cells
    • G. Biffi, D. Tannahill, J. McCafferty, and S. Balasubramanian Quantitative visualization of DNA G-quadruplex structures in human cells Nat. Chem. 5 2013 182 186
    • (2013) Nat. Chem. , vol.5 , pp. 182-186
    • Biffi, G.1    Tannahill, D.2    McCafferty, J.3    Balasubramanian, S.4
  • 44
    • 84890958553 scopus 로고    scopus 로고
    • Visualization and selective chemical targeting of RNA G-quadruplex structures in the cytoplasm of human cells
    • G. Biffi, M. Di Antonio, D. Tannahill, and S. Balasubramanian Visualization and selective chemical targeting of RNA G-quadruplex structures in the cytoplasm of human cells Nat. Chem. 6 2014 75 80
    • (2014) Nat. Chem. , vol.6 , pp. 75-80
    • Biffi, G.1    Di Antonio, M.2    Tannahill, D.3    Balasubramanian, S.4
  • 45
    • 73349110442 scopus 로고    scopus 로고
    • Genome-wide analysis of a G-quadruplex-specific single-chain antibody that regulates gene expression
    • H. Fernando, S. Sewitz, J. Darot, S. Tavaré, J.L. Huppert, and S. Balasubramanian Genome-wide analysis of a G-quadruplex-specific single-chain antibody that regulates gene expression Nucleic Acids Res. 37 2009 6716 6722
    • (2009) Nucleic Acids Res. , vol.37 , pp. 6716-6722
    • Fernando, H.1    Sewitz, S.2    Darot, J.3    Tavaré, S.4    Huppert, J.L.5    Balasubramanian, S.6
  • 47
    • 33748519569 scopus 로고    scopus 로고
    • Gene function correlates with potential for G4 DNA formation in the human genome
    • J. Eddy, and N. Maizels Gene function correlates with potential for G4 DNA formation in the human genome Nucleic Acids Res. 34 2006 3887 3896
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3887-3896
    • Eddy, J.1    Maizels, N.2
  • 48
    • 20144369806 scopus 로고    scopus 로고
    • Highly prevalent putative quadruplex sequence motifs in human DNA
    • A.K. Todd, M. Johnston, and S. Neidle Highly prevalent putative quadruplex sequence motifs in human DNA Nucleic Acids Res. 33 2005 2901 2907
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2901-2907
    • Todd, A.K.1    Johnston, M.2    Neidle, S.3
  • 49
    • 20144364292 scopus 로고    scopus 로고
    • Prevalence of quadruplexes in the human genome
    • J.L. Huppert, and S. Balasubramanian Prevalence of quadruplexes in the human genome Nucleic Acids Res. 33 2005 2908 2916
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2908-2916
    • Huppert, J.L.1    Balasubramanian, S.2
  • 51
    • 84871801926 scopus 로고    scopus 로고
    • C9orf72 hexanucleotide repeat associated with amyotrophic lateral sclerosis and frontotemporal dementia forms RNA G-quadruplexes
    • P. Fratta, S. Mizielinska, A.J. Nicoll, M. Zloh, E.M.C. Fisher, G. Parkinson, and A.M. Isaacs C9orf72 hexanucleotide repeat associated with amyotrophic lateral sclerosis and frontotemporal dementia forms RNA G-quadruplexes Sci. Rep. 2 2012 1016
    • (2012) Sci. Rep. , vol.2 , pp. 1016
    • Fratta, P.1    Mizielinska, S.2    Nicoll, A.J.3    Zloh, M.4    Fisher, E.M.C.5    Parkinson, G.6    Isaacs, A.M.7
  • 53
    • 84922813565 scopus 로고    scopus 로고
    • Characterization of DNA G-quadruplex species forming from C9ORF72 G4C2-expanded repeats associated with amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • P. Šket, J. Pohleven, A. Kovanda, M. Štalekar, V. Župunski, M. Zalar, J. Plavec, and B. Rogelj Characterization of DNA G-quadruplex species forming from C9ORF72 G4C2-expanded repeats associated with amyotrophic lateral sclerosis and frontotemporal lobar degeneration Neurobiol. Aging 36 2015 1091 1096
    • (2015) Neurobiol. Aging , vol.36 , pp. 1091-1096
    • Šket, P.1    Pohleven, J.2    Kovanda, A.3    Štalekar, M.4    Župunski, V.5    Zalar, M.6    Plavec, J.7    Rogelj, B.8
  • 54
    • 84875981640 scopus 로고    scopus 로고
    • The disease-associated r(GGGGCC)n repeat from the C9orf72 gene forms tract length-dependent uni- and multimolecular RNA G-quadruplex structures
    • K. Reddy, B. Zamiri, S.Y.R. Stanley, R.B. Macgregor, and C.E. Pearson The disease-associated r(GGGGCC)n repeat from the C9orf72 gene forms tract length-dependent uni- and multimolecular RNA G-quadruplex structures J. Biol. Chem. 288 2013 9860 9866
    • (2013) J. Biol. Chem. , vol.288 , pp. 9860-9866
    • Reddy, K.1    Zamiri, B.2    Stanley, S.Y.R.3    MacGregor, R.B.4    Pearson, C.E.5
  • 60
    • 84856879093 scopus 로고    scopus 로고
    • Molecular mechanisms of fragile X syndrome: A twenty-year perspective
    • M.R. Santoro, S.M. Bray, and S.T. Warren Molecular mechanisms of fragile X syndrome: a twenty-year perspective Annu. Rev. Pathol. 7 2012 219 245
    • (2012) Annu. Rev. Pathol. , vol.7 , pp. 219-245
    • Santoro, M.R.1    Bray, S.M.2    Warren, S.T.3
  • 61
    • 0028362201 scopus 로고
    • The fragile X syndrome d(CGG)n nucleotide repeats form a stable tetrahelical structure
    • M. Fry, and L.A. Loeb The fragile X syndrome d(CGG)n nucleotide repeats form a stable tetrahelical structure Proc. Natl. Acad. Sci. U.S.A. 91 1994 4950 4954
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 4950-4954
    • Fry, M.1    Loeb, L.A.2
  • 62
    • 0028874391 scopus 로고
    • CGG repeats associated with DNA instability and chromosome fragility form structures that block DNA synthesis in vitro
    • K. Usdin, and K.J. Woodford CGG repeats associated with DNA instability and chromosome fragility form structures that block DNA synthesis in vitro Nucleic Acids Res. 23 1995 4202 4209
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4202-4209
    • Usdin, K.1    Woodford, K.J.2
  • 64
    • 80051549115 scopus 로고    scopus 로고
    • Expansion of intronic GGCCTG hexanucleotide repeat in NOP56 causes SCA36, a type of spinocerebellar ataxia accompanied by motor neuron involvement
    • H. Kobayashi, K. Abe, T. Matsuura, Y. Ikeda, T. Hitomi, Y. Akechi, T. Habu, W. Liu, H. Okuda, and A. Koizumi Expansion of intronic GGCCTG hexanucleotide repeat in NOP56 causes SCA36, a type of spinocerebellar ataxia accompanied by motor neuron involvement Am. J. Hum. Genet. 89 2011 121 130
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 121-130
    • Kobayashi, H.1    Abe, K.2    Matsuura, T.3    Ikeda, Y.4    Hitomi, T.5    Akechi, Y.6    Habu, T.7    Liu, W.8    Okuda, H.9    Koizumi, A.10
  • 69
    • 0032427904 scopus 로고    scopus 로고
    • Neurological illness in transgenic mice expressing a prion protein with an insertional mutation
    • R. Chiesa, P. Piccardo, B. Ghetti, and D.A. Harris Neurological illness in transgenic mice expressing a prion protein with an insertional mutation Neuron 21 1998 1339 1351
    • (1998) Neuron , vol.21 , pp. 1339-1351
    • Chiesa, R.1    Piccardo, P.2    Ghetti, B.3    Harris, D.A.4
  • 72
    • 80051713296 scopus 로고    scopus 로고
    • Angiogenin-induced tRNA fragments inhibit translation initiation
    • P. Ivanov, M.M. Emara, J. Villen, S.P. Gygi, and P. Anderson Angiogenin-induced tRNA fragments inhibit translation initiation Mol. Cell 43 2011 613 623
    • (2011) Mol. Cell , vol.43 , pp. 613-623
    • Ivanov, P.1    Emara, M.M.2    Villen, J.3    Gygi, S.P.4    Anderson, P.5
  • 73
    • 84919934354 scopus 로고    scopus 로고
    • G-quadruplex structures contribute to the neuroprotective effects of angiogenin-induced tRNA fragments
    • P. Ivanov, E. O'Day, M.M. Emara, G. Wagner, J. Lieberman, and P. Anderson G-quadruplex structures contribute to the neuroprotective effects of angiogenin-induced tRNA fragments Proc. Natl. Acad. Sci. U.S.A. 111 2014 18201 18206
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 18201-18206
    • Ivanov, P.1    O'Day, E.2    Emara, M.M.3    Wagner, G.4    Lieberman, J.5    Anderson, P.6
  • 74
    • 84881490873 scopus 로고    scopus 로고
    • Converging mechanisms in ALS and FTD: Disrupted RNA and protein homeostasis
    • S.-C. Ling, M. Polymenidou, and D.W. Cleveland Converging mechanisms in ALS and FTD: disrupted RNA and protein homeostasis Neuron 79 2013 416 438
    • (2013) Neuron , vol.79 , pp. 416-438
    • Ling, S.-C.1    Polymenidou, M.2    Cleveland, D.W.3
  • 75
    • 84908161213 scopus 로고    scopus 로고
    • Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS
    • J. Bennion Callister, and S.M. Pickering-Brown Pathogenesis/genetics of frontotemporal dementia and how it relates to ALS Exp. Neurol. 262 Pt B 2014 84 90
    • (2014) Exp. Neurol. , vol.262 , pp. 84-90
    • Bennion Callister, J.1    Pickering-Brown, S.M.2
  • 81
    • 84862229118 scopus 로고    scopus 로고
    • 5′-UTR RNA G-quadruplexes: Translation regulation and targeting
    • A. Bugaut, and S. Balasubramanian 5′-UTR RNA G-quadruplexes: translation regulation and targeting Nucleic Acids Res. 40 2012 4727 4741
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4727-4741
    • Bugaut, A.1    Balasubramanian, S.2
  • 89
    • 84903819307 scopus 로고    scopus 로고
    • Unconventional features of C9ORF72 expanded repeat in amyotrophic lateral sclerosis and frontotemporal lobar degeneration
    • S. Vatovec, A. Kovanda, and B. Rogelj Unconventional features of C9ORF72 expanded repeat in amyotrophic lateral sclerosis and frontotemporal lobar degeneration Neurobiol. Aging 35 2014 2421.e1 2421.e12
    • (2014) Neurobiol. Aging , vol.35 , pp. 2421.e1-2421.e12
    • Vatovec, S.1    Kovanda, A.2    Rogelj, B.3
  • 90
    • 84909944879 scopus 로고    scopus 로고
    • C9orf72 amyotrophic lateral sclerosis and frontotemporal dementia: Gain or loss of function?
    • S. Mizielinska, and A.M. Isaacs C9orf72 amyotrophic lateral sclerosis and frontotemporal dementia: gain or loss of function? Curr. Opin. Neurol. 27 2014 515 523
    • (2014) Curr. Opin. Neurol. , vol.27 , pp. 515-523
    • Mizielinska, S.1    Isaacs, A.M.2
  • 100
    • 0025905795 scopus 로고
    • Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome
    • A.J. Verkerk, M. Pieretti, J.S. Sutcliffe, Y.H. Fu, D.P. Kuhl, A. Pizzuti, O. Reiner, S. Richards, M.F. Victoria, and F.P. Zhang Identification of a gene (FMR-1) containing a CGG repeat coincident with a breakpoint cluster region exhibiting length variation in fragile X syndrome Cell 65 1991 905 914
    • (1991) Cell , vol.65 , pp. 905-914
    • Verkerk, A.J.1    Pieretti, M.2    Sutcliffe, J.S.3    Fu, Y.H.4    Kuhl, D.P.5    Pizzuti, A.6    Reiner, O.7    Richards, S.8    Victoria, M.F.9    Zhang, F.P.10
  • 104
    • 0027176361 scopus 로고
    • The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation
    • D. Devys, Y. Lutz, N. Rouyer, J.P. Bellocq, and J.L. Mandel The FMR-1 protein is cytoplasmic, most abundant in neurons and appears normal in carriers of a fragile X premutation Nat. Genet. 4 1993 335 340
    • (1993) Nat. Genet. , vol.4 , pp. 335-340
    • Devys, D.1    Lutz, Y.2    Rouyer, N.3    Bellocq, J.P.4    Mandel, J.L.5
  • 105
    • 0031046778 scopus 로고    scopus 로고
    • Fragile X mental retardation protein: Nucleocytoplasmic shuttling and association with somatodendritic ribosomes
    • Y. Feng, C.A. Gutekunst, D.E. Eberhart, H. Yi, S.T. Warren, and S.M. Hersch Fragile X mental retardation protein: nucleocytoplasmic shuttling and association with somatodendritic ribosomes J. Neurosci. 17 1997 1539 1547
    • (1997) J. Neurosci. , vol.17 , pp. 1539-1547
    • Feng, Y.1    Gutekunst, C.A.2    Eberhart, D.E.3    Yi, H.4    Warren, S.T.5    Hersch, S.M.6
  • 107
    • 0027377580 scopus 로고
    • FMR1 protein: Conserved RNP family domains and selective RNA binding
    • C.T. Ashley, K.D. Wilkinson, D. Reines, and S.T. Warren FMR1 protein: conserved RNP family domains and selective RNA binding Science 262 1993 563 566
    • (1993) Science , vol.262 , pp. 563-566
    • Ashley, C.T.1    Wilkinson, K.D.2    Reines, D.3    Warren, S.T.4
  • 110
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • J.C. Darnell, K.B. Jensen, P. Jin, V. Brown, S.T. Warren, and R.B. Darnell Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function Cell 107 2001 489 499
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5    Darnell, R.B.6
  • 111
    • 77952539696 scopus 로고    scopus 로고
    • Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA
    • E. Blackwell, X. Zhang, and S. Ceman Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA Hum. Mol. Genet. 19 2010 1314 1323
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1314-1323
    • Blackwell, E.1    Zhang, X.2    Ceman, S.3
  • 112
    • 0035801393 scopus 로고    scopus 로고
    • The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
    • C. Schaeffer, B. Bardoni, J.L. Mandel, B. Ehresmann, C. Ehresmann, and H. Moine The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif EMBO J. 20 2001 4803 4813
    • (2001) EMBO J. , vol.20 , pp. 4803-4813
    • Schaeffer, C.1    Bardoni, B.2    Mandel, J.L.3    Ehresmann, B.4    Ehresmann, C.5    Moine, H.6
  • 113
    • 47949115691 scopus 로고    scopus 로고
    • Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA
    • L. Menon, S.A. Mader, and M.-R. Mihailescu Fragile X mental retardation protein interactions with the microtubule associated protein 1B RNA RNA 14 2008 1644 1655
    • (2008) RNA , vol.14 , pp. 1644-1655
    • Menon, L.1    Mader, S.A.2    Mihailescu, M.-R.3
  • 114
    • 34548726219 scopus 로고    scopus 로고
    • Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family
    • L. Menon, and M.-R. Mihailescu Interactions of the G quartet forming semaphorin 3F RNA with the RGG box domain of the fragile X protein family Nucleic Acids Res. 35 2007 5379 5392
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5379-5392
    • Menon, L.1    Mihailescu, M.-R.2
  • 115
    • 33947195786 scopus 로고    scopus 로고
    • FMRP mediates mGluR5-dependent translation of amyloid precursor protein
    • C.J. Westmark, and J.S. Malter FMRP mediates mGluR5-dependent translation of amyloid precursor protein PLoS Biol. 5 2007 e52
    • (2007) PLoS Biol. , vol.5 , pp. e52
    • Westmark, C.J.1    Malter, J.S.2
  • 117
    • 0031310667 scopus 로고    scopus 로고
    • FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association
    • Y. Feng, D. Absher, D.E. Eberhart, V. Brown, H.E. Malter, and S.T. Warren FMRP associates with polyribosomes as an mRNP, and the I304N mutation of severe fragile X syndrome abolishes this association Mol. Cell 1 1997 109 118
    • (1997) Mol. Cell , vol.1 , pp. 109-118
    • Feng, Y.1    Absher, D.2    Eberhart, D.E.3    Brown, V.4    Malter, H.E.5    Warren, S.T.6
  • 124
    • 0347382502 scopus 로고    scopus 로고
    • Phosphorylation influences the translation state of FMRP-associated polyribosomes
    • S. Ceman, W.T. O'Donnell, M. Reed, S. Patton, J. Pohl, and S.T. Warren Phosphorylation influences the translation state of FMRP-associated polyribosomes Hum. Mol. Genet. 12 2003 3295 3305
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 3295-3305
    • Ceman, S.1    O'Donnell, W.T.2    Reed, M.3    Patton, S.4    Pohl, J.5    Warren, S.T.6
  • 125
    • 34249064936 scopus 로고    scopus 로고
    • Dysregulated metabotropic glutamate receptor-dependent translation of AMPA receptor and postsynaptic density-95 mRNAs at synapses in a mouse model of fragile X syndrome
    • R.S. Muddashetty, S. Kelić, C. Gross, M. Xu, and G.J. Bassell Dysregulated metabotropic glutamate receptor-dependent translation of AMPA receptor and postsynaptic density-95 mRNAs at synapses in a mouse model of fragile X syndrome J. Neurosci. 27 2007 5338 5348
    • (2007) J. Neurosci. , vol.27 , pp. 5338-5348
    • Muddashetty, R.S.1    Kelić, S.2    Gross, C.3    Xu, M.4    Bassell, G.J.5
  • 126
    • 3042647610 scopus 로고    scopus 로고
    • The mGluR theory of fragile X mental retardation
    • M.F. Bear, K.M. Huber, and S.T. Warren The mGluR theory of fragile X mental retardation Trends Neurosci. 27 2004 370 377
    • (2004) Trends Neurosci. , vol.27 , pp. 370-377
    • Bear, M.F.1    Huber, K.M.2    Warren, S.T.3
  • 131
    • 0028860737 scopus 로고
    • The fragile X syndrome single strand d(CGG)n nucleotide repeats readily fold back to form unimolecular hairpin structures
    • Y. Nadel, P. Weisman-Shomer, and M. Fry The fragile X syndrome single strand d(CGG)n nucleotide repeats readily fold back to form unimolecular hairpin structures J. Biol. Chem. 270 1995 28970 28977
    • (1995) J. Biol. Chem. , vol.270 , pp. 28970-28977
    • Nadel, Y.1    Weisman-Shomer, P.2    Fry, M.3
  • 132
    • 0142009656 scopus 로고    scopus 로고
    • RNA structure of trinucleotide repeats associated with human neurological diseases
    • K. Sobczak, M. de Mezer, G. Michlewski, J. Krol, and W.J. Krzyzosiak RNA structure of trinucleotide repeats associated with human neurological diseases Nucleic Acids Res. 31 2003 5469 5482
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5469-5482
    • Sobczak, K.1    De Mezer, M.2    Michlewski, G.3    Krol, J.4    Krzyzosiak, W.J.5
  • 133
    • 0344442391 scopus 로고    scopus 로고
    • The fragile X syndrome repeats form RNA hairpins that do not activate the interferon-inducible protein kinase, PKR, but are cut by Dicer
    • V. Handa, T. Saha, and K. Usdin The fragile X syndrome repeats form RNA hairpins that do not activate the interferon-inducible protein kinase, PKR, but are cut by Dicer Nucleic Acids Res. 31 2003 6243 6248
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6243-6248
    • Handa, V.1    Saha, T.2    Usdin, K.3
  • 134
    • 0023462494 scopus 로고
    • Ribonucleolytic activity of angiogenin: Essential histidine, lysine, and arginine residues
    • R. Shapiro, S. Weremowicz, J.F. Riordan, and B.L. Vallee Ribonucleolytic activity of angiogenin: essential histidine, lysine, and arginine residues Proc. Natl. Acad. Sci. U.S.A. 84 1987 8783 8787
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8783-8787
    • Shapiro, R.1    Weremowicz, S.2    Riordan, J.F.3    Vallee, B.L.4
  • 139
    • 84886581781 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in neurodegeneration: A new approach to therapy
    • M. Halliday, and G.R. Mallucci Targeting the unfolded protein response in neurodegeneration: a new approach to therapy Neuropharmacology 76 Pt A 2014 169 174
    • (2014) Neuropharmacology , vol.76 , pp. 169-174
    • Halliday, M.1    Mallucci, G.R.2
  • 140
    • 33846928449 scopus 로고    scopus 로고
    • G-quadruplexes in promoters throughout the human genome
    • J.L. Huppert, and S. Balasubramanian G-quadruplexes in promoters throughout the human genome Nucleic Acids Res. 35 2007 406 413
    • (2007) Nucleic Acids Res. , vol.35 , pp. 406-413
    • Huppert, J.L.1    Balasubramanian, S.2
  • 142
    • 77955809107 scopus 로고    scopus 로고
    • Making sense of G-quadruplex and i-motif functions in oncogene promoters
    • T.A. Brooks, S. Kendrick, and L. Hurley Making sense of G-quadruplex and i-motif functions in oncogene promoters FEBS J. 277 2010 3459 3469
    • (2010) FEBS J. , vol.277 , pp. 3459-3469
    • Brooks, T.A.1    Kendrick, S.2    Hurley, L.3
  • 143
    • 84920163445 scopus 로고    scopus 로고
    • Telomeric noncoding RNA: Telomeric repeat-containing RNA in telomere biology
    • E. Cusanelli, and P. Chartrand Telomeric noncoding RNA: telomeric repeat-containing RNA in telomere biology Wiley Interdiscip. Rev. RNA 5 2014 407 419
    • (2014) Wiley Interdiscip. Rev. RNA , vol.5 , pp. 407-419
    • Cusanelli, E.1    Chartrand, P.2
  • 144
    • 84856801825 scopus 로고    scopus 로고
    • Potential G-quadruplexes in the human long non-coding transcriptome
    • G.G. Jayaraj, S. Pandey, V. Scaria, and S. Maiti Potential G-quadruplexes in the human long non-coding transcriptome RNA Biol. 9 2012 81 86
    • (2012) RNA Biol. , vol.9 , pp. 81-86
    • Jayaraj, G.G.1    Pandey, S.2    Scaria, V.3    Maiti, S.4
  • 145
    • 84923205977 scopus 로고    scopus 로고
    • A potassium ion-dependent RNA structural switch regulates human pre-miRNA 92b maturation
    • G. Mirihana Arachchilage, A.C. Dassanayake, and S. Basu A potassium ion-dependent RNA structural switch regulates human pre-miRNA 92b maturation Chem. Biol. 22 2015 262 272
    • (2015) Chem. Biol. , vol.22 , pp. 262-272
    • Mirihana Arachchilage, G.1    Dassanayake, A.C.2    Basu, S.3
  • 146
    • 84920531496 scopus 로고    scopus 로고
    • G quadruplex RNA structures in PSD-95 mRNA: Potential regulators of miR-125a seed binding site accessibility
    • S. Stefanovic, G.J. Bassell, and M.R. Mihailescu G quadruplex RNA structures in PSD-95 mRNA: potential regulators of miR-125a seed binding site accessibility RNA 21 2015 48 60
    • (2015) RNA , vol.21 , pp. 48-60
    • Stefanovic, S.1    Bassell, G.J.2    Mihailescu, M.R.3
  • 149
    • 0037009364 scopus 로고    scopus 로고
    • MicroRNA maturation: Stepwise processing and subcellular localization
    • Y. Lee, K. Jeon, J.-T. Lee, S. Kim, and V.N. Kim MicroRNA maturation: stepwise processing and subcellular localization EMBO J. 21 2002 4663 4670
    • (2002) EMBO J. , vol.21 , pp. 4663-4670
    • Lee, Y.1    Jeon, K.2    Lee, J.-T.3    Kim, S.4    Kim, V.N.5
  • 151
    • 23044502585 scopus 로고    scopus 로고
    • Efficient processing of primary microRNA hairpins by Drosha requires flanking nonstructured RNA sequences
    • Y. Zeng, and B.R. Cullen Efficient processing of primary microRNA hairpins by Drosha requires flanking nonstructured RNA sequences J. Biol. Chem. 280 2005 27595 27603
    • (2005) J. Biol. Chem. , vol.280 , pp. 27595-27603
    • Zeng, Y.1    Cullen, B.R.2
  • 152
    • 1842608548 scopus 로고    scopus 로고
    • MicroRNA precursors in motion: Exportin-5 mediates their nuclear export
    • V.N. Kim MicroRNA precursors in motion: exportin-5 mediates their nuclear export Trends Cell Biol. 14 2004 156 159
    • (2004) Trends Cell Biol. , vol.14 , pp. 156-159
    • Kim, V.N.1
  • 153
    • 0035800521 scopus 로고    scopus 로고
    • A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA
    • G. Hutvágner, J. McLachlan, A.E. Pasquinelli, E. Bálint, T. Tuschl, and P.D. Zamore A cellular function for the RNA-interference enzyme Dicer in the maturation of the let-7 small temporal RNA Science 293 2001 834 838
    • (2001) Science , vol.293 , pp. 834-838
    • Hutvágner, G.1    McLachlan, J.2    Pasquinelli, A.E.3    Bálint, E.4    Tuschl, T.5    Zamore, P.D.6
  • 154
    • 0035905766 scopus 로고    scopus 로고
    • Role for a bidentate ribonuclease in the initiation step of RNA interference
    • E. Bernstein, A.A. Caudy, S.M. Hammond, and G.J. Hannon Role for a bidentate ribonuclease in the initiation step of RNA interference Nature 409 2001 363 366
    • (2001) Nature , vol.409 , pp. 363-366
    • Bernstein, E.1    Caudy, A.A.2    Hammond, S.M.3    Hannon, G.J.4
  • 156
    • 38549157087 scopus 로고    scopus 로고
    • Greglist: A database listing potential G-quadruplex regulated genes
    • R. Zhang, Y. Lin, and C.-T. Zhang Greglist: a database listing potential G-quadruplex regulated genes Nucleic Acids Res. 36 2008 D372 376
    • (2008) Nucleic Acids Res. , vol.36 , pp. D372-376
    • Zhang, R.1    Lin, Y.2    Zhang, C.-T.3
  • 157
    • 84876876209 scopus 로고    scopus 로고
    • MicroRNA-92b regulates the development of intermediate cortical progenitors in embryonic mouse brain
    • T.J. Nowakowski, V. Fotaki, A. Pollock, T. Sun, T. Pratt, and D.J. Price MicroRNA-92b regulates the development of intermediate cortical progenitors in embryonic mouse brain Proc. Natl. Acad. Sci. U.S.A. 110 2013 7056 7061
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 7056-7061
    • Nowakowski, T.J.1    Fotaki, V.2    Pollock, A.3    Sun, T.4    Pratt, T.5    Price, D.J.6
  • 158
    • 84882593725 scopus 로고    scopus 로고
    • The miR-92b functions as a potential oncogene by targeting on Smad3 in glioblastomas
    • Z.B. Wu, L. Cai, S.J. Lin, J.L. Lu, Y. Yao, and L.F. Zhou The miR-92b functions as a potential oncogene by targeting on Smad3 in glioblastomas Brain Res. 1529 2013 16 25
    • (2013) Brain Res. , vol.1529 , pp. 16-25
    • Wu, Z.B.1    Cai, L.2    Lin, S.J.3    Lu, J.L.4    Yao, Y.5    Zhou, L.F.6
  • 159
  • 161
    • 84892599690 scopus 로고    scopus 로고
    • PIWI proteins and PIWI-interacting RNAs in the soma
    • R.J. Ross, M.M. Weiner, and H. Lin PIWI proteins and PIWI-interacting RNAs in the soma Nature 505 2014 353 359
    • (2014) Nature , vol.505 , pp. 353-359
    • Ross, R.J.1    Weiner, M.M.2    Lin, H.3
  • 162
    • 84860320656 scopus 로고    scopus 로고
    • A role for neuronal piRNAs in the epigenetic control of memory-related synaptic plasticity
    • P. Rajasethupathy, I. Antonov, R. Sheridan, S. Frey, C. Sander, T. Tuschl, and E.R. Kandel A role for neuronal piRNAs in the epigenetic control of memory-related synaptic plasticity Cell 149 2012 693 707
    • (2012) Cell , vol.149 , pp. 693-707
    • Rajasethupathy, P.1    Antonov, I.2    Sheridan, R.3    Frey, S.4    Sander, C.5    Tuschl, T.6    Kandel, E.R.7
  • 165
    • 84855927549 scopus 로고    scopus 로고
    • PiRNAs and their involvement in male germline development in mice
    • R.S. Pillai, and S. Chuma PiRNAs and their involvement in male germline development in mice Dev. Growth Differ. 54 2012 78 92
    • (2012) Dev. Growth Differ. , vol.54 , pp. 78-92
    • Pillai, R.S.1    Chuma, S.2
  • 167
    • 80052991624 scopus 로고    scopus 로고
    • 3′ end formation of PIWI-interacting RNAs in vitro
    • S. Kawaoka, N. Izumi, S. Katsuma, and Y. Tomari 3′ end formation of PIWI-interacting RNAs in vitro Mol. Cell 43 2011 1015 1022
    • (2011) Mol. Cell , vol.43 , pp. 1015-1022
    • Kawaoka, S.1    Izumi, N.2    Katsuma, S.3    Tomari, Y.4
  • 168
    • 34247259831 scopus 로고    scopus 로고
    • Mouse Piwi-interacting RNAs are 2′-O-methylated at their 3′ termini
    • Y. Kirino, and Z. Mourelatos Mouse Piwi-interacting RNAs are 2′-O-methylated at their 3′ termini Nat. Struct. Mol. Biol. 14 2007 347 348
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 347-348
    • Kirino, Y.1    Mourelatos, Z.2
  • 171
    • 84863270094 scopus 로고    scopus 로고
    • RNase H-mediated degradation of toxic RNA in myotonic dystrophy type 1
    • J.E. Lee, C.F. Bennett, and T.A. Cooper RNase H-mediated degradation of toxic RNA in myotonic dystrophy type 1 Proc. Natl. Acad. Sci. U.S.A. 109 2012 4221 4226
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 4221-4226
    • Lee, J.E.1    Bennett, C.F.2    Cooper, T.A.3
  • 172
    • 82955237522 scopus 로고    scopus 로고
    • Potent and selective antisense oligonucleotides targeting single-nucleotide polymorphisms in the Huntington disease gene/allele-specific silencing of mutant huntingtin
    • J.B. Carroll, S.C. Warby, A.L. Southwell, C.N. Doty, S. Greenlee, N. Skotte, G. Hung, C.F. Bennett, S.M. Freier, and M.R. Hayden Potent and selective antisense oligonucleotides targeting single-nucleotide polymorphisms in the Huntington disease gene/allele-specific silencing of mutant huntingtin Mol. Ther. 19 2011 2178 2185
    • (2011) Mol. Ther. , vol.19 , pp. 2178-2185
    • Carroll, J.B.1    Warby, S.C.2    Southwell, A.L.3    Doty, C.N.4    Greenlee, S.5    Skotte, N.6    Hung, G.7    Bennett, C.F.8    Freier, S.M.9    Hayden, M.R.10
  • 174
    • 44349142304 scopus 로고    scopus 로고
    • Structural basis of DNA quadruplex recognition by an acridine drug
    • N.H. Campbell, G.N. Parkinson, A.P. Reszka, and S. Neidle Structural basis of DNA quadruplex recognition by an acridine drug J. Am. Chem. Soc. 130 2008 6722 6724
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6722-6724
    • Campbell, N.H.1    Parkinson, G.N.2    Reszka, A.P.3    Neidle, S.4
  • 176
    • 84900824121 scopus 로고    scopus 로고
    • Small-molecule quadruplex-targeted drug discovery
    • S.A. Ohnmacht, and S. Neidle Small-molecule quadruplex-targeted drug discovery Bioorg. Med. Chem. Lett. 24 2014 2602 2612
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 2602-2612
    • Ohnmacht, S.A.1    Neidle, S.2
  • 177
    • 84894465709 scopus 로고    scopus 로고
    • TMPyP4 porphyrin distorts RNA G-quadruplex structures of the disease-associated r(GGGGCC)n repeat of the C9orf72 gene and blocks interaction of RNA-binding proteins
    • B. Zamiri, K. Reddy, R.B. Macgregor, and C.E. Pearson TMPyP4 porphyrin distorts RNA G-quadruplex structures of the disease-associated r(GGGGCC)n repeat of the C9orf72 gene and blocks interaction of RNA-binding proteins J. Biol. Chem. 289 2014 4653 4659
    • (2014) J. Biol. Chem. , vol.289 , pp. 4653-4659
    • Zamiri, B.1    Reddy, K.2    MacGregor, R.B.3    Pearson, C.E.4
  • 179
  • 180
    • 0035394437 scopus 로고    scopus 로고
    • Reduced FMRP and increased FMR1 transcription is proportionally associated with CGG repeat number in intermediate-length and premutation carriers
    • A. Kenneson, F. Zhang, C.H. Hagedorn, and S.T. Warren Reduced FMRP and increased FMR1 transcription is proportionally associated with CGG repeat number in intermediate-length and premutation carriers Hum. Mol. Genet. 10 2001 1449 1454
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1449-1454
    • Kenneson, A.1    Zhang, F.2    Hagedorn, C.H.3    Warren, S.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.