메뉴 건너뛰기




Volumn 10, Issue 6, 2011, Pages 654-665

Human DHX9 helicase preferentially unwinds RNA-containing displacement loops (R-loops) and G-quadruplexes

Author keywords

D loops; DDX9 helicase; Guanine tetraplexes; R loops; Transcription associated recombination

Indexed keywords

DOUBLE STRANDED DNA; GUANINE QUADRUPLEX; HELICASE; OLIGONUCLEOTIDE;

EID: 79957813857     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2011.04.013     Document Type: Article
Times cited : (180)

References (55)
  • 1
    • 0025944523 scopus 로고
    • The maleless protein associates with the X chromosome to regulate dosage compensation in Drosophila
    • Kuroda M.I., Kernan M.J., Kreber R., Ganetzky B., Baker B.S. The maleless protein associates with the X chromosome to regulate dosage compensation in Drosophila. Cell 1991, 66:935-947.
    • (1991) Cell , vol.66 , pp. 935-947
    • Kuroda, M.I.1    Kernan, M.J.2    Kreber, R.3    Ganetzky, B.4    Baker, B.S.5
  • 2
    • 0027327132 scopus 로고
    • Human RNA helicase A is homologous to the maleless protein of Drosophila
    • Lee C.-G., Hurwitz J. Human RNA helicase A is homologous to the maleless protein of Drosophila. J. Biol. Chem. 1993, 268:16822-16830.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16822-16830
    • Lee, C.-G.1    Hurwitz, J.2
  • 4
    • 56249145093 scopus 로고    scopus 로고
    • Comparisons of RNAi approaches for validation of human RNA helicase A as an essential factor in hepatitis C virus replication
    • He Q.S., Tang H., Zhang J., Truong K., Wong-Staal F., Zhou D. Comparisons of RNAi approaches for validation of human RNA helicase A as an essential factor in hepatitis C virus replication. J. Virol. Methods 2008, 154:216-219.
    • (2008) J. Virol. Methods , vol.154 , pp. 216-219
    • He, Q.S.1    Tang, H.2    Zhang, J.3    Truong, K.4    Wong-Staal, F.5    Zhou, D.6
  • 5
    • 1242264341 scopus 로고    scopus 로고
    • DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner
    • Zhang S., Schlott B., Görlach M., Grosse F. DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner. Nucleic Acids Res. 2004, 32:1-10.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1-10
    • Zhang, S.1    Schlott, B.2    Görlach, M.3    Grosse, F.4
  • 7
    • 0031830844 scopus 로고    scopus 로고
    • BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A
    • Anderson S.F., Schlegel B.P., Nakajima T., Wolpin E.S., Parvin J.D. BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A. Nat. Genet. 1998, 19:254-256.
    • (1998) Nat. Genet. , vol.19 , pp. 254-256
    • Anderson, S.F.1    Schlegel, B.P.2    Nakajima, T.3    Wolpin, E.S.4    Parvin, J.D.5
  • 8
    • 4544264117 scopus 로고    scopus 로고
    • RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator
    • Tetsuka T., Uranishi H., Sanda T., Asamitsu K., Yang J.P., Wong-Staal F., Okamoto T. RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator. Eur. J. Biochem. 2004, 271:3741-3751.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3741-3751
    • Tetsuka, T.1    Uranishi, H.2    Sanda, T.3    Asamitsu, K.4    Yang, J.P.5    Wong-Staal, F.6    Okamoto, T.7
  • 9
    • 0035846905 scopus 로고    scopus 로고
    • Sequence-specific DNA binding activity of RNA helicase A to the p16INK4a promoter
    • Myöhänen S., Baylin S.B. Sequence-specific DNA binding activity of RNA helicase A to the p16INK4a promoter. J. Biol. Chem. 2001, 276:1634-1642.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1634-1642
    • Myöhänen, S.1    Baylin, S.B.2
  • 10
    • 2442466854 scopus 로고    scopus 로고
    • Multiple functions of nuclear DNA helicase II (RNA helicase A) in nucleic acid metabolism (review)
    • Zhang S., Grosse F. Multiple functions of nuclear DNA helicase II (RNA helicase A) in nucleic acid metabolism (review). Acta Biochim. Biophys. Sin. (Shanghai) 2004, 36:177-183.
    • (2004) Acta Biochim. Biophys. Sin. (Shanghai) , vol.36 , pp. 177-183
    • Zhang, S.1    Grosse, F.2
  • 11
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace F.V. DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res. 2006, 34:4206-4215.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4206-4215
    • Fuller-Pace, F.V.1
  • 13
    • 3042785608 scopus 로고    scopus 로고
    • Intracellular transcription of G-rich DNAs induces formation of G-loops, novel structures containing G4 DNA
    • Duquette M.L., Handa P., Vincent J.A., Taylor A.F., Maizels N. Intracellular transcription of G-rich DNAs induces formation of G-loops, novel structures containing G4 DNA. Genes Dev. 2004, 18:1618-1629.
    • (2004) Genes Dev. , vol.18 , pp. 1618-1629
    • Duquette, M.L.1    Handa, P.2    Vincent, J.A.3    Taylor, A.F.4    Maizels, N.5
  • 14
    • 0141819093 scopus 로고    scopus 로고
    • Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination
    • Huertas P, Aguilera A. Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol. Cell 2003, 12:711-721.
    • (2003) Mol. Cell , vol.12 , pp. 711-721
    • Huertas, P.1    Aguilera, A.2
  • 15
    • 24744471193 scopus 로고    scopus 로고
    • Nuclear DNA helicase II (RNA helicase A) interacts and stimulates the exonuclease of Werner syndrome helicase (WRN)
    • Friedemann J., Grosse F., Zhang S. Nuclear DNA helicase II (RNA helicase A) interacts and stimulates the exonuclease of Werner syndrome helicase (WRN). J. Biol. Chem. 2005, 280:31303-31313.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31303-31313
    • Friedemann, J.1    Grosse, F.2    Zhang, S.3
  • 16
    • 0030945449 scopus 로고    scopus 로고
    • Domain structure of human nuclear DNA helicase II (RNA helicase A)
    • Zhang S., Grosse F. Domain structure of human nuclear DNA helicase II (RNA helicase A). J. Biol. Chem. 1997, 272:11487-11494.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11487-11494
    • Zhang, S.1    Grosse, F.2
  • 17
    • 77952975783 scopus 로고    scopus 로고
    • Molecular characterization of nuclear DNA helicase II (RNA helicase A)
    • Zhang S., Grosse F. Molecular characterization of nuclear DNA helicase II (RNA helicase A). Methods Mol. Biol. 2010, 587:291-302.
    • (2010) Methods Mol. Biol. , vol.587 , pp. 291-302
    • Zhang, S.1    Grosse, F.2
  • 18
    • 77955705802 scopus 로고    scopus 로고
    • WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase
    • Chakraborty P., Grosse F. WRN helicase unwinds Okazaki fragment-like hybrids in a reaction stimulated by the human DHX9 helicase. Nucleic Acids Res. 2010, 38:4722-4730.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 4722-4730
    • Chakraborty, P.1    Grosse, F.2
  • 19
    • 0023788886 scopus 로고
    • Formation of parallel four-stranded complexes by guanine-rich motifs in DNA and its implications for meiosis
    • Sen D., Gilbert W. Formation of parallel four-stranded complexes by guanine-rich motifs in DNA and its implications for meiosis. Nature 1988, 334:364-366.
    • (1988) Nature , vol.334 , pp. 364-366
    • Sen, D.1    Gilbert, W.2
  • 20
    • 0024843757 scopus 로고
    • Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops
    • Sundquist W.I., Klug A. Telomeric DNA dimerizes by formation of guanine tetrads between hairpin loops. Nature 1989, 342:825-829.
    • (1989) Nature , vol.342 , pp. 825-829
    • Sundquist, W.I.1    Klug, A.2
  • 21
    • 0021989747 scopus 로고
    • The primase activity of DNA polymerase alpha from calf thymus
    • Grosse F., Krauss G. The primase activity of DNA polymerase alpha from calf thymus. J. Biol. Chem. 1985, 260:1881-1888.
    • (1985) J. Biol. Chem. , vol.260 , pp. 1881-1888
    • Grosse, F.1    Krauss, G.2
  • 23
    • 0017111913 scopus 로고
    • Isolation and characterization of the protein coded by gene A of bacteriophage phiX174 DNA
    • Ikeda J.E., Yudelevich A., Hurwitz J. Isolation and characterization of the protein coded by gene A of bacteriophage phiX174 DNA. Proc. Natl. Acad. Sci. U.S.A. 1976, 73:2669-2673.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2669-2673
    • Ikeda, J.E.1    Yudelevich, A.2    Hurwitz, J.3
  • 24
    • 0037166306 scopus 로고    scopus 로고
    • Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation
    • Karmakar P., Piotrowski J., Brosh R.M., Sommers J.A., Miller S.P., Cheng W.H., Snowden C.M., Ramsden D.A., Bohr V.A. Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation. J. Biol. Chem. 2002, 277:18291-18302.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18291-18302
    • Karmakar, P.1    Piotrowski, J.2    Brosh, R.M.3    Sommers, J.A.4    Miller, S.P.5    Cheng, W.H.6    Snowden, C.M.7    Ramsden, D.A.8    Bohr, V.A.9
  • 25
    • 0037137177 scopus 로고    scopus 로고
    • The Werner syndrome helicase/exonuclease (WRN) disrupts and degrades D-loops in vitro
    • Orren D.K, Theodore S., Machwe A. The Werner syndrome helicase/exonuclease (WRN) disrupts and degrades D-loops in vitro. Biochemistry 2002, 41:13483-13488.
    • (2002) Biochemistry , vol.41 , pp. 13483-13488
    • Orren, D.K.1    Theodore, S.2    Machwe, A.3
  • 26
    • 0346660225 scopus 로고
    • Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli
    • McEntee K., Weinstock G.M., Lehman I.R. Initiation of general recombination catalyzed in vitro by the recA protein of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 1979, 76:2615-2619.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 2615-2619
    • McEntee, K.1    Weinstock, G.M.2    Lehman, I.R.3
  • 27
    • 50649118135 scopus 로고    scopus 로고
    • RECQ1 possesses DNA branch migration activity
    • Bugreev D.V., Brosh R.M.J., Mazin A.V. RECQ1 possesses DNA branch migration activity. J. Biol. Chem. 2008, 283:20231-20242.
    • (2008) J. Biol. Chem. , vol.283 , pp. 20231-20242
    • Bugreev, D.V.1    Brosh, R.M.J.2    Mazin, A.V.3
  • 28
    • 33646843592 scopus 로고    scopus 로고
    • Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase
    • Bachrati C.Z., Borts R.H., Hickson I.D. Mobile D-loops are a preferred substrate for the Bloom's syndrome helicase. Nucleic Acids Res. 2006, 34:2269-2279.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 2269-2279
    • Bachrati, C.Z.1    Borts, R.H.2    Hickson, I.D.3
  • 29
    • 62849091779 scopus 로고    scopus 로고
    • The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation
    • Opresko P.L., Sowd G., Wang H. The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation. PLoS One 2009, 4:e4825.
    • (2009) PLoS One , vol.4
    • Opresko, P.L.1    Sowd, G.2    Wang, H.3
  • 30
    • 0033523001 scopus 로고    scopus 로고
    • Binding specificity determines polarity of DNA unwinding by the Sgs1 protein of S. cerevisiae
    • Bennett R.J., Keck J.L., Wang J.C. Binding specificity determines polarity of DNA unwinding by the Sgs1 protein of S. cerevisiae. J. Mol. Biol. 1999, 289:235-248.
    • (1999) J. Mol. Biol. , vol.289 , pp. 235-248
    • Bennett, R.J.1    Keck, J.L.2    Wang, J.C.3
  • 31
    • 68549136741 scopus 로고    scopus 로고
    • G-quadruplex structures: in vivo evidence and function
    • Lipps H.J., Rhodes D. G-quadruplex structures: in vivo evidence and function. Trends Cell Biol. 2009, 19:414-422.
    • (2009) Trends Cell Biol. , vol.19 , pp. 414-422
    • Lipps, H.J.1    Rhodes, D.2
  • 32
    • 0026726096 scopus 로고
    • A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3′-5′ direction
    • Lee C.-G., Hurwitz J. A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3′-5′ direction. J. Biol. Chem. 1992, 267:4398-4407.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4398-4407
    • Lee, C.-G.1    Hurwitz, J.2
  • 33
    • 54049111459 scopus 로고    scopus 로고
    • Processing of G4 DNA by Dna2 helicase/nuclease and replication protein A (RPA) provides insights into the mechanism of Dna2/RPA substrate recognition
    • Masuda-Sasa T., Polaczek P., Peng X.P., Chen L., Campbell J.L. Processing of G4 DNA by Dna2 helicase/nuclease and replication protein A (RPA) provides insights into the mechanism of Dna2/RPA substrate recognition. J. Biol. Chem. 2008, 283:24359-24373.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24359-24373
    • Masuda-Sasa, T.1    Polaczek, P.2    Peng, X.P.3    Chen, L.4    Campbell, J.L.5
  • 34
    • 8144220041 scopus 로고    scopus 로고
    • Formation of deletions during double-strand break repair in Drosophila DmBlm mutants occurs after strand invasion
    • McVey M., Larocque J.R., Adams M.D., Sekelsky J.J. Formation of deletions during double-strand break repair in Drosophila DmBlm mutants occurs after strand invasion. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:15694-15699.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15694-15699
    • McVey, M.1    Larocque, J.R.2    Adams, M.D.3    Sekelsky, J.J.4
  • 35
    • 76749147879 scopus 로고    scopus 로고
    • Srs2: the " Odd-Job Man" in DNA repair
    • Marini V., Krejci L. Srs2: the " Odd-Job Man" in DNA repair. DNA Repair (Amst) 2010, 9:268-275.
    • (2010) DNA Repair (Amst) , vol.9 , pp. 268-275
    • Marini, V.1    Krejci, L.2
  • 36
    • 57749100294 scopus 로고    scopus 로고
    • Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis
    • Stith C.M., Sterling J., Resnick M.A., Gordenin D.A., Burgers P.M. Flexibility of eukaryotic Okazaki fragment maturation through regulated strand displacement synthesis. J. Biol. Chem. 2008, 283:34129-34140.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34129-34140
    • Stith, C.M.1    Sterling, J.2    Resnick, M.A.3    Gordenin, D.A.4    Burgers, P.M.5
  • 37
    • 0030008328 scopus 로고    scopus 로고
    • Recombination by replication
    • Kogoma T. Recombination by replication. Cell 1996, 85:625-627.
    • (1996) Cell , vol.85 , pp. 625-627
    • Kogoma, T.1
  • 40
    • 33645185950 scopus 로고    scopus 로고
    • Critical role of R-loops in processing replication blocks
    • Camps M., Loeb L.A. Critical role of R-loops in processing replication blocks. Front. Biosci. 2005, 10:689-698.
    • (2005) Front. Biosci. , vol.10 , pp. 689-698
    • Camps, M.1    Loeb, L.A.2
  • 41
    • 66749175352 scopus 로고    scopus 로고
    • Transcription-associated recombination in eukaryotes: link between transcription, replication and recombination
    • Gottipati P., Helleday T. Transcription-associated recombination in eukaryotes: link between transcription, replication and recombination. Mutagenesis 2009, 24:203-210.
    • (2009) Mutagenesis , vol.24 , pp. 203-210
    • Gottipati, P.1    Helleday, T.2
  • 42
    • 39449096135 scopus 로고    scopus 로고
    • Genome instability: a mechanistic view of its causes and consequences
    • Aguilera A, Gómez-González B. Genome instability: a mechanistic view of its causes and consequences. Nat. Rev. Genet. 2008, 9:204-217.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 204-217
    • Aguilera, A.1    Gómez-González, B.2
  • 43
    • 23744455164 scopus 로고    scopus 로고
    • Inactivation of the SR protein splicing factor ASF/SF2 results in genomic instability
    • Li X., Manley J.L. Inactivation of the SR protein splicing factor ASF/SF2 results in genomic instability. Cell 2005, 122:365-378.
    • (2005) Cell , vol.122 , pp. 365-378
    • Li, X.1    Manley, J.L.2
  • 44
    • 20144364292 scopus 로고    scopus 로고
    • Prevalence of quadruplexes in the human genome
    • Huppert J.L., Balasubramanian S. Prevalence of quadruplexes in the human genome. Nucleic Acids Res. 2005, 33:2908-2916.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2908-2916
    • Huppert, J.L.1    Balasubramanian, S.2
  • 45
    • 20144369806 scopus 로고    scopus 로고
    • Highly prevalent putative quadruplex sequence motifs in human DNA
    • Todd A.K., Johnston M., Neidle S. Highly prevalent putative quadruplex sequence motifs in human DNA. Nucleic Acids Res. 2005, 33:2901-2907.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2901-2907
    • Todd, A.K.1    Johnston, M.2    Neidle, S.3
  • 46
    • 10344256183 scopus 로고    scopus 로고
    • Defective telomere lagging strand synthesis in cells lacking WRN helicase activity
    • Crabbe L., Verdun R.E., Haggblom C.I., Karlseder J. Defective telomere lagging strand synthesis in cells lacking WRN helicase activity. Science 2004, 306:1951-1953.
    • (2004) Science , vol.306 , pp. 1951-1953
    • Crabbe, L.1    Verdun, R.E.2    Haggblom, C.I.3    Karlseder, J.4
  • 47
    • 33947310727 scopus 로고    scopus 로고
    • An RNA G-quadruplex in the 5' UTR of the NRAS proto-oncogene modulates translation
    • Kumari S., Bugaut A., Huppert J.L., Balasubramanian S. An RNA G-quadruplex in the 5' UTR of the NRAS proto-oncogene modulates translation. Nat. Chem. Biol. 2007, 3:218-221.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 218-221
    • Kumari, S.1    Bugaut, A.2    Huppert, J.L.3    Balasubramanian, S.4
  • 49
    • 0031030491 scopus 로고    scopus 로고
    • A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates
    • Bashkirov V.I., Scherthan H., Solinger J.A., Buerstedde J.M., Heyer W.D. A mouse cytoplasmic exoribonuclease (mXRN1p) with preference for G4 tetraplex substrates. J. Cell Biol. 1997, 136:761-773.
    • (1997) J. Cell Biol. , vol.136 , pp. 761-773
    • Bashkirov, V.I.1    Scherthan, H.2    Solinger, J.A.3    Buerstedde, J.M.4    Heyer, W.D.5
  • 50
    • 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
    • Creacy S.D., Routh E.D., Iwamoto F., Nagamine Y., Akman S.A., Vaughn J.P. 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. 2008, 283:34626-34634.
    • (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
  • 51
    • 78049439594 scopus 로고    scopus 로고
    • Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU
    • Lattmann S., Giri B., Vaughn J.P., Akman S.A., Nagamine Y. Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU. Nucleic Acids Res. 2010, 38:6219-6233.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6219-6233
    • Lattmann, S.1    Giri, B.2    Vaughn, J.P.3    Akman, S.A.4    Nagamine, Y.5
  • 52
    • 0033034413 scopus 로고    scopus 로고
    • High affinity interactions of nucleolin with G-G-paired rDNA
    • Hanakahi L.A., Sun H., Maizels N. High affinity interactions of nucleolin with G-G-paired rDNA. J. Biol. Chem. 1999, 274:15908-15912.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15908-15912
    • Hanakahi, L.A.1    Sun, H.2    Maizels, N.3
  • 53
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • Darnell J.C., Jensen K.B., Jin P., Brown V., Warren S.T., Darnell R.B. Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function. Cell 2001, 107:489-499.
    • (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
  • 54
    • 0035801393 scopus 로고    scopus 로고
    • The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif
    • Schaeffer C., Bardoni B., Mandel J.L., Ehresmann B., Ehresmann C., Moine H. The fragile X mental retardation protein binds specifically to its mRNA via a purine quartet motif. EMBO J. 2001, 20:4803-4813.
    • (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
  • 55
    • 15744362987 scopus 로고    scopus 로고
    • Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II
    • Mischo H.E., Hemmerich P., Grosse F., Zhang S. Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II. J. Biol. Chem. 2005, 280:9586-9594.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9586-9594
    • Mischo, H.E.1    Hemmerich, P.2    Grosse, F.3    Zhang, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.