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Volumn 743-744, Issue , 2013, Pages 118-131

The yin and yang of repair mechanisms in DNA structure-induced genetic instability

Author keywords

DNA repair; DNA structure; Genetic instability; Triplex DNA; Z DNA

Indexed keywords

CRUCIFORM DNA; DEOXYRIBONUCLEOPROTEIN; DNA; DNA H; DNA POLYMERASE; DNA Z; GENOMIC DNA; GUANINE QUADRUPLEX; HELICASE; MISMATCH REPAIR PROTEIN; RNA POLYMERASE; UNCLASSIFIED DRUG;

EID: 84877921309     PISSN: 00275107     EISSN: 09218262     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2012.11.005     Document Type: Review
Times cited : (23)

References (242)
  • 1
  • 3
    • 0029925689 scopus 로고    scopus 로고
    • Characterization of large CTG repeat expansions in myotonic dystrophy alleles using PCR
    • Cheng S., Barcelo J.M., Korneluk R.G. Characterization of large CTG repeat expansions in myotonic dystrophy alleles using PCR. Hum. Mutat. 1996, 7:304-310.
    • (1996) Hum. Mutat. , vol.7 , pp. 304-310
    • Cheng, S.1    Barcelo, J.M.2    Korneluk, R.G.3
  • 4
    • 0030058075 scopus 로고    scopus 로고
    • Molecular basis of genetic instability of triplet repeats
    • Wells R.D. Molecular basis of genetic instability of triplet repeats. J. Biol. Chem. 1996, 271:2875-2878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2875-2878
    • Wells, R.D.1
  • 5
    • 0035201633 scopus 로고    scopus 로고
    • The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders
    • Bowater R.P., Wells R.D. The intrinsically unstable life of DNA triplet repeats associated with human hereditary disorders. Prog. Nucleic Acid Res. Mol. Biol. 2001, 66:159-202.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 159-202
    • Bowater, R.P.1    Wells, R.D.2
  • 6
    • 33745286272 scopus 로고    scopus 로고
    • DM2 CCTG*CAGG repeats are crossover hotspots that are more prone to expansions than the DM1 CTG*CAG repeats in Escherichia coli
    • Dere R., Wells R.D. DM2 CCTG*CAGG repeats are crossover hotspots that are more prone to expansions than the DM1 CTG*CAG repeats in Escherichia coli. J. Mol. Biol. 2006, 360:21-36.
    • (2006) J. Mol. Biol. , vol.360 , pp. 21-36
    • Dere, R.1    Wells, R.D.2
  • 8
    • 81455144644 scopus 로고    scopus 로고
    • Conformational changes of non-B DNA
    • Choi J., Majima T. Conformational changes of non-B DNA. Chem. Soc. Rev. 2011, 40:5893-5909.
    • (2011) Chem. Soc. Rev. , vol.40 , pp. 5893-5909
    • Choi, J.1    Majima, T.2
  • 10
    • 0023909024 scopus 로고
    • Characteristics of Z-DNA helices formed by imperfect (purine-pyrimidine) sequences in plasmids
    • McLean M.J., Lee J.W., Wells R.D. Characteristics of Z-DNA helices formed by imperfect (purine-pyrimidine) sequences in plasmids. J. Biol. Chem. 1988, 263:7378-7385.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7378-7385
    • McLean, M.J.1    Lee, J.W.2    Wells, R.D.3
  • 12
    • 0029883306 scopus 로고    scopus 로고
    • Stability of intrastrand hairpin structures formed by the CAG/CTG class of DNA triplet repeats associated with neurological diseases
    • Petruska J., Arnheim N., Goodman M.F. Stability of intrastrand hairpin structures formed by the CAG/CTG class of DNA triplet repeats associated with neurological diseases. Nucleic Acids Res. 1996, 24:1992-1998.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1992-1998
    • Petruska, J.1    Arnheim, N.2    Goodman, M.F.3
  • 13
    • 25844506224 scopus 로고    scopus 로고
    • Therapeutics development for triplet repeat expansion diseases
    • Di Prospero N.A., Fischbeck K.H. Therapeutics development for triplet repeat expansion diseases. Nat. Rev. Genet. 2005, 6:756-765.
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 756-765
    • Di Prospero, N.A.1    Fischbeck, K.H.2
  • 15
    • 0029762817 scopus 로고    scopus 로고
    • Inverted repeats, stem-loops, and cruciforms: significance for initiation of DNA replication
    • Pearson C.E., Zorbas H., Price G.B., Zannis-Hadjopoulos M. Inverted repeats, stem-loops, and cruciforms: significance for initiation of DNA replication. J. Cell. Biochem. 1996, 63:1-22.
    • (1996) J. Cell. Biochem. , vol.63 , pp. 1-22
    • Pearson, C.E.1    Zorbas, H.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 17
    • 34249907843 scopus 로고    scopus 로고
    • Non-B DNA conformations, mutagenesis and disease
    • Wells R.D. Non-B DNA conformations, mutagenesis and disease. Trends Biochem. Sci. 2007, 32:271-278.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 271-278
    • Wells, R.D.1
  • 18
    • 73749085274 scopus 로고    scopus 로고
    • Non-B DNA structure-induced genetic instability and evolution
    • Zhao J., Bacolla A., Wang G., Vasquez K.M. Non-B DNA structure-induced genetic instability and evolution. Cell. Mol. Life Sci. 2010, 67:43-62.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 43-62
    • Zhao, J.1    Bacolla, A.2    Wang, G.3    Vasquez, K.M.4
  • 22
    • 0033950564 scopus 로고    scopus 로고
    • Molecular and clinical features of non-Burkitt's, diffuse large-cell lymphoma of B-cell type associated with the c-MYC/immunoglobulin heavy-chain fusion gene
    • Akasaka T., Akasaka H., Ueda C., Yonetani N., Maesako Y., Shimizu A., Yamabe H., Fukuhara S., Uchiyama T., Ohno H. Molecular and clinical features of non-Burkitt's, diffuse large-cell lymphoma of B-cell type associated with the c-MYC/immunoglobulin heavy-chain fusion gene. J. Clin. Oncol. 2000, 18:510-518.
    • (2000) J. Clin. Oncol. , vol.18 , pp. 510-518
    • Akasaka, T.1    Akasaka, H.2    Ueda, C.3    Yonetani, N.4    Maesako, Y.5    Shimizu, A.6    Yamabe, H.7    Fukuhara, S.8    Uchiyama, T.9    Ohno, H.10
  • 23
    • 0030687580 scopus 로고    scopus 로고
    • Deletional remodeling of c-MYC-deregulating chromosomal translocations
    • Kovalchuk A.L., Muller J.R., Janz S. Deletional remodeling of c-MYC-deregulating chromosomal translocations. Oncogene 1997, 15:2369-2377.
    • (1997) Oncogene , vol.15 , pp. 2369-2377
    • Kovalchuk, A.L.1    Muller, J.R.2    Janz, S.3
  • 25
    • 0024296386 scopus 로고
    • The t(8;14) breakpoint of the EW 36 undifferentiated lymphoma cell line lies 5' of MYC in a region prone to involvement in endemic Burkitt's lymphomas
    • Haluska F.G., Tsujimoto Y., Croce C.M. The t(8;14) breakpoint of the EW 36 undifferentiated lymphoma cell line lies 5' of MYC in a region prone to involvement in endemic Burkitt's lymphomas. Nucleic Acids Res. 1988, 16:2077-2085.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 2077-2085
    • Haluska, F.G.1    Tsujimoto, Y.2    Croce, C.M.3
  • 28
    • 4143078049 scopus 로고    scopus 로고
    • Level of MYC overexpression in pediatric Burkitt's lymphoma is strongly dependent on genomic breakpoint location within the MYC locus
    • Wilda M., Busch K., Klose I., Keller T., Woessmann W., Kreuder J., Harbott J., Borkhardt A. Level of MYC overexpression in pediatric Burkitt's lymphoma is strongly dependent on genomic breakpoint location within the MYC locus. Genes Chromosomes Cancer 2004, 41:178-182.
    • (2004) Genes Chromosomes Cancer , vol.41 , pp. 178-182
    • Wilda, M.1    Busch, K.2    Klose, I.3    Keller, T.4    Woessmann, W.5    Kreuder, J.6    Harbott, J.7    Borkhardt, A.8
  • 29
    • 0024425127 scopus 로고
    • A cis-acting transcription element of the c-MYC gene can assume an H-DNA conformation
    • Kinniburgh A.J. A cis-acting transcription element of the c-MYC gene can assume an H-DNA conformation. Nucleic Acids Res. 1989, 17:7771-7778.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 7771-7778
    • Kinniburgh, A.J.1
  • 35
    • 4544288618 scopus 로고    scopus 로고
    • Naturally occurring H-DNA-forming sequences are mutagenic in mammalian cells
    • Wang G., Vasquez K.M. Naturally occurring H-DNA-forming sequences are mutagenic in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:13448-13453.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 13448-13453
    • Wang, G.1    Vasquez, K.M.2
  • 37
    • 0022133407 scopus 로고
    • Chemical probes of DNA conformation: detection of Z-DNA at nucleotide resolution
    • Johnston B.H., Rich A. Chemical probes of DNA conformation: detection of Z-DNA at nucleotide resolution. Cell 1985, 42:713-724.
    • (1985) Cell , vol.42 , pp. 713-724
    • Johnston, B.H.1    Rich, A.2
  • 38
    • 0019544304 scopus 로고
    • Effects of methylation on a synthetic polynucleotide: the B--Z transition in poly(dG-m5dC).poly(dG-m5dC)
    • Behe M., Felsenfeld G. Effects of methylation on a synthetic polynucleotide: the B--Z transition in poly(dG-m5dC).poly(dG-m5dC). Proc. Natl. Acad. Sci. U. S. A. 1981, 78:1619-1623.
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , pp. 1619-1623
    • Behe, M.1    Felsenfeld, G.2
  • 39
    • 0023884934 scopus 로고
    • The role of DNA sequence in the formation of Z-DNA versus cruciforms in plasmids
    • McLean M.J., Wells R.D. The role of DNA sequence in the formation of Z-DNA versus cruciforms in plasmids. J. Biol. Chem. 1988, 263:7370-7377.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7370-7377
    • McLean, M.J.1    Wells, R.D.2
  • 41
    • 0022380477 scopus 로고
    • Z-DNA forms without an alternating purine-pyrimidine sequence in solution
    • Feigon J., Wang A.H., van der Marel G.A., van Boom J.H., Rich A. Z-DNA forms without an alternating purine-pyrimidine sequence in solution. Science 1985, 230:82-84.
    • (1985) Science , vol.230 , pp. 82-84
    • Feigon, J.1    Wang, A.H.2    van der Marel, G.A.3    van Boom, J.H.4    Rich, A.5
  • 42
    • 0033555744 scopus 로고    scopus 로고
    • The intrinsic structure and stability of out-of-alternation base pairs in Z-DNA
    • Eichman B.F., Schroth G.P., Basham B.E., Ho P.S. The intrinsic structure and stability of out-of-alternation base pairs in Z-DNA. Nucleic Acids Res. 1999, 27:543-550.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 543-550
    • Eichman, B.F.1    Schroth, G.P.2    Basham, B.E.3    Ho, P.S.4
  • 44
    • 0029588611 scopus 로고
    • Identification of transcriptionally induced Z-DNA segments in the human c-MYC gene
    • Wolfl S., Wittig B., Rich A. Identification of transcriptionally induced Z-DNA segments in the human c-MYC gene. Biochim. Biophys. Acta 1995, 1264:294-302.
    • (1995) Biochim. Biophys. Acta , vol.1264 , pp. 294-302
    • Wolfl, S.1    Wittig, B.2    Rich, A.3
  • 45
    • 0024437912 scopus 로고
    • Alternating purine-pyrimidine tracts may promote chromosomal translocations seen in a variety of human lymphoid tumours
    • Boehm T., Mengle-Gaw L., Kees U.R., Spurr N., Lavenir I., Forster A., Rabbitts T.H. Alternating purine-pyrimidine tracts may promote chromosomal translocations seen in a variety of human lymphoid tumours. EMBO J. 1989, 8:2621-2631.
    • (1989) EMBO J. , vol.8 , pp. 2621-2631
    • Boehm, T.1    Mengle-Gaw, L.2    Kees, U.R.3    Spurr, N.4    Lavenir, I.5    Forster, A.6    Rabbitts, T.H.7
  • 46
    • 79958724230 scopus 로고    scopus 로고
    • Analysis of a breakpoint cluster reveals insight into the mechanism of intrachromosomal amplification in a lymphoid malignancy
    • Sinclair P.B., Parker H., An Q., Rand V., Ensor H., Harrison C.J., Strefford J.C. Analysis of a breakpoint cluster reveals insight into the mechanism of intrachromosomal amplification in a lymphoid malignancy. Hum. Mol. Genet. 2011, 20:2591-2602.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2591-2602
    • Sinclair, P.B.1    Parker, H.2    An, Q.3    Rand, V.4    Ensor, H.5    Harrison, C.J.6    Strefford, J.C.7
  • 47
    • 0023656131 scopus 로고
    • The obtention of simian virus 40 recombinants carrying d(CG.GC)n, d(CA.GT)n and d(CT.GA)n sequences. Stability of the inserted simple repeating sequences
    • Casasnovas J.M., Ellison M.J., Rodriguez-Campos A., Azorin F. The obtention of simian virus 40 recombinants carrying d(CG.GC)n, d(CA.GT)n and d(CT.GA)n sequences. Stability of the inserted simple repeating sequences. Eur. J. Biochem. 1987, 167:489-492.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 489-492
    • Casasnovas, J.M.1    Ellison, M.J.2    Rodriguez-Campos, A.3    Azorin, F.4
  • 49
    • 0035859024 scopus 로고    scopus 로고
    • Neurodegenerative diseases. Origins of instability
    • Sinden R.R. Neurodegenerative diseases. Origins of instability. Nature 2001, 411:757-758.
    • (2001) Nature , vol.411 , pp. 757-758
    • Sinden, R.R.1
  • 50
    • 33644543741 scopus 로고    scopus 로고
    • Z-DNA-forming sequences generate large-scale deletions in mammalian cells
    • Wang G., Christensen L.A., Vasquez K.M. Z-DNA-forming sequences generate large-scale deletions in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:2677-2682.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 2677-2682
    • Wang, G.1    Christensen, L.A.2    Vasquez, K.M.3
  • 51
    • 0019829267 scopus 로고
    • Instability of palindromic DNA in Escherichia coli
    • Collins J. Instability of palindromic DNA in Escherichia coli. Cold Spring Harb. Symp. Quant. Biol. 1981, 45 Pt 1:409-416.
    • (1981) Cold Spring Harb. Symp. Quant. Biol. , pp. 409-416
    • Collins, J.1
  • 52
    • 0020455123 scopus 로고
    • Precise and nearly-precise excision of the symmetrical inverted repeats of Tn5; common features of recA-independent deletion events in Escherichia coli
    • Collins J., Volckaert G., Nevers P. Precise and nearly-precise excision of the symmetrical inverted repeats of Tn5; common features of recA-independent deletion events in Escherichia coli. Gene 1982, 19:139-146.
    • (1982) Gene , vol.19 , pp. 139-146
    • Collins, J.1    Volckaert, G.2    Nevers, P.3
  • 53
    • 0025933719 scopus 로고
    • Seven-base-pair inverted repeats in DNA form stable hairpins in vivo in Saccharomyces cerevisiae
    • Nag D.K., Petes T.D. Seven-base-pair inverted repeats in DNA form stable hairpins in vivo in Saccharomyces cerevisiae. Genetics 1991, 129:669-673.
    • (1991) Genetics , vol.129 , pp. 669-673
    • Nag, D.K.1    Petes, T.D.2
  • 54
    • 35448981532 scopus 로고    scopus 로고
    • Evidence for a large double-cruciform DNA structure on the X chromosome of human and chimpanzee
    • Losch F.O., Bredenbeck A., Hollstein V.M., Walden P., Wrede P. Evidence for a large double-cruciform DNA structure on the X chromosome of human and chimpanzee. Hum. Genet. 2007, 122:337-343.
    • (2007) Hum. Genet. , vol.122 , pp. 337-343
    • Losch, F.O.1    Bredenbeck, A.2    Hollstein, V.M.3    Walden, P.4    Wrede, P.5
  • 55
    • 0033960606 scopus 로고    scopus 로고
    • Palindromes as substrates for multiple pathways of recombination in Escherichia coli
    • Cromie G.A., Millar C.B., Schmidt K.H., Leach D.R. Palindromes as substrates for multiple pathways of recombination in Escherichia coli. Genetics 2000, 154:513-522.
    • (2000) Genetics , vol.154 , pp. 513-522
    • Cromie, G.A.1    Millar, C.B.2    Schmidt, K.H.3    Leach, D.R.4
  • 57
    • 0030794661 scopus 로고    scopus 로고
    • A 140bp-long palindromic sequence induces double-strand breaks during meiosis in the yeast Saccharomyces cerevisiae
    • Nag D.K., Kurst A. A 140bp-long palindromic sequence induces double-strand breaks during meiosis in the yeast Saccharomyces cerevisiae. Genetics 1997, 146:835-847.
    • (1997) Genetics , vol.146 , pp. 835-847
    • Nag, D.K.1    Kurst, A.2
  • 59
    • 0037173105 scopus 로고    scopus 로고
    • Short inverted repeats initiate gene amplification through the formation of a large DNA palindrome in mammalian cells
    • Tanaka H., Tapscott S.J., Trask B.J., Yao M.C. Short inverted repeats initiate gene amplification through the formation of a large DNA palindrome in mammalian cells. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:8772-8777.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8772-8777
    • Tanaka, H.1    Tapscott, S.J.2    Trask, B.J.3    Yao, M.C.4
  • 60
    • 0035902483 scopus 로고    scopus 로고
    • Repeat expansion by homologous recombination in the mouse germ line at palindromic sequences
    • Zhou Z.H., Akgun E., Jasin M. Repeat expansion by homologous recombination in the mouse germ line at palindromic sequences. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:8326-8333.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 8326-8333
    • Zhou, Z.H.1    Akgun, E.2    Jasin, M.3
  • 61
    • 0242637353 scopus 로고    scopus 로고
    • Rapid, stabilizing palindrome rearrangements in somatic cells by the center-break mechanism
    • Cunningham L.A., Cote A.G., Cam-Ozdemir C., Lewis S.M. Rapid, stabilizing palindrome rearrangements in somatic cells by the center-break mechanism. Mol. Cell. Biol. 2003, 23:8740-8750.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 8740-8750
    • Cunningham, L.A.1    Cote, A.G.2    Cam-Ozdemir, C.3    Lewis, S.M.4
  • 62
    • 0035509701 scopus 로고    scopus 로고
    • Long AT-rich palindromes and the constitutional t(11;22) breakpoint
    • Kurahashi H., Emanuel B.S. Long AT-rich palindromes and the constitutional t(11;22) breakpoint. Hum. Mol. Genet. 2001, 10:2605-2617.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2605-2617
    • Kurahashi, H.1    Emanuel, B.S.2
  • 64
    • 0034234453 scopus 로고    scopus 로고
    • Regions of genomic instability on 22q11 and 11q23 as the etiology for the recurrent constitutional t(11;22)
    • Kurahashi H., Shaikh T.H., Hu P., Roe B.A., Emanuel B.S., Budarf M.L. Regions of genomic instability on 22q11 and 11q23 as the etiology for the recurrent constitutional t(11;22). Hum. Mol. Genet. 2000, 9:1665-1670.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1665-1670
    • Kurahashi, H.1    Shaikh, T.H.2    Hu, P.3    Roe, B.A.4    Emanuel, B.S.5    Budarf, M.L.6
  • 65
    • 25844524498 scopus 로고    scopus 로고
    • Slipped (CTG)*(CAG) repeats can be correctly repaired, escape repair or undergo error-prone repair
    • Panigrahi G.B., Lau R., Montgomery S.E., Leonard M.R., Pearson C.E. Slipped (CTG)*(CAG) repeats can be correctly repaired, escape repair or undergo error-prone repair. Nat. Struct. Mol. Biol. 2005, 12:654-662.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 654-662
    • Panigrahi, G.B.1    Lau, R.2    Montgomery, S.E.3    Leonard, M.R.4    Pearson, C.E.5
  • 66
    • 0032559372 scopus 로고    scopus 로고
    • CTG repeats associated with human genetic disease are inherently flexible
    • Chastain P.D., Sinden R.R. CTG repeats associated with human genetic disease are inherently flexible. J. Mol. Biol. 1998, 275:405-411.
    • (1998) J. Mol. Biol. , vol.275 , pp. 405-411
    • Chastain, P.D.1    Sinden, R.R.2
  • 67
    • 0242549824 scopus 로고    scopus 로고
    • DNA repair and trinucleotide repeat instability
    • Lahue R.S., Slater D.L. DNA repair and trinucleotide repeat instability. Front. Biosci. 2003, 8:s653-s665.
    • (2003) Front. Biosci. , vol.8
    • Lahue, R.S.1    Slater, D.L.2
  • 68
    • 0032508613 scopus 로고    scopus 로고
    • A preferred target DNA structure for retroviral integrase in vitro
    • Katz R.A., Gravuer K., Skalka A.M. A preferred target DNA structure for retroviral integrase in vitro. J. Biol. Chem. 1998, 273:24190-24195.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24190-24195
    • Katz, R.A.1    Gravuer, K.2    Skalka, A.M.3
  • 70
    • 77955791569 scopus 로고    scopus 로고
    • G-quadruplex nucleic acids and human disease
    • Wu Y., Brosh R.M. G-quadruplex nucleic acids and human disease. FEBS J. 2010, 277:3470-3488.
    • (2010) FEBS J. , vol.277 , pp. 3470-3488
    • Wu, Y.1    Brosh, R.M.2
  • 71
    • 0034176194 scopus 로고    scopus 로고
    • G-quadruplex DNA: a potential target for anti-cancer drug design
    • Han H., Hurley L.H. G-quadruplex DNA: a potential target for anti-cancer drug design. Trends Pharmacol. Sci. 2000, 21:136-142.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 136-142
    • Han, H.1    Hurley, L.H.2
  • 72
    • 84865076195 scopus 로고    scopus 로고
    • Experimental approaches to identify cellular G-quadruplex structures and functions
    • Di Antonio M., Rodriguez R., Balasubramanian S. Experimental approaches to identify cellular G-quadruplex structures and functions. Methods 2012, 57:84-92.
    • (2012) Methods , vol.57 , pp. 84-92
    • Di Antonio, M.1    Rodriguez, R.2    Balasubramanian, S.3
  • 73
    • 33846928449 scopus 로고    scopus 로고
    • G-quadruplexes in promoters throughout the human genome
    • Huppert J.L., Balasubramanian S. G-quadruplexes in promoters throughout the human genome. Nucleic Acids Res. 2007, 35:406-413.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 406-413
    • Huppert, J.L.1    Balasubramanian, S.2
  • 74
    • 78049298053 scopus 로고    scopus 로고
    • G-quadruplex DNA sequences are evolutionarily conserved and associated with distinct genomic features in Saccharomyces cerevisiae
    • Capra J.A., Paeschke K., Singh M., Zakian V.A. G-quadruplex DNA sequences are evolutionarily conserved and associated with distinct genomic features in Saccharomyces cerevisiae. PLoS Comput. Biol. 2010, 6:e1000861.
    • (2010) PLoS Comput. Biol. , vol.6
    • Capra, J.A.1    Paeschke, K.2    Singh, M.3    Zakian, V.A.4
  • 75
    • 84860168390 scopus 로고    scopus 로고
    • Cell cycle regulation of G-quadruplex DNA structures at telomeres
    • Juranek S.A., Paeschke K. Cell cycle regulation of G-quadruplex DNA structures at telomeres. Curr. Pharm. Des. 2012, 18:1867-1872.
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 1867-1872
    • Juranek, S.A.1    Paeschke, K.2
  • 76
    • 80051762076 scopus 로고    scopus 로고
    • G-quadruplex formation at the 3' end of telomere DNA inhibits its extension by telomerase, polymerase and unwinding by helicase
    • Wang Q., Liu J.Q., Chen Z., Zheng K.W., Chen C.Y., Hao Y.H., Tan Z. G-quadruplex formation at the 3' end of telomere DNA inhibits its extension by telomerase, polymerase and unwinding by helicase. Nucleic Acids Res. 2011, 39:6229-6237.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 6229-6237
    • Wang, Q.1    Liu, J.Q.2    Chen, Z.3    Zheng, K.W.4    Chen, C.Y.5    Hao, Y.H.6    Tan, Z.7
  • 77
    • 0033556134 scopus 로고    scopus 로고
    • A DNA polymerase stop assay for G-quadruplex-interactive compounds
    • Han H., Hurley L.H., Salazar M. A DNA polymerase stop assay for G-quadruplex-interactive compounds. Nucleic Acids Res. 1999, 27:537-542.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 537-542
    • Han, H.1    Hurley, L.H.2    Salazar, M.3
  • 78
    • 79957556530 scopus 로고    scopus 로고
    • DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase
    • Paeschke K., Capra J.A., Zakian V.A. DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase. Cell 2011, 145:678-691.
    • (2011) Cell , vol.145 , pp. 678-691
    • Paeschke, K.1    Capra, J.A.2    Zakian, V.A.3
  • 81
    • 76349116980 scopus 로고    scopus 로고
    • Human telomeric G-quadruplex: thermodynamic and kinetic studies of telomeric quadruplex stability
    • Chaires J.B. Human telomeric G-quadruplex: thermodynamic and kinetic studies of telomeric quadruplex stability. FEBS J. 2010, 277:1098-1106.
    • (2010) FEBS J. , vol.277 , pp. 1098-1106
    • Chaires, J.B.1
  • 82
    • 33744944261 scopus 로고    scopus 로고
    • Non-B DNA structure-induced genetic instability
    • Wang G., Vasquez K.M. Non-B DNA structure-induced genetic instability. Mutat. Res. 2006, 598:103-119.
    • (2006) Mutat. Res. , vol.598 , pp. 103-119
    • Wang, G.1    Vasquez, K.M.2
  • 83
    • 0034870407 scopus 로고    scopus 로고
    • Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins
    • Schwartz T., Behlke J., Lowenhaupt K., Heinemann U., Rich A. Structure of the DLM-1-Z-DNA complex reveals a conserved family of Z-DNA-binding proteins. Nat. Struct. Biol. 2001, 8:761-765.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 761-765
    • Schwartz, T.1    Behlke, J.2    Lowenhaupt, K.3    Heinemann, U.4    Rich, A.5
  • 85
    • 37749024291 scopus 로고    scopus 로고
    • 14-3-3 cruciform-binding proteins as regulators of eukaryotic DNA replication
    • Zannis-Hadjopoulos M., Yahyaoui W., Callejo M. 14-3-3 cruciform-binding proteins as regulators of eukaryotic DNA replication. Trends Biochem. Sci. 2008, 33:44-50.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 44-50
    • Zannis-Hadjopoulos, M.1    Yahyaoui, W.2    Callejo, M.3
  • 87
    • 0037064013 scopus 로고    scopus 로고
    • The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307
    • Callejo M., Alvarez D., Price G.B., Zannis-Hadjopoulos M. The 14-3-3 protein homologues from Saccharomyces cerevisiae, Bmh1p and Bmh2p, have cruciform DNA-binding activity and associate in vivo with ARS307. J. Biol. Chem. 2002, 277:38416-38423.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38416-38423
    • Callejo, M.1    Alvarez, D.2    Price, G.B.3    Zannis-Hadjopoulos, M.4
  • 88
    • 79961111848 scopus 로고    scopus 로고
    • Cruciform structures are a common DNA feature important for regulating biological processes
    • Brazda V., Laister R.C., Jagelska E.B., Arrowsmith C. Cruciform structures are a common DNA feature important for regulating biological processes. BMC Mol. Biol. 2011, 12:33.
    • (2011) BMC Mol. Biol. , vol.12 , pp. 33
    • Brazda, V.1    Laister, R.C.2    Jagelska, E.B.3    Arrowsmith, C.4
  • 89
    • 15544366698 scopus 로고    scopus 로고
    • Interplay between human high mobility group protein 1 and replication protein A on psoralen-cross-linked DNA
    • Reddy M.C., Christensen J., Vasquez K.M. Interplay between human high mobility group protein 1 and replication protein A on psoralen-cross-linked DNA. Biochemistry (Mosc.) 2005, 44:4188-4195.
    • (2005) Biochemistry (Mosc.) , vol.44 , pp. 4188-4195
    • Reddy, M.C.1    Christensen, J.2    Vasquez, K.M.3
  • 91
    • 0029840823 scopus 로고    scopus 로고
    • Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism
    • Gunz D., Hess M.T., Naegeli H. Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism. J. Biol. Chem. 1996, 271:25089-25098.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25089-25098
    • Gunz, D.1    Hess, M.T.2    Naegeli, H.3
  • 94
    • 0032742715 scopus 로고    scopus 로고
    • DNA damage recognition during nucleotide excision repair in mammalian cells
    • Wood R.D. DNA damage recognition during nucleotide excision repair in mammalian cells. Biochimie 1999, 81:39-44.
    • (1999) Biochimie , vol.81 , pp. 39-44
    • Wood, R.D.1
  • 95
    • 0023802737 scopus 로고
    • Site-specific oligonucleotide binding represses transcription of the human c-MYC gene in vitro
    • Cooney M., Czernuszewicz G., Postel E.H., Flint S.J., Hogan M.E. Site-specific oligonucleotide binding represses transcription of the human c-MYC gene in vitro. Science 1988, 241:456-459.
    • (1988) Science , vol.241 , pp. 456-459
    • Cooney, M.1    Czernuszewicz, G.2    Postel, E.H.3    Flint, S.J.4    Hogan, M.E.5
  • 96
    • 0030059301 scopus 로고    scopus 로고
    • Mutagenesis in mammalian cells induced by triple helix formation and transcription-coupled repair
    • Wang G., Seidman M.M., Glazer P.M. Mutagenesis in mammalian cells induced by triple helix formation and transcription-coupled repair. Science 1996, 271:802-805.
    • (1996) Science , vol.271 , pp. 802-805
    • Wang, G.1    Seidman, M.M.2    Glazer, P.M.3
  • 97
    • 0035870553 scopus 로고    scopus 로고
    • Detection and determination of oligonucleotide triplex formation-mediated transcription-coupled DNA repair in HeLa nuclear extracts
    • Wang G., Chen Z., Zhang S., Wilson G.L., Jing K. Detection and determination of oligonucleotide triplex formation-mediated transcription-coupled DNA repair in HeLa nuclear extracts. Nucleic Acids Res. 2001, 29:1801-1807.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1801-1807
    • Wang, G.1    Chen, Z.2    Zhang, S.3    Wilson, G.L.4    Jing, K.5
  • 99
    • 20144366765 scopus 로고    scopus 로고
    • Human XPC-hHR23B interacts with XPA-RPA in the recognition of triplex-directed psoralen DNA interstrand crosslinks
    • Thoma B.S., Wakasugi M., Christensen J., Reddy M.C., Vasquez K.M. Human XPC-hHR23B interacts with XPA-RPA in the recognition of triplex-directed psoralen DNA interstrand crosslinks. Nucleic Acids Res. 2005, 33:2993-3001.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 2993-3001
    • Thoma, B.S.1    Wakasugi, M.2    Christensen, J.3    Reddy, M.C.4    Vasquez, K.M.5
  • 100
    • 58749088076 scopus 로고    scopus 로고
    • Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease
    • Christensen L.A., Wang H., Van Houten B., Vasquez K.M. Efficient processing of TFO-directed psoralen DNA interstrand crosslinks by the UvrABC nuclease. Nucleic Acids Res. 2008, 36:7136-7145.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 7136-7145
    • Christensen, L.A.1    Wang, H.2    Van Houten, B.3    Vasquez, K.M.4
  • 101
    • 0035903189 scopus 로고    scopus 로고
    • Involvement of the nucleotide excision repair protein UvrA in instability of CAG*CTG repeat sequences in Escherichia coli
    • Oussatcheva E.A., Hashem V.I., Zou Y., Sinden R.R., Potaman V.N. Involvement of the nucleotide excision repair protein UvrA in instability of CAG*CTG repeat sequences in Escherichia coli. J. Biol. Chem. 2001, 276:30878-30884.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30878-30884
    • Oussatcheva, E.A.1    Hashem, V.I.2    Zou, Y.3    Sinden, R.R.4    Potaman, V.N.5
  • 102
    • 35648978268 scopus 로고    scopus 로고
    • Chromosomal model for analysis of a long CTG/CAG tract stability in wild-type Escherichia coli and its nucleotide excision repair mutants
    • Szwarocka S.T., Staczek P., Parniewski P. Chromosomal model for analysis of a long CTG/CAG tract stability in wild-type Escherichia coli and its nucleotide excision repair mutants. Can. J. Microbiol. 2007, 53:860-868.
    • (2007) Can. J. Microbiol. , vol.53 , pp. 860-868
    • Szwarocka, S.T.1    Staczek, P.2    Parniewski, P.3
  • 103
    • 0033556218 scopus 로고    scopus 로고
    • Nucleotide excision repair affects the stability of long transcribed (CTG*CAG) tracts in an orientation-dependent manner in Escherichia coli
    • Parniewski P., Bacolla A., Jaworski A., Wells R.D. Nucleotide excision repair affects the stability of long transcribed (CTG*CAG) tracts in an orientation-dependent manner in Escherichia coli. Nucleic Acids Res. 1999, 27:616-623.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 616-623
    • Parniewski, P.1    Bacolla, A.2    Jaworski, A.3    Wells, R.D.4
  • 104
    • 0029831389 scopus 로고    scopus 로고
    • The binding of UvrAB proteins to bubble and loop regions in duplex DNA
    • Ahn B., Grossman L. The binding of UvrAB proteins to bubble and loop regions in duplex DNA. J. Biol. Chem. 1996, 271:21462-21470.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21462-21470
    • Ahn, B.1    Grossman, L.2
  • 105
    • 0030742948 scopus 로고    scopus 로고
    • Repair of DNA loops involves DNA-mismatch and nucleotide-excision repair proteins
    • Kirkpatrick D.T., Petes T.D. Repair of DNA loops involves DNA-mismatch and nucleotide-excision repair proteins. Nature 1997, 387:929-931.
    • (1997) Nature , vol.387 , pp. 929-931
    • Kirkpatrick, D.T.1    Petes, T.D.2
  • 106
    • 32244438870 scopus 로고    scopus 로고
    • Transcription promotes contraction of CAG repeat tracts in human cells
    • Lin Y., Dion V., Wilson J.H. Transcription promotes contraction of CAG repeat tracts in human cells. Nat. Struct. Mol. Biol. 2006, 13:179-180.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 179-180
    • Lin, Y.1    Dion, V.2    Wilson, J.H.3
  • 107
    • 34147136044 scopus 로고    scopus 로고
    • CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease
    • Jung J., Bonini N. CREB-binding protein modulates repeat instability in a Drosophila model for polyQ disease. Science 2007, 315:1857-1859.
    • (2007) Science , vol.315 , pp. 1857-1859
    • Jung, J.1    Bonini, N.2
  • 108
    • 34548204316 scopus 로고    scopus 로고
    • Transcription-induced CAG repeat contraction in human cells is mediated in part by transcription-coupled nucleotide excision repair
    • Lin Y., Wilson J.H. Transcription-induced CAG repeat contraction in human cells is mediated in part by transcription-coupled nucleotide excision repair. Mol. Cell. Biol. 2007, 27:6209-6217.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 6209-6217
    • Lin, Y.1    Wilson, J.H.2
  • 109
    • 0027742295 scopus 로고
    • The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer
    • Fishel R., Lescoe M.K., Rao M.R., Copeland N.G., Jenkins N.A., Garber J., Kane M., Kolodner R. The human mutator gene homolog MSH2 and its association with hereditary nonpolyposis colon cancer. Cell 1993, 75:1027-1038.
    • (1993) Cell , vol.75 , pp. 1027-1038
    • Fishel, R.1    Lescoe, M.K.2    Rao, M.R.3    Copeland, N.G.4    Jenkins, N.A.5    Garber, J.6    Kane, M.7    Kolodner, R.8
  • 110
    • 0030882381 scopus 로고    scopus 로고
    • Mutations predisposing to hereditary nonpolyposis colorectal cancer: database and results of a collaborative study. The International Collaborative Group on Hereditary Nonpolyposis Colorectal Cancer
    • Peltomaki P., Vasen H.F. Mutations predisposing to hereditary nonpolyposis colorectal cancer: database and results of a collaborative study. The International Collaborative Group on Hereditary Nonpolyposis Colorectal Cancer. Gastroenterology 1997, 113:1146-1158.
    • (1997) Gastroenterology , vol.113 , pp. 1146-1158
    • Peltomaki, P.1    Vasen, H.F.2
  • 111
    • 1842841660 scopus 로고    scopus 로고
    • Mutations in DNA mismatch repair genes: implications for DNA damage signaling and drug sensitivity (review)
    • Fedier A., Fink D. Mutations in DNA mismatch repair genes: implications for DNA damage signaling and drug sensitivity (review). Int. J. Oncol. 2004, 24:1039-1047.
    • (2004) Int. J. Oncol. , vol.24 , pp. 1039-1047
    • Fedier, A.1    Fink, D.2
  • 113
    • 27144542066 scopus 로고    scopus 로고
    • Crystal structure of a junction between B-DNA and Z-DNA reveals two extruded bases
    • Ha S.C., Lowenhaupt K., Rich A., Kim Y.G., Kim K.K. Crystal structure of a junction between B-DNA and Z-DNA reveals two extruded bases. Nature 2005, 437:1183-1186.
    • (2005) Nature , vol.437 , pp. 1183-1186
    • Ha, S.C.1    Lowenhaupt, K.2    Rich, A.3    Kim, Y.G.4    Kim, K.K.5
  • 114
    • 0031981941 scopus 로고    scopus 로고
    • Biased short tract repair of palindromic loop mismatches in mammalian cells
    • Taghian D.G., Hough H., Nickoloff J.A. Biased short tract repair of palindromic loop mismatches in mammalian cells. Genetics 1998, 148:1257-1268.
    • (1998) Genetics , vol.148 , pp. 1257-1268
    • Taghian, D.G.1    Hough, H.2    Nickoloff, J.A.3
  • 115
    • 0031053578 scopus 로고    scopus 로고
    • Altered replication and inverted repeats induce mismatch repair-independent recombination between highly diverged DNAs in yeast
    • Tran H., Degtyareva N., Gordenin D., Resnick M.A. Altered replication and inverted repeats induce mismatch repair-independent recombination between highly diverged DNAs in yeast. Mol. Cell. Biol. 1997, 17:1027-1036.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1027-1036
    • Tran, H.1    Degtyareva, N.2    Gordenin, D.3    Resnick, M.A.4
  • 116
    • 0035804817 scopus 로고    scopus 로고
    • Repair bias of large loop mismatches during recombination in mammalian cells depends on loop length and structure
    • Bill C.A., Taghian D.G., Duran W.A., Nickoloff J.A. Repair bias of large loop mismatches during recombination in mammalian cells depends on loop length and structure. Mutat. Res. 2001, 485:255-265.
    • (2001) Mutat. Res. , vol.485 , pp. 255-265
    • Bill, C.A.1    Taghian, D.G.2    Duran, W.A.3    Nickoloff, J.A.4
  • 118
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination, and cancer biology
    • Modrich P., Lahue R. Mismatch repair in replication fidelity, genetic recombination, and cancer biology. Annu. Rev. Biochem. 1996, 65:101-133.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 119
    • 0030947319 scopus 로고    scopus 로고
    • Instability of CAG and CTG trinucleotide repeats in Saccharomyces cerevisiae
    • Miret J.J., Pessoa-Brandao L., Lahue R.S. Instability of CAG and CTG trinucleotide repeats in Saccharomyces cerevisiae. Mol. Cell. Biol. 1997, 17:3382-3387.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3382-3387
    • Miret, J.J.1    Pessoa-Brandao, L.2    Lahue, R.S.3
  • 120
    • 0032514711 scopus 로고    scopus 로고
    • Orientation-dependent and sequence-specific expansions of CTG/CAG trinucleotide repeats in Saccharomyces cerevisiae
    • Miret J.J., Pessoa-Brandao L., Lahue R.S. Orientation-dependent and sequence-specific expansions of CTG/CAG trinucleotide repeats in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:12438-12443.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12438-12443
    • Miret, J.J.1    Pessoa-Brandao, L.2    Lahue, R.S.3
  • 121
    • 0032708840 scopus 로고    scopus 로고
    • Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice
    • Manley K., Shirley T.L., Flaherty L., Messer A. Msh2 deficiency prevents in vivo somatic instability of the CAG repeat in Huntington disease transgenic mice. Nat. Genet. 1999, 23:471-473.
    • (1999) Nat. Genet. , vol.23 , pp. 471-473
    • Manley, K.1    Shirley, T.L.2    Flaherty, L.3    Messer, A.4
  • 122
    • 0037081784 scopus 로고    scopus 로고
    • Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins
    • van den Broek W.J., Nelen M.R., Wansink D.G., Coerwinkel M.M., te Riele H., Groenen P.J., Wieringa B. Somatic expansion behaviour of the (CTG)n repeat in myotonic dystrophy knock-in mice is differentially affected by Msh3 and Msh6 mismatch-repair proteins. Hum. Mol. Genet. 2002, 11:191-198.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 191-198
    • van den Broek, W.J.1    Nelen, M.R.2    Wansink, D.G.3    Coerwinkel, M.M.4    te Riele, H.5    Groenen, P.J.6    Wieringa, B.7
  • 123
    • 4444323468 scopus 로고    scopus 로고
    • Pms2 is a genetic enhancer of trinucleotide CAG.CTG repeat somatic mosaicism: implications for the mechanism of triplet repeat expansion
    • Gomes-Pereira M., Fortune M.T., Ingram L., McAbney J.P., Monckton D.G. Pms2 is a genetic enhancer of trinucleotide CAG.CTG repeat somatic mosaicism: implications for the mechanism of triplet repeat expansion. Hum. Mol. Genet. 2004, 13:1815-1825.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1815-1825
    • Gomes-Pereira, M.1    Fortune, M.T.2    Ingram, L.3    McAbney, J.P.4    Monckton, D.G.5
  • 125
    • 14744275872 scopus 로고    scopus 로고
    • MutSalpha binds to and promotes synapsis of transcriptionally activated immunoglobulin switch regions
    • Larson E.D., Duquette M.L., Cummings W.J., Streiff R.J., Maizels N. MutSalpha binds to and promotes synapsis of transcriptionally activated immunoglobulin switch regions. Curr. Biol. 2005, 15:470-474.
    • (2005) Curr. Biol. , vol.15 , pp. 470-474
    • Larson, E.D.1    Duquette, M.L.2    Cummings, W.J.3    Streiff, R.J.4    Maizels, N.5
  • 126
    • 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
  • 127
    • 22144488799 scopus 로고    scopus 로고
    • Mismatch repair participates in error-free processing of DNA interstrand crosslinks in human cells
    • Wu Q., Christensen L.A., Legerski R.J., Vasquez K.M. Mismatch repair participates in error-free processing of DNA interstrand crosslinks in human cells. EMBO Rep. 2005, 6:551-557.
    • (2005) EMBO Rep. , vol.6 , pp. 551-557
    • Wu, Q.1    Christensen, L.A.2    Legerski, R.J.3    Vasquez, K.M.4
  • 128
    • 52949152426 scopus 로고    scopus 로고
    • Human MLH1 protein participates in genomic damage checkpoint signaling in response to DNA interstrand crosslinks, while MSH2 functions in DNA repair
    • Wu Q., Vasquez K.M. Human MLH1 protein participates in genomic damage checkpoint signaling in response to DNA interstrand crosslinks, while MSH2 functions in DNA repair. PLoS Genet. 2008, 4:e1000189.
    • (2008) PLoS Genet. , vol.4
    • Wu, Q.1    Vasquez, K.M.2
  • 129
    • 67650828240 scopus 로고    scopus 로고
    • Mismatch repair and nucleotide excision repair proteins cooperate in the recognition of DNA interstrand crosslinks
    • Zhao J., Jain A., Iyer R.R., Modrich P.L., Vasquez K.M. Mismatch repair and nucleotide excision repair proteins cooperate in the recognition of DNA interstrand crosslinks. Nucleic Acids Res. 2009, 37:4420-4429.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4420-4429
    • Zhao, J.1    Jain, A.2    Iyer, R.R.3    Modrich, P.L.4    Vasquez, K.M.5
  • 130
    • 62349120246 scopus 로고    scopus 로고
    • DNA repair in mammalian cells: base excision repair: the long and short of it
    • Robertson A.B., Klungland A., Rognes T., Leiros I. DNA repair in mammalian cells: base excision repair: the long and short of it. Cell. Mol. Life Sci. 2009, 66:981-993.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 981-993
    • Robertson, A.B.1    Klungland, A.2    Rognes, T.3    Leiros, I.4
  • 132
    • 74249102052 scopus 로고    scopus 로고
    • Stoichiometry of base excision repair proteins correlates with increased somatic CAG instability in striatum over cerebellum in Huntington's disease transgenic mice
    • Goula A.V., Berquist B.R., Wilson D.M., Wheeler V.C., Trottier Y., Merienne K. Stoichiometry of base excision repair proteins correlates with increased somatic CAG instability in striatum over cerebellum in Huntington's disease transgenic mice. PLoS Genet. 2009, 5:e1000749.
    • (2009) PLoS Genet. , vol.5
    • Goula, A.V.1    Berquist, B.R.2    Wilson, D.M.3    Wheeler, V.C.4    Trottier, Y.5    Merienne, K.6
  • 133
    • 84860745933 scopus 로고    scopus 로고
    • The nucleotide sequence, DNA damage location, and protein stoichiometry influence the base excision repair outcome at CAG/CTG repeats
    • Goula A.V., Pearson C.E., Della Maria J., Trottier Y., Tomkinson A.E., Wilson D.M., Merienne K. The nucleotide sequence, DNA damage location, and protein stoichiometry influence the base excision repair outcome at CAG/CTG repeats. Biochemistry (Mosc.) 2012, 51:3919-3932.
    • (2012) Biochemistry (Mosc.) , vol.51 , pp. 3919-3932
    • Goula, A.V.1    Pearson, C.E.2    Della Maria, J.3    Trottier, Y.4    Tomkinson, A.E.5    Wilson, D.M.6    Merienne, K.7
  • 134
    • 2542494916 scopus 로고    scopus 로고
    • Triplet repeat expansion generated by DNA slippage is suppressed by human flap endonuclease 1
    • Ruggiero B.L., Topal M.D. Triplet repeat expansion generated by DNA slippage is suppressed by human flap endonuclease 1. J. Biol. Chem. 2004, 279:23088-23097.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23088-23097
    • Ruggiero, B.L.1    Topal, M.D.2
  • 135
    • 0031965224 scopus 로고    scopus 로고
    • Expansions of CAG repeat tracts are frequent in a yeast mutant defective in Okazaki fragment maturation
    • Schweitzer J.K., Livingston D.M. Expansions of CAG repeat tracts are frequent in a yeast mutant defective in Okazaki fragment maturation. Hum. Mol. Genet. 1998, 7:69-74.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 69-74
    • Schweitzer, J.K.1    Livingston, D.M.2
  • 136
    • 0032488872 scopus 로고    scopus 로고
    • Expansion and length-dependent fragility of CTG repeats in yeast
    • Freudenreich C.H., Kantrow S.M., Zakian V.A. Expansion and length-dependent fragility of CTG repeats in yeast. Science 1998, 279:853-856.
    • (1998) Science , vol.279 , pp. 853-856
    • Freudenreich, C.H.1    Kantrow, S.M.2    Zakian, V.A.3
  • 137
    • 0037201423 scopus 로고    scopus 로고
    • Human FEN-1 can process the 5'-flap DNA of CTG/CAG triplet repeat derived from human genetic diseases by length and sequence dependent manner
    • Lee S., Park M.S. Human FEN-1 can process the 5'-flap DNA of CTG/CAG triplet repeat derived from human genetic diseases by length and sequence dependent manner. Exp. Mol. Med. 2002, 34:313-317.
    • (2002) Exp. Mol. Med. , vol.34 , pp. 313-317
    • Lee, S.1    Park, M.S.2
  • 139
    • 34249337762 scopus 로고    scopus 로고
    • OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells
    • Kovtun I.V., Liu Y., Bjoras M., Klungland A., Wilson S.H., McMurray C.T. OGG1 initiates age-dependent CAG trinucleotide expansion in somatic cells. Nature 2007, 447:447-452.
    • (2007) Nature , vol.447 , pp. 447-452
    • Kovtun, I.V.1    Liu, Y.2    Bjoras, M.3    Klungland, A.4    Wilson, S.H.5    McMurray, C.T.6
  • 140
    • 79960328293 scopus 로고    scopus 로고
    • Cockayne syndrome B protein antagonizes OGG1 in modulating CAG repeat length in vivo
    • Kovtun I.V., Johnson K.O., McMurray C.T. Cockayne syndrome B protein antagonizes OGG1 in modulating CAG repeat length in vivo. Aging (Milano) 2011, 3:509-514.
    • (2011) Aging (Milano) , vol.3 , pp. 509-514
    • Kovtun, I.V.1    Johnson, K.O.2    McMurray, C.T.3
  • 141
    • 79960698114 scopus 로고    scopus 로고
    • Incidence and persistence of 8-oxo-7,8-dihydroguanine within a hairpin intermediate exacerbates a toxic oxidation cycle associated with trinucleotide repeat expansion
    • Jarem D.A., Wilson N.R., Schermerhorn K.M., Delaney S. Incidence and persistence of 8-oxo-7,8-dihydroguanine within a hairpin intermediate exacerbates a toxic oxidation cycle associated with trinucleotide repeat expansion. DNA Repair 2011, 10:887-896.
    • (2011) DNA Repair , vol.10 , pp. 887-896
    • Jarem, D.A.1    Wilson, N.R.2    Schermerhorn, K.M.3    Delaney, S.4
  • 142
    • 65249130164 scopus 로고    scopus 로고
    • Models for chromosomal replication-independent non-B DNA structure-induced genetic instability
    • Wang G., Vasquez K.M. Models for chromosomal replication-independent non-B DNA structure-induced genetic instability. Mol. Carcinog. 2009, 48:286-298.
    • (2009) Mol. Carcinog. , vol.48 , pp. 286-298
    • Wang, G.1    Vasquez, K.M.2
  • 143
    • 30344434641 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ogg1 prevents poly(GT) tract instability in the mitochondrial genome
    • Vongsamphanh R., Wagner J.R., Ramotar D. Saccharomyces cerevisiae Ogg1 prevents poly(GT) tract instability in the mitochondrial genome. DNA Repair 2006, 5:235-242.
    • (2006) DNA Repair , vol.5 , pp. 235-242
    • Vongsamphanh, R.1    Wagner, J.R.2    Ramotar, D.3
  • 144
    • 69249209608 scopus 로고    scopus 로고
    • RecQ helicases: multifunctional genome caretakers
    • Chu W.K., Hickson I.D. RecQ helicases: multifunctional genome caretakers. Nat. Rev. Cancer 2009, 9:644-654.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 644-654
    • Chu, W.K.1    Hickson, I.D.2
  • 145
    • 56449090762 scopus 로고    scopus 로고
    • Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance
    • Bohr V.A. Rising from the RecQ-age: the role of human RecQ helicases in genome maintenance. Trends Biochem. Sci. 2008, 33:609-620.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 609-620
    • Bohr, V.A.1
  • 147
    • 84862996270 scopus 로고    scopus 로고
    • RecQ helicases; at the crossroad of genome replication, repair, and recombination
    • Rezazadeh S. RecQ helicases; at the crossroad of genome replication, repair, and recombination. Mol. Biol. Rep. 2012, 39:4527-4543.
    • (2012) Mol. Biol. Rep. , vol.39 , pp. 4527-4543
    • Rezazadeh, S.1
  • 148
    • 84864499620 scopus 로고    scopus 로고
    • RecQ helicases in DNA double strand break repair and telomere maintenance
    • Singh D.K., Ghosh A.K., Croteau D.L., Bohr V.A. RecQ helicases in DNA double strand break repair and telomere maintenance. Mutat. Res. 2011, 736:15-24.
    • (2011) Mutat. Res. , vol.736 , pp. 15-24
    • Singh, D.K.1    Ghosh, A.K.2    Croteau, D.L.3    Bohr, V.A.4
  • 149
    • 77953024275 scopus 로고    scopus 로고
    • Probing the structural basis of RecQ helicase function
    • Vindigni A., Marino F., Gileadi O. Probing the structural basis of RecQ helicase function. Biophys. Chem. 2010, 149:67-77.
    • (2010) Biophys. Chem. , vol.149 , pp. 67-77
    • Vindigni, A.1    Marino, F.2    Gileadi, O.3
  • 150
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    • Zhang X.D., Dou S.X., Xie P., Hu J.S., Wang P.Y., Xi X.G. Escherichia coli RecQ is a rapid, efficient, and monomeric helicase. J. Biol. Chem. 2006, 281:12655-12663.
    • (2006) J. Biol. Chem. , vol.281 , pp. 12655-12663
    • Zhang, X.D.1    Dou, S.X.2    Xie, P.3    Hu, J.S.4    Wang, P.Y.5    Xi, X.G.6
  • 151
    • 77952108629 scopus 로고    scopus 로고
    • Small scale genetic alterations contribute to increased mutability at the X-linked Hprt locus in vivo in Blm hypomorphic mice
    • Tereshchenko I.V., Chen Y., McDaniel L.D., Schultz R.A., Tischfield J.A., Shao C. Small scale genetic alterations contribute to increased mutability at the X-linked Hprt locus in vivo in Blm hypomorphic mice. DNA Repair 2010, 9:551-557.
    • (2010) DNA Repair , vol.9 , pp. 551-557
    • Tereshchenko, I.V.1    Chen, Y.2    McDaniel, L.D.3    Schultz, R.A.4    Tischfield, J.A.5    Shao, C.6
  • 152
    • 0037179865 scopus 로고    scopus 로고
    • Genetic interaction between the unstable v-Ha-RAS transgene (Tg.AC) and the murine Werner syndrome gene: transgene instability and tumorigenesis
    • Leder A., Lebel M., Zhou F., Fontaine K., Bishop A., Leder P. Genetic interaction between the unstable v-Ha-RAS transgene (Tg.AC) and the murine Werner syndrome gene: transgene instability and tumorigenesis. Oncogene 2002, 21:6657-6668.
    • (2002) Oncogene , vol.21 , pp. 6657-6668
    • Leder, A.1    Lebel, M.2    Zhou, F.3    Fontaine, K.4    Bishop, A.5    Leder, P.6
  • 154
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon F.G., Kowalczykowski S.C. RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev. 1998, 12:1134-1144.
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 155
    • 0035393720 scopus 로고    scopus 로고
    • The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases
    • Mohaghegh P., Karow J.K., Brosh R.M., Bohr V.A., Hickson I.D. The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases. Nucleic Acids Res. 2001, 29:2843-2849.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 2843-2849
    • Mohaghegh, P.1    Karow, J.K.2    Brosh, R.M.3    Bohr, V.A.4    Hickson, I.D.5
  • 156
    • 77955070324 scopus 로고    scopus 로고
    • Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase
    • Nora G.J., Buncher N.A., Opresko P.L. Telomeric protein TRF2 protects Holliday junctions with telomeric arms from displacement by the Werner syndrome helicase. Nucleic Acids Res. 2010, 38:3984-3998.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 3984-3998
    • Nora, G.J.1    Buncher, N.A.2    Opresko, P.L.3
  • 157
    • 0347362703 scopus 로고    scopus 로고
    • Werner syndrome protein contains three structure-specific DNA binding domains
    • von Kobbe C., Thoma N.H., Czyzewski B.K., Pavletich N.P., Bohr V.A. Werner syndrome protein contains three structure-specific DNA binding domains. J. Biol. Chem. 2003, 278:52997-53006.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52997-53006
    • von Kobbe, C.1    Thoma, N.H.2    Czyzewski, B.K.3    Pavletich, N.P.4    Bohr, V.A.5
  • 158
    • 24044521924 scopus 로고    scopus 로고
    • Current advances in unraveling the function of the Werner syndrome protein
    • Ozgenc A., Loeb L.A. Current advances in unraveling the function of the Werner syndrome protein. Mutat. Res. 2005, 577:237-251.
    • (2005) Mutat. Res. , vol.577 , pp. 237-251
    • Ozgenc, A.1    Loeb, L.A.2
  • 159
    • 28544438312 scopus 로고    scopus 로고
    • Identification of RecQL1 as a Holliday junction processing enzyme in human cell lines
    • LeRoy G., Carroll R., Kyin S., Seki M., Cole M.D. Identification of RecQL1 as a Holliday junction processing enzyme in human cell lines. Nucleic Acids Res. 2005, 33:6251-6257.
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6251-6257
    • LeRoy, G.1    Carroll, R.2    Kyin, S.3    Seki, M.4    Cole, M.D.5
  • 160
    • 36249015877 scopus 로고    scopus 로고
    • The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?
    • Mankouri H.W., Hickson I.D. The RecQ helicase-topoisomerase III-Rmi1 complex: a DNA structure-specific 'dissolvasome'?. Trends Biochem. Sci. 2007, 32:538-546.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 538-546
    • Mankouri, H.W.1    Hickson, I.D.2
  • 161
    • 84859699244 scopus 로고    scopus 로고
    • BLM helicase ortholog Sgs1 is a central regulator of meiotic recombination intermediate metabolism
    • De Muyt A., Jessop L., Kolar E., Sourirajan A., Chen J., Dayani Y., Lichten M. BLM helicase ortholog Sgs1 is a central regulator of meiotic recombination intermediate metabolism. Mol. Cell 2012, 46:43-53.
    • (2012) Mol. Cell , vol.46 , pp. 43-53
    • De Muyt, A.1    Jessop, L.2    Kolar, E.3    Sourirajan, A.4    Chen, J.5    Dayani, Y.6    Lichten, M.7
  • 163
    • 79953196154 scopus 로고    scopus 로고
    • Holliday junction-containing DNA structures persist in cells lacking Sgs1 or Top3 following exposure to DNA damage
    • Mankouri H.W., Ashton T.M., Hickson I.D. Holliday junction-containing DNA structures persist in cells lacking Sgs1 or Top3 following exposure to DNA damage. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:4944-4949.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 4944-4949
    • Mankouri, H.W.1    Ashton, T.M.2    Hickson, I.D.3
  • 164
    • 79955456518 scopus 로고    scopus 로고
    • Pathways for Holliday junction processing during homologous recombination in Saccharomyces cerevisiae
    • Ashton T.M., Mankouri H.W., Heidenblut A., McHugh P.J., Hickson I.D. Pathways for Holliday junction processing during homologous recombination in Saccharomyces cerevisiae. Mol. Cell. Biol. 2011, 31:1921-1933.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1921-1933
    • Ashton, T.M.1    Mankouri, H.W.2    Heidenblut, A.3    McHugh, P.J.4    Hickson, I.D.5
  • 165
    • 49049113852 scopus 로고    scopus 로고
    • RecQ and RecG helicases have distinct roles in maintaining the stability of polypurine.polypyrimidine sequences
    • Dixon B.P., Lu L., Chu A., Bissler J.J. RecQ and RecG helicases have distinct roles in maintaining the stability of polypurine.polypyrimidine sequences. Mutat. Res. 2008, 643:20-28.
    • (2008) Mutat. Res. , vol.643 , pp. 20-28
    • Dixon, B.P.1    Lu, L.2    Chu, A.3    Bissler, J.J.4
  • 168
    • 0035844242 scopus 로고    scopus 로고
    • Interactions between the Werner syndrome helicase and DNA polymerase delta specifically facilitate copying of tetraplex and hairpin structures of the d(CGG)n trinucleotide repeat sequence
    • Kamath-Loeb A.S., Loeb L.A., Johansson E., Burgers P.M., Fry M. Interactions between the Werner syndrome helicase and DNA polymerase delta specifically facilitate copying of tetraplex and hairpin structures of the d(CGG)n trinucleotide repeat sequence. J. Biol. Chem. 2001, 276:16439-16446.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16439-16446
    • Kamath-Loeb, A.S.1    Loeb, L.A.2    Johansson, E.3    Burgers, P.M.4    Fry, M.5
  • 169
    • 33646100776 scopus 로고    scopus 로고
    • A conserved G4 DNA binding domain in RecQ family helicases
    • Huber M.D., Duquette M.L., Shiels J.C., Maizels N. A conserved G4 DNA binding domain in RecQ family helicases. J. Mol. Biol. 2006, 358:1071-1080.
    • (2006) J. Mol. Biol. , vol.358 , pp. 1071-1080
    • Huber, M.D.1    Duquette, M.L.2    Shiels, J.C.3    Maizels, N.4
  • 170
    • 18144413898 scopus 로고    scopus 로고
    • In the end, it's all structure
    • Crabbe L., Karlseder J. In the end, it's all structure. Curr. Mol. Med. 2005, 5:135-143.
    • (2005) Curr. Mol. Med. , vol.5 , pp. 135-143
    • Crabbe, L.1    Karlseder, J.2
  • 171
    • 0037142071 scopus 로고    scopus 로고
    • Crystal structure of parallel quadruplexes from human telomeric DNA
    • Parkinson G.N., Lee M.P., Neidle S. Crystal structure of parallel quadruplexes from human telomeric DNA. Nature 2002, 417:876-880.
    • (2002) Nature , vol.417 , pp. 876-880
    • Parkinson, G.N.1    Lee, M.P.2    Neidle, S.3
  • 172
    • 38949094875 scopus 로고    scopus 로고
    • ResQue and preservation-roles for the Werner syndrome protein and other RecQ helicases
    • Opresko P.L., Telomere ResQue and preservation-roles for the Werner syndrome protein and other RecQ helicases. Mech. Ageing Dev. 2008, 129:79-90.
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 79-90
    • Opresko, P.L.1    Telomere2
  • 174
    • 69749106825 scopus 로고    scopus 로고
    • Recruitment of Fanconi anemia and breast cancer proteins to DNA damage sites is differentially governed by replication
    • Shen X., Do H., Li Y., Chung W.H., Tomasz M., de Winter J.P., Xia B., Elledge S.J., Wang W., Li L. Recruitment of Fanconi anemia and breast cancer proteins to DNA damage sites is differentially governed by replication. Mol. Cell 2009, 35:716-723.
    • (2009) Mol. Cell , vol.35 , pp. 716-723
    • Shen, X.1    Do, H.2    Li, Y.3    Chung, W.H.4    Tomasz, M.5    de Winter, J.P.6    Xia, B.7    Elledge, S.J.8    Wang, W.9    Li, L.10
  • 175
    • 77955878471 scopus 로고    scopus 로고
    • Assessing the link between BACH1/FANCJ and MLH1 in DNA crosslink repair
    • Cantor S.B., Xie J. Assessing the link between BACH1/FANCJ and MLH1 in DNA crosslink repair. Environ. Mol. Mutagen. 2010, 51:500-507.
    • (2010) Environ. Mol. Mutagen. , vol.51 , pp. 500-507
    • Cantor, S.B.1    Xie, J.2
  • 176
    • 68349128255 scopus 로고    scopus 로고
    • FANCJ helicase operates in the Fanconi anemia DNA repair pathway and the response to replicational stress
    • Wu Y., Brosh R.M. FANCJ helicase operates in the Fanconi anemia DNA repair pathway and the response to replicational stress. Curr. Mol. Med. 2009, 9:470-482.
    • (2009) Curr. Mol. Med. , vol.9 , pp. 470-482
    • Wu, Y.1    Brosh, R.M.2
  • 177
    • 0036699095 scopus 로고    scopus 로고
    • Disruption of Dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA
    • Cheung I., Schertzer M., Rose A., Lansdorp P.M. Disruption of Dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA. Nat. Genet. 2002, 31:405-409.
    • (2002) Nat. Genet. , vol.31 , pp. 405-409
    • Cheung, I.1    Schertzer, M.2    Rose, A.3    Lansdorp, P.M.4
  • 178
    • 33745407668 scopus 로고    scopus 로고
    • Homologous recombination is required for genome stability in the absence of Dog-1 in Caenorhabditis elegans
    • Youds J.L., O'Neil N.J., Rose A.M. Homologous recombination is required for genome stability in the absence of Dog-1 in Caenorhabditis elegans. Genetics 2006, 173:697-708.
    • (2006) Genetics , vol.173 , pp. 697-708
    • Youds, J.L.1    O'Neil, N.J.2    Rose, A.M.3
  • 179
    • 76749129611 scopus 로고    scopus 로고
    • Unwinding the functions of the Pif1 family helicases
    • Bochman M.L., Sabouri N., Zakian V.A. Unwinding the functions of the Pif1 family helicases. DNA Repair 2010, 9:237-249.
    • (2010) DNA Repair , vol.9 , pp. 237-249
    • Bochman, M.L.1    Sabouri, N.2    Zakian, V.A.3
  • 180
    • 77955809107 scopus 로고    scopus 로고
    • Making sense of G-quadruplex and i-motif functions in oncogene promoters
    • Brooks T.A., Kendrick S., Hurley L. Making sense of G-quadruplex and i-motif functions in oncogene promoters. FEBS J. 2010, 277:3459-3469.
    • (2010) FEBS J. , vol.277 , pp. 3459-3469
    • Brooks, T.A.1    Kendrick, S.2    Hurley, L.3
  • 181
    • 77955487510 scopus 로고    scopus 로고
    • Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity
    • Sanders C.M. Human Pif1 helicase is a G-quadruplex DNA-binding protein with G-quadruplex DNA-unwinding activity. Biochem. J. 2010, 430:119-128.
    • (2010) Biochem. J. , vol.430 , pp. 119-128
    • Sanders, C.M.1
  • 182
    • 79957813857 scopus 로고    scopus 로고
    • Human DHX9 helicase preferentially unwinds RNA-containing displacement loops (R-loops) and G-quadruplexes
    • Chakraborty P., Grosse F. Human DHX9 helicase preferentially unwinds RNA-containing displacement loops (R-loops) and G-quadruplexes. DNA Repair 2011, 10:654-665.
    • (2011) DNA Repair , vol.10 , pp. 654-665
    • Chakraborty, P.1    Grosse, F.2
  • 183
    • 34447093618 scopus 로고    scopus 로고
    • Werner syndrome helicase (WRN), nuclear DNA helicase II (NDH II) and histone gammaH2AX are localized to the centrosome
    • Zhang S., Hemmerich P., Grosse F. Werner syndrome helicase (WRN), nuclear DNA helicase II (NDH II) and histone gammaH2AX are localized to the centrosome. Cell Biol. Int. 2007, 31:1109-1121.
    • (2007) Cell Biol. Int. , vol.31 , pp. 1109-1121
    • Zhang, S.1    Hemmerich, P.2    Grosse, F.3
  • 185
    • 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
  • 186
    • 0029966659 scopus 로고    scopus 로고
    • Unwinding of the third strand of a DNA triple helix, a novel activity of the SV40 large T-antigen helicase
    • Kopel V., Pozner A., Baran N., Manor H. Unwinding of the third strand of a DNA triple helix, a novel activity of the SV40 large T-antigen helicase. Nucleic Acids Res. 1996, 24:330-335.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 330-335
    • Kopel, V.1    Pozner, A.2    Baran, N.3    Manor, H.4
  • 187
    • 84860854071 scopus 로고    scopus 로고
    • RTEL1 dismantles T loops and counteracts telomeric G4-DNA to maintain telomere integrity
    • Vannier J.B., Pavicic-Kaltenbrunner V., Petalcorin M.I., Ding H., Boulton S.J. RTEL1 dismantles T loops and counteracts telomeric G4-DNA to maintain telomere integrity. Cell 2012, 149:795-806.
    • (2012) Cell , vol.149 , pp. 795-806
    • Vannier, J.B.1    Pavicic-Kaltenbrunner, V.2    Petalcorin, M.I.3    Ding, H.4    Boulton, S.J.5
  • 190
    • 4344636050 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Srs2 DNA helicase selectively blocks expansions of trinucleotide repeats
    • Bhattacharyya S., Lahue R.S. Saccharomyces cerevisiae Srs2 DNA helicase selectively blocks expansions of trinucleotide repeats. Mol. Cell. Biol. 2004, 24:7324-7330.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 7324-7330
    • Bhattacharyya, S.1    Lahue, R.S.2
  • 193
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: a molecular perspective
    • Wang J.C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell Biol. 2002, 3:430-440.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 194
    • 0028242701 scopus 로고
    • Site-specific cleavage of a DNA hairpin by topoisomerase II. DNA secondary structure as a determinant of enzyme recognition/cleavage
    • Froelich-Ammon S.J., Gale K.C., Osheroff N. Site-specific cleavage of a DNA hairpin by topoisomerase II. DNA secondary structure as a determinant of enzyme recognition/cleavage. J. Biol. Chem. 1994, 269:7719-7725.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7719-7725
    • Froelich-Ammon, S.J.1    Gale, K.C.2    Osheroff, N.3
  • 195
    • 0026739913 scopus 로고
    • Does cruciform DNA provide a recognition signal for DNA-topoisomerase II?
    • Pognan F., Paoletti C. Does cruciform DNA provide a recognition signal for DNA-topoisomerase II?. Biochimie 1992, 74:1019-1023.
    • (1992) Biochimie , vol.74 , pp. 1019-1023
    • Pognan, F.1    Paoletti, C.2
  • 198
    • 79955092142 scopus 로고    scopus 로고
    • The in vitro fidelity of yeast DNA polymerase delta and polymerase epsilon holoenzymes during dinucleotide microsatellite DNA synthesis
    • Abdulovic A.L., Hile S.E., Kunkel T.A., Eckert K.A. The in vitro fidelity of yeast DNA polymerase delta and polymerase epsilon holoenzymes during dinucleotide microsatellite DNA synthesis. DNA Repair 2011, 10:497-505.
    • (2011) DNA Repair , vol.10 , pp. 497-505
    • Abdulovic, A.L.1    Hile, S.E.2    Kunkel, T.A.3    Eckert, K.A.4
  • 199
    • 0029982353 scopus 로고    scopus 로고
    • In vitro expansion of GGC:GCC repeats: identification of the preferred strand of expansion
    • Ji J., Clegg N.J., Peterson K.R., Jackson A.L., Laird C.D., Loeb L.A. In vitro expansion of GGC:GCC repeats: identification of the preferred strand of expansion. Nucleic Acids Res. 1996, 24:2835-2840.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2835-2840
    • Ji, J.1    Clegg, N.J.2    Peterson, K.R.3    Jackson, A.L.4    Laird, C.D.5    Loeb, L.A.6
  • 201
    • 0037150492 scopus 로고    scopus 로고
    • Cellular roles of DNA polymerase zeta and Rev1 protein
    • Lawrence C.W. Cellular roles of DNA polymerase zeta and Rev1 protein. DNA Repair 2002, 1:425-435.
    • (2002) DNA Repair , vol.1 , pp. 425-435
    • Lawrence, C.W.1
  • 202
    • 33845778588 scopus 로고    scopus 로고
    • Rev1 enhances CAG.CTG repeat stability in Saccharomyces cerevisiae
    • Collins N.S., Bhattacharyya S., Lahue R.S. Rev1 enhances CAG.CTG repeat stability in Saccharomyces cerevisiae. DNA Repair 2007, 6:38-44.
    • (2007) DNA Repair , vol.6 , pp. 38-44
    • Collins, N.S.1    Bhattacharyya, S.2    Lahue, R.S.3
  • 203
    • 0034198471 scopus 로고    scopus 로고
    • Radiation damage to triplex DNA induced by gamma-rays: a footprinting study and Monte Carlo simulation
    • Barone F., Begusova M., La Nave E., Matzeu M., Mazzei F., Sy D. Radiation damage to triplex DNA induced by gamma-rays: a footprinting study and Monte Carlo simulation. Int. J. Radiat. Biol. 2000, 76:731-740.
    • (2000) Int. J. Radiat. Biol. , vol.76 , pp. 731-740
    • Barone, F.1    Begusova, M.2    La Nave, E.3    Matzeu, M.4    Mazzei, F.5    Sy, D.6
  • 205
    • 0025900145 scopus 로고
    • Site-specific intercalation at the triplex-duplex junction induces a conformational change which is detectable by hypersensitivity to diethylpyrocarbonate
    • Collier D.A., Mergny J.L., Thuong N.T., Helene C. Site-specific intercalation at the triplex-duplex junction induces a conformational change which is detectable by hypersensitivity to diethylpyrocarbonate. Nucleic Acids Res. 1991, 19:4219-4224.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4219-4224
    • Collier, D.A.1    Mergny, J.L.2    Thuong, N.T.3    Helene, C.4
  • 207
    • 67949123270 scopus 로고    scopus 로고
    • Base extrusion is found at helical junctions between right- and left-handed forms of DNA and RNA
    • Kim D., Reddy S., Kim D.Y., Rich A., Lee S., Kim K.K., Kim Y.G. Base extrusion is found at helical junctions between right- and left-handed forms of DNA and RNA. Nucleic Acids Res. 2009, 37:4353-4359.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 4353-4359
    • Kim, D.1    Reddy, S.2    Kim, D.Y.3    Rich, A.4    Lee, S.5    Kim, K.K.6    Kim, Y.G.7
  • 208
    • 0030980019 scopus 로고    scopus 로고
    • Structural analysis of Z-Z DNA junctions with A:A and T:T mismatched base pairs by NMR
    • Yang X.L., Wang A.H. Structural analysis of Z-Z DNA junctions with A:A and T:T mismatched base pairs by NMR. Biochemistry (Mosc.) 1997, 36:4258-4267.
    • (1997) Biochemistry (Mosc.) , vol.36 , pp. 4258-4267
    • Yang, X.L.1    Wang, A.H.2
  • 209
    • 0028298247 scopus 로고
    • The ultimate carcinogen of 4-nitroquinoline 1-oxide does not react with Z-DNA and hyperreacts with B-Z junctions
    • Rodolfo C., Lanza A., Tornaletti S., Fronza G., Pedrini A.M. The ultimate carcinogen of 4-nitroquinoline 1-oxide does not react with Z-DNA and hyperreacts with B-Z junctions. Nucleic Acids Res. 1994, 22:314-320.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 314-320
    • Rodolfo, C.1    Lanza, A.2    Tornaletti, S.3    Fronza, G.4    Pedrini, A.M.5
  • 210
    • 0022133407 scopus 로고
    • Chemical probes of DNA conformation: detection of Z-DNA at nucleotide resolution
    • Johnston B.H., Rich A. Chemical probes of DNA conformation: detection of Z-DNA at nucleotide resolution. Cell 1985, 42:713-724.
    • (1985) Cell , vol.42 , pp. 713-724
    • Johnston, B.H.1    Rich, A.2
  • 211
    • 0020022917 scopus 로고
    • The three-dimensional structure of DNA
    • Zimmerman S.B. The three-dimensional structure of DNA. Annu. Rev. Biochem. 1982, 51:395-427.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 395-427
    • Zimmerman, S.B.1
  • 213
    • 67650501195 scopus 로고    scopus 로고
    • Structure-dependent DNA damage and repair in a trinucleotide repeat sequence
    • Jarem D.A., Wilson N.R., Delaney S. Structure-dependent DNA damage and repair in a trinucleotide repeat sequence. Biochemistry (Mosc.) 2009, 48:6655-6663.
    • (2009) Biochemistry (Mosc.) , vol.48 , pp. 6655-6663
    • Jarem, D.A.1    Wilson, N.R.2    Delaney, S.3
  • 214
    • 84861584060 scopus 로고    scopus 로고
    • Promoter G-quadruplex sequences are targets for base oxidation and strand cleavage during hypoxia-induced transcription
    • Clark D.W., Phang T., Edwards M.G., Geraci M.W., Gillespie M.N. Promoter G-quadruplex sequences are targets for base oxidation and strand cleavage during hypoxia-induced transcription. Free Radic. Biol. Med. 2012, 53:51-59.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 51-59
    • Clark, D.W.1    Phang, T.2    Edwards, M.G.3    Geraci, M.W.4    Gillespie, M.N.5
  • 215
    • 33750154642 scopus 로고    scopus 로고
    • Long-distance radical cation transport in DNA: horizontal charge hopping in a dimeric quadruplex
    • Ndlebe T., Schuster G.B. Long-distance radical cation transport in DNA: horizontal charge hopping in a dimeric quadruplex. Org. Biomol. Chem. 2006, 4:4015-4021.
    • (2006) Org. Biomol. Chem. , vol.4 , pp. 4015-4021
    • Ndlebe, T.1    Schuster, G.B.2
  • 216
    • 0344198178 scopus 로고    scopus 로고
    • Charge transport in DNA duplex/quadruplex conjugates
    • Delaney S., Barton J.K. Charge transport in DNA duplex/quadruplex conjugates. Biochemistry (Mosc.) 2003, 42:14159-14165.
    • (2003) Biochemistry (Mosc.) , vol.42 , pp. 14159-14165
    • Delaney, S.1    Barton, J.K.2
  • 218
    • 0021194150 scopus 로고
    • Ring-opened alkylated guanine is not repaired in Z-DNA
    • Lagravere C., Malfoy B., Leng M., Laval J. Ring-opened alkylated guanine is not repaired in Z-DNA. Nature 1984, 310:798-800.
    • (1984) Nature , vol.310 , pp. 798-800
    • Lagravere, C.1    Malfoy, B.2    Leng, M.3    Laval, J.4
  • 219
    • 0022273752 scopus 로고
    • The Escherichia coli O6-methylguanine-DNA methyltransferase does not repair promutagenic O6-methylguanine residues when present in Z-DNA
    • Boiteux S., Costa de Oliveira R., Laval J. The Escherichia coli O6-methylguanine-DNA methyltransferase does not repair promutagenic O6-methylguanine residues when present in Z-DNA. J. Biol. Chem. 1985, 260:8711-8715.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8711-8715
    • Boiteux, S.1    Costa de Oliveira, R.2    Laval, J.3
  • 220
    • 0021893277 scopus 로고
    • Repair of O6-methylguanine, by mammalian cell extracts, in alkylated DNA and poly(dG-m5dC).(poly dG-m5dC) in B and Z forms
    • Boiteux S., Laval F. Repair of O6-methylguanine, by mammalian cell extracts, in alkylated DNA and poly(dG-m5dC).(poly dG-m5dC) in B and Z forms. Carcinogenesis 1985, 6:805-807.
    • (1985) Carcinogenesis , vol.6 , pp. 805-807
    • Boiteux, S.1    Laval, F.2
  • 221
    • 0346097741 scopus 로고
    • Psoralen-crosslinked secondary structure map of single-stranded virus DNA
    • Shen C.K., Hearst J.E. Psoralen-crosslinked secondary structure map of single-stranded virus DNA. Proc. Natl. Acad. Sci. U. S. A. 1976, 73:2649-2653.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 2649-2653
    • Shen, C.K.1    Hearst, J.E.2
  • 222
    • 67649948771 scopus 로고    scopus 로고
    • DNA repair and DNA triplet repeat expansion: the impact of abasic lesions on triplet repeat DNA energetics
    • Volker J., Plum G.E., Klump H.H., Breslauer K.J. DNA repair and DNA triplet repeat expansion: the impact of abasic lesions on triplet repeat DNA energetics. J. Am. Chem. Soc. 2009, 131:9354-9360.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 9354-9360
    • Volker, J.1    Plum, G.E.2    Klump, H.H.3    Breslauer, K.J.4
  • 223
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8. A resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8. A resolution. Nature 1997, 389:251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 224
    • 52949145609 scopus 로고    scopus 로고
    • Friedreich's ataxia GAA.TTC duplex and GAA.GAA.TTC triplex structures exclude nucleosome assembly
    • Ruan H., Wang Y.H. Friedreich's ataxia GAA.TTC duplex and GAA.GAA.TTC triplex structures exclude nucleosome assembly. J. Mol. Biol. 2008, 383:292-300.
    • (2008) J. Mol. Biol. , vol.383 , pp. 292-300
    • Ruan, H.1    Wang, Y.H.2
  • 225
    • 0029016341 scopus 로고
    • Triple helix DNA alters nucleosomal histone-DNA interactions and acts as a nucleosome barrier
    • Westin L., Blomquist P., Milligan J.F., Wrange O. Triple helix DNA alters nucleosomal histone-DNA interactions and acts as a nucleosome barrier. Nucleic Acids Res. 1995, 23:2184-2191.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2184-2191
    • Westin, L.1    Blomquist, P.2    Milligan, J.F.3    Wrange, O.4
  • 226
    • 0032542023 scopus 로고    scopus 로고
    • Triple-helix formation at different positions on nucleosomal DNA
    • Brown P.M., Madden C.A., Fox K.R. Triple-helix formation at different positions on nucleosomal DNA. Biochemistry (Mosc.) 1998, 37:16139-16151.
    • (1998) Biochemistry (Mosc.) , vol.37 , pp. 16139-16151
    • Brown, P.M.1    Madden, C.A.2    Fox, K.R.3
  • 227
    • 0032527766 scopus 로고    scopus 로고
    • DNA triple-helix formation on nucleosome-bound poly(dA).poly(dT) tracts
    • Brown P.M., Fox K.R. DNA triple-helix formation on nucleosome-bound poly(dA).poly(dT) tracts. Biochem. J. 1998, 333(Pt 2):259-267.
    • (1998) Biochem. J. , vol.333 , Issue.PART 2 , pp. 259-267
    • Brown, P.M.1    Fox, K.R.2
  • 228
    • 0033119030 scopus 로고    scopus 로고
    • DNA triple-helix formation on nucleosome core particles. Effect of length of the oligopurine tract
    • Brown P.M., Fox K.R. DNA triple-helix formation on nucleosome core particles. Effect of length of the oligopurine tract. Eur. J. Biochem./FEBS 1999, 261:301-310.
    • (1999) Eur. J. Biochem./FEBS , vol.261 , pp. 301-310
    • Brown, P.M.1    Fox, K.R.2
  • 229
    • 0029753770 scopus 로고    scopus 로고
    • Formation of triple-stranded DNA at d(GA.TC)n sequences prevents nucleosome assembly and is hindered by nucleosomes
    • Espinas M.L., Jimenez-Garcia E., Martinez-Balbas A., Azorin F. Formation of triple-stranded DNA at d(GA.TC)n sequences prevents nucleosome assembly and is hindered by nucleosomes. J. Biol. Chem. 1996, 271:31807-31812.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31807-31812
    • Espinas, M.L.1    Jimenez-Garcia, E.2    Martinez-Balbas, A.3    Azorin, F.4
  • 230
    • 33847787053 scopus 로고    scopus 로고
    • Characterization of Z-DNA as a nucleosome-boundary element in yeast Saccharomyces cerevisiae
    • Wong B., Chen S., Kwon J.A., Rich A. Characterization of Z-DNA as a nucleosome-boundary element in yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:2229-2234.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2229-2234
    • Wong, B.1    Chen, S.2    Kwon, J.A.3    Rich, A.4
  • 231
    • 0031588962 scopus 로고    scopus 로고
    • CpG methylation remodels chromatin structure in vitro
    • Davey C., Pennings S., Allan J. CpG methylation remodels chromatin structure in vitro. J. Mol. Biol. 1997, 267:276-288.
    • (1997) J. Mol. Biol. , vol.267 , pp. 276-288
    • Davey, C.1    Pennings, S.2    Allan, J.3
  • 232
    • 14244266721 scopus 로고    scopus 로고
    • Effect of CAT or AGG interruptions and CpG methylation on nucleosome assembly upon trinucleotide repeats on spinocerebellar ataxia, type 1 and fragile X syndrome
    • Mulvihill D.J., Nichol Edamura K., Hagerman K.A., Pearson C.E., Wang Y.H. Effect of CAT or AGG interruptions and CpG methylation on nucleosome assembly upon trinucleotide repeats on spinocerebellar ataxia, type 1 and fragile X syndrome. J. Biol. Chem. 2005, 280:4498-4503.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4498-4503
    • Mulvihill, D.J.1    Nichol Edamura, K.2    Hagerman, K.A.3    Pearson, C.E.4    Wang, Y.H.5
  • 233
    • 0029744342 scopus 로고    scopus 로고
    • Nucleosome assembly on methylated CGG triplet repeats in the fragile X mental retardation gene 1 promoter
    • Godde J.S., Kass S.U., Hirst M.C., Wolffe A.P. Nucleosome assembly on methylated CGG triplet repeats in the fragile X mental retardation gene 1 promoter. J. Biol. Chem. 1996, 271:24325-24328.
    • (1996) J. Biol. Chem. , vol.271 , pp. 24325-24328
    • Godde, J.S.1    Kass, S.U.2    Hirst, M.C.3    Wolffe, A.P.4
  • 234
    • 72949086633 scopus 로고    scopus 로고
    • Stable G-quadruplexes are found outside nucleosome-bound regions
    • Wong H.M., Huppert J.L., Stable G-quadruplexes are found outside nucleosome-bound regions. Mol. Biosyst. 2009, 5:1713-1719.
    • (2009) Mol. Biosyst. , vol.5 , pp. 1713-1719
    • Wong, H.M.1    Huppert, J.L.2
  • 236
    • 0028932050 scopus 로고
    • Expanded CTG triplet blocks from the myotonic dystrophy gene create the strongest known natural nucleosome positioning elements
    • Wang Y.H., Griffith J. Expanded CTG triplet blocks from the myotonic dystrophy gene create the strongest known natural nucleosome positioning elements. Genomics 1995, 25:570-573.
    • (1995) Genomics , vol.25 , pp. 570-573
    • Wang, Y.H.1    Griffith, J.2
  • 237
    • 0027941198 scopus 로고
    • Preferential nucleosome assembly at DNA triplet repeats from the myotonic dystrophy gene
    • Wang Y.H., Amirhaeri S., Kang S., Wells R.D., Griffith J.D. Preferential nucleosome assembly at DNA triplet repeats from the myotonic dystrophy gene. Science 1994, 265:669-671.
    • (1994) Science , vol.265 , pp. 669-671
    • Wang, Y.H.1    Amirhaeri, S.2    Kang, S.3    Wells, R.D.4    Griffith, J.D.5
  • 239
    • 0029059218 scopus 로고
    • Triplet repeat expansion in myotonic dystrophy alters the adjacent chromatin structure
    • Otten A.D., Tapscott S.J. Triplet repeat expansion in myotonic dystrophy alters the adjacent chromatin structure. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:5465-5469.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 5465-5469
    • Otten, A.D.1    Tapscott, S.J.2
  • 240
    • 0344054184 scopus 로고
    • In Z-DNA the sequence G-C-G-C is neither methylated by Hha I methyltransferase nor cleaved by Hha I restriction endonuclease
    • Vardimon L., Rich A. In Z-DNA the sequence G-C-G-C is neither methylated by Hha I methyltransferase nor cleaved by Hha I restriction endonuclease. Proc. Natl. Acad. Sci. U. S. A. 1984, 81:3268-3272.
    • (1984) Proc. Natl. Acad. Sci. U. S. A. , vol.81 , pp. 3268-3272
    • Vardimon, L.1    Rich, A.2
  • 241
    • 33645777446 scopus 로고    scopus 로고
    • CpG island methylation in human lymphocytes is highly correlated with DNA sequence, repeats, and predicted DNA structure
    • Bock C., Paulsen M., Tierling S., Mikeska T., Lengauer T., Walter J. CpG island methylation in human lymphocytes is highly correlated with DNA sequence, repeats, and predicted DNA structure. PLoS Genet. 2006, 2:e26.
    • (2006) PLoS Genet. , vol.2
    • Bock, C.1    Paulsen, M.2    Tierling, S.3    Mikeska, T.4    Lengauer, T.5    Walter, J.6
  • 242
    • 37849002353 scopus 로고    scopus 로고
    • Naturally extended CT. AG repeats increase H-DNA structures and promoter activity in the smooth muscle myosin light chain kinase gene
    • Han Y.J., de Lanerolle P. Naturally extended CT. AG repeats increase H-DNA structures and promoter activity in the smooth muscle myosin light chain kinase gene. Mol. Cell. Biol. 2008, 28:863-872.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 863-872
    • Han, Y.J.1    de Lanerolle, P.2


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