메뉴 건너뛰기




Volumn 379, Issue 3, 2008, Pages 492-504

Characterization of Dnmt3b:Thymine-DNA Glycosylase Interaction and Stimulation of Thymine Glycosylase-Mediated Repair by DNA Methyltransferase(s) and RNA

Author keywords

base excision repair; DNA methyltransferase; glycosylase; heterochromatin

Indexed keywords

DNA METHYLTRANSFERASE; DNA METHYLTRANSFERASE 3B; RNA METHYLTRANSFERASE; THYMINE DNA GLYCOSYLASE;

EID: 43449097507     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.02.049     Document Type: Article
Times cited : (47)

References (56)
  • 2
    • 0033385702 scopus 로고    scopus 로고
    • CpG methylation reduces genomic instability
    • R. Rizwana P.J. Hahn CpG methylation reduces genomic instability J. Cell Sci. 112 1999 4513 4519
    • (1999) J. Cell Sci. , vol.112 , pp. 4513-4519
    • Rizwana, R.1    Hahn, P.J.2
  • 3
    • 0036733675 scopus 로고    scopus 로고
    • Chromatin modification and epigenetic reprogramming in mammalian development
    • E. Li Chromatin modification and epigenetic reprogramming in mammalian development Nat. Rev. Genet. 3 2002 662 673
    • (2002) Nat. Rev. Genet. , vol.3 , pp. 662-673
    • Li, E.1
  • 4
    • 0033615717 scopus 로고    scopus 로고
    • DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development
    • M. Okano D.W. Bell D.A. Haber E. Li DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo methylation and mammalian development Cell 99 1999 247 257
    • (1999) Cell , vol.99 , pp. 247-257
    • Okano, M.1    Bell, D.W.2    Haber, D.A.3    Li, E.4
  • 5
    • 0031860739 scopus 로고    scopus 로고
    • Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases
    • M. Okano S. Xie E. Li Cloning and characterization of a family of novel mammalian DNA (cytosine-5) methyltransferases Nat. Genet. 19 1998 219 220
    • (1998) Nat. Genet. , vol.19 , pp. 219-220
    • Okano, M.1    Xie, S.2    Li, E.3
  • 6
    • 0033499867 scopus 로고    scopus 로고
    • In vivo activity of murine de novo methyltransferases, Dnmt3a and Dnmt3b
    • C.L. Hsieh In vivo activity of murine de novo methyltransferases, Dnmt3a and Dnmt3b Mol. Cell. Biol. 19 1999 8211 8218
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8211-8218
    • Hsieh, C.L.1
  • 7
    • 4744366752 scopus 로고    scopus 로고
    • The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA methylation to the major satellite repeats at pericentric heterochromatin
    • T. Chen N. Tsujimoto E. Li The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA methylation to the major satellite repeats at pericentric heterochromatin Mol. Cell. Biol. 24 2004 9048 9058
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9048-9058
    • Chen, T.1    Tsujimoto, N.2    Li, E.3
  • 9
    • 0018672228 scopus 로고
    • Multibranched chromosomes 1, 9, and 16 in a patient with combined IgA and IgE deficiency
    • L. Tiepolo P. Maraschio G. Gimelli C. Cuoco G.F. Gargani C. Romano Multibranched chromosomes 1, 9, and 16 in a patient with combined IgA and IgE deficiency Hum. Genet. 51 1979 127 137
    • (1979) Hum. Genet. , vol.51 , pp. 127-137
    • Tiepolo, L.1    Maraschio, P.2    Gimelli, G.3    Cuoco, C.4    Gargani, G.F.5    Romano, C.6
  • 11
    • 0033547330 scopus 로고    scopus 로고
    • Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene
    • G.L. Xu T.H. Bestor D. Bourc'his C.L. Hsieh N. Tommerup M. Bugge Chromosome instability and immunodeficiency syndrome caused by mutations in a DNA methyltransferase gene Nature 402 1999 187 191
    • (1999) Nature , vol.402 , pp. 187-191
    • Xu, G.L.1    Bestor, T.H.2    Bourc'his, D.3    Hsieh, C.L.4    Tommerup, N.5    Bugge, M.6
  • 13
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • T. Lindahl Instability and decay of the primary structure of DNA Nature 362 1993 709 715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 14
    • 0028358421 scopus 로고
    • The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA
    • J. Shen W. Rideout 3rd P. Jones The rate of hydrolytic deamination of 5-methylcytosine in double-stranded DNA Nucleic Acids Res. 22 1994 972 976
    • (1994) Nucleic Acids Res. , vol.22 , pp. 972-976
    • Shen, J.1    Rideout, W.2    Jones, P.3
  • 15
    • 0034930217 scopus 로고    scopus 로고
    • Base excision repair in a network of defence and tolerance
    • H. Nilsen H.E. Krokan Base excision repair in a network of defence and tolerance Carcinogenesis 22 2001 987 998
    • (2001) Carcinogenesis , vol.22 , pp. 987-998
    • Nilsen, H.1    Krokan, H.E.2
  • 16
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway
    • R.A. Bennett D.M. Wilson 3rd D. Wong B. Demple Interaction of human apurinic endonuclease and DNA polymerase beta in the base excision repair pathway Proc. Natl Acad. Sci. USA 94 1997 7166 7169
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.1    Wilson, D.M.2    Wong, D.3    Demple, B.4
  • 17
    • 0024541790 scopus 로고
    • In vitro correction of G·T mispairs to G·C pairs in nuclear extracts from human cells
    • K. Wiebauer J. Jiricny In vitro correction of G·T mispairs to G·C pairs in nuclear extracts from human cells Nature 339 1989 234 236
    • (1989) Nature , vol.339 , pp. 234-236
    • Wiebauer, K.1    Jiricny, J.2
  • 18
    • 0027383758 scopus 로고
    • The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells
    • P. Neddermann J. Jiricny The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells J. Biol. Chem. 268 1993 21218 21224
    • (1993) J. Biol. Chem. , vol.268 , pp. 21218-21224
    • Neddermann, P.1    Jiricny, J.2
  • 20
    • 0029824077 scopus 로고    scopus 로고
    • Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts
    • F.L. Chung H.J. Chen R.G. Nath Lipid peroxidation as a potential endogenous source for the formation of exocyclic DNA adducts Carcinogenesis 17 1996 2105 2111
    • (1996) Carcinogenesis , vol.17 , pp. 2105-2111
    • Chung, F.L.1    Chen, H.J.2    Nath, R.G.3
  • 21
    • 0032555065 scopus 로고    scopus 로고
    • 3,N4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase
    • 4-ethenocytosine, a highly mutagenic adduct, is a primary substrate for Escherichia coli double-stranded uracil-DNA glycosylase and human mismatch-specific thymine-DNA glycosylase Proc. Natl Acad. Sci. USA 95 1998 8508 8513
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 8508-8513
    • Saparbaev, M.1    Laval, J.2
  • 22
    • 0027756934 scopus 로고
    • Incision at DNA G·T mispairs by extracts of mammalian cells occurs preferentially at cytosine methylation sites and is not targeted by a separate G·T binding reaction
    • S. Griffin P. Karran Incision at DNA G·T mispairs by extracts of mammalian cells occurs preferentially at cytosine methylation sites and is not targeted by a separate G·T binding reaction Biochemistry 32 1993 13032 13039
    • (1993) Biochemistry , vol.32 , pp. 13032-13039
    • Griffin, S.1    Karran, P.2
  • 23
    • 0029794522 scopus 로고    scopus 로고
    • Base analog and neighboring base effects on substrate specificity of recombinant human G:T mismatch-specific thymine DNA-glycosylase
    • U. Sibghat P. Gallinari Y.Z. Xu M.F. Goodman L.B. Bloom J. Jiricny R.S. Day 3rd Base analog and neighboring base effects on substrate specificity of recombinant human G:T mismatch-specific thymine DNA-glycosylase Biochemistry 35 1996 12926 12932
    • (1996) Biochemistry , vol.35 , pp. 12926-12932
    • Sibghat, U.1    Gallinari, P.2    Xu, Y.Z.3    Goodman, M.F.4    Bloom, L.B.5    Jiricny, J.6    Day, R.S.7
  • 24
    • 0032493637 scopus 로고    scopus 로고
    • Kinetics of the action of thymine DNA glycosylase
    • T.R. Waters P.F. Swann Kinetics of the action of thymine DNA glycosylase J. Biol. Chem. 273 1998 20007 20014
    • (1998) J. Biol. Chem. , vol.273 , pp. 20007-20014
    • Waters, T.R.1    Swann, P.F.2
  • 25
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • B. Hendrich U. Hardeland H.H. Ng J. Jiricny A. Bird The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites Nature 401 1999 301 304
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3    Jiricny, J.4    Bird, A.5
  • 27
    • 18944404300 scopus 로고    scopus 로고
    • The thymine DNA glycosylase MBD4 represses transcription and is associated with methylated p16INK4a and hMLH1 genes
    • INK4a and hMLH1 genes Mol. Cell. Biol. 25 2005 4388 4396
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4388-4396
    • Kondo, E.1    Gu, Z.2    Horii, A.3    Fukushige, S.4
  • 28
    • 0242363151 scopus 로고    scopus 로고
    • Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin
    • S. Watanabe T. Ichimura N. Fujita S. Tsuruzoe I. Ohki M. Shirakawa Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin Proc. Natl Acad. Sci. USA 100 2003 12859 12864
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 12859-12864
    • Watanabe, S.1    Ichimura, T.2    Fujita, N.3    Tsuruzoe, S.4    Ohki, I.5    Shirakawa, M.6
  • 29
    • 0141755305 scopus 로고    scopus 로고
    • T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha
    • D. Chen M.J. Lucey F. Phoenix J. Lopez-Garcia S.M. Hart R. Losson T:G mismatch-specific thymine-DNA glycosylase potentiates transcription of estrogen-regulated genes through direct interaction with estrogen receptor alpha J. Biol. Chem. 278 2003 38586 38592
    • (2003) J. Biol. Chem. , vol.278 , pp. 38586-38592
    • Chen, D.1    Lucey, M.J.2    Phoenix, F.3    Lopez-Garcia, J.4    Hart, S.M.5    Losson, R.6
  • 30
    • 28544432100 scopus 로고    scopus 로고
    • T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif
    • M.J. Lucey D. Chen J. Lopez-Garcia S.M. Hart F. Phoenix R. Al-Jehani T:G mismatch-specific thymine-DNA glycosylase (TDG) as a coregulator of transcription interacts with SRC1 family members through a novel tyrosine repeat motif Nucleic Acids Res. 33 2005 6393 6404
    • (2005) Nucleic Acids Res. , vol.33 , pp. 6393-6404
    • Lucey, M.J.1    Chen, D.2    Lopez-Garcia, J.3    Hart, S.M.4    Phoenix, F.5    Al-Jehani, R.6
  • 31
    • 0036184090 scopus 로고    scopus 로고
    • Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription
    • M. Tini A. Benecke S.J. Um J. Torchia R.M. Evans P. Chambon Association of CBP/p300 acetylase and thymine DNA glycosylase links DNA repair and transcription Mol. Cell 9 2002 265 277
    • (2002) Mol. Cell , vol.9 , pp. 265-277
    • Tini, M.1    Benecke, A.2    Um, S.J.3    Torchia, J.4    Evans, R.M.5    Chambon, P.6
  • 32
    • 0035823623 scopus 로고    scopus 로고
    • The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription
    • C. Missero M.T. Pirro S. Simeone M. Pischetola R. Di Lauro The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription J. Biol. Chem. 276 2001 33569 33575
    • (2001) J. Biol. Chem. , vol.276 , pp. 33569-33575
    • Missero, C.1    Pirro, M.T.2    Simeone, S.3    Pischetola, M.4    Di Lauro, R.5
  • 34
    • 0036176982 scopus 로고    scopus 로고
    • The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds
    • C. Qiu K. Sawada X. Zhang X. Cheng The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds Nat. Struct. Biol. 9 2002 217 224
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 217-224
    • Qiu, C.1    Sawada, K.2    Zhang, X.3    Cheng, X.4
  • 35
    • 0035943709 scopus 로고    scopus 로고
    • Dnmt3a and Dnmt3b are transcriptional repressors that exhibit unique localization properties to heterochromatin
    • K.E. Bachman M.R. Rountree S.B. Baylin Dnmt3a and Dnmt3b are transcriptional repressors that exhibit unique localization properties to heterochromatin J. Biol. Chem. 276 2001 32282 32287
    • (2001) J. Biol. Chem. , vol.276 , pp. 32282-32287
    • Bachman, K.E.1    Rountree, M.R.2    Baylin, S.B.3
  • 36
    • 0034603990 scopus 로고    scopus 로고
    • The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation?
    • I. Stec S.B. Nagl G.J. van Ommen J.T. den Dunnen The PWWP domain: a potential protein–protein interaction domain in nuclear proteins influencing differentiation? FEBS Lett. 473 2000 1 5
    • (2000) FEBS Lett. , vol.473 , pp. 1-5
    • Stec, I.1    Nagl, S.B.2    van Ommen, G.J.3    den Dunnen, J.T.4
  • 37
    • 33846909036 scopus 로고    scopus 로고
    • Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair
    • Y.Q. Li P.Z. Zhou X.D. Zheng C.P. Walsh G.L. Xu Association of Dnmt3a and thymine DNA glycosylase links DNA methylation with base-excision repair Nucleic Acids Res. 35 2007 390 400
    • (2007) Nucleic Acids Res. , vol.35 , pp. 390-400
    • Li, Y.Q.1    Zhou, P.Z.2    Zheng, X.D.3    Walsh, C.P.4    Xu, G.L.5
  • 38
    • 0036933456 scopus 로고    scopus 로고
    • Structural basis of ICF-causing mutations in the methyltransferase domain of DNMT3B
    • I. Lappalainen M. Vihinen Structural basis of ICF-causing mutations in the methyltransferase domain of DNMT3B Protein Eng. 15 2002 1005 1014
    • (2002) Protein Eng. , vol.15 , pp. 1005-1014
    • Lappalainen, I.1    Vihinen, M.2
  • 39
    • 0031792779 scopus 로고    scopus 로고
    • Identification and characterization of a family of mammalian methyl-CpG binding proteins
    • B. Hendrich A. Bird Identification and characterization of a family of mammalian methyl-CpG binding proteins Mol. Cell. Biol. 18 1998 6538 6547
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6538-6547
    • Hendrich, B.1    Bird, A.2
  • 40
    • 0025314841 scopus 로고
    • Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G·T mispairs in nuclear extracts from human cells
    • K. Wiebauer J. Jiricny Mismatch-specific thymine DNA glycosylase and DNA polymerase beta mediate the correction of G·T mispairs in nuclear extracts from human cells Proc. Natl Acad. Sci. USA 87 1990 5842 5845
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5842-5845
    • Wiebauer, K.1    Jiricny, J.2
  • 41
    • 0042132027 scopus 로고    scopus 로고
    • Establishment and maintenance of genomic methylation patterns in mouse embryonic stem cells by Dnmt3a and Dnmt3b
    • T. Chen Y. Ueda J.E. Dodge Z. Wang E. Li Establishment and maintenance of genomic methylation patterns in mouse embryonic stem cells by Dnmt3a and Dnmt3b Mol. Cell. Biol. 23 2003 5594 5605
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5594-5605
    • Chen, T.1    Ueda, Y.2    Dodge, J.E.3    Wang, Z.4    Li, E.5
  • 42
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • M. Zuker Mfold web server for nucleic acid folding and hybridization prediction Nucleic Acids Res. 31 2003 3406 3415
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3406-3415
    • Zuker, M.1
  • 43
    • 0026708177 scopus 로고
    • Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
    • E. Li T.H. Bestor R. Jaenisch Targeted mutation of the DNA methyltransferase gene results in embryonic lethality Cell 69 1992 915 926
    • (1992) Cell , vol.69 , pp. 915-926
    • Li, E.1    Bestor, T.H.2    Jaenisch, R.3
  • 44
    • 0021770949 scopus 로고
    • DNA methylation. Inhibition of de novo and maintenance methylation in vitro by RNA and synthetic polynucleotides
    • A. Bolden C. Ward J.A. Siedlecki A. Weissbach DNA methylation. Inhibition of de novo and maintenance methylation in vitro by RNA and synthetic polynucleotides J. Biol. Chem. 259 1984 12437 12443
    • (1984) J. Biol. Chem. , vol.259 , pp. 12437-12443
    • Bolden, A.1    Ward, C.2    Siedlecki, J.A.3    Weissbach, A.4
  • 45
    • 34547101263 scopus 로고    scopus 로고
    • Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2
    • U. Hardeland C. Kunz F. Focke M. Szadkowski P. Schar Cell cycle regulation as a mechanism for functional separation of the apparently redundant uracil DNA glycosylases TDG and UNG2 Nucleic Acids Res 35 2007 3859 3867
    • (2007) Nucleic Acids Res , vol.35 , pp. 3859-3867
    • Hardeland, U.1    Kunz, C.2    Focke, F.3    Szadkowski, M.4    Schar, P.5
  • 46
    • 0034766776 scopus 로고    scopus 로고
    • Mammalian DNA methyltransferases show different subnuclear distributions
    • J.B. Margot M.C. Cardoso H. Leonhardt Mammalian DNA methyltransferases show different subnuclear distributions J. Cell. Biochem. 83 2001 373 379
    • (2001) J. Cell. Biochem. , vol.83 , pp. 373-379
    • Margot, J.B.1    Cardoso, M.C.2    Leonhardt, H.3
  • 49
    • 0034625141 scopus 로고    scopus 로고
    • 5-Methylcytosine-DNA glycosylase activity is present in a cloned G/T mismatch DNA glycosylase associated with the chicken embryo DNA demethylation complex
    • B. Zhu Y. Zheng D. Hess H. Angliker S. Schwarz M. Siegmann 5-Methylcytosine-DNA glycosylase activity is present in a cloned G/T mismatch DNA glycosylase associated with the chicken embryo DNA demethylation complex Proc. Natl Acad. Sci. USA 97 2000 5135 5139
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 5135-5139
    • Zhu, B.1    Zheng, Y.2    Hess, D.3    Angliker, H.4    Schwarz, S.5    Siegmann, M.6
  • 50
    • 1842289276 scopus 로고    scopus 로고
    • The RNA moiety of chick embryo 5-methylcytosine-DNA glycosylase targets DNA demethylation
    • J.P. Jost M. Fremont M. Siegmann J. Hofsteenge The RNA moiety of chick embryo 5-methylcytosine-DNA glycosylase targets DNA demethylation Nucleic Acids Res. 25 1997 4545 4550
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4545-4550
    • Jost, J.P.1    Fremont, M.2    Siegmann, M.3    Hofsteenge, J.4
  • 51
    • 0345467527 scopus 로고    scopus 로고
    • Demethylation of DNA by purified chick embryo 5-methylcytosine-DNA glycosylase requires both protein and RNA
    • M. Fremont M. Siegmann S. Gaulis R. Matthies D. Hess J.P. Jost Demethylation of DNA by purified chick embryo 5-methylcytosine-DNA glycosylase requires both protein and RNA Nucleic Acids Res. 25 1997 2375 2380
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2375-2380
    • Fremont, M.1    Siegmann, M.2    Gaulis, S.3    Matthies, R.4    Hess, D.5    Jost, J.P.6
  • 52
    • 0001992028 scopus 로고    scopus 로고
    • Satellite DNA hypomethylation vs. overall genomic hypomethylation in ovarian epithelial tumors of different malignant potential
    • G. Qu L. Dubeau A. Narayan M.C. Yu M. Ehrlich Satellite DNA hypomethylation vs. overall genomic hypomethylation in ovarian epithelial tumors of different malignant potential Mutat. Res. 423 1999 91 101
    • (1999) Mutat. Res. , vol.423 , pp. 91-101
    • Qu, G.1    Dubeau, L.2    Narayan, A.3    Yu, M.C.4    Ehrlich, M.5
  • 53
    • 0033081639 scopus 로고    scopus 로고
    • Frequent hypomethylation in Wilms tumors of pericentromeric DNA in chromosomes 1 and 16
    • G.Z. Qu P.E. Grundy A. Narayan M. Ehrlich Frequent hypomethylation in Wilms tumors of pericentromeric DNA in chromosomes 1 and 16 Cancer Genet. Cytogenet. 109 1999 34 39
    • (1999) Cancer Genet. Cytogenet. , vol.109 , pp. 34-39
    • Qu, G.Z.1    Grundy, P.E.2    Narayan, A.3    Ehrlich, M.4
  • 55
    • 0036731869 scopus 로고    scopus 로고
    • Correlation of DNA hypomethylation at pericentromeric heterochromatin regions of chromosomes 16 and 1 with histological features and chromosomal abnormalities of human breast carcinomas
    • H. Tsuda T. Takarabe Y. Kanai T. Fukutomi S. Hirohashi Correlation of DNA hypomethylation at pericentromeric heterochromatin regions of chromosomes 16 and 1 with histological features and chromosomal abnormalities of human breast carcinomas Am. J. Pathol. 161 2002 859 866
    • (2002) Am. J. Pathol. , vol.161 , pp. 859-866
    • Tsuda, H.1    Takarabe, T.2    Kanai, Y.3    Fukutomi, T.4    Hirohashi, S.5
  • 56
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • S.N. Ho H.D. Hunt R.M. Horton J.K. Pullen L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.