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Volumn 11, Issue 3, 2012, Pages 251-264

The role of methyl-binding proteins in chromatin organization and epigenome maintenance

Author keywords

Cancer; DNA methylation recognition; Epigenetic cooperation; Heterochromatin formation and maintenance; Transcriptional repression

Indexed keywords

KAISO LIKE PROTEIN; KAISO PROTEIN; METHYL CPG BINDING PROTEIN; METHYL CPG BINDING PROTEIN 2; UHRF1 PROTEIN; UNCLASSIFIED DRUG; ZBTB4 PROTEIN;

EID: 84864301890     PISSN: 20412649     EISSN: 20412657     Source Type: Journal    
DOI: 10.1093/bfgp/elr040     Document Type: Article
Times cited : (84)

References (146)
  • 1
    • 61349117970 scopus 로고    scopus 로고
    • Genetics and epigenetics: stability and plasticity during cellular differentiation
    • Mohn F, Schubeler D. Genetics and epigenetics: stability and plasticity during cellular differentiation. Trends Genet 2009;25:129-36.
    • (2009) Trends Genet , vol.25 , pp. 129-136
    • Mohn, F.1    Schubeler, D.2
  • 2
    • 79956330964 scopus 로고    scopus 로고
    • CpG islands and the regulation of transcription
    • Deaton AM, Bird A. CpG islands and the regulation of transcription. Genes Dev 2011;25:1010-22.
    • (2011) Genes Dev , vol.25 , pp. 1010-1022
    • Deaton, A.M.1    Bird, A.2
  • 3
    • 79951500297 scopus 로고    scopus 로고
    • CpG island chromatin: a platform for gene regulation
    • Blackledge NP, Klose R. CpG island chromatin: a platform for gene regulation. Epigenetics 2011;6:147-52.
    • (2011) Epigenetics , vol.6 , pp. 147-152
    • Blackledge, N.P.1    Klose, R.2
  • 4
    • 15744401773 scopus 로고    scopus 로고
    • Eukaryotic cytosine methyltransferases
    • Goll MG, Bestor TH. Eukaryotic cytosine methyltransferases. Annu Rev Biochem 2005;74:481-514.
    • (2005) Annu Rev Biochem , vol.74 , pp. 481-514
    • Goll, M.G.1    Bestor, T.H.2
  • 5
    • 34347334590 scopus 로고    scopus 로고
    • Biological functions of DNA methyltransferase 1 require its methyltransferase activity
    • Damelin M, Bestor TH. Biological functions of DNA methyltransferase 1 require its methyltransferase activity. Mol Cell Biol 2007;27:3891-9.
    • (2007) Mol Cell Biol , vol.27 , pp. 3891-3899
    • Damelin, M.1    Bestor, T.H.2
  • 6
    • 36849082927 scopus 로고    scopus 로고
    • Major and essential role for the DNA methylation mark in mouse embryogenesis and stable association of DNMT1 with newly replicated regions
    • Takebayashi S, Tamura T, Matsuoka C, et al. Major and essential role for the DNA methylation mark in mouse embryogenesis and stable association of DNMT1 with newly replicated regions. Mol Cell Biol 2007;27:8243-58.
    • (2007) Mol Cell Biol , vol.27 , pp. 8243-8258
    • Takebayashi, S.1    Tamura, T.2    Matsuoka, C.3
  • 7
    • 0035901498 scopus 로고    scopus 로고
    • Loss of the maintenance methyltransferase, xDnmt1, induces apoptosis in Xenopus embryos
    • Stancheva I, Hensey C, Meehan RR. Loss of the maintenance methyltransferase, xDnmt1, induces apoptosis in Xenopus embryos. EmboJ 2001;20:1963-73.
    • (2001) EmboJ , vol.20 , pp. 1963-1973
    • Stancheva, I.1    Hensey, C.2    Meehan, R.R.3
  • 8
    • 0343485074 scopus 로고    scopus 로고
    • Transient depletion of xDnmt1 leads to premature gene activation in Xenopus embryos
    • Stancheva I, Meehan RR. Transient depletion of xDnmt1 leads to premature gene activation in Xenopus embryos. Genes Dev 2000;14:313-27.
    • (2000) Genes Dev , vol.14 , pp. 313-327
    • Stancheva, I.1    Meehan, R.R.2
  • 9
    • 70249141961 scopus 로고    scopus 로고
    • Loss of Dnmt1 catalytic activity reveals multiple roles for DNA methylation during pancreas development and regeneration
    • Anderson RM, Bosch JA, Goll MG, et al. Loss of Dnmt1 catalytic activity reveals multiple roles for DNA methylation during pancreas development and regeneration. Dev Biol 2009;334:213-23.
    • (2009) Dev Biol , vol.334 , pp. 213-223
    • Anderson, R.M.1    Bosch, J.A.2    Goll, M.G.3
  • 10
    • 78651242877 scopus 로고    scopus 로고
    • Uhrf1 and Dnmt1 are required for development and maintenance of the zebrafish lens
    • Tittle RK, Sze R, Ng A, et al. Uhrf1 and Dnmt1 are required for development and maintenance of the zebrafish lens. Dev Biol 2011;350:50-63.
    • (2011) Dev Biol , vol.350 , pp. 50-63
    • Tittle, R.K.1    Sze, R.2    Ng, A.3
  • 11
    • 33745270104 scopus 로고    scopus 로고
    • Maintenance of self-renewal ability of mouse embryonic stem cells in the absence of DNA methyltransferases Dnmt1 Dnmt3a and Dnmt3b
    • Tsumura A, Hayakawa T, Kumaki Y, et al. Maintenance of self-renewal ability of mouse embryonic stem cells in the absence of DNA methyltransferases Dnmt1, Dnmt3a and Dnmt3b. Genes Cells 2006;11:805-14.
    • (2006) Genes Cells , vol.11 , pp. 805-814
    • Tsumura, A.1    Hayakawa, T.2    Kumaki, Y.3
  • 12
    • 77957824513 scopus 로고    scopus 로고
    • DNA methylation is dispensable for the growth and survival of the extraembryonic lineages
    • Sakaue M, Ohta H, Kumaki Y, et al. DNA methylation is dispensable for the growth and survival of the extraembryonic lineages. Curr Biol 2011;20:1452-7.
    • (2011) Curr Biol , vol.20 , pp. 1452-1457
    • Sakaue, M.1    Ohta, H.2    Kumaki, Y.3
  • 13
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • Ciccone DN, Su H, Hevi S, et al. KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 2009;461:415-8.
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3
  • 14
    • 33751209468 scopus 로고    scopus 로고
    • Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication
    • Esteve PO, Chin HG, Smallwood A, et al. Direct interaction between DNMT1 and G9a coordinates DNA and histone methylation during replication. Genes Dev 2006;20: 3089-103.
    • (2006) Genes Dev , vol.20 , pp. 3089-3103
    • Esteve, P.O.1    Chin, H.G.2    Smallwood, A.3
  • 15
    • 0037041422 scopus 로고    scopus 로고
    • Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase
    • Jackson JP, Lindroth AM, Cao X, et al. Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase. Nature 2002;416:556-60.
    • (2002) Nature , vol.416 , pp. 556-560
    • Jackson, J.P.1    Lindroth, A.M.2    Cao, X.3
  • 16
    • 10744230544 scopus 로고    scopus 로고
    • Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin
    • Lehnertz B, Ueda Y, Derijck AA, et al. Suv39h-mediated histone H3 lysine 9 methylation directs DNA methylation to major satellite repeats at pericentric heterochromatin. Curr Biol 2003;13:1192-200.
    • (2003) Curr Biol , vol.13 , pp. 1192-1200
    • Lehnertz, B.1    Ueda, Y.2    Derijck, A.A.3
  • 17
    • 0035891265 scopus 로고    scopus 로고
    • A histone H3 methyltransferase controls DNA methylation in Neurospora crassa
    • Tamaru H, Selker EU. A histone H3 methyltransferase controls DNA methylation in Neurospora crassa. Nature 2001;414: 277-83.
    • (2001) Nature , vol.414 , pp. 277-283
    • Tamaru, H.1    Selker, E.U.2
  • 18
    • 32844459336 scopus 로고    scopus 로고
    • The Polycomb group protein EZH2 directly controls DNA methylation
    • Vire E, Brenner C, Deplus R, et al. The Polycomb group protein EZH2 directly controls DNA methylation. Nature 2006;439:871-4.
    • (2006) Nature , vol.439 , pp. 871-874
    • Vire, E.1    Brenner, C.2    Deplus, R.3
  • 19
    • 58149156264 scopus 로고    scopus 로고
    • The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation
    • Wang J, Hevi S, Kurash JK, et al. The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nat Genet 2009;41:125-9.
    • (2009) Nat Genet , vol.41 , pp. 125-129
    • Wang, J.1    Hevi, S.2    Kurash, J.K.3
  • 20
    • 49649125042 scopus 로고    scopus 로고
    • Genome-scale DNA methylation maps of pluripotent and differentiated cells
    • Meissner A, Mikkelsen TS, Gu H, et al. Genome-scale DNA methylation maps of pluripotent and differentiated cells. Nature 2008;454:766-70.
    • (2008) Nature , vol.454 , pp. 766-770
    • Meissner, A.1    Mikkelsen, T.S.2    Gu, H.3
  • 21
    • 55549141877 scopus 로고    scopus 로고
    • Histone H2A Z and DNA methylation are mutually antagonistic chromatin marks
    • Zilberman D, Coleman-Derr D, Ballinger T, et al. Histone H2A.Z and DNA methylation are mutually antagonistic chromatin marks. Nature 2008;456:125-9.
    • (2008) Nature , vol.456 , pp. 125-129
    • Zilberman, D.1    Coleman-Derr, D.2    Ballinger, T.3
  • 22
    • 34547725157 scopus 로고    scopus 로고
    • DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA
    • Ooi SK, Qiu C, Bernstein E, et al. DNMT3L connects unmethylated lysine 4 of histone H3 to de novo methylation of DNA. Nature 2007;448:714-7.
    • (2007) Nature , vol.448 , pp. 714-717
    • Ooi, S.K.1    Qiu, C.2    Bernstein, E.3
  • 23
    • 70449099301 scopus 로고    scopus 로고
    • Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain
    • Otani J, Nankumo T, Arita K, et al. Structural basis for recognition of H3K4 methylation status by the DNA methyltransferase 3A ATRX-DNMT3-DNMT3L domain. EMBORep 2009;10:1235-41.
    • (2009) EMBORep , vol.10 , pp. 1235-1241
    • Otani, J.1    Nankumo, T.2    Arita, K.3
  • 24
    • 0037406067 scopus 로고    scopus 로고
    • The methyl-CpG binding domain and the evolving role of DNA methylation in animals
    • Hendrich B, Tweedie S. The methyl-CpG binding domain and the evolving role of DNA methylation in animals. TrendsGenet 2003;19:269-77.
    • (2003) TrendsGenet , vol.19 , pp. 269-277
    • Hendrich, B.1    Tweedie, S.2
  • 25
    • 77957809220 scopus 로고    scopus 로고
    • The Human Proteins MBD5 and MBD6 Associate with Heterochromatin but They Do Not Bind Methylated DNA
    • Laget S, Joulie M, Le Masson F, et al. The Human Proteins MBD5 and MBD6 Associate with Heterochromatin but They Do Not Bind Methylated DNA. PLoS One 2010;5(8):e11982.
    • (2010) PLoS One , vol.5 , Issue.8
    • Laget, S.1    Joulie, M.2    Le Masson, F.3
  • 26
    • 9144246375 scopus 로고    scopus 로고
    • Comparative study of methyl-CpG-binding domain proteins
    • Roloff TC, Ropers HH, Nuber UA. Comparative study of methyl-CpG-binding domain proteins. BMC Genomics 2003;4:1.
    • (2003) BMC Genomics , vol.4 , pp. 1
    • Roloff, T.C.1    Ropers, H.H.2    Nuber, U.A.3
  • 27
    • 0032830639 scopus 로고    scopus 로고
    • Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2
    • Amir RE, Van den Veyver IB, Wan M, et al. Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2. Nat Genet 1999;23:185-8.
    • (1999) Nat Genet , vol.23 , pp. 185-188
    • Amir, R.E.1    Van den Veyver, I.B.2    Wan, M.3
  • 28
    • 8444253290 scopus 로고    scopus 로고
    • Mild overexpression of MeCP2 causes a progressive neurological disorder in mice
    • Collins AL, Levenson JM, Vilaythong AP, et al. Mild overexpression of MeCP2 causes a progressive neurological disorder in mice. HumanMol Genet 2004;13:2679-89.
    • (2004) HumanMol Genet , vol.13 , pp. 2679-2689
    • Collins, A.L.1    Levenson, J.M.2    Vilaythong, A.P.3
  • 29
    • 0035094767 scopus 로고    scopus 로고
    • A mouse Mecp2-null mutation causes neurological symptoms that mimic Rett syndrome
    • Guy J, Hendrich B, Holmes M, et al. A mouse Mecp2-null mutation causes neurological symptoms that mimic Rett syndrome. Nat Genet 2001;27:322-6.
    • (2001) Nat Genet , vol.27 , pp. 322-326
    • Guy, J.1    Hendrich, B.2    Holmes, M.3
  • 30
    • 0035093830 scopus 로고    scopus 로고
    • Deficiency of methyl-CpG binding protein-2 in CNS neurons results in a Rett-like phenotype in mice
    • Chen RZ, Akbarian S, Tudor M, et al. Deficiency of methyl-CpG binding protein-2 in CNS neurons results in a Rett-like phenotype in mice. Nat Genet 2001;27:327-31.
    • (2001) Nat Genet , vol.27 , pp. 327-331
    • Chen, R.Z.1    Akbarian, S.2    Tudor, M.3
  • 31
    • 0032915423 scopus 로고    scopus 로고
    • The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor
    • Daniel JM, Reynolds AB. The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain zinc finger transcription factor. Mol Cell Biol 1999;19:3614-23.
    • (1999) Mol Cell Biol , vol.19 , pp. 3614-3623
    • Daniel, J.M.1    Reynolds, A.B.2
  • 32
    • 0035394961 scopus 로고    scopus 로고
    • The p120 catenin partner Kaiso is a DNA methylationdependent transcriptional repressor
    • Prokhortchouk A, Hendrich B, Jorgensen H, et al. The p120 catenin partner Kaiso is a DNA methylationdependent transcriptional repressor. Genes Dev 2001;15: 1613-8.
    • (2001) Genes Dev , vol.15 , pp. 1613-1618
    • Prokhortchouk, A.1    Hendrich, B.2    Jorgensen, H.3
  • 33
    • 0036640736 scopus 로고    scopus 로고
    • The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides
    • Daniel JM, Spring CM, Crawford HC, et al. The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein that recognizes both a sequence-specific consensus and methylated CpG dinucleotides. Nucleic Acids Res 2002;30: 2911-9.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2911-2919
    • Daniel, J.M.1    Spring, C.M.2    Crawford, H.C.3
  • 34
    • 77956120147 scopus 로고    scopus 로고
    • Sequence-specific recognition of methylated DNA by human zinc-finger proteins
    • Sasai N, Nakao M, Defossez PA. Sequence-specific recognition of methylated DNA by human zinc-finger proteins. Nucleic Acids Res 2010;38:5015-22.
    • (2010) Nucleic Acids Res , vol.38 , pp. 5015-5022
    • Sasai, N.1    Nakao, M.2    Defossez, P.A.3
  • 35
    • 33845534761 scopus 로고    scopus 로고
    • Born to bind: the BTB protein-protein interaction domain
    • Perez-Torrado R, Yamada D, Defossez PA. Born to bind: the BTB protein-protein interaction domain. Bioessays 2006;28:1194-202.
    • (2006) Bioessays , vol.28 , pp. 1194-1202
    • Perez-Torrado, R.1    Yamada, D.2    Defossez, P.A.3
  • 36
    • 65549160578 scopus 로고    scopus 로고
    • The non-methylated DNA-binding function of Kaiso is not required in early Xenopus laevis development
    • Ruzov A, Savitskaya E, Hackett JA, et al. The non-methylated DNA-binding function of Kaiso is not required in early Xenopus laevis development. Development 2009;136:729-38.
    • (2009) Development , vol.136 , pp. 729-738
    • Ruzov, A.1    Savitskaya, E.2    Hackett, J.A.3
  • 37
    • 12344301501 scopus 로고    scopus 로고
    • Kaiso is a genome-wide repressor of transcription that is essential for amphibian development
    • Ruzov A, Dunican DS, Prokhortchouk A, et al. Kaiso is a genome-wide repressor of transcription that is essential for amphibian development. Development 2004;131: 6185-94.
    • (2004) Development , vol.131 , pp. 6185-6194
    • Ruzov, A.1    Dunican, D.S.2    Prokhortchouk, A.3
  • 38
    • 0036499523 scopus 로고    scopus 로고
    • DNA methylation at promoter regions regulates the timing of gene activation in Xenopus laevis embryos
    • Stancheva I, El-Maarri O, Walter J, et al. DNA methylation at promoter regions regulates the timing of gene activation in Xenopus laevis embryos. Dev Biol 2002;243:155-65.
    • (2002) Dev Biol , vol.243 , pp. 155-165
    • Stancheva, I.1    El-Maarri, O.2    Walter, J.3
  • 39
    • 77950101058 scopus 로고    scopus 로고
    • The transcriptional repressor Kaiso localizes at the mitotic spindle and is a constituent of the pericentriolar material
    • Soubry A, Staes K, Parthoens E, et al. The transcriptional repressor Kaiso localizes at the mitotic spindle and is a constituent of the pericentriolar material. PLoS One 2011;5: e9203.
    • (2011) PLoS One , vol.5
    • Soubry, A.1    Staes, K.2    Parthoens, E.3
  • 40
    • 33645218438 scopus 로고    scopus 로고
    • A family of human zinc finger proteins that bind methylated DNA and repress transcription
    • Filion GJ, Zhenilo S, Salozhin S, et al. A family of human zinc finger proteins that bind methylated DNA and repress transcription. Mol Cell Biol 2006;26:169-81.
    • (2006) Mol Cell Biol , vol.26 , pp. 169-181
    • Filion, G.J.1    Zhenilo, S.2    Salozhin, S.3
  • 41
    • 70349329405 scopus 로고    scopus 로고
    • Many paths to one goal? The proteins that recognize methylated DNA in eukaryotes
    • Sasai N, Defossez PA. Many paths to one goal? The proteins that recognize methylated DNA in eukaryotes. Int JDevBiol 2009;53:323-34.
    • (2009) Int JDevBiol , vol.53 , pp. 323-334
    • Sasai, N.1    Defossez, P.A.2
  • 42
    • 35748984132 scopus 로고    scopus 로고
    • Functional analysis of the role of POK transcriptional repressors
    • Costoya JA. Functional analysis of the role of POK transcriptional repressors. Brief Funct Genomic Proteomic 2007;6: 8-18.
    • (2007) Brief Funct Genomic Proteomic , vol.6 , pp. 8-18
    • Costoya, J.A.1
  • 43
    • 24344443646 scopus 로고    scopus 로고
    • Identification of a novel BTB-zinc finger transcriptional repressor, CIBZ, that interacts with CtBP corepressor
    • Sasai N, Matsuda E, Sarashina E, et al. Identification of a novel BTB-zinc finger transcriptional repressor, CIBZ, that interacts with CtBP corepressor. Genes Cells 2005;10: 871-85.
    • (2005) Genes Cells , vol.10 , pp. 871-885
    • Sasai, N.1    Matsuda, E.2    Sarashina, E.3
  • 44
    • 77958481159 scopus 로고    scopus 로고
    • Nucleosomeinteracting proteins regulated by DNA and histone methylation
    • Bartke T, Vermeulen M, Xhemalce B, et al. Nucleosomeinteracting proteins regulated by DNA and histone methylation. Cell 2010;143:470-84.
    • (2010) Cell , vol.143 , pp. 470-484
    • Bartke, T.1    Vermeulen, M.2    Xhemalce, B.3
  • 45
    • 0033984257 scopus 로고    scopus 로고
    • ICBP90, a novel human CCAAT binding protein, involved in the regulation of topoisomerase IIalpha expression
    • Hopfner R, Mousli M, Jeltsch JM, et al. ICBP90, a novel human CCAAT binding protein, involved in the regulation of topoisomerase IIalpha expression. Cancer Res 2000;60: 121-8.
    • (2000) Cancer Res , vol.60 , pp. 121-128
    • Hopfner, R.1    Mousli, M.2    Jeltsch, J.M.3
  • 46
    • 7044245474 scopus 로고    scopus 로고
    • ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain
    • Unoki M, Nishidate T, Nakamura Y. ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene 2004;23:7601-10.
    • (2004) Oncogene , vol.23 , pp. 7601-7610
    • Unoki, M.1    Nishidate, T.2    Nakamura, Y.3
  • 47
    • 66349103332 scopus 로고    scopus 로고
    • UHRF1, a modular multi-domain protein, regulates replicationcoupled crosstalk between DNA methylation and histone modifications
    • Hashimoto H, Horton JR, Zhang X, et al. UHRF1, a modular multi-domain protein, regulates replicationcoupled crosstalk between DNA methylation and histone modifications. Epigenetics 2009;4:8-14.
    • (2009) Epigenetics , vol.4 , pp. 8-14
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3
  • 48
    • 37849038263 scopus 로고    scopus 로고
    • ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation
    • Karagianni P, Amazit L, Qin J, et al. ICBP90, a novel methyl K9 H3 binding protein linking protein ubiquitination with heterochromatin formation. MolCellBiol 2008;28: 705-17.
    • (2008) MolCellBiol , vol.28 , pp. 705-717
    • Karagianni, P.1    Amazit, L.2    Qin, J.3
  • 49
    • 53749095742 scopus 로고    scopus 로고
    • The PHD domain of Np95 (mUHRF1) is involved in large-scale reorganization of pericentromeric heterochromatin
    • Papait R, Pistore C, Grazini U, et al. The PHD domain of Np95 (mUHRF1) is involved in large-scale reorganization of pericentromeric heterochromatin. Mol Biol Cell 2008;19: 3554-63.
    • (2008) Mol Biol Cell , vol.19 , pp. 3554-3563
    • Papait, R.1    Pistore, C.2    Grazini, U.3
  • 50
    • 77950655451 scopus 로고    scopus 로고
    • The multi-domain protein Np95 connects DNA methylation and histone modification
    • Rottach A, Frauer C, Pichler G, et al. The multi-domain protein Np95 connects DNA methylation and histone modification. Nucleic Acids Res 2010;38:1796-804.
    • (2010) Nucleic Acids Res , vol.38 , pp. 1796-1804
    • Rottach, A.1    Frauer, C.2    Pichler, G.3
  • 51
    • 36849072573 scopus 로고    scopus 로고
    • The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA
    • Sharif J, Muto M, Takebayashi S, et al. The SRA protein Np95 mediates epigenetic inheritance by recruiting Dnmt1 to methylated DNA. Nature 2007;450:908-12.
    • (2007) Nature , vol.450 , pp. 908-912
    • Sharif, J.1    Muto, M.2    Takebayashi, S.3
  • 52
    • 1542330106 scopus 로고    scopus 로고
    • Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-dependent DNA-damage checkpoint signals contributes to cell cycle arrest at G1/S transition
    • Arima Y, Hirota T, Bronner C, et al. Down-regulation of nuclear protein ICBP90 by p53/p21Cip1/WAF1-dependent DNA-damage checkpoint signals contributes to cell cycle arrest at G1/S transition. Genes Cells 2004;9: 131-42.
    • (2004) Genes Cells , vol.9 , pp. 131-142
    • Arima, Y.1    Hirota, T.2    Bronner, C.3
  • 53
    • 0037054539 scopus 로고    scopus 로고
    • Np95 is regulated by E1A during mitotic reactivation of terminally differentiated cells and is essential for S phase entry
    • Bonapace IM, Latella L, Papait R, etal. Np95 is regulated by E1A during mitotic reactivation of terminally differentiated cells and is essential for S phase entry. J Cell Biol 2002;157: 909-14.
    • (2002) J Cell Biol , vol.157 , pp. 909-914
    • Bonapace, I.M.1    Latella, L.2    Papait, R.3
  • 54
    • 27744564626 scopus 로고    scopus 로고
    • The retinoblastoma gene and its product are targeted by ICBP90: a key mechanism in the G1/S transition during the cell cycle
    • Jeanblanc M, Mousli M, Hopfner R, et al. The retinoblastoma gene and its product are targeted by ICBP90: a key mechanism in the G1/S transition during the cell cycle. Oncogene 2005;24:7337-45.
    • (2005) Oncogene , vol.24 , pp. 7337-7345
    • Jeanblanc, M.1    Mousli, M.2    Hopfner, R.3
  • 55
    • 0037072831 scopus 로고    scopus 로고
    • Targeted disruption of Np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks
    • Muto M, Kanari Y, Kubo E, et al. Targeted disruption of Np95 gene renders murine embryonic stem cells hypersensitive to DNA damaging agents and DNA replication blocks. J BiolChem 2002;277:34549-55.
    • (2002) J BiolChem , vol.277 , pp. 34549-34555
    • Muto, M.1    Kanari, Y.2    Kubo, E.3
  • 56
    • 33947109937 scopus 로고    scopus 로고
    • Np95 is implicated in pericentromeric heterochromatin replication and in major satellite silencing
    • Papait R, Pistore C, Negri D, et al. Np95 is implicated in pericentromeric heterochromatin replication and in major satellite silencing. Mol Biol Cell 2007;18:1098-106.
    • (2007) Mol Biol Cell , vol.18 , pp. 1098-1106
    • Papait, R.1    Pistore, C.2    Negri, D.3
  • 57
    • 34648833002 scopus 로고    scopus 로고
    • UHRF1 plays a role in maintaining DNA methylation in mammalian cells
    • Bostick M, Kim JK, Esteve PO, etal. UHRF1 plays a role in maintaining DNA methylation in mammalian cells. Science 2007;317:1760-4.
    • (2007) Science , vol.317 , pp. 1760-1764
    • Bostick, M.1    Kim, J.K.2    Esteve, P.O.3
  • 58
    • 34548451241 scopus 로고    scopus 로고
    • The UHRF family: oncogenes that are drugable targets for cancer therapy in the near future?
    • Bronner C, Achour M, Arima Y, et al. The UHRF family: oncogenes that are drugable targets for cancer therapy in the near future? Pharmacol Ther 2007;115:419-34.
    • (2007) Pharmacol Ther , vol.115 , pp. 419-434
    • Bronner, C.1    Achour, M.2    Arima, Y.3
  • 59
    • 84860389582 scopus 로고    scopus 로고
    • Cooperative DNA and histone binding by Uhrf2 links the two major repressive epigenetic pathways
    • Pichler G, Wolf P, Schmidt CS, et al. Cooperative DNA and histone binding by Uhrf2 links the two major repressive epigenetic pathways. JCell Biochem 2011;112:2585-93.
    • (2011) JCell Biochem , vol.112 , pp. 2585-2593
    • Pichler, G.1    Wolf, P.2    Schmidt, C.S.3
  • 60
    • 0036384371 scopus 로고    scopus 로고
    • NIRF, a novel RING finger protein, is involved in cell-cycle regulation
    • Mori T, Li Y, Hata H, et al. NIRF, a novel RING finger protein, is involved in cell-cycle regulation. BiochemBiophys Res Commun 2002;296:530-6.
    • (2002) BiochemBiophys Res Commun , vol.296 , pp. 530-536
    • Mori, T.1    Li, Y.2    Hata, H.3
  • 61
    • 50849106398 scopus 로고    scopus 로고
    • Three SRA-domain methylcytosine-binding proteins cooperate to maintain global CpG methylation and epigenetic silencing in Arabidopsis
    • Woo HR, Dittmer TA, Richards EJ. Three SRA-domain methylcytosine-binding proteins cooperate to maintain global CpG methylation and epigenetic silencing in Arabidopsis. PLoS Genet 2008;4:e1000156.
    • (2008) PLoS Genet , vol.4
    • Woo, H.R.1    Dittmer, T.A.2    Richards, E.J.3
  • 62
    • 77952734605 scopus 로고    scopus 로고
    • Conservation and divergence of methylation patterning in plants and animals
    • Feng S, Cokus SJ, Zhang X, et al. Conservation and divergence of methylation patterning in plants and animals. Proc Natl Acad SciUSA 2010;107:8689-94.
    • (2010) Proc Natl Acad SciUSA , vol.107 , pp. 8689-8694
    • Feng, S.1    Cokus, S.J.2    Zhang, X.3
  • 63
    • 77649267695 scopus 로고    scopus 로고
    • Dynamic changes in the human methylome during differentiation
    • Laurent L, Wong E, Li G, et al. Dynamic changes in the human methylome during differentiation. GenomeRes 2010; 20:320-31.
    • (2010) GenomeRes , vol.20 , pp. 320-331
    • Laurent, L.1    Wong, E.2    Li, G.3
  • 64
    • 70450217879 scopus 로고    scopus 로고
    • Human DNA methylomes at base resolution show widespread epigenomic differences
    • Lister R, Pelizzola M, Dowen RH, et al. Human DNA methylomes at base resolution show widespread epigenomic differences. Nature 2009;462(7271):315-22.
    • (2009) Nature , vol.462 , Issue.7271 , pp. 315-322
    • Lister, R.1    Pelizzola, M.2    Dowen, R.H.3
  • 65
    • 0034625064 scopus 로고    scopus 로고
    • Non-CpG methylation is prevalent in embryonic stem cells and may be mediated by DNA methyltransferase 3a
    • Ramsahoye BH, Biniszkiewicz D, Lyko F, et al. Non-CpG methylation is prevalent in embryonic stem cells and may be mediated by DNA methyltransferase 3a. Proc Natl Acad Sci USA 2000;97:5237-42.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5237-5242
    • Ramsahoye, B.H.1    Biniszkiewicz, D.2    Lyko, F.3
  • 66
    • 33846931283 scopus 로고    scopus 로고
    • The SRA methyl-cytosine-binding domain links DNA and histone methylation
    • Johnson LM, Bostick M, Zhang X, et al. The SRA methyl-cytosine-binding domain links DNA and histone methylation. Curr Biol 2007;17:379-84.
    • (2007) Curr Biol , vol.17 , pp. 379-384
    • Johnson, L.M.1    Bostick, M.2    Zhang, X.3
  • 67
    • 0141638426 scopus 로고    scopus 로고
    • N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso
    • Yoon HG, Chan DW, Reynolds AB, et al. N-CoR mediates DNA methylation-dependent repression through a methyl CpG binding protein Kaiso. Mol Cell 2003;12: 723-34.
    • (2003) Mol Cell , vol.12 , pp. 723-734
    • Yoon, H.G.1    Chan, D.W.2    Reynolds, A.B.3
  • 68
    • 0242669199 scopus 로고    scopus 로고
    • Coordinated histone modifications mediated by a CtBP co-repressor complex
    • Shi Y, Sawada J, Sui G, et al. Coordinated histone modifications mediated by a CtBP co-repressor complex. Nature 2003;422:735-8.
    • (2003) Nature , vol.422 , pp. 735-738
    • Shi, Y.1    Sawada, J.2    Sui, G.3
  • 69
    • 44649137548 scopus 로고    scopus 로고
    • Zbtb4 represses transcription of P21CIP1 and controls the cellular response to p53 activation
    • Weber A, Marquardt J, Elzi D, et al. Zbtb4 represses transcription of P21CIP1 and controls the cellular response to p53 activation. EmboJ 2008;27:1563-74.
    • (2008) EmboJ , vol.27 , pp. 1563-1574
    • Weber, A.1    Marquardt, J.2    Elzi, D.3
  • 70
    • 84857355139 scopus 로고    scopus 로고
    • Identification of oncogenic microRNA-17-92/ZBTB4/specificity protein axis in breast cancer
    • doi: 10.1038/ onc.2011.296. [Epub ahead of print]
    • Kim K, Chadalapaka G, Lee SO, et al. Identification of oncogenic microRNA-17-92/ZBTB4/specificity protein axis in breast cancer. Oncogene 2011; doi: 10.1038/ onc.2011.296. [Epub ahead of print].
    • (2011) Oncogene
    • Kim, K.1    Chadalapaka, G.2    Lee, S.O.3
  • 71
    • 80052429757 scopus 로고    scopus 로고
    • Crystal structure of PHD domain of UHRF1 and insights into recognition of unmodified histone H3 arginine residue 2
    • Hu L, Li Z, Wang P, et al. Crystal structure of PHD domain of UHRF1 and insights into recognition of unmodified histone H3 arginine residue 2. Cell Res 2011; 21:1374-8.
    • (2011) Cell Res , vol.21 , pp. 1374-1378
    • Hu, L.1    Li, Z.2    Wang, P.3
  • 72
    • 79960464001 scopus 로고    scopus 로고
    • PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression
    • Rajakumara E, Wang Z, Ma H, et al. PHD finger recognition of unmodified histone H3R2 links UHRF1 to regulation of euchromatic gene expression. Mol Cell 2011;43: 275-84.
    • (2011) Mol Cell , vol.43 , pp. 275-284
    • Rajakumara, E.1    Wang, Z.2    Ma, H.3
  • 73
    • 80052493266 scopus 로고    scopus 로고
    • Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger
    • Wang C, Shen J, Yang Z, et al. Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger. Cell Res 2011;21:1379-82.
    • (2011) Cell Res , vol.21 , pp. 1379-1382
    • Wang, C.1    Shen, J.2    Yang, Z.3
  • 74
    • 45849105557 scopus 로고    scopus 로고
    • MeCP2, a key contributor to neurological disease, activates and represses transcription
    • Chahrour M, Jung SY, Shaw C, et al. MeCP2, a key contributor to neurological disease, activates and represses transcription. Science 2008;320:1224-9.
    • (2008) Science , vol.320 , pp. 1224-1229
    • Chahrour, M.1    Jung, S.Y.2    Shaw, C.3
  • 75
    • 37649022627 scopus 로고    scopus 로고
    • Integrated epigenomic analyses of neuronal MeCP2 reveal a role for long-range interaction with active genes
    • Yasui DH, Peddada S, Bieda MC, et al. Integrated epigenomic analyses of neuronal MeCP2 reveal a role for long-range interaction with active genes. Proc Natl Acad Sci USA 2007;104:19416-21.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19416-19421
    • Yasui, D.H.1    Peddada, S.2    Bieda, M.C.3
  • 76
    • 0032168678 scopus 로고    scopus 로고
    • CpG methylation, chromatin structure and gene silencing-a three-way connection
    • Razin A. CpG methylation, chromatin structure and gene silencing-a three-way connection. EMBO J 1998;17: 4905-8.
    • (1998) EMBO J , vol.17 , pp. 4905-4908
    • Razin, A.1
  • 77
    • 24044523177 scopus 로고    scopus 로고
    • DNA binding selectivity of MeCP2 due to a requirement for A/T sequences adjacent to methyl-CpG
    • Klose RJ, Sarraf SA, Schmiedeberg L, et al. DNA binding selectivity of MeCP2 due to a requirement for A/T sequences adjacent to methyl-CpG. Mol Cell 2005;19: 667-78.
    • (2005) Mol Cell , vol.19 , pp. 667-678
    • Klose, R.J.1    Sarraf, S.A.2    Schmiedeberg, L.3
  • 78
    • 34948908780 scopus 로고    scopus 로고
    • MeCP2-chromatin interactions include the formation of chromatosome-like structures and are altered in mutations causing Rett syndrome
    • Nikitina T, Ghosh RP, Horowitz-Scherer RA, et al. MeCP2-chromatin interactions include the formation of chromatosome-like structures and are altered in mutations causing Rett syndrome. J Biol Chem 2007;282:28237-45.
    • (2007) J Biol Chem , vol.282 , pp. 28237-28245
    • Nikitina, T.1    Ghosh, R.P.2    Horowitz-Scherer, R.A.3
  • 79
    • 40949088498 scopus 로고    scopus 로고
    • MeCP2 preferentially binds to methylated linker DNA in the absence of the terminal tail of histone H3 and independently of histone acetylation
    • Ishibashi T, Thambirajah AA, Ausio J. MeCP2 preferentially binds to methylated linker DNA in the absence of the terminal tail of histone H3 and independently of histone acetylation. FEBS Lett 2008;582:1157-62.
    • (2008) FEBS Lett , vol.582 , pp. 1157-1162
    • Ishibashi, T.1    Thambirajah, A.A.2    Ausio, J.3
  • 80
    • 77956683757 scopus 로고    scopus 로고
    • MeCP2 binds cooperatively to its substrate and competes with histone H1 for chromatin binding sites
    • Ghosh RP, Horowitz-Scherer RA, Nikitina T, et al. MeCP2 binds cooperatively to its substrate and competes with histone H1 for chromatin binding sites. Mol Cell Biol 2010;30:4656-70.
    • (2010) Mol Cell Biol , vol.30 , pp. 4656-4670
    • Ghosh, R.P.1    Horowitz-Scherer, R.A.2    Nikitina, T.3
  • 81
    • 76849094693 scopus 로고    scopus 로고
    • Neuronal MeCP2 is expressed at near histone-octamer levels and globally alters the chromatin state
    • Skene PJ, Illingworth RS, Webb S, et al. Neuronal MeCP2 is expressed at near histone-octamer levels and globally alters the chromatin state. Mol Cell 2010;37:457-68.
    • (2010) Mol Cell , vol.37 , pp. 457-468
    • Skene, P.J.1    Illingworth, R.S.2    Webb, S.3
  • 82
    • 0037180492 scopus 로고    scopus 로고
    • Transcriptional profiling of a mouse model for Rett syndrome reveals subtle transcriptional changes in the brain
    • Tudor M, Akbarian S, Chen RZ, et al. Transcriptional profiling of a mouse model for Rett syndrome reveals subtle transcriptional changes in the brain. Proc Natl Acad Sci USA 2002;99:15536-41.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 15536-15541
    • Tudor, M.1    Akbarian, S.2    Chen, R.Z.3
  • 83
    • 8744229966 scopus 로고    scopus 로고
    • MeCP2 behaves as an elongated monomer that does not stably associate with the Sin3a chromatin remodeling complex
    • Klose RJ, Bird AP. MeCP2 behaves as an elongated monomer that does not stably associate with the Sin3a chromatin remodeling complex. J Biol Chem 2004;279: 46490-6.
    • (2004) J Biol Chem , vol.279 , pp. 46490-46496
    • Klose, R.J.1    Bird, A.P.2
  • 85
    • 79960619676 scopus 로고    scopus 로고
    • Role of ATRX in chromatin structure and function: implications for chromosome instability and human disease
    • De La Fuente R, Baumann C, Viveiros MM. Role of ATRX in chromatin structure and function: implications for chromosome instability and human disease. Reproduction 2011;142:221-34.
    • (2011) Reproduction , vol.142 , pp. 221-234
    • De La Fuente, R.1    Baumann, C.2    Viveiros, M.M.3
  • 86
    • 33847282970 scopus 로고    scopus 로고
    • Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation
    • Nan X, Hou J, Maclean A, et al. Interaction between chromatin proteins MECP2 and ATRX is disrupted by mutations that cause inherited mental retardation. Proc Natl Acad SciUSA 2007;104:2709-14.
    • (2007) Proc Natl Acad SciUSA , vol.104 , pp. 2709-2714
    • Nan, X.1    Hou, J.2    Maclean, A.3
  • 87
    • 76249083210 scopus 로고    scopus 로고
    • ATRX partners with cohesin and MeCP2 and contributes to developmental silencing of imprinted genes in the brain
    • Kernohan KD, Jiang Y, Tremblay DC, et al. ATRX partners with cohesin and MeCP2 and contributes to developmental silencing of imprinted genes in the brain. DevCell 2010;18: 191-202.
    • (2010) DevCell , vol.18 , pp. 191-202
    • Kernohan, K.D.1    Jiang, Y.2    Tremblay, D.C.3
  • 88
    • 67549119096 scopus 로고    scopus 로고
    • CTCF: master weaver of the genome
    • Phillips JE, Corces VG. CTCF: master weaver of the genome. Cell 2009;137:1194-211.
    • (2009) Cell , vol.137 , pp. 1194-1211
    • Phillips, J.E.1    Corces, V.G.2
  • 89
    • 80053997718 scopus 로고    scopus 로고
    • MeCP2 Rett mutations affect large scale chromatin organization
    • Agarwal N, Becker A, Jost KL, et al. MeCP2 Rett mutations affect large scale chromatin organization. Hum Mol Genet 2011;20(21):4187-95.
    • (2011) Hum Mol Genet , vol.20 , Issue.21 , pp. 4187-4195
    • Agarwal, N.1    Becker, A.2    Jost, K.L.3
  • 90
    • 11244328520 scopus 로고    scopus 로고
    • Loss of silent-chromatin looping and impaired imprinting of DLX5 in Rett syndrome
    • Horike S, Cai S, Miyano M, et al. Loss of silent-chromatin looping and impaired imprinting of DLX5 in Rett syndrome. Nat Genet 2005;37:31-40.
    • (2005) Nat Genet , vol.37 , pp. 31-40
    • Horike, S.1    Cai, S.2    Miyano, M.3
  • 91
    • 84883798471 scopus 로고    scopus 로고
    • PcG proteins, DNA methylation, and gene repression by chromatin looping
    • Tiwari VK, McGarvey KM, Licchesi JD, etal. PcG proteins, DNA methylation, and gene repression by chromatin looping. PLoS Biol 2008;6:2911-27.
    • (2008) PLoS Biol , vol.6 , pp. 2911-2927
    • Tiwari, V.K.1    McGarvey, K.M.2    Licchesi, J.D.3
  • 93
    • 79959869345 scopus 로고    scopus 로고
    • Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein
    • Nady N, Lemak A, Walker JR, et al. Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein. J Biol Chem 2011;286:24300-11.
    • (2011) J Biol Chem , vol.286 , pp. 24300-24311
    • Nady, N.1    Lemak, A.2    Walker, J.R.3
  • 94
    • 1542344326 scopus 로고    scopus 로고
    • Np95 is a histone-binding protein endowed with ubiquitin ligase activity
    • Citterio E, Papait R, Nicassio F, et al. Np95 is a histone-binding protein endowed with ubiquitin ligase activity. Mol Cell Biol 2004;24:2526-35.
    • (2004) Mol Cell Biol , vol.24 , pp. 2526-2535
    • Citterio, E.1    Papait, R.2    Nicassio, F.3
  • 95
    • 0036889390 scopus 로고    scopus 로고
    • Two ubiquitinconjugating enzymes, Rhp6 and UbcX, regulate heterochromatin silencing in Schizosaccharomyces pombe
    • Choi ES, Kim HS, Jang YK, et al. Two ubiquitinconjugating enzymes, Rhp6 and UbcX, regulate heterochromatin silencing in Schizosaccharomyces pombe. Mol Cell Biol 2002;22:8366-74.
    • (2002) Mol Cell Biol , vol.22 , pp. 8366-8374
    • Choi, E.S.1    Kim, H.S.2    Jang, Y.K.3
  • 96
    • 33644626412 scopus 로고    scopus 로고
    • Heterochromatin assembly: a new twist on an old model
    • Horn PJ, Peterson CL. Heterochromatin assembly: a new twist on an old model. Chromosome Res 2006;14:83-94.
    • (2006) Chromosome Res , vol.14 , pp. 83-94
    • Horn, P.J.1    Peterson, C.L.2
  • 98
    • 0037405867 scopus 로고    scopus 로고
    • The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1
    • Reese BE, Bachman KE, Baylin SB, et al. The methyl-CpG binding protein MBD1 interacts with the p150 subunit of chromatin assembly factor 1. MolCellBiol 2003;23:3226-36.
    • (2003) MolCellBiol , vol.23 , pp. 3226-3236
    • Reese, B.E.1    Bachman, K.E.2    Baylin, S.B.3
  • 99
    • 4344685735 scopus 로고    scopus 로고
    • Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly
    • Sarraf SA, Stancheva I. Methyl-CpG binding protein MBD1 couples histone H3 methylation at lysine 9 by SETDB1 to DNA replication and chromatin assembly. Mol Cell 2004;15:595-605.
    • (2004) Mol Cell , vol.15 , pp. 595-605
    • Sarraf, S.A.1    Stancheva, I.2
  • 100
    • 79957844585 scopus 로고    scopus 로고
    • DNA methylation and SETDB1/H3K9me3 regulate predominantly distinct sets of genes, retroelements, and chimeric transcripts in mESCs
    • Karimi MM, Goyal P, Maksakova IA, et al. DNA methylation and SETDB1/H3K9me3 regulate predominantly distinct sets of genes, retroelements, and chimeric transcripts in mESCs. Cell Stem Cell 2011;8:676-87.
    • (2011) Cell Stem Cell , vol.8 , pp. 676-687
    • Karimi, M.M.1    Goyal, P.2    Maksakova, I.A.3
  • 101
    • 0037591867 scopus 로고    scopus 로고
    • Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression
    • Fujita N, Watanabe S, Ichimura T, etal. Methyl-CpG binding domain 1 (MBD1) interacts with the Suv39h1-HP1 heterochromatic complex for DNA methylation-based transcriptional repression. J Biol Chem 2003;278:24132-8.
    • (2003) J Biol Chem , vol.278 , pp. 24132-24138
    • Fujita, N.1    Watanabe, S.2    Ichimura, T.3
  • 102
    • 34447504392 scopus 로고    scopus 로고
    • Overlapping roles of the methylated DNA-binding protein MBD1 and polycomb group proteins in transcriptional repression of HOXA genes and heterochromatin foci formation
    • Sakamoto Y, Watanabe S, Ichimura T, et al. Overlapping roles of the methylated DNA-binding protein MBD1 and polycomb group proteins in transcriptional repression of HOXA genes and heterochromatin foci formation. J Biol Chem 2007;282:16391-400.
    • (2007) J Biol Chem , vol.282 , pp. 16391-16400
    • Sakamoto, Y.1    Watanabe, S.2    Ichimura, T.3
  • 103
    • 0033883260 scopus 로고    scopus 로고
    • MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase
    • Tatematsu KI, Yamazaki T, Ishikawa F. MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase. Genes Cells 2000;5:677-88.
    • (2000) Genes Cells , vol.5 , pp. 677-688
    • Tatematsu, K.I.1    Yamazaki, T.2    Ishikawa, F.3
  • 104
    • 0038136913 scopus 로고    scopus 로고
    • Methyl-CpG-binding protein, MeCP2, is a target molecule for maintenance DNA methyltransferase Dnmt1
    • Kimura H, Shiota K. Methyl-CpG-binding protein, MeCP2, is a target molecule for maintenance DNA methyltransferase, Dnmt1. J BiolChem 2003;278:4806-12.
    • (2003) J BiolChem , vol.278 , pp. 4806-4812
    • Kimura, H.1    Shiota, K.2
  • 105
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation
    • Uchimura Y, Ichimura T, Uwada J, et al. Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation. J Biol Chem 2006;281: 23180-90.
    • (2006) J Biol Chem , vol.281 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3
  • 106
    • 33751099563 scopus 로고    scopus 로고
    • Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins
    • Lyst MJ, Nan X, Stancheva I. Regulation of MBD1-mediated transcriptional repression by SUMO and PIAS proteins. EMBOJ 2006;25:5317-28.
    • (2006) EMBOJ , vol.25 , pp. 5317-5328
    • Lyst, M.J.1    Nan, X.2    Stancheva, I.3
  • 107
    • 72949107120 scopus 로고    scopus 로고
    • The p150 subunit of CAF-1 causes association of SUMO2/3 with the DNA replication foci
    • Uwada J, Tanaka N, Yamaguchi Y, et al. The p150 subunit of CAF-1 causes association of SUMO2/3 with the DNA replication foci. Biochem Biophys Res Commun 2010;391: 407-13.
    • (2010) Biochem Biophys Res Commun , vol.391 , pp. 407-413
    • Uwada, J.1    Tanaka, N.2    Yamaguchi, Y.3
  • 108
    • 36749009119 scopus 로고    scopus 로고
    • PHD domainmediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing
    • Ivanov AV, Peng H, Yurchenko V, et al. PHD domainmediated E3 ligase activity directs intramolecular sumoylation of an adjacent bromodomain required for gene silencing. Mol Cell 2007;28:823-37.
    • (2007) Mol Cell , vol.28 , pp. 823-837
    • Ivanov, A.V.1    Peng, H.2    Yurchenko, V.3
  • 109
    • 77149144362 scopus 로고    scopus 로고
    • ERG-associated protein with SET domain (ESET)-Oct4 interaction regulates pluripotency and represses the trophectoderm lineage
    • Yeap LS, Hayashi K, Surani MA. ERG-associated protein with SET domain (ESET)-Oct4 interaction regulates pluripotency and represses the trophectoderm lineage. Epigenet Chromatin 2009;2:12.
    • (2009) Epigenet Chromatin , vol.2 , pp. 12
    • Yeap, L.S.1    Hayashi, K.2    Surani, M.A.3
  • 110
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau JR, Lima CD. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat RevMol Cell Biol 2010;11:861-71.
    • (2010) Nat RevMol Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 111
    • 79959335296 scopus 로고    scopus 로고
    • Twists and turns of DNA methylation
    • 8919-20
    • Frauer C, Leonhardt H. Twists and turns of DNA methylation. ProcNatl Acad SciUSA 2011;108:8919-20. 112.
    • (2011) ProcNatl Acad SciUSA , vol.108 , pp. 112
    • Frauer, C.1    Leonhardt, H.2
  • 112
    • 39149094639 scopus 로고    scopus 로고
    • Cytosine methylation: remaining faithful
    • Ooi SK, Bestor TH. Cytosine methylation: remaining faithful. Curr Biol 2008;18:R174-6.
    • (2008) Curr Biol , vol.18
    • Ooi, S.K.1    Bestor, T.H.2
  • 113
    • 53649088595 scopus 로고    scopus 로고
    • Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1
    • Avvakumov GV, Walker JR, Xue S, et al. Structural basis for recognition of hemi-methylated DNA by the SRA domain of human UHRF1. Nature 2008;455:822-5.
    • (2008) Nature , vol.455 , pp. 822-825
    • Avvakumov, G.V.1    Walker, J.R.2    Xue, S.3
  • 114
    • 59649127791 scopus 로고    scopus 로고
    • UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells
    • Kim JK, Esteve PO, Jacobsen SE, et al. UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells. Nucleic Acids Res 2009;37:493-505.
    • (2009) Nucleic Acids Res , vol.37 , pp. 493-505
    • Kim, J.K.1    Esteve, P.O.2    Jacobsen, S.E.3
  • 115
    • 0033857546 scopus 로고    scopus 로고
    • Temporal and spatial localization of novel nuclear protein NP95 in mitotic and meiotic cells
    • Uemura T, Kubo E, Kanari Y, et al. Temporal and spatial localization of novel nuclear protein NP95 in mitotic and meiotic cells. Cell Struct Funct 2000;25:149-59.
    • (2000) Cell Struct Funct , vol.25 , pp. 149-159
    • Uemura, T.1    Kubo, E.2    Kanari, Y.3
  • 116
    • 41649115827 scopus 로고    scopus 로고
    • The interaction of the SRA domain of ICBP90 with a novel domain of DNMT1 is involved in the regulation of VEGF gene expression
    • Achour M, Jacq X, Ronde P, et al. The interaction of the SRA domain of ICBP90 with a novel domain of DNMT1 is involved in the regulation of VEGF gene expression. Oncogene 2008;27:2187-97.
    • (2008) Oncogene , vol.27 , pp. 2187-2197
    • Achour, M.1    Jacq, X.2    Ronde, P.3
  • 117
    • 53649097070 scopus 로고    scopus 로고
    • Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism
    • Arita K, Ariyoshi M, Tochio H, et al. Recognition of hemi-methylated DNA by the SRA protein UHRF1 by a base-flipping mechanism. Nature 2008;455:818-21.
    • (2008) Nature , vol.455 , pp. 818-821
    • Arita, K.1    Ariyoshi, M.2    Tochio, H.3
  • 118
    • 53649089723 scopus 로고    scopus 로고
    • The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix
    • Hashimoto H, Horton JR, Zhang X, et al. The SRA domain of UHRF1 flips 5-methylcytosine out of the DNA helix. Nature 2008;455:826-9.
    • (2008) Nature , vol.455 , pp. 826-829
    • Hashimoto, H.1    Horton, J.R.2    Zhang, X.3
  • 119
    • 58049193603 scopus 로고    scopus 로고
    • Structure and hemimethylated CpG binding of the SRA domain from human UHRF1
    • Qian C, Li S, Jakoncic J, etal. Structure and hemimethylated CpG binding of the SRA domain from human UHRF1. J Biol Chem 2008;283:34490-4.
    • (2008) J Biol Chem , vol.283 , pp. 34490-34494
    • Qian, C.1    Li, S.2    Jakoncic, J.3
  • 120
    • 79251508434 scopus 로고    scopus 로고
    • UHRF1 links the histone code and DNA methylation to ensure faithful epigenetic memory inheritance
    • Bronner C, Fuhrmann G, Chedin FL, et al. UHRF1 links the histone code and DNA methylation to ensure faithful epigenetic memory inheritance. Genet Epigenet 2011;2009: 29-36.
    • (2011) Genet Epigenet , vol.2009 , pp. 29-36
    • Bronner, C.1    Fuhrmann, G.2    Chedin, F.L.3
  • 121
    • 53549133654 scopus 로고    scopus 로고
    • Reading and writing DNA methylation
    • Jeltsch A. Reading and writing DNA methylation. Nat StructMol Biol 2008;15:1003-4.
    • (2008) Nat StructMol Biol , vol.15 , pp. 1003-1004
    • Jeltsch, A.1
  • 122
    • 79251504611 scopus 로고    scopus 로고
    • Control of DNMT1 abundance in epigenetic inheritance by acetylation, ubiquitylation, and the histone code
    • Bronner C. Control of DNMT1 abundance in epigenetic inheritance by acetylation, ubiquitylation, and the histone code. Sci Signal 2011;4:pe3.
    • (2011) Sci Signal , vol.4
    • Bronner, C.1
  • 123
    • 78049510229 scopus 로고    scopus 로고
    • DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylationdriven ubiquitination
    • Du Z, Song J, Wang Y, et al. DNMT1 stability is regulated by proteins coordinating deubiquitination and acetylationdriven ubiquitination. Sci Signal 2011;3:ra80.
    • (2011) Sci Signal , vol.3
    • Du, Z.1    Song, J.2    Wang, Y.3
  • 124
    • 79251489223 scopus 로고    scopus 로고
    • Usp7 Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1
    • Qin W, Leonhardt H, Spada F. Usp7 and Uhrf1 control ubiquitination and stability of the maintenance DNA methyltransferase Dnmt1. JCellBiochem 2011;112:439-44.
    • (2011) JCellBiochem , vol.112 , pp. 439-444
    • Qin, W.1    Leonhardt, H.2    Spada, F.3
  • 125
    • 77955311548 scopus 로고    scopus 로고
    • Disruption of Dnmt1/ PCNA/UHRF1 interactions promotes tumorigenesis from human and mice glial cells
    • Hervouet E, Lalier L, Debien E, etal. Disruption of Dnmt1/ PCNA/UHRF1 interactions promotes tumorigenesis from human and mice glial cells. PLoS One 2011;5:e11333.
    • (2011) PLoS One , vol.5
    • Hervouet, E.1    Lalier, L.2    Debien, E.3
  • 126
    • 44349186294 scopus 로고    scopus 로고
    • Epigenetic regulation of heterochromatic DNA stability
    • Peng JC, Karpen GH. Epigenetic regulation of heterochromatic DNA stability. Curr Opin GenetDev 2008;18:204-11.
    • (2008) Curr Opin GenetDev , vol.18 , pp. 204-211
    • Peng, J.C.1    Karpen, G.H.2
  • 127
    • 78549247463 scopus 로고    scopus 로고
    • L1 retrotransposition in neurons is modulated by MeCP2
    • Muotri AR, Marchetto MC, Coufal NG, et al. L1 retrotransposition in neurons is modulated by MeCP2. Nature 2010;468:443-6.
    • (2010) Nature , vol.468 , pp. 443-446
    • Muotri, A.R.1    Marchetto, M.C.2    Coufal, N.G.3
  • 128
    • 0037636512 scopus 로고    scopus 로고
    • Mice lacking methyl-CpG binding protein 1 have deficits in adult neurogenesis and hippocampal function
    • Zhao X, Ueba T, Christie BR, et al. Mice lacking methyl-CpG binding protein 1 have deficits in adult neurogenesis and hippocampal function. Proc Natl Acad Sci USA 2003;100:6777-82.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6777-6782
    • Zhao, X.1    Ueba, T.2    Christie, B.R.3
  • 129
    • 0242363151 scopus 로고    scopus 로고
    • Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin
    • Watanabe S, Ichimura T, Fujita N, et al. Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin. Proc Natl Acad Sci USA 2003;100: 12859-64.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12859-12864
    • Watanabe, S.1    Ichimura, T.2    Fujita, N.3
  • 130
    • 0033575886 scopus 로고    scopus 로고
    • The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites
    • Hendrich B, Hardeland U, Ng HH, et al. The thymine glycosylase MBD4 can bind to the product of deamination at methylated CpG sites. Nature 1999;401:301-4.
    • (1999) Nature , vol.401 , pp. 301-304
    • Hendrich, B.1    Hardeland, U.2    Ng, H.H.3
  • 131
    • 57649196594 scopus 로고    scopus 로고
    • DNA demethylation in zebrafish involves the coupling of a deaminase, a glycosylase, and gadd45
    • Rai K, Huggins IJ, James SR, et al. DNA demethylation in zebrafish involves the coupling of a deaminase, a glycosylase, and gadd45. Cell 2008;135:1201-12.
    • (2008) Cell , vol.135 , pp. 1201-1212
    • Rai, K.1    Huggins, I.J.2    James, S.R.3
  • 132
    • 70350044885 scopus 로고    scopus 로고
    • DNA demethylation in hormone-induced transcriptional derepression
    • Kim MS, Kondo T, Takada I, et al. DNA demethylation in hormone-induced transcriptional derepression. Nature 2009; 461:1007-12.
    • (2009) Nature , vol.461 , pp. 1007-1012
    • Kim, M.S.1    Kondo, T.2    Takada, I.3
  • 133
    • 77956095231 scopus 로고    scopus 로고
    • Active DNA demethylation: many roads lead to Rome
    • Wu SC, Zhang Y. Active DNA demethylation: many roads lead to Rome. Nat RevMol Cell Biol 2010;11:607-20.
    • (2010) Nat RevMol Cell Biol , vol.11 , pp. 607-620
    • Wu, S.C.1    Zhang, Y.2
  • 134
    • 78649513916 scopus 로고    scopus 로고
    • Mammalian methylbinding proteins: what might they do?
    • Joulie M, Miotto B, Defossez PA. Mammalian methylbinding proteins: what might they do? Bioessays 2010;32: 1025-32.
    • (2010) Bioessays , vol.32 , pp. 1025-1032
    • Joulie, M.1    Miotto, B.2    Defossez, P.A.3
  • 135
    • 80555156105 scopus 로고    scopus 로고
    • In embryonic stem cells ZFP57/KAP1 recognize a methylated hexanucleotide to affect chromatin and DNA methylation of imprinting control regions
    • Quenneville S, Verde G, Corsinotti A, et al. In embryonic stem cells, ZFP57/KAP1 recognize a methylated hexanucleotide to affect chromatin and DNA methylation of imprinting control regions. Mol Cell 2011;44:361-72.
    • (2011) Mol Cell , vol.44 , pp. 361-372
    • Quenneville, S.1    Verde, G.2    Corsinotti, A.3
  • 136
    • 66149123748 scopus 로고    scopus 로고
    • The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain
    • Kriaucionis S, Heintz N. The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain. Science 2009;324:929-30.
    • (2009) Science , vol.324 , pp. 929-930
    • Kriaucionis, S.1    Heintz, N.2
  • 137
    • 66149146320 scopus 로고    scopus 로고
    • Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1
    • Tahiliani M, Koh KP, Shen Y, et al. Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1. Science 2009;324:930-5.
    • (2009) Science , vol.324 , pp. 930-935
    • Tahiliani, M.1    Koh, K.P.2    Shen, Y.3
  • 138
    • 79961125686 scopus 로고    scopus 로고
    • Tet1 and 5-hydroxymethylation: A genome-wide view in mouse embryonic stem cells
    • Wu H, Zhang Y. Tet1 and 5-hydroxymethylation: A genome-wide view in mouse embryonic stem cells. Cell Cycle 2011;10:2428-36.
    • (2011) Cell Cycle , vol.10 , pp. 2428-2436
    • Wu, H.1    Zhang, Y.2
  • 139
    • 77749277177 scopus 로고    scopus 로고
    • The behaviour of 5-hydroxymethylcytosine in bisulfite sequencing
    • Huang Y, Pastor WA, Shen Y, et al. The behaviour of 5-hydroxymethylcytosine in bisulfite sequencing. PLoS One 2010;5:e8888.
    • (2010) PLoS One , vol.5
    • Huang, Y.1    Pastor, W.A.2    Shen, Y.3
  • 140
    • 77954362183 scopus 로고    scopus 로고
    • Examination of the specificity of DNA methylation profiling techniques towards 5-methylcytosine and 5-hydroxymethylcytosine
    • Jin SG, Kadam S, Pfeifer GP. Examination of the specificity of DNA methylation profiling techniques towards 5-methylcytosine and 5-hydroxymethylcytosine. Nucleic Acids Res 2010;38(11):e125.
    • (2010) Nucleic Acids Res , vol.38 , Issue.11
    • Jin, S.G.1    Kadam, S.2    Pfeifer, G.P.3
  • 141
    • 77954061853 scopus 로고    scopus 로고
    • Enzymatic approaches and bisulfite sequencing cannot distinguish between 5-methylcytosine and 5-hydroxymethylcytosine in DNA
    • Nestor C, Ruzov A, Meehan R, etal. Enzymatic approaches and bisulfite sequencing cannot distinguish between 5-methylcytosine and 5-hydroxymethylcytosine in DNA. Biotechniques 2010;48:317-9.
    • (2010) Biotechniques , vol.48 , pp. 317-319
    • Nestor, C.1    Ruzov, A.2    Meehan, R.3
  • 142
    • 79960273984 scopus 로고    scopus 로고
    • Characterization of PvuRts1I endonuclease as a tool to investigate genomic 5-hydroxymethylcytosine
    • Szwagierczak A, Brachmann A, Schmidt CS, et al. Characterization of PvuRts1I endonuclease as a tool to investigate genomic 5-hydroxymethylcytosine. Nucleic Acids Res 2011;39:5149-56.
    • (2011) Nucleic Acids Res , vol.39 , pp. 5149-5156
    • Szwagierczak, A.1    Brachmann, A.2    Schmidt, C.S.3
  • 143
    • 78049401678 scopus 로고    scopus 로고
    • Sensitive enzymatic quantification of 5-hydroxymethylcytosine in genomic DNA
    • Szwagierczak A, Bultmann S, Schmidt CS, et al. Sensitive enzymatic quantification of 5-hydroxymethylcytosine in genomic DNA. Nucleic Acids Res 2011;38:e181.
    • (2011) Nucleic Acids Res , vol.38
    • Szwagierczak, A.1    Bultmann, S.2    Schmidt, C.S.3
  • 144
    • 4043112183 scopus 로고    scopus 로고
    • Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2)
    • Valinluck V, Tsai HH, Rogstad DK, etal. Oxidative damage to methyl-CpG sequences inhibits the binding of the methyl-CpG binding domain (MBD) of methyl-CpG binding protein 2 (MeCP2). Nucleic Acids Res 2004;32:4100-8.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4100-4108
    • Valinluck, V.1    Tsai, H.H.2    Rogstad, D.K.3
  • 145
    • 79959431845 scopus 로고    scopus 로고
    • Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain
    • Frauer C, Hoffmann T, Bultmann S, et al. Recognition of 5-hydroxymethylcytosine by the Uhrf1 SRA domain. PLoS One 2011;6:e21306.
    • (2011) PLoS One , vol.6
    • Frauer, C.1    Hoffmann, T.2    Bultmann, S.3
  • 146
    • 80051712275 scopus 로고    scopus 로고
    • Emerging roles of TET proteins and 5-hydroxymethylcytosines in active DNA demethylation and beyond
    • Guo JU, Su Y, Zhong C, et al. Emerging roles of TET proteins and 5-hydroxymethylcytosines in active DNA demethylation and beyond. Cell Cycle 2011;10:2662-8.
    • (2011) Cell Cycle , vol.10 , pp. 2662-2668
    • Guo, J.U.1    Su, Y.2    Zhong, C.3


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