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Volumn 319, Issue , 2015, Pages 165-220

Emerging Roles of JmjC Domain-Containing Proteins

Author keywords

FIH; Histone demethylase; JmjC; Jumonji C domain; KDM; LSD1; PAD4

Indexed keywords

2 OXOGLUTARIC ACID; HISTONE; HISTONE DEMETHYLASE; IRON; JMJC DOMAIN CONTAINING PROTEIN; UNCLASSIFIED DRUG; HISTONE LYSINE METHYLTRANSFERASE; HISTONE METHYLTRANSFERASE; VEGETABLE PROTEIN;

EID: 84939817245     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ircmb.2015.07.003     Document Type: Article
Times cited : (76)

References (176)
  • 1
    • 57349176997 scopus 로고    scopus 로고
    • Mutations in JARID1C are associated with X-linked mental retardation, short stature and hyperreflexia
    • Abidi F.E., et al. Mutations in JARID1C are associated with X-linked mental retardation, short stature and hyperreflexia. J. Med. Genet. 2008, 45:787-793.
    • (2008) J. Med. Genet. , vol.45 , pp. 787-793
    • Abidi, F.E.1
  • 2
    • 34347341762 scopus 로고    scopus 로고
    • A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate
    • Abidi F.E., et al. A novel mutation in the PHF8 gene is associated with X-linked mental retardation with cleft lip/cleft palate. Clin. Genet. 2007, 72:19-22.
    • (2007) Clin. Genet. , vol.72 , pp. 19-22
    • Abidi, F.E.1
  • 4
    • 38849159213 scopus 로고    scopus 로고
    • A novel mutation in JARID1C/SMCX in a patient with autism spectrum disorder (ASD)
    • Adegbola A., et al. A novel mutation in JARID1C/SMCX in a patient with autism spectrum disorder (ASD). Am. J. Med. Genet. A 2008, 146A:505-511.
    • (2008) Am. J. Med. Genet. A , vol.146 A , pp. 505-511
    • Adegbola, A.1
  • 5
    • 44149105533 scopus 로고    scopus 로고
    • The emerging functions of histone demethylases
    • Agger K., et al. The emerging functions of histone demethylases. Curr. Opin. Genet. Dev. 2008, 18:159-168.
    • (2008) Curr. Opin. Genet. Dev. , vol.18 , pp. 159-168
    • Agger, K.1
  • 6
    • 66149138053 scopus 로고    scopus 로고
    • The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence
    • Agger K., et al. The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence. Genes Dev. 2009, 23:1171-1176.
    • (2009) Genes Dev. , vol.23 , pp. 1171-1176
    • Agger, K.1
  • 7
    • 35148867907 scopus 로고    scopus 로고
    • UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
    • Agger K., et al. UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development. Nature 2007, 449:731-734.
    • (2007) Nature , vol.449 , pp. 731-734
    • Agger, K.1
  • 8
    • 37249024572 scopus 로고    scopus 로고
    • Structure and mechanism of lysine-specific demethylase enzymes
    • Anand R., Marmorstein R. Structure and mechanism of lysine-specific demethylase enzymes. J. Biol. Chem. 2007, 282:35425-35429.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35425-35429
    • Anand, R.1    Marmorstein, R.2
  • 9
    • 0038655454 scopus 로고    scopus 로고
    • A novel jmjC domain protein modulates heterochromatization in fission yeast
    • Ayoub N., et al. A novel jmjC domain protein modulates heterochromatization in fission yeast. Mol. Cell Biol. 2003, 23:4356-4370.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4356-4370
    • Ayoub, N.1
  • 10
    • 66149135288 scopus 로고    scopus 로고
    • Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS
    • Barradas M., et al. Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS. Genes Dev. 2009, 23:1177-1182.
    • (2009) Genes Dev. , vol.23 , pp. 1177-1182
    • Barradas, M.1
  • 11
    • 0037145309 scopus 로고    scopus 로고
    • PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?
    • Barrett A., et al. PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?. Int. J. Cancer 2002, 101:581-588.
    • (2002) Int. J. Cancer , vol.101 , pp. 581-588
    • Barrett, A.1
  • 12
    • 34250320926 scopus 로고    scopus 로고
    • Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases
    • Barrett A., et al. Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts directly with histone deacetylases. Int. J. Cancer 2007, 121:265-275.
    • (2007) Int. J. Cancer , vol.121 , pp. 265-275
    • Barrett, A.1
  • 13
    • 34948900481 scopus 로고    scopus 로고
    • Histone H3K4 demethylases are essential in development and differentiation
    • Benevolenskaya E.V. Histone H3K4 demethylases are essential in development and differentiation. Biochem. Cell Biol. Biochim. Biol. Cell. 2007, 85:435-443.
    • (2007) Biochem. Cell Biol. Biochim. Biol. Cell. , vol.85 , pp. 435-443
    • Benevolenskaya, E.V.1
  • 14
    • 61349088682 scopus 로고    scopus 로고
    • The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF
    • Beyer S., et al. The histone demethylases JMJD1A and JMJD2B are transcriptional targets of hypoxia-inducible factor HIF. J. Biol. Chem. 2008, 283:36542-36552.
    • (2008) J. Biol. Chem. , vol.283 , pp. 36542-36552
    • Beyer, S.1
  • 15
    • 78649920344 scopus 로고    scopus 로고
    • Conserved antagonism between JMJD2A/KDM4A and HP1gamma during cell cycle progression
    • Black J.C., et al. Conserved antagonism between JMJD2A/KDM4A and HP1gamma during cell cycle progression. Mol. Cell 2010, 40:736-748.
    • (2010) Mol. Cell , vol.40 , pp. 736-748
    • Black, J.C.1
  • 16
    • 79953708822 scopus 로고    scopus 로고
    • Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer
    • Blair L.P., et al. Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer. Cancers 2011, 3:1383-1404.
    • (2011) Cancers , vol.3 , pp. 1383-1404
    • Blair, L.P.1
  • 17
    • 23044433837 scopus 로고    scopus 로고
    • The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal
    • Bose J., et al. The phosphatidylserine receptor has essential functions during embryogenesis but not in apoptotic cell removal. J. Biol. 2004, 3:15.
    • (2004) J. Biol. , vol.3 , pp. 15
    • Bose, J.1
  • 18
    • 35348938519 scopus 로고    scopus 로고
    • JMJD6 is a histone arginine demethylase
    • Chang B.S., et al. JMJD6 is a histone arginine demethylase. Science 2007, 318:444-447.
    • (2007) Science , vol.318 , pp. 444-447
    • Chang, B.S.1
  • 19
    • 79961209798 scopus 로고    scopus 로고
    • Epigenetic gene regulation by plant Jumonji group of histone demethylase
    • Chen X., et al. Epigenetic gene regulation by plant Jumonji group of histone demethylase. Biochim. Biophys. Acta 2011, 1809:421-426.
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 421-426
    • Chen, X.1
  • 20
    • 34547471432 scopus 로고    scopus 로고
    • Structural basis of the recognition of a methylated histone tail by JMJD2A
    • Chen Z.Z., et al. Structural basis of the recognition of a methylated histone tail by JMJD2A. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:10818-10823.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 10818-10823
    • Chen, Z.Z.1
  • 21
    • 34547122520 scopus 로고    scopus 로고
    • PTIP associates with MLL3-and MLL4-containing histone H3 lysine 4 methyltransferase complex
    • Cho Y.W., et al. PTIP associates with MLL3-and MLL4-containing histone H3 lysine 4 methyltransferase complex. J. Biol. Chem. 2007, 282:20395-20406.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20395-20406
    • Cho, Y.W.1
  • 22
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri- and dimethylated lysine 4 on histone 3
    • Christensen J., et al. RBP2 belongs to a family of demethylases, specific for tri- and dimethylated lysine 4 on histone 3. Cell 2007, 128:1063-1076.
    • (2007) Cell , vol.128 , pp. 1063-1076
    • Christensen, J.1
  • 23
    • 10144255178 scopus 로고    scopus 로고
    • The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity
    • Cikala M., et al. The phosphatidylserine receptor from Hydra is a nuclear protein with potential Fe(II) dependent oxygenase activity. BMC Cell Biol. 2004, 5:26.
    • (2004) BMC Cell Biol. , vol.5 , pp. 26
    • Cikala, M.1
  • 25
    • 33645891676 scopus 로고    scopus 로고
    • Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins
    • Clifton I.J., et al. Structural studies on 2-oxoglutarate oxygenases and related double-stranded beta-helix fold proteins. J. Inorg. Biochem. 2006, 100:644-669.
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 644-669
    • Clifton, I.J.1
  • 26
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
    • Cloos P.A., et al. The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature 2006, 442:307-311.
    • (2006) Nature , vol.442 , pp. 307-311
    • Cloos, P.A.1
  • 27
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease
    • Cloos P.A.C., et al. Erasing the methyl mark: histone demethylases at the center of cellular differentiation and disease. Genes Dev. 2008, 22:1115-1140.
    • (2008) Genes Dev. , vol.22 , pp. 1115-1140
    • Cloos, P.A.C.1
  • 28
    • 34547688895 scopus 로고    scopus 로고
    • Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase
    • Couture J.F., et al. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nat. Struct. Mol. Biol. 2007, 14:689-695.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 689-695
    • Couture, J.F.1
  • 29
    • 0346690073 scopus 로고    scopus 로고
    • Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals
    • Cui P., et al. Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals. Exp. Cell Res. 2004, 293:154-163.
    • (2004) Exp. Cell Res. , vol.293 , pp. 154-163
    • Cui, P.1
  • 30
    • 35348812522 scopus 로고    scopus 로고
    • LSD1 and the chemistry of histone demethylation
    • Culhane J.C., Cole P.A. LSD1 and the chemistry of histone demethylation. Curr. Opin. Chem. Biol. 2007, 11:561-568.
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 561-568
    • Culhane, J.C.1    Cole, P.A.2
  • 31
    • 4444372638 scopus 로고    scopus 로고
    • Histone deimination antagonizes arginine methylation
    • Cuthbert G.L., et al. Histone deimination antagonizes arginine methylation. Cell 2004, 118:545-553.
    • (2004) Cell , vol.118 , pp. 545-553
    • Cuthbert, G.L.1
  • 32
    • 70350754328 scopus 로고    scopus 로고
    • Jmjd3 contributes to the control of gene expression in LPS-activated macrophages
    • De Santa F., et al. Jmjd3 contributes to the control of gene expression in LPS-activated macrophages. EMBO J. 2009, 28:3341-3352.
    • (2009) EMBO J. , vol.28 , pp. 3341-3352
    • Santa, D.F.1
  • 33
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F., et al. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 2007, 130:1083-1094.
    • (2007) Cell , vol.130 , pp. 1083-1094
    • Santa, D.F.1
  • 34
    • 49349092791 scopus 로고    scopus 로고
    • The histone demethylase KDM5b/JARID1b plays a role in cell fate decisions by blocking terminal differentiation
    • Dey B.K., et al. The histone demethylase KDM5b/JARID1b plays a role in cell fate decisions by blocking terminal differentiation. Mol. Cell Biol. 2008, 28:5312-5327.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 5312-5327
    • Dey, B.K.1
  • 35
    • 0035663539 scopus 로고    scopus 로고
    • Evolution of functional diversity in the cupin superfamily
    • Dunwell J.M., et al. Evolution of functional diversity in the cupin superfamily. Trends Biochem. Sci. 2001, 26:740-746.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 740-746
    • Dunwell, J.M.1
  • 36
    • 34247253752 scopus 로고    scopus 로고
    • The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase
    • Eissenberg J.C., et al. The trithorax-group gene in Drosophila little imaginal discs encodes a trimethylated histone H3 Lys4 demethylase. Nat. Struct. Mol. Biol. 2007, 14:344-346.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 344-346
    • Eissenberg, J.C.1
  • 37
    • 0037449811 scopus 로고    scopus 로고
    • Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha
    • Elkins J.M., et al. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. J. Biol. Chem. 2003, 278:1802-1806.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1802-1806
    • Elkins, J.M.1
  • 38
    • 0034604029 scopus 로고    scopus 로고
    • A receptor for phosphatidylserine-specific clearance of apoptotic cells
    • Fadok V.A., et al. A receptor for phosphatidylserine-specific clearance of apoptotic cells. Nature 2000, 405:85-90.
    • (2000) Nature , vol.405 , pp. 85-90
    • Fadok, V.A.1
  • 39
    • 0041423663 scopus 로고    scopus 로고
    • Apoptosis: giving phosphatidylserine recognition an assist-with a twist
    • Fadok V.A., Henson P.M. Apoptosis: giving phosphatidylserine recognition an assist-with a twist. Curr. Biol. 2003, 13:R655-R657.
    • (2003) Curr. Biol. , vol.13 , pp. R655-R657
    • Fadok, V.A.1    Henson, P.M.2
  • 40
    • 34347342789 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2
    • Fang J., et al. The Saccharomyces cerevisiae histone demethylase Jhd1 fine-tunes the distribution of H3K36me2. Mol. Cell. Biol. 2007, 27:5055-5065.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5055-5065
    • Fang, J.1
  • 41
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng W., et al. PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation. Nat. Struct. Mol. Biol. 2010, 17:445-450.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 445-450
    • Feng, W.1
  • 42
    • 33745146571 scopus 로고    scopus 로고
    • Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells
    • Fodor B.D., et al. Jmjd2b antagonizes H3K9 trimethylation at pericentric heterochromatin in mammalian cells. Genes Dev. 2006, 20:1557-1562.
    • (2006) Genes Dev. , vol.20 , pp. 1557-1562
    • Fodor, B.D.1
  • 43
    • 41549132495 scopus 로고    scopus 로고
    • LSD1: oxidative chemistry for multifaceted functions in chromatin regulation
    • Forneris F., et al. LSD1: oxidative chemistry for multifaceted functions in chromatin regulation. Trends Biochem. Sci. 2008, 33:181-189.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 181-189
    • Forneris, F.1
  • 44
    • 78651240488 scopus 로고    scopus 로고
    • Plant homeodomain fingers form a helping hand for transcription
    • Fortschegger K., Shiekhattar R. Plant homeodomain fingers form a helping hand for transcription. Epigenetics 2011, 6.
    • (2011) Epigenetics , vol.6
    • Fortschegger, K.1    Shiekhattar, R.2
  • 45
    • 36049022778 scopus 로고    scopus 로고
    • JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
    • Frescas D., et al. JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes. Nature 2007, 450:309-313.
    • (2007) Nature , vol.450 , pp. 309-313
    • Frescas, D.1
  • 46
    • 56449126497 scopus 로고    scopus 로고
    • KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state
    • Frescas D., et al. KDM2A represses transcription of centromeric satellite repeats and maintains the heterochromatic state. Cell Cycle 2008, 7:3539-3547.
    • (2008) Cell Cycle , vol.7 , pp. 3539-3547
    • Frescas, D.1
  • 47
    • 77954507353 scopus 로고    scopus 로고
    • Regulation of H3K27me3 and H3K4me3 during early porcine embryonic development
    • Gao Y., et al. Regulation of H3K27me3 and H3K4me3 during early porcine embryonic development. Mol. Reprod. Dev. 2010, 77:540-549.
    • (2010) Mol. Reprod. Dev. , vol.77 , pp. 540-549
    • Gao, Y.1
  • 48
    • 23344436787 scopus 로고    scopus 로고
    • Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein
    • Gray S.G., et al. Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein. J. Biol. Chem. 2005, 280:28507-28518.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28507-28518
    • Gray, S.G.1
  • 49
    • 47249153638 scopus 로고    scopus 로고
    • Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins
    • Hahn P., et al. Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins. BMC Genomics 2008, 9:293.
    • (2008) BMC Genomics , vol.9 , pp. 293
    • Hahn, P.1
  • 50
    • 78149438134 scopus 로고    scopus 로고
    • Analysis of jmjd6 cellular localization and testing for its involvement in histone demethylation
    • Hahn P., et al. Analysis of jmjd6 cellular localization and testing for its involvement in histone demethylation. PLoS One 2010, 5:e13769.
    • (2010) PLoS One , vol.5
    • Hahn, P.1
  • 51
    • 0032788052 scopus 로고    scopus 로고
    • PHF2, a novel PHD finger gene located on human chromosome 9q22
    • Hasenpusch-Theil K., et al. PHF2, a novel PHD finger gene located on human chromosome 9q22. Mamm. Genome 1999, 10:294-298.
    • (1999) Mamm. Genome , vol.10 , pp. 294-298
    • Hasenpusch-Theil, K.1
  • 52
    • 79953815457 scopus 로고    scopus 로고
    • KDM2b/JHDM1b, an H3K36me2-specific demethylase, is required for initiation and maintenance of acute myeloid leukemia
    • He J., et al. KDM2b/JHDM1b, an H3K36me2-specific demethylase, is required for initiation and maintenance of acute myeloid leukemia. Blood 2011, 117:3869-3880.
    • (2011) Blood , vol.117 , pp. 3869-3880
    • He, J.1
  • 53
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery D.M., et al. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 1997, 387:733-736.
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1
  • 54
    • 77951980558 scopus 로고    scopus 로고
    • The H3K27me3 demethylase dUTX is a suppressor of Notch- and Rb-dependent tumors in Drosophila
    • Herz H.M., et al. The H3K27me3 demethylase dUTX is a suppressor of Notch- and Rb-dependent tumors in Drosophila. Mol. Cell Biol. 2010, 30:2485-2497.
    • (2010) Mol. Cell Biol. , vol.30 , pp. 2485-2497
    • Herz, H.M.1
  • 55
    • 36749082438 scopus 로고    scopus 로고
    • Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases
    • Hong S.H., et al. Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:18439-18444.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 18439-18444
    • Hong, S.H.1
  • 56
    • 77957061888 scopus 로고    scopus 로고
    • Interaction of JMJD6 with single-stranded RNA
    • Hong X., et al. Interaction of JMJD6 with single-stranded RNA. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:14568-14572.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 14568-14572
    • Hong, X.1
  • 57
    • 0025790483 scopus 로고
    • Analysis of a murine male germ cell-specific transcript that encodes a putative zinc finger protein
    • Hoog C., et al. Analysis of a murine male germ cell-specific transcript that encodes a putative zinc finger protein. Mol. Reprod. Dev. 1991, 30:173-181.
    • (1991) Mol. Reprod. Dev. , vol.30 , pp. 173-181
    • Hoog, C.1
  • 58
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton J.R., et al. Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases. Nat. Struct. Mol. Biol. 2010, 17:38-43.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 38-43
    • Horton, J.R.1
  • 59
    • 77954662295 scopus 로고    scopus 로고
    • Crosstalk between histone modifications maintains the developmental pattern of gene expression on a tissue-specific locus
    • Hosey A.M., et al. Crosstalk between histone modifications maintains the developmental pattern of gene expression on a tissue-specific locus. Epigenetics 2010, 5:273-281.
    • (2010) Epigenetics , vol.5 , pp. 273-281
    • Hosey, A.M.1
  • 60
    • 78649664485 scopus 로고    scopus 로고
    • Structural insights into histone lysine demethylation
    • Hou H., Yu H. Structural insights into histone lysine demethylation. Curr. Opin. Struct. Biol. 2010, 20:739-748.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 739-748
    • Hou, H.1    Yu, H.2
  • 61
    • 77953084666 scopus 로고    scopus 로고
    • KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation
    • Hsia D.A., et al. KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:9671-9676.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9671-9676
    • Hsia, D.A.1
  • 62
    • 0035909531 scopus 로고    scopus 로고
    • A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31
    • Hu Z., et al. A novel nuclear protein, 5qNCA (LOC51780) is a candidate for the myeloid leukemia tumor suppressor gene on chromosome 5 band q31. Oncogene 2001, 20:6946-6954.
    • (2001) Oncogene , vol.20 , pp. 6946-6954
    • Hu, Z.1
  • 63
    • 76449085537 scopus 로고    scopus 로고
    • Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4
    • Huang C., et al. Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4. Cell Res. 2010, 20:154-165.
    • (2010) Cell Res. , vol.20 , pp. 154-165
    • Huang, C.1
  • 64
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y., et al. Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A. Science 2006, 312:748-751.
    • (2006) Science , vol.312 , pp. 748-751
    • Huang, Y.1
  • 65
    • 34547585721 scopus 로고    scopus 로고
    • The fission yeast Jmj2 reverses histone H3 lysine 4 trimethylation
    • Huarte M., et al. The fission yeast Jmj2 reverses histone H3 lysine 4 trimethylation. J. Biol. Chem. 2007, 282:21662-21670.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21662-21670
    • Huarte, M.1
  • 66
    • 34249106820 scopus 로고    scopus 로고
    • Interaction of Epe1 with the heterochromatin assembly pathway in Schizosaccharomyces pombe
    • Isaac S., et al. Interaction of Epe1 with the heterochromatin assembly pathway in Schizosaccharomyces pombe. Genetics 2007, 175:1549-1560.
    • (2007) Genetics , vol.175 , pp. 1549-1560
    • Isaac, S.1
  • 67
    • 33947302685 scopus 로고    scopus 로고
    • The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases
    • Iwase S., et al. The X-linked mental retardation gene SMCX/JARID1C defines a family of histone H3 lysine 4 demethylases. Cell 2007, 128:1077-1088.
    • (2007) Cell , vol.128 , pp. 1077-1088
    • Iwase, S.1
  • 68
    • 0345286865 scopus 로고    scopus 로고
    • RPH1 and GIS1 are damage-responsive repressors of PHR1
    • Jang Y.K., et al. RPH1 and GIS1 are damage-responsive repressors of PHR1. Mol. Cell Biol. 1999, 19:7630-7638.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 7630-7638
    • Jang, Y.K.1
  • 69
    • 3242663720 scopus 로고    scopus 로고
    • Identification and characterization of TRIP8 gene in silico
    • Katoh M., Katoh M. Identification and characterization of TRIP8 gene in silico. Int. J. Mol. Med. 2003, 12:817-821.
    • (2003) Int. J. Mol. Med. , vol.12 , pp. 817-821
    • Katoh, M.1    Katoh, M.2
  • 70
    • 16544389546 scopus 로고    scopus 로고
    • Identification and characterization of JMJD2 family genes in silico
    • Katoh M., Katoh M. Identification and characterization of JMJD2 family genes in silico. Int. J. Oncol. 2004, 24:1623-1628.
    • (2004) Int. J. Oncol. , vol.24 , pp. 1623-1628
    • Katoh, M.1    Katoh, M.2
  • 71
    • 34548574729 scopus 로고    scopus 로고
    • Comparative integromics on JMJD1C gene encoding histone demethylase: conserved POU5F1 binding site elucidating mechanism of JMJD1C expression in undifferentiated ES cells and diffuse-type gastric cancer
    • Katoh M., Katoh M. Comparative integromics on JMJD1C gene encoding histone demethylase: conserved POU5F1 binding site elucidating mechanism of JMJD1C expression in undifferentiated ES cells and diffuse-type gastric cancer. Int. J. Oncol. 2007, 31:219-223.
    • (2007) Int. J. Oncol. , vol.31 , pp. 219-223
    • Katoh, M.1    Katoh, M.2
  • 72
    • 78049412365 scopus 로고    scopus 로고
    • Regulation of mouse steroidogenesis by WHISTLE and JMJD1C through histone methylation balance
    • Kim S.M., et al. Regulation of mouse steroidogenesis by WHISTLE and JMJD1C through histone methylation balance. Nucleic Acids Res. 2010, 38:6389-6403.
    • (2010) Nucleic Acids Res. , vol.38 , pp. 6389-6403
    • Kim, S.M.1
  • 73
    • 34547102488 scopus 로고    scopus 로고
    • Two Saccharomyces cerevisiae JmjC domain proteins demethylate histone H3 Lys(36) in transcribed regions to promote elongation
    • Kim T., Buratowski S. Two Saccharomyces cerevisiae JmjC domain proteins demethylate histone H3 Lys(36) in transcribed regions to promote elongation. J. Biol. Chem. 2007, 282:20827-20835.
    • (2007) J. Biol. Chem. , vol.282 , pp. 20827-20835
    • Kim, T.1    Buratowski, S.2
  • 74
    • 37449019096 scopus 로고    scopus 로고
    • Repression of Smad3 activity by histone demethylase SMCX/JARID1C
    • Kim T.D., et al. Repression of Smad3 activity by histone demethylase SMCX/JARID1C. Biochem. Biophys. Res. Commun. 2008, 366:563-567.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 563-567
    • Kim, T.D.1
  • 75
    • 34347346108 scopus 로고    scopus 로고
    • Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae?
    • Klose R.J., et al. Demethylation of histone H3K36 and H3K9 by Rph1: a vestige of an H3K9 methylation system in Saccharomyces cerevisiae?. Mol. Cell Biol. 2007, 27:3951-3961.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 3951-3961
    • Klose, R.J.1
  • 76
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose R.J., et al. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 2006, 7:715-727.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1
  • 77
    • 33847401344 scopus 로고    scopus 로고
    • The retinoblastoma binding protein RBP2 is an H3K4 demethylase
    • Klose R.J., et al. The retinoblastoma binding protein RBP2 is an H3K4 demethylase. Cell 2007, 128:889-900.
    • (2007) Cell , vol.128 , pp. 889-900
    • Klose, R.J.1
  • 78
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose R.J., Zhang Y. Regulation of histone methylation by demethylimination and demethylation. Nat. Rev. Mol. Cell Biol. 2007, 8:307-318.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 307-318
    • Klose, R.J.1    Zhang, Y.2
  • 79
    • 33748059529 scopus 로고    scopus 로고
    • Repression of transcription by TSGA/Jmjd1a, a novel interaction partner of the ETS protein ER71
    • Knebel J., et al. Repression of transcription by TSGA/Jmjd1a, a novel interaction partner of the ETS protein ER71. J. Cell Biochem. 2006, 99:319-329.
    • (2006) J. Cell Biochem. , vol.99 , pp. 319-329
    • Knebel, J.1
  • 80
    • 34547862845 scopus 로고    scopus 로고
    • Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate
    • Koivisto A.M., et al. Screening of mutations in the PHF8 gene and identification of a novel mutation in a Finnish family with XLMR and cleft lip/cleft palate. Clin. Genet. 2007, 72:145-149.
    • (2007) Clin. Genet. , vol.72 , pp. 145-149
    • Koivisto, A.M.1
  • 81
    • 34548349350 scopus 로고    scopus 로고
    • The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun
    • Koyama-Nasu R., et al. The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun. Nat. Cell Biol. 2007, 9:1074-1080.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1074-1080
    • Koyama-Nasu, R.1
  • 82
    • 84976318219 scopus 로고    scopus 로고
    • The leukemia gene 5qNCA is a tissue-specific co-repressor of retinoic acid receptor which interacts with c-Myb
    • 972-a-
    • Kravarusic J., et al. The leukemia gene 5qNCA is a tissue-specific co-repressor of retinoic acid receptor which interacts with c-Myb. AACR Meeting Abstracts 2004, 972-a-.
    • (2004) AACR Meeting Abstracts
    • Kravarusic, J.1
  • 83
    • 73549088729 scopus 로고    scopus 로고
    • Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth
    • Krieg A.J., et al. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Mol. Cell Biol. 2010, 30:344-353.
    • (2010) Mol. Cell Biol. , vol.30 , pp. 344-353
    • Krieg, A.J.1
  • 84
    • 78751610660 scopus 로고    scopus 로고
    • Structure and function of histone H3 lysine 9 methyltransferases and demethylases
    • Krishnan S., et al. Structure and function of histone H3 lysine 9 methyltransferases and demethylases. Chembiochem 2011, 12:254-263.
    • (2011) Chembiochem , vol.12 , pp. 254-263
    • Krishnan, S.1
  • 85
    • 35148898348 scopus 로고    scopus 로고
    • A histone H3 lysine 27 demethylase regulates animal posterior development
    • Lan F., et al. A histone H3 lysine 27 demethylase regulates animal posterior development. Nature 2007, 449:689-694.
    • (2007) Nature , vol.449 , pp. 689-694
    • Lan, F.1
  • 86
    • 44649163849 scopus 로고    scopus 로고
    • Mechanisms involved in the regulation of histone lysine demethylases
    • Lan F., et al. Mechanisms involved in the regulation of histone lysine demethylases. Curr. Opin. Cell Biol. 2008, 20:316-325.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 316-325
    • Lan, F.1
  • 87
    • 26944461197 scopus 로고    scopus 로고
    • Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate
    • Laumonnier F., et al. Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate. J. Med. Genet. 2005, 42:780-786.
    • (2005) J. Med. Genet. , vol.42 , pp. 780-786
    • Laumonnier, F.1
  • 88
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee M.G., et al. Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein. Cell 2007, 128:877-887.
    • (2007) Cell , vol.128 , pp. 877-887
    • Lee, M.G.1
  • 89
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • Lee M.G., et al. Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science 2007, 318:447-450.
    • (2007) Science , vol.318 , pp. 447-450
    • Lee, M.G.1
  • 90
    • 33644877451 scopus 로고    scopus 로고
    • SMART 5: domains in the context of genomes and networks
    • Letunic I., et al. SMART 5: domains in the context of genomes and networks. Nucleic Acids Res. 2006, 34:D257-D260.
    • (2006) Nucleic Acids Res. , vol.34 , pp. D257-D260
    • Letunic, I.1
  • 91
    • 0345374586 scopus 로고    scopus 로고
    • Phosphatidylserine receptor is required for clearance of apoptotic cells
    • Li M.O., et al. Phosphatidylserine receptor is required for clearance of apoptotic cells. Science 2003, 302:1560-1563.
    • (2003) Science , vol.302 , pp. 1560-1563
    • Li, M.O.1
  • 92
    • 77949366450 scopus 로고    scopus 로고
    • Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex
    • Liefke R., et al. Histone demethylase KDM5A is an integral part of the core Notch-RBP-J repressor complex. Genes Dev. 2010, 24:590-601.
    • (2010) Genes Dev. , vol.24 , pp. 590-601
    • Liefke, R.1
  • 93
    • 77956636685 scopus 로고    scopus 로고
    • Epigenetic regulation of cancer growth by histone demethylases
    • Lim S., et al. Epigenetic regulation of cancer growth by histone demethylases. Int. J. Cancer 2010, 127:1991-1998.
    • (2010) Int. J. Cancer , vol.127 , pp. 1991-1998
    • Lim, S.1
  • 94
    • 56849114113 scopus 로고    scopus 로고
    • Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase
    • Lin C.H., et al. Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase. Mol. Cell 2008, 32:696-706.
    • (2008) Mol. Cell , vol.32 , pp. 696-706
    • Lin, C.H.1
  • 95
    • 77954954200 scopus 로고    scopus 로고
    • PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression
    • Liu W., et al. PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression. Nature 2010, 466:508-512.
    • (2010) Nature , vol.466 , pp. 508-512
    • Liu, W.1
  • 96
    • 37349079055 scopus 로고    scopus 로고
    • The histone demethylase, Jmjd1a, interacts with the myocardin factors to regulate SMC differentiation marker gene expression
    • Lockman K., et al. The histone demethylase, Jmjd1a, interacts with the myocardin factors to regulate SMC differentiation marker gene expression. Circ. Res. 2007, 101:e115-23.
    • (2007) Circ. Res. , vol.101
    • Lockman, K.1
  • 97
    • 35348982301 scopus 로고    scopus 로고
    • Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells
    • Loh Y.H., et al. Jmjd1a and Jmjd2c histone H3 Lys 9 demethylases regulate self-renewal in embryonic stem cells. Genes Dev. 2007, 21:2545-2557.
    • (2007) Genes Dev. , vol.21 , pp. 2545-2557
    • Loh, Y.H.1
  • 98
    • 49349114931 scopus 로고    scopus 로고
    • Genome-wide analysis of the H3K4 histone demethylase RBP2 reveals a transcriptional program controlling differentiation
    • Lopez-Bigas N., et al. Genome-wide analysis of the H3K4 histone demethylase RBP2 reveals a transcriptional program controlling differentiation. Mol. Cell 2008, 31:520-530.
    • (2008) Mol. Cell , vol.31 , pp. 520-530
    • Lopez-Bigas, N.1
  • 99
    • 77949269527 scopus 로고    scopus 로고
    • JMJ14 is an H3K4 demethylase regulating flowering time in Arabidopsis
    • Lu F., et al. JMJ14 is an H3K4 demethylase regulating flowering time in Arabidopsis. Cell Res. 2010, 20:387-390.
    • (2010) Cell Res. , vol.20 , pp. 387-390
    • Lu, F.1
  • 100
    • 48249088454 scopus 로고    scopus 로고
    • Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice
    • Lu F., et al. Comparative analysis of JmjC domain-containing proteins reveals the potential histone demethylases in Arabidopsis and rice. J. Integr. Plant Biol. 2008, 50:886-896.
    • (2008) J. Integr. Plant Biol. , vol.50 , pp. 886-896
    • Lu, F.1
  • 101
    • 0038748632 scopus 로고    scopus 로고
    • A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer
    • Lu P.J., et al. A novel gene (PLU-1) containing highly conserved putative DNA/chromatin binding motifs is specifically up-regulated in breast cancer. J. Biol. Chem. 1999, 274:15633-15645.
    • (1999) J. Biol. Chem. , vol.274 , pp. 15633-15645
    • Lu, P.J.1
  • 102
    • 70349490830 scopus 로고    scopus 로고
    • Validation-based insertional mutagenesis identifies lysine demethylase FBXL11 as a negative regulator of NFkappaB
    • Lu T., et al. Validation-based insertional mutagenesis identifies lysine demethylase FBXL11 as a negative regulator of NFkappaB. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:16339-16344.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16339-16344
    • Lu, T.1
  • 103
    • 76249100563 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by NSD1/FBXL11-dependent reversible lysine methylation of p65
    • Lu T., et al. Regulation of NF-kappaB by NSD1/FBXL11-dependent reversible lysine methylation of p65. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:46-51.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 46-51
    • Lu, T.1
  • 104
    • 77955085896 scopus 로고    scopus 로고
    • Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6
    • Mantri M., et al. Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6. J. Mol. Biol. 2010, 401:211-222.
    • (2010) J. Mol. Biol. , vol.401 , pp. 211-222
    • Mantri, M.1
  • 105
    • 59449087016 scopus 로고    scopus 로고
    • Histone modifying enzymes: structures, mechanisms, and specificities
    • Marmorstein R., Trievel R.C. Histone modifying enzymes: structures, mechanisms, and specificities. Biochim. Biophys. Acta 2009, 1789:58-68.
    • (2009) Biochim. Biophys. Acta , vol.1789 , pp. 58-68
    • Marmorstein, R.1    Trievel, R.C.2
  • 106
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C., Zhang Y. The diverse functions of histone lysine methylation. Nat. Rev. Mol. Cell Biol. 2005, 6:838-849.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 838-849
    • Martin, C.1    Zhang, Y.2
  • 107
    • 34247242605 scopus 로고    scopus 로고
    • The expanding world of histone lysine demethylases
    • Metzger E., Schule R. The expanding world of histone lysine demethylases. Nat. Struct. Mol. Biol. 2007, 14:252-254.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 252-254
    • Metzger, E.1    Schule, R.2
  • 108
    • 79952817214 scopus 로고    scopus 로고
    • JmjC-domain-containing histone demethylases of the JMJD1B type as putative precursors of endogenous DSIP
    • Mikhaleva I.I., et al. JmjC-domain-containing histone demethylases of the JMJD1B type as putative precursors of endogenous DSIP. Peptides 2011, 32:826-831.
    • (2011) Peptides , vol.32 , pp. 826-831
    • Mikhaleva, I.I.1
  • 109
    • 77953644347 scopus 로고    scopus 로고
    • Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases
    • Mosammaparast N., Shi Y. Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases. Annu. Rev. Biochem. 2010, 79:155-179.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 155-179
    • Mosammaparast, N.1    Shi, Y.2
  • 110
    • 34447133035 scopus 로고    scopus 로고
    • Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity
    • Ng S.S., et al. Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature 2007, 448:87-91.
    • (2007) Nature , vol.448 , pp. 87-91
    • Ng, S.S.1
  • 111
    • 16444370435 scopus 로고    scopus 로고
    • Divergent roles of a pair of homologous jumonji/zinc-finger-class transcription factor proteins in the regulation of Arabidopsis flowering time
    • Noh B., et al. Divergent roles of a pair of homologous jumonji/zinc-finger-class transcription factor proteins in the regulation of Arabidopsis flowering time. Plant Cell 2004, 16:2601-2613.
    • (2004) Plant Cell , vol.16 , pp. 2601-2613
    • Noh, B.1
  • 112
    • 35948993829 scopus 로고    scopus 로고
    • Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis
    • Okada Y., et al. Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis. Nature 2007, 450:119-123.
    • (2007) Nature , vol.450 , pp. 119-123
    • Okada, Y.1
  • 113
    • 78049286684 scopus 로고    scopus 로고
    • Histone demethylases in development and disease
    • Pedersen M.T., Helin K. Histone demethylases in development and disease. Trends Cell Biol. 2010, 20:662-671.
    • (2010) Trends Cell Biol. , vol.20 , pp. 662-671
    • Pedersen, M.T.1    Helin, K.2
  • 114
    • 41149116609 scopus 로고    scopus 로고
    • Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process
    • Pfau R., et al. Members of a family of JmjC domain-containing oncoproteins immortalize embryonic fibroblasts via a JmjC domain-dependent process. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:1907-1912.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 1907-1912
    • Pfau, R.1
  • 115
    • 58949097017 scopus 로고    scopus 로고
    • Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha
    • Pollard P.J., et al. Regulation of Jumonji-domain-containing histone demethylases by hypoxia-inducible factor (HIF)-1alpha. Biochem. J. 2008, 416:387-394.
    • (2008) Biochem. J. , vol.416 , pp. 387-394
    • Pollard, P.J.1
  • 116
    • 57349151485 scopus 로고    scopus 로고
    • The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress
    • Polytarchou C., et al. The JmjC domain histone demethylase Ndy1 regulates redox homeostasis and protects cells from oxidative stress. Mol. Cell Biol. 2008, 28:7451-7464.
    • (2008) Mol. Cell Biol. , vol.28 , pp. 7451-7464
    • Polytarchou, C.1
  • 117
    • 70350134699 scopus 로고    scopus 로고
    • Identification of non-histone substrates for JMJD2A-C histone demethylases
    • Ponnaluri V.K., et al. Identification of non-histone substrates for JMJD2A-C histone demethylases. Biochem. Biophys. Res. Commun. 2009, 390:280-284.
    • (2009) Biochem. Biophys. Res. Commun. , vol.390 , pp. 280-284
    • Ponnaluri, V.K.1
  • 118
    • 77954957901 scopus 로고    scopus 로고
    • Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development
    • Qi H.H., et al. Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development. Nature 2010, 466:503-507.
    • (2010) Nature , vol.466 , pp. 503-507
    • Qi, H.H.1
  • 119
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J., et al. The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation. Cell Res. 2010, 20:908-918.
    • (2010) Cell Res. , vol.20 , pp. 908-918
    • Qiu, J.1
  • 120
    • 68449090024 scopus 로고    scopus 로고
    • Identification and characterization of demethylase JMJD1A as a gene upregulated in the human cellular response to hypoxia
    • Sar A., et al. Identification and characterization of demethylase JMJD1A as a gene upregulated in the human cellular response to hypoxia. Cell Tissue Res. 2009, 337:223-234.
    • (2009) Cell Tissue Res. , vol.337 , pp. 223-234
    • Sar, A.1
  • 121
    • 33749576106 scopus 로고    scopus 로고
    • Histone demethylation by hydroxylation: chemistry in action
    • Schneider J., Shilatifard A. Histone demethylation by hydroxylation: chemistry in action. ACS Chem. Biol. 2006, 1:75-81.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 75-81
    • Schneider, J.1    Shilatifard, A.2
  • 122
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J., et al. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5857-5864
    • Schultz, J.1
  • 123
    • 35148835080 scopus 로고    scopus 로고
    • Functional analysis of the transcription repressor PLU-1/JARID1B
    • Scibetta A.G., et al. Functional analysis of the transcription repressor PLU-1/JARID1B. Mol. Cell Biol. 2007, 27:7220-7235.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 7220-7235
    • Scibetta, A.G.1
  • 124
    • 77952352352 scopus 로고    scopus 로고
    • JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to-cell movement of an RNA silencing signal in Arabidopsis
    • Searle I.R., et al. JMJ14, a JmjC domain protein, is required for RNA silencing and cell-to-cell movement of an RNA silencing signal in Arabidopsis. Genes Dev. 2010, 24:986-991.
    • (2010) Genes Dev. , vol.24 , pp. 986-991
    • Searle, I.R.1
  • 125
    • 33947152396 scopus 로고    scopus 로고
    • The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth [Review]
    • Secombe J., et al. The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase required for dMyc-induced cell growth [Review]. Genes Dev. 2007, 21:537-551.
    • (2007) Genes Dev. , vol.21 , pp. 537-551
    • Secombe, J.1
  • 126
    • 77951428293 scopus 로고    scopus 로고
    • UTX mediates demethylation of H3K27me3 at muscle-specific genes during myogenesis
    • Seenundun S., et al. UTX mediates demethylation of H3K27me3 at muscle-specific genes during myogenesis. EMBO J. 2010, 29:1401-1411.
    • (2010) EMBO J. , vol.29 , pp. 1401-1411
    • Seenundun, S.1
  • 127
    • 47549105128 scopus 로고    scopus 로고
    • Control of differentiation in a self-renewing mammalian tissue by the histone demethylase JMJD3
    • Sen G.L., et al. Control of differentiation in a self-renewing mammalian tissue by the histone demethylase JMJD3. Genes Dev. 2008, 22:1865-1870.
    • (2008) Genes Dev. , vol.22 , pp. 1865-1870
    • Sen, G.L.1
  • 128
    • 35349006314 scopus 로고    scopus 로고
    • Histone lysine demethylases: emerging roles in development, physiology and disease
    • Shi Y. Histone lysine demethylases: emerging roles in development, physiology and disease. Nat. Rev. Genet. 2007, 8:829-833.
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 829-833
    • Shi, Y.1
  • 129
    • 11144332565 scopus 로고    scopus 로고
    • Histone demethylation mediated by the nuclear amine oxidase homolog LSD1
    • Shi Y., et al. Histone demethylation mediated by the nuclear amine oxidase homolog LSD1. Cell 2004, 119:941-953.
    • (2004) Cell , vol.119 , pp. 941-953
    • Shi, Y.1
  • 130
    • 33846132573 scopus 로고    scopus 로고
    • Diversity within the JMJD2 histone demethylase family
    • Shin S., Janknecht R. Diversity within the JMJD2 histone demethylase family. Biochem. Biophys. Res. Commun. 2007, 353:973-977.
    • (2007) Biochem. Biophys. Res. Commun. , vol.353 , pp. 973-977
    • Shin, S.1    Janknecht, R.2
  • 131
    • 59449098322 scopus 로고    scopus 로고
    • A jumonji (Jarid2) protein complex represses cyclin D1 expression by methylation of histone H3-K9
    • Shirato H., et al. A jumonji (Jarid2) protein complex represses cyclin D1 expression by methylation of histone H3-K9. J. Biol. Chem. 2008, 284:733-739.
    • (2008) J. Biol. Chem. , vol.284 , pp. 733-739
    • Shirato, H.1
  • 132
    • 0035969239 scopus 로고    scopus 로고
    • Tethering and tickling: a new role for the phosphatidylserine receptor
    • Somersan S., Bhardwaj N. Tethering and tickling: a new role for the phosphatidylserine receptor. J. Cell Biol. 2001, 155:501-504.
    • (2001) J. Cell Biol. , vol.155 , pp. 501-504
    • Somersan, S.1    Bhardwaj, N.2
  • 133
    • 77955274004 scopus 로고    scopus 로고
    • Features of the PHF8/KIAA1718 histone demethylase
    • Suganuma T., Workman J.L. Features of the PHF8/KIAA1718 histone demethylase. Cell Res. 2010, 20:861-862.
    • (2010) Cell Res. , vol.20 , pp. 861-862
    • Suganuma, T.1    Workman, J.L.2
  • 134
    • 51649112913 scopus 로고    scopus 로고
    • Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development
    • Sun Q., Zhou D.X. Rice jmjC domain-containing gene JMJ706 encodes H3K9 demethylase required for floral organ development. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:13679-13684.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13679-13684
    • Sun, Q.1    Zhou, D.X.2
  • 135
    • 34848815014 scopus 로고    scopus 로고
    • H3K27 demethylases, at long last
    • Swigut T., Wysocka J. H3K27 demethylases, at long last. Cell 2007, 131:29-32.
    • (2007) Cell , vol.131 , pp. 29-32
    • Swigut, T.1    Wysocka, J.2
  • 136
    • 34249900454 scopus 로고    scopus 로고
    • The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
    • Tahiliani M., et al. The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation. Nature 2007, 447:601-605.
    • (2007) Nature , vol.447 , pp. 601-605
    • Tahiliani, M.1
  • 137
    • 0029004775 scopus 로고
    • Gene trap capture of a novel mouse gene, jumonji, required for neural tube formation
    • Takeuchi T., et al. Gene trap capture of a novel mouse gene, jumonji, required for neural tube formation. Genes Dev. 1995, 9:1211-1222.
    • (1995) Genes Dev. , vol.9 , pp. 1211-1222
    • Takeuchi, T.1
  • 138
    • 77951976595 scopus 로고    scopus 로고
    • JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation
    • Tanaka Y., et al. JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation. EMBO J. 2010, 29:1510-1522.
    • (2010) EMBO J. , vol.29 , pp. 1510-1522
    • Tanaka, Y.1
  • 139
    • 78651086487 scopus 로고    scopus 로고
    • Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity
    • Tausendschon M., et al. Hypoxia causes epigenetic gene regulation in macrophages by attenuating Jumonji histone demethylase activity. Cytokine 2011, 53:256-262.
    • (2011) Cytokine , vol.53 , pp. 256-262
    • Tausendschon, M.1
  • 141
    • 0034596260 scopus 로고    scopus 로고
    • Jumonji is a nuclear protein that participates in the negative regulation of cell growth
    • Toyoda M., et al. Jumonji is a nuclear protein that participates in the negative regulation of cell growth. Biochem. Biophys. Res. Commun. 2000, 274:332-336.
    • (2000) Biochem. Biophys. Res. Commun. , vol.274 , pp. 332-336
    • Toyoda, M.1
  • 142
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick S.C., et al. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 2002, 419:174-178.
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1
  • 143
    • 17644392469 scopus 로고    scopus 로고
    • Methylation: lost in hydroxylation?
    • Trewick S.C., et al. Methylation: lost in hydroxylation?. EMBO Rep. 2005, 6:315-320.
    • (2005) EMBO Rep. , vol.6 , pp. 315-320
    • Trewick, S.C.1
  • 144
    • 33845895736 scopus 로고    scopus 로고
    • The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact with 19 proteins involved in transcription, sumoylation and DNA repair
    • Tronnersjo S., et al. The jmjN and jmjC domains of the yeast zinc finger protein Gis1 interact with 19 proteins involved in transcription, sumoylation and DNA repair. Mol. Genet. Genomics 2007, 277:57-70.
    • (2007) Mol. Genet. Genomics , vol.277 , pp. 57-70
    • Tronnersjo, S.1
  • 145
    • 77953564915 scopus 로고    scopus 로고
    • Tumor suppression by the histone demethylase UTX
    • Tsai M.C., et al. Tumor suppression by the histone demethylase UTX. Cell Cycle 2010, 9.
    • (2010) Cell Cycle , vol.9
    • Tsai, M.C.1
  • 146
    • 32844454603 scopus 로고    scopus 로고
    • Histone demethylation by a family of JmjC domain-containing proteins
    • Tsukada Y., et al. Histone demethylation by a family of JmjC domain-containing proteins. Nature 2006, 439:811-816.
    • (2006) Nature , vol.439 , pp. 811-816
    • Tsukada, Y.1
  • 147
    • 77649152293 scopus 로고    scopus 로고
    • KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development
    • Tsukada Y., et al. KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development. Genes Dev. 2010, 24:432-437.
    • (2010) Genes Dev. , vol.24 , pp. 432-437
    • Tsukada, Y.1
  • 148
    • 34347207597 scopus 로고    scopus 로고
    • Identification of histone demethylases in Saccharomyces cerevisiae
    • Tu S.J., et al. Identification of histone demethylases in Saccharomyces cerevisiae. J. Biol. Chem. 2007, 282:14262-14271.
    • (2007) J. Biol. Chem. , vol.282 , pp. 14262-14271
    • Tu, S.J.1
  • 149
    • 76749139057 scopus 로고    scopus 로고
    • The histone demethylase UTX enables RB-dependent cell fate control
    • Wang J.K., et al. The histone demethylase UTX enables RB-dependent cell fate control. Genes Dev. 2010, 24:327-332.
    • (2010) Genes Dev. , vol.24 , pp. 327-332
    • Wang, J.K.1
  • 150
    • 5044228483 scopus 로고    scopus 로고
    • Human PAD4 regulates histone arginine methylation levels via demethylimination
    • Wang Y., et al. Human PAD4 regulates histone arginine methylation levels via demethylimination. Science 2004, 306:279-283.
    • (2004) Science , vol.306 , pp. 279-283
    • Wang, Y.1
  • 151
    • 67650072604 scopus 로고    scopus 로고
    • Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing
    • Webby C.J., et al. Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science 2009, 325:90-93.
    • (2009) Science , vol.325 , pp. 90-93
    • Webby, C.J.1
  • 152
    • 45449110185 scopus 로고    scopus 로고
    • Hypoxia upregulates the histone demethylase JMJD1A via HIF-1
    • Wellmann S., et al. Hypoxia upregulates the histone demethylase JMJD1A via HIF-1. Biochem. Biophys. Res. Commun. 2008, 372:892-897.
    • (2008) Biochem. Biophys. Res. Commun. , vol.372 , pp. 892-897
    • Wellmann, S.1
  • 153
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen H., et al. Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation. J. Biol. Chem. 2010, 285:9322-9326.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9322-9326
    • Wen, H.1
  • 154
    • 84976261863 scopus 로고    scopus 로고
    • Novel nuclear receptor coactivator is a candidate for the del(5q) leukemia tumor suppressor gene
    • Westbrook C.A., et al. Novel nuclear receptor coactivator is a candidate for the del(5q) leukemia tumor suppressor gene. Exp. Hematol. 2000, 28:1492.
    • (2000) Exp. Hematol. , vol.28 , pp. 1492
    • Westbrook, C.A.1
  • 155
    • 33646124469 scopus 로고    scopus 로고
    • Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases
    • Whetstine J.R., et al. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 2006, 125:467-481.
    • (2006) Cell , vol.125 , pp. 467-481
    • Whetstine, J.R.1
  • 156
    • 33847392500 scopus 로고    scopus 로고
    • Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression
    • Wissmann M., et al. Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression. Nat. Cell Biol. 2007, 9:347-353.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 347-353
    • Wissmann, M.1
  • 157
    • 34247890161 scopus 로고    scopus 로고
    • Changing story of the receptor for phosphatidylserine-dependent clearance of apoptotic cells
    • Wolf A., et al. Changing story of the receptor for phosphatidylserine-dependent clearance of apoptotic cells. EMBO Rep. 2007, 8:465-469.
    • (2007) EMBO Rep. , vol.8 , pp. 465-469
    • Wolf, A.1
  • 158
    • 33947608608 scopus 로고    scopus 로고
    • A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR
    • Wolf S.S., et al. A novel variant of the putative demethylase gene, s-JMJD1C, is a coactivator of the AR. Arch. Biochem. Biophys. 2007, 460:56-66.
    • (2007) Arch. Biochem. Biophys. , vol.460 , pp. 56-66
    • Wolf, S.S.1
  • 159
    • 37649023563 scopus 로고    scopus 로고
    • JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
    • Xiang Y., et al. JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer. Proc. Natl. Acad. Sci. U.S.A. 2007, 104:19226-19231.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 19226-19231
    • Xiang, Y.1
  • 160
    • 35348826654 scopus 로고    scopus 로고
    • JMJD3 is a histone H3K27 demethylase
    • Xiang Y., et al. JMJD3 is a histone H3K27 demethylase. Cell Res. 2007, 17:850-857.
    • (2007) Cell Res. , vol.17 , pp. 850-857
    • Xiang, Y.1
  • 161
    • 79952709255 scopus 로고    scopus 로고
    • Reversible histone methylation regulates brain gene expression and behavior
    • Xu J., Andreassi M. Reversible histone methylation regulates brain gene expression and behavior. Horm. Behav. 2010, 59:383-392.
    • (2010) Horm. Behav. , vol.59 , pp. 383-392
    • Xu, J.1    Andreassi, M.2
  • 162
    • 49749114829 scopus 로고    scopus 로고
    • Sex-specific expression of the X-linked histone demethylase gene Jarid1c in brain
    • Xu J., et al. Sex-specific expression of the X-linked histone demethylase gene Jarid1c in brain. PLoS One 2008, 3:e2553.
    • (2008) PLoS One , vol.3
    • Xu, J.1
  • 163
    • 43749094750 scopus 로고    scopus 로고
    • Sex-specific differences in expression of histone demethylases Utx and Uty in mouse brain and neurons
    • Xu J., et al. Sex-specific differences in expression of histone demethylases Utx and Uty in mouse brain and neurons. J. Neurosci. 2008, 28:4521-4527.
    • (2008) J. Neurosci. , vol.28 , pp. 4521-4527
    • Xu, J.1
  • 164
    • 33947244845 scopus 로고    scopus 로고
    • PLU-1 is an H3K4 dernethylase involved in transcriptional repression and breast cancer cell proliferation
    • Yamane K., et al. PLU-1 is an H3K4 dernethylase involved in transcriptional repression and breast cancer cell proliferation. Mol. Cell 2007, 25:801-812.
    • (2007) Mol. Cell , vol.25 , pp. 801-812
    • Yamane, K.1
  • 165
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K., et al. JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor. Cell 2006, 125:483-495.
    • (2006) Cell , vol.125 , pp. 483-495
    • Yamane, K.1
  • 166
    • 77955267400 scopus 로고    scopus 로고
    • Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans
    • Yang Y., et al. Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans. Cell Res. 2010, 20:886-898.
    • (2010) Cell Res. , vol.20 , pp. 886-898
    • Yang, Y.1
  • 167
    • 0034282790 scopus 로고    scopus 로고
    • Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines
    • Yang Z.Q., et al. Identification of a novel gene, GASC1, within an amplicon at 9p23-24 frequently detected in esophageal cancer cell lines. Cancer Res. 2000, 60:4735-4739.
    • (2000) Cancer Res. , vol.60 , pp. 4735-4739
    • Yang, Z.Q.1
  • 168
    • 77954722645 scopus 로고    scopus 로고
    • KIAA1718 is a histone demethylase that erases repressive histone methyl marks
    • Yokoyama A., et al. KIAA1718 is a histone demethylase that erases repressive histone methyl marks. Genes Cells 2010, 15:867-873.
    • (2010) Genes Cells , vol.15 , pp. 867-873
    • Yokoyama, A.1
  • 169
    • 76449093977 scopus 로고    scopus 로고
    • Structural insights into a novel histone demethylase PHF8
    • Yu L., et al. Structural insights into a novel histone demethylase PHF8. Cell Res. 2010, 20:166-173.
    • (2010) Cell Res. , vol.20 , pp. 166-173
    • Yu, L.1
  • 170
    • 44949220180 scopus 로고    scopus 로고
    • Modulation of brassinosteroid-regulated gene expression by Jumonji domain-containing proteins ELF6 and REF6 in Arabidopsis
    • Yu X., et al. Modulation of brassinosteroid-regulated gene expression by Jumonji domain-containing proteins ELF6 and REF6 in Arabidopsis. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:7618-7623.
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 7618-7623
    • Yu, X.1
  • 171
    • 77649270417 scopus 로고    scopus 로고
    • Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase
    • Yue W.W., et al. Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase. FEBS Lett. 2010, 584:825-830.
    • (2010) FEBS Lett. , vol.584 , pp. 825-830
    • Yue, W.W.1
  • 172
    • 22544465244 scopus 로고    scopus 로고
    • JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2)
    • Zhang D., et al. JMJD2A is a novel N-CoR-interacting protein and is involved in repression of the human transcription factor achaete scute-like homologue 2 (ASCL2/Hash2). Mol. Cell Biol. 2005, 25:6404-6414.
    • (2005) Mol. Cell Biol. , vol.25 , pp. 6404-6414
    • Zhang, D.1
  • 173
    • 77950533626 scopus 로고    scopus 로고
    • Phylogenetic detection of numerous gene duplications shared by animals, fungi and plants
    • Zhou X., et al. Phylogenetic detection of numerous gene duplications shared by animals, fungi and plants. Genome Biol. 2010, 11:R38.
    • (2010) Genome Biol. , vol.11 , pp. R38
    • Zhou, X.1
  • 174
    • 55349106954 scopus 로고    scopus 로고
    • Evolutionary history of histone demethylase families: distinct evolutionary patterns suggest functional divergence
    • Zhou X., Ma H. Evolutionary history of histone demethylase families: distinct evolutionary patterns suggest functional divergence. BMC Evol. Biol. 2008, 8:294.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 294
    • Zhou, X.1    Ma, H.2
  • 175
    • 77955710635 scopus 로고    scopus 로고
    • PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis
    • Zhu Z., et al. PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis. Cell Res. 2010, 20:794-801.
    • (2010) Cell Res. , vol.20 , pp. 794-801
    • Zhu, Z.1
  • 176
    • 33744552663 scopus 로고    scopus 로고
    • Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats
    • Zofall M., Grewal S.I. Swi6/HP1 recruits a JmjC domain protein to facilitate transcription of heterochromatic repeats. Mol. Cell 2006, 22:681-692.
    • (2006) Mol. Cell , vol.22 , pp. 681-692
    • Zofall, M.1    Grewal, S.I.2


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