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Volumn 44, Issue 1, 2012, Pages 14-27

Lysine methylation: Beyond histones

Author keywords

epigenetics; lysine demethylase (KDM); lysine methyltransferase (KMT); methylation; p53

Indexed keywords

DOT1L PROTEIN, HUMAN; HISTONE DEMETHYLASE; HISTONE LYSINE METHYLTRANSFERASE; LYSINE; METHYLTRANSFERASE; PROTEIN METHYLTRANSFERASE; PROTEIN P53;

EID: 84555208833     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmr100     Document Type: Review
Times cited : (188)

References (193)
  • 2
    • 33845487512 scopus 로고    scopus 로고
    • SET domain protein lysine methyltransferases: Structure, specificity and catalysis
    • Qian C and Zhou MM. SET domain protein lysine methyltransferases: structure, specificity and catalysis. Cell Mol Life Sci 2006, 63: 2755-2763.
    • (2006) Cell Mol Life Sci , vol.63 , pp. 2755-2763
    • Qian, C.1    Zhou, M.M.2
  • 3
    • 79955057405 scopus 로고    scopus 로고
    • Natural history of the eukaryotic chromatin protein methylation system
    • Aravind L, Abhiman S and Iyer LM. Natural history of the eukaryotic chromatin protein methylation system. Prog Mol Biol Transl Sci 2011, 101: 105-176.
    • (2011) Prog Mol Biol Transl Sci , vol.101 , pp. 105-176
    • Aravind, L.1    Abhiman, S.2    Iyer, L.M.3
  • 6
    • 77954265666 scopus 로고    scopus 로고
    • Negative regulation of hypoxic responses via induced Reptin methylation
    • Lee JS, Kim Y, Kim IS, Kim B, Choi HJ, Lee JM and Shin HJ, et al. Negative regulation of hypoxic responses via induced Reptin methylation. Mol Cell 2010, 39: 71-85.
    • (2010) Mol Cell , vol.39 , pp. 71-85
    • Lee, J.S.1    Kim, Y.2    Kim, I.S.3    Kim, B.4    Choi, H.J.5    Lee, J.M.6    Shin, H.J.7
  • 9
    • 55949127661 scopus 로고    scopus 로고
    • Modulation of retinoic acid receptor alpha activity by lysine methylation in the DNA binding domain
    • Huq MD, Ha SG and Wei LN. Modulation of retinoic acid receptor alpha activity by lysine methylation in the DNA binding domain. J Proteome Res 2008, 7: 4538-4545.
    • (2008) J Proteome Res , vol.7 , pp. 4538-4545
    • Huq, M.D.1    Ha, S.G.2    Wei, L.N.3
  • 11
    • 24144449573 scopus 로고    scopus 로고
    • The Set1 methyltransferase opposes Ipl1 aurora kinase functions in chromosome segregation
    • Zhang K, Lin W, Latham JA, Riefler GM, Schumacher JM, Chan C and Tatchell K, et al. The Set1 methyltransferase opposes Ipl1 aurora kinase functions in chromosome segregation. Cell 2005, 122: 723-734.
    • (2005) Cell , vol.122 , pp. 723-734
    • Zhang, K.1    Lin, W.2    Latham, J.A.3    Riefler, G.M.4    Schumacher, J.M.5    Chan, C.6    Tatchell, K.7
  • 15
    • 36348996694 scopus 로고    scopus 로고
    • The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3
    • Kunizaki M, Hamamoto R, Silva FP, Yamaguchi K, Nagayasu T, Shibuya M and Nakamura Y, et al. The lysine 831 of vascular endothelial growth factor receptor 1 is a novel target of methylation by SMYD3. Cancer Res 2007, 67: 10759-10765.
    • (2007) Cancer Res , vol.67 , pp. 10759-10765
    • Kunizaki, M.1    Hamamoto, R.2    Silva, F.P.3    Yamaguchi, K.4    Nagayasu, T.5    Shibuya, M.6    Nakamura, Y.7
  • 17
    • 58149156264 scopus 로고    scopus 로고
    • The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation
    • Wang J, Hevi S, Kurash JK, Lei H, Gay F, Bajko J and Su H, et al. The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation. Nat Genet 2009, 41: 125-129.
    • (2009) Nat Genet , vol.41 , pp. 125-129
    • Wang, J.1    Hevi, S.2    Kurash, J.K.3    Lei, H.4    Gay, F.5    Bajko, J.6    Su, H.7
  • 19
    • 79952124926 scopus 로고    scopus 로고
    • Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1)
    • Liu X, Wang D, Zhao Y, Tu B, Zheng Z, Wang L and Wang H, et al. Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1). Proc Natl Acad Sci USA 2011, 108: 1925-1930.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1925-1930
    • Liu, X.1    Wang, D.2    Zhao, Y.3    Tu, B.4    Zheng, Z.5    Wang, L.6    Wang, H.7
  • 20
    • 1942534675 scopus 로고    scopus 로고
    • Gene-specific modulation of TAF10 function by SET9-mediated methylation
    • Kouskouti A, Scheer E, Staub A, Tora L and Talianidis I. Gene-specific modulation of TAF10 function by SET9-mediated methylation. Mol Cell 2004, 14: 175-182.
    • (2004) Mol Cell , vol.14 , pp. 175-182
    • Kouskouti, A.1    Scheer, E.2    Staub, A.3    Tora, L.4    Talianidis, I.5
  • 21
    • 77951623834 scopus 로고    scopus 로고
    • Lysine methylation regulates the pRb tumour suppressor protein
    • Munro S, Khaire N, Inche A, Carr S and La Thangue NB. Lysine methylation regulates the pRb tumour suppressor protein. Oncogene 2010, 29: 2357-2367.
    • (2010) Oncogene , vol.29 , pp. 2357-2367
    • Munro, S.1    Khaire, N.2    Inche, A.3    Carr, S.4    La Thangue, N.B.5
  • 25
    • 67349285384 scopus 로고    scopus 로고
    • Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit
    • Yang XD, Huang B, Li M, Lamb A, Kelleher NL and Chen LF. Negative regulation of NF-kappaB action by Set9-mediated lysine methylation of the RelA subunit. EMBO J 2009, 28: 1055-1066.
    • (2009) EMBO J , vol.28 , pp. 1055-1066
    • Yang, X.D.1    Huang, B.2    Li, M.3    Lamb, A.4    Kelleher, N.L.5    Chen, L.F.6
  • 26
    • 77954274181 scopus 로고    scopus 로고
    • Lysine methylation regulates E2F1-induced cell death
    • Kontaki H and Talianidis I. Lysine methylation regulates E2F1-induced cell death. Mol Cell 2010, 39: 152-160.
    • (2010) Mol Cell , vol.39 , pp. 152-160
    • Kontaki, H.1    Talianidis, I.2
  • 27
    • 79251590753 scopus 로고    scopus 로고
    • Specificity analysisbased identification of new methylation targets of the SET7/9 protein lysine methyltransferase
    • Dhayalan A, Kudithipudi S, Rathert P and Jeltsch A. Specificity analysisbased identification of new methylation targets of the SET7/9 protein lysine methyltransferase. Chem Biol 2011, 18: 111-120.
    • (2011) Chem Biol , vol.18 , pp. 111-120
    • Dhayalan, A.1    Kudithipudi, S.2    Rathert, P.3    Jeltsch, A.4
  • 28
    • 55549140173 scopus 로고    scopus 로고
    • Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation
    • Li Y, Reddy MA, Miao F, Shanmugam N, Yee JK, Hawkins D and Ren B, et al. Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation. J Biol Chem 2008, 283: 26771-26781.
    • (2008) J Biol Chem , vol.283 , pp. 26771-26781
    • Li, Y.1    Reddy, M.A.2    Miao, F.3    Shanmugam, N.4    Yee, J.K.5    Hawkins, D.6    Ren, B.7
  • 29
    • 77749342901 scopus 로고    scopus 로고
    • The cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription
    • Pagans S, Kauder SE, Kaehlcke K, Sakane N, Schroeder S, Dormeyer W and Trievel RC, et al. The cellular lysine methyltransferase Set7/9-KMT7 binds HIV-1 TAR RNA, monomethylates the viral transactivator Tat, and enhances HIV transcription. Cell Host Microbe 2010, 7: 234-244.
    • (2010) Cell Host Microbe , vol.7 , pp. 234-244
    • Pagans, S.1    Kauder, S.E.2    Kaehlcke, K.3    Sakane, N.4    Schroeder, S.5    Dormeyer, W.6    Trievel, R.C.7
  • 30
    • 79952155998 scopus 로고    scopus 로고
    • Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase
    • Ko S, Ahn J, Song CS, Kim S, Knapczyk-Stwora K and Chatterjee B. Lysine methylation and functional modulation of androgen receptor by Set9 methyltransferase. Mol Endocrinol 2011, 25: 433-444.
    • (2011) Mol Endocrinol , vol.25 , pp. 433-444
    • Ko, S.1    Ahn, J.2    Song, C.S.3    Kim, S.4    Knapczyk-Stwora, K.5    Chatterjee, B.6
  • 31
    • 61649127975 scopus 로고    scopus 로고
    • Multiple lysine methylation of PCAF by Set9 methyltransferase
    • Masatsugu T and Yamamoto K. Multiple lysine methylation of PCAF by Set9 methyltransferase. Biochem Biophys Res Commun 2009, 381: 22-26.
    • (2009) Biochem Biophys Res Commun , vol.381 , pp. 22-26
    • Masatsugu, T.1    Yamamoto, K.2
  • 33
    • 0347955358 scopus 로고    scopus 로고
    • Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains
    • Rice JC, Briggs SD, Ueberheide B, Barber CM, Shabanowitz J, Hunt DF and Shinkai Y, et al. Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains. Mol Cell 2003, 12: 1591-1598.
    • (2003) Mol Cell , vol.12 , pp. 1591-1598
    • Rice, J.C.1    Briggs, S.D.2    Ueberheide, B.3    Barber, C.M.4    Shabanowitz, J.5    Hunt, D.F.6    Shinkai, Y.7
  • 35
    • 0043127085 scopus 로고    scopus 로고
    • Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains
    • Fischle W, Wang Y, Jacobs SA, Kim Y, Allis CD and Khorasanizadeh S. Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by polycomb and HP1 chromodomains. Genes Dev 2003, 17: 1870-1881.
    • (2003) Genes Dev , vol.17 , pp. 1870-1881
    • Fischle, W.1    Wang, Y.2    Jacobs, S.A.3    Kim, Y.4    Allis, C.D.5    Khorasanizadeh, S.6
  • 37
    • 20144388930 scopus 로고    scopus 로고
    • Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9
    • Tachibana M, Ueda J, Fukuda M, Takeda N, Ohta T, Iwanari H and Sakihama T, et al. Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9. Genes Dev 2005, 19: 815-826.
    • (2005) Genes Dev , vol.19 , pp. 815-826
    • Tachibana, M.1    Ueda, J.2    Fukuda, M.3    Takeda, N.4    Ohta, T.5    Iwanari, H.6    Sakihama, T.7
  • 38
    • 77953734190 scopus 로고    scopus 로고
    • CLLD8/KMT1F is a lysine methyltransferase that is important for chromosome segregation
    • Falandry C, Fourel G, Galy V, Ristriani T, Horard B, Bensimon E and Salles G, et al. CLLD8/KMT1F is a lysine methyltransferase that is important for chromosome segregation. J Biol Chem 2010, 285: 20234-20241.
    • (2010) J Biol Chem , vol.285 , pp. 20234-20241
    • Falandry, C.1    Fourel, G.2    Galy, V.3    Ristriani, T.4    Horard, B.5    Bensimon, E.6    Salles, G.7
  • 40
    • 77955838329 scopus 로고    scopus 로고
    • Recruitment of MBD1 to target genes requires sequence-specific interaction of the MBD domain with methylated DNA
    • Clouaire T, de Las Heras JI, Merusi C and Stancheva I. Recruitment of MBD1 to target genes requires sequence-specific interaction of the MBD domain with methylated DNA. Nucleic Acids Res 2010, 38: 4620-4634.
    • (2010) Nucleic Acids Res , vol.38 , pp. 4620-4634
    • Clouaire, T.1    De Las Heras, J.I.2    Merusi, C.3    Stancheva, I.4
  • 42
    • 35548934558 scopus 로고    scopus 로고
    • MLL translocations, histone modifications and leukaemia stem-cell development
    • Krivtsov AV and Armstrong SA. MLL translocations, histone modifications and leukaemia stem-cell development. Nat Rev Cancer 2007, 7: 823-833.
    • (2007) Nat Rev Cancer , vol.7 , pp. 823-833
    • Krivtsov, A.V.1    Armstrong, S.A.2
  • 44
    • 2942715029 scopus 로고    scopus 로고
    • Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression
    • Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I and Herr W, et al. Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression. Mol Cell Biol 2004, 24: 5639-5649.
    • (2004) Mol Cell Biol , vol.24 , pp. 5639-5649
    • Yokoyama, A.1    Wang, Z.2    Wysocka, J.3    Sanyal, M.4    Aufiero, D.J.5    Kitabayashi, I.6    Herr, W.7
  • 46
    • 35348993743 scopus 로고    scopus 로고
    • Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination
    • Lee MG, Villa R, Trojer P, Norman J, Yan KP, Reinberg D and Croce LD, 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    Villa, R.2    Trojer, P.3    Norman, J.4    Yan, K.P.5    Reinberg, D.6    Croce, L.D.7
  • 48
    • 27744577727 scopus 로고    scopus 로고
    • Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription
    • Carrozza MJ, Li B, Florens L, Suganuma T, Swanson SK, Lee KK and Shia WJ, et al. Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription. Cell 2005, 123: 581-592.
    • (2005) Cell , vol.123 , pp. 581-592
    • Carrozza, M.J.1    Li, B.2    Florens, L.3    Suganuma, T.4    Swanson, S.K.5    Lee, K.K.6    Shia, W.J.7
  • 49
    • 34347392874 scopus 로고    scopus 로고
    • NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis
    • Wang GG, Cai L, Pasillas MP and Kamps MP. NUP98-NSD1 links H3K36 methylation to Hox-A gene activation and leukaemogenesis. Nat Cell Biol 2007, 9: 804-812.
    • (2007) Nat Cell Biol , vol.9 , pp. 804-812
    • Wang, G.G.1    Cai, L.2    Pasillas, M.P.3    Kamps, M.P.4
  • 50
    • 0037599617 scopus 로고    scopus 로고
    • NSD1 is essential for early post-implantation development and has a catalytically active SET domain
    • Rayasam GV, Wendling O, Angrand PO, Mark M, Niederreither K, Song L and Lerouge T, et al. NSD1 is essential for early post-implantation development and has a catalytically active SET domain. EMBO J 2003, 22: 3153-3163.
    • (2003) EMBO J , vol.22 , pp. 3153-3163
    • Rayasam, G.V.1    Wendling, O.2    Angrand, P.O.3    Mark, M.4    Niederreither, K.5    Song, L.6    Lerouge, T.7
  • 51
  • 52
    • 67650461956 scopus 로고    scopus 로고
    • A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-Hirschhorn syndrome
    • Nimura K, Ura K, Shiratori H, Ikawa M, Okabe M, Schwartz RJ and Kaneda Y. A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf-Hirschhorn syndrome. Nature 2009, 460: 287-291.
    • (2009) Nature , vol.460 , pp. 287-291
    • Nimura, K.1    Ura, K.2    Shiratori, H.3    Ikawa, M.4    Okabe, M.5    Schwartz, R.J.6    Kaneda, Y.7
  • 53
    • 79551665780 scopus 로고    scopus 로고
    • MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
    • Pei H, Zhang L, Luo K, Qin Y, Chesi M, Fei F and Bergsagel PL, et al. MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites. Nature 2011, 470: 124-128.
    • (2011) Nature , vol.470 , pp. 124-128
    • Pei, H.1    Zhang, L.2    Luo, K.3    Qin, Y.4    Chesi, M.5    Fei, F.6    Bergsagel, P.L.7
  • 54
    • 77955268518 scopus 로고    scopus 로고
    • The NSD3L histone methyltransferase regulates cell cycle and cell invasion in breast cancer cells
    • Zhou Z, Thomsen R, Kahns S and Nielsen AL. The NSD3L histone methyltransferase regulates cell cycle and cell invasion in breast cancer cells. Biochem Biophys Res Commun 2010, 398: 565-570.
    • (2010) Biochem Biophys Res Commun , vol.398 , pp. 565-570
    • Zhou, Z.1    Thomsen, R.2    Kahns, S.3    Nielsen, A.L.4
  • 56
    • 33746832077 scopus 로고    scopus 로고
    • Identification and characterization of Smyd2: A split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex
    • Brown MA, Sims RJ, 3rd, Gottlieb PD and Tucker PW. Identification and characterization of Smyd2: a split SET/MYND domain-containing histone H3 lysine 36-specific methyltransferase that interacts with the Sin3 histone deacetylase complex. Mol Cancer 2006, 5: 26.
    • (2006) Mol Cancer , vol.5 , pp. 26
    • Brown, M.A.1    Sims III, R.J.2    Gottlieb, P.D.3    Tucker, P.W.4
  • 57
    • 4143074854 scopus 로고    scopus 로고
    • SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells
    • Hamamoto R, Furukawa Y, Morita M, Iimura Y, Silva FP, Li M and Yagyu R, et al. SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells. Nat Cell Biol 2004, 6: 731-740.
    • (2004) Nat Cell Biol , vol.6 , pp. 731-740
    • Hamamoto, R.1    Furukawa, Y.2    Morita, M.3    Iimura, Y.4    Silva, F.P.5    Li, M.6    Yagyu, R.7
  • 58
    • 0036578662 scopus 로고    scopus 로고
    • Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis
    • Gottlieb PD, Pierce SA, Sims RJ, Yamagishi H, Weihe EK, Harriss JV and Maika SD, et al. Bop encodes a muscle-restricted protein containing MYND and SET domains and is essential for cardiac differentiation and morphogenesis. Nat Genet 2002, 31: 25-32.
    • (2002) Nat Genet , vol.31 , pp. 25-32
    • Gottlieb, P.D.1    Pierce, S.A.2    Sims, R.J.3    Yamagishi, H.4    Weihe, E.K.5    Harriss, J.V.6    Maika, S.D.7
  • 59
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH, Erdjument-Bromage H, Tempst P, Struhl K and Zhang Y. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 2002, 12: 1052-1058.
    • (2002) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3    Erdjument-Bromage, H.4    Tempst, P.5    Struhl, K.6    Zhang, Y.7
  • 60
    • 79959960773 scopus 로고    scopus 로고
    • The diverse functions of Dot1 and H3K79 methylation
    • Nguyen AT and Zhang Y. The diverse functions of Dot1 and H3K79 methylation. Genes Dev 2011, 25: 1345-1358.
    • (2011) Genes Dev , vol.25 , pp. 1345-1358
    • Nguyen, A.T.1    Zhang, Y.2
  • 61
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen F, Gafken PR and Gottschling DE. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 2002, 109: 745-756.
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 62
    • 13744259076 scopus 로고    scopus 로고
    • Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase
    • Shanower GA, Muller M, Blanton JL, Honti V, Gyurkovics H and Schedl P. Characterization of the grappa gene, the Drosophila histone H3 lysine 79 methyltransferase. Genetics 2005, 169: 173-184.
    • (2005) Genetics , vol.169 , pp. 173-184
    • Shanower, G.A.1    Muller, M.2    Blanton, J.L.3    Honti, V.4    Gyurkovics, H.5    Schedl, P.6
  • 63
    • 52949107241 scopus 로고    scopus 로고
    • The histone H3K79 methyltransferase Dot1L is essential for mammalian development and heterochromatin structure
    • Jones B, Su H, Bhat A, Lei H, Bajko J, Hevi S and Baltus GA, et al. The histone H3K79 methyltransferase Dot1L is essential for mammalian development and heterochromatin structure. PLoS Genet 2008, 4: e1000190.
    • (2008) PLoS Genet , vol.4
    • Jones, B.1    Su, H.2    Bhat, A.3    Lei, H.4    Bajko, J.5    Hevi, S.6    Baltus, G.A.7
  • 68
    • 13844269327 scopus 로고    scopus 로고
    • PR-Set7-dependent methylation of histone H4 Lys 20 unctions in repression of gene expression and is essential for mitosis
    • Karachentsev D, Sarma K, Reinberg D and Steward R.PR-Set7-dependent methylation of histone H4 Lys 20 unctions in repression of gene expression and is essential for mitosis. Genes Dev 2005, 19: 431-435.
    • (2005) Genes Dev , vol.19 , pp. 431-435
    • Karachentsev, D.1    Sarma, K.2    Reinberg, D.3    Steward, R.4
  • 69
    • 18444392703 scopus 로고    scopus 로고
    • PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin
    • Nishioka K, Rice JC, Sarma K, Erdjument-Bromage H, Werner J, Wang Y and Chuikov S, et al. PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin. Mol Cell 2002, 9: 1201-1213.
    • (2002) Mol Cell , vol.9 , pp. 1201-1213
    • Nishioka, K.1    Rice, J.C.2    Sarma, K.3    Erdjument-Bromage, H.4    Werner, J.5    Wang, Y.6    Chuikov, S.7
  • 70
    • 79952762476 scopus 로고    scopus 로고
    • Histone H4 Lys 20 monomethylation by histone methylase SET8 mediates Wnt target gene activation
    • Li Z, Nie F, Wang S and Li L. Histone H4 Lys 20 monomethylation by histone methylase SET8 mediates Wnt target gene activation. Proc Natl Acad Sci USA 2011, 108: 3116-3123.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 3116-3123
    • Li, Z.1    Nie, F.2    Wang, S.3    Li, L.4
  • 71
    • 77952692464 scopus 로고    scopus 로고
    • PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression
    • Congdon LM, Houston SI, Veerappan CS, Spektor TM and Rice JC. PR-Set7-mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression. J Cell Biochem 2010, 110: 609-619.
    • (2010) J Cell Biochem , vol.110 , pp. 609-619
    • Congdon, L.M.1    Houston, S.I.2    Veerappan, C.S.3    Spektor, T.M.4    Rice, J.C.5
  • 73
    • 77957367739 scopus 로고    scopus 로고
    • CRL4(Cdt2)-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase
    • Centore RC, Havens CG, Manning AL, Li JM, Flynn RL, Tse A and Jin J, et al. CRL4(Cdt2)-mediated destruction of the histone methyltransferase Set8 prevents premature chromatin compaction in S phase. Mol Cell 2010, 40: 22-33.
    • (2010) Mol Cell , vol.40 , pp. 22-33
    • Centore, R.C.1    Havens, C.G.2    Manning, A.L.3    Li, J.M.4    Flynn, R.L.5    Tse, A.6    Jin, J.7
  • 74
    • 77957378110 scopus 로고    scopus 로고
    • CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation
    • Abbas T, Shibata E, Park J, Jha S, Karnani N and Dutta A. CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation. Mol Cell 2010, 40: 9-21.
    • (2010) Mol Cell , vol.40 , pp. 9-21
    • Abbas, T.1    Shibata, E.2    Park, J.3    Jha, S.4    Karnani, N.5    Dutta, A.6
  • 75
    • 45549087777 scopus 로고    scopus 로고
    • Direct interaction between SET8 and proliferating cell nuclear antigen couples 4-K20 methylation with DNA replication
    • Huen MS, Sy SM, van Deursen JM and Chen J. Direct interaction between SET8 and proliferating cell nuclear antigen couples 4-K20 methylation with DNA replication. J Biol Chem 2008, 283: 11073-11077.
    • (2008) J Biol Chem , vol.283 , pp. 11073-11077
    • Huen, M.S.1    Sy, S.M.2    Van Deursen, J.M.3    Chen, J.4
  • 77
    • 78149281634 scopus 로고    scopus 로고
    • The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells
    • Tardat M, Brustel J, Kirsh O, Lefevbre C, Callanan M, Sardet C and Julien E. The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells. Nat Cell Biol 2010, 12: 1086-1093.
    • (2010) Nat Cell Biol , vol.12 , pp. 1086-1093
    • Tardat, M.1    Brustel, J.2    Kirsh, O.3    Lefevbre, C.4    Callanan, M.5    Sardet, C.6    Julien, E.7
  • 78
    • 2642542643 scopus 로고    scopus 로고
    • A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin
    • Schotta G, Lachner M, Sarma K, Ebert A, Sengupta R, Reuter G and Reinberg D, et al. A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes Dev 2004, 18: 1251-1262.
    • (2004) Genes Dev , vol.18 , pp. 1251-1262
    • Schotta, G.1    Lachner, M.2    Sarma, K.3    Ebert, A.4    Sengupta, R.5    Reuter, G.6    Reinberg, D.7
  • 79
    • 48749102722 scopus 로고    scopus 로고
    • A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse
    • Schotta G, Sengupta R, Kubicek S, Malin S, Kauer M, Callen E and Celeste A, et al. A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mouse. Genes Dev 2008, 22: 2048-2061.
    • (2008) Genes Dev , vol.22 , pp. 2048-2061
    • Schotta, G.1    Sengupta, R.2    Kubicek, S.3    Malin, S.4    Kauer, M.5    Callen, E.6    Celeste, A.7
  • 80
    • 57749086992 scopus 로고    scopus 로고
    • Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage
    • Greeson NT, Sengupta R, Arida AR, Jenuwein T and Sanders SL. Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage. J Biol Chem 2008, 283: 33168-33174.
    • (2008) J Biol Chem , vol.283 , pp. 33168-33174
    • Greeson, N.T.1    Sengupta, R.2    Arida, A.R.3    Jenuwein, T.4    Sanders, S.L.5
  • 81
    • 33845666681 scopus 로고    scopus 로고
    • Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair
    • Botuyan MV, Lee J, Ward IM, Kim JE, Thompson JR, Chen J and Mer G. Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell 2006, 127: 1361-1373.
    • (2006) Cell , vol.127 , pp. 1361-1373
    • Botuyan, M.V.1    Lee, J.2    Ward, I.M.3    Kim, J.E.4    Thompson, J.R.5    Chen, J.6    Mer, G.7
  • 83
    • 0037111831 scopus 로고    scopus 로고
    • Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein
    • Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P and Reinberg D. Histone methyltransferase activity associated with a human multiprotein complex containing the enhancer of Zeste protein. Genes Dev 2002, 16: 2893-2905.
    • (2002) Genes Dev , vol.16 , pp. 2893-2905
    • Kuzmichev, A.1    Nishioka, K.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 84
    • 78751662908 scopus 로고    scopus 로고
    • The polycomb complex PRC2 and its mark in life
    • Margueron R and Reinberg D. The polycomb complex PRC2 and its mark in life. Nature 2011, 469: 343-349.
    • (2011) Nature , vol.469 , pp. 343-349
    • Margueron, R.1    Reinberg, D.2
  • 85
    • 78650495421 scopus 로고    scopus 로고
    • Olycomb proteins in hematologic malignancies
    • Martin-Perez D, Piris MA and Sanchez-Beato M. olycomb proteins in hematologic malignancies. Blood 2010, 116: 5465-5475.
    • (2010) Blood , vol.116 , pp. 5465-5475
    • Martin-Perez, D.1    Piris, M.A.2    Sanchez-Beato, M.3
  • 86
    • 62149122634 scopus 로고    scopus 로고
    • Ezh2 orchestrates gene expression for the stepwise differentiation of tissue-specific stem cells
    • Ezhkova E, Pasolli HA, Parker JS, Stokes N, Su IH, Hannon G and Tarakhovsky A, et al. Ezh2 orchestrates gene expression for the stepwise differentiation of tissue-specific stem cells. Cell 2009, 136: 1122-1135.
    • (2009) Cell , vol.136 , pp. 1122-1135
    • Ezhkova, E.1    Pasolli, H.A.2    Parker, J.S.3    Stokes, N.4    Su, I.H.5    Hannon, G.6    Tarakhovsky, A.7
  • 87
    • 78650511231 scopus 로고    scopus 로고
    • CDK1-dependent phosphorylation of EZH2 suppresses methylation of H3K27 and promotes osteogenic differentiation of human mesenchymal stem cells
    • Wei Y, Chen YH, Li LY, Lang J, Yeh SP, Shi B and Yang CC, et al. CDK1-dependent phosphorylation of EZH2 suppresses methylation of H3K27 and promotes osteogenic differentiation of human mesenchymal stem cells. Nat Cell Biol 2011, 13: 87-94.
    • (2011) Nat Cell Biol , vol.13 , pp. 87-94
    • Wei, Y.1    Chen, Y.H.2    Li, L.Y.3    Lang, J.4    Yeh, S.P.5    Shi, B.6    Yang, C.C.7
  • 88
    • 78649807567 scopus 로고    scopus 로고
    • Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA
    • Kaneko S, Li G, Son J, Xu CF, Margueron R, Neubert TA and Reinberg D. Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNA. Genes Dev 2010, 24: 2615-2620.
    • (2010) Genes Dev , vol.24 , pp. 2615-2620
    • Kaneko, S.1    Li, G.2    Son, J.3    Xu, C.F.4    Margueron, R.5    Neubert, T.A.6    Reinberg, D.7
  • 89
    • 78149285100 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2
    • Chen S, Bohrer LR, Rai AN, Pan Y, Gan L, Zhou X and Bagchi A, et al. Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2. Nat Cell Biol 2010, 12: 1108-1114.
    • (2010) Nat Cell Biol , vol.12 , pp. 1108-1114
    • Chen, S.1    Bohrer, L.R.2    Rai, A.N.3    Pan, Y.4    Gan, L.5    Zhou, X.6    Bagchi, A.7
  • 90
    • 79952220410 scopus 로고    scopus 로고
    • EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair
    • Ezhkova E, Lien WH, Stokes N, Pasolli HA, Silva JM and Fuchs E. EZH1 and EZH2 cogovern histone H3K27 trimethylation and are essential for hair follicle homeostasis and wound repair. Genes Dev 2011, 25: 485-498.
    • (2011) Genes Dev , vol.25 , pp. 485-498
    • Ezhkova, E.1    Lien, W.H.2    Stokes, N.3    Pasolli, H.A.4    Silva, J.M.5    Fuchs, E.6
  • 91
    • 55949124844 scopus 로고    scopus 로고
    • EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency
    • Shen X, Liu Y, Hsu YJ, Fujiwara Y, Kim J, Mao X and Yuan GC, et al. EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency. Mol Cell 2008, 32: 491-502.
    • (2008) Mol Cell , vol.32 , pp. 491-502
    • Shen, X.1    Liu, Y.2    Hsu, Y.J.3    Fujiwara, Y.4    Kim, J.5    Mao, X.6    Yuan, G.C.7
  • 92
    • 0037083757 scopus 로고    scopus 로고
    • Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation
    • Nishioka K, Chuikov S, Sarma K, Erdjument-Bromage H, Allis CD, Tempst P and Reinberg D. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Genes Dev 2002, 16: 479-489.
    • (2002) Genes Dev , vol.16 , pp. 479-489
    • Nishioka, K.1    Chuikov, S.2    Sarma, K.3    Erdjument-Bromage, H.4    Allis, C.D.5    Tempst, P.6    Reinberg, D.7
  • 93
    • 73449092853 scopus 로고    scopus 로고
    • SET7/9 mediated methylation of non-histone proteins in mammalian cells
    • Pradhan S, Chin HG, Esteve PO and Jacobsen SE. SET7/9 mediated methylation of non-histone proteins in mammalian cells. Epigenetics 2009, 4: 383-387.
    • (2009) Epigenetics , vol.4 , pp. 383-387
    • Pradhan, S.1    Chin, H.G.2    Esteve, P.O.3    Jacobsen, S.E.4
  • 94
    • 32244444118 scopus 로고    scopus 로고
    • Structural basis for the methylation site specificity of SET7/9
    • Couture JF, Collazo E, Hauk G and Trievel RC. Structural basis for the methylation site specificity of SET7/9. Nat Struct Mol Biol 2006, 13: 140-146.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 140-146
    • Couture, J.F.1    Collazo, E.2    Hauk, G.3    Trievel, R.C.4
  • 95
    • 12944328744 scopus 로고    scopus 로고
    • The retinoblastoma-interacting zinc-finger protein RIZ is a downstream effector of estrogen action
    • Abbondanza C, Medici N, Nigro V, Rossi V, Gallo L, Piluso G and Belsito A, et al. The retinoblastoma-interacting zinc-finger protein RIZ is a downstream effector of estrogen action. Proc Natl Acad Sci USA 2000, 97: 3130-3135.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3130-3135
    • Abbondanza, C.1    Medici, N.2    Nigro, V.3    Rossi, V.4    Gallo, L.5    Piluso, G.6    Belsito, A.7
  • 96
    • 0036593394 scopus 로고    scopus 로고
    • Histone methyltransferases, diet nutrients and tumour suppressors
    • Huang S. Histone methyltransferases, diet nutrients and tumour suppressors. Nat Rev Cancer 2002, 2: 469-476.
    • (2002) Nat Rev Cancer , vol.2 , pp. 469-476
    • Huang, S.1
  • 97
    • 0345275880 scopus 로고    scopus 로고
    • Inactivation of a histone methyltransferase by mutations in human cancers
    • Kim KC, Geng L and Huang S. Inactivation of a histone methyltransferase by mutations in human cancers. Cancer Res 2003, 63: 7619-7623.
    • (2003) Cancer Res , vol.63 , pp. 7619-7623
    • Kim, K.C.1    Geng, L.2    Huang, S.3
  • 100
    • 33846025127 scopus 로고    scopus 로고
    • Dynamic regulation of histone lysine methylation by demethylases
    • Shi Y and Whetstine JR. Dynamic regulation of histone lysine methylation by demethylases. Mol Cell 2007, 25: 1-14.
    • (2007) Mol Cell , vol.25 , pp. 1-14
    • Shi, Y.1    Whetstine, J.R.2
  • 101
    • 43249102851 scopus 로고    scopus 로고
    • Erasing the methyl mark: Histone demethylases at the center of cellular differentiation and disease
    • Cloos PA, Christensen J, Agger K and Helin K. 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.1    Christensen, J.2    Agger, K.3    Helin, K.4
  • 102
    • 33947513027 scopus 로고    scopus 로고
    • Regulation of histone methylation by demethylimination and demethylation
    • Klose RJ and 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
  • 104
    • 79551519643 scopus 로고    scopus 로고
    • Demethylation of RB regulator MYPT1 by histone demethylase LSD1 promotes cell cycle progression in cancer cells
    • Cho HS, Suzuki T, Dohmae N, Hayami S, Unoki M, Yoshimatsu M and Toyokawa G, et al. Demethylation of RB regulator MYPT1 by histone demethylase LSD1 promotes cell cycle progression in cancer cells. Cancer Res 2011, 71: 655-660.
    • (2011) Cancer Res , vol.71 , pp. 655-660
    • Cho, H.S.1    Suzuki, T.2    Dohmae, N.3    Hayami, S.4    Unoki, M.5    Yoshimatsu, M.6    Toyokawa, G.7
  • 105
    • 25144519737 scopus 로고    scopus 로고
    • An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation
    • Lee MG, Wynder C, Cooch N and Shiekhattar R. An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation. Nature 2005, 437: 432-435.
    • (2005) Nature , vol.437 , pp. 432-435
    • Lee, M.G.1    Wynder, C.2    Cooch, N.3    Shiekhattar, R.4
  • 106
    • 33746435258 scopus 로고    scopus 로고
    • Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase
    • Yang M, Gocke CB, Luo X, Borek D, Tomchick DR, Machius M and Otwinowski Z, et al. Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase. Mol Cell 2006, 23: 377-387.
    • (2006) Mol Cell , vol.23 , pp. 377-387
    • Yang, M.1    Gocke, C.B.2    Luo, X.3    Borek, D.4    Tomchick, D.R.5    MacHius, M.6    Otwinowski, Z.7
  • 107
    • 24144462170 scopus 로고    scopus 로고
    • LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription
    • Metzger E, Wissmann M, Yin N, Muller JM, Schneider R, Peters AH and Günther T, et al. LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription. Nature 2005, 437: 436-439.
    • (2005) Nature , vol.437 , pp. 436-439
    • Metzger, E.1    Wissmann, M.2    Yin, N.3    Muller, J.M.4    Schneider, R.5    Peters, A.H.6    Günther, T.7
  • 108
    • 33847392500 scopus 로고    scopus 로고
    • Cooperative demethylation by JMJD2C and LSD1 promotes androgen receptor-dependent gene expression
    • Wissmann M, Yin N, Muller JM, Greschik H, Fodor BD, Jenuwein T and Vogler C, 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    Yin, N.2    Muller, J.M.3    Greschik, H.4    Fodor, B.D.5    Jenuwein, T.6    Vogler, C.7
  • 109
    • 58049208232 scopus 로고    scopus 로고
    • Enhancing nuclear receptor-induced transcription requires nuclear motor and LSD1-dependent gene networking in interchromatin granules
    • Hu Q, Kwon YS, Nunez E, Cardamone MD, Hutt KR, Ohgi KA and Garcia-Bassets I, et al. Enhancing nuclear receptor-induced transcription requires nuclear motor and LSD1-dependent gene networking in interchromatin granules. Proc Natl Acad Sci USA 2008, 105: 19199-19204.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 19199-19204
    • Hu, Q.1    Kwon, Y.S.2    Nunez, E.3    Cardamone, M.D.4    Hutt, K.R.5    Ohgi, K.A.6    Garcia-Bassets, I.7
  • 110
    • 66449097375 scopus 로고    scopus 로고
    • LSD1 demethylates histone and non-histone proteins
    • Nicholson TB and Chen T. LSD1 demethylates histone and non-histone proteins. Epigenetics 2009, 4: 129-132.
    • (2009) Epigenetics , vol.4 , pp. 129-132
    • Nicholson, T.B.1    Chen, T.2
  • 111
    • 77949269612 scopus 로고    scopus 로고
    • AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function
    • Yang Z, Jiang J, Stewart DM, Qi S, Yamane K, Li J and Zhang Y, et al. AOF1 is a histone H3K4 demethylase possessing demethylase activity-independent repression function. Cell Res 2010, 20: 276-287.
    • (2010) Cell Res , vol.20 , pp. 276-287
    • Yang, Z.1    Jiang, J.2    Stewart, D.M.3    Qi, S.4    Yamane, K.5    Li, J.6    Zhang, Y.7
  • 112
    • 70349272130 scopus 로고    scopus 로고
    • KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints
    • Ciccone DN, Su H, Hevi S, Gay F, Lei H, Bajko J and Xu G, et al. KDM1B is a histone H3K4 demethylase required to establish maternal genomic imprints. Nature 2009, 461: 415-418.
    • (2009) Nature , vol.461 , pp. 415-418
    • Ciccone, D.N.1    Su, H.2    Hevi, S.3    Gay, F.4    Lei, H.5    Bajko, J.6    Xu, G.7
  • 114
    • 77955497653 scopus 로고    scopus 로고
    • Human LSD2/KDM1b/AOF1 regulates gene transcription by modulating intragenic H3K4me2 methylation
    • Fang R, Barbera AJ, Xu Y, Rutenberg M, Leonor T, Bi Q and Lan F, et al. Human LSD2/KDM1b/AOF1 regulates gene transcription by modulating intragenic H3K4me2 methylation. Mol Cell 2011, 39: 222-233.
    • (2011) Mol Cell , vol.39 , pp. 222-233
    • Fang, R.1    Barbera, A.J.2    Xu, Y.3    Rutenberg, M.4    Leonor, T.5    Bi, Q.6    Lan, F.7
  • 115
    • 77956541159 scopus 로고    scopus 로고
    • A feed-forward circuit controlling inducible NF-kappaB target gene activation by promoter histone demethylation
    • van Essen D, Zhu Y and Saccani S. A feed-forward circuit controlling inducible NF-kappaB target gene activation by promoter histone demethylation. Mol Cell 2011, 39: 750-760.
    • (2011) Mol Cell , vol.39 , pp. 750-760
    • Van Essen, D.1    Zhu, Y.2    Saccani, S.3
  • 116
    • 36049022778 scopus 로고    scopus 로고
    • JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes
    • Frescas D, Guardavaccaro D, Bassermann F, Koyama-Nasu R and Pagano M. 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    Guardavaccaro, D.2    Bassermann, F.3    Koyama-Nasu, R.4    Pagano, M.5
  • 117
    • 55549147132 scopus 로고    scopus 로고
    • The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b)
    • He J, Kallin EM, Tsukada Y and Zhang Y. The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15(Ink4b). Nat Struct Mol Biol 2008, 15: 1169-1175.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1169-1175
    • He, J.1    Kallin, E.M.2    Tsukada, Y.3    Zhang, Y.4
  • 118
    • 34548349350 scopus 로고    scopus 로고
    • The F-box protein Fbl10 is a novel transcriptional repressor of c-Jun
    • Koyama-Nasu R, David G and Tanese N. 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    David, G.2    Tanese, N.3
  • 119
    • 77951976595 scopus 로고    scopus 로고
    • JmjC enzyme KDM2A is a regulator of rRNA transcription in response to starvation
    • Tanaka Y, Okamoto K, Teye K, Umata T, Yamagiwa N, Suto Y and Zhang 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    Okamoto, K.2    Teye, K.3    Umata, T.4    Yamagiwa, N.5    Suto, Y.6    Zhang, Y.7
  • 120
    • 34249715325 scopus 로고    scopus 로고
    • Proteomics analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor
    • Sanchez C, Sanchez I, Demmers JA, Rodriguez P, Strouboulis J and Vidal M. Proteomics analysis of Ring1B/Rnf2 interactors identifies a novel complex with the Fbxl10/Jhdm1B histone demethylase and the Bcl6 interacting corepressor. Mol Cell Proteomics 2007, 6: 820-834.
    • (2007) Mol Cell Proteomics , vol.6 , pp. 820-834
    • Sanchez, C.1    Sanchez, I.2    Demmers, J.A.3    Rodriguez, P.4    Strouboulis, J.5    Vidal, M.6
  • 121
    • 33646138230 scopus 로고    scopus 로고
    • JHDM2A, a JmjC-containing H3K9 demethylase, facilitates transcription activation by androgen receptor
    • Yamane K, Toumazou C, Tsukada Y, Erdjument-Bromage H, Tempst P, Wong J and Zhang Y. 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    Toumazou, C.2    Tsukada, Y.3    Erdjument-Bromage, H.4    Tempst, P.5    Wong, J.6    Zhang, Y.7
  • 122
    • 35948993829 scopus 로고    scopus 로고
    • Histone demethylase JHDM2A is critical for Tnp1 and Prm1 transcription and spermatogenesis
    • Okada Y, Scott G, Ray MK, Mishina Y and Zhang Y. 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    Scott, G.2    Ray, M.K.3    Mishina, Y.4    Zhang, Y.5
  • 123
    • 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 AJ, Rankin EB, Chan D, Razorenova O, Fernandez S and Giaccia AJ. Regulation of the histone demethylase JMJD1A by hypoxia-inducible factor 1 alpha enhances hypoxic gene expression and tumor growth. Mol Cell Biol 2009, 30: 344-353.
    • (2009) Mol Cell Biol , vol.30 , pp. 344-353
    • Krieg, A.J.1    Rankin, E.B.2    Chan, D.3    Razorenova, O.4    Fernandez, S.5    Giaccia, A.J.6
  • 124
    • 64749111074 scopus 로고    scopus 로고
    • Role of Jhdm2a in regulating metabolic gene expression and obesity resistance
    • Tateishi K, Okada Y, Kallin EM and Zhang Y. Role of Jhdm2a in regulating metabolic gene expression and obesity resistance. Nature 2009, 458: 757-761.
    • (2009) Nature , vol.458 , pp. 757-761
    • Tateishi, K.1    Okada, Y.2    Kallin, E.M.3    Zhang, Y.4
  • 125
    • 33646124469 scopus 로고    scopus 로고
    • Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases
    • Whetstine JR, Nottke A, Lan F, Huarte M, Smolikov S, Chen Z and Spooner E, 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    Nottke, A.2    Lan, F.3    Huarte, M.4    Smolikov, S.5    Chen, Z.6    Spooner, E.7
  • 126
    • 33745847680 scopus 로고    scopus 로고
    • The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36
    • Klose RJ, Yamane K, Bae Y, Zhang D, Erdjument-Bromage H, Tempst P and Wong J, et al. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 2006, 442: 312-316.
    • (2006) Nature , vol.442 , pp. 312-316
    • Klose, R.J.1    Yamane, K.2    Bae, Y.3    Zhang, D.4    Erdjument-Bromage, H.5    Tempst, P.6    Wong, J.7
  • 128
    • 33646438365 scopus 로고    scopus 로고
    • Recognition of histone H3 lysine-4 methylation by the double tudor domain of JMJD2A
    • Huang Y, Fang J, Bedford MT, Zhang Y and Xu RM. 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    Fang, J.2    Bedford, M.T.3    Zhang, Y.4    Xu, R.M.5
  • 129
    • 65249151919 scopus 로고    scopus 로고
    • Structure and function of histone methylation binding proteins
    • Adams-Cioaba MA and Min J. Structure and function of histone methylation binding proteins. Biochem Cell Biol 2009, 87: 93-105.
    • (2009) Biochem Cell Biol , vol.87 , pp. 93-105
    • Adams-Cioaba, M.A.1    Min, J.2
  • 130
    • 34250168304 scopus 로고    scopus 로고
    • Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D
    • Shin S and Janknecht R. Activation of androgen receptor by histone demethylases JMJD2A and JMJD2D. Biochem Biophys Res Commun 2007, 359: 742-746.
    • (2007) Biochem Biophys Res Commun , vol.359 , pp. 742-746
    • Shin, S.1    Janknecht, R.2
  • 131
    • 79952800100 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development
    • Kawazu M, Saso K, Tong KI, McQuire T, Goto K, Son DO and Wakeham A, et al. Histone demethylase JMJD2B functions as a co-factor of estrogen receptor in breast cancer proliferation and mammary gland development. PLoS One 2011, 6: e17830.
    • (2011) PLoS One , vol.6
    • Kawazu, M.1    Saso, K.2    Tong, K.I.3    McQuire, T.4    Goto, K.5    Son, D.O.6    Wakeham, A.7
  • 132
    • 79956291600 scopus 로고    scopus 로고
    • Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis
    • Shi L, Sun L, Li Q, Liang J, Yu W, Yi X and Yang X, et al. Histone demethylase JMJD2B coordinates H3K4/H3K9 methylation and promotes hormonally responsive breast carcinogenesis. Proc Natl Acad Sci USA 2011, 108: 7541-7546.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 7541-7546
    • Shi, L.1    Sun, L.2    Li, Q.3    Liang, J.4    Yu, W.5    Yi, X.6    Yang, X.7
  • 134
  • 135
    • 37649023563 scopus 로고    scopus 로고
    • JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer
    • Xiang Y, Zhu Z, Han G, Ye X, Xu B, Peng Z and Ma Y, et al. JARID1B is a histone H3 lysine 4 demethylase up-regulated in prostate cancer. Proc Natl Acad Sci USA 2007, 104: 19226-19231.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19226-19231
    • Xiang, Y.1    Zhu, Z.2    Han, G.3    Ye, X.4    Xu, B.5    Peng, Z.6    Ma, Y.7
  • 136
    • 33947245128 scopus 로고    scopus 로고
    • RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3
    • Christensen J, Agger K, Cloos PA, Pasini D, Rose S, Sennels L and Rappsilber 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    Agger, K.2    Cloos, P.A.3    Pasini, D.4    Rose, S.5    Sennels, L.6    Rappsilber, J.7
  • 137
    • 33947302685 scopus 로고    scopus 로고
    • The X-linked mental retardation gene SMCX/ JARID1C defines a family of histone H3 lysine 4 demethylases
    • Iwase S, Lan F, Bayliss P, de la Torre-Ubieta L, Huarte M, Qi HH and Whetstine JR, 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    Lan, F.2    Bayliss, P.3    De La Torre-Ubieta, L.4    Huarte, M.5    Qi, H.H.6    Whetstine, J.R.7
  • 140
    • 34249900454 scopus 로고    scopus 로고
    • The histone H3K4 demethylase SMCX links REST target genes to X-linked mental retardation
    • Tahiliani M, Mei P, Fang R, Leonor T, Rutenberg M, Shimizu F and Li J, 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    Mei, P.2    Fang, R.3    Leonor, T.4    Rutenberg, M.5    Shimizu, F.6    Li, J.7
  • 141
    • 33847383585 scopus 로고    scopus 로고
    • Physical and functional association of a trimethyl H3K4 demethylase and Ring6a/MBLR, a polycomb-like protein
    • Lee MG, Norman J, Shilatifard A and Shiekhattar R. 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    Norman, J.2    Shilatifard, A.3    Shiekhattar, R.4
  • 142
    • 67349266612 scopus 로고    scopus 로고
    • Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
    • Wang GG, Song J, Wang Z, Dormann HL, Casadio F, Li H and Luo JL, et al. Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature 2009, 459: 847-851.
    • (2009) Nature , vol.459 , pp. 847-851
    • Wang, G.G.1    Song, J.2    Wang, Z.3    Dormann, H.L.4    Casadio, F.5    Li, H.6    Luo, J.L.7
  • 143
    • 79953708822 scopus 로고    scopus 로고
    • Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer
    • Blair LP, Cao J, Zou MR, Sayegh J and Yan Q. Epigenetic regulation by lysine demethylase 5 (KDM5) enzymes in cancer. Cancers (Basel) 2011, 3: 1383-1404.
    • (2011) Cancers (Basel) , vol.3 , pp. 1383-1404
    • Blair, L.P.1    Cao, J.2    Zou, M.R.3    Sayegh, J.4    Yan, Q.5
  • 144
    • 34548644772 scopus 로고    scopus 로고
    • The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing
    • De Santa F, Totaro MG, Prosperini E, Notarbartolo S, Testa G and Natoli G. 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
    • De Santa, F.1    Totaro, M.G.2    Prosperini, E.3    Notarbartolo, S.4    Testa, G.5    Natoli, G.6
  • 145
    • 36749082438 scopus 로고    scopus 로고
    • Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases
    • Hong S, Cho YW, Yu LR, Yu H, Veenstra TD and Ge K. Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Proc Natl Acad Sci USA 2007, 104: 18439-18444.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18439-18444
    • Hong, S.1    Cho, Y.W.2    Yu, L.R.3    Yu, H.4    Veenstra, T.D.5    Ge, K.6
  • 147
    • 35148867907 scopus 로고    scopus 로고
    • UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development
    • Agger K, Cloos PA, Christensen J, Pasini D, Rose S, Rappsilber J and Issaeva I, 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    Cloos, P.A.2    Christensen, J.3    Pasini, D.4    Rose, S.5    Rappsilber, J.6    Issaeva, I.7
  • 150
    • 79952140358 scopus 로고    scopus 로고
    • Human papillomavirus E7 oncoprotein induces KDM6A and KDM6B histone demethylase expression and causes epigenetic reprogramming
    • McLaughlin-Drubin ME, Crum CP and Munger K. Human papillomavirus E7 oncoprotein induces KDM6A and KDM6B histone demethylase expression and causes epigenetic reprogramming. Proc Natl Acad Sci USA 2011, 108: 2130-2135.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2130-2135
    • McLaughlin-Drubin, M.E.1    Crum, C.P.2    Munger, K.3
  • 151
    • 77951240318 scopus 로고    scopus 로고
    • Recognition of histone H3K4 trimethylation by the plant homeodomain of PHF2 modulates histone demethylation
    • Wen H, Li J, Song T, Lu M, Kan PY, Lee MG and Sha B, 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    Li, J.2    Song, T.3    Lu, M.4    Kan, P.Y.5    Lee, M.G.6    Sha, B.7
  • 152
    • 77950521594 scopus 로고    scopus 로고
    • PHF8 activates transcription of rRNA genes through H3K4me3 binding and H3K9me1/2 demethylation
    • Feng W, Yonezawa M, Ye J, Jenuwein T and Grummt I. 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    Yonezawa, M.2    Ye, J.3    Jenuwein, T.4    Grummt, I.5
  • 154
    • 77955280094 scopus 로고    scopus 로고
    • The X-linked mental retardation gene PHF8 is a histone demethylase involved in neuronal differentiation
    • Qiu J, Shi G, Jia Y, Li J, Wu M, Li J and Dong S, 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    Shi, G.2    Jia, Y.3    Li, J.4    Wu, M.5    Li, J.6    Dong, S.7
  • 155
    • 77955710635 scopus 로고    scopus 로고
    • PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis
    • Zhu Z, Wang Y, Li X, Wang Y, Xu L, Wang X and Sun T, 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    Wang, Y.2    Li, X.3    Wang, Y.4    Xu, L.5    Wang, X.6    Sun, T.7
  • 156
    • 77950893589 scopus 로고    scopus 로고
    • A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation
    • Kleine-Kohlbrecher D, Christensen J, Vandamme J, Abarrategui I, Bak M, Tommerup N and Shi X, et al. A functional link between the histone demethylase PHF8 and the transcription factor ZNF711 in X-linked mental retardation. Mol Cell 2010, 38: 165-178.
    • (2010) Mol Cell , vol.38 , pp. 165-178
    • Kleine-Kohlbrecher, D.1    Christensen, J.2    Vandamme, J.3    Abarrategui, I.4    Bak, M.5    Tommerup, N.6    Shi, X.7
  • 157
    • 79957906726 scopus 로고    scopus 로고
    • PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B
    • Baba A, Ohtake F, Okuno Y, Yokota K, Okada M, Imai Y and Ni M, et al. PKA-dependent regulation of the histone lysine demethylase complex PHF2-ARID5B. Nat Cell Biol 2011, 13: 669-676.
    • (2011) Nat Cell Biol , vol.13 , pp. 669-676
    • Baba, A.1    Ohtake, F.2    Okuno, Y.3    Yokota, K.4    Okada, M.5    Imai, Y.6    Ni, M.7
  • 158
    • 77954954200 scopus 로고    scopus 로고
    • PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression
    • Liu W, Tanasa B, Tyurina OV, Zhou TY, Gassmann R, Liu WT and Ohgi KA, 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    Tanasa, B.2    Tyurina, O.V.3    Zhou, T.Y.4    Gassmann, R.5    Liu, W.T.6    Ohgi, K.A.7
  • 159
    • 77954957901 scopus 로고    scopus 로고
    • Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development
    • Qi HH, Sarkissian M, Hu GQ, Wang Z, Bhattacharjee A, Gordon DB and Gonzales M, 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    Sarkissian, M.2    Hu, G.Q.3    Wang, Z.4    Bhattacharjee, A.5    Gordon, D.B.6    Gonzales, M.7
  • 160
    • 76449093977 scopus 로고    scopus 로고
    • Structural insights into a novel histone demethylase PHF8
    • Yu L, Wang Y, Huang S, Wang J, Deng Z, Zhang Q and Wu W, 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    Wang, Y.2    Huang, S.3    Wang, J.4    Deng, Z.5    Zhang, Q.6    Wu, W.7
  • 161
    • 77449127237 scopus 로고    scopus 로고
    • Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases
    • Horton JR, Upadhyay AK, Qi HH, Zhang X, Shi Y and Cheng X. 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    Upadhyay, A.K.2    Qi, H.H.3    Zhang, X.4    Shi, Y.5    Cheng, X.6
  • 162
    • 77955415488 scopus 로고    scopus 로고
    • MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output
    • Chen L, Li Z, Zwolinska AK, Smith MA, Cross B, oomen J and Yuan ZM, et al. MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output. EMBO J 2010, 29: 2538-2552.
    • (2010) EMBO J , vol.29 , pp. 2538-2552
    • Chen, L.1    Li, Z.2    Zwolinska, A.K.3    Smith, M.A.4    Cross, B.5    Oomen, J.6    Yuan, Z.M.7
  • 163
    • 0030941458 scopus 로고    scopus 로고
    • P53, the cellular gatekeeper for growth and division
    • Levine AJ. p53, the cellular gatekeeper for growth and division. Cell 1997, 88: 323-331.
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 164
    • 65549120715 scopus 로고    scopus 로고
    • Modes of p53 regulation
    • Kruse JP and Gu W. Modes of p53 regulation. Cell 2009, 137: 609-622.
    • (2009) Cell , vol.137 , pp. 609-622
    • Kruse, J.P.1    Gu, W.2
  • 165
    • 77956153243 scopus 로고    scopus 로고
    • The language of histone crosstalk
    • Lee JS, Smith E and Shilatifard A. The language of histone crosstalk. Cell 2010, 142: 682-685.
    • (2010) Cell , vol.142 , pp. 682-685
    • Lee, J.S.1    Smith, E.2    Shilatifard, A.3
  • 166
    • 35848936709 scopus 로고    scopus 로고
    • Cross-regulation of histone modifications
    • Latham JA and Dent SY. Cross-regulation of histone modifications. Nat Struct Mol Biol 2007, 14: 1017-1024.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1017-1024
    • Latham, J.A.1    Dent, S.Y.2
  • 168
    • 38949178369 scopus 로고    scopus 로고
    • Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo
    • Kurash JK, Lei H, Shen Q, Marston WL, Granda BW, Fan H and Wall D, et al. Methylation of p53 by Set7/9 mediates p53 acetylation and activity in vivo. Mol Cell 2008, 29: 392-400.
    • (2008) Mol Cell , vol.29 , pp. 392-400
    • Kurash, J.K.1    Lei, H.2    Shen, Q.3    Marston, W.L.4    Granda, B.W.5    Fan, H.6    Wall, D.7
  • 169
    • 80455176677 scopus 로고    scopus 로고
    • Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins
    • Xu S, Zhong C, Zhang T and Ding J. Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins. J Mol Cell Biol 2011, 3: 293-300.
    • (2011) J Mol Cell Biol , vol.3 , pp. 293-300
    • Xu, S.1    Zhong, C.2    Zhang, T.3    Ding, J.4
  • 170
    • 27644589675 scopus 로고    scopus 로고
    • The diverse functions of histone lysine methylation
    • Martin C and 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
  • 171
    • 78549291445 scopus 로고    scopus 로고
    • The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression
    • West LE, Roy S, Lachmi-Weiner K, Hayashi R, Shi X, Appella E and Kutateladze TG, et al. The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression. J Biol Chem 2010, 285: 37725-37732.
    • (2010) J Biol Chem , vol.285 , pp. 37725-37732
    • West, L.E.1    Roy, S.2    Lachmi-Weiner, K.3    Hayashi, R.4    Shi, X.5    Appella, E.6    Kutateladze, T.G.7
  • 172
    • 58049203867 scopus 로고    scopus 로고
    • Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling
    • Kachirskaia I, Shi X, Yamaguchi H, Tanoue K, Wen H, Wang EW and Appella E, et al. Role for 53BP1 Tudor domain recognition of p53 dimethylated at lysine 382 in DNA damage signaling. J Biol Chem 2008, 283: 34660-34666.
    • (2008) J Biol Chem , vol.283 , pp. 34660-34666
    • Kachirskaia, I.1    Shi, X.2    Yamaguchi, H.3    Tanoue, K.4    Wen, H.5    Wang, E.W.6    Appella, E.7
  • 174
    • 80051733367 scopus 로고    scopus 로고
    • And Rossi FMV. p53-dependent transcription and tumor suppression are not affected in Set7/9-deficient mice
    • Lehnertz B, Rogalski JC, Schulze FM, Yi L, Lin S, Kast J and Rossi FMV. p53-dependent transcription and tumor suppression are not affected in Set7/9-deficient mice. Mol Cell 2011, 43: 673-680.
    • (2011) Mol Cell , vol.43 , pp. 673-680
    • Lehnertz, B.1    Rogalski, J.C.2    Schulze, F.M.3    Yi, L.4    Lin, S.5    Kast, J.6
  • 175
    • 80051733486 scopus 로고    scopus 로고
    • The methyltransferase set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo
    • Campaner S, Spreafico F, Burgold T, Doni M, Rosato U, Amati B and Testa G. The methyltransferase set7/9 (Setd7) is dispensable for the p53-mediated DNA damage response in vivo. Mol Cell 2011, 43: 681-688.
    • (2011) Mol Cell , vol.43 , pp. 681-688
    • Campaner, S.1    Spreafico, F.2    Burgold, T.3    Doni, M.4    Rosato, U.5    Amati, B.6    Testa, G.7
  • 176
    • 20744448187 scopus 로고    scopus 로고
    • Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity
    • Feng L, Lin T, Uranishi H, Gu W and Xu Y. Functional analysis of the roles of posttranslational modifications at the p53 C terminus in regulating p53 stability and activity. Mol Cell Biol 2005, 25: 5389-5395.
    • (2005) Mol Cell Biol , vol.25 , pp. 5389-5395
    • Feng, L.1    Lin, T.2    Uranishi, H.3    Gu, W.4    Xu, Y.5
  • 177
    • 22544484456 scopus 로고    scopus 로고
    • The C-terminal lysines fine-tune P53 stress responses in a mouse model but are not required for stability control or transactivation
    • Krummel KA, Lee CJ, Toledo F and Wahl GM. The C-terminal lysines fine-tune P53 stress responses in a mouse model but are not required for stability control or transactivation. Proc Natl Acad Sci USA 2005, 102: 10188-10193.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10188-10193
    • Krummel, K.A.1    Lee, C.J.2    Toledo, F.3    Wahl, G.M.4
  • 178
    • 0035694922 scopus 로고    scopus 로고
    • Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase
    • Wang H, Cao R, Xia L, Erdjument-Bromage H, Borchers C, Tempst P and Zhang Y. Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase. Mol Cell 2001, 8: 1207-1217.
    • (2001) Mol Cell , vol.8 , pp. 1207-1217
    • Wang, H.1    Cao, R.2    Xia, L.3    Erdjument-Bromage, H.4    Borchers, C.5    Tempst, P.6    Zhang, Y.7
  • 179
    • 78751629039 scopus 로고    scopus 로고
    • Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein
    • Carr SM, Munro S, Kessler B, Oppermann U and La Thangue NB. Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein. EMBO J 2011, 30: 317-327.
    • (2011) EMBO J , vol.30 , pp. 317-327
    • Carr, S.M.1    Munro, S.2    Kessler, B.3    Oppermann, U.4    La Thangue, N.B.5
  • 180
    • 73149099403 scopus 로고    scopus 로고
    • Regulation of NF-kappaB activity through lysine monomethylation of p65
    • Ea CK and Baltimore D. Regulation of NF-kappaB activity through lysine monomethylation of p65. Proc Natl Acad Sci USA 2009, 106: 18972-18977.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 18972-18977
    • Ea, C.K.1    Baltimore, D.2
  • 181
    • 78650308842 scopus 로고    scopus 로고
    • Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling
    • Levy D, Kuo AJ, Chang Y, Schaefer U, Kitson C, Cheung P and Espejo A, et al. Lysine methylation of the NF-kappaB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-kappaB signaling. Nat Immunol 2011, 12: 29-36.
    • (2011) Nat Immunol , vol.12 , pp. 29-36
    • Levy, D.1    Kuo, A.J.2    Chang, Y.3    Schaefer, U.4    Kitson, C.5    Cheung, P.6    Espejo, A.7
  • 182
  • 183
    • 58149095554 scopus 로고    scopus 로고
    • Identification of two SET domain proteins required for methylation of lysine residues in yeast ribosomal protein Rpl42ab
    • Webb KJ, Laganowsky A, Whitelegge JP and Clarke SG. Identification of two SET domain proteins required for methylation of lysine residues in yeast ribosomal protein Rpl42ab. J Biol Chem 2008, 283: 35561-35568.
    • (2008) J Biol Chem , vol.283 , pp. 35561-35568
    • Webb, K.J.1    Laganowsky, A.2    Whitelegge, J.P.3    Clarke, S.G.4
  • 184
    • 27144441000 scopus 로고    scopus 로고
    • A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast
    • Porras-Yakushi TR, Whitelegge JP, Miranda TB and Clarke S. A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast. J Biol Chem 2005, 280: 34590-34598.
    • (2005) J Biol Chem , vol.280 , pp. 34590-34598
    • Porras-Yakushi, T.R.1    Whitelegge, J.P.2    Miranda, T.B.3    Clarke, S.4
  • 185
    • 0033579564 scopus 로고    scopus 로고
    • Rubisco small and large subunit N-methyltransferases. Bi- and mono-functional methyltransferases that methylate the small and large subunits of Rubisco
    • Ying Z, Mulligan RM, Janney N and Houtz RL. Rubisco small and large subunit N-methyltransferases. Bi- and mono-functional methyltransferases that methylate the small and large subunits of Rubisco. J Biol Chem 1999, 274: 36750-36756.
    • (1999) J Biol Chem , vol.274 , pp. 36750-36756
    • Ying, Z.1    Mulligan, R.M.2    Janney, N.3    Houtz, R.L.4
  • 186
    • 56349155647 scopus 로고    scopus 로고
    • Specificity of protein lysine methyltransferases and methods for detection of lysine methylation of non-histone proteins
    • Rathert P, Dhayalan A, Ma H and Jeltsch A. Specificity of protein lysine methyltransferases and methods for detection of lysine methylation of non-histone proteins. Mol Biosyst 2008, 4: 1186-1190.
    • (2008) Mol Biosyst , vol.4 , pp. 1186-1190
    • Rathert, P.1    Dhayalan, A.2    Ma, H.3    Jeltsch, A.4
  • 187
    • 77952986553 scopus 로고    scopus 로고
    • Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs
    • ra12
    • Mok J, Kim PM, Lam HY, Piccirillo S, Zhou X, Jeschke GR and Sheridan DL, et al. Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci Signal 2010, 3: ra12.
    • (2010) Sci Signal , pp. 3
    • Mok, J.1    Kim, P.M.2    Lam, H.Y.3    Piccirillo, S.4    Zhou, X.5    Jeschke, G.R.6    Sheridan, D.L.7
  • 188
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong SE and Mann M. A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 2006, 1: 2650-2660.
    • (2006) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 190
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P and Mann M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 2006, 127: 635-648.
    • (2006) Cell , vol.127 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    MacEk, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 191
    • 77149148756 scopus 로고    scopus 로고
    • Regulation of cellular metabolism by protein lysine acetylation
    • Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T and Yao J, et al. Regulation of cellular metabolism by protein lysine acetylation. Science 2010, 327: 1000-1004.
    • (2010) Science , vol.327 , pp. 1000-1004
    • Zhao, S.1    Xu, W.2    Jiang, W.3    Yu, W.4    Lin, Y.5    Zhang, T.6    Yao, J.7


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