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Volumn 11, Issue 1 P.1-446, 2006, Pages 344-355

Histone arginine methylation and its dynamic regulation

Author keywords

Arginine; Chromatin; De methylation; DNA; Methylation; Nucleosome; Review

Indexed keywords

MAMMALIA;

EID: 32844468049     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1802     Document Type: Review
Times cited : (197)

References (79)
  • 1
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger, S. L.: Histone modifications in transcriptional regulation. Curr Opin Genet Dev, 12, 142-8 (2002)
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 142-148
    • Berger, S.L.1
  • 2
    • 85015069067 scopus 로고    scopus 로고
    • Controlling the double helix
    • Felsenfeld, G. & M. Groudine: Controlling the double helix. Nature, 421, 448-53 (2003)
    • (2003) Nature , vol.421 , pp. 448-453
    • Felsenfeld, G.1    Groudine, M.2
  • 3
    • 23644436275 scopus 로고    scopus 로고
    • Histone modifications as key regulators of transcription
    • Khan, A. U. & S. Krishnamurthy: Histone modifications as key regulators of transcription. Front Biosci, 10, 866-72 (2005)
    • (2005) Front Biosci , vol.10 , pp. 866-872
    • Khan, A.U.1    Krishnamurthy, S.2
  • 4
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects
    • Richards, E. J. & S. C. Elgin: Epigenetic codes for heterochromatin formation and silencing: rounding up the usual suspects. Cell, 108, 489-500 (2002)
    • (2002) Cell , vol.108 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.2
  • 5
    • 0037672689 scopus 로고    scopus 로고
    • An epigenetic road map for histone lysine methylation
    • Lachner, M., R. J. O'Sullivan & T. Jenuwein: An epigenetic road map for histone lysine methylation. J Cell Sci, 116, 2117-24 (2003)
    • (2003) J Cell Sci , vol.116 , pp. 2117-2124
    • Lachner, M.1    O'Sullivan, R.J.2    Jenuwein, T.3
  • 6
    • 2942746711 scopus 로고    scopus 로고
    • The indexing potential of histone lysine methylation
    • discussion 37-47, 163-9
    • Schotta, G., M. Lachner, A. H. Peters & T. Jenuwein: The indexing potential of histone lysine methylation. Novartis Found Symp, 259, 22-37; discussion 37-47, 163-9 (2004)
    • (2004) Novartis Found Symp , vol.259 , pp. 22-37
    • Schotta, G.1    Lachner, M.2    Peters, A.H.3    Jenuwein, T.4
  • 7
    • 0242348752 scopus 로고    scopus 로고
    • Histone lysine methylation: A signature for chromatin function
    • Sims, R. J., 3rd, K. Nishioka & D. Reinberg: Histone lysine methylation: a signature for chromatin function. Trends Genet, 19, 629-39 (2003)
    • (2003) Trends Genet , vol.19 , pp. 629-639
    • Sims III, R.J.1    Nishioka, K.2    Reinberg, D.3
  • 8
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • Lee, D. Y., C. Teyssier, B. D. Strahl & M. R. Stallcup: Role of protein methylation in regulation of transcription. Endocr Rev, 26, 147-70 (2005)
    • (2005) Endocr Rev , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 9
    • 0037154312 scopus 로고    scopus 로고
    • Transcriptional control: An activating role for arginine methylation
    • Davie, J. K. & S. Y. Dent: Transcriptional control: an activating role for arginine methylation. Curr Biol, 12, R59-61 (2002)
    • (2002) Curr Biol , vol.12
    • Davie, J.K.1    Dent, S.Y.2
  • 10
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary, J. D. & S. Clarke: RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acid Res Mol Biol, 61, 65-131 (1998)
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 11
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: An emerging regulator of protein function
    • Bedford, M. T. & S. Richard: Arginine Methylation: An Emerging Regulator of Protein Function. Molecular Cell, 18, 263-272 (2005)
    • (2005) Molecular Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 13
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal, S., S. N. Vishwanath, H. Erdjument-Bromage, P. Tempst & S. Sif: Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol, 24, 9630-45 (2004)
    • (2004) Mol Cell Biol , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 15
    • 0035883954 scopus 로고    scopus 로고
    • Transcription regulation by histone methylation: Interplay between different covalent modifications of the core histone tails
    • Zhang, Y. & D. Reinberg: Transcription regulation by histone methylation: interplay between different covalent modifications of the core histone tails. Genes Dev, 15, 2343-60 (2001)
    • (2001) Genes Dev , vol.15 , pp. 2343-2360
    • Zhang, Y.1    Reinberg, D.2
  • 17
    • 0034731452 scopus 로고    scopus 로고
    • Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
    • Chen, D., S. M. Huang & M. R. Stallcup: Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300. J Biol Chem, 275, 40810-6 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 40810-40816
    • Chen, D.1    Huang, S.M.2    Stallcup, M.R.3
  • 18
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT, p300, and CARM1 in transcriptional activation by p53
    • An, W., J. Kim & R. G. Roeder: Ordered cooperative functions of PRMT, p300, and CARM1 in transcriptional activation by p53. Cell, 117, 735-48 (2004)
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 19
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Kwak, Y. T., J. Guo, S. Prajapati, K. J. Park, R. M. Surabhi, B. Miller, P. Gehrig & R. B. Gaynor: Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell, 11, 1055-66 (2003)
    • (2003) Mol Cell , vol.11 , pp. 1055-1066
    • Kwak, Y.T.1    Guo, J.2    Prajapati, S.3    Park, K.J.4    Surabhi, R.M.5    Miller, B.6    Gehrig, P.7    Gaynor, R.B.8
  • 20
    • 0030462232 scopus 로고    scopus 로고
    • The essential yeast RNA binding protein Np13p is methylated
    • Siebel, C. W. & C. Guthrie: The essential yeast RNA binding protein Np13p is methylated. Proc Natl Acad Sci U S A, 93, 13641-6 (1996)
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13641-13646
    • Siebel, C.W.1    Guthrie, C.2
  • 21
    • 0028957320 scopus 로고
    • In vivo and in vitro arginine methylation of RNA-binding proteins
    • Liu, Q. & G. Dreyfuss: In vivo and in vitro arginine methylation of RNA-binding proteins. Mol Cell Biol, 15, 2800-8 (1995)
    • (1995) Mol Cell Biol , vol.15 , pp. 2800-2808
    • Liu, Q.1    Dreyfuss, G.2
  • 22
    • 0036727126 scopus 로고    scopus 로고
    • Signalling through nuclear receptors
    • Tata, J. R.: Signalling through nuclear receptors. Nat Rev Mol Cell Biol, 3, 702-10 (2002)
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 702-710
    • Tata, J.R.1
  • 23
    • 3242784885 scopus 로고    scopus 로고
    • Mechanism of the nuclear receptor molecular switch
    • Nagy, L. & J. W. Schwabe: Mechanism of the nuclear receptor molecular switch. Trends Biochem Sci, 29, 317-24 (2004)
    • (2004) Trends Biochem Sci , vol.29 , pp. 317-324
    • Nagy, L.1    Schwabe, J.W.2
  • 24
    • 0242474622 scopus 로고    scopus 로고
    • Acetylation and methylation in nuclear receptor gene activation
    • Xu, W., H. Cho & R. M. Evans: Acetylation and methylation in nuclear receptor gene activation. Methods Enzymol, 364, 205-23 (2003)
    • (2003) Methods Enzymol , vol.364 , pp. 205-223
    • Xu, W.1    Cho, H.2    Evans, R.M.3
  • 25
    • 0042889568 scopus 로고    scopus 로고
    • The roles of protein-protein interactions and protein methylation in transcriptional activation by nuclear receptors and their coactivators
    • Stallcup, M. R., J. H. Kim, C. Teyssier, Y. H. Lee, H. Ma & D. Chen: The roles of protein-protein interactions and protein methylation in transcriptional activation by nuclear receptors and their coactivators. J Steroid Biochem Mol Biol, 85, 139-45 (2003)
    • (2003) J Steroid Biochem Mol Biol , vol.85 , pp. 139-145
    • Stallcup, M.R.1    Kim, J.H.2    Teyssier, C.3    Lee, Y.H.4    Ma, H.5    Chen, D.6
  • 26
    • 0037810854 scopus 로고    scopus 로고
    • Changes in histone acetylation during mouse oocyte meiosis
    • Kim, J. M., H. Liu, M. Tazaki, M. Nagata & F. Aoki: Changes in histone acetylation during mouse oocyte meiosis. J Cell Biol, 162, 37-46 (2003)
    • (2003) J Cell Biol , vol.162 , pp. 37-46
    • Kim, J.M.1    Liu, H.2    Tazaki, M.3    Nagata, M.4    Aoki, F.5
  • 29
    • 0034658463 scopus 로고    scopus 로고
    • The steroid receptor coactivator, GRIP-1, is necessary for MEF-2C-dependent gene expression and skeletal muscle differentiation
    • Chen, S. L., D. H. Dowhan, B. M. Hosking & G. E. Muscat: The steroid receptor coactivator, GRIP-1, is necessary for MEF-2C-dependent gene expression and skeletal muscle differentiation. Genes Dev, 14, 1209-28 (2000)
    • (2000) Genes Dev , vol.14 , pp. 1209-1228
    • Chen, S.L.1    Dowhan, D.H.2    Hosking, B.M.3    Muscat, G.E.4
  • 30
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: Selective requirement for protein methyltransferase and acetyltransferase activities
    • Lee, Y. H., S. S. Koh, X. Zhang, X. Cheng & M. R. Stallcup: Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol Cell Biol, 22, 3621-32 (2002)
    • (2002) Mol Cell Biol , vol.22 , pp. 3621-3632
    • Lee, Y.H.1    Koh, S.S.2    Zhang, X.3    Cheng, X.4    Stallcup, M.R.5
  • 31
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p 160 coactivators and two coactivators with protein methyltransferase activities
    • Koh, S. S., D. Chen, Y. H. Lee & M. R. Stallcup: Synergistic enhancement of nuclear receptor function by p 160 coactivators and two coactivators with protein methyltransferase activities. J Biol Chem, 276, 1089-98 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 32
    • 0037135602 scopus 로고    scopus 로고
    • Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators
    • Koh, S. S., H. Li, Y. H. Lee, R. B. Widelitz, C. M. Chuong & M. R. Stallcup: Synergistic coactivator function by coactivator-associated arginine methyltransferase (CARM) 1 and beta-catenin with two different classes of DNA-binding transcriptional activators. J Biol Chem, 277, 26031-5 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 26031-26035
    • Koh, S.S.1    Li, H.2    Lee, Y.H.3    Widelitz, R.B.4    Chuong, C.M.5    Stallcup, M.R.6
  • 33
    • 0037047399 scopus 로고    scopus 로고
    • Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha
    • Qi, C., J. Chang, Y. Zhu, A. V. Yeldandi, S. M. Rao & Y. J. Zhu: Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha. J Biol Chem, 277, 28624-30 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 28624-28630
    • Qi, C.1    Chang, J.2    Zhu, Y.3    Yeldandi, A.V.4    Rao, S.M.5    Zhu, Y.J.6
  • 36
    • 0142123234 scopus 로고    scopus 로고
    • mSinSA/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad
    • Pal, S., R. Yun, A. Datta, L. Lacomis, H. Erdjument-Bromage, J. Kumar, P. Tempst & S. Sif: mSinSA/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. Mol Cell Biol, 23, 7475-87 (2003)
    • (2003) Mol Cell Biol , vol.23 , pp. 7475-7487
    • Pal, S.1    Yun, R.2    Datta, A.3    Lacomis, L.4    Erdjument-Bromage, H.5    Kumar, J.6    Tempst, P.7    Sif, S.8
  • 37
    • 0038204415 scopus 로고    scopus 로고
    • The diverse functions of histone acetyltransferase complexes
    • Carrozza, M. J., R. T. Utley, J. L. Workman & J. Cote: The diverse functions of histone acetyltransferase complexes. Trends Genet, 19, 321-9 (2003)
    • (2003) Trends Genet , vol.19 , pp. 321-329
    • Carrozza, M.J.1    Utley, R.T.2    Workman, J.L.3    Cote, J.4
  • 38
    • 7544241632 scopus 로고    scopus 로고
    • Regulated nucleosome mobility and the histone code
    • Cosgrove, M. S., J. D. Boeke & C. Wolberger: Regulated nucleosome mobility and the histone code. Nat Struct Mol Biol, 11, 1037-43 (2004)
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1037-1043
    • Cosgrove, M.S.1    Boeke, J.D.2    Wolberger, C.3
  • 39
    • 0037098044 scopus 로고    scopus 로고
    • Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association
    • Ng, H. H., Q. Feng, H. Wang, H. Erdjument-Bromage, P. Tempst, Y. Zhang & K. Struhl: Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association. Genes Dev, 16, 1518-27 (2002)
    • (2002) Genes Dev , vol.16 , pp. 1518-1527
    • Ng, H.H.1    Feng, Q.2    Wang, H.3    Erdjument-Bromage, H.4    Tempst, P.5    Zhang, Y.6    Struhl, K.7
  • 40
    • 0037077178 scopus 로고    scopus 로고
    • Dot1p modulates silencing in yeast by methylation of the nucleosome core
    • van Leeuwen, F., P. R. Gafken & D. E. Gottschling: Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell, 109, 745-56 (2002)
    • (2002) Cell , vol.109 , pp. 745-756
    • Van Leeuwen, F.1    Gafken, P.R.2    Gottschling, D.E.3
  • 41
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat, S., U. M. Bauer, V. Shah, B. Turner, S. Berger & T. Kouzarides: Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr Biol, 12, 2090-7 (2002)
    • (2002) Curr Biol , vol.12 , pp. 2090-2097
    • Daujat, S.1    Bauer, U.M.2    Shah, V.3    Turner, B.4    Berger, S.5    Kouzarides, T.6
  • 43
    • 0037195877 scopus 로고    scopus 로고
    • Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function
    • Teyssier, C., D. Chen & M. R. Stallcup: Requirement for multiple domains of the protein arginine methyltransferase CARM1 in its transcriptional coactivator function. J Biol Chem, 277, 46066-72 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 46066-46072
    • Teyssier, C.1    Chen, D.2    Stallcup, M.R.3
  • 44
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle, W., Y. Wang & C. D. Allis: Binary switches and modification cassettes in histone biology and beyond. Nature, 425, 475-9 (2003)
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Allis, C.D.3
  • 46
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex
    • Zegerman, P., B. Canas, D. Pappin & T. Kouzarides: Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex. J Biol Chem, 277, 11621-4 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 48
    • 0037459239 scopus 로고    scopus 로고
    • High-resolution X-ray and NMR structures of the SMN Tudor domain: Conformational variation in the binding site for symmetrically dimethylated arginine residues
    • Sprangers, R., M. R. Groves, I. Sinning & M. Sattler: High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. J Mol Biol, 327, 507-20 (2003)
    • (2003) J Mol Biol , vol.327 , pp. 507-520
    • Sprangers, R.1    Groves, M.R.2    Sinning, I.3    Sattler, M.4
  • 49
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
    • Pawlak, M. R., C. A. Scherer, J. Chen, M. J. Roshon & H. E. Ruley: Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable. Mol Cell Biol, 20, 4859-69 (2000)
    • (2000) Mol Cell Biol , vol.20 , pp. 4859-4869
    • Pawlak, M.R.1    Scherer, C.A.2    Chen, J.3    Roshon, M.J.4    Ruley, H.E.5
  • 50
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
    • Yadav, N., J. Lee, J. Kim, J. Shen, M. C. Hu, C. M. Aldaz & M. T. Bedford: Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice. Proc Natl Acad Sci U S A, 100, 6464-8 (2003)
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6464-6468
    • Yadav, N.1    Lee, J.2    Kim, J.3    Shen, J.4    Hu, M.C.5    Aldaz, C.M.6    Bedford, M.T.7
  • 51
    • 0037083055 scopus 로고    scopus 로고
    • Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1
    • Cimato, T. R., J. Tang, Y. Xu, C. Guarnaccia, H. R. Herschman, S. Pongor & J. M. Aletta: Nerve growth factor-mediated increases in protein methylation occur predominantly at type I arginine methylation sites and involve protein arginine methyltransferase 1. J Neurosci Res, 67, 435-42 (2002)
    • (2002) J Neurosci Res , vol.67 , pp. 435-442
    • Cimato, T.R.1    Tang, J.2    Xu, Y.3    Guarnaccia, C.4    Herschman, H.R.5    Pongor, S.6    Aletta, J.M.7
  • 53
    • 2942537778 scopus 로고    scopus 로고
    • Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development
    • Kim, J., J. Lee, N. Yadav, Q. Wu, C. Carter, S. Richard, E. Richie & M. T. Bedford: Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development. J Biol Chem, 279, 25339-44 (2004)
    • (2004) J Biol Chem , vol.279 , pp. 25339-25344
    • Kim, J.1    Lee, J.2    Yadav, N.3    Wu, Q.4    Carter, C.5    Richard, S.6    Richie, E.7    Bedford, M.T.8
  • 54
    • 0037040245 scopus 로고    scopus 로고
    • The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2
    • Chen, S. L., K. A. Loffler, D. Chen, M. R. Stallcup & G. E. Muscat: The coactivator-associated arginine methyltransferase is necessary for muscle differentiation: CARM1 coactivates myocyte enhancer factor-2. J Biol Chem, 277, 4324-33 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 4324-4333
    • Chen, S.L.1    Loffler, K.A.2    Chen, D.3    Stallcup, M.R.4    Muscat, G.E.5
  • 55
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride, A. E. & P. A. Silver: State of the arg: protein methylation at arginine comes of age. Cell, 106, 5-8 (2001)
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 56
    • 0015412099 scopus 로고
    • In vivo turnover and distribution of radio-N-methyl in arginine-rich histones from rat tissues
    • Byvoet, P.: In vivo turnover and distribution of radio-N-methyl in arginine-rich histones from rat tissues. Arch Biochem Biophys, 152, 887-8 (1972)
    • (1972) Arch Biochem Biophys , vol.152 , pp. 887-888
    • Byvoet, P.1
  • 57
    • 0016271161 scopus 로고
    • In vivo methylation and turnover of rat brain histones
    • Duerre, J. A. & C. T. Lee: In vivo methylation and turnover of rat brain histones. J Neurochem, 23, 541-7 (1974)
    • (1974) J Neurochem , vol.23 , pp. 541-547
    • Duerre, J.A.1    Lee, C.T.2
  • 58
    • 0029817763 scopus 로고    scopus 로고
    • Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
    • Hecht, A., S. Strahl-Bolsinger & M. Grunstein: Spreading of transcriptional repressor SIR3 from telomeric heterochromatin. Nature, 383, 92-6 (1996)
    • (1996) Nature , vol.383 , pp. 92-96
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 59
    • 0242439142 scopus 로고    scopus 로고
    • Nuclear localization and histone acetylation: A pathway for chromatin opening and transcriptional activation of the human beta-globin locus
    • Schubeler, D., C. Francastel, D. M. Cimbora, A. Reik, D. I. Martin & M. Groudine: Nuclear localization and histone acetylation: a pathway for chromatin opening and transcriptional activation of the human beta-globin locus. Genes Dev, 14, 940-50 (2000)
    • (2000) Genes Dev , vol.14 , pp. 940-950
    • Schubeler, D.1    Francastel, C.2    Cimbora, D.M.3    Reik, A.4    Martin, D.I.5    Groudine, M.6
  • 60
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier, R., G. Penot, M. R. Hubner, G. Reid, H. Brand, M. Kos & F. Gannon: Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell, 115, 751-63 (2003)
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 61
  • 62
    • 0035874481 scopus 로고    scopus 로고
    • The marks, mechanisms and memory of epigenetic states in mammals
    • Rakyan, V. K., J. Preis, H. D. Morgan & E. Whitelaw: The marks, mechanisms and memory of epigenetic states in mammals. Biochem J, 356, 1-10 (2001)
    • (2001) Biochem J , vol.356 , pp. 1-10
    • Rakyan, V.K.1    Preis, J.2    Morgan, H.D.3    Whitelaw, E.4
  • 63
    • 0038699156 scopus 로고    scopus 로고
    • Reprogramming DNA methylation in the preimplantation stage: Peeping with Dolly's eyes
    • Kang, Y. K., K. K. Lee & Y. M. Han: Reprogramming DNA methylation in the preimplantation stage: peeping with Dolly's eyes. Curr Opin Cell Biol, 15, 290-5 (2003)
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 290-295
    • Kang, Y.K.1    Lee, K.K.2    Han, Y.M.3
  • 64
    • 0242720407 scopus 로고    scopus 로고
    • PAD, a growing family of citrullinating enzymes: Genes, features and involvement in disease
    • Vossenaar, E. R., A. J. Zendman, W. J. van Venrooij & G. J. Pruijn: PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. Bioessays, 25, 1106-18 (2003)
    • (2003) Bioessays , vol.25 , pp. 1106-1118
    • Vossenaar, E.R.1    Zendman, A.J.2    Van Venrooij, W.J.3    Pruijn, G.J.4
  • 65
    • 0035782680 scopus 로고    scopus 로고
    • The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide-containing lipid monolayers
    • Ishiyama, N., I. R. Bates, C. M. Hill, D. D. Wood, P. Matharu, N. J. Viner, M. A. Moscarello & G. Harauz: The effects of deimination of myelin basic protein on structures formed by its interaction with phosphoinositide- containing lipid monolayers. J Struct Biol, 136, 30-45 (2001)
    • (2001) J Struct Biol , vol.136 , pp. 30-45
    • Ishiyama, N.1    Bates, I.R.2    Hill, C.M.3    Wood, D.D.4    Matharu, P.5    Viner, N.J.6    Moscarello, M.A.7    Harauz, G.8
  • 66
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • Lamensa, J. W. & M. A. Moscarello: Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J Neurochem, 61, 987-96 (1993)
    • (1993) J Neurochem , vol.61 , pp. 987-996
    • Lamensa, J.W.1    Moscarello, M.A.2
  • 68
    • 0033600723 scopus 로고    scopus 로고
    • Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D (3)
    • Nakashima, K., T. Hagiwara, A. Ishigami, S. Nagata, H. Asaga, M. Kuramoto, T. Senshu & M. Yamada: Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D (3). J Biol Chem, 274, 27786-92 (1999)
    • (1999) J Biol Chem , vol.274 , pp. 27786-27792
    • Nakashima, K.1    Hagiwara, T.2    Ishigami, A.3    Nagata, S.4    Asaga, H.5    Kuramoto, M.6    Senshu, T.7    Yamada, M.8
  • 69
    • 0036295234 scopus 로고    scopus 로고
    • Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes
    • Hagiwara, T., K. Nakashima, H. Hirano, T. Senshu & M. Yamada: Deimination of arginine residues in nucleophosmin/B23 and histones in HL-60 granulocytes. Biochem Biophys Res Commun, 290, 979-83 (2002)
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 979-983
    • Hagiwara, T.1    Nakashima, K.2    Hirano, H.3    Senshu, T.4    Yamada, M.5
  • 70
    • 0037147140 scopus 로고    scopus 로고
    • Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes
    • Nakashima, K., T. Hagiwara & M. Yamada: Nuclear localization of peptidylarginine deiminase V and histone deimination in granulocytes. J Biol Chem, 277, 49562-8 (2002)
    • (2002) J Biol Chem , vol.277 , pp. 49562-49568
    • Nakashima, K.1    Hagiwara, T.2    Yamada, M.3
  • 73
    • 0037188911 scopus 로고    scopus 로고
    • Histone methylation: Dynamic or static?
    • Bannister, A. J., R. Schneider & T. Kouzarides: Histone methylation: dynamic or static? Cell, 109, 801-6 (2002)
    • (2002) Cell , vol.109 , pp. 801-806
    • Bannister, A.J.1    Schneider, R.2    Kouzarides, T.3
  • 74
    • 0015501421 scopus 로고
    • Studies of histone methylation during the HeLa S-3 cell cycle
    • Borun, T. W., D. Pearson & W. K. Paik: Studies of histone methylation during the HeLa S-3 cell cycle. J Biol Chem, 247, 4288-98 (1972)
    • (1972) J Biol Chem , vol.247 , pp. 4288-4298
    • Borun, T.W.1    Pearson, D.2    Paik, W.K.3
  • 75
    • 0016317384 scopus 로고
    • Epsilon-alkyllysinase. New assay method, purification, and biological significance
    • Paik, W. K. & S. Kim: Epsilon-alkyllysinase. New assay method, purification, and biological significance. Arch Biochem Biophys, 165, 369-78 (1974)
    • (1974) Arch Biochem Biophys , vol.165 , pp. 369-378
    • Paik, W.K.1    Kim, S.2
  • 76
  • 78
  • 79
    • 0037436410 scopus 로고    scopus 로고
    • Chromatin fiber folding: Requirement for the histone H4 N-terminal tail
    • Dorigo, B., T. Schalch, K. Bystricky & T. J. Richmond: Chromatin fiber folding: requirement for the histone H4 N-terminal tail. J Mol Biol, 327, 85-96 (2003)
    • (2003) J Mol Biol , vol.327 , pp. 85-96
    • Dorigo, B.1    Schalch, T.2    Bystricky, K.3    Richmond, T.J.4


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