메뉴 건너뛰기




Volumn 24, Issue C, 2006, Pages 105-121

4 Structure of protein arginine methyltransferases

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956698509     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-6047(06)80006-5     Document Type: Article
Times cited : (3)

References (67)
  • 1
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation an emerging regulator of protein function
    • Bedford M.T., and Richard S. Arginine methylation an emerging regulator of protein function. Mol Cell 18 (2005) 263-272
    • (2005) Mol Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 2
    • 0017337454 scopus 로고
    • S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme
    • Lee H.W., Kim S., and Paik W.K. S-adenosylmethionine: protein-arginine methyltransferase. Purification and mechanism of the enzyme. Biochemistry 16 (1977) 78-85
    • (1977) Biochemistry , vol.16 , pp. 78-85
    • Lee, H.W.1    Kim, S.2    Paik, W.K.3
  • 3
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe T.L., Frankel A., Lee J.H., Cook J.R., Yang Z., Pestka S., and Clarke S. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J Biol Chem 276 (2001) 32971-32976
    • (2001) J Biol Chem , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1    Frankel, A.2    Lee, J.H.3    Cook, J.R.4    Yang, Z.5    Pestka, S.6    Clarke, S.7
  • 5
    • 0030849362 scopus 로고    scopus 로고
    • Biological methylation of myelin basic protein: enzymology and biological significance
    • Kim S., Lim I.K., Park G.H., and Paik W.K. Biological methylation of myelin basic protein: enzymology and biological significance. Int J Biochem Cell Biol 29 (1997) 743-751
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 743-751
    • Kim, S.1    Lim, I.K.2    Park, G.H.3    Paik, W.K.4
  • 7
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., and Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 andnegatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol Cell Biol 24 (2004) 9630-9645
    • (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
  • 8
    • 0033615656 scopus 로고    scopus 로고
    • The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity
    • Pollack B.R., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., and Pestka S. The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity. J Biol Chem 274 (1999) 31531-31542
    • (1999) J Biol Chem , vol.274 , pp. 31531-31542
    • Pollack, B.R.1    Kotenko, S.V.2    He, W.3    Izotova, L.S.4    Barnoski, B.L.5    Pestka, S.6
  • 9
    • 0035815625 scopus 로고    scopus 로고
    • Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
    • Rho J., Choi S., Seong Y.R., Cho W.K., Kim S.H., and Im D.S. Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family. J Biol Chem 276 (2001) 11393-11401
    • (2001) J Biol Chem , vol.276 , pp. 11393-11401
    • Rho, J.1    Choi, S.2    Seong, Y.R.3    Cho, W.K.4    Kim, S.H.5    Im, D.S.6
  • 10
    • 0345826181 scopus 로고    scopus 로고
    • Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes
    • Yanagida M., Hayano T., Yamauchi Y., Shinkawa T., Natsume T., Isobe T., and Takahashi N. Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes. J Biol Chem 279 (2004) 1607-1614
    • (2004) J Biol Chem , vol.279 , pp. 1607-1614
    • Yanagida, M.1    Hayano, T.2    Yamauchi, Y.3    Shinkawa, T.4    Natsume, T.5    Isobe, T.6    Takahashi, N.7
  • 11
    • 0142123234 scopus 로고    scopus 로고
    • mSin3A/histone deacetylase 2- and PRMT5-containing Brgl complex is involved in transcriptional repression of the Myc target gene cad
    • Pal S., Yun R., Datta A., Lacomis L., Erdjument-Bromage H., Kumar J., Tempst P., and Sif S. mSin3A/histone deacetylase 2- and PRMT5-containing Brgl complex is involved in transcriptional repression of the Myc target gene cad. Mol Cell Biol 23 (2003) 7475-7487
    • (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
  • 12
    • 0036845335 scopus 로고    scopus 로고
    • Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs
    • Meister G., and Fischer U. Assisted RNP assembly: SMN and PRMT5 complexes cooperate in the formation of spliceosomal UsnRNPs. Embo J 21 (2002) 5853-5863
    • (2002) Embo J , vol.21 , pp. 5853-5863
    • Meister, G.1    Fischer, U.2
  • 13
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor plCln
    • Meister G., Eggert C., Buhler D., Brahms H., Kambach C., and Fischer U. Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor plCln. Curr Biol 11 (2001) 1990-1994
    • (2001) Curr Biol , vol.11 , pp. 1990-1994
    • Meister, G.1    Eggert, C.2    Buhler, D.3    Brahms, H.4    Kambach, C.5    Fischer, U.6
  • 14
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • Lin W.J., Gary J.D., Yang M.C., Clarke S., and Herschman H.R. The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase. J Biol Chem 271 (1996) 15034-15044
    • (1996) J Biol Chem , vol.271 , pp. 15034-15044
    • Lin, W.J.1    Gary, J.D.2    Yang, M.C.3    Clarke, S.4    Herschman, H.R.5
  • 15
    • 0031025092 scopus 로고    scopus 로고
    • A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
    • Abramovich C., Yakobson B., Chebath J., and Revel M. A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor. Embo J 16 (1997) 260-266
    • (1997) Embo J , vol.16 , pp. 260-266
    • Abramovich, C.1    Yakobson, B.2    Chebath, J.3    Revel, M.4
  • 16
    • 0031177791 scopus 로고    scopus 로고
    • Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene
    • Katsanis N., Yaspo M.L., and Fisher E.M. Identification and mapping of a novel human gene, HRMT1L1, homologous to the rat protein arginine N-methyltransferase 1 (PRMT1) gene. Mamm Genome 8 (1997) 526-529
    • (1997) Mamm Genome , vol.8 , pp. 526-529
    • Katsanis, N.1    Yaspo, M.L.2    Fisher, E.M.3
  • 17
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1and analysis of its binding to substrate peptides
    • Zhang X., and Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1and analysis of its binding to substrate peptides. Structure 11 (2003) 509-520
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 18
    • 0032521176 scopus 로고    scopus 로고
    • Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2)
    • Scott H.S., Antonarakis S.E., Lalioti M.D., Rossier C., Silver P.A., and Henry M.F. Identification and characterization of two putative human arginine methyltransferases (HRMT1L1 and HRMT1L2). Genomics 48 (1998) 330-340
    • (1998) Genomics , vol.48 , pp. 330-340
    • Scott, H.S.1    Antonarakis, S.E.2    Lalioti, M.D.3    Rossier, C.4    Silver, P.A.5    Henry, M.F.6
  • 19
    • 0032479171 scopus 로고    scopus 로고
    • PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation
    • Tang J., Gary J.D., Clarke S., and Herschman H.R. PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation. J Biol Chem 273 (1998) 16935-16945
    • (1998) J Biol Chem , vol.273 , pp. 16935-16945
    • Tang, J.1    Gary, J.D.2    Clarke, S.3    Herschman, H.R.4
  • 22
    • 0036479327 scopus 로고    scopus 로고
    • The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity
    • Frankel A., Yadav N., Lee J., Branscombe T.L., Clarke S., and Bedford M.T. The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity. J Biol Chem 277 (2002) 3537-3543
    • (2002) J Biol Chem , vol.277 , pp. 3537-3543
    • Frankel, A.1    Yadav, N.2    Lee, J.3    Branscombe, T.L.4    Clarke, S.5    Bedford, M.T.6
  • 23
    • 2542429259 scopus 로고    scopus 로고
    • PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity
    • Miranda T.B., Miranda M., Frankel A., and Clarke S. PRMT7 is a member of the protein arginine methyltransferase family with a distinct substrate specificity. J Biol Chem 279 (2004) 22902-22907
    • (2004) J Biol Chem , vol.279 , pp. 22902-22907
    • Miranda, T.B.1    Miranda, M.2    Frankel, A.3    Clarke, S.4
  • 25
    • 20544461679 scopus 로고    scopus 로고
    • Structural and sequence motifs of protein (histone) methylation enzymes
    • Cheng X., Collins R.E., and Zhang X. Structural and sequence motifs of protein (histone) methylation enzymes. Annu Rev Biophys Biomol Struct 34 (2005) 267-294
    • (2005) Annu Rev Biophys Biomol Struct , vol.34 , pp. 267-294
    • Cheng, X.1    Collins, R.E.2    Zhang, X.3
  • 32
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., and Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117 (2004) 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 33
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 34
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr Opin Genet Dev 12 (2002) 198-209
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 36
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities
    • Lee Y.H., Koh S.S., Zhang X., Cheng X., and Stallcup M.R. Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol Cell Biol 22 (2002) 3621-3632
    • (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
  • 37
    • 0037164736 scopus 로고    scopus 로고
    • Crosstalk between CARM1 methylation and CBP acetylation on histone H3
    • Daujat S., Bauer U.M., Shah V., Turner B., Berger S., and Kouzarides T. Crosstalk between CARM1 methylation and CBP acetylation on histone H3. Curr Biol 12 (2002) 2090-2097
    • (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
  • 38
    • 0034733748 scopus 로고    scopus 로고
    • Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3
    • Tang J., Kao P.N., and Herschman H.R. Protein-arginine methyltransferase I, the predominant protein-arginine methyltransferase in cells, interacts with and is regulated by interleukin enhancer-binding factor 3. J Biol Chem 275 (2000) 19866-19876
    • (2000) J Biol Chem , vol.275 , pp. 19866-19876
    • Tang, J.1    Kao, P.N.2    Herschman, H.R.3
  • 39
    • 0034045559 scopus 로고    scopus 로고
    • Arginine N-methyltransferase 1 is required for early postimplantation mousedevelopment, but cells deficient in the enzyme are viable
    • Pawlak M.R., Scherer C.A., Chen J., Roshon M.J., and Ruley H.E. Arginine N-methyltransferase 1 is required for early postimplantation mousedevelopment, but cells deficient in the enzyme are viable. Mol Cell Biol 20 (2000) 4859-4869
    • (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
  • 40
    • 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., Tang J., Xu Y., Guarnaccia C., Herschman H.R., Pongor S., and Aletta J.M. 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 (2002) 435-442
    • (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
  • 41
    • 0036031888 scopus 로고    scopus 로고
    • Protein arginine methyltransferase I: substrate specificity and role in hnRNPassembly
    • Pawlak M.R., Banik-Maiti S., Pietenpol J.A., and Ruley H.E. Protein arginine methyltransferase I: substrate specificity and role in hnRNPassembly. J Cell Biochem 87 (2002) 394-407
    • (2002) J Cell Biochem , vol.87 , pp. 394-407
    • Pawlak, M.R.1    Banik-Maiti, S.2    Pietenpol, J.A.3    Ruley, H.E.4
  • 42
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary J.D., and Clarke S. RNA and protein interactions modulated by protein arginine methylation. Prog Nucleic Acid Res Mol Biol 61 (1998) 65-131
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 43
    • 0039374447 scopus 로고    scopus 로고
    • Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3
    • Smith J.J., Rucknagel K.P., Schierhorn A., Tang J., Nemeth A., Linder M., Herschman H.R., and Wahle E. Unusual sites of arginine methylation in Poly(A)-binding protein II and in vitro methylation by protein arginine methyltransferases PRMT1 and PRMT3. J Biol Chem 274 (1999) 13229-13234
    • (1999) J Biol Chem , vol.274 , pp. 13229-13234
    • Smith, J.J.1    Rucknagel, K.P.2    Schierhorn, A.3    Tang, J.4    Nemeth, A.5    Linder, M.6    Herschman, H.R.7    Wahle, E.8
  • 45
    • 0037623333 scopus 로고    scopus 로고
    • Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties
    • Kwak Y.T., Guo J., Prajapati S., Park K.J., Surabhi R.M., Miller B., Gehrig P., and Gaynor R.B. Methylation of SPT5 regulates its interaction with RNA polymerase II and transcriptional elongation properties. Mol Cell 11 (2003) 1055-1066
    • (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
  • 46
    • 0035831040 scopus 로고    scopus 로고
    • Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription
    • Mowen K.A., Tang J., Zhu W., Schurter B.T., Shuai K., Herschman H.R., and David M. Arginine methylation of STAT1 modulates IFNalpha/beta-induced transcription. Cell 104 (2001) 731-741
    • (2001) Cell , vol.104 , pp. 731-741
    • Mowen, K.A.1    Tang, J.2    Zhu, W.3    Schurter, B.T.4    Shuai, K.5    Herschman, H.R.6    David, M.7
  • 47
    • 8844266055 scopus 로고    scopus 로고
    • Arginine methylation of STAT1: a reassessment
    • discussion 589-590
    • discussion 589-590. Meissner T., Krause E., Lodige I., and Vinkemeier U. Arginine methylation of STAT1: a reassessment. Cell 119 (2004) 587-589
    • (2004) Cell , vol.119 , pp. 587-589
    • Meissner, T.1    Krause, E.2    Lodige, I.3    Vinkemeier, U.4
  • 48
    • 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., Kim J.H., Teyssier C., Lee Y.H., Ma H., and Chen D. The roles of protein-protein interactions and protein methylation in transcriptional activation by nuclear receptors and their coactivators. J Steroid Biochem Mol Biol 85 (2003) 139-145
    • (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
  • 49
    • 0035962649 scopus 로고    scopus 로고
    • Role of protein methylation in chromatin remodeling and transcriptional regulation
    • Stallcup M.R. Role of protein methylation in chromatin remodeling and transcriptional regulation. Oncogene 20 (2001) 3014-3020
    • (2001) Oncogene , vol.20 , pp. 3014-3020
    • Stallcup, M.R.1
  • 50
    • 3342936604 scopus 로고    scopus 로고
    • PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits
    • Bachand F., and Silver P.A. PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits. Embo J 23 (2004) 2641-2650
    • (2004) Embo J , vol.23 , pp. 2641-2650
    • Bachand, F.1    Silver, P.A.2
  • 51
    • 14244255860 scopus 로고    scopus 로고
    • Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)
    • Swiercz R., Person M.D., and Bedford M.T. Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3). Biochem J 386 (2005) 85-91
    • (2005) Biochem J , vol.386 , pp. 85-91
    • Swiercz, R.1    Person, M.D.2    Bedford, M.T.3
  • 52
    • 7644222810 scopus 로고    scopus 로고
    • DAL-1/4.IB tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo
    • Singh V., Miranda T.B., Jiang W., Frankel A., Roemer M.E., Robb V.A., Gutmann D.H., Herschman H.R., Clarke S., and Newsham I.F. DAL-1/4.IB tumor suppressor interacts with protein arginine N-methyltransferase 3 (PRMT3) and inhibits its ability to methylate substrates in vitro and in vivo. Oncogene 23 (2004) 7761-7771
    • (2004) Oncogene , vol.23 , pp. 7761-7771
    • Singh, V.1    Miranda, T.B.2    Jiang, W.3    Frankel, A.4    Roemer, M.E.5    Robb, V.A.6    Gutmann, D.H.7    Herschman, H.R.8    Clarke, S.9    Newsham, I.F.10
  • 53
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • Zhang X., Zhou L., and Cheng X. Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. Embo J 19 (2000) 3509-3519
    • (2000) Embo J , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.3
  • 55
    • 0035883736 scopus 로고    scopus 로고
    • AdoMet-dependent methylation, DNA methyltransferases and base flipping
    • Cheng X., and Roberts R.J. AdoMet-dependent methylation, DNA methyltransferases and base flipping. Nucleic Acids Res 29 (2001) 3784-3795
    • (2001) Nucleic Acids Res , vol.29 , pp. 3784-3795
    • Cheng, X.1    Roberts, R.J.2
  • 56
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: a chronicle of convergence
    • Schubert H.L., Blumenthal R.M., and Cheng X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 28 (2003) 329-335
    • (2003) Trends Biochem Sci , vol.28 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 58
    • 0022273098 scopus 로고
    • Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23
    • Lischwe M.A., Cook R.G., Ahn Y.S., Yeoman L.C., and Busch H. Clustering of glycine and NG,NG-dimethylarginine in nucleolar protein C23. Biochemistry 24 (1985) 6025-6028
    • (1985) Biochemistry , vol.24 , pp. 6025-6028
    • Lischwe, M.A.1    Cook, R.G.2    Ahn, Y.S.3    Yeoman, L.C.4    Busch, H.5
  • 59
    • 0022405831 scopus 로고
    • Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine
    • Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M., Reichlin M., and Busch H. Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine. J Biol Chem 260 (1985) 14304-14310
    • (1985) J Biol Chem , vol.260 , pp. 14304-14310
    • Lischwe, M.A.1    Ochs, R.L.2    Reddy, R.3    Cook, R.G.4    Yeoman, L.C.5    Tan, E.M.6    Reichlin, M.7    Busch, H.8
  • 61
    • 16344368814 scopus 로고    scopus 로고
    • Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process
    • Forneris F., Binda C., Vanoni M.A., Mattevi A., and Battaglioli E. Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process. FEBS Lett 579 (2005) 2203-2207
    • (2005) FEBS Lett , vol.579 , pp. 2203-2207
    • Forneris, F.1    Binda, C.2    Vanoni, M.A.3    Mattevi, A.4    Battaglioli, E.5
  • 66
    • 17244368913 scopus 로고    scopus 로고
    • Genomic characterization reveals a simple histone H4 acetylation code
    • Dion M.F., Altschuler S.J., Wu L.F., and Rando O.J. Genomic characterization reveals a simple histone H4 acetylation code. Proc Natl Acad Sci USA 102 (2005) 5501-5506
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5501-5506
    • Dion, M.F.1    Altschuler, S.J.2    Wu, L.F.3    Rando, O.J.4
  • 67
    • 17244370475 scopus 로고    scopus 로고
    • Histone modifications: combinatorial complexity or cumulative simplicity?
    • Henikoff S. Histone modifications: combinatorial complexity or cumulative simplicity?. Proc Nad Acad Sci USA 102 (2005) 5308-5309
    • (2005) Proc Nad Acad Sci USA , vol.102 , pp. 5308-5309
    • Henikoff, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.