메뉴 건너뛰기




Volumn 377, Issue 3, 2008, Pages 668-678

Protein Arginine Methyltransferase 1 Coactivates NF-κB-Dependent Gene Expression Synergistically with CARM1 and PARP1

Author keywords

CARM1; NF B; PARP1; PRMT1; transcription

Indexed keywords

COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1; HISTONE ACETYLTRANSFERASE PCAF; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MACROPHAGE INFLAMMATORY PROTEIN 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE 1; TRANSCRIPTION FACTOR RELA; UNCLASSIFIED DRUG;

EID: 40649124718     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.044     Document Type: Article
Times cited : (85)

References (50)
  • 1
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses
    • S. Ghosh M.J. May E.B. Kopp NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses Annu. Rev. Immunol. 16 1998 225 260
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 2
    • 0031906550 scopus 로고    scopus 로고
    • Signal transduction through NF-kappa B
    • M.J. May S. Ghosh Signal transduction through NF-kappa B Immunol. Today 19 1998 80 88
    • (1998) Immunol. Today , vol.19 , pp. 80-88
    • May, M.J.1    Ghosh, S.2
  • 3
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: new discoveries and insights
    • A.S. Baldwin Jr The NF-kappa B and I kappa B proteins: new discoveries and insights Annu. Rev. Immunol. 14 1996 649 683
    • (1996) Annu. Rev. Immunol. , vol.14 , pp. 649-683
    • Baldwin, A.S.1
  • 4
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa B transcription factor
    • P.A. Baeuerle D. Baltimore I kappa B: a specific inhibitor of the NF-kappa B transcription factor Science 242 1988 540 546
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 5
    • 0031126395 scopus 로고    scopus 로고
    • I kappa B proteins: structure, function and regulation
    • S.T. Whiteside A. Israel I kappa B proteins: structure, function and regulation Semin. Cancer Biol. 8 1997 75 82
    • (1997) Semin. Cancer Biol. , vol.8 , pp. 75-82
    • Whiteside, S.T.1    Israel, A.2
  • 6
    • 0031816705 scopus 로고    scopus 로고
    • The NF-kappa B activation pathway: its regulation and role in inflammation and cell survival
    • M. Karin The NF-kappa B activation pathway: its regulation and role in inflammation and cell survival Cancer J. Sci. Am. 4 1998 S92 S99
    • (1998) Cancer J. Sci. Am. , vol.4 , pp. S92-S99
    • Karin, M.1
  • 7
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
    • M. Karin Y. Ben-Neriah Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity Annu. Rev. Immunol. 18 2000 621 663
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 8
    • 0033681250 scopus 로고    scopus 로고
    • Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter
    • T. Agalioti S. Lomvardas B. Parekh J. Yie T. Maniatis D. Thanos Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter Cell 103 2000 667 678
    • (2000) Cell , vol.103 , pp. 667-678
    • Agalioti, T.1    Lomvardas, S.2    Parekh, B.3    Yie, J.4    Maniatis, T.5    Thanos, D.6
  • 9
    • 0031604766 scopus 로고    scopus 로고
    • Recruitment of CBP/p300 by the IFN beta enhanceosome is required for synergistic activation of transcription
    • M. Merika A.J. Williams G. Chen T. Collins D. Thanos Recruitment of CBP/p300 by the IFN beta enhanceosome is required for synergistic activation of transcription Mol. Cell 1 1998 277 287
    • (1998) Mol. Cell , vol.1 , pp. 277-287
    • Merika, M.1    Williams, A.J.2    Chen, G.3    Collins, T.4    Thanos, D.5
  • 12
    • 0242496900 scopus 로고    scopus 로고
    • Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1
    • P.O. Hassa C. Buerki C. Lombardi R. Imhof M.O. Hottiger Transcriptional coactivation of nuclear factor-kappaB-dependent gene expression by p300 is regulated by poly(ADP)-ribose polymerase-1 J. Biol. Chem. 278 2003 45145 45153
    • (2003) J. Biol. Chem. , vol.278 , pp. 45145-45153
    • Hassa, P.O.1    Buerki, C.2    Lombardi, C.3    Imhof, R.4    Hottiger, M.O.5
  • 13
    • 0030614504 scopus 로고    scopus 로고
    • Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator
    • N.D. Perkins L.K. Felzien J.C. Betts K. Leung D.H. Beach G.J. Nabel Regulation of NF-kappaB by cyclin-dependent kinases associated with the p300 coactivator Science 275 1997 523 527
    • (1997) Science , vol.275 , pp. 523-527
    • Perkins, N.D.1    Felzien, L.K.2    Betts, J.C.3    Leung, K.4    Beach, D.H.5    Nabel, G.J.6
  • 15
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP1 are not required for NF-kappa B coactivator function
    • P.O. Hassa M. Covic S. Hasan R. Imhof M.O. Hottiger The enzymatic and DNA binding activity of PARP1 are not required for NF-kappa B coactivator function J. Biol. Chem. 276 2001 45588 45597
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 16
    • 19944431570 scopus 로고    scopus 로고
    • Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression
    • M. Covic P.O. Hassa S. Saccani C. Buerki N.I. Meier C. Lombardi Arginine methyltransferase CARM1 is a promoter-specific regulator of NF-kappaB-dependent gene expression EMBO J. 24 2005 85 96
    • (2005) EMBO J. , vol.24 , pp. 85-96
    • Covic, M.1    Hassa, P.O.2    Saccani, S.3    Buerki, C.4    Meier, N.I.5    Lombardi, C.6
  • 17
    • 17044392996 scopus 로고    scopus 로고
    • Role of protein methylation in regulation of transcription
    • D.Y. Lee C. Teyssier B.D. Strahl M.R. Stallcup Role of protein methylation in regulation of transcription Endocr. Rev. 26 2005 147 170
    • (2005) Endocr. Rev. , vol.26 , pp. 147-170
    • Lee, D.Y.1    Teyssier, C.2    Strahl, B.D.3    Stallcup, M.R.4
  • 18
    • 0034677814 scopus 로고    scopus 로고
    • PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells
    • J. Tang A. Frankel R.J. Cook S. Kim W.K. Paik K.R. Williams PRMT1 is the predominant type I protein arginine methyltransferase in mammalian cells J. Biol. Chem. 275 2000 7723 7730
    • (2000) J. Biol. Chem. , vol.275 , pp. 7723-7730
    • Tang, J.1    Frankel, A.2    Cook, R.J.3    Kim, S.4    Paik, W.K.5    Williams, K.R.6
  • 19
  • 20
    • 0035954274 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1
    • B.D. Strahl S.D. Briggs C.J. Brame J.A. Caldwell S.S. Koh H. Ma Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1 Curr. Biol. 11 2001 996 1000
    • (2001) Curr. Biol. , vol.11 , pp. 996-1000
    • Strahl, B.D.1    Briggs, S.D.2    Brame, C.J.3    Caldwell, J.A.4    Koh, S.S.5    Ma, H.6
  • 21
    • 0035800524 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor
    • H. Wang Z.Q. Huang L. Xia Q. Feng H. Erdjument-Bromage B.D. Strahl Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor Science 293 2001 853 857
    • (2001) Science , vol.293 , pp. 853-857
    • Wang, H.1    Huang, Z.Q.2    Xia, L.3    Feng, Q.4    Erdjument-Bromage, H.5    Strahl, B.D.6
  • 22
    • 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
    • S.S. Koh 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 2002 26031 26035
    • (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
  • 23
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • W. An J. Kim R.G. Roeder 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
  • 24
    • 0037447302 scopus 로고    scopus 로고
    • Targeted recruitment of a histone H4-specific methyltransferase by the transcription factor YY1
    • N. Rezai-Zadeh X. Zhang F. Namour G. Fejer Y.D. Wen Y.L. Yao Targeted recruitment of a histone H4-specific methyltransferase by the transcription factor YY1 Genes Dev. 17 2003 1019 1029
    • (2003) Genes Dev. , vol.17 , pp. 1019-1029
    • Rezai-Zadeh, N.1    Zhang, X.2    Namour, F.3    Fejer, G.4    Wen, Y.D.5    Yao, Y.L.6
  • 26
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • X. Zhang X. Cheng Structure of the predominant protein arginine methyltransferase PRMT1 and 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
  • 27
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential
    • C.D. Krause Z.H. Yang Y.S. Kim J.H. Lee J.R. Cook S. Pestka Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutic potential Pharmacol. Ther. 113 2007 50 87
    • (2007) Pharmacol. Ther. , vol.113 , pp. 50-87
    • Krause, C.D.1    Yang, Z.H.2    Kim, Y.S.3    Lee, J.H.4    Cook, J.R.5    Pestka, S.6
  • 28
    • 17544370102 scopus 로고    scopus 로고
    • The mammalian immediate-early TIS21 protein and the leukemia-associated BTG1 protein interact with a protein-arginine N-methyltransferase
    • W.J. Lin J.D. Gary M.C. Yang S. Clarke H.R. Herschman 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
  • 29
    • 0031025092 scopus 로고    scopus 로고
    • A protein-arginine methyltransferase binds to the intracytoplasmic domain of the IFNAR1 chain in the type I interferon receptor
    • C. Abramovich B. Yakobson J. Chebath M. Revel 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
  • 30
    • 0035846640 scopus 로고    scopus 로고
    • Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter
    • H. Ma C.T. Baumann H. Li B.D. Strahl R. Rice M.A. Jelinek Hormone-dependent, CARM1-directed, arginine-specific methylation of histone H3 on a steroid-regulated promoter Curr. Biol. 11 2001 1981 1985
    • (2001) Curr. Biol. , vol.11 , pp. 1981-1985
    • Ma, H.1    Baumann, C.T.2    Li, H.3    Strahl, B.D.4    Rice, R.5    Jelinek, M.A.6
  • 31
    • 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
    • S. Pal 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 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
  • 32
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • S.S. Koh D. Chen Y.H. Lee M.R. Stallcup Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities J. Biol. Chem. 276 2001 1089 1098
    • (2001) J. Biol. Chem. , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 33
    • 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
    • J. Tang J.D. Gary S. Clarke H.R. Herschman 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
  • 34
    • 4344629701 scopus 로고    scopus 로고
    • Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes
    • K.A. Mowen B.T. Schurter J.W. Fathman M. David L.H. Glimcher Arginine methylation of NIP45 modulates cytokine gene expression in effector T lymphocytes Mol. Cell 15 2004 559 571
    • (2004) Mol. Cell , vol.15 , pp. 559-571
    • Mowen, K.A.1    Schurter, B.T.2    Fathman, J.W.3    David, M.4    Glimcher, L.H.5
  • 35
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B.D. Strahl C.D. Allis 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
  • 36
    • 0347955358 scopus 로고    scopus 로고
    • Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains
    • J.C. Rice S.D. Briggs B. Ueberheide C.M. Barber J. Shabanowitz D.F. Hunt Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains Mol. Cell 12 2003 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
  • 37
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities
    • Y.H. Lee 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 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
  • 38
    • 28844493947 scopus 로고    scopus 로고
    • Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription
    • P.O. Hassa S.S. Haenni C. Buerki N.I. Meier W.S. Lane H. Owen Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription J. Biol. Chem. 280 2005 40450 40464
    • (2005) J. Biol. Chem. , vol.280 , pp. 40450-40464
    • Hassa, P.O.1    Haenni, S.S.2    Buerki, C.3    Meier, N.I.4    Lane, W.S.5    Owen, H.6
  • 39
    • 23944435995 scopus 로고    scopus 로고
    • Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications
    • S. Huang M. Litt G. Felsenfeld Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications Genes Dev. 19 2005 1885 1893
    • (2005) Genes Dev. , vol.19 , pp. 1885-1893
    • Huang, S.1    Litt, M.2    Felsenfeld, G.3
  • 40
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • R. Metivier 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 2003 751 763
    • (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
  • 41
    • 0035930726 scopus 로고    scopus 로고
    • A transcriptional switch mediated by cofactor methylation
    • W. Xu H. Chen K. Du H. Asahara M. Tini B.M. Emerson A transcriptional switch mediated by cofactor methylation Science 294 2001 2507 2511
    • (2001) Science , vol.294 , pp. 2507-2511
    • Xu, W.1    Chen, H.2    Du, K.3    Asahara, H.4    Tini, M.5    Emerson, B.M.6
  • 42
    • 0037107417 scopus 로고    scopus 로고
    • Control of CBP co-activating activity by arginine methylation
    • M. Chevillard-Briet D. Trouche L. Vandel Control of CBP co-activating activity by arginine methylation EMBO J. 21 2002 5457 5466
    • (2002) EMBO J. , vol.21 , pp. 5457-5466
    • Chevillard-Briet, M.1    Trouche, D.2    Vandel, L.3
  • 43
    • 34250868257 scopus 로고    scopus 로고
    • Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function
    • D.Y. Lee I. Ianculescu D. Purcell X. Zhang X. Cheng M.R. Stallcup Surface-scanning mutational analysis of protein arginine methyltransferase 1: roles of specific amino acids in methyltransferase substrate specificity, oligomerization, and coactivator function Mol. Endocrinol. 21 2007 1381 1393
    • (2007) Mol. Endocrinol. , vol.21 , pp. 1381-1393
    • Lee, D.Y.1    Ianculescu, I.2    Purcell, D.3    Zhang, X.4    Cheng, X.5    Stallcup, M.R.6
  • 44
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • T.L. Branscombe A. Frankel J.H. Lee J.R. Cook Z. Yang S. Pestka S. Clarke 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
  • 45
    • 0035824647 scopus 로고    scopus 로고
    • The enzymatic and DNA binding activity of PARP1 are not required for NF-kappa B coactivator function
    • P.O. Hassa M. Covic S. Hasan R. Imhof M.O. Hottiger The enzymatic and DNA binding activity of PARP1 are not required for NF-kappa B coactivator function J. Biol. Chem. 276 2001 45588 45597
    • (2001) J. Biol. Chem. , vol.276 , pp. 45588-45597
    • Hassa, P.O.1    Covic, M.2    Hasan, S.3    Imhof, R.4    Hottiger, M.O.5
  • 46
  • 47
    • 0031690395 scopus 로고    scopus 로고
    • Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein
    • M.O. Hottiger G.J. Nabel Interaction of human immunodeficiency virus type 1 Tat with the transcriptional coactivators p300 and CREB binding protein J. Virol. 72 1998 8252 8256
    • (1998) J. Virol. , vol.72 , pp. 8252-8256
    • Hottiger, M.O.1    Nabel, G.J.2
  • 49
    • 2942537778 scopus 로고    scopus 로고
    • Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development
    • J. Kim J. Lee N. Yadav Q. Wu C. Carter S. Richard Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated phosphoprotein and deregulated early T cell development J. Biol. Chem. 279 2004 25339 25344
    • (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
  • 50
    • 0038313055 scopus 로고    scopus 로고
    • Specific protein methylation defects and gene expression perturbations in coactivator-associated arginine methyltransferase 1-deficient mice
    • N. Yadav 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. USA 100 2003 6464 6468
    • (2003) Proc. Natl Acad. Sci. USA , 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.