메뉴 건너뛰기




Volumn 5, Issue 18, 2013, Pages 2199-2206

Targeting protein arginine N-methyltransferases with peptide-based inhibitors: Opportunities and challenges

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME INHIBITOR; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HISTONE H4; N(G),N(G) DIMETHYLARGININE; PEPTIDE; PROTEIN ARGININE METHYLTRANSFERASE; SINEFUNGIN;

EID: 84889575945     PISSN: 17568919     EISSN: 17568927     Source Type: Journal    
DOI: 10.4155/fmc.13.184     Document Type: Review
Times cited : (11)

References (36)
  • 2
  • 3
    • 84871712509 scopus 로고    scopus 로고
    • Protein arginine methyltransferases and cancer
    • Yang Y, Bedford MT. Protein arginine methyltransferases and cancer. Nat. Rev. Cancer. 13(1), 37-50 (2013).
    • (2013) Nat. Rev. Cancer. , vol.13 , Issue.1 , pp. 37-50
    • Yang, Y.1    Bedford, M.T.2
  • 4
    • 58149295717 scopus 로고    scopus 로고
    • Protein arginine methylation in mammals: Who, what, and why
    • Bedford MT, Clarke SG. Protein arginine methylation in mammals: who, what, and why. Mol. Cell 33(1), 1-13 (2009).
    • (2009) Mol. Cell , vol.33 , Issue.1 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 5
    • 79959829510 scopus 로고    scopus 로고
    • Histone arginine methylation
    • Di Lorenzo A, Bedford MT. Histone arginine methylation. FEBS Lett. 585(13), 2024-2031 (2011).
    • (2011) FEBS Lett. , vol.585 , Issue.13 , pp. 2024-2031
    • Di Lorenzo, A.1    Bedford, M.T.2
  • 6
    • 80052385986 scopus 로고    scopus 로고
    • Targets in epigenetics: Inhibiting the methyl writers of the histone code
    • Yost JM, Korboukh I, Liu F, Gao C, Jin J. Targets in epigenetics: inhibiting the methyl writers of the histone code. Curr. Chem. Genomics 5(Suppl. 1), 72-84 (2011).
    • (2011) Curr. Chem. Genomics , vol.5 , Issue.SUPPL. 1 , pp. 72-84
    • Yost, J.M.1    Korboukh, I.2    Liu, F.3    Gao, C.4    Jin, J.5
  • 7
    • 69949148388 scopus 로고    scopus 로고
    • Protein methyltransferases as a target class for drug discovery
    • Copeland RA, Solomon ME, Richon VM. Protein methyltransferases as a target class for drug discovery. Nat. Rev. Drug Discov. 8(9), 724-732 (2009).
    • (2009) Nat. Rev. Drug Discov. , vol.8 , Issue.9 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 8
    • 84862551032 scopus 로고    scopus 로고
    • Protein arginine methyltransferases (PRMTs) as therapeutic targets
    • Cha B, Jho EH. Protein arginine methyltransferases (PRMTs) as therapeutic targets. Expert Opin. Ther. Targets 16(7), 651-664 (2012).
    • (2012) Expert Opin. Ther. Targets , vol.16 , Issue.7 , pp. 651-664
    • Cha, B.1    Jho, E.H.2
  • 9
    • 78649684721 scopus 로고    scopus 로고
    • Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases
    • Lakowski TM, t Hart P, Ahern CA, Martin NI, Frankel A. Neta-substituted arginyl peptide inhibitors of protein arginine N-methyltransferases. ACS Chem. Biol. 5(11), 1053-1063 (2010).
    • (2010) ACS Chem. Biol , vol.5 , Issue.11 , pp. 1053-1063
    • Lakowski, T.M.1    Hart P, T.2    Ahern, C.A.3    Martin, N.I.4    Frankel, A.5
  • 10
    • 0031603283 scopus 로고    scopus 로고
    • RNA and protein interactions modulated by protein arginine methylation
    • Gary JD, Clarke S. 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
    • 51549095388 scopus 로고    scopus 로고
    • Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the RGG' paradigm
    • Wooderchak WL, Zang T, Zhou ZS, Acuna M, Tahara SM, Hevel JM. Substrate profiling of PRMT1 reveals amino acid sequences that extend beyond the RGG' paradigm. Biochemistry 47(36), 9456-9466 (2008).
    • (2008) Biochemistry , vol.47 , Issue.36 , pp. 9456-9466
    • Wooderchak, W.L.1    Zang, T.2    Zhou, Z.S.3    Acuna, M.4    Tahara, S.M.5    Hevel, J.M.6
  • 12
    • 0037904754 scopus 로고    scopus 로고
    • Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides
    • DOI 10.1016/S0969-2126(03)00071-6
    • Zhang X, Cheng X. Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 11(5), 509-520 (2003). (Pubitemid 36579129)
    • (2003) Structure , vol.11 , Issue.5 , pp. 509-520
    • Zhang, X.1    Cheng, X.2
  • 13
    • 84863773769 scopus 로고    scopus 로고
    • Peptide backbone conformation affects the substrate preference of protein arginine methyltransferase i
    • Kolbel K, Ihling C, Kuhn U et al. Peptide backbone conformation affects the substrate preference of protein arginine methyltransferase I. Biochemistry 51(27), 5463-5475 (2012).
    • (2012) Biochemistry , vol.51 , Issue.27 , pp. 5463-5475
    • Kolbel, K.1    Ihling, C.2    Kuhn, U.3
  • 14
    • 36248991292 scopus 로고    scopus 로고
    • Protein arginine methyltransferase 1: Positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis
    • DOI 10.1021/bi701558t
    • Osborne TC, Obianyo O, Zhang X, Cheng X, Thompson PR. Protein arginine methyltransferase 1: positively charged residues in substrate peptides distal to the site of methylation are important for substrate binding and catalysis. Biochemistry 46(46), 13370-13381 (2007). (Pubitemid 350136376)
    • (2007) Biochemistry , vol.46 , Issue.46 , pp. 13370-13381
    • Osborne, T.C.1    Obianyo, O.2    Zhang, X.3    Cheng, X.4    Thompson, P.R.5
  • 15
    • 84872120623 scopus 로고    scopus 로고
    • Substrate-induced control of product formation by protein arginine methyltransferase 1
    • Gui S, Wooderchak-Donahue WL, Zang T et al. Substrate-induced control of product formation by protein arginine methyltransferase 1. Biochemistry 52(1), 199-209 (2013).
    • (2013) Biochemistry , vol.52 , Issue.1 , pp. 199-209
    • Gui, S.1    Wooderchak-Donahue, W.L.2    Zang, T.3
  • 16
    • 33846001366 scopus 로고    scopus 로고
    • The Arginine Methyltransferase CARM1 Regulates the Coupling of Transcription and mRNA Processing
    • DOI 10.1016/j.molcel.2006.11.019, PII S1097276506007908
    • Cheng D, Cote J, Shaaban S, Bedford MT. The arginine methyltransferase CARM1 regulates the coupling of transcription and mRNA processing. Mol. Cell 25(1), 71-83 (2007). (Pubitemid 46049059)
    • (2007) Molecular Cell , vol.25 , Issue.1 , pp. 71-83
    • Cheng, D.1    Cote, J.2    Shaaban, S.3    Bedford, M.T.4
  • 17
    • 67650882496 scopus 로고    scopus 로고
    • Kinetic analysis of human protein arginine N-methyltransferase 2: Formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4
    • Lakowski TM, Frankel A. Kinetic analysis of human protein arginine N-methyltransferase 2: formation of monomethyl- and asymmetric dimethyl-arginine residues on histone H4. Biochem. J. 421(2), 253-261 (2009).
    • (2009) Biochem. J. , vol.421 , Issue.2 , pp. 253-261
    • Lakowski, T.M.1    Frankel, A.2
  • 18
    • 33645607060 scopus 로고    scopus 로고
    • Protein interfaces in signaling regulated by arginine methylation
    • Boisvert FM, Chenard CA, Richard S. Protein interfaces in signaling regulated by arginine methylation. Sci. STKE 2005(271), re2 (2005).
    • (2005) Sci. STKE 2005 , vol.271 , pp. 2
    • Boisvert, F.M.1    Chenard, C.A.2    Richard, S.3
  • 19
    • 79956042756 scopus 로고    scopus 로고
    • Structural basis for CARM1 inhibition by indole and pyrazole inhibitors
    • Sack JS, Thieffine S, Bandiera T et al. Structural basis for CARM1 inhibition by indole and pyrazole inhibitors. Biochem. J. 436(2), 331-339 (2011).
    • (2011) Biochem. J. , vol.436 , Issue.2 , pp. 331-339
    • Sack, J.S.1    Thieffine, S.2    Bandiera, T.3
  • 20
    • 53049103191 scopus 로고    scopus 로고
    • Preparation of N(G)-substituted l-arginine analogues suitable for solid phase peptide synthesis
    • Martin NI, Liskamp RM. Preparation of N(G)-substituted l-arginine analogues suitable for solid phase peptide synthesis. J. Org. Chem. 73(19), 7849-7851 (2008).
    • (2008) J. Org. Chem. , vol.73 , Issue.19 , pp. 7849-7851
    • Martin, N.I.1    Liskamp, R.M.2
  • 21
    • 78349299395 scopus 로고    scopus 로고
    • Forster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization
    • Thomas D, Lakowski TM, Pak ML, Kim JJ, Frankel A. Forster resonance energy transfer measurements of cofactor-dependent effects on protein arginine N-methyltransferase homodimerization. Protein Sci. 19(11), 2141-2151 (2010).
    • (2010) Protein Sci. , vol.19 , Issue.11 , pp. 2141-2151
    • Thomas, D.1    Lakowski, T.M.2    Pak, M.L.3    Kim, J.J.4    Frankel, A.5
  • 22
    • 84867007812 scopus 로고    scopus 로고
    • Analogues of the HIV-Tat peptide containing N-modified arginines as potent inhibitors of protein arginine N-methyltransferases
    • t Hart P, Thomas D, van Ommeren R, Lakowski TM, Frankel A, Martin NI. Analogues of the HIV-Tat peptide containing N?-modified arginines as potent inhibitors of protein arginine N-methyltransferases. Med. Chem. Commun. 3, 1235-1244 (2012).
    • (2012) Med. Chem. Commun. , vol.3 , pp. 1235-1244
    • Hart P, T.1    Thomas, D.2    Van Ommeren, R.3    Lakowski, T.M.4    Frankel, A.5    Martin, N.I.6
  • 23
    • 0017899194 scopus 로고
    • Sinefungin, a potent inhibitor of virion mRNA (guanine-7-)- methyltransferase, mRNA (nucleoside-2'-)-methyltransferase, and viral multiplication
    • Pugh CS, Borchardt RT, Stone HO. Sinefungin, a potent inhibitor of virion mRNA(guanine-7-)-methyltransferase, mRNA(nucleoside-2'-)-methyltransferase, and viral multiplication. J. Biol. Chem. 253(12), 4075-4077 (1978). (Pubitemid 8380622)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.12 , pp. 4075-4077
    • Pugh, C.S.G.1    Borchardt, R.T.2    Stone, H.O.3
  • 24
    • 33745842198 scopus 로고    scopus 로고
    • Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases
    • DOI 10.1074/jbc.M602257200
    • Couture JF, Hauk G, Thompson MJ, Blackburn GM, Trievel RC. Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases. J. Biol. Chem. 281(28), 19280-19287 (2006). (Pubitemid 44035432)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.28 , pp. 19280-19287
    • Couture, J.-F.1    Hauk, G.2    Thompson, M.J.3    Blackburn, G.M.4    Trievel, R.C.5
  • 25
    • 77949491799 scopus 로고    scopus 로고
    • Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases
    • Dowden J, Hong W, Parry RV, Pike RA, Ward SG. Toward the development of potent and selective bisubstrate inhibitors of protein arginine methyltransferases. Bioorg. Med. Chem. Lett. 20(7), 2103-2105 (2010).
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , Issue.7 , pp. 2103-2105
    • Dowden, J.1    Hong, W.2    Parry, R.V.3    Pike, R.A.4    Ward, S.G.5
  • 26
    • 80055010291 scopus 로고    scopus 로고
    • Small molecule inhibitors that discriminate between protein arginine N-methyltransferases PRMT1 and CARM1
    • Dowden J, Pike RA, Parry RV, Hong W, Muhsen UA, Ward SG. Small molecule inhibitors that discriminate between protein arginine N-methyltransferases PRMT1 and CARM1. Org. Biomol. Chem. 9(22), 7814-7821 (2011).
    • (2011) Org. Biomol. Chem. , vol.9 , Issue.22 , pp. 7814-7821
    • Dowden, J.1    Pike, R.A.2    Parry, R.V.3    Hong, W.4    Muhsen, U.A.5    Ward, S.G.6
  • 27
    • 79958713709 scopus 로고    scopus 로고
    • Peptidic partial bisubstrates as inhibitors of the protein arginine N-methyltransferases
    • t Hart P, Lakowski TM, Thomas D, Frankel A, Martin NI. Peptidic partial bisubstrates as inhibitors of the protein arginine N-methyltransferases. ChemBioChem 12(9), 1427-1432 (2011).
    • (2011) ChemBioChem , vol.12 , Issue.9 , pp. 1427-1432
    • Hart P, T.1    Lakowski, T.M.2    Thomas, D.3    Frankel, A.4    Martin, N.I.5
  • 28
    • 41849105766 scopus 로고    scopus 로고
    • In situ generation of a bisubstrate analogue for protein arginine methyltransferase 1
    • DOI 10.1021/ja077104v
    • Osborne T, Roska RL, Rajski SR, Thompson PR. In situ generation of a bisubstrate analogue for protein arginine methyltransferase 1. J. Am. Chem. Soc. 130(14), 4574-4575 (2008). (Pubitemid 351500080)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.14 , pp. 4574-4575
    • Osborne, T.1    Roska, R.L.W.2    Rajski, S.R.3    Thompson, P.R.4
  • 29
    • 31944448153 scopus 로고    scopus 로고
    • A fluoroacetamidine-based inactivator of protein arginine deiminase 4: Design, synthesis, and in vitro and in vivo evaluation
    • DOI 10.1021/ja0576233
    • Luo Y, Knuckley B, Lee YH, Stallcup MR, Thompson PR. A fluoroacetamidine-based inactivator of protein arginine deiminase 4: design, synthesis, and in vitro and in vivo evaluation. J. Am. Chem. Soc. 128(4), 1092-1093 (2006). (Pubitemid 43190618)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.4 , pp. 1092-1093
    • Luo, Y.1    Knuckley, B.2    Lee, Y.-H.3    Stallcup, M.R.4    Thompson, P.R.5
  • 30
    • 77953372136 scopus 로고    scopus 로고
    • A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation
    • Obianyo O, Causey CP, Osborne TC et al. A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: design, synthesis, and in vitro and in vivo evaluation. ChemBioChem 11(9), 1219-1223 (2010).
    • (2010) ChemBioChem , vol.11 , Issue.9 , pp. 1219-1223
    • Obianyo, O.1    Causey, C.P.2    Osborne, T.C.3
  • 31
    • 80054971718 scopus 로고    scopus 로고
    • Activity-based protein profiling of protein arginine methyltransferase 1
    • Obianyo O, Causey CP, Jones JE, Thompson PR. Activity-based protein profiling of protein arginine methyltransferase 1. ACS Chem. Biol. 6(10), 1127-1135 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , Issue.10 , pp. 1127-1135
    • Obianyo, O.1    Causey, C.P.2    Jones, J.E.3    Thompson, P.R.4
  • 32
    • 78650099217 scopus 로고    scopus 로고
    • A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1
    • Bicker KL, Obianyo O, Rust HL, Thompson PR. A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1. Mol. Biosyst 7(1), 48-51 (2011).
    • (2011) Mol. Biosyst , vol.7 , Issue.1 , pp. 48-51
    • Bicker, K.L.1    Obianyo, O.2    Rust, H.L.3    Thompson, P.R.4
  • 35
    • 58549089210 scopus 로고    scopus 로고
    • Virtual screening and biological characterization of novel histone arginine methyltransferase PRMT1 inhibitors
    • Heinke R, Spannhoff A, Meier R et al. Virtual screening and biological characterization of novel histone arginine methyltransferase PRMT1 inhibitors. ChemMedChem 4(1), 69-77 (2009).
    • (2009) Chem MedChem , vol.4 , Issue.1 , pp. 69-77
    • Heinke, R.1    Spannhoff, A.2    Meier, R.3
  • 36
    • 84866865006 scopus 로고    scopus 로고
    • Pharmacophore-based virtual screening and biological evaluation of small molecule inhibitors for protein arginine methylation
    • Wang J, Chen L, Sinha SH et al. Pharmacophore-based virtual screening and biological evaluation of small molecule inhibitors for protein arginine methylation. J. Med. Chem. 55(18), 7978-7987 (2012).
    • (2012) J. Med. Chem. , vol.55 , Issue.18 , pp. 7978-7987
    • Wang, J.1    Chen, L.2    Sinha, S.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.