메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages

Theoretical Insights into Catalytic Mechanism of Protein Arginine Methyltransferase 1

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLIC ACID DERIVATIVE; PROTEIN ARGININE METHYLTRANSFERASE; S ADENOSYLMETHIONINE; ARGININE; PRMT1 PROTEIN, RAT; PROTON;

EID: 84882654707     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0072424     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 58149295717 scopus 로고    scopus 로고
    • Protein Arginine Methylation in Mammals: Who, What, and Why
    • doi: 10.1016/j.molcel.2008.12.013
    • Bedford MT, Clarke SG, (2009) Protein Arginine Methylation in Mammals: Who, What, and Why. Mol Cell 33: 1-13. doi:10.1016/j.molcel.2008.12.013. PubMed: 19150423.
    • (2009) Mol Cell , vol.33 , pp. 1-13
    • Bedford, M.T.1    Clarke, S.G.2
  • 2
    • 0035800524 scopus 로고    scopus 로고
    • Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor
    • doi: 10.1126/science.1060781
    • Wang HB, Huang ZQ, Xia L, Feng Q, Erdjument-Bromage H, et al. (2001) Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor. Science 293: 853-857. doi:10.1126/science.1060781. PubMed: 11387442.
    • (2001) Science , vol.293 , pp. 853-857
    • Wang, H.B.1    Huang, Z.Q.2    Xia, L.3    Feng, Q.4    Erdjument-Bromage, H.5
  • 3
    • 47549090307 scopus 로고    scopus 로고
    • Regulation of estrogen rapid signaling through arginine methylation by PRMT1
    • doi: 10.1016/j.molcel.2008.05.025
    • Le Romancer M, Treilleux I, Leconte N, Robin-Lespinasse Y, Sentis S, et al. (2008) Regulation of estrogen rapid signaling through arginine methylation by PRMT1. Mol Cell 31: 212-221. doi:10.1016/j.molcel.2008.05.025. PubMed: 18657504.
    • (2008) Mol Cell , vol.31 , pp. 212-221
    • Le Romancer, M.1    Treilleux, I.2    Leconte, N.3    Robin-Lespinasse, Y.4    Sentis, S.5
  • 4
    • 63049100536 scopus 로고    scopus 로고
    • PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function
    • doi: 10.1016/j.yexcr.2008.12.008
    • Jobert L, Argentini M, Tora L, (2009) PRMT1 mediated methylation of TAF15 is required for its positive gene regulatory function. Exp Cell Res 315: 1273-1286. doi:10.1016/j.yexcr.2008.12.008. PubMed: 19124016.
    • (2009) Exp Cell Res , vol.315 , pp. 1273-1286
    • Jobert, L.1    Argentini, M.2    Tora, L.3
  • 5
    • 79953314028 scopus 로고    scopus 로고
    • Protein-arginine Methyltransferase 1 (PRMT1) Methylates Ash2L, a Shared Component of Mammalian Histone H3K4 Methyltransferase Complexes
    • PubMed: 21285357
    • Butler JS, Zurita-Lopez CI, Clarke SG, Bedford MT, Dent SYR, (2011) Protein-arginine Methyltransferase 1 (PRMT1) Methylates Ash2L, a Shared Component of Mammalian Histone H3K4 Methyltransferase Complexes. J Biol Chem 286: 12234-44. PubMed: 21285357.
    • (2011) J Biol Chem , vol.286 , pp. 12234-12244
    • Butler, J.S.1    Zurita-Lopez, C.I.2    Clarke, S.G.3    Bedford, M.T.4    Dent, S.Y.R.5
  • 6
    • 84862551032 scopus 로고    scopus 로고
    • Protein arginine methyltransferases (PRMTs) as therapeutic targets
    • doi: 10.1517/14728222.2012.688030
    • Cha B, Jho EH, (2012) Protein arginine methyltransferases (PRMTs) as therapeutic targets. Expert Opin Ther Tar 16: 651-664. doi:10.1517/14728222.2012.688030.
    • (2012) Expert Opin Ther Tar , vol.16 , pp. 651-664
    • Cha, B.1    Jho, E.H.2
  • 7
    • 34249066117 scopus 로고    scopus 로고
    • Target-based approach to inhibitors of histone arginine methyltransferases
    • doi: 10.1021/jm061250e
    • Spannhoff A, Heinke R, Bauer I, Trojer P, Metzger E, et al. (2007) Target-based approach to inhibitors of histone arginine methyltransferases. J Med Chem 50: 2319-2325. doi:10.1021/jm061250e. PubMed: 17432842.
    • (2007) J Med Chem , vol.50 , pp. 2319-2325
    • Spannhoff, A.1    Heinke, R.2    Bauer, I.3    Trojer, P.4    Metzger, E.5
  • 8
    • 84866865006 scopus 로고    scopus 로고
    • Pharmacophore-Based Virtual Screening and Biological Evaluation of Small Molecule Inhibitors for Protein Arginine Methylation
    • doi: 10.1021/jm300521m
    • Wang JX, Chen LM, Sinha SH, Liang ZJ, Chai HF, et al. (2012) Pharmacophore-Based Virtual Screening and Biological Evaluation of Small Molecule Inhibitors for Protein Arginine Methylation. J Med Chem 55: 7978-7987. doi:10.1021/jm300521m. PubMed: 22928876.
    • (2012) J Med Chem , vol.55 , pp. 7978-7987
    • Wang, J.X.1    Chen, L.M.2    Sinha, S.H.3    Liang, Z.J.4    Chai, H.F.5
  • 9
    • 31944437048 scopus 로고    scopus 로고
    • Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: An ab initio QM/MM-FE study with multiple initial structures
    • doi:10.1021/ja056153+. PubMed: 16433545
    • Hu P, Zhang YK, (2006) Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: An ab initio QM/MM-FE study with multiple initial structures. J Am Chem Soc 128: 1272-1278 doi:10.1021/ja056153+. PubMed: 16433545.
    • (2006) J Am Chem Soc , vol.128 , pp. 1272-1278
    • Hu, P.1    Zhang, Y.K.2
  • 10
    • 44449162039 scopus 로고    scopus 로고
    • Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases
    • doi: 10.1073/pnas.0801788105
    • Zhang X, Bruice TC, (2008) Enzymatic mechanism and product specificity of SET-domain protein lysine methyltransferases. Proc Natl Acad Sci U S A 105: 5728-5732. doi:10.1073/pnas.0801788105. PubMed: 18391193.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5728-5732
    • Zhang, X.1    Bruice, T.C.2
  • 11
    • 79956279966 scopus 로고    scopus 로고
    • Modeling a New Water Channel That Allows SET9 to Dimethylate p53
    • doi: 10.1371/journal.pone.0019856
    • Bai QF, Shen YL, Yao XJ, Wang F, Du YP, et al. (2011) Modeling a New Water Channel That Allows SET9 to Dimethylate p53. PLOS ONE 6(5):: e19856. doi:10.1371/journal.pone.0019856. PubMed: 21625555.
    • (2011) PLOS ONE , vol.6
    • Bai, Q.F.1    Shen, Y.L.2    Yao, X.J.3    Wang, F.4    Du, Y.P.5
  • 12
    • 37349096313 scopus 로고    scopus 로고
    • Histone lysine methyltransferase SET7/9: Formation of a water channel precedes each methyl transfer
    • doi: 10.1021/bi7014579
    • Zhang X, Bruice TC, (2007) Histone lysine methyltransferase SET7/9: Formation of a water channel precedes each methyl transfer. Biochemistry 46: 14838-14844. doi:10.1021/bi7014579. PubMed: 18044969.
    • (2007) Biochemistry , vol.46 , pp. 14838-14844
    • Zhang, X.1    Bruice, T.C.2
  • 13
    • 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 XD, (2003) Structure of the predominant protein arginine methyltransferase PRMT1 and analysis of its binding to substrate peptides. Structure 11: 509-520. doi:10.1016/S0969-2126(03)00071-6. PubMed: 12737817.
    • (2003) Structure , vol.11 , pp. 509-520
    • Zhang, X.1    Cheng, X.D.2
  • 14
    • 0033669186 scopus 로고    scopus 로고
    • The structure and oligomerization of the yeast arginine methyltransferase, Hmt1
    • doi: 10.1038/82028
    • Weiss VH, McBride AE, Soriano MA, Filman DJ, Silver PA, et al. (2000) The structure and oligomerization of the yeast arginine methyltransferase, Hmt1. Nat Struct Biol 7: 1165-1171. doi:10.1038/82028. PubMed: 11101900.
    • (2000) Nat Struct Biol , vol.7 , pp. 1165-1171
    • Weiss, V.H.1    McBride, A.E.2    Soriano, M.A.3    Filman, D.J.4    Silver, P.A.5
  • 15
    • 0034679591 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of protein arginine methyltransferase PRMT3
    • doi: 10.1093/emboj/19.14.3509
    • Zhang X, Zhou L, Cheng XD, (2000) Crystal structure of the conserved core of protein arginine methyltransferase PRMT3. EMBO J 19: 3509-3519. doi:10.1093/emboj/19.14.3509. PubMed: 10899106.
    • (2000) EMBO J , vol.19 , pp. 3509-3519
    • Zhang, X.1    Zhou, L.2    Cheng, X.D.3
  • 16
    • 35348861410 scopus 로고    scopus 로고
    • Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase
    • doi: 10.1038/sj.emboj.7601856
    • Yue WW, Hassler M, Roe SM, Thompson-Vale V, Pearl LH, (2007) Insights into histone code syntax from structural and biochemical studies of CARM1 methyltransferase. EMBO J 26: 4402-4412. doi:10.1038/sj.emboj.7601856. PubMed: 17882261.
    • (2007) EMBO J , vol.26 , pp. 4402-4412
    • Yue, W.W.1    Hassler, M.2    Roe, S.M.3    Thompson-Vale, V.4    Pearl, L.H.5
  • 17
    • 79955079071 scopus 로고    scopus 로고
    • Mechanistic Studies on Transcriptional Coactivator Protein Arginine Methyltransferase 1
    • doi: 10.1021/bi102022e
    • Rust HL, Zurita-Lopez CI, Clarke S, Thompson PR, (2011) Mechanistic Studies on Transcriptional Coactivator Protein Arginine Methyltransferase 1. Biochemistry 50: 3332-3345. doi:10.1021/bi102022e. PubMed: 21417440.
    • (2011) Biochemistry , vol.50 , pp. 3332-3345
    • Rust, H.L.1    Zurita-Lopez, C.I.2    Clarke, S.3    Thompson, P.R.4
  • 18
    • 84879394415 scopus 로고    scopus 로고
    • QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3
    • Chu Y, Li G, Guo H, (2013) QM/MM MD and free energy simulations of the methylation reactions catalyzed by protein arginine methyltransferase PRMT3. Can J Chem.
    • (2013) Can J Chem
    • Chu, Y.1    Li, G.2    Guo, H.3
  • 19
    • 23444454552 scopus 로고    scopus 로고
    • The Amber biomolecular simulation programs
    • doi: 10.1002/jcc.20290
    • Case DA, Cheatham TE, Darden T, Gohlke H, Luo R, et al. (2005) The Amber biomolecular simulation programs. J Comput Chem 26: 1668-1688. doi:10.1002/jcc.20290. PubMed: 16200636.
    • (2005) J Comput Chem , vol.26 , pp. 1668-1688
    • Case, D.A.1    Cheatham, T.E.2    Darden, T.3    Gohlke, H.4    Luo, R.5
  • 20
    • 35348916034 scopus 로고    scopus 로고
    • Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains
    • doi: 10.1038/sj.emboj.7601855
    • Troffer-Charlier N, Cura V, Hassenboehler P, Moras D, Cavarelli J, (2007) Functional insights from structures of coactivator-associated arginine methyltransferase 1 domains. EMBO J 26: 4391-4401. doi:10.1038/sj.emboj.7601855. PubMed: 17882262.
    • (2007) EMBO J , vol.26 , pp. 4391-4401
    • Troffer-Charlier, N.1    Cura, V.2    Hassenboehler, P.3    Moras, D.4    Cavarelli, J.5
  • 21
    • 79960367903 scopus 로고    scopus 로고
    • Chemogenetic Analysis of Human Protein Methyltransferases
    • doi: 10.1111/j.1747-0285.2011.01135.x
    • Richon VM, Johnston D, Sneeringer CJ, Jin L, Majer CR, et al. (2011) Chemogenetic Analysis of Human Protein Methyltransferases. Chem Bio Drugs Des 78: 199-210. doi:10.1111/j.1747-0285.2011.01135.x. PubMed: 21564555.
    • (2011) Chem Bio Drugs Des , vol.78 , pp. 199-210
    • Richon, V.M.1    Johnston, D.2    Sneeringer, C.J.3    Jin, L.4    Majer, C.R.5
  • 22
    • 23144457576 scopus 로고    scopus 로고
    • H++: a server for estimating pK(a)s and adding missing hydrogens to macromolecules
    • doi: 10.1093/nar/gki464
    • Gordon JC, Myers JB, Folta T, Shoja V, Heath LS, et al. (2005) H++: a server for estimating pK(a)s and adding missing hydrogens to macromolecules. Nucleic Acids Res 33: W368-W371. doi:10.1093/nar/gki464. PubMed: 15980491.
    • (2005) Nucleic Acids Res , vol.33
    • Gordon, J.C.1    Myers, J.B.2    Folta, T.3    Shoja, V.4    Heath, L.S.5
  • 23
    • 2942532422 scopus 로고    scopus 로고
    • Development and testing of a general amber force field
    • doi: 10.1002/jcc.20035
    • Wang JM, Wolf RM, Caldwell JW, Kollman PA, Case DA, (2004) Development and testing of a general amber force field. J Comput Chem 25: 1157-1174. doi:10.1002/jcc.20035. PubMed: 15116359.
    • (2004) J Comput Chem , vol.25 , pp. 1157-1174
    • Wang, J.M.1    Wolf, R.M.2    Caldwell, J.W.3    Kollman, P.A.4    Case, D.A.5
  • 24
    • 3042524904 scopus 로고
    • A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges - the Resp Model
    • doi: 10.1021/j100142a004
    • Bayly CI, Cieplak P, Cornell WD, Kollman PA, (1993) A Well-Behaved Electrostatic Potential Based Method Using Charge Restraints for Deriving Atomic Charges- the Resp Model. J Phys Chem 97: 10269-10280. doi:10.1021/j100142a004.
    • (1993) J Phys Chem , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 25
    • 0001216964 scopus 로고    scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (vol 117, pg 5179, 1995)
    • doi: 10.1021/ja955032e
    • Cornell WD, Cieplak P, Bayly CI, Gould IR, Merz KM, et al. (1996) A second generation force field for the simulation of proteins, nucleic acids, and organic molecules (vol 117, pg 5179, 1995). J Am Chem Soc 118: 2309-2309. doi:10.1021/ja955032e.
    • (1996) J Am Chem Soc , vol.118 , pp. 2309
    • Cornell, W.D.1    Cieplak, P.2    Bayly, C.I.3    Gould, I.R.4    Merz, K.M.5
  • 26
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple amber force fields and development of improved protein backbone parameters
    • doi: 10.1002/prot.21123
    • Hornak V, Abel R, Okur A, Strockbine B, Roitberg A, et al. (2006) Comparison of multiple amber force fields and development of improved protein backbone parameters. Proteins Struct Funct Bioinformatics 65: 712-725. doi:10.1002/prot.21123. PubMed: 16981200.
    • (2006) Proteins Struct Funct Bioinformatics , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5
  • 27
    • 0004016501 scopus 로고
    • Comparison of Simple Potential Functions for Simulating Liquid Water
    • doi: 10.1063/1.445869
    • Jorgensen WL, Chandrasekhar J, Madura JD, Impey RW, Klein ML, (1983) Comparison of Simple Potential Functions for Simulating Liquid Water. J Chem Phys 79: 926-935. doi:10.1063/1.445869.
    • (1983) J Chem Phys , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3    Impey, R.W.4    Klein, M.L.5
  • 28
    • 33646940952 scopus 로고
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints - Molecular-Dynamics of N-Alkanes
    • doi: 10.1016/0021-9991(77)90098-5
    • Ryckaert JP, Ciccotti G, Berendsen HJC, (1977) Numerical-Integration of Cartesian Equations of Motion of a System with Constraints- Molecular-Dynamics of N-Alkanes. J Comput Phys 23: 327-341. doi:10.1016/0021-9991(77)90098-5.
    • (1977) J Comput Phys , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 30
    • 0037473497 scopus 로고    scopus 로고
    • Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints
    • doi: 10.1002/jcc.10156
    • Vreven T, Morokuma K, Farkas O, Schlegel HB, Frisch MJ, (2003) Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints. J Comput Chem 24: 760-769. doi:10.1002/jcc.10156. PubMed: 12666168.
    • (2003) J Comput Chem , vol.24 , pp. 760-769
    • Vreven, T.1    Morokuma, K.2    Farkas, O.3    Schlegel, H.B.4    Frisch, M.J.5
  • 31
    • 77956509704 scopus 로고    scopus 로고
    • Investigation of the Catalytic Mechanism of Sir2 Enzyme with QM/MM Approach: SN1 vs SN2?
    • doi: 10.1021/jp1054183
    • Liang ZJ, Shi T, Ouyang SS, Li HL, Yu KQ, et al. (2010) Investigation of the Catalytic Mechanism of Sir2 Enzyme with QM/MM Approach: SN1 vs SN2? J Phys Chem B 114: 11927-11933. doi:10.1021/jp1054183. PubMed: 20726530.
    • (2010) J Phys Chem B , vol.114 , pp. 11927-11933
    • Liang, Z.J.1    Shi, T.2    Ouyang, S.S.3    Li, H.L.4    Yu, K.Q.5
  • 32
    • 80053578497 scopus 로고    scopus 로고
    • Catalytic Mechanism Investigation of Lysine-Specific Demethylase 1 (LSD1): A Computational Study
    • PubMed: 21984927
    • Kong XQ, Ouyang SS, Liang ZJ, Lu JY, Chen L, et al. (2011) Catalytic Mechanism Investigation of Lysine-Specific Demethylase 1 (LSD1): A Computational Study. PLOS ONE 6: e25444. PubMed: 21984927.
    • (2011) PLOS ONE , vol.6
    • Kong, X.Q.1    Ouyang, S.S.2    Liang, Z.J.3    Lu, J.Y.4    Chen, L.5
  • 33
    • 84860540565 scopus 로고    scopus 로고
    • Investigation of the Acetylation Mechanism by GCN5 Histone Acetyltransferase
    • doi: 10.1371/journal.pone.0036660
    • Jiang JF, Lu JY, Lu D, Liang ZJ, Li LC, et al. (2012) Investigation of the Acetylation Mechanism by GCN5 Histone Acetyltransferase. PLOS ONE 7(5):: e36660. doi:10.1371/journal.pone.0036660. PubMed: 22574209.
    • (2012) PLOS ONE , vol.7
    • Jiang, J.F.1    Lu, J.Y.2    Lu, D.3    Liang, Z.J.4    Li, L.C.5
  • 34
    • 0000189651 scopus 로고
    • Density-Functional Thermochemistry. 3. The Role of Exact Exchange
    • Becke AD, (1993) Density-Functional Thermochemistry. 3. The Role of Exact Exchange. Role Exact Exch J Chem Phys 98: 5648-5652.
    • (1993) Role Exact Exch J Chem Phys , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 35
    • 2842520383 scopus 로고
    • Potential-Energy Surfaces of the Gas-Phase S(N)2 Reactions X(-)+Ch(3)X=Xch(3)+X(-) (X=F, Cl, Br, I) - a Comparative-Study by Density-Functional Theory and Ab-Initio Methods
    • Deng LQ, Branchadell V, Ziegler T, (1994) Potential-Energy Surfaces of the Gas-Phase S(N)2 Reactions X(-)+Ch(3)X=Xch(3)+X(-) (X=F, Cl, Br, I)- a Comparative-Study by Density-Functional Theory and Ab-Initio Methods. J Am Chem Soc 116: 10645-10656.
    • (1994) J Am Chem Soc , vol.116 , pp. 10645-10656
    • Deng, L.Q.1    Branchadell, V.2    Ziegler, T.3
  • 36
    • 84986513644 scopus 로고
    • A Combined Quantum-Mechanical and Molecular Mechanical Potential for Molecular-Dynamics Simulations
    • doi: 10.1002/jcc.540110605
    • Field MJ, Bash PA, Karplus M, (1990) A Combined Quantum-Mechanical and Molecular Mechanical Potential for Molecular-Dynamics Simulations. J Comput Chem 11: 700-733. doi:10.1002/jcc.540110605.
    • (1990) J Comput Chem , vol.11 , pp. 700-733
    • Field, M.J.1    Bash, P.A.2    Karplus, M.3
  • 37
    • 0036917889 scopus 로고    scopus 로고
    • SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold
    • doi: 10.1016/S0959-440X(02)00391-3
    • Martin JL, McMillan FM, (2002) SAM (dependent) I AM: the S-adenosylmethionine-dependent methyltransferase fold. Curr Opin Struct Biol 12: 783-793. doi:10.1016/S0959-440X(02)00391-3. PubMed: 12504684.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 783-793
    • Martin, J.L.1    McMillan, F.M.2
  • 38
    • 80051681311 scopus 로고    scopus 로고
    • Investigation of the Molecular Origins of Protein-arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues
    • doi: 10.1074/jbc.M111.224097
    • Gui SY, Wooderchak WL, Daly MP, Porter PJ, Johnson SJ, et al. (2011) Investigation of the Molecular Origins of Protein-arginine Methyltransferase I (PRMT1) Product Specificity Reveals a Role for Two Conserved Methionine Residues. J Biol Chem 286: 29118-29126. doi:10.1074/jbc.M111.224097. PubMed: 21697082.
    • (2011) J Biol Chem , vol.286 , pp. 29118-29126
    • Gui, S.Y.1    Wooderchak, W.L.2    Daly, M.P.3    Porter, P.J.4    Johnson, S.J.5
  • 39
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • doi: 10.1016/0263-7855(96)00018-5
    • Humphrey W, Dalke A, Schulten K, (1996) VMD: Visual molecular dynamics. J Mol Graph Modell 14: 33-38. doi:10.1016/0263-7855(96)00018-5. PubMed: 8744570.
    • (1996) J Mol Graph Modell , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 40
    • 77952488976 scopus 로고    scopus 로고
    • Structural Biology of Human H3K9 Methyltransferases
    • doi: 10.1371/journal.pone.0008570
    • Wu H, Min J, Lunin VV, Antoshenko T, Dombrovski L, et al. (2010) Structural Biology of Human H3K9 Methyltransferases. PLOS ONE 5(1):: e8570. doi:10.1371/journal.pone.0008570. PubMed: 20084102.
    • (2010) PLOS ONE , vol.5
    • Wu, H.1    Min, J.2    Lunin, V.V.3    Antoshenko, T.4    Dombrovski, L.5
  • 41
    • 52949145297 scopus 로고    scopus 로고
    • Kinetic mechanism of protein arginine methyltransferase 1
    • doi: 10.1021/bi800904m
    • Obianyo O, Osborne TC, Thompson PR, (2008) Kinetic mechanism of protein arginine methyltransferase 1. Biochemistry 47: 10420-10427. doi:10.1021/bi800904m. PubMed: 18771293.
    • (2008) Biochemistry , vol.47 , pp. 10420-10427
    • Obianyo, O.1    Osborne, T.C.2    Thompson, P.R.3
  • 42
    • 84857562890 scopus 로고    scopus 로고
    • Understanding Product Specificity of Protein Lysine Methyltransferases from QM/MM MD and Free Energy Simulations: the Effects of Mutation on SET7/9 beyond the Tyr/Phe Switch
    • Guo H, Yao J, Chu Y, Ran A, (2012) Understanding Product Specificity of Protein Lysine Methyltransferases from QM/MM MD and Free Energy Simulations: the Effects of Mutation on SET7/9 beyond the Tyr/Phe Switch. J Chem Inf Model.
    • (2012) J Chem Inf Model
    • Guo, H.1    Yao, J.2    Chu, Y.3    Ran, A.4
  • 43
    • 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, (2007) 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: 13370-13381. doi:10.1021/bi701558t. PubMed: 17960915.
    • (2007) Biochemistry , vol.46 , pp. 13370-13381
    • Osborne, T.C.1    Obianyo, O.2    Zhang, X.3    Cheng, X.4    Thompson, P.R.5
  • 44
    • 0038419637 scopus 로고    scopus 로고
    • Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT
    • doi: 10.1038/nsb946
    • Trievel RC, Flynn EM, Houtz RL, Hurley JH, (2003) Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT. Nat Struct Biol 10: 545-552. doi:10.1038/nsb946. PubMed: 12819771.
    • (2003) Nat Struct Biol , vol.10 , pp. 545-552
    • Trievel, R.C.1    Flynn, E.M.2    Houtz, R.L.3    Hurley, J.H.4
  • 45
    • 34548201646 scopus 로고    scopus 로고
    • A quantum mechanics/molecular mechanics study of the catalytic mechanism and product specificity of viral histone lysine methyltransferase
    • doi: 10.1021/bi700515q
    • Zhang XD, Bruice TC, (2007) A quantum mechanics/molecular mechanics study of the catalytic mechanism and product specificity of viral histone lysine methyltransferase. Biochemistry 46: 9743-9751. doi:10.1021/bi700515q. PubMed: 17676763.
    • (2007) Biochemistry , vol.46 , pp. 9743-9751
    • Zhang, X.D.1    Bruice, T.C.2
  • 46
    • 80051496127 scopus 로고    scopus 로고
    • A Transient Kinetic Analysis of PRMT1 Catalysis
    • doi: 10.1021/bi200456u
    • Feng Y, Xie N, Jin M, Stahley MR, Stivers JT, et al. (2011) A Transient Kinetic Analysis of PRMT1 Catalysis. Biochemistry 50: 7033-7044. doi:10.1021/bi200456u. PubMed: 21736313.
    • (2011) Biochemistry , vol.50 , pp. 7033-7044
    • Feng, Y.1    Xie, N.2    Jin, M.3    Stahley, M.R.4    Stivers, J.T.5
  • 47
    • 37549006850 scopus 로고
    • Application of the pople-santry-segal CNDO method to the cyclopropylcarbinyl and cyclobutyl cation and to bicyclobutane
    • doi: 10.1016/0040-4020(68)88057-3
    • Wiberg KB, (1968) Application of the pople-santry-segal CNDO method to the cyclopropylcarbinyl and cyclobutyl cation and to bicyclobutane. Tetrahedron 24: 1083-1096. doi:10.1016/0040-4020(68)88057-3.
    • (1968) Tetrahedron , vol.24 , pp. 1083-1096
    • Wiberg, K.B.1
  • 48
    • 84862908725 scopus 로고    scopus 로고
    • Structural insights into protein arginine symmetric dimethylation by PRMT5
    • doi: 10.1073/pnas.1106946108
    • Sun L, Wang M, Lv Z, Yang N, Liu Y, et al. (2011) Structural insights into protein arginine symmetric dimethylation by PRMT5. Proc Natl Acad Sci U S A 108: 20538-20543. doi:10.1073/pnas.1106946108. PubMed: 22143770.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 20538-20543
    • Sun, L.1    Wang, M.2    Lv, Z.3    Yang, N.4    Liu, Y.5
  • 49
    • 81055156654 scopus 로고    scopus 로고
    • Crystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10
    • doi: 10.1016/j.jmb.2011.09.040
    • Cheng Y, Frazier M, Lu FL, Cao XF, Redinbo MR, (2011) Crystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10. J Mol Biol 414: 106-122. doi:10.1016/j.jmb.2011.09.040. PubMed: 21986201.
    • (2011) J Mol Biol , vol.414 , pp. 106-122
    • Cheng, Y.1    Frazier, M.2    Lu, F.L.3    Cao, X.F.4    Redinbo, M.R.5
  • 50
    • 84872120623 scopus 로고    scopus 로고
    • Substrate-Induced Control of Product Formation by Protein Arginine Methyltransferase 1
    • doi: 10.1021/bi301283t
    • Gui SY, Wooderchak-Donahue WL, Zang TZ, Chen D, Daly MP, et al. (2013) Substrate-Induced Control of Product Formation by Protein Arginine Methyltransferase 1. Biochemistry 52: 199-209. doi:10.1021/bi301283t. PubMed: 23214442.
    • (2013) Biochemistry , vol.52 , pp. 199-209
    • Gui, S.Y.1    Wooderchak-Donahue, W.L.2    Zang, T.Z.3    Chen, D.4    Daly, M.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.