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Volumn 11, Issue 4, 2013, Pages 227-236

Assay development for histone methyltransferases

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H3; HISTONE H4; HISTONE METHYLTRANSFERASE; PROTEIN ARGININE METHYLTRANSFERASE; RADIOISOTOPE; S ADENOSYLMETHIONINE; SURAMIN;

EID: 84880194087     PISSN: 1540658X     EISSN: 15578127     Source Type: Journal    
DOI: 10.1089/adt.2012.480     Document Type: Article
Times cited : (66)

References (57)
  • 2
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, et al.: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 2000;406:593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3
  • 3
    • 2342475666 scopus 로고    scopus 로고
    • Polycomb complexes and silencing mechanisms
    • Lund AH, van Lohuizen M: Polycomb complexes and silencing mechanisms. Curr Opin Cell Biol 2004;16:239-246.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 239-246
    • Lund, A.H.1    Van Lohuizen, M.2
  • 4
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH, et al.: Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 2002;12:1052-1058.
    • (2002) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3
  • 5
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund AH, van Lohuizen M: Epigenetics and cancer. Genes Dev 2004;18:2315- 2335.
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    Van Lohuizen, M.2
  • 6
    • 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 2009;8:724-732.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 7
    • 55949132133 scopus 로고    scopus 로고
    • Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms
    • Margueron R, Li G, Sarma K, et al.: Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell 2008;32:503-518.
    • (2008) Mol Cell , vol.32 , pp. 503-518
    • Margueron, R.1    Li, G.2    Sarma, K.3
  • 8
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R, Wang L, Wang H, et al.: Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002;298:1039-1043.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3
  • 9
    • 1942502862 scopus 로고    scopus 로고
    • Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • Kuzmichev A, Jenuwein T, Tempst P, Reinberg D: Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell 2004;14:183-193.
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 10
    • 77955085750 scopus 로고    scopus 로고
    • Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders
    • Ernst T, Chase AJ, Score J, et al.: Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders. Nat Genet 2010;42:722-726.
    • (2010) Nat Genet , vol.42 , pp. 722-726
    • Ernst, T.1    Chase, A.J.2    Score, J.3
  • 11
    • 77951233574 scopus 로고    scopus 로고
    • G9a and glp methylate lysine 373 in the tumor suppressor p53
    • Huang J, Dorsey J, Chuikov S, et al.: G9a and Glp Methylate Lysine 373 in the Tumor Suppressor p53. J Biol Chem 2010;285:9636-9641.
    • (2010) J Biol Chem , vol.285 , pp. 9636-9641
    • Huang, J.1    Dorsey, J.2    Chuikov, S.3
  • 13
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, et al.: Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 2000;406:593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3
  • 14
    • 2342475666 scopus 로고    scopus 로고
    • Polycomb complexes and silencing mechanisms
    • Lund AH, van Lohuizen M: Polycomb complexes and silencing mechanisms. Curr Opin Cell Biol 2004;16:239-246.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 239-246
    • Lund, A.H.1    Van Lohuizen, M.2
  • 15
    • 0037172665 scopus 로고    scopus 로고
    • Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain
    • Feng Q, Wang H, Ng HH, et al.: Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr Biol 2002;12:1052-1058.
    • (2002) Curr Biol , vol.12 , pp. 1052-1058
    • Feng, Q.1    Wang, H.2    Ng, H.H.3
  • 16
    • 4744344066 scopus 로고    scopus 로고
    • Epigenetics and cancer
    • Lund AH, van Lohuizen M: Epigenetics and cancer. Genes Dev 2004;18:2315- 2335.
    • (2004) Genes Dev , vol.18 , pp. 2315-2335
    • Lund, A.H.1    Van Lohuizen, M.2
  • 17
    • 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 2009;8:724-732.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 724-732
    • Copeland, R.A.1    Solomon, M.E.2    Richon, V.M.3
  • 18
    • 55949132133 scopus 로고    scopus 로고
    • Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms
    • Margueron R, Li G, Sarma K, et al.: Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms. Mol Cell 2008;32:503-518.
    • (2008) Mol Cell , vol.32 , pp. 503-518
    • Margueron, R.1    Li, G.2    Sarma, K.3
  • 19
    • 0036830642 scopus 로고    scopus 로고
    • Role of histone H3 lysine 27 methylation in Polycomb-group silencing
    • Cao R, Wang L, Wang H, et al.: Role of histone H3 lysine 27 methylation in Polycomb-group silencing. Science 2002;298:1039-1043.
    • (2002) Science , vol.298 , pp. 1039-1043
    • Cao, R.1    Wang, L.2    Wang, H.3
  • 20
    • 1942502862 scopus 로고    scopus 로고
    • Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3
    • Kuzmichev A, Jenuwein T, Tempst P, Reinberg D: Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3. Mol Cell 2004;14:183-193.
    • (2004) Mol Cell , vol.14 , pp. 183-193
    • Kuzmichev, A.1    Jenuwein, T.2    Tempst, P.3    Reinberg, D.4
  • 21
    • 77955085750 scopus 로고    scopus 로고
    • Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders
    • Ernst T, Chase AJ, Score J, et al.: Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders. Nat Genet 2010;42:722-726.
    • (2010) Nat Genet , vol.42 , pp. 722-726
    • Ernst, T.1    Chase, A.J.2    Score, J.3
  • 22
    • 77951233574 scopus 로고    scopus 로고
    • G9a and glp methylate lysine 373 in the tumor suppressor p53
    • Huang J, Dorsey J, Chuikov S, et al.: G9a and Glp Methylate Lysine 373 in the Tumor Suppressor p53. J Biol Chem 2010;285:9636-9641
    • (2010) J Biol Chem , vol.285 , pp. 9636-9641
    • Huang, J.1    Dorsey, J.2    Chuikov, S.3
  • 23
    • 79952171495 scopus 로고    scopus 로고
    • Regulation of the androgen receptor by SET9-mediated methylation
    • Gaughan L, Stockley J, Wang N, et al.: Regulation of the androgen receptor by SET9-mediated methylation. Nucleic Acids Res 2011;39:1266-1279.
    • (2011) Nucleic Acids Res , vol.39 , pp. 1266-1279
    • Gaughan, L.1    Stockley, J.2    Wang, N.3
  • 24
    • 17444375685 scopus 로고    scopus 로고
    • HDOT1L links histone methylation to leukemogenesis
    • Okada Y, Feng Q, Lin Y, et al.: hDOT1L links histone methylation to leukemogenesis. Cell 2005;121:167-178.
    • (2005) Cell , vol.121 , pp. 167-178
    • Okada, Y.1    Feng, Q.2    Lin, Y.3
  • 25
    • 67649968054 scopus 로고    scopus 로고
    • The protein arginine methyltransferase family: An update about function, new perspectives and the physiological role in humans
    • Wolf SS: The protein arginine methyltransferase family: an update about function, new perspectives and the physiological role in humans. Cell Mol Life Sci 2009;66:2109-2121.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2109-2121
    • Wolf, S.S.1
  • 26
    • 33845896853 scopus 로고    scopus 로고
    • Protein arginine methyltransferases: Evolution and assessment of their pharmacological and therapeutical potential
    • Krause CD, Yang Z-H, Kim Y-S, Lee J-H, Cook JR, Pestka S: Protein arginine methyltransferases: evolution and assessment of their pharmacological and therapeutical potential. Pharmacol Ther 2007;113:50-87.
    • (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
  • 27
    • 4143111261 scopus 로고    scopus 로고
    • Histone methyltransferases in Aspergillus nidulans: Evidence for a novel enzyme with a unique substrate specificity
    • Trojer P, Dangl M, Bauer I, Graessle S, Loidl P, Brosch G: Histone methyltransferases in Aspergillus nidulans: evidence for a novel enzyme with a unique substrate specificity. Biochemisty 2004;43:10834-10843.
    • (2004) Biochemisty , vol.43 , pp. 10834-10843
    • Trojer, P.1    Dangl, M.2    Bauer, I.3    Graessle, S.4    Loidl, P.5    Brosch, G.6
  • 28
    • 33845418030 scopus 로고    scopus 로고
    • Protein arginine methylation: Cellular functions and methods of analysis
    • Pahlich S, Zakaryan RP, Gehling H: Protein arginine methylation: cellular functions and methods of analysis. Biochim Biophys Acta 2006;1764:1890-1903.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1890-1903
    • Pahlich, S.1    Zakaryan, R.P.2    Gehling, H.3
  • 29
    • 67650882496 scopus 로고    scopus 로고
    • Kinetic analysis of human protein arginine methyltransferase 2: Formation of monomethyl and asymmetric dimethylarginine residues on histone 4
    • Lakowski, TM, Frankel, A: Kinetic analysis of human protein arginine methyltransferase 2: formation of monomethyl and asymmetric dimethylarginine residues on histone 4. Biochem J 2009;421:253-261.
    • (2009) Biochem J , vol.421 , pp. 253-261
    • Lakowski, T.M.1    Frankel, A.2
  • 30
    • 33847678615 scopus 로고    scopus 로고
    • Historical review: The field of protein methylation
    • Paik WK, Paik DC, Kim S: Historical review: the field of protein methylation. Trends Biochem Sci 2007;32:146-152.
    • (2007) Trends Biochem Sci , vol.32 , pp. 146-152
    • Paik, W.K.1    Paik, D.C.2    Kim, S.3
  • 31
    • 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 1998;61:65-131.
    • (1998) Prog Nucleic Acid Res Mol Biol , vol.61 , pp. 65-131
    • Gary, J.D.1    Clarke, S.2
  • 32
    • 46149123246 scopus 로고    scopus 로고
    • Protein arginine methylation in health and disease
    • Aletta JM, Hu JC: Protein arginine methylation in health and disease. Biotechnol Annu Rev 2008;14:203-224.
    • (2008) Biotechnol Annu Rev , vol.14 , pp. 203-224
    • Aletta, J.M.1    Hu, J.C.2
  • 33
    • 35848951163 scopus 로고    scopus 로고
    • Covalent modifications of histones during development and disease pathogenesis
    • Bhaumik SR, Smith E, Shilatifard A: Covalent modifications of histones during development and disease pathogenesis. Nat Struct Mol Biol 2007;14:1008-1016.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1008-1016
    • Bhaumik, S.R.1    Smith, E.2    Shilatifard, A.3
  • 34
    • 45949106612 scopus 로고    scopus 로고
    • The challenge of selecting protein kinase assays for lead discovery optimization
    • Ma H, Deacon SW, Horiuchi KY: The challenge of selecting protein kinase assays for lead discovery optimization. Expert Opin Drug Discov 2008;3:607-621.
    • (2008) Expert Opin Drug Discov , vol.3 , pp. 607-621
    • Ma, H.1    Deacon, S.W.2    Horiuchi, K.Y.3
  • 35
    • 80755125565 scopus 로고    scopus 로고
    • Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity
    • Anastassiadis T, Deacon SW, Devarajan K, Ma H, Peterson JR: Comprehensive assay of kinase catalytic activity reveals features of kinase inhibitor selectivity. Nat Biotech 2011;29:1039-1045.
    • (2011) Nat Biotech , vol.29 , pp. 1039-1045
    • Anastassiadis, T.1    Deacon, S.W.2    Devarajan, K.3    Ma, H.4    Peterson, J.R.5
  • 36
    • 1642556015 scopus 로고    scopus 로고
    • Isolation of histones and nucleosome cores from mammalian cells
    • New York: John Wiley & Sons, Inc
    • Schnitzler GR: Isolation of Histones and Nucleosome Cores from Mammalian Cells. Current Protocols in Molecular Biology. New York: John Wiley & Sons, Inc., 2000;21.5.1-21.5.12.
    • (2000) Current Protocols in Molecular Biology , vol.21 , pp. 5121-5512
    • Schnitzler, G.R.1
  • 37
    • 84858636152 scopus 로고    scopus 로고
    • Current chemical biology approaches to interrogate protein methyltransferases
    • Luo M: Current chemical biology approaches to interrogate protein methyltransferases. ACS Chem Biol 2012;7:443-463.
    • (2012) ACS Chem Biol , vol.7 , pp. 443-463
    • Luo, M.1
  • 38
    • 0035816682 scopus 로고    scopus 로고
    • Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3
    • Tachibana M, Sugimoto K, Fukushima T, Shinkai Y: Set domain-containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. J Biol Chem 2001;276:25309-25317.
    • (2001) J Biol Chem , vol.276 , pp. 25309-25317
    • Tachibana, M.1    Sugimoto, K.2    Fukushima, T.3    Shinkai, Y.4
  • 39
    • 34547949573 scopus 로고    scopus 로고
    • A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: Identification of a new trans-histone pathway
    • Fingerman IM, Li H-C, Briggs SD: A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway. Genes Dev 2007;21:2018-2029.
    • (2007) Genes Dev , vol.21 , pp. 2018-2029
    • Fingerman, I.M.1    Li, H.-C.2    Briggs, S.D.3
  • 41
    • 0037020199 scopus 로고    scopus 로고
    • Structure and catalytic mechanism of a SET domain protein methyltransferase
    • Trievel RC, Beach BM, Dirk LMA, Houtz RL, Hurley JH: Structure and catalytic mechanism of a SET domain protein methyltransferase. Cell 2002;111:91-103.
    • (2002) Cell , vol.111 , pp. 91-103
    • Trievel, R.C.1    Beach, B.M.2    Lma, D.3    Houtz, R.L.4    Hurley, J.H.5
  • 42
    • 33947615716 scopus 로고    scopus 로고
    • Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases
    • Dirk LMA, Flynn EM, Dietzel K, Couture J-F, Trievel RC, Houtz RL: Kinetic manifestation of processivity during multiple methylations catalyzed by SET domain protein methyltransferases. Biochemistry 2007;46:3905-3915.
    • (2007) Biochemistry , vol.46 , pp. 3905-3915
    • Lma, D.1    Flynn, E.M.2    Dietzel, K.3    Couture, J.-F.4    Trievel, R.C.5    Houtz, R.L.6
  • 43
    • 79960367903 scopus 로고    scopus 로고
    • Chemogenetic analysis of human protein methyltransferases
    • Richon VM, Johnston D, Sneeringer CJ, et al.: Chemogenetic analysis of human protein methyltransferases. Chem Biol Drug Des 2011;78:199-210.
    • (2011) Chem Biol Drug des , vol.78 , pp. 199-210
    • Richon, V.M.1    Johnston, D.2    Sneeringer, C.J.3
  • 44
    • 33846783261 scopus 로고    scopus 로고
    • Reversal of H3K9me2 by a smallmolecule inhibitor for the G9a histone methyltransferase
    • Kubicek S, O'Sullivan RJ, August EM, et al.: Reversal of H3K9me2 by a smallmolecule inhibitor for the G9a histone methyltransferase. Mol Cell 2007;25: 473-481.
    • (2007) Mol Cell , vol.25 , pp. 473-481
    • Kubicek, S.1    O'Sullivan, R.J.2    August, E.M.3
  • 45
    • 62049083789 scopus 로고    scopus 로고
    • Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294
    • Chang Y, Zhang X, Horton JR, et al.: Structural basis for G9a-like protein lysine methyltransferase inhibition by BIX-01294. Nat Struct Mol Biol 2009;16:312-317.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 312-317
    • Chang, Y.1    Zhang, X.2    Horton, J.R.3
  • 46
    • 77955363182 scopus 로고    scopus 로고
    • Protein lysine methyltransferase G9a inhibitors: Design, synthesis, and structure activity relationships of 2,4- diamino-7-aminoalkoxy-quinazolines
    • Liu F, Chen X, Allali-Hassani A, et al.: Protein lysine methyltransferase G9a inhibitors: design, synthesis, and structure activity relationships of 2,4- diamino-7-aminoalkoxy-quinazolines. J Med Chem 2010;53:5844-5857.
    • (2010) J Med Chem , vol.53 , pp. 5844-5857
    • Liu, F.1    Chen, X.2    Allali-Hassani, A.3
  • 47
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high-throughput screening assays
    • Zhang JH, Chung TDY, Oldenburg KR: A simple statistical parameter for use in evaluation and validation of high-throughput screening assays. J Biomol Screen 1999;4:67-73.
    • (1999) J Biomol Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Tdy, C.2    Oldenburg, K.R.3
  • 48
    • 0842326028 scopus 로고    scopus 로고
    • The use of mass spectrometry for the analysis of histone modifications
    • Bonaldi T, Regula JT, Imhof A: The use of mass spectrometry for the analysis of histone modifications. Methods Enzymol 2004;377:111-130.
    • (2004) Methods Enzymol , vol.377 , pp. 111-130
    • Bonaldi, T.1    Regula, J.T.2    Imhof, A.3
  • 49
    • 36448944661 scopus 로고    scopus 로고
    • Continuous enzymatic assay for histone lysine methyltransferases
    • Rathert P, Cheng X, Jeltsch A: Continuous enzymatic assay for histone lysine methyltransferases. BioTechniques 2007;43:602-608.
    • (2007) BioTechniques , vol.43 , pp. 602-608
    • Rathert, P.1    Cheng, X.2    Jeltsch, A.3
  • 50
    • 77952361615 scopus 로고    scopus 로고
    • A chemiluminescencebased method for identification of histone lysine methyltransferase inhibitors
    • Quinn AM, Allali-Hassani A, Vedadi M, Simeonov A: A chemiluminescencebased method for identification of histone lysine methyltransferase inhibitors. Mol BioSyst 2010;6:782-788.
    • (2010) Mol BioSyst , vol.6 , pp. 782-788
    • Quinn, A.M.1    Allali-Hassani, A.2    Vedadi, M.3    Simeonov, A.4
  • 51
    • 37549057973 scopus 로고    scopus 로고
    • A universal competitive fluorescence polarization activity assay for S-adenosylmethionine utilizing methyltransferases
    • Graves TL, Zhang Y, Scott JE: A universal competitive fluorescence polarization activity assay for S-adenosylmethionine utilizing methyltransferases. Anal Biochem 2008;373:296-306.
    • (2008) Anal Biochem , vol.373 , pp. 296-306
    • Graves, T.L.1    Zhang, Y.2    Scott, J.E.3
  • 52
  • 53
    • 77955399089 scopus 로고    scopus 로고
    • Accessing protein methyltransferase and demethylase enzymology using microfluidic capillary electrophoresis
    • Wigle TJ, Provencher LM, Norris JL, et al.: Accessing protein methyltransferase and demethylase enzymology using microfluidic capillary electrophoresis. Chem Biol 2010;17:695-704.
    • (2010) Chem Biol , vol.17 , pp. 695-704
    • Wigle, T.J.1    Provencher, L.M.2    Norris, J.L.3
  • 55
    • 79955460159 scopus 로고    scopus 로고
    • H3K9 methyltransferase G9a and the related molecule GLP
    • Shinkai Y, Tachibana M: H3K9 methyltransferase G9a and the related molecule GLP. Genes Dev 2011;25:781-788.
    • (2011) Genes Dev , vol.25 , pp. 781-788
    • Shinkai, Y.1    Tachibana, M.2
  • 56
    • 84860575652 scopus 로고    scopus 로고
    • A high throughput scintillation proximity imaging assay for protein methyltransferases
    • Ibanez G, Shum D, Blum G, et al.: A high throughput scintillation proximity imaging assay for protein methyltransferases. Comb Chem High Throughput Screen 2012;15:359-371.
    • (2012) Comb Chem High Throughput Screen , vol.15 , pp. 359-371
    • Ibanez, G.1    Shum, D.2    Blum, G.3


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