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Volumn 28, Issue , 2015, Pages 131-140

Synthetic histone code

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; HISTONE; PROTEIN; CHROMATIN;

EID: 84938699268     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2015.07.005     Document Type: Review
Times cited : (28)

References (70)
  • 1
    • 0017331464 scopus 로고
    • Structure of chromatin
    • Kornberg R.D. Structure of chromatin. Ann Rev Biochem 1977, 46:931-954.
    • (1977) Ann Rev Biochem , vol.46 , pp. 931-954
    • Kornberg, R.D.1
  • 2
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science 2001, 293:1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 3
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. Chromatin modifications and their function. Cell 2007, 128:693-705.
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 4
    • 84930726369 scopus 로고    scopus 로고
    • Application of the protein semisynthesis strategy to the generation of modified chromatin
    • Holt M., Muir T. Application of the protein semisynthesis strategy to the generation of modified chromatin. Annu Rev Biochem 2015, 84:265-290. 10.1146/annurev-biochem-060614-034429.
    • (2015) Annu Rev Biochem , vol.84 , pp. 265-290
    • Holt, M.1    Muir, T.2
  • 5
    • 84925832272 scopus 로고    scopus 로고
    • Histones: at the crossroads of peptide and protein chemistry
    • Muller M.M., Muir T.W. Histones: at the crossroads of peptide and protein chemistry. Chem Rev 2015, 115:2296-2349.
    • (2015) Chem Rev , vol.115 , pp. 2296-2349
    • Muller, M.M.1    Muir, T.W.2
  • 6
    • 84872085517 scopus 로고    scopus 로고
    • Systematic analysis of histone modification readout
    • Nikolov M., Fischle W. Systematic analysis of histone modification readout. Mol Biosyst 2013, 9:182-194.
    • (2013) Mol Biosyst , vol.9 , pp. 182-194
    • Nikolov, M.1    Fischle, W.2
  • 7
    • 78149379276 scopus 로고    scopus 로고
    • Chemical tools in chromatin research
    • Schwarzer D. Chemical tools in chromatin research. J Pept Sci 2010, 16:530-537.
    • (2010) J Pept Sci , vol.16 , pp. 530-537
    • Schwarzer, D.1
  • 8
    • 58049198236 scopus 로고    scopus 로고
    • Talk is cheap-cross-talk in establishment, maintenance, and readout of chromatin modifications
    • Fischle W. Talk is cheap-cross-talk in establishment, maintenance, and readout of chromatin modifications. Genes Dev 2008, 22:3375-3382.
    • (2008) Genes Dev , vol.22 , pp. 3375-3382
    • Fischle, W.1
  • 9
    • 78751490445 scopus 로고    scopus 로고
    • Spreading chromatin into chemical biology
    • Allis C.D., Muir T.W. Spreading chromatin into chemical biology. Chembiochem 2011, 12:264-279.
    • (2011) Chembiochem , vol.12 , pp. 264-279
    • Allis, C.D.1    Muir, T.W.2
  • 10
    • 84859836380 scopus 로고    scopus 로고
    • Chromatin as an expansive canvas for chemical biology
    • Fierz B., Muir T.W. Chromatin as an expansive canvas for chemical biology. Nat Chem Biol 2012, 8:417-427.
    • (2012) Nat Chem Biol , vol.8 , pp. 417-427
    • Fierz, B.1    Muir, T.W.2
  • 11
    • 84929628382 scopus 로고    scopus 로고
    • Chemical and biological tools for the preparation of modified histone proteins
    • Howard C.J., Yu R.R., Gardner M.L., Shimko J.C., Ottesen J.J. Chemical and biological tools for the preparation of modified histone proteins. Top Curr Chem 2015, 363:193-226.
    • (2015) Top Curr Chem , vol.363 , pp. 193-226
    • Howard, C.J.1    Yu, R.R.2    Gardner, M.L.3    Shimko, J.C.4    Ottesen, J.J.5
  • 12
    • 84931025395 scopus 로고    scopus 로고
    • The study of the chemical synthesis and preparation of histone with post-translational modifications
    • Wang Z.P., Wang Y.H., Chu G.C., Shi J., Li Y.M. The study of the chemical synthesis and preparation of histone with post-translational modifications. Curr Org Synth 2015, 12:150-162.
    • (2015) Curr Org Synth , vol.12 , pp. 150-162
    • Wang, Z.P.1    Wang, Y.H.2    Chu, G.C.3    Shi, J.4    Li, Y.M.5
  • 14
    • 84874619010 scopus 로고    scopus 로고
    • Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding
    • Le D.D., Cortesi A.T., Myers S.A., Burlingame A.L., Fujimori D.G. Site-specific and regiospecific installation of methylarginine analogues into recombinant histones and insights into effector protein binding. J Am Chem Soc 2013, 135:2879-2882.
    • (2013) J Am Chem Soc , vol.135 , pp. 2879-2882
    • Le, D.D.1    Cortesi, A.T.2    Myers, S.A.3    Burlingame, A.L.4    Fujimori, D.G.5
  • 17
    • 84856887479 scopus 로고    scopus 로고
    • Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications
    • Chalker J.M., Lercher L., Rose N.R., Schofield C.J., Davis B.G. Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications. Angew Chem Int Ed Engl 2012, 51:1835-1839.
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 1835-1839
    • Chalker, J.M.1    Lercher, L.2    Rose, N.R.3    Schofield, C.J.4    Davis, B.G.5
  • 18
    • 84941119192 scopus 로고    scopus 로고
    • Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks
    • Chen Z., Grzybowski A.T., Ruthenburg A.J. Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks. Chembiochem 2014, 15:2071-2075.
    • (2014) Chembiochem , vol.15 , pp. 2071-2075
    • Chen, Z.1    Grzybowski, A.T.2    Ruthenburg, A.J.3
  • 19
    • 80054914428 scopus 로고    scopus 로고
    • Purification and assay protocols for obtaining highly active Jumonji C demethylases
    • Krishnan S., Collazo E., Ortiz-Tello P.A., Trievel R.C. Purification and assay protocols for obtaining highly active Jumonji C demethylases. Anal Biochem 2012, 420:48-53.
    • (2012) Anal Biochem , vol.420 , pp. 48-53
    • Krishnan, S.1    Collazo, E.2    Ortiz-Tello, P.A.3    Trievel, R.C.4
  • 20
    • 84856144675 scopus 로고    scopus 로고
    • Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches
    • Seeliger D., Soeroes S., Klingberg R., Schwarzer D., Grubmuller H., Fischle W. Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches. ACS Chem Biol 2012, 7:150-154.
    • (2012) ACS Chem Biol , vol.7 , pp. 150-154
    • Seeliger, D.1    Soeroes, S.2    Klingberg, R.3    Schwarzer, D.4    Grubmuller, H.5    Fischle, W.6
  • 21
    • 77949874828 scopus 로고    scopus 로고
    • Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation
    • Chatterjee C., McGinty R.K., Fierz B., Muir T.W. Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation. Nat Chem Biol 2010, 6:267-269.
    • (2010) Nat Chem Biol , vol.6 , pp. 267-269
    • Chatterjee, C.1    McGinty, R.K.2    Fierz, B.3    Muir, T.W.4
  • 22
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., Brock A., Herberich B., Schultz P.G. Expanding the genetic code of Escherichia coli. Science 2001, 292:498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 23
    • 84870906814 scopus 로고    scopus 로고
    • Synthesis of epsilon-N-propionyl-, epsilon-N-butyryl-, and epsilon-N-crotonyl-lysine containing histone H3 using the pyrrolysine system
    • Gattner M.J., Vrabel M., Carell T. Synthesis of epsilon-N-propionyl-, epsilon-N-butyryl-, and epsilon-N-crotonyl-lysine containing histone H3 using the pyrrolysine system. Chem Commun (Camb) 2013, 49:379-381.
    • (2013) Chem Commun (Camb) , vol.49 , pp. 379-381
    • Gattner, M.J.1    Vrabel, M.2    Carell, T.3
  • 24
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu C.C., Schultz P.G. Adding new chemistries to the genetic code. Annu Rev Biochem 2010, 79:413-444.
    • (2010) Annu Rev Biochem , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 25
    • 70449571896 scopus 로고    scopus 로고
    • A pyrrolysine analogue for site-specific protein ubiquitination
    • Li X., Fekner T., Ottesen J.J., Chan M.K. A pyrrolysine analogue for site-specific protein ubiquitination. Angew Chem Int Ed Engl 2009, 48:9184-9187.
    • (2009) Angew Chem Int Ed Engl , vol.48 , pp. 9184-9187
    • Li, X.1    Fekner, T.2    Ottesen, J.J.3    Chan, M.K.4
  • 26
    • 80053897247 scopus 로고    scopus 로고
    • Expanded click conjugation of recombinant proteins with ubiquitin-like modifiers reveals altered substrate preference of SUMO2-modified Ubc9
    • Sommer S., Weikart N.D., Brockmeyer A., Janning P., Mootz H.D. Expanded click conjugation of recombinant proteins with ubiquitin-like modifiers reveals altered substrate preference of SUMO2-modified Ubc9. Angew Chem Int Ed Engl 2011, 50:9888-9892.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 9888-9892
    • Sommer, S.1    Weikart, N.D.2    Brockmeyer, A.3    Janning, P.4    Mootz, H.D.5
  • 30
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding N(epsilon)-acetyllysine in recombinant proteins
    • Neumann H., Peak-Chew S.Y., Chin J.W. Genetically encoding N(epsilon)-acetyllysine in recombinant proteins. Nat Chem Biol 2008, 4:232-234.
    • (2008) Nat Chem Biol , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 33
    • 84878039908 scopus 로고    scopus 로고
    • A facile strategy for selective incorporation of phosphoserine into histones
    • Lee S., Oh S., Yang A., Kim J., Soll D., Lee D., Park H.S. A facile strategy for selective incorporation of phosphoserine into histones. Angew Chem Int Ed Engl 2013, 52:5771-5775.
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 5771-5775
    • Lee, S.1    Oh, S.2    Yang, A.3    Kim, J.4    Soll, D.5    Lee, D.6    Park, H.S.7
  • 35
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson P.E., Kent S.B. Synthesis of native proteins by chemical ligation. Annu Rev Biochem 2000, 69:923-960.
    • (2000) Annu Rev Biochem , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 36
    • 57749121492 scopus 로고    scopus 로고
    • Chemoselective ligation and modification strategies for peptides and proteins
    • Hackenberger C.P., Schwarzer D. Chemoselective ligation and modification strategies for peptides and proteins. Angew Chem Int Ed Engl 2008, 47:10030-10074.
    • (2008) Angew Chem Int Ed Engl , vol.47 , pp. 10030-10074
    • Hackenberger, C.P.1    Schwarzer, D.2
  • 38
    • 70349390704 scopus 로고    scopus 로고
    • A semisynthetic strategy to generate phosphorylated and acetylated histone H2B
    • Chiang K.P., Jensen M.S., McGinty R.K., Muir T.W. A semisynthetic strategy to generate phosphorylated and acetylated histone H2B. Chembiochem 2009, 10:2182-2187.
    • (2009) Chembiochem , vol.10 , pp. 2182-2187
    • Chiang, K.P.1    Jensen, M.S.2    McGinty, R.K.3    Muir, T.W.4
  • 39
    • 84870708220 scopus 로고    scopus 로고
    • Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis
    • Fierz B., Kilic S., Hieb A.R., Luger K., Muir T.W. Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. J Am Chem Soc 2012, 134:19548-19551.
    • (2012) J Am Chem Soc , vol.134 , pp. 19548-19551
    • Fierz, B.1    Kilic, S.2    Hieb, A.R.3    Luger, K.4    Muir, T.W.5
  • 41
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
    • McGinty R.K., Kim J., Chatterjee C., Roeder R.G., Muir T.W. Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 2008, 453:812-816.
    • (2008) Nature , vol.453 , pp. 812-816
    • McGinty, R.K.1    Kim, J.2    Chatterjee, C.3    Roeder, R.G.4    Muir, T.W.5
  • 42
    • 0038047672 scopus 로고    scopus 로고
    • A native peptide ligation strategy for deciphering nucleosomal histone modifications
    • Shogren-Knaak M.A., Fry C.J., Peterson C.L. A native peptide ligation strategy for deciphering nucleosomal histone modifications. J Biol Chem 2003, 278:15744-15748.
    • (2003) J Biol Chem , vol.278 , pp. 15744-15748
    • Shogren-Knaak, M.A.1    Fry, C.J.2    Peterson, C.L.3
  • 43
    • 84880816458 scopus 로고    scopus 로고
    • Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34
    • Siman P., Karthikeyan S.V., Nikolov M., Fischle W., Brik A. Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34. Angew Chem Int Ed Engl 2013, 52:8059-8063.
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 8059-8063
    • Siman, P.1    Karthikeyan, S.V.2    Nikolov, M.3    Fischle, W.4    Brik, A.5
  • 45
    • 37349094422 scopus 로고    scopus 로고
    • Free-radical-based, specific desulfurization of cysteine: a powerful advance in the synthesis of polypeptides and glycopolypeptides
    • Wan Q., Danishefsky S.J. Free-radical-based, specific desulfurization of cysteine: a powerful advance in the synthesis of polypeptides and glycopolypeptides. Angew Chem Int Ed Engl 2007, 46:9248-9252.
    • (2007) Angew Chem Int Ed Engl , vol.46 , pp. 9248-9252
    • Wan, Q.1    Danishefsky, S.J.2
  • 46
    • 84879160099 scopus 로고    scopus 로고
    • Sequential peptide ligation by combining the Cys-Pro Ester (CPE) and thioester methods and its application to the synthesis of histone H3 containing a trimethyl lysine residue
    • Kawakami T., Akai Y., Fujimoto H., Kita C., Aoki Y., Konishi T., Waseda M., Takemura L., Aimoto S. Sequential peptide ligation by combining the Cys-Pro Ester (CPE) and thioester methods and its application to the synthesis of histone H3 containing a trimethyl lysine residue. Bull Chem Soc Jpn 2013, 86:690-697.
    • (2013) Bull Chem Soc Jpn , vol.86 , pp. 690-697
    • Kawakami, T.1    Akai, Y.2    Fujimoto, H.3    Kita, C.4    Aoki, Y.5    Konishi, T.6    Waseda, M.7    Takemura, L.8    Aimoto, S.9
  • 47
    • 84903762615 scopus 로고    scopus 로고
    • One-pot native chemical ligation of peptide hydrazides enables total synthesis of modified histones
    • Li J.B., Li Y.Y., He Q.Q., Li Y.M., Li H.T., Liu L. One-pot native chemical ligation of peptide hydrazides enables total synthesis of modified histones. Org Biomol Chem 2014, 12:5435-5441.
    • (2014) Org Biomol Chem , vol.12 , pp. 5435-5441
    • Li, J.B.1    Li, Y.Y.2    He, Q.Q.3    Li, Y.M.4    Li, H.T.5    Liu, L.6
  • 48
    • 70350533119 scopus 로고    scopus 로고
    • Split inteins as versatile tools for protein semisynthesis
    • Mootz H.D. Split inteins as versatile tools for protein semisynthesis. Chembiochem 2009, 10:2579-2589.
    • (2009) Chembiochem , vol.10 , pp. 2579-2589
    • Mootz, H.D.1
  • 49
    • 84907818379 scopus 로고    scopus 로고
    • Sortase-mediated ligations for the site-specific modification of proteins
    • Schmohl L., Schwarzer D. Sortase-mediated ligations for the site-specific modification of proteins. Curr Opin Chem Biol 2014, 22:122-128.
    • (2014) Curr Opin Chem Biol , vol.22 , pp. 122-128
    • Schmohl, L.1    Schwarzer, D.2
  • 50
    • 80155161989 scopus 로고    scopus 로고
    • Split inteins: nature's protein ligases
    • Shah N.H., Muir T.W. Split inteins: nature's protein ligases. Isr J Chem 2011, 51:854-861.
    • (2011) Isr J Chem , vol.51 , pp. 854-861
    • Shah, N.H.1    Muir, T.W.2
  • 51
    • 79956154315 scopus 로고    scopus 로고
    • Making and breaking peptide bonds: protein engineering using sortase
    • Popp M.W., Ploegh H.L. Making and breaking peptide bonds: protein engineering using sortase. Angew Chem Int Ed Engl 2011, 50:5024-5032.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 5024-5032
    • Popp, M.W.1    Ploegh, H.L.2
  • 53
    • 84859592838 scopus 로고    scopus 로고
    • In-cell fluorescence activation and labeling of proteins mediated by FRET-quenched split inteins
    • Borra R., Dong D., Elnagar A.Y., Woldemariam G.A., Camarero J.A. In-cell fluorescence activation and labeling of proteins mediated by FRET-quenched split inteins. J Am Chem Soc 2012, 134:6344-6353.
    • (2012) J Am Chem Soc , vol.134 , pp. 6344-6353
    • Borra, R.1    Dong, D.2    Elnagar, A.Y.3    Woldemariam, G.A.4    Camarero, J.A.5
  • 54
    • 0037774580 scopus 로고    scopus 로고
    • Protein semi-synthesis in living cells
    • Giriat I., Muir T.W. Protein semi-synthesis in living cells. J Am Chem Soc 2003, 125:7180-7181.
    • (2003) J Am Chem Soc , vol.125 , pp. 7180-7181
    • Giriat, I.1    Muir, T.W.2
  • 56
    • 32444434989 scopus 로고    scopus 로고
    • Histone H4-K16 acetylation controls chromatin structure and protein interactions
    • Shogren-Knaak M., Ishii H., Sun J.M., Pazin M.J., Davie J.R., Peterson C.L. Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 2006, 311:844-847.
    • (2006) Science , vol.311 , pp. 844-847
    • Shogren-Knaak, M.1    Ishii, H.2    Sun, J.M.3    Pazin, M.J.4    Davie, J.R.5    Peterson, C.L.6
  • 58
    • 84881612908 scopus 로고    scopus 로고
    • Systematic identification of proteins binding to chromatin-embedded ubiquitylated H2B reveals recruitment of SWI/SNF to regulate transcription
    • Shema-Yaacoby E., Nikolov M., Haj-Yahya M., Siman P., Allemand E., Yamaguchi Y., Muchardt C., Urlaub H., Brik A., Oren M., et al. Systematic identification of proteins binding to chromatin-embedded ubiquitylated H2B reveals recruitment of SWI/SNF to regulate transcription. Cell Rep 2013, 4:601-608.
    • (2013) Cell Rep , vol.4 , pp. 601-608
    • Shema-Yaacoby, E.1    Nikolov, M.2    Haj-Yahya, M.3    Siman, P.4    Allemand, E.5    Yamaguchi, Y.6    Muchardt, C.7    Urlaub, H.8    Brik, A.9    Oren, M.10
  • 60
    • 53549124960 scopus 로고    scopus 로고
    • The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure
    • Lu X., Simon M.D., Chodaparambil J.V., Hansen J.C., Shokat K.M., Luger K. The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure. Nat Struct Mol Biol 2008, 15:1122-1124.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 1122-1124
    • Lu, X.1    Simon, M.D.2    Chodaparambil, J.V.3    Hansen, J.C.4    Shokat, K.M.5    Luger, K.6
  • 61
    • 77958481159 scopus 로고    scopus 로고
    • Nucleosome-interacting proteins regulated by DNA and histone methylation
    • Bartke T., Vermeulen M., Xhemalce B., Robson S.C., Mann M., Kouzarides T. Nucleosome-interacting proteins regulated by DNA and histone methylation. Cell 2010, 143:470-484.
    • (2010) Cell , vol.143 , pp. 470-484
    • Bartke, T.1    Vermeulen, M.2    Xhemalce, B.3    Robson, S.C.4    Mann, M.5    Kouzarides, T.6
  • 62
    • 80555136767 scopus 로고    scopus 로고
    • Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns
    • 10.M110 005371
    • Nikolov M., Stutzer A., Mosch K., Krasauskas A., Soeroes S., Stark H., Urlaub H., Fischle W. Chromatin affinity purification and quantitative mass spectrometry defining the interactome of histone modification patterns. Mol Cell Proteom 2011, 10. M110 005371.
    • (2011) Mol Cell Proteom
    • Nikolov, M.1    Stutzer, A.2    Mosch, K.3    Krasauskas, A.4    Soeroes, S.5    Stark, H.6    Urlaub, H.7    Fischle, W.8
  • 64
    • 84866924932 scopus 로고    scopus 로고
    • Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1beta with the nucleosome
    • Munari F., Soeroes S., Zenn H.M., Schomburg A., Kost N., Schroder S., Klingberg R., Rezaei-Ghaleh N., Stutzer A., Gelato K.A., et al. Methylation of lysine 9 in histone H3 directs alternative modes of highly dynamic interaction of heterochromatin protein hHP1beta with the nucleosome. J Biol Chem 2012, 287:33756-33765.
    • (2012) J Biol Chem , vol.287 , pp. 33756-33765
    • Munari, F.1    Soeroes, S.2    Zenn, H.M.3    Schomburg, A.4    Kost, N.5    Schroder, S.6    Klingberg, R.7    Rezaei-Ghaleh, N.8    Stutzer, A.9    Gelato, K.A.10
  • 67
    • 84927722587 scopus 로고    scopus 로고
    • Targeted histone peptides: insights into the spatial regulation of the methyltransferase PRC2 by using a surrogate of heterotypic chromatin
    • Brown Z.Z., Muller M.M., Kong H.E., Lewis P.W., Muir T.W. Targeted histone peptides: insights into the spatial regulation of the methyltransferase PRC2 by using a surrogate of heterotypic chromatin. Angew Chem Int Ed Engl 2015, 54:6457-6461.
    • (2015) Angew Chem Int Ed Engl , vol.54 , pp. 6457-6461
    • Brown, Z.Z.1    Muller, M.M.2    Kong, H.E.3    Lewis, P.W.4    Muir, T.W.5
  • 70
    • 84928552345 scopus 로고    scopus 로고
    • Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins
    • David Y., Vila-Perello M., Verma S., Muir T.W. Chemical tagging and customizing of cellular chromatin states using ultrafast trans-splicing inteins. Nat Chem 2015, 7:394-402.
    • (2015) Nat Chem , vol.7 , pp. 394-402
    • David, Y.1    Vila-Perello, M.2    Verma, S.3    Muir, T.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.