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Volumn 84, Issue , 2015, Pages 265-290

Application of the protein semisynthesis strategy to the generation of modified chromatin

Author keywords

Epigenetics; Expressed protein ligation; Histone; Posttranslational modification

Indexed keywords

CYSTEINE; DNA; HISTONE; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; HYBRID PROTEIN; LYSINE; PENICILLAMINE; PEPTIDE FRAGMENT; PROTEIN; RECOMBINANT PROTEIN; SYNTHETIC PEPTIDE; UBIQUITIN; CHROMATIN; PEPTIDE;

EID: 84930726369     PISSN: 00664154     EISSN: 15454509     Source Type: Book Series    
DOI: 10.1146/annurev-biochem-060614-034429     Document Type: Review
Times cited : (59)

References (129)
  • 2
  • 3
  • 4
    • 84875424617 scopus 로고    scopus 로고
    • Emerging roles for chromatin as a signal integration and storage platform
    • Badeaux AI, Shi Y. 2013. Emerging roles for chromatin as a signal integration and storage platform. Nat. Rev. Mol. Cell Biol. 14:211-24
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 211-224
    • Badeaux, A.I.1    Shi, Y.2
  • 5
    • 80052942443 scopus 로고    scopus 로고
    • Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification
    • Tan M, Luo H, Lee S, Jin F, Yang JS, et al. 2011. Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146:1016-28
    • (2011) Cell , vol.146 , pp. 1016-1028
    • Tan, M.1    Luo, H.2    Lee, S.3    Jin, F.4    Yang, J.S.5
  • 6
    • 33847076849 scopus 로고    scopus 로고
    • Chromatin modifications and their function
    • Kouzarides T. 2007. Chromatin modifications and their function. Cell 128:693-705
    • (2007) Cell , vol.128 , pp. 693-705
    • Kouzarides, T.1
  • 7
    • 84878944044 scopus 로고    scopus 로고
    • Readout of epigenetic modifications
    • Patel DJ, Wang Z. 2013. Readout of epigenetic modifications. Annu. Rev. Biochem. 82:81-118
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 81-118
    • Patel, D.J.1    Wang, Z.2
  • 9
    • 9144268924 scopus 로고    scopus 로고
    • Partitioning and plasticity of repressive histone methylation states in mammalian chromatin
    • Peters AH, Kubicek S, Mechtler K, O'Sullivan RJ, Derijck AA, et al. 2003. Partitioning and plasticity of repressive histone methylation states in mammalian chromatin. Mol. Cell 12:1577-89
    • (2003) Mol. Cell , vol.12 , pp. 1577-1589
    • Peters, A.H.1    Kubicek, S.2    Mechtler, K.3    O'sullivan, R.J.4    Derijck, A.A.5
  • 11
    • 84866882318 scopus 로고    scopus 로고
    • Enhanced top-down characterization of histone post-translational modifications
    • Tian Z, Tolic N, Zhao R, Moore RJ, Hengel SM, et al. 2012. Enhanced top-down characterization of histone post-translational modifications. Genome Biol. 13:R86
    • (2012) Genome Biol. , vol.13 , pp. R86
    • Tian, Z.1    Tolic, N.2    Zhao, R.3    Moore, R.J.4    Hengel, S.M.5
  • 12
  • 13
    • 84860371870 scopus 로고    scopus 로고
    • Combinatorial complexity in chromatin structure and function: Revisiting the histone code
    • Rando OJ. 2012. Combinatorial complexity in chromatin structure and function: revisiting the histone code. Curr. Opin. Genet. Dev. 22:148-55
    • (2012) Curr. Opin. Genet. Dev. , vol.22 , pp. 148-155
    • Rando, O.J.1
  • 14
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl BD, Allis CD. 2000. The language of covalent histone modifications. Nature 403:41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 15
    • 44849100496 scopus 로고    scopus 로고
    • Chemically ubiquitylated histoneH2B stimulates hDot1L-mediated intranucleosomal methylation
    • McGinty RK, Kim J, Chatterjee C, Roeder RG, Muir TW. 2008. Chemically ubiquitylated histoneH2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 453:812-16
    • (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
  • 16
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun ZW, Allis CD. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418:104-8
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.W.1    Allis, C.D.2
  • 18
    • 79955583542 scopus 로고    scopus 로고
    • Mapping and analysis of chromatin state dynamics in nine human cell types
    • Ernst J, Kheradpour P, Mikkelsen TS, Shoresh N, Ward LD, et al. 2011. Mapping and analysis of chromatin state dynamics in nine human cell types. Nature 473:43-49
    • (2011) Nature , vol.473 , pp. 43-49
    • Ernst, J.1    Kheradpour, P.2    Mikkelsen, T.S.3    Shoresh, N.4    Ward, L.D.5
  • 19
  • 21
    • 84892747377 scopus 로고    scopus 로고
    • A cascade of histone modifications induces chromatin condensation in mitosis
    • Wilkins BJ, Rall NA, Ostwal Y, Kruitwagen T, Hiragami-Hamada K, et al. 2014. A cascade of histone modifications induces chromatin condensation in mitosis. Science 343:77-80
    • (2014) Science , vol.343 , pp. 77-80
    • Wilkins, B.J.1    Rall, N.A.2    Ostwal, Y.3    Kruitwagen, T.4    Hiragami-Hamada, K.5
  • 22
    • 23244448558 scopus 로고    scopus 로고
    • The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing
    • Zhou Y, Grummt I. 2005. The PHD finger/bromodomain of NoRC interacts with acetylated histone H4K16 and is sufficient for rDNA silencing. Curr. Biol. 15:1434-38
    • (2005) Curr. Biol. , vol.15 , pp. 1434-1438
    • Zhou, Y.1    Grummt, I.2
  • 23
    • 79957537645 scopus 로고    scopus 로고
    • Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions
    • Ruthenburg AJ, Li H, Milne TA, Dewell S, McGinty RK, et al. 2011. Recognition of a mononucleosomal histone modification pattern by BPTF via multivalent interactions. Cell 145:692-706
    • (2011) Cell , vol.145 , pp. 692-706
    • Ruthenburg, A.J.1    Li, H.2    Milne, T.A.3    Dewell, S.4    McGinty, R.K.5
  • 24
    • 84878924943 scopus 로고    scopus 로고
    • Scratching the (lateral) surface of chromatin regulation by histone modifications
    • Tropberger P, Schneider R. 2013. Scratching the (lateral) surface of chromatin regulation by histone modifications. Nat. Struct. Mol. Biol. 20:657-61
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 657-661
    • Tropberger, P.1    Schneider, R.2
  • 25
    • 84930733171 scopus 로고    scopus 로고
    • Novel types and sites of histone modifications emerge as players in the transcriptional regulation contest
    • In press
    • Kebede AF, Schneider R, Daujat S. 2014. Novel types and sites of histone modifications emerge as players in the transcriptional regulation contest. FEBS J. In press
    • (2014) FEBS J.
    • Kebede, A.F.1    Schneider, R.2    Daujat, S.3
  • 26
    • 0028235824 scopus 로고
    • Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution
    • Davies N, Lindsey GG. 1994. Histone H2B (and H2A) ubiquitination allows normal histone octamer and core particle reconstitution. Biochim. Biophys. Acta 1218:187-93
    • (1994) Biochim. Biophys. Acta , vol.1218 , pp. 187-193
    • Davies, N.1    Lindsey, G.G.2
  • 27
    • 0019332014 scopus 로고
    • Histone 2B can be modified by the attachment of ubiquitin
    • West MH, Bonner WM. 1980. Histone 2B can be modified by the attachment of ubiquitin. Nucleic Acids Res. 8:4671-80
    • (1980) Nucleic Acids Res. , vol.8 , pp. 4671-4680
    • West, M.H.1    Bonner, W.M.2
  • 28
    • 58249086425 scopus 로고    scopus 로고
    • Understanding the words of chromatin regulation
    • Wu JI, Lessard J, Crabtree GR. 2009. Understanding the words of chromatin regulation. Cell 136:200-6
    • (2009) Cell , vol.136 , pp. 200-206
    • Wu, J.I.1    Lessard, J.2    Crabtree, G.R.3
  • 29
    • 84905217856 scopus 로고    scopus 로고
    • Accelerated chromatin biochemistry using DNA-barcoded nucleosome libraries
    • Nguyen UT, Bittova L, Müller MM, Fierz B, David Y, et al. 2014. Accelerated chromatin biochemistry using DNA-barcoded nucleosome libraries. Nat. Methods 11:834-40
    • (2014) Nat. Methods , vol.11 , pp. 834-840
    • Nguyen, U.T.1    Bittova, L.2    Müller, M.M.3    Fierz, B.4    David, Y.5
  • 30
    • 84880534096 scopus 로고    scopus 로고
    • SET1 and p300 act synergistically, through coupled histone modifications, in transcriptional activation by p53
    • Tang Z, Chen WY, Shimada M, Nguyen UT, Kim J, et al. 2013. SET1 and p300 act synergistically, through coupled histone modifications, in transcriptional activation by p53. Cell 154:297-310
    • (2013) Cell , vol.154 , pp. 297-310
    • Tang, Z.1    Chen, W.Y.2    Shimada, M.3    Nguyen, U.T.4    Kim, J.5
  • 31
    • 84859836380 scopus 로고    scopus 로고
    • Chromatin as an expansive canvas for chemical biology
    • Fierz B, Muir TW. 2012. Chromatin as an expansive canvas for chemical biology. Nat. Chem. Biol. 8:417-27
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 417-427
    • Fierz, B.1    Muir, T.W.2
  • 32
    • 78751489882 scopus 로고    scopus 로고
    • Histone tails: Ideal motifs for probing epigenetics through chemical biology approaches
    • Voigt P, Reinberg D. 2011. Histone tails: ideal motifs for probing epigenetics through chemical biology approaches. ChemBioChem 12:236-52
    • (2011) ChemBioChem , vol.12 , pp. 236-252
    • Voigt, P.1    Reinberg, D.2
  • 33
    • 78751490445 scopus 로고    scopus 로고
    • Spreading chromatin into chemical biology
    • Allis CD, Muir TW. 2011. Spreading chromatin into chemical biology. ChemBioChem 12:264-79
    • (2011) ChemBioChem , vol.12 , pp. 264-279
    • Allis, C.D.1    Muir, T.W.2
  • 34
    • 40949099577 scopus 로고    scopus 로고
    • Genetically encoding Nε-acetyllysine in recombinant proteins
    • Neumann H, Peak-Chew SY, Chin JW. 2008. Genetically encoding Nε-acetyllysine in recombinant proteins. Nat. Chem. Biol. 4:232-34
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 232-234
    • Neumann, H.1    Peak-Chew, S.Y.2    Chin, J.W.3
  • 35
    • 84857451064 scopus 로고    scopus 로고
    • Designer proteins: Applications of genetic code expansion in cell biology
    • Davis L, Chin JW. 2012. Designer proteins: applications of genetic code expansion in cell biology. Nat. Rev. Mol. Cell Biol. 13:168-82
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 168-182
    • Davis, L.1    Chin, J.W.2
  • 36
    • 70349765673 scopus 로고    scopus 로고
    • A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation
    • Neumann H, Hancock SM, Buning R, Routh A, Chapman L, et al. 2009. A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation. Mol. Cell 36:153-63
    • (2009) Mol. Cell , vol.36 , pp. 153-163
    • Neumann, H.1    Hancock, S.M.2    Buning, R.3    Routh, A.4    Chapman, L.5
  • 37
    • 84870906814 scopus 로고    scopus 로고
    • Synthesis of ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyllysine containing histone H3 using the pyrrolysine system
    • Gattner MJ, Vrabel M, Carell T. 2013. Synthesis of ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyllysine containing histone H3 using the pyrrolysine system. Chem. Commun. 49:379-81
    • (2013) Chem. Commun. , vol.49 , pp. 379-381
    • Gattner, M.J.1    Vrabel, M.2    Carell, T.3
  • 39
    • 78049412986 scopus 로고    scopus 로고
    • Genetically directing ε-N, N-dimethyl-L-lysine in recombinant histones
    • Nguyen DP, Garcia Alai MM, Virdee S, Chin JW. 2010. Genetically directing ε-N, N-dimethyl-L-lysine in recombinant histones. Chem. Biol. 17:1072-76
    • (2010) Chem. Biol. , vol.17 , pp. 1072-1076
    • Nguyen, D.P.1    Garcia Alai, M.M.2    Virdee, S.3    Chin, J.W.4
  • 40
    • 80052165817 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli with phosphoserine
    • Park HS, Hohn MJ, Umehara T, Guo LT, Osborne EM, et al. 2011. Expanding the genetic code of Escherichia coli with phosphoserine. Science 333:1151-54
    • (2011) Science , vol.333 , pp. 1151-1154
    • Park, H.S.1    Hohn, M.J.2    Umehara, T.3    Guo, L.T.4    Osborne, E.M.5
  • 41
    • 70449571896 scopus 로고    scopus 로고
    • A pyrrolysine analogue for site-specific protein ubiquitination
    • Li X, Fekner T, Ottesen JJ, Chan MK. 2009. A pyrrolysine analogue for site-specific protein ubiquitination. Angew. Chem. Int. Ed. 48:9184-87
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 9184-9187
    • Li, X.1    Fekner, T.2    Ottesen, J.J.3    Chan, M.K.4
  • 42
    • 79960883438 scopus 로고    scopus 로고
    • Genetically encoded 1, 2-aminothiols facilitate rapid and site-specific protein labeling via a bio-orthogonal cyanobenzothiazole condensation
    • Nguyen DP, Elliott T, Holt M, Muir TW, Chin JW. 2011. Genetically encoded 1, 2-aminothiols facilitate rapid and site-specific protein labeling via a bio-orthogonal cyanobenzothiazole condensation. J. Am. Chem. Soc. 133:11418-21
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11418-11421
    • Nguyen, D.P.1    Elliott, T.2    Holt, M.3    Muir, T.W.4    Chin, J.W.5
  • 43
    • 33847386172 scopus 로고    scopus 로고
    • The site-specific installation of methyl-lysine analogs into recombinant histones
    • Simon MD, Chu F, Racki LR, de la Cruz CC, Burlingame AL, et al. 2007. The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 128:1003-12
    • (2007) Cell , vol.128 , pp. 1003-1012
    • Simon, M.D.1    Chu, F.2    Racki, L.R.3    De La Cruz, C.C.4    Burlingame, A.L.5
  • 44
    • 77949874828 scopus 로고    scopus 로고
    • Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation
    • Chatterjee C, McGinty RK, Fierz B, Muir TW. 2010. Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation. Nat. Chem. Biol. 6:267-69
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 267-269
    • Chatterjee, C.1    McGinty, R.K.2    Fierz, B.3    Muir, T.W.4
  • 47
    • 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. 2012. Quantitative assessment of protein interaction with methyl-lysine analogues by hybrid computational and experimental approaches. ACS Chem. Biol. 7:150-54
    • (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
  • 48
    • 0015984408 scopus 로고
    • Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei
    • Krieger DE, Levine R, Merrifield RB, Vidali G, Allfrey VG. 1974. Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei. J. Biol. Chem. 249:332-34
    • (1974) J. Biol. Chem. , vol.249 , pp. 332-334
    • Krieger, D.E.1    Levine, R.2    Merrifield, R.B.3    Vidali, G.4    Allfrey, V.G.5
  • 49
    • 84869087517 scopus 로고    scopus 로고
    • Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation
    • Rothbart SB, Krajewski K, Nady N, Tempel W, Xue S, et al. 2012. Association of UHRF1 with methylated H3K9 directs the maintenance of DNA methylation. Nat. Struct. Mol. Biol. 19:1155-60
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 1155-1160
    • Rothbart, S.B.1    Krajewski, K.2    Nady, N.3    Tempel, W.4    Xue, S.5
  • 51
    • 77949874334 scopus 로고    scopus 로고
    • Combinatorial profiling of chromatin binding modules reveals multisite discrimination
    • Garske AL, Oliver SS, Wagner EK, Musselman CA, LeRoy G, et al. 2010. Combinatorial profiling of chromatin binding modules reveals multisite discrimination. Nat. Chem. Biol. 6:283-90
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 283-290
    • Garske, A.L.1    Oliver, S.S.2    Wagner, E.K.3    Musselman, C.A.4    Leroy, G.5
  • 52
    • 48649109948 scopus 로고    scopus 로고
    • A combinatorial H4 tail library for exploring the histone code
    • Garske AL, Craciun G, Denu JM. 2008. A combinatorial H4 tail library for exploring the histone code. Biochemistry 47:8094-102
    • (2008) Biochemistry , vol.47 , pp. 8094-8102
    • Garske, A.L.1    Craciun, G.2    Denu, J.M.3
  • 53
    • 0034839973 scopus 로고    scopus 로고
    • Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin
    • Suka N, Suka Y, Carmen AA, Wu J, Grunstein M. 2001. Highly specific antibodies determine histone acetylation site usage in yeast heterochromatin and euchromatin. Mol. Cell 8:473-79
    • (2001) Mol. Cell , vol.8 , pp. 473-479
    • Suka, N.1    Suka, Y.2    Carmen, A.A.3    Wu, J.4    Grunstein, M.5
  • 54
    • 0024602986 scopus 로고
    • Specific antibodies reveal ordered and cell-cycle-related use of histone H4 acetylation sites in mammalian cells
    • Turner BM, Fellows G. 1989. Specific antibodies reveal ordered and cell-cycle-related use of histone H4 acetylation sites in mammalian cells. Eur. J. Biochem. 179:131-39
    • (1989) Eur. J. Biochem. , vol.179 , pp. 131-139
    • Turner, B.M.1    Fellows, G.2
  • 55
    • 37349110743 scopus 로고    scopus 로고
    • Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide
    • Smith BC, Denu JM. 2007. Mechanism-based inhibition of Sir2 deacetylases by thioacetyl-lysine peptide. Biochemistry 46:14478-86
    • (2007) Biochemistry , vol.46 , pp. 14478-14486
    • Smith, B.C.1    Denu, J.M.2
  • 56
    • 37549067781 scopus 로고    scopus 로고
    • Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases
    • Smith BC, Denu JM. 2007. Acetyl-lysine analog peptides as mechanistic probes of protein deacetylases. J. Biol. Chem. 282:37256-65
    • (2007) J. Biol. Chem. , vol.282 , pp. 37256-37265
    • Smith, B.C.1    Denu, J.M.2
  • 57
    • 0037086355 scopus 로고    scopus 로고
    • Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail
    • Jacobs SA, Khorasanizadeh S. 2002. Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science 295:2080-83
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 58
    • 33745839365 scopus 로고    scopus 로고
    • A PHDfinger ofNURF couples histone H3 lysine 4 trimethylation with chromatin remodelling
    • Wysocka J, Swigut T, Xiao H, Milne TA, Kwon SY, et al. 2006. A PHDfinger ofNURF couples histone H3 lysine 4 trimethylation with chromatin remodelling. Nature 442:86-90
    • (2006) Nature , vol.442 , pp. 86-90
    • Wysocka, J.1    Swigut, T.2    Xiao, H.3    Milne, T.A.4    Kwon, S.Y.5
  • 59
    • 20444417108 scopus 로고    scopus 로고
    • WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development
    • Wysocka J, Swigut T, Milne TA, Dou Y, Zhang X, et al. 2005. WDR5 associates with histone H3 methylated at K4 and is essential for H3 K4 methylation and vertebrate development. Cell 121:859-72
    • (2005) Cell , vol.121 , pp. 859-872
    • Wysocka, J.1    Swigut, T.2    Milne, T.A.3    Dou, Y.4    Zhang, X.5
  • 60
    • 69249217925 scopus 로고    scopus 로고
    • Epigenome microarray platform for proteome-wide dissection of chromatin-signaling networks
    • Bua DJ, Kuo AJ, Cheung P, Liu CL, Migliori V, et al. 2009. Epigenome microarray platform for proteome-wide dissection of chromatin-signaling networks. PLOS ONE 4:e6789
    • (2009) PLOS ONE , vol.4 , pp. e6789
    • Bua, D.J.1    Kuo, A.J.2    Cheung, P.3    Liu, C.L.4    Migliori, V.5
  • 61
    • 34047248383 scopus 로고    scopus 로고
    • Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine
    • Shi X, Kachirskaia I, Walter KL, Kuo JH, Lake A, et al. 2007. Proteome-wide analysis in Saccharomyces cerevisiae identifies several PHD fingers as novel direct and selective binding modules of histone H3 methylated at either lysine 4 or lysine 36. J. Biol. Chem. 282:2450-55
    • (2007) J. Biol. Chem. , vol.282 , pp. 2450-2455
    • Shi, X.1    Kachirskaia, I.2    Walter, K.L.3    Kuo, J.H.4    Lake, A.5
  • 62
    • 78149374556 scopus 로고    scopus 로고
    • Systematic identification of methyllysine-driven interactions for histone and nonhistone targets
    • Liu H, Galka M, Iberg A, Wang Z, Li L, et al. 2010. Systematic identification of methyllysine-driven interactions for histone and nonhistone targets. J. Proteome Res. 9:5827-36
    • (2010) J. Proteome Res. , vol.9 , pp. 5827-5836
    • Liu, H.1    Galka, M.2    Iberg, A.3    Wang, Z.4    Li, L.5
  • 64
    • 84878838423 scopus 로고    scopus 로고
    • Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation
    • Rothbart SB, Dickson BM, Ong MS, Krajewski K, Houliston S, et al. 2013. Multivalent histone engagement by the linked tandem Tudor and PHD domains of UHRF1 is required for the epigenetic inheritance of DNA methylation. Genes Dev. 27:1288-98
    • (2013) Genes Dev. , vol.27 , pp. 1288-1298
    • Rothbart, S.B.1    Dickson, B.M.2    Ong, M.S.3    Krajewski, K.4    Houliston, S.5
  • 65
    • 77749246186 scopus 로고    scopus 로고
    • Biochemical profiling of histone binding selectivity of the yeast bromodomain family
    • Zhang Q, Chakravarty S, Ghersi D, Zeng L, Plotnikov AN, et al. 2010. Biochemical profiling of histone binding selectivity of the yeast bromodomain family. PLOS ONE 5:e8903
    • (2010) PLOS ONE , vol.5 , pp. e8903
    • Zhang, Q.1    Chakravarty, S.2    Ghersi, D.3    Zeng, L.4    Plotnikov, A.N.5
  • 66
    • 84863800734 scopus 로고    scopus 로고
    • Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies
    • Rothbart SB, Lin S, Britton LM, Krajewski K, Keogh MC, et al. 2012. Poly-acetylated chromatin signatures are preferred epitopes for site-specific histone H4 acetyl antibodies. Sci. Rep. 2:489
    • (2012) Sci. Rep. , vol.2 , pp. 489
    • Rothbart, S.B.1    Lin, S.2    Britton, L.M.3    Krajewski, K.4    Keogh, M.C.5
  • 67
    • 34250721648 scopus 로고    scopus 로고
    • Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion
    • Hilpert K, Winkler DF, Hancock RE. 2007. Peptide arrays on cellulose support: SPOT synthesis, a time and cost efficient method for synthesis of large numbers of peptides in a parallel and addressable fashion. Nat. Protoc. 2:1333-49
    • (2007) Nat. Protoc , vol.2 , pp. 1333-1349
    • Hilpert, K.1    Winkler, D.F.2    Hancock, R.E.3
  • 68
    • 0023889559 scopus 로고
    • Chemical synthesis of peptides and proteins
    • Kent SB. 1988. Chemical synthesis of peptides and proteins. Annu. Rev. Biochem. 57:957-89
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 957-989
    • Kent, S.B.1
  • 69
    • 84875771630 scopus 로고    scopus 로고
    • The n-SET domain of Set1 regulates H2B ubiquitylation-dependent H3K4 methylation
    • Kim J, Kim JA, McGinty RK, Nguyen UT, Muir TW, et al. 2013. The n-SET domain of Set1 regulates H2B ubiquitylation-dependent H3K4 methylation. Mol. Cell 49:1121-33
    • (2013) Mol. Cell , vol.49 , pp. 1121-1133
    • Kim, J.1    Kim, J.A.2    McGinty, R.K.3    Nguyen, U.T.4    Muir, T.W.5
  • 70
    • 65249105512 scopus 로고    scopus 로고
    • RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells
    • Kim J, Guermah M, McGinty RK, Lee JS, Tang Z, et al. 2009. RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells. Cell 137:459-71
    • (2009) Cell , vol.137 , pp. 459-471
    • Kim, J.1    Guermah, M.2    McGinty, R.K.3    Lee, J.S.4    Tang, Z.5
  • 71
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: An enabling technology for the biophysical analysis of proteins
    • Muralidharan V, Muir TW. 2006. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat. Methods 3:429-38
    • (2006) Nat. Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2
  • 72
    • 0037548053 scopus 로고    scopus 로고
    • Semisynthesis of proteins by expressed protein ligation
    • Muir TW. 2003. Semisynthesis of proteins by expressed protein ligation. Annu. Rev. Biochem. 72:249-89
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 249-289
    • Muir, T.W.1
  • 73
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • Dawson PE, Kent SB. 2000. Synthesis of native proteins by chemical ligation. Annu. Rev. Biochem. 69:923-60
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 75
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • Muir TW, Sondhi D, Cole PA. 1998. Expressed protein ligation: a general method for protein engineering. PNAS 95:6705-10
    • (1998) PNAS , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 76
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing
    • Vila-Perelló M, Muir TW. 2010. Biological applications of protein splicing. Cell 143:191-200
    • (2010) Cell , vol.143 , pp. 191-200
    • Vila-Perelló, M.1    Muir, T.W.2
  • 77
  • 78
    • 0038047672 scopus 로고    scopus 로고
    • A native peptide ligation strategy for deciphering nucleosomal histone modifications
    • Shogren-Knaak MA, Fry CJ, Peterson CL. 2003. A native peptide ligation strategy for deciphering nucleosomal histone modifications. J. Biol. Chem. 278:15744-48
    • (2003) J. Biol. Chem. , vol.278 , pp. 15744-15748
    • Shogren-Knaak, M.A.1    Fry, C.J.2    Peterson, C.L.3
  • 79
    • 35548941098 scopus 로고    scopus 로고
    • Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms
    • Ferreira H, Flaus A, Owen-Hughes T. 2007. Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. J. Mol. Biol. 374:563-79
    • (2007) J. Mol. Biol. , vol.374 , pp. 563-579
    • Ferreira, H.1    Flaus, A.2    Owen-Hughes, T.3
  • 80
    • 0035977638 scopus 로고    scopus 로고
    • Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization
    • Yan LZ, Dawson PE. 2001. Synthesis of peptides and proteins without cysteine residues by native chemical ligation combined with desulfurization. J. Am. Chem. Soc. 123:526-33
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 526-533
    • Yan, L.Z.1    Dawson, P.E.2
  • 81
    • 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 SJ. 2007. Free-radical-based, specific desulfurization of cysteine: a powerful advance in the synthesis of polypeptides and glycopolypeptides. Angew. Chem. Int. Ed. 46:9248-52
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 9248-9252
    • Wan, Q.1    Danishefsky, S.J.2
  • 83
    • 84875002264 scopus 로고    scopus 로고
    • Peptide ligation-desulfurization chemistry at arginine
    • Malins LR, Cergol KM, Payne RJ. 2013. Peptide ligation-desulfurization chemistry at arginine. Chem- BioChem 14:559-63
    • (2013) Chem- BioChem , vol.14 , pp. 559-563
    • Malins, L.R.1    Cergol, K.M.2    Payne, R.J.3
  • 85
    • 77953463939 scopus 로고    scopus 로고
    • Protein synthesis assisted by native chemical ligation at leucine
    • Harpaz Z, Siman P, Kumar KS, Brik A. 2010. Protein synthesis assisted by native chemical ligation at leucine. ChemBioChem 11:1232-35
    • (2010) ChemBioChem , vol.11 , pp. 1232-1235
    • Harpaz, Z.1    Siman, P.2    Kumar, K.S.3    Brik, A.4
  • 86
    • 77649190705 scopus 로고    scopus 로고
    • A program for ligation at threonine sites: Application to the controlled total synthesis of glycopeptides
    • Chen J, Wang P, Zhu J, Wan Q, Danishefsky SJ. 2010. A program for ligation at threonine sites: application to the controlled total synthesis of glycopeptides. Tetrahedron 66:2277-83
    • (2010) Tetrahedron , vol.66 , pp. 2277-2283
    • Chen, J.1    Wang, P.2    Zhu, J.3    Wan, Q.4    Danishefsky, S.J.5
  • 88
    • 34548153495 scopus 로고    scopus 로고
    • Native chemical ligation at phenylalanine
    • Crich D, Banerjee A. 2007. Native chemical ligation at phenylalanine. J. Am. Chem. Soc. 129:10064-65
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 10064-10065
    • Crich, D.1    Banerjee, A.2
  • 89
    • 84870708220 scopus 로고    scopus 로고
    • Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis
    • Fierz B, Kilic S, Hieb AR, Luger K, Muir TW. 2012. Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. J. Am. Chem. Soc. 134:19548-51
    • (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
  • 90
    • 84880816458 scopus 로고    scopus 로고
    • Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34
    • Siman P, Karthikeyan SV, Nikolov M, Fischle W, Brik A. 2013. Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34. Angew. Chem. Int. Ed. 52:8059-63
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 8059-8063
    • Siman, P.1    Karthikeyan, S.V.2    Nikolov, M.3    Fischle, W.4    Brik, A.5
  • 92
    • 79551670677 scopus 로고    scopus 로고
    • 9-Fluorenylmethoxycarbonyl-based solid-phase synthesis of peptide α- Thioesters
    • Mende F, Seitz O. 2011. 9-Fluorenylmethoxycarbonyl-based solid-phase synthesis of peptide α- thioesters. Angew. Chem. Int. Ed. 50:1232-40
    • (2011) Angew. Chem. Int. Ed. , vol.50 , pp. 1232-1240
    • Mende, F.1    Seitz, O.2
  • 93
    • 0034023981 scopus 로고    scopus 로고
    • Peptide thioester preparation by Fmoc solid phase peptide synthesis for use in native chemical ligation
    • Clippingdale AB, Barrow CJ, Wade JD. 2000. Peptide thioester preparation by Fmoc solid phase peptide synthesis for use in native chemical ligation. J. Pept. Sci. 6:225-34
    • (2000) J. Pept. Sci. , vol.6 , pp. 225-234
    • Clippingdale, A.B.1    Barrow, C.J.2    Wade, J.D.3
  • 94
    • 12344274321 scopus 로고    scopus 로고
    • Native chemical ligation through in situ O to S acyl shift
    • Botti P, Villain M, Manganiello S, Gaertner H. 2004. Native chemical ligation through in situ O to S acyl shift. Org. Lett. 6:4861-64
    • (2004) Org. Lett , vol.6 , pp. 4861-4864
    • Botti, P.1    Villain, M.2    Manganiello, S.3    Gaertner, H.4
  • 95
    • 52449107990 scopus 로고    scopus 로고
    • An efficient Fmoc-SPPS approach for the generation of thioester peptide precursors for use in native chemical ligation
    • Blanco-Canosa JB, Dawson PE. 2008. An efficient Fmoc-SPPS approach for the generation of thioester peptide precursors for use in native chemical ligation. Angew. Chem. Int. Ed. 47:6851-55
    • (2008) Angew. Chem. Int. Ed. , vol.47 , pp. 6851-6855
    • Blanco-Canosa, J.B.1    Dawson, P.E.2
  • 97
    • 66349104608 scopus 로고    scopus 로고
    • Peptide ligation via the in-situ transformation of an amide into a thioester at a cysteine residue
    • Kawakami T, Aimoto S. 2009. Peptide ligation via the in-situ transformation of an amide into a thioester at a cysteine residue. Adv. Exp. Med. Biol. 611:117-18
    • (2009) Adv. Exp. Med. Biol. , vol.611 , pp. 117-118
    • Kawakami, T.1    Aimoto, S.2
  • 98
    • 70349390704 scopus 로고    scopus 로고
    • A semisynthetic strategy to generate phosphorylated and acetylated histone H2B
    • Chiang KP, Jensen MS, McGinty RK, Muir TW. 2009. A semisynthetic strategy to generate phosphorylated and acetylated histone H2B. ChemBioChem 10:2182-87
    • (2009) ChemBioChem , vol.10 , pp. 2182-2187
    • Chiang, K.P.1    Jensen, M.S.2    McGinty, R.K.3    Muir, T.W.4
  • 99
    • 84883815400 scopus 로고    scopus 로고
    • H3R42me2a is a histone modification with positive transcriptional effects
    • Casadio F, Lu X, Pollock SB, LeRoy G, Garcia BA, et al. 2013. H3R42me2a is a histone modification with positive transcriptional effects. PNAS 110:14894-99
    • (2013) PNAS , vol.110 , pp. 14894-14899
    • Casadio, F.1    Lu, X.2    Pollock, S.B.3    Leroy, G.4    Garcia, B.A.5
  • 100
    • 0142123130 scopus 로고    scopus 로고
    • Facile synthesis of site-specifically acetylated and methylated histone proteins: Reagents for evaluation of the histone code hypothesis
    • He S, Bauman D, Davis JS, Loyola A, Nishioka K, et al. 2003. Facile synthesis of site-specifically acetylated and methylated histone proteins: reagents for evaluation of the histone code hypothesis. PNAS 100:12033-38
    • (2003) PNAS , vol.100 , pp. 12033-12038
    • He, S.1    Bauman, D.2    Davis, J.S.3    Loyola, A.4    Nishioka, K.5
  • 101
    • 2442688260 scopus 로고    scopus 로고
    • Direct production of proteins with N-terminal cysteine for site-specific conjugation
    • Gentle IE, De Souza DP, Baca M. 2004. Direct production of proteins with N-terminal cysteine for site-specific conjugation. Bioconjug. Chem. 15:658-63
    • (2004) Bioconjug. Chem. , vol.15 , pp. 658-663
    • Gentle, I.E.1    De Souza, D.P.2    Baca, M.3
  • 102
    • 0034938752 scopus 로고    scopus 로고
    • Covalent capture: A new tool for the purification of synthetic and recombinant polypeptides
    • Villain M, Vizzavona J, Rose K. 2001. Covalent capture: a new tool for the purification of synthetic and recombinant polypeptides. Chem. Biol. 8:673-79
    • (2001) Chem. Biol. , vol.8 , pp. 673-679
    • Villain, M.1    Vizzavona, J.2    Rose, K.3
  • 103
    • 0030482408 scopus 로고    scopus 로고
    • The leucine zipper domain controls the orientation of AP-1 in the NFAT·AP-1·DNA complex
    • Erlanson DA, Chytil M, Verdine GL. 1996. The leucine zipper domain controls the orientation of AP-1 in the NFAT·AP-1·DNA complex. Chem. Biol. 3:981-91
    • (1996) Chem. Biol. , vol.3 , pp. 981-991
    • Erlanson, D.A.1    Chytil, M.2    Verdine, G.L.3
  • 105
    • 11844283271 scopus 로고    scopus 로고
    • A new strategy for glycoprotein synthesis: Ligation of synthetic glycopeptides with truncated proteins expressed in E. Coli as TEV protease cleavable fusion protein
    • Tolbert TJ, Franke D, Wong CH. 2005. A new strategy for glycoprotein synthesis: ligation of synthetic glycopeptides with truncated proteins expressed in E. Coli as TEV protease cleavable fusion protein. Bioorg. Med. Chem. 13:909-15
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 909-915
    • Tolbert, T.J.1    Franke, D.2    Wong, C.H.3
  • 106
    • 84891412552 scopus 로고    scopus 로고
    • Inteins: Nature's gift to protein chemists
    • Shah NH, Muir TW. 2014. Inteins: nature's gift to protein chemists. Chem. Sci. 5:446-61
    • (2014) Chem. Sci. , vol.5 , pp. 446-461
    • Shah, N.H.1    Muir, T.W.2
  • 107
    • 0344351815 scopus 로고    scopus 로고
    • Semisynthesis of cytotoxic proteins using a modified protein splicing element
    • Evans TC Jr, Benner J, Xu MQ. 1998. Semisynthesis of cytotoxic proteins using a modified protein splicing element. Protein Sci. 7:2256-64
    • (1998) Protein Sci. , vol.7 , pp. 2256-2264
    • Evans, T.C.1    Benner, J.2    Xu, M.Q.3
  • 108
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein
    • Southworth MW, Amaya K, Evans TC, Xu MQ, Perler FB. 1999. Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques 27:110-20
    • (1999) Biotechniques , vol.27 , pp. 110-120
    • Southworth, M.W.1    Amaya, K.2    Evans, T.C.3    Xu, M.Q.4    Perler, F.B.5
  • 109
    • 17744415288 scopus 로고    scopus 로고
    • Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element
    • Chong S, Mersha FB, Comb DG, Scott ME, Landry D, et al. 1997. Single-column purification of free recombinant proteins using a self-cleavable affinity tag derived from a protein splicing element. Gene 192:271-81
    • (1997) Gene , vol.192 , pp. 271-281
    • Chong, S.1    Mersha, F.B.2    Comb, D.G.3    Scott, M.E.4    Landry, D.5
  • 110
    • 84863893133 scopus 로고    scopus 로고
    • Ultrafast protein splicing is common among cyanobacterial split inteins: Implications for protein engineering
    • Shah NH, Dann GP, Vila-Perelló M, Liu Z, Muir TW. 2012. Ultrafast protein splicing is common among cyanobacterial split inteins: implications for protein engineering. J. Am. Chem. Soc. 134:11338-41
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11338-11341
    • Shah, N.H.1    Dann, G.P.2    Vila-Perelló, M.3    Liu, Z.4    Muir, T.W.5
  • 111
    • 60749092724 scopus 로고    scopus 로고
    • The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction
    • Zettler J, Schütz V, Mootz HD. 2009. The naturally split Npu DnaE intein exhibits an extraordinarily high rate in the protein trans-splicing reaction. FEBS Lett. 583:909-14
    • (2009) FEBS Lett , vol.583 , pp. 909-914
    • Zettler, J.1    Schütz, V.2    Mootz, H.D.3
  • 114
    • 33646728877 scopus 로고    scopus 로고
    • Insights into the mechanism and catalysis of the native chemical ligation reaction
    • Johnson EC, Kent SB. 2006. Insights into the mechanism and catalysis of the native chemical ligation reaction. J. Am. Chem. Soc. 128:6640-46
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6640-6646
    • Johnson, E.C.1    Kent, S.B.2
  • 115
    • 84893139184 scopus 로고    scopus 로고
    • Histone H3K27 trimethylation inhibits H3 binding and function of SET1-like H3K4 methyltransferase complexes
    • Kim DH, Tang Z, Shimada M, Fierz B, Houck-Loomis B, et al. 2013. Histone H3K27 trimethylation inhibits H3 binding and function of SET1-like H3K4 methyltransferase complexes. Mol. Cell. Biol. 33:4936-46
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 4936-4946
    • Kim, D.H.1    Tang, Z.2    Shimada, M.3    Fierz, B.4    Houck-Loomis, B.5
  • 117
    • 84863634911 scopus 로고    scopus 로고
    • Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2
    • Whitcomb SJ, Fierz B, McGinty RK, Holt M, Ito T, et al. 2012. Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2. J. Biol. Chem. 287:23718-25
    • (2012) J. Biol. Chem. , vol.287 , pp. 23718-23725
    • Whitcomb, S.J.1    Fierz, B.2    McGinty, R.K.3    Holt, M.4    Ito, T.5
  • 119
    • 73449105394 scopus 로고    scopus 로고
    • Structure-activity analysis of semisynthetic nucleosomes: Mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B
    • McGinty RK, Kohn M, Chatterjee C, Chiang KP, Pratt MR, Muir TW. 2009. Structure-activity analysis of semisynthetic nucleosomes: mechanistic insights into the stimulation of Dot1L by ubiquitylated histone H2B. ACS Chem. Biol. 4:958-68
    • (2009) ACS Chem. Biol. , vol.4 , pp. 958-968
    • McGinty, R.K.1    Kohn, M.2    Chatterjee, C.3    Chiang, K.P.4    Pratt, M.R.5    Muir, T.W.6
  • 120
    • 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, et al. 2013. Systematic identification of proteins binding to chromatin-embedded ubiquitylated H2B reveals recruitment of SWI/SNF to regulate transcription. Cell Rep. 4:601-8
    • (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
  • 122
    • 84904637945 scopus 로고    scopus 로고
    • Using chemistry to investigate the molecular consequences of protein ubiquitylation
    • Abeywardana T, Pratt MR. 2014. Using chemistry to investigate the molecular consequences of protein ubiquitylation. ChemBioChem 15:1547-54
    • (2014) ChemBioChem , vol.15 , pp. 1547-1554
    • Abeywardana, T.1    Pratt, M.R.2
  • 125
    • 79953719035 scopus 로고    scopus 로고
    • Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes
    • Shimko JC, North JA, Bruns AN, Poirier MG, Ottesen JJ. 2011. Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes. J. Mol. Biol. 408:187-204
    • (2011) J. Mol. Biol. , vol.408 , pp. 187-204
    • Shimko, J.C.1    North, J.A.2    Bruns, A.N.3    Poirier, M.G.4    Ottesen, J.J.5
  • 126
    • 69949176722 scopus 로고    scopus 로고
    • Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding
    • Manohar M, Mooney AM, North JA, Nakkula RJ, Picking JW, et al. 2009. Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding. J. Biol. Chem. 284:23312-21
    • (2009) J. Biol. Chem. , vol.284 , pp. 23312-23321
    • Manohar, M.1    Mooney, A.M.2    North, J.A.3    Nakkula, R.J.4    Picking, J.W.5
  • 128
    • 79953148278 scopus 로고    scopus 로고
    • The effects of histoneH4 tail acetylations on cation-induced chromatin folding and self-association
    • Allahverdi A, Yang R, Korolev N, Fan Y, Davey CA, et al. 2011. The effects of histoneH4 tail acetylations on cation-induced chromatin folding and self-association. Nucleic Acids Res. 39:1680-91
    • (2011) Nucleic Acids Res. , vol.39 , pp. 1680-1691
    • Allahverdi, A.1    Yang, R.2    Korolev, N.3    Fan, Y.4    Davey, C.A.5
  • 129
    • 79961217626 scopus 로고    scopus 로고
    • Histone fold modifications control nucleosome unwrapping and disassembly
    • Simon M, North JA, Shimko JC, Forties RA, Ferdinand MB, et al. 2011. Histone fold modifications control nucleosome unwrapping and disassembly. PNAS 108:12711-16
    • (2011) PNAS , vol.108 , pp. 12711-12716
    • Simon, M.1    North, J.A.2    Shimko, J.C.3    Forties, R.A.4    Ferdinand, M.B.5


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