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Volumn 27, Issue 2, 2005, Pages 164-175

Do protein motifs read the histone code?

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE; ENZYME; HISTONE; PROTEIN;

EID: 14344251024     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20176     Document Type: Review
Times cited : (205)

References (91)
  • 1
    • 0033119021 scopus 로고    scopus 로고
    • Chromatin-modifying and remodelling complexes
    • Konberg RD, Lorch Y. 1999. Chromatin-modifying and remodelling complexes. Curr Opin Genet Dev 9:148-151.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 148-151
    • Konberg, R.D.1    Lorch, Y.2
  • 2
    • 0024003456 scopus 로고
    • A direct link between core histone acetylation and transcriptionally active chromatin
    • Hebbes TR, Thorne AW, Crane-Robinson C. 1988. A direct link between core histone acetylation and transcriptionally active chromatin. EMBO J 7:1395-1402.
    • (1988) EMBO J , vol.7 , pp. 1395-1402
    • Hebbes, T.R.1    Thorne, A.W.2    Crane-Robinson, C.3
  • 3
    • 0034632829 scopus 로고    scopus 로고
    • Regulation of chromatin structure by site-specific histone H3 methyltransferases
    • Rea S, Eisenhaber F, O'Carroll D, Strahl BD, Sun ZW, et al. 2000. Regulation of chromatin structure by site-specific histone H3 methyltransferases. Nature 406:593-599.
    • (2000) Nature , vol.406 , pp. 593-599
    • Rea, S.1    Eisenhaber, F.2    O'Carroll, D.3    Strahl, B.D.4    Sun, Z.W.5
  • 4
    • 0034387004 scopus 로고    scopus 로고
    • 25 Years after the nucleosome model: Chromatin modifications
    • Wu J, Grunstein M. 2000. 25 years after the nucleosome model: Chromatin modifications. Trends Biochem Sci 25:619-623.
    • (2000) Trends Biochem Sci , vol.25 , pp. 619-623
    • Wu, J.1    Grunstein, M.2
  • 5
    • 0036532026 scopus 로고    scopus 로고
    • Histone modifications in transcriptional regulation
    • Berger S. 2002. Histone modifications in transcriptional regulation. Curr Opin Genet Dev 12:142-148.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 142-148
    • Berger, S.1
  • 6
    • 0033568312 scopus 로고    scopus 로고
    • ATP-dependent remodelling and acetylation as regulators of chromatin fluidity
    • Kingston RE, Narlikar GJ. 1999. ATP-dependent remodelling and acetylation as regulators of chromatin fluidity. Genes Dev 13:2339-2352.
    • (1999) Genes Dev , vol.13 , pp. 2339-2352
    • Kingston, R.E.1    Narlikar, G.J.2
  • 7
    • 0026566417 scopus 로고
    • Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei
    • Turner BM, Birley AJ, Lavender J. 1992. Histone H4 isoforms acetylated at specific lysine residues define individual chromosomes and chromatin domains in Drosophila polytene nuclei. Cell 69:375-384.
    • (1992) Cell , vol.69 , pp. 375-384
    • Turner, B.M.1    Birley, A.J.2    Lavender, J.3
  • 8
    • 0027525056 scopus 로고
    • Decoding the nucleosome
    • Turner BM. 1993. Decoding the nucleosome. Cell 75:5-8.
    • (1993) Cell , vol.75 , pp. 5-8
    • Turner, B.M.1
  • 9
    • 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
  • 10
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T, Allis CD. 2001. Translating the histone code. Science 293: 1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 12
    • 0036850325 scopus 로고    scopus 로고
    • Cellular memory and the histone code
    • Turner BM. 2002. Cellular memory and the histone code. Cell 111:285-291.
    • (2002) Cell , vol.111 , pp. 285-291
    • Turner, B.M.1
  • 13
    • 0035377556 scopus 로고    scopus 로고
    • Protein modules that manipulate histone tails for chromatin regulation
    • Marmorstein R. 2001. Protein modules that manipulate histone tails for chromatin regulation. Nature Rev 2:422-432.
    • (2001) Nature Rev , vol.2 , pp. 422-432
    • Marmorstein, R.1
  • 14
    • 0035282458 scopus 로고    scopus 로고
    • Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain
    • Bannister AJ, Zegerman P, Partridge JF, Miska EA, Thomas JO, et al. 2001. Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain. Nature 410:120-124.
    • (2001) Nature , vol.410 , pp. 120-124
    • Bannister, A.J.1    Zegerman, P.2    Partridge, J.F.3    Miska, E.A.4    Thomas, J.O.5
  • 15
    • 0035282573 scopus 로고    scopus 로고
    • Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins
    • Lachner M, O'Carroll D, Rea S, Mechtler K, Jenuwein T. 2001. Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins. Nature 410:116-120.
    • (2001) Nature , vol.410 , pp. 116-120
    • Lachner, M.1    O'Carroll, D.2    Rea, S.3    Mechtler, K.4    Jenuwein, T.5
  • 16
    • 0037167839 scopus 로고    scopus 로고
    • Histone methylation by Drosophila epigenetic regulator Ash1
    • Beisel C, Imhof A, Greene J, Kremmer E, Sauer F. 2002. Histone methylation by Drosophila epigenetic regulator Ash1. Nature 419:857-862.
    • (2002) Nature , vol.419 , pp. 857-862
    • Beisel, C.1    Imhof, A.2    Greene, J.3    Kremmer, E.4    Sauer, F.5
  • 17
    • 0037023681 scopus 로고    scopus 로고
    • Histone H3 lysine 4 methylation disrupts binding of nucleosome remodelling and deacetylase (NuRD) repressor complex
    • Zegerman P, Canas B, Pappin D, Kouzarides T. 2002. Histone H3 lysine 4 methylation disrupts binding of nucleosome remodelling and deacetylase (NuRD) repressor complex. J Biol Chem 227:11621-11624.
    • (2002) J Biol Chem , vol.227 , pp. 11621-11624
    • Zegerman, P.1    Canas, B.2    Pappin, D.3    Kouzarides, T.4
  • 18
    • 0037019333 scopus 로고    scopus 로고
    • Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
    • Sun Z-W, Allis CD. 2002. Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast. Nature 418:104-108.
    • (2002) Nature , vol.418 , pp. 104-108
    • Sun, Z.-W.1    Allis, C.D.2
  • 19
    • 0141929385 scopus 로고    scopus 로고
    • Binary switches and modification cassettes in histone biology and beyond
    • Fischle W, Wang Y, Alis CD. 2003. Binary switches and modification cassettes in histone biology and beyond. Nature 425:475-479.
    • (2003) Nature , vol.425 , pp. 475-479
    • Fischle, W.1    Wang, Y.2    Alis, C.D.3
  • 20
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • Agalioti T, Chen G, Thanos D. 2002. Deciphering the transcriptional histone acetylation code for a human gene. Cell 111:381-392.
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 21
    • 0037131523 scopus 로고    scopus 로고
    • Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites
    • Czermin B, Melfi R, McCabe D, Seitz V, Imhof A, et al. 2002. Drosophila enhancer of Zeste/ESC complexes have a histone H3 methyltransferase activity that marks chromosomal Polycomb sites. Cell 111:185-196.
    • (2002) Cell , vol.111 , pp. 185-196
    • Czermin, B.1    Melfi, R.2    McCabe, D.3    Seitz, V.4    Imhof, A.5
  • 22
    • 18644383738 scopus 로고    scopus 로고
    • Histone methyltransferase activity of a Drosophila polycomb group represor complex
    • Müller J, Hart CM, Francis NJ, Vargas ML, Sengupta A, et al. 2002. Histone methyltransferase activity of a Drosophila polycomb group represor complex. Cell 111:197-208.
    • (2002) Cell , vol.111 , pp. 197-208
    • Müller, J.1    Hart, C.M.2    Francis, N.J.3    Vargas, M.L.4    Sengupta, A.5
  • 24
    • 0026580006 scopus 로고
    • Brahma: A regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2
    • Tankum JW, Deuring R, Scott MP, Kissinger M, Pattatucci AM, et al. 1992. brahma: a regulator of Drosophila homeotic genes structurally related to the yeast transcriptional activator SNF2/SWI2. Cell 68:561-572.
    • (1992) Cell , vol.68 , pp. 561-572
    • Tankum, J.W.1    Deuring, R.2    Scott, M.P.3    Kissinger, M.4    Pattatucci, A.M.5
  • 25
    • 0035432099 scopus 로고    scopus 로고
    • The bromodomain: A regulator of ATP-dependent chromatin remodelling?
    • Horn PJ, Peterson CL. 2001. The bromodomain: a regulator of ATP-dependent chromatin remodelling? Front Biosci 6:01019-01023.
    • (2001) Front Biosci , vol.6 , pp. 1019-1023
    • Horn, P.J.1    Peterson, C.L.2
  • 26
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: An acetyl-lysine binding domain
    • Zheng L, Zhou M. 2002. Bromodomain: an acetyl-lysine binding domain. FEBS Lett 513:124-128.
    • (2002) FEBS Lett , vol.513 , pp. 124-128
    • Zheng, L.1    Zhou, M.2
  • 27
    • 0033519641 scopus 로고    scopus 로고
    • Structure and ligand of a histone acetyltransferase bromodomain
    • Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, et al. 1999. Structure and ligand of a histone acetyltransferase bromodomain. Nature 399: 491-496.
    • (1999) Nature , vol.399 , pp. 491-496
    • Dhalluin, C.1    Carlson, J.E.2    Zeng, L.3    He, C.4    Aggarwal, A.K.5
  • 28
    • 2942519726 scopus 로고    scopus 로고
    • Structures of proteins that create or recognize histone modifications
    • Bottomley M. 2004. Structures of proteins that create or recognize histone modifications. EMBO Rep 5:464-469.
    • (2004) EMBO Rep , vol.5 , pp. 464-469
    • Bottomley, M.1
  • 29
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE. 2000. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J Mol Biol 304:355-370.
    • (2000) J Mol Biol , vol.304 , pp. 355-370
    • Hudson, B.P.1    Martinez-Yamout, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 30
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p
    • Owen DJ, Ornaghi P, Yang J-C, Lowe N, Evans PR, et al. 2000. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase Gcn5p. EMBO J 19:6141-6149.
    • (2000) EMBO J , vol.19 , pp. 6141-6149
    • Owen, D.J.1    Ornaghi, P.2    Yang, J.-C.3    Lowe, N.4    Evans, P.R.5
  • 32
    • 17444386662 scopus 로고    scopus 로고
    • The bromodomain: A chromatin-targeting module?
    • Winston F, Allis CD. 1999. The bromodomain: a chromatin-targeting module? Nat Struct Biol 6:601-604.
    • (1999) Nat Struct Biol , vol.6 , pp. 601-604
    • Winston, F.1    Allis, C.D.2
  • 33
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan AH, Prochasson P, Neely KE, Galasinski SC, Chandy M, et al. 2002. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 111:369-379.
    • (2002) Cell , vol.111 , pp. 369-379
    • Hassan, A.H.1    Prochasson, P.2    Neely, K.E.3    Galasinski, S.C.4    Chandy, M.5
  • 34
    • 0034704815 scopus 로고    scopus 로고
    • The Gcn5 bromodomain coordinates nucleosome remodelling
    • Syntichaki P, Topalidou I, Thireos G. 2000. The Gcn5 bromodomain coordinates nucleosome remodelling. Nature 404:414-417.
    • (2000) Nature , vol.404 , pp. 414-417
    • Syntichaki, P.1    Topalidou, I.2    Thireos, G.3
  • 35
    • 0032566001 scopus 로고    scopus 로고
    • Isolation and characterisation of a Pufferfish MLL (mixed lineage leukaemia)-like gene (fMII) reveals evolutionary conservation in vertebrate genes related Drosophila tritorax
    • Caldas C, Myeong-Hee K, MacGregor A, Cain D, Aparicio S, et al. 1998. Isolation and characterisation of a Pufferfish MLL (mixed lineage leukaemia)-like gene (fMII) reveals evolutionary conservation in vertebrate genes related Drosophila tritorax. Oncogene 16:3233-3241.
    • (1998) Oncogene , vol.16 , pp. 3233-3241
    • Caldas, C.1    Myeong-Hee, K.2    MacGregor, A.3    Cain, D.4    Aparicio, S.5
  • 36
    • 1942535223 scopus 로고    scopus 로고
    • Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14
    • Kasten M, Szerlong H, Erdjument-Bromage H, Tempst P, Werner M, et al. 2004. Tandem bromodomains in the chromatin remodeler RSC recognize acetylated histone H3 Lys14. EMBO J 23:1348-1359.
    • (2004) EMBO J , vol.23 , pp. 1348-1359
    • Kasten, M.1    Szerlong, H.2    Erdjument-Bromage, H.3    Tempst, P.4    Werner, M.5
  • 37
    • 0026098009 scopus 로고
    • Polycomb protein shares a homologous domain with a heterochromatin- associated protein of Drosophila
    • Paro R, Hogness DS. 1991. Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila. Proc Natl Acad Sci USA 88:263-267.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 263-267
    • Paro, R.1    Hogness, D.S.2
  • 38
    • 0033964661 scopus 로고    scopus 로고
    • Mammalian chromodomain proteins: Their role in genome organisation and expression
    • Jones DO, Cowell IG, Singh PB. 2000. Mammalian chromodomain proteins: Their role in genome organisation and expression. Bioessays 22:124-137.
    • (2000) Bioessays , vol.22 , pp. 124-137
    • Jones, D.O.1    Cowell, I.G.2    Singh, P.B.3
  • 39
    • 0035812294 scopus 로고    scopus 로고
    • Molecular biology of the chromodomain: An ancient chromatin module comes of age
    • Eissenberg JC. 2001. Molecular biology of the chromodomain: an ancient chromatin module comes of age. Gene 275:19-29.
    • (2001) Gene , vol.275 , pp. 19-29
    • Eissenberg, J.C.1
  • 40
    • 0030922584 scopus 로고    scopus 로고
    • Structure of the chromatin binding (chromo) domain from mouse modifier protein 1
    • Ball LJ, Murzina NV, Broadhurst RW, Raine AR, Archer S, et al. 1997. Structure of the chromatin binding (chromo) domain from mouse modifier protein 1. EMBO J 16:2473-2481.
    • (1997) EMBO J , vol.16 , pp. 2473-2481
    • Ball, L.J.1    Murzina, N.V.2    Broadhurst, R.W.3    Raine, A.R.4    Archer, S.5
  • 41
    • 0037034911 scopus 로고    scopus 로고
    • Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9
    • Nielsen PR, Nietlispach D, Mott HR, Callaghan J, Bannister A, et al. 2002. Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9. Nature 416:103-107.
    • (2002) Nature , vol.416 , pp. 103-107
    • Nielsen, P.R.1    Nietlispach, D.2    Mott, H.R.3    Callaghan, J.4    Bannister, A.5
  • 42
    • 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 295:2080-2083.
    • (2002) Science , vol.295 , pp. 2080-2083
    • Jacobs, S.A.1    Khorasanizadeh, S.2
  • 43
    • 0026928683 scopus 로고
    • Position effect variegation and chromatin proteins
    • Reuter G, Spierer P. 1992. Position effect variegation and chromatin proteins. Bioessays 14:605-612.
    • (1992) Bioessays , vol.14 , pp. 605-612
    • Reuter, G.1    Spierer, P.2
  • 44
    • 0031559029 scopus 로고    scopus 로고
    • Self-association of chromo domain peptides
    • Cowell IG, Austin CA. 1997. Self-association of chromo domain peptides. Biochim Biophys Acta 2:198-206.
    • (1997) Biochim Biophys Acta , vol.2 , pp. 198-206
    • Cowell, I.G.1    Austin, C.A.2
  • 45
    • 0035815360 scopus 로고    scopus 로고
    • Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly
    • Nakayama J, Rice JC, Strahl BD, Allis CD, Grewal SI. 2001. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly. Science 292:110-113.
    • (2001) Science , vol.292 , pp. 110-113
    • Nakayama, J.1    Rice, J.C.2    Strahl, B.D.3    Allis, C.D.4    Grewal, S.I.5
  • 46
    • 0035903443 scopus 로고    scopus 로고
    • Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3
    • Jacobs SA, Taverna SD, Zhang Y, Briggs SD, Li J, et al. 2001. Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3. EMBO J 20:5232-5241.
    • (2001) EMBO J , vol.20 , pp. 5232-5241
    • Jacobs, S.A.1    Taverna, S.D.2    Zhang, Y.3    Briggs, S.D.4    Li, J.5
  • 47
    • 0037093537 scopus 로고    scopus 로고
    • The dMi-2 chromodomains are DNA binding modules important for ATP-dependent nucleosome binding and mobilization properties
    • Bouazone K, Mitterweger A, Langst G, Imhof A, Becker PB, et al. 2002. The dMi-2 chromodomains are DNA binding modules important for ATP-dependent nucleosome binding and mobilization properties. EMBO J 21:2430-2440.
    • (2002) EMBO J , vol.21 , pp. 2430-2440
    • Bouazone, K.1    Mitterweger, A.2    Langst, G.3    Imhof, A.4    Becker, P.B.5
  • 48
    • 0034699391 scopus 로고    scopus 로고
    • Chromodomains are protein-RNA interaction modules
    • Akhtar A, Zink D, Becker PB. 2000. Chromodomains are protein-RNA interaction modules. Nature 407:405-409.
    • (2000) Nature , vol.407 , pp. 405-409
    • Akhtar, A.1    Zink, D.2    Becker, P.B.3
  • 49
    • 0031917787 scopus 로고    scopus 로고
    • Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster
    • Gu W, Szauter P, Lecchesi JC. 1998. Targeting of MOF, a putative histone acetyl transferase, to the X chromosome of Drosophila melanogaster. Dev Genet 22:56-64.
    • (1998) Dev Genet , vol.22 , pp. 56-64
    • Gu, W.1    Szauter, P.2    Lecchesi, J.C.3
  • 50
    • 0033588309 scopus 로고    scopus 로고
    • Epigenetic spreading of the Drosophila dosage compensation complex from roX RNA genes into flanking chromatin
    • Kelley RL, Meiler VH, Gordadze PR, Roman G, Davis RL, et al. 1999. Epigenetic spreading of the Drosophila dosage compensation complex from roX RNA genes into flanking chromatin. Cell 98:513-522.
    • (1999) Cell , vol.98 , pp. 513-522
    • Kelley, R.L.1    Meiler, V.H.2    Gordadze, P.R.3    Roman, G.4    Davis, R.L.5
  • 51
    • 0034628634 scopus 로고    scopus 로고
    • Ordered assembly of the roX RNAs into MSL complexes on the dosage-compensated X chromosome in Drosophila
    • Meiler VH, Gordadze PR, Park Y, Chu X, Stuckenholz C, et al. 2000. Ordered assembly of the roX RNAs into MSL complexes on the dosage-compensated X chromosome in Drosophila. Curr Biol 10:136-143.
    • (2000) Curr Biol , vol.10 , pp. 136-143
    • Meiler, V.H.1    Gordadze, P.R.2    Park, Y.3    Chu, X.4    Stuckenholz, C.5
  • 52
    • 0036509836 scopus 로고    scopus 로고
    • Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component
    • Maison C, Bailly D, Peters AH, Quivy JP, Roche D, et al. 2002. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat Genet 30:329-334.
    • (2002) Nat Genet , vol.30 , pp. 329-334
    • Maison, C.1    Bailly, D.2    Peters, A.H.3    Quivy, J.P.4    Roche, D.5
  • 53
    • 0035019466 scopus 로고    scopus 로고
    • Heterochromatin formation in mammalian cells: Interaction between histones and HP1 proteins
    • Nielsen AL, Oulad-Abdelghani M, Ortiz JA, Remboustsika E, Chambon P, et al. 2001. Heterochromatin formation in mammalian cells: interaction between histones and HP1 proteins. Mol Cell 7:729-739.
    • (2001) Mol Cell , vol.7 , pp. 729-739
    • Nielsen, A.L.1    Oulad-Abdelghani, M.2    Ortiz, J.A.3    Remboustsika, E.4    Chambon, P.5
  • 54
    • 0345654336 scopus 로고    scopus 로고
    • Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factors-like genes
    • Bertram MJ, Berube NG, Hang-Swanson X, Ran Q, Leung JK, et al. 1999. Identification of a gene that reverses the immortal phenotype of a subset of cells and is a member of a novel family of transcription factors-like genes. Mol Cell Biol 19:1479-1485.
    • (1999) Mol Cell Biol , vol.19 , pp. 1479-1485
    • Bertram, M.J.1    Berube, N.G.2    Hang-Swanson, X.3    Ran, Q.4    Leung, J.K.5
  • 55
    • 0035925659 scopus 로고    scopus 로고
    • Conservation of the MORF4 related gene family: Identification of a new chromo domain subfamily and a novel protein motif
    • Bertam MJ, Pereira-Smith OM. 2001. Conservation of the MORF4 related gene family: identification of a new chromo domain subfamily and a novel protein motif. Gene 266:111-121.
    • (2001) Gene , vol.266 , pp. 111-121
    • Bertam, M.J.1    Pereira-Smith, O.M.2
  • 56
    • 0033988212 scopus 로고    scopus 로고
    • The drosophilae MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation
    • Smith ER, Pannuti A, Gu W, Steurnagel A, Cook RG, et al. 2000. The drosophilae MSL complex acetylates histone H4 at lysine 16, a chromatin modification linked to dosage compensation. Mol Cell Biol 20: 312-318.
    • (2000) Mol Cell Biol , vol.20 , pp. 312-318
    • Smith, E.R.1    Pannuti, A.2    Gu, W.3    Steurnagel, A.4    Cook, R.G.5
  • 57
    • 0035793642 scopus 로고    scopus 로고
    • The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcriptional regulation
    • Eisen A, Utley RT, Nourani A, Allard S, Schmidt P, et al. 2001. The yeast NuA4 and Drosophila MSL complexes contain homologous subunits important for transcriptional regulation. J Biol Chem 276:3484-3491.
    • (2001) J Biol Chem , vol.276 , pp. 3484-3491
    • Eisen, A.1    Utley, R.T.2    Nourani, A.3    Allard, S.4    Schmidt, P.5
  • 58
    • 0033567954 scopus 로고    scopus 로고
    • NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p
    • Allard S, Utley RT, Savard J, Clarke A, Grant P, et al. 1999. NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p. EMBO J 18: 5108-5119.
    • (1999) EMBO J , vol.18 , pp. 5108-5119
    • Allard, S.1    Utley, R.T.2    Savard, J.3    Clarke, A.4    Grant, P.5
  • 60
    • 0037173065 scopus 로고    scopus 로고
    • Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis
    • Lahn BT, Tang ZL, Zhou J, Barndt RJ, Parvinen M, et al. 2002. Previously uncharacterized histone acetyltransferases implicated in mammalian spermatogenesis. Proc Natl Acad Sci USA 99:8707-8712.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8707-8712
    • Lahn, B.T.1    Tang, Z.L.2    Zhou, J.3    Barndt, R.J.4    Parvinen, M.5
  • 61
    • 0242438555 scopus 로고    scopus 로고
    • Members of the CDY family have different expression patterns: CDY1 transcripts have the best correlation with complete spermatogenesis
    • Kleiman SE, Yogev L, Hauser R, Botchan A, Bar-Shira Maymon B, et al. 2003. Members of the CDY family have different expression patterns: CDY1 transcripts have the best correlation with complete spermatogenesis. Hum Genet 113:486-492.
    • (2003) Hum Genet , vol.113 , pp. 486-492
    • Kleiman, S.E.1    Yogev, L.2    Hauser, R.3    Botchan, A.4    Bar-Shira Maymon, B.5
  • 62
    • 0031865511 scopus 로고    scopus 로고
    • The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast
    • Ivanova AV, Bonaduce MJ, Ivanov SV, Klar SJS. 1998. The chromo and SET domains of the Clr4 protein are essential for silencing in fission yeast. Nat Genet 19:192-195.
    • (1998) Nat Genet , vol.19 , pp. 192-195
    • Ivanova, A.V.1    Bonaduce, M.J.2    Ivanov, S.V.3    Klar, S.J.S.4
  • 63
    • 0033598804 scopus 로고    scopus 로고
    • PICKLE is a CHD3 chromatin-remodeling factor that regulates the transition from embryonic to vegetative development in Arabidopsis
    • Ogas J, Kaufmann S, Henderson J, Somerville C. 1999. PICKLE is a CHD3 chromatin-remodeling factor that regulates the transition from embryonic to vegetative development in Arabidopsis. Proc Natl Acad Sci USA 96:13839-13844.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13839-13844
    • Ogas, J.1    Kaufmann, S.2    Henderson, J.3    Somerville, C.4
  • 64
    • 0032484081 scopus 로고    scopus 로고
    • DMi-2, a hunchback-interacting protein that functions in Polycomb repression
    • Kehle J, Beuchle D, treuheit S, Christen B, Kennison JA, et al. 1998. dMi-2, a hunchback-interacting protein that functions in Polycomb repression. Science 282:1897-1900.
    • (1998) Science , vol.282 , pp. 1897-1900
    • Kehle, J.1    Beuchle, D.2    Treuheit, S.3    Christen, B.4    Kennison, J.A.5
  • 65
    • 0034520843 scopus 로고    scopus 로고
    • The C. elegant Mi-2 chromatin-remodelling proteins function in vulval cell fate determination
    • Zelewsky TV, Palladino F, Brunschwig K, Tobler H, Hajnal A, et al. 2000. The C. elegant Mi-2 chromatin-remodelling proteins function in vulval cell fate determination. Development 127:5277-5284.
    • (2000) Development , vol.127 , pp. 5277-5284
    • Zelewsky, T.V.1    Palladino, F.2    Brunschwig, K.3    Tobler, H.4    Hajnal, A.5
  • 66
    • 0028788212 scopus 로고
    • The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation
    • Seelig HP, Moosbrugger I, Ehrfed H, Fink T, Renz M, et al. 1995. The major dermatomyositis specific Mi-2 autoantigen is a presumed helicase involved in transcriptional activation. Arthritis Rheum 38:389-1399.
    • (1995) Arthritis Rheum , vol.38 , pp. 389-1399
    • Seelig, H.P.1    Moosbrugger, I.2    Ehrfed, H.3    Fink, T.4    Renz, M.5
  • 67
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3 histone deacetylase complexes in development
    • Ahringer J. 2000. NuRD and SIN3 histone deacetylase complexes in development. Trends Genet 16:351-356.
    • (2000) Trends Genet , vol.16 , pp. 351-356
    • Ahringer, J.1
  • 69
    • 0036150409 scopus 로고    scopus 로고
    • CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like helicases
    • Schuster EF, Stoeger RJ. 2002. CHD5 defines a new subfamily of chromodomain-SWI2/SNF2-like helicases. Mamm Genome 13:117-119.
    • (2002) Mamm Genome , vol.13 , pp. 117-119
    • Schuster, E.F.1    Stoeger, R.J.2
  • 70
    • 85047671736 scopus 로고    scopus 로고
    • The SANT domain: A putative DNA-binding domain in the SWI_SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIB
    • Aasland R, Stewart AF, Gibson T. 1996. The SANT domain: a putative DNA-binding domain in the SWI_SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIB. Trends Biochem Sci 21:87-88.
    • (1996) Trends Biochem Sci , vol.21 , pp. 87-88
    • Aasland, R.1    Stewart, A.F.2    Gibson, T.3
  • 71
    • 0141922979 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI
    • Grüne T, Brzeski J, Eberharter A, Clapier CR, Corona DF, et al. 2003. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol Cell 12:449-460.
    • (2003) Mol Cell , vol.12 , pp. 449-460
    • Grüne, T.1    Brzeski, J.2    Eberharter, A.3    Clapier, C.R.4    Corona, D.F.5
  • 72
    • 0028138773 scopus 로고
    • Crystal structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices
    • Ogata K, Morikawa S, Nakamura H, Sekikawa A, Inoue T, et al. 1994. Crystal structure of a specific DNA complex of the Myb DNA-binding domain with cooperative recognition helices. Cell 79:639-648.
    • (1994) Cell , vol.79 , pp. 639-648
    • Ogata, K.1    Morikawa, S.2    Nakamura, H.3    Sekikawa, A.4    Inoue, T.5
  • 73
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer LA, Langer MR, Crowley KA, Tan S, Denu JM, et al. 2002. Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol Cell 4:935-942.
    • (2002) Mol Cell , vol.4 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5
  • 75
    • 0037925529 scopus 로고    scopus 로고
    • A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation
    • Yu J, Li Y, Ishizuka T, Guenther MG, Lazar MA. 2003. A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation. EMBO J 13:3403-3410.
    • (2003) EMBO J , vol.13 , pp. 3403-3410
    • Yu, J.1    Li, Y.2    Ishizuka, T.3    Guenther, M.G.4    Lazar, M.A.5
  • 76
    • 0035852637 scopus 로고    scopus 로고
    • CoRest is an integral component of the CoREST human histone deacetylase complex
    • You A, Tong JK, Grozinger CM, Schreiber SL. 2001. CoRest is an integral component of the CoREST human histone deacetylase complex. Proc Natl Acad Sci USA 98:1454-1458.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1454-1458
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 77
    • 0035929621 scopus 로고    scopus 로고
    • Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo
    • Fischle W, Dequiedt F, Fillion M. Hendzel MJ, Voelter W, et al. 2001. Human HDAC7 histone deacetylase activity is associated with HDAC3 in vivo. J Biol Chem 38:35826-35835.
    • (2001) J Biol Chem , vol.38 , pp. 35826-35835
    • Fischle, W.1    Dequiedt, F.2    Fillion, M.3    Hendzel, M.J.4    Voelter, W.5
  • 78
    • 0037040978 scopus 로고    scopus 로고
    • The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex
    • Sterner DE, Wang X, Bloom MH, Simon GM, Berger SL. 2002. The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. J Biol Chem 277:8178-8186.
    • (2002) J Biol Chem , vol.277 , pp. 8178-8186
    • Sterner, D.E.1    Wang, X.2    Bloom, M.H.3    Simon, G.M.4    Berger, S.L.5
  • 79
    • 18744373853 scopus 로고    scopus 로고
    • MLL targets SET domain methyltransferase activity to Hox gene promoters
    • Milne TA, Briggs SD, Brock HW, Martin ME, Gibbs D, et al. 2002. MLL targets SET domain methyltransferase activity to Hox gene promoters. Mol Cell 5:1107-1117.
    • (2002) Mol Cell , vol.5 , pp. 1107-1117
    • Milne, T.A.1    Briggs, S.D.2    Brock, H.W.3    Martin, M.E.4    Gibbs, D.5
  • 80
    • 0029645289 scopus 로고
    • Functional analysis of the chromo domain of HP1
    • Platero JS, Harnett T, Eissenberg JC. 1995. Functional analysis of the chromo domain of HP1. EMBO J 14:3977-3986
    • (1995) EMBO J , vol.14 , pp. 3977-3986
    • Platero, J.S.1    Harnett, T.2    Eissenberg, J.C.3
  • 81
  • 82
    • 1642564551 scopus 로고    scopus 로고
    • Selective recognition of acetylated histones by bromodomain proteins visualized in living cells
    • Kanno T, Kanno Y, Siegel RM, Jang MK, Lenardo MJ, et al. 2004. Selective recognition of acetylated histones by bromodomain proteins visualized in living cells. Mol Cell 1:33-43.
    • (2004) Mol Cell , vol.1 , pp. 33-43
    • Kanno, T.1    Kanno, Y.2    Siegel, R.M.3    Jang, M.K.4    Lenardo, M.J.5
  • 83
    • 0033617334 scopus 로고    scopus 로고
    • Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- And developmentally regulated promoter
    • Cosma MP, Tanaka T, Nasmyth K. 1999. Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell 97:299-311.
    • (1999) Cell , vol.97 , pp. 299-311
    • Cosma, M.P.1    Tanaka, T.2    Nasmyth, K.3
  • 84
    • 0033582943 scopus 로고    scopus 로고
    • Bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4
    • Ornaghi P, Ballario P, Lena AM, Gonzalez A, Filetici P. 1999. Bromodomain of Gcn5p interacts in vitro with specific residues in the N terminus of histone H4. J Mol Biol 1:1-7.
    • (1999) J Mol Biol , vol.1 , pp. 1-7
    • Ornaghi, P.1    Ballario, P.2    Lena, A.M.3    Gonzalez, A.4    Filetici, P.5
  • 85
    • 0037072661 scopus 로고    scopus 로고
    • Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi
    • Volpe TA, Kidner C, Hall IM, Teng G, Grewall SIS, et al. 2002. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 297:1833-1837.
    • (2002) Science , vol.297 , pp. 1833-1837
    • Volpe, T.A.1    Kidner, C.2    Hall, I.M.3    Teng, G.4    Grewall, S.I.S.5
  • 86
    • 0037154972 scopus 로고    scopus 로고
    • Epigenetic codes for heterochromatin formation and silencing: Rounding up the usual suspects
    • Richards EJ, Elgin SC. 2002. Epigenetic codes for heterochromatin formation and silencing: rounding up the usual suspects. Cell 108:489-500.
    • (2002) Cell , vol.108 , pp. 489-500
    • Richards, E.J.1    Elgin, S.C.2
  • 87
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A Program to Produce Both Detailed and Schematic Plots of Protein Structures. J Appl Cryst 24:946-950.
    • (1991) J Appl Cryst , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 88
    • 84856043672 scopus 로고
    • A mathematical theory of communication
    • Shannon CE. 1948. A mathematical theory of communication. Bell System Tech J 27:379-423.
    • (1948) Bell System Tech J , vol.27 , pp. 379-423
    • Shannon, C.E.1
  • 89
    • 0036681416 scopus 로고    scopus 로고
    • Scoring residue conservation
    • Valdar WS. 2002. Scoring residue conservation. Proteins 48:227-241.
    • (2002) Proteins , vol.48 , pp. 227-241
    • Valdar, W.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.