메뉴 건너뛰기




Volumn 618, Issue 1-2, 2007, Pages 3-17

Mechanisms of ATP dependent chromatin remodeling

Author keywords

Bulge propagation; CHD; Chromatin remodeling; INO80; ISWI; Nucleosome; Nucleosome spacing; SWI SNF; SWR1; Twist diffusion

Indexed keywords

ADENOSINE TRIPHOSPHATE; DNA BINDING PROTEIN; HISTONE;

EID: 34147102171     PISSN: 00275107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mrfmmm.2006.08.015     Document Type: Article
Times cited : (122)

References (152)
  • 1
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg R.D., and Lorch Y. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell 98 (1999) 285-294
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 2
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • Strahl B.D., and Allis C.D. The language of covalent histone modifications. Nature 403 (2000) 41-45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 3
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • Becker P.B., and Horz W. ATP-dependent nucleosome remodeling. Annu. Rev. Biochem. 71 (2002) 247-273
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 4
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., and Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389 (1997) 251-260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 5
    • 0026584855 scopus 로고
    • Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription
    • Peterson C.L., and Herskowitz I. Characterization of the yeast SWI1, SWI2, and SWI3 genes, which encode a global activator of transcription. Cell 68 (1992) 573-583
    • (1992) Cell , vol.68 , pp. 573-583
    • Peterson, C.L.1    Herskowitz, I.2
  • 6
    • 0034255298 scopus 로고    scopus 로고
    • The Swi/Snf family nucleosome-remodeling complexes and transcriptional control
    • Sudarsanam P., and Winston F. The Swi/Snf family nucleosome-remodeling complexes and transcriptional control. Trends Genet. 16 (2000) 345-351
    • (2000) Trends Genet. , vol.16 , pp. 345-351
    • Sudarsanam, P.1    Winston, F.2
  • 7
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman J.L., and Kingston R.E. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu. Rev. Biochem. 67 (1998) 545-579
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 8
    • 0031769946 scopus 로고    scopus 로고
    • Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins
    • Du J., Nasir I., Benton B.K., Kladde M.P., and Laurent B.C. Sth1p, a Saccharomyces cerevisiae Snf2p/Swi2p homolog, is an essential ATPase in RSC and differs from Snf/Swi in its interactions with histones and chromatin-associated proteins. Genetics 150 (1998) 987-1005
    • (1998) Genetics , vol.150 , pp. 987-1005
    • Du, J.1    Nasir, I.2    Benton, B.K.3    Kladde, M.P.4    Laurent, B.C.5
  • 9
    • 0033231625 scopus 로고    scopus 로고
    • Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains
    • Cairns B.R., Schlichter A., Erdjument-Bromage H., Tempst P., Kornberg R.D., and Winston F. Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains. Mol. Cell 4 (1999) 715-723
    • (1999) Mol. Cell , vol.4 , pp. 715-723
    • Cairns, B.R.1    Schlichter, A.2    Erdjument-Bromage, H.3    Tempst, P.4    Kornberg, R.D.5    Winston, F.6
  • 10
    • 14544308853 scopus 로고    scopus 로고
    • Composition and functional specificity of SWI2/SNF2 class chromatin remodeling complexes
    • Mohrmann L., and Verrijzer C.P. Composition and functional specificity of SWI2/SNF2 class chromatin remodeling complexes. Biochim. Biophys. Acta 1681 (2005) 59-73
    • (2005) Biochim. Biophys. Acta , vol.1681 , pp. 59-73
    • Mohrmann, L.1    Verrijzer, C.P.2
  • 11
    • 0037238113 scopus 로고    scopus 로고
    • The SWI/SNF family of ATP-dependent chromatin remodelers: similar mechanisms for diverse functions
    • Wang W. The SWI/SNF family of ATP-dependent chromatin remodelers: similar mechanisms for diverse functions. Curr. Top. Microbiol. Immunol. 274 (2003) 143-169
    • (2003) Curr. Top. Microbiol. Immunol. , vol.274 , pp. 143-169
    • Wang, W.1
  • 12
    • 0034697973 scopus 로고    scopus 로고
    • BRCA1 is associated with a human SWI/SNF-related complex: linking chromatin remodeling to breast cancer
    • Bochar D.A., Wang L., Beniya H., Kinev A., Xue Y., Lane W.S., Wang W., Kashanchi F., and Shiekhattar R. BRCA1 is associated with a human SWI/SNF-related complex: linking chromatin remodeling to breast cancer. Cell 102 (2000) 257-265
    • (2000) Cell , vol.102 , pp. 257-265
    • Bochar, D.A.1    Wang, L.2    Beniya, H.3    Kinev, A.4    Xue, Y.5    Lane, W.S.6    Wang, W.7    Kashanchi, F.8    Shiekhattar, R.9
  • 13
    • 0035199533 scopus 로고    scopus 로고
    • Characterization of SWI/SNF protein expression in human breast cancer cell lines and other malignancies
    • Decristofaro M.F., Betz B.L., Rorie C.J., Reisman D.N., Wang W., and Weissman B.E. Characterization of SWI/SNF protein expression in human breast cancer cell lines and other malignancies. J. Cell Physiol. 186 (2001) 136-145
    • (2001) J. Cell Physiol. , vol.186 , pp. 136-145
    • Decristofaro, M.F.1    Betz, B.L.2    Rorie, C.J.3    Reisman, D.N.4    Wang, W.5    Weissman, B.E.6
  • 14
    • 0035281938 scopus 로고    scopus 로고
    • Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes
    • Sif S., Saurin A.J., Imbalzano A.N., and Kingston R.E. Purification and characterization of mSin3A-containing Brg1 and hBrm chromatin remodeling complexes. Genes Dev. 15 (2001) 603-618
    • (2001) Genes Dev. , vol.15 , pp. 603-618
    • Sif, S.1    Saurin, A.J.2    Imbalzano, A.N.3    Kingston, R.E.4
  • 15
    • 0142123234 scopus 로고    scopus 로고
    • mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad
    • Pal S., Yun R., Datta A., Lacomis L., Erdjument-Bromage H., Kumar J., Tempst P., and Sif S. mSin3A/histone deacetylase 2- and PRMT5-containing Brg1 complex is involved in transcriptional repression of the Myc target gene cad. Mol. Cell. Biol. 23 (2003) 7475-7487
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7475-7487
    • Pal, S.1    Yun, R.2    Datta, A.3    Lacomis, L.4    Erdjument-Bromage, H.5    Kumar, J.6    Tempst, P.7    Sif, S.8
  • 16
    • 6344222803 scopus 로고    scopus 로고
    • Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes
    • Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., and Sif S. Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and negatively regulates expression of ST7 and NM23 tumor suppressor genes. Mol. Cell. Biol. 24 (2004) 9630-9645
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9630-9645
    • Pal, S.1    Vishwanath, S.N.2    Erdjument-Bromage, H.3    Tempst, P.4    Sif, S.5
  • 17
    • 10644231814 scopus 로고    scopus 로고
    • Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits
    • Lee K.K., Prochasson P., Florens L., Swanson S.K., Washburn M.P., and Workman J.L. Proteomic analysis of chromatin-modifying complexes in Saccharomyces cerevisiae identifies novel subunits. Biochem. Soc. Trans. 32 (2004) 899-903
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 899-903
    • Lee, K.K.1    Prochasson, P.2    Florens, L.3    Swanson, S.K.4    Washburn, M.P.5    Workman, J.L.6
  • 20
    • 0035134330 scopus 로고    scopus 로고
    • Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation
    • de la Serna I.L., Carlson K.A., and Imbalzano A.N. Mammalian SWI/SNF complexes promote MyoD-mediated muscle differentiation. Nat. Genet. 27 (2001) 187-190
    • (2001) Nat. Genet. , vol.27 , pp. 187-190
    • de la Serna, I.L.1    Carlson, K.A.2    Imbalzano, A.N.3
  • 21
    • 32544460284 scopus 로고    scopus 로고
    • Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase Brg1
    • Ohkawa Y., Marfella C.G., and Imbalzano A.N. Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF ATPase Brg1. EMBO J. 25 (2006) 490-501
    • (2006) EMBO J. , vol.25 , pp. 490-501
    • Ohkawa, Y.1    Marfella, C.G.2    Imbalzano, A.N.3
  • 26
    • 22944448744 scopus 로고    scopus 로고
    • Geminin regulates neuronal differentiation by antagonizing Brg1 activity
    • Seo S., Herr A., Lim J.W., Richardson G.A., Richardson H., and Kroll K.L. Geminin regulates neuronal differentiation by antagonizing Brg1 activity. Genes Dev. 19 (2005) 1723-1734
    • (2005) Genes Dev. , vol.19 , pp. 1723-1734
    • Seo, S.1    Herr, A.2    Lim, J.W.3    Richardson, G.A.4    Richardson, H.5    Kroll, K.L.6
  • 28
    • 0036791792 scopus 로고    scopus 로고
    • Identification of a polymorphic, neuron-specific chromatin remodeling complex
    • Olave I., Wang W., Xue Y., Kuo A., and Crabtree G.R. Identification of a polymorphic, neuron-specific chromatin remodeling complex. Genes Dev. 16 (2002) 2509-2517
    • (2002) Genes Dev. , vol.16 , pp. 2509-2517
    • Olave, I.1    Wang, W.2    Xue, Y.3    Kuo, A.4    Crabtree, G.R.5
  • 30
    • 2442691703 scopus 로고    scopus 로고
    • Temporal recruitment of transcription factors and SWI/SNF chromatin-remodeling enzymes during adipogenic induction of the peroxisome proliferator-activated receptor gamma nuclear hormone receptor
    • Salma N., Xiao H., Mueller E., and Imbalzano A.N. Temporal recruitment of transcription factors and SWI/SNF chromatin-remodeling enzymes during adipogenic induction of the peroxisome proliferator-activated receptor gamma nuclear hormone receptor. Mol. Cell. Biol. 24 (2004) 4651-4663
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4651-4663
    • Salma, N.1    Xiao, H.2    Mueller, E.3    Imbalzano, A.N.4
  • 31
    • 33645287706 scopus 로고    scopus 로고
    • Mammalian chromatin remodeling complex SWI/SNF is essential for enhanced expression of the albumin gene during liver development
    • Inayoshi Y., Miyake K., Machida Y., Kaneoka H., Terajima M., Dohda T., Takahashi M., and Iijima S. Mammalian chromatin remodeling complex SWI/SNF is essential for enhanced expression of the albumin gene during liver development. J. Biochem. (Tokyo) 139 (2006) 177-188
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 177-188
    • Inayoshi, Y.1    Miyake, K.2    Machida, Y.3    Kaneoka, H.4    Terajima, M.5    Dohda, T.6    Takahashi, M.7    Iijima, S.8
  • 32
    • 15244341696 scopus 로고    scopus 로고
    • Multiple interactions between BRG1 and MHC class II promoter binding proteins
    • Mudhasani R., and Fontes J.D. Multiple interactions between BRG1 and MHC class II promoter binding proteins. Mol. Immunol. 42 (2005) 673-682
    • (2005) Mol. Immunol. , vol.42 , pp. 673-682
    • Mudhasani, R.1    Fontes, J.D.2
  • 33
    • 0348223783 scopus 로고    scopus 로고
    • The role of Brg1, a catalytic subunit of mammalian chromatin-remodeling complexes, in T cell development
    • Gebuhr T.C., Kovalev G.I., Bultman S., Godfrey V., Su L., and Magnuson T. The role of Brg1, a catalytic subunit of mammalian chromatin-remodeling complexes, in T cell development. J. Exp. Med. 198 (2003) 1937-1949
    • (2003) J. Exp. Med. , vol.198 , pp. 1937-1949
    • Gebuhr, T.C.1    Kovalev, G.I.2    Bultman, S.3    Godfrey, V.4    Su, L.5    Magnuson, T.6
  • 34
    • 23044479628 scopus 로고    scopus 로고
    • Distinct roles for the RSC and Swi/Snf ATP-dependent chromatin remodelers in DNA double-strand break repair
    • Chai B., Huang J., Cairns B.R., and Laurent B.C. Distinct roles for the RSC and Swi/Snf ATP-dependent chromatin remodelers in DNA double-strand break repair. Genes Dev. 19 (2005) 1656-1661
    • (2005) Genes Dev. , vol.19 , pp. 1656-1661
    • Chai, B.1    Huang, J.2    Cairns, B.R.3    Laurent, B.C.4
  • 35
    • 29244467720 scopus 로고    scopus 로고
    • ATP-dependent chromatin-remodeling complexes in DNA double-strand break repair: remodeling, pairing and (re)pairing
    • Huang J., Liang B., Qiu J., and Laurent B.C. ATP-dependent chromatin-remodeling complexes in DNA double-strand break repair: remodeling, pairing and (re)pairing. Cell Cycle 4 (2005) 1713-1715
    • (2005) Cell Cycle , vol.4 , pp. 1713-1715
    • Huang, J.1    Liang, B.2    Qiu, J.3    Laurent, B.C.4
  • 36
    • 13944262860 scopus 로고    scopus 로고
    • A Role for the RSC chromatin remodeler in regulating cohesion of sister chromatid arms
    • Huang J., and Laurent B.C. A Role for the RSC chromatin remodeler in regulating cohesion of sister chromatid arms. Cell Cycle 3 (2004) 973-975
    • (2004) Cell Cycle , vol.3 , pp. 973-975
    • Huang, J.1    Laurent, B.C.2
  • 37
    • 1642266517 scopus 로고    scopus 로고
    • The RSC nucleosome-remodeling complex is required for Cohesin's association with chromosome arms
    • Huang J., Hsu J.M., and Laurent B.C. The RSC nucleosome-remodeling complex is required for Cohesin's association with chromosome arms. Mol. Cell 13 (2004) 739-750
    • (2004) Mol. Cell , vol.13 , pp. 739-750
    • Huang, J.1    Hsu, J.M.2    Laurent, B.C.3
  • 38
    • 29144519877 scopus 로고    scopus 로고
    • Targeting of cohesin by transcriptionally silent chromatin
    • Chang C.R., Wu C.S., Hom Y., and Gartenberg M.R. Targeting of cohesin by transcriptionally silent chromatin. Genes Dev. 19 (2005) 3031-3042
    • (2005) Genes Dev. , vol.19 , pp. 3031-3042
    • Chang, C.R.1    Wu, C.S.2    Hom, Y.3    Gartenberg, M.R.4
  • 39
    • 30044441988 scopus 로고    scopus 로고
    • The human SWI/SNF subunit Brm is a regulator of alternative splicing
    • Batsche E., Yaniv M., and Muchardt C. The human SWI/SNF subunit Brm is a regulator of alternative splicing. Nat. Struct. Mol. Biol. 13 (2006) 22-29
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 22-29
    • Batsche, E.1    Yaniv, M.2    Muchardt, C.3
  • 40
    • 4444257692 scopus 로고    scopus 로고
    • The Swi/Snf chromatin remodeling complex is required for ribosomal DNA and telomeric silencing in Saccharomyces cerevisiae
    • Dror V., and Winston F. The Swi/Snf chromatin remodeling complex is required for ribosomal DNA and telomeric silencing in Saccharomyces cerevisiae. Mol. Cell. Biol. 24 (2004) 8227-8235
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8227-8235
    • Dror, V.1    Winston, F.2
  • 42
    • 18844457346 scopus 로고    scopus 로고
    • X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA
    • Durr H., Korner C., Muller M., Hickmann V., and Hopfner K.P. X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA. Cell 121 (2005) 363-373
    • (2005) Cell , vol.121 , pp. 363-373
    • Durr, H.1    Korner, C.2    Muller, M.3    Hickmann, V.4    Hopfner, K.P.5
  • 43
  • 44
    • 0034387879 scopus 로고    scopus 로고
    • Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain
    • Hudson B.P., Martinez-Yamout M.A., Dyson H.J., and Wright P.E. Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. J. Mol. Biol. 304 (2000) 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
  • 45
    • 0034717183 scopus 로고    scopus 로고
    • Structure and function of a human TAFII250 double bromodomain module
    • Jacobson R.H., Ladurner A.G., King D.S., and Tjian R. Structure and function of a human TAFII250 double bromodomain module. Science 288 (2000) 1422-1425
    • (2000) Science , vol.288 , pp. 1422-1425
    • Jacobson, R.H.1    Ladurner, A.G.2    King, D.S.3    Tjian, R.4
  • 46
    • 0035845006 scopus 로고    scopus 로고
    • Structure and function of bromodomains in chromatin-regulating complexes
    • Marmorstein R., and Berger S.L. Structure and function of bromodomains in chromatin-regulating complexes. Gene 272 (2001) 1-9
    • (2001) Gene , vol.272 , pp. 1-9
    • Marmorstein, R.1    Berger, S.L.2
  • 47
    • 0034669210 scopus 로고    scopus 로고
    • The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p
    • Owen D.J., Ornaghi P., Yang J.C., Lowe N., Evans P.R., Ballario P., Neuhaus D., Filetici P., and Travers A.A. The structural basis for the recognition of acetylated histone H4 by the bromodomain of histone acetyltransferase gcn5p. EMBO J. 19 (2000) 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    Ballario, P.6    Neuhaus, D.7    Filetici, P.8    Travers, A.A.9
  • 48
    • 0037138363 scopus 로고    scopus 로고
    • Bromodomain: an acetyl-lysine binding domain
    • Zeng L., and Zhou M.M. Bromodomain: an acetyl-lysine binding domain. FEBS Lett. 513 (2002) 124-128
    • (2002) FEBS Lett. , vol.513 , pp. 124-128
    • Zeng, L.1    Zhou, M.M.2
  • 49
    • 0036847620 scopus 로고    scopus 로고
    • Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes
    • Hassan A.H., Prochasson P., Neely K.E., Galasinski S.C., Chandy M., Carrozza M.J., and Workman J.L. Function and selectivity of bromodomains in anchoring chromatin-modifying complexes to promoter nucleosomes. Cell 111 (2002) 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    Carrozza, M.J.6    Workman, J.L.7
  • 50
    • 0037291760 scopus 로고    scopus 로고
    • Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries
    • Ladurner A.G., Inouye C., Jain R., and Tjian R. Bromodomains mediate an acetyl-histone encoded antisilencing function at heterochromatin boundaries. Mol. Cell 11 (2003) 365-376
    • (2003) Mol. Cell , vol.11 , pp. 365-376
    • Ladurner, A.G.1    Inouye, C.2    Jain, R.3    Tjian, R.4
  • 51
    • 0033572948 scopus 로고    scopus 로고
    • Osa associates with the Brahma chromatin remodeling complex and promotes the activation of some target genes
    • Collins R.T., Furukawa T., Tanese N., and Treisman J.E. Osa associates with the Brahma chromatin remodeling complex and promotes the activation of some target genes. EMBO J. 18 (1999) 7029-7040
    • (1999) EMBO J. , vol.18 , pp. 7029-7040
    • Collins, R.T.1    Furukawa, T.2    Tanese, N.3    Treisman, J.E.4
  • 52
    • 13744250058 scopus 로고    scopus 로고
    • DNA-binding properties of ARID family proteins
    • Patsialou A., Wilsker D., and Moran E. DNA-binding properties of ARID family proteins. Nucleic Acids Res. 33 (2005) 66-80
    • (2005) Nucleic Acids Res. , vol.33 , pp. 66-80
    • Patsialou, A.1    Wilsker, D.2    Moran, E.3
  • 53
    • 0036250668 scopus 로고    scopus 로고
    • ARID proteins: a diverse family of DNA binding proteins implicated in the control of cell growth, differentiation, and development
    • Wilsker D., Patsialou A., Dallas P.B., and Moran E. ARID proteins: a diverse family of DNA binding proteins implicated in the control of cell growth, differentiation, and development. Cell Growth Differ. 13 (2002) 95-106
    • (2002) Cell Growth Differ. , vol.13 , pp. 95-106
    • Wilsker, D.1    Patsialou, A.2    Dallas, P.B.3    Moran, E.4
  • 54
    • 0029610034 scopus 로고
    • The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family
    • Herrscher R.F., Kaplan M.H., Lelsz D.L., Das C., Scheuermann R., and Tucker P.W. The immunoglobulin heavy-chain matrix-associating regions are bound by Bright: a B cell-specific trans-activator that describes a new DNA-binding protein family. Genes Dev. 9 (1995) 3067-3082
    • (1995) Genes Dev. , vol.9 , pp. 3067-3082
    • Herrscher, R.F.1    Kaplan, M.H.2    Lelsz, D.L.3    Das, C.4    Scheuermann, R.5    Tucker, P.W.6
  • 55
    • 0030066080 scopus 로고    scopus 로고
    • Characterization of the dead ringer gene identifies a novel, highly conserved family of sequence-specific DNA-binding proteins
    • Gregory S.L., Kortschak R.D., Kalionis B., and Saint R. Characterization of the dead ringer gene identifies a novel, highly conserved family of sequence-specific DNA-binding proteins. Mol. Cell. Biol. 16 (1996) 792-799
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 792-799
    • Gregory, S.L.1    Kortschak, R.D.2    Kalionis, B.3    Saint, R.4
  • 56
    • 1942469319 scopus 로고    scopus 로고
    • Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition
    • Kim S., Zhang Z., Upchurch S., Isern N., and Chen Y. Structure and DNA-binding sites of the SWI1 AT-rich interaction domain (ARID) suggest determinants for sequence-specific DNA recognition. J. Biol. Chem. 279 (2004) 16670-16676
    • (2004) J. Biol. Chem. , vol.279 , pp. 16670-16676
    • Kim, S.1    Zhang, Z.2    Upchurch, S.3    Isern, N.4    Chen, Y.5
  • 57
    • 0033229821 scopus 로고    scopus 로고
    • Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID)
    • Iwahara J., and Clubb R.T. Solution structure of the DNA binding domain from Dead ringer, a sequence-specific AT-rich interaction domain (ARID). EMBO J. 18 (1999) 6084-6094
    • (1999) EMBO J. , vol.18 , pp. 6084-6094
    • Iwahara, J.1    Clubb, R.T.2
  • 58
    • 2542592428 scopus 로고    scopus 로고
    • The DNA-binding properties of the ARID-containing subunits of yeast and mammalian SWI/SNF complexes
    • Wilsker D., Patsialou A., Zumbrun S.D., Kim S., Chen Y., Dallas P.B., and Moran E. The DNA-binding properties of the ARID-containing subunits of yeast and mammalian SWI/SNF complexes. Nucleic Acids Res. 32 (2004) 1345-1353
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1345-1353
    • Wilsker, D.1    Patsialou, A.2    Zumbrun, S.D.3    Kim, S.4    Chen, Y.5    Dallas, P.B.6    Moran, E.7
  • 60
    • 18844468317 scopus 로고    scopus 로고
    • The SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities
    • RESEARCH0039
    • Aravind L., and Iyer L.M. The SWIRM domain: a conserved module found in chromosomal proteins points to novel chromatin-modifying activities. Genome Biol. 3 (2002) RESEARCH0039
    • (2002) Genome Biol. , vol.3
    • Aravind, L.1    Iyer, L.M.2
  • 61
    • 33144483781 scopus 로고    scopus 로고
    • Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes
    • Da G., Lenkart J., Zhao K., Shiekhattar R., Cairns B.R., and Marmorstein R. Structure and function of the SWIRM domain, a conserved protein module found in chromatin regulatory complexes. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 2057-2062
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 2057-2062
    • Da, G.1    Lenkart, J.2    Zhao, K.3    Shiekhattar, R.4    Cairns, B.R.5    Marmorstein, R.6
  • 62
    • 24944535335 scopus 로고    scopus 로고
    • Regulation of LSD1 histone demethylase activity by its associated factors
    • Shi Y.J., Matson C., Lan F., Iwase S., Baba T., and Shi Y. Regulation of LSD1 histone demethylase activity by its associated factors. Mol. Cell 19 (2005) 857-864
    • (2005) Mol. Cell , vol.19 , pp. 857-864
    • Shi, Y.J.1    Matson, C.2    Lan, F.3    Iwase, S.4    Baba, T.5    Shi, Y.6
  • 64
    • 0038185286 scopus 로고    scopus 로고
    • Multiple mechanistically distinct functions of SAGA at the PHO5 promoter
    • Barbaric S., Reinke H., and Horz W. Multiple mechanistically distinct functions of SAGA at the PHO5 promoter. Mol. Cell. Biol. 23 (2003) 3468-3476
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3468-3476
    • Barbaric, S.1    Reinke, H.2    Horz, W.3
  • 65
    • 0036809731 scopus 로고    scopus 로고
    • Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes
    • Boyer L.A., Langer M.R., Crowley K.A., Tan S., Denu J.M., and Peterson C.L. Essential role for the SANT domain in the functioning of multiple chromatin remodeling enzymes. Mol. Cell 10 (2002) 935-942
    • (2002) Mol. Cell , vol.10 , pp. 935-942
    • Boyer, L.A.1    Langer, M.R.2    Crowley, K.A.3    Tan, S.4    Denu, J.M.5    Peterson, C.L.6
  • 66
    • 0037040978 scopus 로고    scopus 로고
    • The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex
    • Sterner D.E., Wang X., Bloom M.H., Simon G.M., and Berger S.L. The SANT domain of Ada2 is required for normal acetylation of histones by the yeast SAGA complex. J. Biol. Chem. 277 (2002) 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
  • 67
    • 0035852637 scopus 로고    scopus 로고
    • CoREST is an integral component of the CoREST - human histone deacetylase complex
    • You A., Tong J.K., Grozinger C.M., and Schreiber S.L. CoREST is an integral component of the CoREST - human histone deacetylase complex. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 1454-1458
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1454-1458
    • You, A.1    Tong, J.K.2    Grozinger, C.M.3    Schreiber, S.L.4
  • 68
    • 0035724413 scopus 로고    scopus 로고
    • The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3
    • Guenther M.G., Barak O., and Lazar M.A. The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol. Cell. Biol. 21 (2001) 6091-6101
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6091-6101
    • Guenther, M.G.1    Barak, O.2    Lazar, M.A.3
  • 69
    • 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 M.G., and Lazar M.A. A SANT motif in the SMRT corepressor interprets the histone code and promotes histone deacetylation. EMBO J. 22 (2003) 3403-3410
    • (2003) EMBO J. , vol.22 , pp. 3403-3410
    • Yu, J.1    Li, Y.2    Ishizuka, T.3    Guenther, M.G.4    Lazar, M.A.5
  • 71
    • 26944472827 scopus 로고    scopus 로고
    • Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain
    • Mo X., Kowenz-Leutz E., Laumonnier Y., Xu H., and Leutz A. Histone H3 tail positioning and acetylation by the c-Myb but not the v-Myb DNA-binding SANT domain. Genes Dev. 19 (2005) 2447-2457
    • (2005) Genes Dev. , vol.19 , pp. 2447-2457
    • Mo, X.1    Kowenz-Leutz, E.2    Laumonnier, Y.3    Xu, H.4    Leutz, A.5
  • 72
    • 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 C.R., Corona D.F.V., Becker P.B., and Müller C.W. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol. Cell 12 (2003) 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.V.5    Becker, P.B.6    Müller, C.W.7
  • 73
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodeling factor
    • Tsukiyama T., and Wu C. Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell 83 (1995) 1011-1020
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Tsukiyama, T.1    Wu, C.2
  • 74
    • 0030839857 scopus 로고    scopus 로고
    • Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
    • Varga-Weisz P.D., Wilm M., Bonte E., Dumas K., Mann M., and Becker P.B. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II. Nature 388 (1997) 598-602
    • (1997) Nature , vol.388 , pp. 598-602
    • Varga-Weisz, P.D.1    Wilm, M.2    Bonte, E.3    Dumas, K.4    Mann, M.5    Becker, P.B.6
  • 75
    • 0033558873 scopus 로고    scopus 로고
    • Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae
    • Tsukiyama T., Palmer J., Landel C.C., Shiloach J., and Wu C. Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae. Genes Dev. 13 (1999) 686-697
    • (1999) Genes Dev. , vol.13 , pp. 686-697
    • Tsukiyama, T.1    Palmer, J.2    Landel, C.C.3    Shiloach, J.4    Wu, C.5
  • 77
    • 0035823613 scopus 로고    scopus 로고
    • Functional differences between the human ATP-dependent nucleosome remodeling proteins BRG1 and SNF2H
    • Aalfs J.D., Narlikar G.J., and Kingston R.E. Functional differences between the human ATP-dependent nucleosome remodeling proteins BRG1 and SNF2H. J. Biol. Chem. 276 (2001) 34270-34278
    • (2001) J. Biol. Chem. , vol.276 , pp. 34270-34278
    • Aalfs, J.D.1    Narlikar, G.J.2    Kingston, R.E.3
  • 78
    • 0035007781 scopus 로고    scopus 로고
    • Cloning and characterization of the murine Imitation Switch (ISWI) genes: differential expression patterns suggest distinct developmental roles for Snf2h and Snf2l
    • Lazzaro M.A., and Picketts D.J. Cloning and characterization of the murine Imitation Switch (ISWI) genes: differential expression patterns suggest distinct developmental roles for Snf2h and Snf2l. J. Neurochem. 77 (2001) 1145-1156
    • (2001) J. Neurochem. , vol.77 , pp. 1145-1156
    • Lazzaro, M.A.1    Picketts, D.J.2
  • 79
    • 0034634578 scopus 로고    scopus 로고
    • Multiple ISWI ATPase complexes from xenopus laevis. Functional conservation of an ACF/CHRAC homolog
    • Guschin D., Geiman T.M., Kikyo N., Tremethick D.J., Wolffe A.P., and Wade P.A. Multiple ISWI ATPase complexes from xenopus laevis. Functional conservation of an ACF/CHRAC homolog. J. Biol. Chem. 275 (2000) 35248-35255
    • (2000) J. Biol. Chem. , vol.275 , pp. 35248-35255
    • Guschin, D.1    Geiman, T.M.2    Kikyo, N.3    Tremethick, D.J.4    Wolffe, A.P.5    Wade, P.A.6
  • 80
    • 0141922979 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI
    • Grune T., Brzeski J., Eberharter A., Clapier C.R., Corona D.F., Becker P.B., and Muller C.W. Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. Mol. Cell 12 (2003) 449-460
    • (2003) Mol. Cell , vol.12 , pp. 449-460
    • Grune, T.1    Brzeski, J.2    Eberharter, A.3    Clapier, C.R.4    Corona, D.F.5    Becker, P.B.6    Muller, C.W.7
  • 81
    • 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 TFIIIB
    • Aasland R., Stewart A.F., and Gibson T. The SANT domain: a putative DNA-binding domain in the SWI-SNF and ADA complexes, the transcriptional co-repressor N-CoR and TFIIIB. Trends Biochem. Sci. 21 (1996) 87-88
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 87-88
    • Aasland, R.1    Stewart, A.F.2    Gibson, T.3
  • 82
    • 0033603212 scopus 로고    scopus 로고
    • Nucleosome movement by CHRAC and ISWI without disruption or trans-displacement of the histone octamer
    • Langst G., Bonte E.J., Corona D.F., and Becker P.B. Nucleosome movement by CHRAC and ISWI without disruption or trans-displacement of the histone octamer. Cell 97 (1999) 843-852
    • (1999) Cell , vol.97 , pp. 843-852
    • Langst, G.1    Bonte, E.J.2    Corona, D.F.3    Becker, P.B.4
  • 83
    • 0029618369 scopus 로고
    • ISWI, a member of the SWI2/SNF2 ATPase family, encodes the 140 kDa subunit of the nucleosome remodeling factor
    • Tsukiyama T., Daniel C., Tamkun J., and Wu C. ISWI, a member of the SWI2/SNF2 ATPase family, encodes the 140 kDa subunit of the nucleosome remodeling factor. Cell 83 (1995) 1021-1026
    • (1995) Cell , vol.83 , pp. 1021-1026
    • Tsukiyama, T.1    Daniel, C.2    Tamkun, J.3    Wu, C.4
  • 84
    • 0031953828 scopus 로고    scopus 로고
    • Chromatin remodeling mediated by Drosophila GAGA factor and ISWI activates fushi tarazu gene transcription in vitro
    • Okada M., and Hirose S. Chromatin remodeling mediated by Drosophila GAGA factor and ISWI activates fushi tarazu gene transcription in vitro. Mol. Cell. Biol. 18 (1998) 2455-2461
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 2455-2461
    • Okada, M.1    Hirose, S.2
  • 85
    • 0030741529 scopus 로고    scopus 로고
    • Role of histone tails in nucleosome remodeling by Drosophila NURF
    • Georgel P.T., Tsukiyama T., and Wu C. Role of histone tails in nucleosome remodeling by Drosophila NURF. EMBO J. 16 (1997) 4717-4726
    • (1997) EMBO J. , vol.16 , pp. 4717-4726
    • Georgel, P.T.1    Tsukiyama, T.2    Wu, C.3
  • 86
    • 0035807901 scopus 로고    scopus 로고
    • Histone tails modulate nucleosome mobility and regulate ATP-dependent nucleosome sliding by NURF
    • Hamiche A., Kang J.G., Dennis C., Xiao H., and Wu C. Histone tails modulate nucleosome mobility and regulate ATP-dependent nucleosome sliding by NURF. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 14316-14321
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 14316-14321
    • Hamiche, A.1    Kang, J.G.2    Dennis, C.3    Xiao, H.4    Wu, C.5
  • 87
    • 0031306557 scopus 로고    scopus 로고
    • Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin
    • Mizuguchi G., Tsukiyama T., Wisniewski J., and Wu C. Role of nucleosome remodeling factor NURF in transcriptional activation of chromatin. Mol. Cell 1 (1997) 141-150
    • (1997) Mol. Cell , vol.1 , pp. 141-150
    • Mizuguchi, G.1    Tsukiyama, T.2    Wisniewski, J.3    Wu, C.4
  • 88
    • 0037115473 scopus 로고    scopus 로고
    • Biological functions of the ISWI chromatin remodeling complex NURF
    • Badenhorst P., Voas M., Rebay I., and Wu C. Biological functions of the ISWI chromatin remodeling complex NURF. Genes Dev. 16 (2002) 3186-3198
    • (2002) Genes Dev. , vol.16 , pp. 3186-3198
    • Badenhorst, P.1    Voas, M.2    Rebay, I.3    Wu, C.4
  • 89
    • 27644580861 scopus 로고    scopus 로고
    • The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis
    • Badenhorst P., Xiao H., Cherbas L., Kwon S.Y., Voas M., Rebay I., Cherbas P., and Wu C. The Drosophila nucleosome remodeling factor NURF is required for Ecdysteroid signaling and metamorphosis. Genes Dev. 19 (2005) 2540-2545
    • (2005) Genes Dev. , vol.19 , pp. 2540-2545
    • Badenhorst, P.1    Xiao, H.2    Cherbas, L.3    Kwon, S.Y.4    Voas, M.5    Rebay, I.6    Cherbas, P.7    Wu, C.8
  • 90
    • 0033603238 scopus 로고    scopus 로고
    • ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF
    • Hamiche A., Sandaltzopoulos R., Gdula D.A., and Wu C. ATP-dependent histone octamer sliding mediated by the chromatin remodeling complex NURF. Cell 97 (1999) 833-842
    • (1999) Cell , vol.97 , pp. 833-842
    • Hamiche, A.1    Sandaltzopoulos, R.2    Gdula, D.A.3    Wu, C.4
  • 91
    • 0034796040 scopus 로고    scopus 로고
    • Dual functions of largest NURF subunit NURF301 in nucleosome sliding and transcription factor interactions
    • Xiao H., Sandaltzopoulos R., Wang H.M., Hamiche A., Ranallo R., Lee K.M., Fu D., and Wu C. Dual functions of largest NURF subunit NURF301 in nucleosome sliding and transcription factor interactions. Mol. Cell 8 (2001) 531-543
    • (2001) Mol. Cell , vol.8 , pp. 531-543
    • Xiao, H.1    Sandaltzopoulos, R.2    Wang, H.M.3    Hamiche, A.4    Ranallo, R.5    Lee, K.M.6    Fu, D.7    Wu, C.8
  • 92
    • 0037086537 scopus 로고    scopus 로고
    • GAL4 directs nucleosome sliding induced by NURF
    • Kang J.G., Hamiche A., and Wu C. GAL4 directs nucleosome sliding induced by NURF. EMBO J. 21 (2002) 1406-1413
    • (2002) EMBO J. , vol.21 , pp. 1406-1413
    • Kang, J.G.1    Hamiche, A.2    Wu, C.3
  • 93
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito T., Bulger M., Pazin M.J., Kobayashi R., and Kadonaga J.T. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90 (1997) 145-155
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 94
    • 0037158744 scopus 로고    scopus 로고
    • Dynamics of ATP-dependent chromatin assembly by ACF
    • Fyodorov D.V., and Kadonaga J.T. Dynamics of ATP-dependent chromatin assembly by ACF. Nature 418 (2002) 897-900
    • (2002) Nature , vol.418 , pp. 897-900
    • Fyodorov, D.V.1    Kadonaga, J.T.2
  • 95
    • 4243824006 scopus 로고    scopus 로고
    • The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding
    • Bonaldi T., Langst G., Strohner R., Becker P.B., and Bianchi M.E. The DNA chaperone HMGB1 facilitates ACF/CHRAC-dependent nucleosome sliding. EMBO J. 21 (2002) 6865-6873
    • (2002) EMBO J. , vol.21 , pp. 6865-6873
    • Bonaldi, T.1    Langst, G.2    Strohner, R.3    Becker, P.B.4    Bianchi, M.E.5
  • 96
    • 0942290537 scopus 로고    scopus 로고
    • Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo
    • Fyodorov D.V., Blower M.D., Karpen G.H., and Kadonaga J.T. Acf1 confers unique activities to ACF/CHRAC and promotes the formation rather than disruption of chromatin in vivo. Genes Dev. 18 (2004) 170-183
    • (2004) Genes Dev. , vol.18 , pp. 170-183
    • Fyodorov, D.V.1    Blower, M.D.2    Karpen, G.H.3    Kadonaga, J.T.4
  • 97
    • 0034660258 scopus 로고    scopus 로고
    • Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally regulated subunits of chromatin accessibility complex (CHRAC)
    • Corona D.F., Eberharter A., Budde A., Deuring R., Ferrari S., Varga-Weisz P., Wilm M., Tamkun J., and Becker P.B. Two histone fold proteins, CHRAC-14 and CHRAC-16, are developmentally regulated subunits of chromatin accessibility complex (CHRAC). EMBO J. 19 (2000) 3049-3059
    • (2000) EMBO J. , vol.19 , pp. 3049-3059
    • Corona, D.F.1    Eberharter, A.2    Budde, A.3    Deuring, R.4    Ferrari, S.5    Varga-Weisz, P.6    Wilm, M.7    Tamkun, J.8    Becker, P.B.9
  • 98
    • 1542358192 scopus 로고    scopus 로고
    • ISWI complexes in Saccharomyces cerevisiae
    • Mellor J., and Morillon A. ISWI complexes in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1677 (2004) 100-112
    • (2004) Biochim. Biophys. Acta , vol.1677 , pp. 100-112
    • Mellor, J.1    Morillon, A.2
  • 100
    • 0035016612 scopus 로고    scopus 로고
    • Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates
    • Gelbart M.E., Rechsteiner T., Richmond T.J., and Tsukiyama T. Interactions of Isw2 chromatin remodeling complex with nucleosomal arrays: analyses using recombinant yeast histones and immobilized templates. Mol. Cell. Biol. 21 (2001) 2098-2106
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2098-2106
    • Gelbart, M.E.1    Rechsteiner, T.2    Richmond, T.J.3    Tsukiyama, T.4
  • 101
    • 0033564199 scopus 로고    scopus 로고
    • ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly
    • Ito T., Levenstein M.E., Fyodorov D.V., Kutach A.K., Kobayashi R., and Kadonaga J.T. ACF consists of two subunits, Acf1 and ISWI, that function cooperatively in the ATP-dependent catalysis of chromatin assembly. Genes Dev. 13 (1999) 1529-1539
    • (1999) Genes Dev. , vol.13 , pp. 1529-1539
    • Ito, T.1    Levenstein, M.E.2    Fyodorov, D.V.3    Kutach, A.K.4    Kobayashi, R.5    Kadonaga, J.T.6
  • 102
    • 8144224380 scopus 로고    scopus 로고
    • ACF1 improves the effectiveness of nucleosome mobilization by ISWI through PHD-histone contacts
    • Eberharter A., Vetter I., Ferreira R., and Becker P.B. ACF1 improves the effectiveness of nucleosome mobilization by ISWI through PHD-histone contacts. EMBO J. 23 (2004) 4029-4039
    • (2004) EMBO J. , vol.23 , pp. 4029-4039
    • Eberharter, A.1    Vetter, I.2    Ferreira, R.3    Becker, P.B.4
  • 103
    • 0031009397 scopus 로고    scopus 로고
    • Chromatin remodeling and transcription
    • Tsukiyama T., and Wu C. Chromatin remodeling and transcription. Curr. Opin. Genet. Dev. 7 (1997) 182-191
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 182-191
    • Tsukiyama, T.1    Wu, C.2
  • 104
    • 0027474628 scopus 로고
    • A mammalian DNA-binding protein that contains a chromodomain and an SNF2/SWI2-like helicase domain
    • Delmas V., Stokes D.G., and Perry R.P. A mammalian DNA-binding protein that contains a chromodomain and an SNF2/SWI2-like helicase domain. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 2414-2418
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2414-2418
    • Delmas, V.1    Stokes, D.G.2    Perry, R.P.3
  • 105
    • 0028948315 scopus 로고
    • DNA-binding and chromatin localization properties of CHD1
    • Stokes D.G., and Perry R.P. DNA-binding and chromatin localization properties of CHD1. Mol. Cell. Biol. 15 (1995) 2745-2753
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2745-2753
    • Stokes, D.G.1    Perry, R.P.2
  • 106
    • 0029901861 scopus 로고    scopus 로고
    • CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes
    • Stokes D.G., Tartof K.D., and Perry R.P. CHD1 is concentrated in interbands and puffed regions of Drosophila polytene chromosomes. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 7137-7142
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 7137-7142
    • Stokes, D.G.1    Tartof, K.D.2    Perry, R.P.3
  • 107
    • 0034657071 scopus 로고    scopus 로고
    • The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor
    • Tran H.G., Steger D.J., Iyer V.R., and Johnson A.D. The chromo domain protein chd1p from budding yeast is an ATP-dependent chromatin-modifying factor. EMBO J. 19 (2000) 2323-2331
    • (2000) EMBO J. , vol.19 , pp. 2323-2331
    • Tran, H.G.1    Steger, D.J.2    Iyer, V.R.3    Johnson, A.D.4
  • 108
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • Shen X., Mizuguchi G., Hamiche A., and Wu C. A chromatin remodelling complex involved in transcription and DNA processing. Nature 406 (2000) 541-544
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 109
  • 110
    • 10944233962 scopus 로고    scopus 로고
    • Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair
    • van Attikum H., Fritsch O., Hohn B., and Gasser S.M. Recruitment of the INO80 complex by H2A phosphorylation links ATP-dependent chromatin remodeling with DNA double-strand break repair. Cell 119 (2004) 777-788
    • (2004) Cell , vol.119 , pp. 777-788
    • van Attikum, H.1    Fritsch, O.2    Hohn, B.3    Gasser, S.M.4
  • 111
    • 0032489520 scopus 로고    scopus 로고
    • DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
    • Rogakou E.P., Pilch D.R., Orr A.H., Ivanova V.S., and Bonner W.M. DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. J. Biol. Chem. 273 (1998) 5858-5868
    • (1998) J. Biol. Chem. , vol.273 , pp. 5858-5868
    • Rogakou, E.P.1    Pilch, D.R.2    Orr, A.H.3    Ivanova, V.S.4    Bonner, W.M.5
  • 112
    • 10944230851 scopus 로고    scopus 로고
    • Around the world of DNA damage INO80 days
    • Cairns B.R. Around the world of DNA damage INO80 days. Cell 119 (2004) 733-735
    • (2004) Cell , vol.119 , pp. 733-735
    • Cairns, B.R.1
  • 113
    • 11144355550 scopus 로고    scopus 로고
    • SWRred not shaken; mixing the histones
    • Korber P., and Horz W. SWRred not shaken; mixing the histones. Cell 117 (2004) 5-7
    • (2004) Cell , vol.117 , pp. 5-7
    • Korber, P.1    Horz, W.2
  • 114
    • 1342289542 scopus 로고    scopus 로고
    • Molecular biology. Breaking the silence
    • Owen-Hughes T., and Bruno M. Molecular biology. Breaking the silence. Science 303 (2004) 324-325
    • (2004) Science , vol.303 , pp. 324-325
    • Owen-Hughes, T.1    Bruno, M.2
  • 117
    • 0348184963 scopus 로고    scopus 로고
    • ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex
    • Mizuguchi G., Shen X., Landry J., Wu W.H., Sen S., and Wu C. ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex. Science 303 (2004) 343-348
    • (2004) Science , vol.303 , pp. 343-348
    • Mizuguchi, G.1    Shen, X.2    Landry, J.3    Wu, W.H.4    Sen, S.5    Wu, C.6
  • 118
    • 0037423930 scopus 로고    scopus 로고
    • Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin
    • Meneghini M.D., Wu M., and Madhani H.D. Conserved histone variant H2A.Z protects euchromatin from the ectopic spread of silent heterochromatin. Cell 112 (2003) 725-736
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 119
    • 6344279816 scopus 로고    scopus 로고
    • The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres
    • Zhang H., Richardson D.O., Roberts D.N., Utley R., Erdjument-Bromage H., Tempst P., Cote J., and Cairns B.R. The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres. Mol. Cell. Biol. 24 (2004) 9424-9436
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9424-9436
    • Zhang, H.1    Richardson, D.O.2    Roberts, D.N.3    Utley, R.4    Erdjument-Bromage, H.5    Tempst, P.6    Cote, J.7    Cairns, B.R.8
  • 121
    • 29444454191 scopus 로고    scopus 로고
    • Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling
    • Li B., Pattenden S.G., Lee D., Gutierrez J., Chen J., Seidel C., Gerton J., and Workman J.L. Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 18385-18390
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 18385-18390
    • Li, B.1    Pattenden, S.G.2    Lee, D.3    Gutierrez, J.4    Chen, J.5    Seidel, C.6    Gerton, J.7    Workman, J.L.8
  • 122
    • 28544442465 scopus 로고    scopus 로고
    • Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
    • Wu W.H., Alami S., Luk E., Wu C.H., Sen S., Mizuguchi G., Wei D., and Wu C. Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange. Nat. Struct. Mol. Biol. 12 (2005) 1064-1071
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1064-1071
    • Wu, W.H.1    Alami, S.2    Luk, E.3    Wu, C.H.4    Sen, S.5    Mizuguchi, G.6    Wei, D.7    Wu, C.8
  • 123
    • 33644999042 scopus 로고    scopus 로고
    • Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae
    • Babiarz J.E., Halley J.E., and Rine J. Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae. Genes Dev. 20 (2006) 700-710
    • (2006) Genes Dev. , vol.20 , pp. 700-710
    • Babiarz, J.E.1    Halley, J.E.2    Rine, J.3
  • 126
    • 0036837670 scopus 로고    scopus 로고
    • High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2
    • Kassabov S.R., Henry N.M., Zofall M., Tsukiyama T., and Bartholomew B. High-resolution mapping of changes in histone-DNA contacts of nucleosomes remodeled by ISW2. Mol. Cell. Biol. 22 (2002) 7524-7534
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7524-7534
    • Kassabov, S.R.1    Henry, N.M.2    Zofall, M.3    Tsukiyama, T.4    Bartholomew, B.5
  • 127
    • 0037512311 scopus 로고    scopus 로고
    • Distinct strategies to make nucleosomal DNA accessible
    • Fan H.Y., He X., Kingston R.E., and Narlikar G.J. Distinct strategies to make nucleosomal DNA accessible. Mol. Cell 11 (2003) 1311-1322
    • (2003) Mol. Cell , vol.11 , pp. 1311-1322
    • Fan, H.Y.1    He, X.2    Kingston, R.E.3    Narlikar, G.J.4
  • 128
    • 4544266390 scopus 로고    scopus 로고
    • Spatial contacts and nucleosome step movements induced by the NURF chromatin remodeling complex
    • Schwanbeck R., Xiao H., and Wu C. Spatial contacts and nucleosome step movements induced by the NURF chromatin remodeling complex. J. Biol. Chem. 279 (2004) 39933-39941
    • (2004) J. Biol. Chem. , vol.279 , pp. 39933-39941
    • Schwanbeck, R.1    Xiao, H.2    Wu, C.3
  • 130
    • 2942561969 scopus 로고    scopus 로고
    • Topography of the ISW2-nucleosome complex: insights into nucleosome spacing and chromatin remodeling
    • Kagalwala M.N., Glaus B.J., Dang W., Zofall M., and Bartholomew B. Topography of the ISW2-nucleosome complex: insights into nucleosome spacing and chromatin remodeling. EMBO J. 23 (2004) 2092-2104
    • (2004) EMBO J. , vol.23 , pp. 2092-2104
    • Kagalwala, M.N.1    Glaus, B.J.2    Dang, W.3    Zofall, M.4    Bartholomew, B.5
  • 132
    • 26944461283 scopus 로고    scopus 로고
    • Chromatin remodeling through directional DNA translocation from an internal nucleosomal site
    • Saha A., Wittmeyer J., and Cairns B.R. Chromatin remodeling through directional DNA translocation from an internal nucleosomal site. Nat. Struct. Mol. Biol. 12 (2005) 747-755
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 747-755
    • Saha, A.1    Wittmeyer, J.2    Cairns, B.R.3
  • 134
    • 0017250384 scopus 로고
    • Studies on the mechanism of DNA cleavage by ethidium
    • Deniss I.S., and Morgan A.R. Studies on the mechanism of DNA cleavage by ethidium. Nucleic Acids Res. 3 (1976) 315-323
    • (1976) Nucleic Acids Res. , vol.3 , pp. 315-323
    • Deniss, I.S.1    Morgan, A.R.2
  • 135
    • 0025141798 scopus 로고
    • A photochemical method to map ethidium bromide binding sites on DNA: application to a bent DNA fragment
    • Krishnamurthy G., Polte T., Rooney T., and Hogan M.E. A photochemical method to map ethidium bromide binding sites on DNA: application to a bent DNA fragment. Biochemistry 29 (1990) 981-988
    • (1990) Biochemistry , vol.29 , pp. 981-988
    • Krishnamurthy, G.1    Polte, T.2    Rooney, T.3    Hogan, M.E.4
  • 137
    • 0032484098 scopus 로고    scopus 로고
    • Requirement of RSF and FACT for transcription of chromatin templates in vitro
    • LeRoy G., Orphanides G., Lane W.S., and Reinberg D. Requirement of RSF and FACT for transcription of chromatin templates in vitro. Science 282 (1998) 1900-1904
    • (1998) Science , vol.282 , pp. 1900-1904
    • LeRoy, G.1    Orphanides, G.2    Lane, W.S.3    Reinberg, D.4
  • 138
    • 0034686020 scopus 로고    scopus 로고
    • Purification and characterization of a human factor that assembles and remodels chromatin
    • LeRoy G., Loyola A., Lane W.S., and Reinberg D. Purification and characterization of a human factor that assembles and remodels chromatin. J. Biol. Chem. 275 (2000) 14787-14790
    • (2000) J. Biol. Chem. , vol.275 , pp. 14787-14790
    • LeRoy, G.1    Loyola, A.2    Lane, W.S.3    Reinberg, D.4
  • 140
    • 0036464569 scopus 로고    scopus 로고
    • A critical epitope for substrate recognition by the nucleosome remodeling ATPase ISWI
    • Clapier C.R., Nightingale K.P., and Becker P.B. A critical epitope for substrate recognition by the nucleosome remodeling ATPase ISWI. Nucleic Acids Res. 30 (2002) 649-655
    • (2002) Nucleic Acids Res. , vol.30 , pp. 649-655
    • Clapier, C.R.1    Nightingale, K.P.2    Becker, P.B.3
  • 141
    • 0035499905 scopus 로고    scopus 로고
    • Reconstitution of recombinant chromatin establishes a requirement for histone-tail modifications during chromatin assembly and transcription
    • Loyola A., LeRoy G., Wang Y.H., and Reinberg D. Reconstitution of recombinant chromatin establishes a requirement for histone-tail modifications during chromatin assembly and transcription. Genes Dev. 15 (2001) 2837-2851
    • (2001) Genes Dev. , vol.15 , pp. 2837-2851
    • Loyola, A.1    LeRoy, G.2    Wang, Y.H.3    Reinberg, D.4
  • 142
    • 33745809637 scopus 로고    scopus 로고
    • Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF
    • Li H., Ilin S., Wang W., Duncan E.M., Wysocka J., Allis C.D., and Patel D.J. Molecular basis for site-specific read-out of histone H3K4me3 by the BPTF PHD finger of NURF. Nature 442 (2006) 91-95
    • (2006) Nature , vol.442 , pp. 91-95
    • Li, H.1    Ilin, S.2    Wang, W.3    Duncan, E.M.4    Wysocka, J.5    Allis, C.D.6    Patel, D.J.7
  • 145
    • 0035937419 scopus 로고    scopus 로고
    • Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes
    • Hassan A.H., Neely K.E., and Workman J.L. Histone acetyltransferase complexes stabilize swi/snf binding to promoter nucleosomes. Cell 104 (2001) 817-827
    • (2001) Cell , vol.104 , pp. 817-827
    • Hassan, A.H.1    Neely, K.E.2    Workman, J.L.3
  • 146
    • 0036850346 scopus 로고    scopus 로고
    • Deciphering the transcriptional histone acetylation code for a human gene
    • Agalioti T., Chen G., and Thanos D. Deciphering the transcriptional histone acetylation code for a human gene. Cell 111 (2002) 381-392
    • (2002) Cell , vol.111 , pp. 381-392
    • Agalioti, T.1    Chen, G.2    Thanos, D.3
  • 147
    • 0038558164 scopus 로고    scopus 로고
    • A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription
    • Huang Z.Q., Li J., Sachs L.M., Cole P.A., and Wong J. A role for cofactor-cofactor and cofactor-histone interactions in targeting p300, SWI/SNF and Mediator for transcription. EMBO J. 22 (2003) 2146-2155
    • (2003) EMBO J. , vol.22 , pp. 2146-2155
    • Huang, Z.Q.1    Li, J.2    Sachs, L.M.3    Cole, P.A.4    Wong, J.5
  • 148
    • 0346993663 scopus 로고    scopus 로고
    • Recruitment of SWI/SNF to the human immunodeficiency virus type 1 promoter
    • Henderson A., Holloway A., Reeves R., and Tremethick D.J. Recruitment of SWI/SNF to the human immunodeficiency virus type 1 promoter. Mol. Cell. Biol. 24 (2004) 389-397
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 389-397
    • Henderson, A.1    Holloway, A.2    Reeves, R.3    Tremethick, D.J.4
  • 149
    • 0842263749 scopus 로고    scopus 로고
    • Roles of SWI/SNF and HATs throughout the dynamic transcription of a yeast glucose-repressible gene
    • Geng F., and Laurent B.C. Roles of SWI/SNF and HATs throughout the dynamic transcription of a yeast glucose-repressible gene. EMBO J. 23 (2004) 127-137
    • (2004) EMBO J. , vol.23 , pp. 127-137
    • Geng, F.1    Laurent, B.C.2
  • 150
    • 18844413266 scopus 로고    scopus 로고
    • Acetylation in histone H3 globular domain regulates gene expression in yeast
    • Xu F., Zhang K., and Grunstein M. Acetylation in histone H3 globular domain regulates gene expression in yeast. Cell 121 (2005) 375-385
    • (2005) Cell , vol.121 , pp. 375-385
    • Xu, F.1    Zhang, K.2    Grunstein, M.3
  • 151
    • 0346095323 scopus 로고    scopus 로고
    • Analysis of a mutant histone H3 that perturbs the association of Swi/Snf with chromatin
    • Duina A.A., and Winston F. Analysis of a mutant histone H3 that perturbs the association of Swi/Snf with chromatin. Mol. Cell. Biol. 24 (2004) 561-572
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 561-572
    • Duina, A.A.1    Winston, F.2
  • 152
    • 0033596723 scopus 로고    scopus 로고
    • The core histone N-terminal domains are required for multiple rounds of catalytic chromatin remodeling by the SWI/SNF and RSC complexes
    • Logie C., Tse C., Hansen J.C., and Peterson C.L. The core histone N-terminal domains are required for multiple rounds of catalytic chromatin remodeling by the SWI/SNF and RSC complexes. Biochemistry 38 (1999) 2514-2522
    • (1999) Biochemistry , vol.38 , pp. 2514-2522
    • Logie, C.1    Tse, C.2    Hansen, J.C.3    Peterson, C.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.