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Volumn 1677, Issue 1-3, 2004, Pages 12-23

To the 30-nm chromatin fiber and beyond

Author keywords

Chromatin; Chromatin associated proteins; Higher order structure; Linker DNA; Nucleosome

Indexed keywords

CHROMOSOME PROTEIN; DNA; HIGH MOBILITY GROUP B PROTEIN; HIGH MOBILITY GROUP N PROTEIN; HISTONE; ISOPROTEIN; SILENT INFORMATION REGULATOR PROTEIN;

EID: 1542358197     PISSN: 01674781     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbaexp.2003.09.013     Document Type: Review
Times cited : (27)

References (126)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nuleosome core particle at 2.8 angstrom resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D., Richmond T.J. Crystal structure of the nuleosome core particle at 2.8 angstrom 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.4    Richmond, T.J.5
  • 2
    • 0035313770 scopus 로고    scopus 로고
    • Higher-order structure of chromatin and chromosomes
    • Woodcock C.L., Dimitrov S. Higher-order structure of chromatin and chromosomes. Curr. Opin. Genet. Dev. 11:2001;130-135.
    • (2001) Curr. Opin. Genet. Dev. , vol.11 , pp. 130-135
    • Woodcock, C.L.1    Dimitrov, S.2
  • 3
    • 0036089388 scopus 로고    scopus 로고
    • Conformational dynamics of the chromatin fiber in solution: Determinants, mechanisms and functions
    • Hansen J.C. Conformational dynamics of the chromatin fiber in solution: determinants, mechanisms and functions. Annu. Rev. Biophys. Biomol. Struct. 31:2002;361-392.
    • (2002) Annu. Rev. Biophys. Biomol. Struct. , vol.31 , pp. 361-392
    • Hansen, J.C.1
  • 4
    • 0034622637 scopus 로고    scopus 로고
    • Chromatin organization and transcriptional control of gene expression in Drosophila
    • Farkas G., Leibovitch B.A., Elgin S.C. Chromatin organization and transcriptional control of gene expression in Drosophila. Gene. 253:2000;117-136.
    • (2000) Gene , vol.253 , pp. 117-136
    • Farkas, G.1    Leibovitch, B.A.2    Elgin, S.C.3
  • 5
    • 0031831516 scopus 로고    scopus 로고
    • Structure, dynamics, and function of chromatin in vitro
    • Widom J. Structure, dynamics, and function of chromatin in vitro. Annu. Rev. Biophys. Biomol. Struct. 27:1998;285-327.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 285-327
    • Widom, J.1
  • 6
    • 0000878535 scopus 로고
    • Solenoidal model for superstructure in chromatin
    • Finch J.T., Klug A. Solenoidal model for superstructure in chromatin. Proc. Natl. Acad. Sci. U. S. A. 73:1976;1897-1901.
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1897-1901
    • Finch, J.T.1    Klug, A.2
  • 7
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and the salt-dependent superstructures of chromatin
    • Thoma F., Koller T., Klug A. Involvement of histone H1 in the organization of the nucleosome and the salt-dependent superstructures of chromatin. J. Cell Biol. 83:1979;402-427.
    • (1979) J. Cell Biol. , vol.83 , pp. 402-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 8
    • 0027517831 scopus 로고
    • A chromatin folding model that incorporates linker variability generates fibers resembling the native structures
    • Woodcock C.L., Grigoryev S.A., Horowitz R.A., Whitaker N. A chromatin folding model that incorporates linker variability generates fibers resembling the native structures. Proc. Natl. Acad. Sci. U. S. A. 90:1993;9021-9025.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 9021-9025
    • Woodcock, C.L.1    Grigoryev, S.A.2    Horowitz, R.A.3    Whitaker, N.4
  • 10
    • 0029583420 scopus 로고
    • Chromatin conformation and salt-induced compaction: Three-dimensional structural information from cryoelectron microscopy
    • Bednar J., Horowitz R.A., Dubochet J., Woodcock C.L. Chromatin conformation and salt-induced compaction: three-dimensional structural information from cryoelectron microscopy. J. Cell Biol. 131:1995;1365-1376.
    • (1995) J. Cell Biol. , vol.131 , pp. 1365-1376
    • Bednar, J.1    Horowitz, R.A.2    Dubochet, J.3    Woodcock, C.L.4
  • 11
    • 0032564478 scopus 로고    scopus 로고
    • Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-oredr folding and compaction of chromatin
    • Bednar J., Horowitz R.A., Grigoryev S.A., Carruthers L.M., Hansen J.C. Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-oredr folding and compaction of chromatin. Proc. Natl. Acad. Sci. U. S. A. 95:1998;14173-14178.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 14173-14178
    • Bednar, J.1    Horowitz, R.A.2    Grigoryev, S.A.3    Carruthers, L.M.4    Hansen, J.C.5
  • 12
    • 0033039286 scopus 로고    scopus 로고
    • Cryoelectron microscopic analysis of nucleosomes and chromatin
    • Bednar J., Woodcock C.L. Cryoelectron microscopic analysis of nucleosomes and chromatin. Methods Enzymol. 304:1999;191-213.
    • (1999) Methods Enzymol. , vol.304 , pp. 191-213
    • Bednar, J.1    Woodcock, C.L.2
  • 13
    • 0034602688 scopus 로고    scopus 로고
    • Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure
    • Cui Y., Bustamante C. Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure. Proc. Natl. Acad. Sci. U. S. A. 97:2000;127-132.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 127-132
    • Cui, Y.1    Bustamante, C.2
  • 14
    • 0034614436 scopus 로고    scopus 로고
    • Pulling chromatin fibers: Computer simulations of direct physical micromanipulations
    • Katritch V., Bustamante C., Olson W.K. Pulling chromatin fibers: computer simulations of direct physical micromanipulations. J. Mol. Biol. 295:2000;29-40.
    • (2000) J. Mol. Biol. , vol.295 , pp. 29-40
    • Katritch, V.1    Bustamante, C.2    Olson, W.K.3
  • 15
    • 0032553448 scopus 로고    scopus 로고
    • Chromatin conformation in living cells: Support for a zig-zag model of the 30 nm chromatin fiber
    • Rydberg B., Holley W.R., Mian I.S., Chatterjee A. Chromatin conformation in living cells: support for a zig-zag model of the 30 nm chromatin fiber. J. Mol. Biol. 284:1998;71-84.
    • (1998) J. Mol. Biol. , vol.284 , pp. 71-84
    • Rydberg, B.1    Holley, W.R.2    Mian, I.S.3    Chatterjee, A.4
  • 16
    • 0036574913 scopus 로고    scopus 로고
    • Unravelling heterochromatin: Competition between positive and negative factors regulates accessibility
    • Dillon N., Festenstein R. Unravelling heterochromatin: competition between positive and negative factors regulates accessibility. Trends Genet. 18:2002;252-258.
    • (2002) Trends Genet. , vol.18 , pp. 252-258
    • Dillon, N.1    Festenstein, R.2
  • 17
    • 0037385490 scopus 로고    scopus 로고
    • Structures and interactions of the core histone tail domains
    • Zheng C., Hayes J.J. Structures and interactions of the core histone tail domains. Biopolymers. 68:2003;539-546.
    • (2003) Biopolymers , vol.68 , pp. 539-546
    • Zheng, C.1    Hayes, J.J.2
  • 18
    • 0024468871 scopus 로고
    • Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1
    • Hansen J.C., Ausio J., Stanik V.H., van Holde K.E. Homogeneous reconstituted oligonucleosomes, evidence for salt-dependent folding in the absence of histone H1. Biochemistry. 28:1989;9129-9136.
    • (1989) Biochemistry , vol.28 , pp. 9129-9136
    • Hansen, J.C.1    Ausio, J.2    Stanik, V.H.3    Van Holde, K.E.4
  • 19
    • 0028363760 scopus 로고
    • Formation and stability of higher order chromatin structures. Contributions of the histone octamer
    • Schwartz P.M., Hansen J.C. Formation and stability of higher order chromatin structures. Contributions of the histone octamer. J. Biol. Chem. 269:1994;16284-16289.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16284-16289
    • Schwartz, P.M.1    Hansen, J.C.2
  • 20
    • 0029882454 scopus 로고    scopus 로고
    • Reversible oligonucleosome self-association: Dependence on divalent cations and core histone tail domains
    • Schwartz P.M., Felthauser A., Fletcher T.M., Hansen J.C. Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry. 35:1996;4009-4015.
    • (1996) Biochemistry , vol.35 , pp. 4009-4015
    • Schwartz, P.M.1    Felthauser, A.2    Fletcher, T.M.3    Hansen, J.C.4
  • 21
    • 0032553013 scopus 로고    scopus 로고
    • Linker histones stabilize the intrinsic salt-dependent folding of nucloeosmal arrays mechanistic ramifications for higher-order chromatin folding
    • Carruthers L.M., Bednar J., Woodcock C.L., Hansen J.C. Linker histones stabilize the intrinsic salt-dependent folding of nucloeosmal arrays mechanistic ramifications for higher-order chromatin folding. Biochemistry. 37:1998;14776-14787.
    • (1998) Biochemistry , vol.37 , pp. 14776-14787
    • Carruthers, L.M.1    Bednar, J.2    Woodcock, C.L.3    Hansen, J.C.4
  • 22
    • 0026782131 scopus 로고
    • Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1
    • Garcia-Ramirez M., Dong F., Ausio J. Role of the histone "tails" in the folding of oligonucleosomes depleted of histone H1. J. Biol. Chem. 267:1992;19587-19595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19587-19595
    • Garcia-Ramirez, M.1    Dong, F.2    Ausio, J.3
  • 25
    • 0042357071 scopus 로고    scopus 로고
    • Chromatin compaction by human MeCP2: Assembly of novel secondary chromatin structures in the absence of DNA methylation
    • (Epub ahead of print)
    • Georgel P.T., Horowitz-Scherer R.A., Adkins N., Woodcock C.L., Wade P.A., Hansen J.C. Chromatin compaction by human MeCP2: Assembly of novel secondary chromatin structures in the absence of DNA methylation. J. Biol. Chem. 2003;. (Epub ahead of print).
    • (2003) J. Biol. Chem.
    • Georgel, P.T.1    Horowitz-Scherer, R.A.2    Adkins, N.3    Woodcock, C.L.4    Wade, P.A.5    Hansen, J.C.6
  • 26
    • 0037648395 scopus 로고    scopus 로고
    • Heterochromatin protein 1 (HP1) is associated with induced gene expression in Drosophila euchromatin
    • Piacentini L., Fanti L., Berloco M., Perrini B., Pimpinelli S. Heterochromatin protein 1 (HP1) is associated with induced gene expression in Drosophila euchromatin. J. Cell Biol. 161:2003;707-714.
    • (2003) J. Cell Biol. , vol.161 , pp. 707-714
    • Piacentini, L.1    Fanti, L.2    Berloco, M.3    Perrini, B.4    Pimpinelli, S.5
  • 27
    • 0003903126 scopus 로고
    • New York: Springer-Verlag Publishers
    • van Holde E. Chromatin. 1988;Springer-Verlag Publishers, New York.
    • (1988) Chromatin
    • Van Holde, E.1
  • 28
    • 0004142945 scopus 로고    scopus 로고
    • Chromatin: Structure and Function
    • New York: Academic Publishers
    • Wolffe A.P. Chromatin: Structure and Function. 3rd ed. 1998;Academic Publishers, New York.
    • (1998) 3rd Ed.
    • Wolffe, A.P.1
  • 29
    • 0034881774 scopus 로고    scopus 로고
    • A compendium of the histone H1 family of somatic subtypes: An elusive cast of characters and their characteristics
    • Parseghian M.H., Hamkalo B.A. A compendium of the histone H1 family of somatic subtypes: an elusive cast of characters and their characteristics. Biochem. Cell. Biol. 79:2001;289-304.
    • (2001) Biochem. Cell. Biol. , vol.79 , pp. 289-304
    • Parseghian, M.H.1    Hamkalo, B.A.2
  • 30
    • 0034881775 scopus 로고    scopus 로고
    • Linker histone function in chromatin: Dual mechanisms of action
    • Georgel P.T., Hansen J.C. Linker histone function in chromatin: dual mechanisms of action. Biochem. Cell. Biol. 79:2001;313-316.
    • (2001) Biochem. Cell. Biol. , vol.79 , pp. 313-316
    • Georgel, P.T.1    Hansen, J.C.2
  • 31
    • 0029013311 scopus 로고
    • Linker histones are not essential and affect chromatin condensation in vivo
    • Shen X., Yu L., Weir J.W., Gorovsky M.A. Linker histones are not essential and affect chromatin condensation in vivo. Cell. 82:1995;47-56.
    • (1995) Cell , vol.82 , pp. 47-56
    • Shen, X.1    Yu, L.2    Weir, J.W.3    Gorovsky, M.A.4
  • 32
    • 0033771361 scopus 로고    scopus 로고
    • Are linker histones (histone H1) dispensable for survival?
    • Ausio J. Are linker histones (histone H1) dispensable for survival? BioEssays. 22:2000;873-877.
    • (2000) BioEssays , vol.22 , pp. 873-877
    • Ausio, J.1
  • 33
    • 0029127222 scopus 로고
    • A variety of DNA-binding and multimeric proteins contain the histone fold motif
    • Baxevanis A.D., Arents G., Moudrianakis E.N., Landsman D. A variety of DNA-binding and multimeric proteins contain the histone fold motif. Nucleic Acids Res. 23:1995;2685-2691.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2685-2691
    • Baxevanis, A.D.1    Arents, G.2    Moudrianakis, E.N.3    Landsman, D.4
  • 34
    • 0028867087 scopus 로고
    • The histone fold: A ubiquitous architectural motif utilized in DNA compaction and protein dimerization
    • Arents G., Moudrianakis E.N. The histone fold: a ubiquitous architectural motif utilized in DNA compaction and protein dimerization. Proc. Natl. Acad. Sci. U. S. A. 92:1995;11170-11174.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 11170-11174
    • Arents, G.1    Moudrianakis, E.N.2
  • 35
    • 0033151772 scopus 로고    scopus 로고
    • Histone H1: Location and role
    • Thomas J.O. Histone H1: location and role. Curr. Opin. Cell Biol. 11:1999;312-317.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 312-317
    • Thomas, J.O.1
  • 36
    • 0032972980 scopus 로고    scopus 로고
    • The location of the linker histone on the nucleosome
    • Travers A. The location of the linker histone on the nucleosome. Trends Biochem. Sci. 24:1999;4-7.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 4-7
    • Travers, A.1
  • 37
    • 0024264685 scopus 로고
    • Differences in the binding of H1 variants to DNA. Cooperativity and linker-length related distribution
    • Clark D.J., Thomas J.O. Differences in the binding of H1 variants to DNA. Cooperativity and linker-length related distribution. Eur. J. Biochem. 178:1988;225-233.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 225-233
    • Clark, D.J.1    Thomas, J.O.2
  • 40
    • 0029004739 scopus 로고
    • Energy-dependent chromatin accessibility and nucleosome mobility in a cell-free system
    • Varga-Weisz P.D., Blank T.A., Becker P.B. Energy-dependent chromatin accessibility and nucleosome mobility in a cell-free system. EMBO J. 14:1995;2209-2216.
    • (1995) EMBO J. , vol.14 , pp. 2209-2216
    • Varga-Weisz, P.D.1    Blank, T.A.2    Becker, P.B.3
  • 42
    • 0022446807 scopus 로고
    • Roles of H1 domains in determining higher order chromatin structure and H1 location
    • Allan J., Mitchell T., Harborne N., Bohm L., Crane-Robinson C. Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol. 187:1986;591-601.
    • (1986) J. Mol. Biol. , vol.187 , pp. 591-601
    • Allan, J.1    Mitchell, T.2    Harborne, N.3    Bohm, L.4    Crane-Robinson, C.5
  • 43
    • 0031972528 scopus 로고    scopus 로고
    • Electron microscopic imaging of chromatin with nucleosome resolution
    • Woodcock C.L., Horowitz R.A. Electron microscopic imaging of chromatin with nucleosome resolution. Methods Cell Biol. 167:1998;167-186.
    • (1998) Methods Cell Biol. , vol.167 , pp. 167-186
    • Woodcock, C.L.1    Horowitz, R.A.2
  • 44
    • 0031594183 scopus 로고    scopus 로고
    • When more is less
    • Wolffe A.P. When more is less. Nat. Genet. 18:1998;5-6.
    • (1998) Nat. Genet. , vol.18 , pp. 5-6
    • Wolffe, A.P.1
  • 45
    • 0031968760 scopus 로고    scopus 로고
    • Chromatin fiber structure: Morphologhy, molecular determinants, structural transition
    • Zlatanova J., Leuba S.H., van Holde K. Chromatin fiber structure: morphologhy, molecular determinants, structural transition. Biophys. J. 74:1998;2554-2566.
    • (1998) Biophys. J. , vol.74 , pp. 2554-2566
    • Zlatanova, J.1    Leuba, S.H.2    Van Holde, K.3
  • 46
    • 0033287307 scopus 로고    scopus 로고
    • Analysis of chromatin by scanning force microscopy
    • Leuba S.H., Bustamante C. Analysis of chromatin by scanning force microscopy. Methods Mol. Biol. 119:1999;143-160.
    • (1999) Methods Mol. Biol. , vol.119 , pp. 143-160
    • Leuba, S.H.1    Bustamante, C.2
  • 47
  • 48
    • 0036208731 scopus 로고    scopus 로고
    • Histone H1 represses estrogen receptor alpha transcriptional activity by selectively inhibiting receptor-mediated transcription initiation
    • Cheung E., Zarifyan A.S., Kraus W.L. Histone H1 represses estrogen receptor alpha transcriptional activity by selectively inhibiting receptor-mediated transcription initiation. Mol. Cell. Biol. 22:2002;2463-2471.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2463-2471
    • Cheung, E.1    Zarifyan, A.S.2    Kraus, W.L.3
  • 49
    • 0034741833 scopus 로고    scopus 로고
    • HMG1 and 2: Architectural DNA-binding proteins
    • Thomas J.O. HMG1 and 2: architectural DNA-binding proteins. Biochem. Soc. Trans. 29:2001;395-401.
    • (2001) Biochem. Soc. Trans. , vol.29 , pp. 395-401
    • Thomas, J.O.1
  • 50
    • 0035399963 scopus 로고    scopus 로고
    • Chromatin unfolding and activation by HMGN(*) chromosomal proteins
    • Bustin M. Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Trends Biochem. Sci. 26:2001;431-437.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 431-437
    • Bustin, M.1
  • 51
    • 0035281548 scopus 로고    scopus 로고
    • HMG1 and 2, and related 'architectural' DNA-binding proteins
    • Thomas J.O., Travers A.A. HMG1 and 2, and related 'architectural' DNA-binding proteins. Trends Biochem. Sci. 26:2001;167-174.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 167-174
    • Thomas, J.O.1    Travers, A.A.2
  • 52
    • 0026704583 scopus 로고
    • A high-mobility-group protein and its cDNAs from Drosophila melanogaster
    • Wagner C.R., Hamana K., Elgin S.C. A high-mobility-group protein and its cDNAs from Drosophila melanogaster. Mol. Cell. Biol. 12:1992;1915-1923.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1915-1923
    • Wagner, C.R.1    Hamana, K.2    Elgin, S.C.3
  • 53
    • 0040602752 scopus 로고    scopus 로고
    • HMG1 proteins from evolutionary distant organisms distort B-DNA conformation in similar way
    • Wisniewski J.R., Krohn N.M., Heyduk E., Grasser K.D., Heyduk T. HMG1 proteins from evolutionary distant organisms distort B-DNA conformation in similar way. Biochim. Biophys. Acta. 1447:1999;25-34.
    • (1999) Biochim. Biophys. Acta , vol.1447 , pp. 25-34
    • Wisniewski, J.R.1    Krohn, N.M.2    Heyduk, E.3    Grasser, K.D.4    Heyduk, T.5
  • 54
    • 0029790690 scopus 로고    scopus 로고
    • Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: Structural transitions and transcriptional repression
    • Ura K., Nightingale K., Wolffe A.P. Differential association of HMG1 and linker histones B4 and H1 with dinucleosomal DNA: structural transitions and transcriptional repression. EMBO J. 15:1996;4959-4969.
    • (1996) EMBO J. , vol.15 , pp. 4959-4969
    • Ura, K.1    Nightingale, K.2    Wolffe, A.P.3
  • 55
    • 0037388605 scopus 로고    scopus 로고
    • Quantitative characterization of specific genomic promoters using agarose gel electrophoresis
    • Georgel P.T., Hansen J.C. Quantitative characterization of specific genomic promoters using agarose gel electrophoresis. Biopolymers. 68:2003;557-562.
    • (2003) Biopolymers , vol.68 , pp. 557-562
    • Georgel, P.T.1    Hansen, J.C.2
  • 56
    • 0028921810 scopus 로고
    • High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors
    • Zwilling S., Konig H., Wirth T. High mobility group protein 2 functionally interacts with the POU domains of octamer transcription factors. EMBO J. 14:1995;1198-1208.
    • (1995) EMBO J. , vol.14 , pp. 1198-1208
    • Zwilling, S.1    Konig, H.2    Wirth, T.3
  • 57
    • 0036199666 scopus 로고    scopus 로고
    • HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme a
    • Fan Z., Beresford P.J., Zhang D., Lieberman J. HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A. Mol. Cell. Biol. 22:2002;2810-2820.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2810-2820
    • Fan, Z.1    Beresford, P.J.2    Zhang, D.3    Lieberman, J.4
  • 58
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin M., Reeves R. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54:1996;35-100.
    • (1996) Prog. Nucleic Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 59
    • 0032933141 scopus 로고    scopus 로고
    • Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes
    • Herrera J.E., Sakaguchi K., Bergel M., Trieschmann L., Nakatani Y., Bustin M. Specific acetylation of chromosomal protein HMG-17 by PCAF alters its interaction with nucleosomes. Mol. Cell. Biol. 19:1999;3466-3473.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3466-3473
    • Herrera, J.E.1    Sakaguchi, K.2    Bergel, M.3    Trieschmann, L.4    Nakatani, Y.5    Bustin, M.6
  • 60
    • 0032510746 scopus 로고    scopus 로고
    • The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes
    • Trieschmann L., Martin B., Bustin M. The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes. Proc. Natl. Acad. Sci. U. S. A. 95:1998;5468-5473.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5468-5473
    • Trieschmann, L.1    Martin, B.2    Bustin, M.3
  • 61
    • 0029348071 scopus 로고
    • The HMG-14/-17 chromosomal protein family: Architectural elements that enhance transcription from chromatin templates
    • Bustin M., Trieschmann L., Postnikov Y.V. The HMG-14/-17 chromosomal protein family: architectural elements that enhance transcription from chromatin templates. Sem. Cell Biol. 6:1995;247-255.
    • (1995) Sem. Cell Biol. , vol.6 , pp. 247-255
    • Bustin, M.1    Trieschmann, L.2    Postnikov, Y.V.3
  • 62
    • 0025969983 scopus 로고
    • Distribution of high mobility group proteins 1/2, e and 14/17 and linker histones H1 and H5 on transcribed and non-transcribed regions of chicken erythrocyte chromatin
    • Postnikov Y.V., Shick V.V., Belyavsky A.V., Khrapko K.R., Brodolin K.L., Nikolskaya T.A., Mirzabekov A.D. Distribution of high mobility group proteins 1/2, E and 14/17 and linker histones H1 and H5 on transcribed and non-transcribed regions of chicken erythrocyte chromatin. Nucleic Acids Res. 19:1991;717-725.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 717-725
    • Postnikov, Y.V.1    Shick, V.V.2    Belyavsky, A.V.3    Khrapko, K.R.4    Brodolin, K.L.5    Nikolskaya, T.A.6    Mirzabekov, A.D.7
  • 63
    • 0036668636 scopus 로고    scopus 로고
    • Competition between histone H1 and HMGN proteins for chromatin binding sites
    • Catez F., Brown D.T., Misteli T., Bustin M. Competition between histone H1 and HMGN proteins for chromatin binding sites. EMBO Rep. 3:2002;760-766.
    • (2002) EMBO Rep. , vol.3 , pp. 760-766
    • Catez, F.1    Brown, D.T.2    Misteli, T.3    Bustin, M.4
  • 64
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., Allis C.D. Translating the histone code. Science. 293:2001;1074-1080.
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 65
    • 0033605391 scopus 로고    scopus 로고
    • MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member
    • Grigoryev S.A., Bednar J., Woodcock C.L. MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. J. Biol. Chem. 274:1999;5626-5636.
    • (1999) J. Biol. Chem. , vol.274 , pp. 5626-5636
    • Grigoryev, S.A.1    Bednar, J.2    Woodcock, C.L.3
  • 66
    • 0032579273 scopus 로고    scopus 로고
    • Chromatin structure in granulocytes. a link between tight compaction and accumulation of a heterochromatin-associated protein (MENT)
    • Grigoryev S.A., Woodcock C.L. Chromatin structure in granulocytes. A link between tight compaction and accumulation of a heterochromatin-associated protein (MENT). J. Biol. Chem. 273:1998;3082-3089.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3082-3089
    • Grigoryev, S.A.1    Woodcock, C.L.2
  • 67
    • 0026597552 scopus 로고
    • Cooperative binding of the globular domains of histones H1 and H5 to DNA
    • Thomas J.O., Rees C., Finch J.T. Cooperative binding of the globular domains of histones H1 and H5 to DNA. Nucleic Acids Res. 20:1992;187-194.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 187-194
    • Thomas, J.O.1    Rees, C.2    Finch, J.T.3
  • 69
    • 0022818549 scopus 로고
    • Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene
    • James T.C., Elgin S.C. Identification of a nonhistone chromosomal protein associated with heterochromatin in Drosophila melanogaster and its gene. Mol. Cell. Biol. 6:1986;3862-3872.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 3862-3872
    • James, T.C.1    Elgin, S.C.2
  • 70
    • 0032215539 scopus 로고    scopus 로고
    • The heterochromatin protein 1 prevents telomere fusions in Drosophila
    • Fanti L., Giovinazzo G., Berloco M., Pimpinelli S. The heterochromatin protein 1 prevents telomere fusions in Drosophila. Mol. Cell. 2:1998;527-538.
    • (1998) Mol. Cell , vol.2 , pp. 527-538
    • Fanti, L.1    Giovinazzo, G.2    Berloco, M.3    Pimpinelli, S.4
  • 71
    • 0038615854 scopus 로고    scopus 로고
    • Chromosomal distribution of heterochromatin protein 1 (HP1) in Drosophila: A cytological map of euchromatin HP1 binding sites
    • Fanti L., Berloco M., Piacentini L., Pimpinelli S. Chromosomal distribution of heterochromatin protein 1 (HP1) in Drosophila: a cytological map of euchromatin HP1 binding sites. Genetica. 117:2003;135-147.
    • (2003) Genetica , vol.117 , pp. 135-147
    • Fanti, L.1    Berloco, M.2    Piacentini, L.3    Pimpinelli, S.4
  • 72
    • 0037464584 scopus 로고    scopus 로고
    • DNA triplet repeats mediate heterochromatin-protein-1-sensitive variegated gene silencing
    • Saveliev A., Everett C., Sharpe T., Webster Z., Festenstein R. DNA triplet repeats mediate heterochromatin-protein-1-sensitive variegated gene silencing. Nature. 422:2003;909-913.
    • (2003) Nature , vol.422 , pp. 909-913
    • Saveliev, A.1    Everett, C.2    Sharpe, T.3    Webster, Z.4    Festenstein, R.5
  • 75
    • 0033964661 scopus 로고    scopus 로고
    • Mammalian chromodomain proteins: Their role in genome organisation and expression
    • Jones D.O., Cowell I.G., Singh P.B. Mammalian chromodomain proteins: their role in genome organisation and expression. BioEssays. 22:2000;124-137.
    • (2000) BioEssays , vol.22 , pp. 124-137
    • Jones, D.O.1    Cowell, I.G.2    Singh, P.B.3
  • 76
    • 0034026194 scopus 로고    scopus 로고
    • The HP1 protein family: Getting a grip on chromatin
    • Eissenberg J.C., Elgin S.C.R. The HP1 protein family: getting a grip on chromatin. Curr. Opin. Genet. Dev. 10:2000;204-210.
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 204-210
    • Eissenberg, J.C.1    Elgin, S.C.R.2
  • 78
    • 0034353169 scopus 로고    scopus 로고
    • HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes
    • Minc E., Courvalin J.C., Buendia B. HP1gamma associates with euchromatin and heterochromatin in mammalian nuclei and chromosomes. Cytogenet. Cell Genet. 90:2000;279-284.
    • (2000) Cytogenet. Cell Genet. , vol.90 , pp. 279-284
    • Minc, E.1    Courvalin, J.C.2    Buendia, B.3
  • 79
    • 0026098009 scopus 로고
    • The Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila
    • Paro R., Hogness D.S. The Polycomb protein shares a homologous domain with a heterochromatin-associated protein of Drosophila. Proc. Natl. Acad. Sci. U. S. A. 88:1991;263-267.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 263-267
    • Paro, R.1    Hogness, D.S.2
  • 82
    • 0034194376 scopus 로고    scopus 로고
    • Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis
    • Cowieson N.P., Partridge J.F., Allshire R.C., McLaughin P.J. Dimerisation of a chromo shadow domain and distinctions from the chromodomain as revealed by structural analysis. Curr. Biol. 10:2000;517-525.
    • (2000) Curr. Biol. , vol.10 , pp. 517-525
    • Cowieson, N.P.1    Partridge, J.F.2    Allshire, R.C.3    McLaughin, P.J.4
  • 83
    • 0029781631 scopus 로고    scopus 로고
    • Human homolog of Drosophila heterochromatin-associated protein 1 (HP1) is a DNA-binding protein which possesses a DNA-binding motif with weak similarity to that of human centromere protein C (CENP-C)
    • (Tokyo)
    • Sugimoto K., Yamada T., Muro Y., Himeno M. Human homolog of Drosophila heterochromatin-associated protein 1 (HP1) is a DNA-binding protein which possesses a DNA-binding motif with weak similarity to that of human centromere protein C (CENP-C). J. Biochem. 120:1996;153-159. (Tokyo).
    • (1996) J. Biochem. , vol.120 , pp. 153-159
    • Sugimoto, K.1    Yamada, T.2    Muro, Y.3    Himeno, M.4
  • 84
    • 0040082217 scopus 로고    scopus 로고
    • SU(VAR)3-7, a Drosophila heterochromatin-associated protein and companion of HP1 in the genomic silencing of position-effect variegation
    • Cléard F., Delattre M., Spierer P. SU(VAR)3-7, a Drosophila heterochromatin-associated protein and companion of HP1 in the genomic silencing of position-effect variegation. EMBO J. 16:1997;5280-5288.
    • (1997) EMBO J. , vol.16 , pp. 5280-5288
    • Cléard, F.1    Delattre, M.2    Spierer, P.3
  • 85
    • 0028110864 scopus 로고
    • The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes
    • Tschiersch B., Hofmann A., Krauss V., Dorn R., Korge G., Reuter G. The protein encoded by the Drosophila position-effect variegation suppressor gene Su(var)3-9 combines domains of antagonistic regulators of homeotic gene complexes. EMBO J. 13:1994;3822-3831.
    • (1994) EMBO J. , vol.13 , pp. 3822-3831
    • Tschiersch, B.1    Hofmann, A.2    Krauss, V.3    Dorn, R.4    Korge, G.5    Reuter, G.6
  • 86
    • 0038412822 scopus 로고    scopus 로고
    • The DNA methyltransferases associate with HP1 and the SUB39H1 histone methyltransferase
    • Fuks F., Hurd P.J., Deplus R., Kouzarides T. The DNA methyltransferases associate with HP1 and the SUB39H1 histone methyltransferase. Nucleic Acids Res. 31:2003;2305-2312.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2305-2312
    • Fuks, F.1    Hurd, P.J.2    Deplus, R.3    Kouzarides, T.4
  • 87
    • 0034531519 scopus 로고    scopus 로고
    • The genomic silencing of position-effect variegation in Drosophila melanogaster: Interaction between the heterochromatin-associated proteins Su(var)3-7 and HP1
    • Delattre M., Spierer A., Tonka C.H., Spierer P. The genomic silencing of position-effect variegation in Drosophila melanogaster: interaction between the heterochromatin-associated proteins Su(var)3-7 and HP1. J. Cell. Sci. 113:2000;4253-4261.
    • (2000) J. Cell. Sci. , vol.113 , pp. 4253-4261
    • Delattre, M.1    Spierer, A.2    Tonka, C.H.3    Spierer, P.4
  • 88
    • 0035865437 scopus 로고    scopus 로고
    • Ectopic HP1 promotes chromosome loops and variegated silencing in Drosophila
    • Seum C., Delattre M., Spierer A., Spierer P. Ectopic HP1 promotes chromosome loops and variegated silencing in Drosophila. EMBO J. 15:2001;812-818.
    • (2001) EMBO J. , vol.15 , pp. 812-818
    • Seum, C.1    Delattre, M.2    Spierer, A.3    Spierer, P.4
  • 89
    • 0036846539 scopus 로고    scopus 로고
    • Selective interaction between the chromatin-remodeling factor BRG1 and the heterochromatin-associated protein HP1alpha
    • Nielsen A.L., Sanchez C., Ichinose H., Cervino M., Lerouge T., Chambon P., Losson R. Selective interaction between the chromatin-remodeling factor BRG1 and the heterochromatin-associated protein HP1alpha. EMBO J. 21:2002;5797-5806.
    • (2002) EMBO J. , vol.21 , pp. 5797-5806
    • Nielsen, A.L.1    Sanchez, C.2    Ichinose, H.3    Cervino, M.4    Lerouge, T.5    Chambon, P.6    Losson, R.7
  • 90
    • 0037197845 scopus 로고    scopus 로고
    • Isoform-specific interaction of HP1 with human TAFII130
    • Vassallo M.F., Tanese N. Isoform-specific interaction of HP1 with human TAFII130. Proc. Natl. Acad. Sci. U. S. A. 99:2002;5919-5924.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 5919-5924
    • Vassallo, M.F.1    Tanese, N.2
  • 92
    • 0032576619 scopus 로고    scopus 로고
    • INCENP centromere and spindle targeting: Identification of essential conserved motifs and involvement of heterochromatin protein HP1
    • Ainsztein A.M., Kandels-Lewis S.E., Mackay A.M., Earnshaw W.C. INCENP centromere and spindle targeting: identification of essential conserved motifs and involvement of heterochromatin protein HP1. J. Cell Biol. 143:1998;1763-1774.
    • (1998) J. Cell Biol. , vol.143 , pp. 1763-1774
    • Ainsztein, A.M.1    Kandels-Lewis, S.E.2    MacKay, A.M.3    Earnshaw, W.C.4
  • 94
    • 0031794379 scopus 로고    scopus 로고
    • Characterization of sequences associated with position-effect variegation at pericentric sites in Drosophila heterochromatin
    • Cryderman D.E., Cuaycong M.H., Elgin S.C., Wallrath L.L. Characterization of sequences associated with position-effect variegation at pericentric sites in Drosophila heterochromatin. Chromosoma. 107:1998;277-285.
    • (1998) Chromosoma , vol.107 , pp. 277-285
    • Cryderman, D.E.1    Cuaycong, M.H.2    Elgin, S.C.3    Wallrath, L.L.4
  • 95
    • 0033566809 scopus 로고    scopus 로고
    • Heterochromatic silencing of Drosophila heat shock genes acts at the level of promoter potentiation
    • Cryderman D.E., Tang H., Bell C., Gilmour D.S., Wallrath L.L. Heterochromatic silencing of Drosophila heat shock genes acts at the level of promoter potentiation. Nucleic Acids Res. 27:1999;3364-3370.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3364-3370
    • Cryderman, D.E.1    Tang, H.2    Bell, C.3    Gilmour, D.S.4    Wallrath, L.L.5
  • 97
    • 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 A.H., Quivy J.P., Roche D., Taddei A., Lachner M., Jenuwein T., Almouzni G. Higher-order structure in pericentric heterochromatin involves a distinct pattern of histone modification and an RNA component. Nat. Genet. 30:2002;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    Taddei, A.6    Lachner, M.7    Jenuwein, T.8    Almouzni, G.9
  • 98
    • 0026443594 scopus 로고
    • Silencers, silencing, and heritable transcriptional states
    • Laurenson P., Rine J. Silencers, silencing, and heritable transcriptional states. Microbiol. Rev. 56:1992;543-560.
    • (1992) Microbiol. Rev. , vol.56 , pp. 543-560
    • Laurenson, P.1    Rine, J.2
  • 100
    • 0034735990 scopus 로고    scopus 로고
    • Role of NAD(+) in the deacetylase activity of the SIR2-like proteins
    • Landry J., Slama J.T., Sternglanz R. Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278:2000;685-690.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 685-690
    • Landry, J.1    Slama, J.T.2    Sternglanz, R.3
  • 101
    • 0032055730 scopus 로고    scopus 로고
    • Mechanisms of silencing in Saccharomyces cerevisiae
    • Lustig A.J. Mechanisms of silencing in Saccharomyces cerevisiae. Curr. Opin. Genet. Dev. 8:1998;233-239.
    • (1998) Curr. Opin. Genet. Dev. , vol.8 , pp. 233-239
    • Lustig, A.J.1
  • 102
    • 0032412476 scopus 로고    scopus 로고
    • Mating-type gene switching in Saccharomyces cerevisiae
    • Haber J.E. Mating-type gene switching in Saccharomyces cerevisiae. Annu. Rev. Genet. 32:1998;561-599.
    • (1998) Annu. Rev. Genet. , vol.32 , pp. 561-599
    • Haber, J.E.1
  • 103
    • 0027423154 scopus 로고
    • SIR3 and SIR4 proteins are required for the positioning and integrity of yeast telomeres
    • Palladino F., Laroche T., Gilson E., Axelrod A., Pillus L., Gasser S.M. SIR3 and SIR4 proteins are required for the positioning and integrity of yeast telomeres. Cell. 75:1993;543-555.
    • (1993) Cell , vol.75 , pp. 543-555
    • Palladino, F.1    Laroche, T.2    Gilson, E.3    Axelrod, A.4    Pillus, L.5    Gasser, S.M.6
  • 104
    • 0033612287 scopus 로고    scopus 로고
    • Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast
    • Martin S.G., Laroche T., Suka N., Grunstein M., Gasser S.M. Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell. 97:1999;621-633.
    • (1999) Cell , vol.97 , pp. 621-633
    • Martin, S.G.1    Laroche, T.2    Suka, N.3    Grunstein, M.4    Gasser, S.M.5
  • 105
    • 0027184524 scopus 로고
    • Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage
    • Renauld H., Aparicio O.M., Zierath P.D., Billington B.L., Chhablani S.K., Gottschling D.E. Silent domains are assembled continuously from the telomere and are defined by promoter distance and strength, and by SIR3 dosage. Genes Dev. 7:1993;1133-1145.
    • (1993) Genes Dev. , vol.7 , pp. 1133-1145
    • Renauld, H.1    Aparicio, O.M.2    Zierath, P.D.3    Billington, B.L.4    Chhablani, S.K.5    Gottschling, D.E.6
  • 106
    • 0029817763 scopus 로고    scopus 로고
    • Spreading of transcriptional repressor SIR3 from telomeric heterochromatin
    • Hecht A., Strahl-Bolsinger S., Grunstein M. Spreading of transcriptional repressor SIR3 from telomeric heterochromatin. Nature. 383:1996;92-96.
    • (1996) Nature , vol.383 , pp. 92-96
    • Hecht, A.1    Strahl-Bolsinger, S.2    Grunstein, M.3
  • 107
    • 0034109318 scopus 로고    scopus 로고
    • The Sir proteins of Saccharomyces cerevisiae: Mediators of transcriptional silencing and much more
    • Gartenberg M.R. The Sir proteins of Saccharomyces cerevisiae: mediators of transcriptional silencing and much more. Curr. Opin. Microbiol. 3:2000;132-137.
    • (2000) Curr. Opin. Microbiol. , vol.3 , pp. 132-137
    • Gartenberg, M.R.1
  • 108
    • 0037380112 scopus 로고    scopus 로고
    • Runge, Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespan
    • Ray R.E., Hector N., Roy J.H., Song K.L., Berkner K.W. Runge, Sir3p phosphorylation by the Slt2p pathway effects redistribution of silencing function and shortened lifespan. Nat. Genet. 33:2003;522-526.
    • (2003) Nat. Genet. , vol.33 , pp. 522-526
    • Ray, R.E.1    Hector, N.2    Roy, J.H.3    Song, K.L.4    Berkner, K.W.5
  • 109
    • 0028919756 scopus 로고
    • Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: A molecular model for the formation of heterochromatin in yeast
    • Hecht A., Laroche T., Strahl-Bolsinger S., Gasser S.M., Grunstein M. Histone H3 and H4 N-termini interact with SIR3 and SIR4 proteins: a molecular model for the formation of heterochromatin in yeast. Cell. 80:1995;583-592.
    • (1995) Cell , vol.80 , pp. 583-592
    • Hecht, A.1    Laroche, T.2    Strahl-Bolsinger, S.3    Gasser, S.M.4    Grunstein, M.5
  • 110
    • 0037085264 scopus 로고    scopus 로고
    • Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3
    • Carmen A.A., Milne L., Grunstein M. Acetylation of the yeast histone H4 N terminus regulates its binding to heterochromatin protein SIR3. J. Biol. Chem. 277:2002;4778-4781.
    • (2002) J. Biol. Chem. , vol.277 , pp. 4778-4781
    • Carmen, A.A.1    Milne, L.2    Grunstein, M.3
  • 111
    • 0142134870 scopus 로고    scopus 로고
    • Structure of the coiled-coil dimerization motif of sir4 and its interaction with sir3
    • Chang J.F., Hall B.E., Tanny J.C., Moazed D., Filman D., Ellenberger T. Structure of the coiled-coil dimerization motif of sir4 and its interaction with sir3. Structure. 2003;637-649.
    • (2003) Structure , pp. 637-649
    • Chang, J.F.1    Hall, B.E.2    Tanny, J.C.3    Moazed, D.4    Filman, D.5    Ellenberger, T.6
  • 112
    • 0033603240 scopus 로고    scopus 로고
    • Sir-Ku-itous routes to make ends meet
    • Haber J.E. Sir-Ku-itous routes to make ends meet. Cell. 97:1999;829-832.
    • (1999) Cell , vol.97 , pp. 829-832
    • Haber, J.E.1
  • 113
    • 0033612189 scopus 로고    scopus 로고
    • MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks
    • Mills K.D., Sinclair D.A., Guarente L. MEC1-dependent redistribution of the Sir3 silencing protein from telomeres to DNA double-strand breaks. Cell. 97:1999;609-620.
    • (1999) Cell , vol.97 , pp. 609-620
    • Mills, K.D.1    Sinclair, D.A.2    Guarente, L.3
  • 114
    • 0024977788 scopus 로고
    • Similarity between the transcriptional silencer binding proteins ABF1 and RAP1
    • Diffley J.F., Stillman B. Similarity between the transcriptional silencer binding proteins ABF1 and RAP1. Science. 246:1989;1034-1038.
    • (1989) Science , vol.246 , pp. 1034-1038
    • Diffley, J.F.1    Stillman, B.2
  • 115
    • 0026747761 scopus 로고
    • Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA
    • Lewis J.D., Meehan R.R., Henzel W.J., Maurer-Fogy I., Jeppesen P., Klein F., Bird A. Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA. Cell. 69:1992;905-914.
    • (1992) Cell , vol.69 , pp. 905-914
    • Lewis, J.D.1    Meehan, R.R.2    Henzel, W.J.3    Maurer-Fogy, I.4    Jeppesen, P.5    Klein, F.6    Bird, A.7
  • 116
    • 0029655782 scopus 로고    scopus 로고
    • DNA methylation specifies chromosomal localization of MeCP2
    • Nan X., Tate P., Li E., Bird A. DNA methylation specifies chromosomal localization of MeCP2. Mol. Cell. Biol. 16:1996;414-421.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 414-421
    • Nan, X.1    Tate, P.2    Li, E.3    Bird, A.4
  • 117
    • 0342437491 scopus 로고    scopus 로고
    • MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin
    • Nan X., Campoy F.J., Bird A. MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin. Cell. 88:1997;471-481.
    • (1997) Cell , vol.88 , pp. 471-481
    • Nan, X.1    Campoy, F.J.2    Bird, A.3
  • 120
    • 0035542974 scopus 로고    scopus 로고
    • Methyl CpG-binding proteins and transcriptional repression
    • Wade P.A. Methyl CpG-binding proteins and transcriptional repression. BioEssays. 23:2001;1131-1137.
    • (2001) BioEssays , vol.23 , pp. 1131-1137
    • Wade, P.A.1
  • 121
    • 0027495467 scopus 로고
    • Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2
    • Nan X., Meehan R.R., Bird A. Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2. Nucleic Acids Res. 21:1993;4886-4892.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4886-4892
    • Nan, X.1    Meehan, R.R.2    Bird, A.3
  • 122
    • 0032574977 scopus 로고    scopus 로고
    • Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex
    • Nan X., Ng H.H., Johnson C.A., Laherty C.D., Turner B.M., Eisenman R.N., Bird A. Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex. Nature. 393:1998;386-389.
    • (1998) Nature , vol.393 , pp. 386-389
    • Nan, X.1    Ng, H.H.2    Johnson, C.A.3    Laherty, C.D.4    Turner, B.M.5    Eisenman, R.N.6    Bird, A.7
  • 123
    • 0033152745 scopus 로고    scopus 로고
    • The methyl-CpG binding transcriptional repressor MeCP2 stably associates with nucleosomal DNA
    • Chandler S.P., Guschin D., Landsberger N., Wolffe A.P. The methyl-CpG binding transcriptional repressor MeCP2 stably associates with nucleosomal DNA. Biochemistry. 38:1999;7008-7018.
    • (1999) Biochemistry , vol.38 , pp. 7008-7018
    • Chandler, S.P.1    Guschin, D.2    Landsberger, N.3    Wolffe, A.P.4
  • 124
    • 0038677661 scopus 로고    scopus 로고
    • Formation of higher-order secondary and tertiary chromatin structures by genomic mouse mammary tumor virus promoters
    • Georgel P.T., Fletcher T.M., Hager G.L., Hansen J.C. Formation of higher-order secondary and tertiary chromatin structures by genomic mouse mammary tumor virus promoters. Genes Dev. 17:2003;1617-1629.
    • (2003) Genes Dev. , vol.17 , pp. 1617-1629
    • Georgel, P.T.1    Fletcher, T.M.2    Hager, G.L.3    Hansen, J.C.4
  • 125
    • 0034882165 scopus 로고    scopus 로고
    • Higher order folding of heterochromatin: Protein bridges span the nucleosome arrays
    • Grigoryev S.A. Higher order folding of heterochromatin: protein bridges span the nucleosome arrays. Biochem. Cell. Biol. 79:2001;227-241.
    • (2001) Biochem. Cell. Biol. , vol.79 , pp. 227-241
    • Grigoryev, S.A.1
  • 126
    • 0343415609 scopus 로고    scopus 로고
    • The glucocorticoid receptor: Rapid exchange with regulatory sites in living cells
    • McNally J.G., Muller W.G., Walker D., Wolford R., Hager G.L. The glucocorticoid receptor: rapid exchange with regulatory sites in living cells. Science. 287:2000;1262-1265.
    • (2000) Science , vol.287 , pp. 1262-1265
    • McNally, J.G.1    Muller, W.G.2    Walker, D.3    Wolford, R.4    Hager, G.L.5


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