메뉴 건너뛰기




Volumn 181, Issue 2, 1999, Pages 240-250

Nuclear structure/gene expression interrelationships

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS; CELL STRUCTURE; CHROMATIN; GENE EXPRESSION; GENE SEQUENCE; GENETIC TRANSCRIPTION; HUMAN; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; REVIEW;

EID: 0032826056     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199911)181:2<240::AID-JCP6>3.0.CO;2-K     Document Type: Review
Times cited : (12)

References (126)
  • 1
    • 0028246161 scopus 로고
    • E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators
    • Arany Z, Sellers WR, Livingston DM, Eckner R. 1994. E1A-associated p300 and CREB-associated CBP belong to a conserved family of coactivators (letter). Cell 77:799-800.
    • (1994) Cell , vol.77 , pp. 799-800
    • Arany, Z.1    Sellers, W.R.2    Livingston, D.M.3    Eckner, R.4
  • 3
    • 0025312172 scopus 로고
    • Factors that promote progressive development of the osteoblast phenotype in cultured fetal rat calvaria cells
    • Aronow MA, Gerstenfeld LC, Owen TA, Tassinari MS, Stein GS, Lian JB. 1990. Factors that promote progressive development of the osteoblast phenotype in cultured fetal rat calvaria cells. J Cell Physiol 143:213-221.
    • (1990) J Cell Physiol , vol.143 , pp. 213-221
    • Aronow, M.A.1    Gerstenfeld, L.C.2    Owen, T.A.3    Tassinari, M.S.4    Stein, G.S.5    Lian, J.B.6
  • 4
    • 0029953941 scopus 로고    scopus 로고
    • An AML-1 consensus sequence binds an osteoblast-specific complex and transcriptionally activates the osteocalcin gene
    • Banerjee C, Hiebert SW, Stein JL, Lian JB, Stein GS. 1996. An AML-1 consensus sequence binds an osteoblast-specific complex and transcriptionally activates the osteocalcin gene. Proc Natl Acad Sci USA 93:4968-4973.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4968-4973
    • Banerjee, C.1    Hiebert, S.W.2    Stein, J.L.3    Lian, J.B.4    Stein, G.S.5
  • 5
    • 0029585553 scopus 로고
    • Stimulation of c-Jun activity by CBP: C-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro
    • Bannister AJ, Oehler T, Wilhelm D, Angel P, Kouzarides T. 1995. Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/73 are required for CBP induced stimulation in vivo and CBP binding in vitro. Oncogene 11:2509-2514.
    • (1995) Oncogene , vol.11 , pp. 2509-2514
    • Bannister, A.J.1    Oehler, T.2    Wilhelm, D.3    Angel, P.4    Kouzarides, T.5
  • 6
    • 0016861690 scopus 로고
    • Nuclear protein matrix: Association with newly synthesized DNA
    • Berezney R and Coffey DS. 1975. Nuclear protein matrix: association with newly synthesized DNA. Science 189:291-292.
    • (1975) Science , vol.189 , pp. 291-292
    • Berezney, R.1    Coffey, D.S.2
  • 8
    • 0028034042 scopus 로고
    • Association of nuclear matrix antigens with exon-containing splicing complexes
    • Blencowe BJ, Nickerson JA, Issner R, Penman S, Sharp PA. 1994. Association of nuclear matrix antigens with exon-containing splicing complexes. J Cell Biol 127:593-607.
    • (1994) J Cell Biol , vol.127 , pp. 593-607
    • Blencowe, B.J.1    Nickerson, J.A.2    Issner, R.3    Penman, S.4    Sharp, P.A.5
  • 9
    • 0030796314 scopus 로고    scopus 로고
    • Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies
    • Boddy MN, Duprez E, Borden KL, Freemont PS. 1997. Surface residue mutations of the PML RING finger domain alter the formation of nuclear matrix-associated PML bodies. J Cell Sci 110:2197-2205.
    • (1997) J Cell Sci , vol.110 , pp. 2197-2205
    • Boddy, M.N.1    Duprez, E.2    Borden, K.L.3    Freemont, P.S.4
  • 11
    • 0028589335 scopus 로고
    • In vivo occupancy of the vitamin D responsive element in the osteocalcin gene supports vitamin D-dependent transcriptional upregulation in intact cells
    • Breen EC, van Wijnen AJ, Lian JB, Stein GS, Stein JL. 1994. In vivo occupancy of the vitamin D responsive element in the osteocalcin gene supports vitamin D-dependent transcriptional upregulation in intact cells. Proc Natl Acad Sci USA 91:12902-12906.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12902-12906
    • Breen, E.C.1    Van Wijnen, A.J.2    Lian, J.B.3    Stein, G.S.4    Stein, J.L.5
  • 12
    • 0025297904 scopus 로고
    • Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate
    • Bresnick EH, John S, Berard DS, Lefebvre P, Hager GL. 1990. Glucocorticoid receptor-dependent disruption of a specific nucleosome on the mouse mammary tumor virus promoter is prevented by sodium butyrate. Proc Natl Acad Sci USA 87:3977-3981.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3977-3981
    • Bresnick, E.H.1    John, S.2    Berard, D.S.3    Lefebvre, P.4    Hager, G.L.5
  • 13
    • 0025756207 scopus 로고
    • Histone hyperacetylation does not alter the position or stability of phased nucleosomes on the MMTV LTR
    • Bresnick EH, John S, Hager GL. 1991. Histone hyperacetylation does not alter the position or stability of phased nucleosomes on the MMTV LTR. Biochemistry 30:3490-3497.
    • (1991) Biochemistry , vol.30 , pp. 3490-3497
    • Bresnick, E.H.1    John, S.2    Hager, G.L.3
  • 14
    • 0026733493 scopus 로고
    • Specificity of Zea mays histone deacetylase is regulated by phosphorylation
    • Brosch G, Georgieva EI, Lopez-Rodas G, Lindner H, Loidl P. 1992. Specificity of Zea mays histone deacetylase is regulated by phosphorylation. J Biol Chem 267:20561-20564.
    • (1992) J Biol Chem , vol.267 , pp. 20561-20564
    • Brosch, G.1    Georgieva, E.I.2    Lopez-Rodas, G.3    Lindner, H.4    Loidl, P.5
  • 15
    • 0029984469 scopus 로고    scopus 로고
    • Tetrahymena histone acetyltransferase A: A homolog to yeast Gcn5p linking histone acetylation to gene activation
    • Brownell JE, Zhou J, Ranalli T, Kobayashi R, Edmondson DG, Roth SY, Allis CD. 1996. Tetrahymena histone acetyltransferase A: a homolog to yeast Gcn5p linking histone acetylation to gene activation. Cell 84:843-851.
    • (1996) Cell , vol.84 , pp. 843-851
    • Brownell, J.E.1    Zhou, J.2    Ranalli, T.3    Kobayashi, R.4    Edmondson, D.G.5    Roth, S.Y.6    Allis, C.D.7
  • 16
    • 0028314013 scopus 로고
    • A multisubunit complex containing the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated from yeast
    • Cairns BR, Kim YJ, Sayre MH, Laurent BC, Kornberg RD. 1994. A multisubunit complex containing the SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated from yeast. Proc Natl Acad Sci USA 91:1950-1954.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1950-1954
    • Cairns, B.R.1    Kim, Y.J.2    Sayre, M.H.3    Laurent, B.C.4    Kornberg, R.D.5
  • 18
    • 0032214123 scopus 로고    scopus 로고
    • Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF
    • Cairns BR, Erdjument-Bromage H, Tempst P, Winston F, Kornberg RD. 1998. Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF. Mol Cell 2:639-651.
    • (1998) Mol Cell , vol.2 , pp. 639-651
    • Cairns, B.R.1    Erdjument-Bromage, H.2    Tempst, P.3    Winston, F.4    Kornberg, R.D.5
  • 21
    • 0030740253 scopus 로고    scopus 로고
    • Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300
    • Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM. 1997. Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell 90:569-580.
    • (1997) Cell , vol.90 , pp. 569-580
    • Chen, H.1    Lin, R.J.2    Schiltz, R.L.3    Chakravarti, D.4    Nash, A.5    Nagy, L.6    Privalsky, M.L.7    Nakatani, Y.8    Evans, R.M.9
  • 22
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD and Evans RM. 1995. A transcriptional co-repressor that interacts with nuclear hormone receptors [see comments]. Nature 377:454-457.
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 24
    • 0022409258 scopus 로고
    • A human histone H4 gene exhibits cell cycle-dependent changes in chromatin structure that correlate with its expression
    • Chrysogelos S, Riley DE, Stein G, Stein J. 1985. A human histone H4 gene exhibits cell cycle-dependent changes in chromatin structure that correlate with its expression. Proc Natl Acad Sci USA 82:7535-7539.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 7535-7539
    • Chrysogelos, S.1    Riley, D.E.2    Stein, G.3    Stein, J.4
  • 25
    • 0030034051 scopus 로고    scopus 로고
    • XIST RNA paints the inactive X chromosome at interphase: Evidence for a novel RNA involved in nuclear/chromosome structure
    • Clemson CM, McNeil JA, Willard HF, Lawrence JB. 1996. XIST RNA paints the inactive X chromosome at interphase: evidence for a novel RNA involved in nuclear/chromosome structure. J Cell Biol 132:259-275.
    • (1996) J Cell Biol , vol.132 , pp. 259-275
    • Clemson, C.M.1    McNeil, J.A.2    Willard, H.F.3    Lawrence, J.B.4
  • 26
    • 0028467446 scopus 로고
    • Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/ SNF complex
    • Cote J, Quinn J, Workman JL, Peterson CL. 1994. Stimulation of GAL4 derivative binding to nucleosomal DNA by the yeast SWI/ SNF complex. Science 265:53-60.
    • (1994) Science , vol.265 , pp. 53-60
    • Cote, J.1    Quinn, J.2    Workman, J.L.3    Peterson, C.L.4
  • 27
    • 0032574802 scopus 로고    scopus 로고
    • Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding
    • Cote J, Peterson CL, Workman JL. 1998. Perturbation of nucleosome core structure by the SWI/SNF complex persists after its detachment, enhancing subsequent transcription factor binding. Proc Natl Acad Sci USA 95:4947-4952.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4947-4952
    • Cote, J.1    Peterson, C.L.2    Workman, J.L.3
  • 29
    • 0031214069 scopus 로고    scopus 로고
    • Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin
    • Davie JR. 1997. Nuclear matrix, dynamic histone acetylation and transcriptionally active chromatin. Mol Biol Rep 24:197-207.
    • (1997) Mol Biol Rep , vol.24 , pp. 197-207
    • Davie, J.R.1
  • 30
    • 0025060802 scopus 로고
    • DNA sequences in the rat osteocalcin gene that bind the 1,25-dihydroxyvitamin D3 receptor and confer responsive to 1,25-dihydroxyvitamin D3
    • Demay MB, Gerardi JM, DeLuca HF, Kronenberg HM. 1990. DNA sequences in the rat osteocalcin gene that bind the 1,25-dihydroxyvitamin D3 receptor and confer responsive to 1,25-dihydroxyvitamin D3. Proc Natl Acad Sci USA 87:369-373.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 369-373
    • Demay, M.B.1    Gerardi, J.M.2    DeLuca, H.F.3    Kronenberg, H.M.4
  • 31
    • 0028927556 scopus 로고
    • Two distinct osteoblast-specific cis-acting elements control expression of a mouse osteocalcin gene
    • Ducy P and Karsenty G. 1995. Two distinct osteoblast-specific cis-acting elements control expression of a mouse osteocalcin gene. Mol Cell Biol 15:1858-1869.
    • (1995) Mol Cell Biol , vol.15 , pp. 1858-1869
    • Ducy, P.1    Karsenty, G.2
  • 32
    • 0025372116 scopus 로고
    • Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation
    • Dworetzky SI, Fey EG, Penman S, Lian JB, Stein JL, Stein GS. 1990. Progressive changes in the protein composition of the nuclear matrix during rat osteoblast differentiation. Proc Natl Acad Sci USA 87:4605-4609.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4605-4609
    • Dworetzky, S.I.1    Fey, E.G.2    Penman, S.3    Lian, J.B.4    Stein, J.L.5    Stein, G.S.6
  • 34
    • 0028179010 scopus 로고
    • A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
    • Dyck JA, Maul GG, Miller WH, Chen JD, Kakizuka A, Evans RM. 1994. A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein. Cell 76:333-343.
    • (1994) Cell , vol.76 , pp. 333-343
    • Dyck, J.A.1    Maul, G.G.2    Miller, W.H.3    Chen, J.D.4    Kakizuka, A.5    Evans, R.M.6
  • 35
    • 0029758906 scopus 로고    scopus 로고
    • Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
    • Fondell JD, Ge H, Roeder RG. 1996. Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex. Proc Natl Acad Sci USA 93:8329-8333.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8329-8333
    • Fondell, J.D.1    Ge, H.2    Roeder, R.G.3
  • 36
    • 0029616633 scopus 로고
    • The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B
    • Frank R, Zhang J, Uchida H, Meyers S, Hiebert SW, Nimer SD. 1995. The AML1/ETO fusion protein blocks transactivation of the GM-CSF promoter by AML1B. Oncogene 11:2667-2674.
    • (1995) Oncogene , vol.11 , pp. 2667-2674
    • Frank, R.1    Zhang, J.2    Uchida, H.3    Meyers, S.4    Hiebert, S.W.5    Nimer, S.D.6
  • 37
    • 0026050308 scopus 로고
    • Histone acetylation in Zea mays. II. Biological significance of post-translational histone acetylation during embryo germination
    • Georgieva EI, Lopez-Rodas G, Sendra R, Grobner P, Loidl P. 1991. Histone acetylation in Zea mays. II. Biological significance of post-translational histone acetylation during embryo germination. J Biol Chem 266:18751-18760.
    • (1991) J Biol Chem , vol.266 , pp. 18751-18760
    • Georgieva, E.I.1    Lopez-Rodas, G.2    Sendra, R.3    Grobner, P.4    Loidl, P.5
  • 38
    • 0025107396 scopus 로고
    • Tissue specificity of the hormonal response in sex accessory tissues is associated with nuclear matrix protein patterns
    • Getzenberg RH, Coffey DS. 1990. Tissue specificity of the hormonal response in sex accessory tissues is associated with nuclear matrix protein patterns. Mol Endocrinol 4:1336-1342.
    • (1990) Mol Endocrinol , vol.4 , pp. 1336-1342
    • Getzenberg, R.H.1    Coffey, D.S.2
  • 39
    • 0025036184 scopus 로고
    • Identification and functional characterization of the human T-cell receptor β gene transcriptional enhancer: Common nuclear proteins interact with the transcriptional regulatory elements of the T-cell receptor a and β genes
    • Gottschalk LR, Leiden JM. 1990. Identification and functional characterization of the human T-cell receptor β gene transcriptional enhancer: common nuclear proteins interact with the transcriptional regulatory elements of the T-cell receptor a and β genes. Mol Cell Biol 10:5486-5495.
    • (1990) Mol Cell Biol , vol.10 , pp. 5486-5495
    • Gottschalk, L.R.1    Leiden, J.M.2
  • 45
    • 0028144413 scopus 로고
    • Regulation of the T-cell receptor delta enhancer by functional cooperation between c-Myb and core-binding factors
    • Hernandez-Munain C and Krangel MS. 1994. Regulation of the T-cell receptor delta enhancer by functional cooperation between c-Myb and core-binding factors. Mol Cell Biol 14:473-483.
    • (1994) Mol Cell Biol , vol.14 , pp. 473-483
    • Hernandez-Munain, C.1    Krangel, M.S.2
  • 47
    • 0024342647 scopus 로고
    • A T-cell-specific transcriptional enhancer element 3' of Ca in the human T-cell receptor a locus
    • Ho I-C, Yang L-H, Morle G, Leiden JM. 1989. A T-cell-specific transcriptional enhancer element 3' of Ca in the human T-cell receptor a locus. Proc Natl Acad Sci USA 86:6714-6718.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 6714-6718
    • Ho, I.-C.1    Yang, L.-H.2    Morle, G.3    Leiden, J.M.4
  • 48
    • 0028587853 scopus 로고
    • Transcriptional control of the tissue-specific, developmentally regulated osteocalcin gene requires a binding motif for the Msx family of homeodomain proteins
    • Hoffmann HM, Catron KM, van Wijnen AJ, McCabe LR, Lian JB, Stein GS, Stein JL. 1994. Transcriptional control of the tissue-specific, developmentally regulated osteocalcin gene requires a binding motif for the Msx family of homeodomain proteins. Proc Natl Acad Sci USA 91:12887-12891.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12887-12891
    • Hoffmann, H.M.1    Catron, K.M.2    Van Wijnen, A.J.3    McCabe, L.R.4    Lian, J.B.5    Stein, G.S.6    Stein, J.L.7
  • 50
    • 0029943273 scopus 로고    scopus 로고
    • Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera
    • Htun H, Barsony J, Renyi I, Gould DL, Hager GL. 1996. Visualization of glucocorticoid receptor translocation and intranuclear organization in living cells with a green fluorescent protein chimera. Proc Natl Acad Sci USA 93:4845-4850.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4845-4850
    • Htun, H.1    Barsony, J.2    Renyi, I.3    Gould, D.L.4    Hager, G.L.5
  • 51
    • 0032470510 scopus 로고    scopus 로고
    • Energy-dependent chromatin remodelers: Complex complexes and their components
    • Imbalzano AN. 1998. Energy-dependent chromatin remodelers: complex complexes and their components. Crit Rev Eukaryot Gene Expr 8:225-255.
    • (1998) Crit Rev Eukaryot Gene Expr , vol.8 , pp. 225-255
    • Imbalzano, A.N.1
  • 52
    • 0031444148 scopus 로고    scopus 로고
    • ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor
    • Ito T, Bulger M, Pazin MJ, Kobayashi R, Kadonaga JT. 1997. ACF, an ISWI-containing and ATP-utilizing chromatin assembly and remodeling factor. Cell 90:145-155.
    • (1997) Cell , vol.90 , pp. 145-155
    • Ito, T.1    Bulger, M.2    Pazin, M.J.3    Kobayashi, R.4    Kadonaga, J.T.5
  • 53
  • 56
    • 0028093378 scopus 로고
    • Nucleosome disruption and enhancement of activator binding by a human SWI/SNF complex
    • Kwon H, Imbalzano AN, Khavari PA, Kingston RE, Green MR. 1994. Nucleosome disruption and enhancement of activator binding by a human SWI/SNF complex. Nature 370:477-481.
    • (1994) Nature , vol.370 , pp. 477-481
    • Kwon, H.1    Imbalzano, A.N.2    Khavari, P.A.3    Kingston, R.E.4    Green, M.R.5
  • 57
    • 0032562608 scopus 로고    scopus 로고
    • Structure and function in the nucleus
    • Lamond AI and Earnshaw WC. 1998. Structure and function in the nucleus. Science 280:547-553.
    • (1998) Science , vol.280 , pp. 547-553
    • Lamond, A.I.1    Earnshaw, W.C.2
  • 58
    • 0024498788 scopus 로고
    • Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization
    • Lawrence JB, Singer RH, Marselle LM. 1989. Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell 57:493-502.
    • (1989) Cell , vol.57 , pp. 493-502
    • Lawrence, J.B.1    Singer, R.H.2    Marselle, L.M.3
  • 60
    • 0028136578 scopus 로고
    • AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization
    • Levanon D, Negreanu V, Bernstein Y, Bar-Am I, Avivi L, Groner Y. 1994. AML1, AML2, and AML3, the human members of the runt domain gene-family: cDNA structure, expression, and chromosomal localization. Genomics 23:425-432.
    • (1994) Genomics , vol.23 , pp. 425-432
    • Levanon, D.1    Negreanu, V.2    Bernstein, Y.3    Bar-Am, I.4    Avivi, L.5    Groner, Y.6
  • 61
    • 0026594997 scopus 로고
    • Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum
    • Lopez-Rodas G, Brosch G, Golderer G, Lindner H, Grobner P, Loidl P. 1992. Enzymes involved in the dynamic equilibrium of core histone acetylation of Physarum polycephalum. FEBS Lett 296:82-86.
    • (1992) FEBS Lett , vol.296 , pp. 82-86
    • Lopez-Rodas, G.1    Brosch, G.2    Golderer, G.3    Lindner, H.4    Grobner, P.5    Loidl, P.6
  • 62
    • 0032504059 scopus 로고    scopus 로고
    • Activated RSC-nucleosome complex and persistently altered form of the nucleosome
    • Lorch Y, Cairns BR, Zhang M, Kornberg RD. 1998. Activated RSC-nucleosome complex and persistently altered form of the nucleosome. Cell 94:29-34.
    • (1998) Cell , vol.94 , pp. 29-34
    • Lorch, Y.1    Cairns, B.R.2    Zhang, M.3    Kornberg, R.D.4
  • 63
    • 0025220704 scopus 로고
    • Vitamin D-mediated modifications in protein-DNA interactions at two promoter elements of the osteocalcin gene
    • Markose ER, Stein JL, Stein GS, Lian JB. 1990. Vitamin D-mediated modifications in protein-DNA interactions at two promoter elements of the osteocalcin gene. Proc Natl Acad Sci USA 87:1701-1705.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1701-1705
    • Markose, E.R.1    Stein, J.L.2    Stein, G.S.3    Lian, J.B.4
  • 64
    • 0032521368 scopus 로고    scopus 로고
    • Targeting of the YY1 transcription factor to the nucleolus and the nuclear matrix in situ: The C-terminus is a principal determinant for nuclear trafficking
    • McNeil S, Guo B, Stein JL, Lian JB, Bushmeyer S, Seto E, Atchison ML, Penman S, van Wijnen AJ, Stein GS. 1998. Targeting of the YY1 transcription factor to the nucleolus and the nuclear matrix in situ: the C-terminus is a principal determinant for nuclear trafficking. J Cell Biochem 68:500-510.
    • (1998) J Cell Biochem , vol.68 , pp. 500-510
    • McNeil, S.1    Guo, B.2    Stein, J.L.3    Lian, J.B.4    Bushmeyer, S.5    Seto, E.6    Atchison, M.L.7    Penman, S.8    Van Wijnen, A.J.9    Stein, G.S.10
  • 65
    • 0028874666 scopus 로고
    • The tissue-specific nuclear matrix protein, NMP-2, is a member of the AML/CBF/PEBP2/runt domain transcription factor family: Interactions with the osteocalcin gene promoter
    • Merriman HL, van Wijnen AJ, Hiebert S, Bidwell JP, Fey E, Lian J, Stein J, Stein GS. 1995. The tissue-specific nuclear matrix protein, NMP-2, is a member of the AML/CBF/PEBP2/runt domain transcription factor family: interactions with the osteocalcin gene promoter. Biochemistry 34:13125-13132.
    • (1995) Biochemistry , vol.34 , pp. 13125-13132
    • Merriman, H.L.1    Van Wijnen, A.J.2    Hiebert, S.3    Bidwell, J.P.4    Fey, E.5    Lian, J.6    Stein, J.7    Stein, G.S.8
  • 66
    • 0029810924 scopus 로고    scopus 로고
    • AML-2 is a potential target for transcriptional regulation by the t(8;21) and t(12;21) fusion proteins in acute leukemia
    • Meyers S, Lenny N, Sun W-H, Hiebert SW. 1996. AML-2 is a potential target for transcriptional regulation by the t(8;21) and t(12;21) fusion proteins in acute leukemia. Oncogene 13:303-312.
    • (1996) Oncogene , vol.13 , pp. 303-312
    • Meyers, S.1    Lenny, N.2    Sun, W.-H.3    Hiebert, S.W.4
  • 67
    • 0025746321 scopus 로고
    • T(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1
    • Miyoshi H, Shimizu K, Kozu T, Maseki N, Kaneko Y, Ohki M. 1991. t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are clustered within a limited region of a single gene, AML1. Proc Natl Acad Sci USA 88:10431-10434.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10431-10434
    • Miyoshi, H.1    Shimizu, K.2    Kozu, T.3    Maseki, N.4    Kaneko, Y.5    Ohki, M.6
  • 69
    • 0001421052 scopus 로고
    • Specific nucleosomal organization supports developmentally regulated expression of the osteocalcin gene
    • Abstract
    • Montecino M, Lian J, Stein G, Stein J. 1994a. Specific nucleosomal organization supports developmentally regulated expression of the osteocalcin gene. J Bone Miner Res 9:S352 (Abstract).
    • (1994) J Bone Miner Res , vol.9
    • Montecino, M.1    Lian, J.2    Stein, G.3    Stein, J.4
  • 70
    • 0028157614 scopus 로고
    • DNase I hypersensitive sites in promoter elements associated with basal and vitamin D dependent transcription of the bone- Specific osteocalcin gene
    • Montecino M, Pockwinse S, Lian J, Stein G, Stein J. 1994b. DNase I hypersensitive sites in promoter elements associated with basal and vitamin D dependent transcription of the bone- specific osteocalcin gene. Biochemistry 33:348-353.
    • (1994) Biochemistry , vol.33 , pp. 348-353
    • Montecino, M.1    Pockwinse, S.2    Lian, J.3    Stein, G.4    Stein, J.5
  • 71
    • 0029883812 scopus 로고    scopus 로고
    • Changes in chromatin structure support constitutive and developmentally regulated transcription of the bone-specific osteocalcin gene in osteoblastic cells
    • Montecino M, Lian J, Stein G, Stein J. 1996. Changes in chromatin structure support constitutive and developmentally regulated transcription of the bone-specific osteocalcin gene in osteoblastic cells. Biochemistry 35:5093-5102.
    • (1996) Biochemistry , vol.35 , pp. 5093-5102
    • Montecino, M.1    Lian, J.2    Stein, G.3    Stein, J.4
  • 72
    • 0033604835 scopus 로고    scopus 로고
    • Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo
    • Montecino M, Frenkel B, van Wijnen AJ, Lian JB, Stein GS, Stein JL. 1999. Chromatin hyperacetylation abrogates vitamin D-mediated transcriptional upregulation of the tissue-specific osteocalcin gene in vivo. Biochemistry 38:1338-1345.
    • (1999) Biochemistry , vol.38 , pp. 1338-1345
    • Montecino, M.1    Frenkel, B.2    Van Wijnen, A.J.3    Lian, J.B.4    Stein, G.S.5    Stein, J.L.6
  • 73
    • 0019142257 scopus 로고
    • Localization of SV40 genes within supercoiled loop domains
    • Nelkin BD, Pardoll DM, Vogelstein B. 1980. Localization of SV40 genes within supercoiled loop domains. Nucl Acids Res 8:5623-5633.
    • (1980) Nucl Acids Res , vol.8 , pp. 5623-5633
    • Nelkin, B.D.1    Pardoll, D.M.2    Vogelstein, B.3
  • 74
    • 0031803402 scopus 로고    scopus 로고
    • The nucleus: A target site for parathyroid hormone-related peptide (PTHrP) action
    • Nguyen MTA and Karaplis AC. 1998. The nucleus: a target site for parathyroid hormone-related peptide (PTHrP) action. J Cell Biochem 70:193-199.
    • (1998) J Cell Biochem , vol.70 , pp. 193-199
    • Nguyen, M.T.A.1    Karaplis, A.C.2
  • 75
    • 0025261920 scopus 로고
    • Immunolocalization in three dimensions: Immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections
    • Nickerson JA, He DC, Krochmalnic G, Penman S. 1990. Immunolocalization in three dimensions: immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections. Proc Natl Acad Sci USA 87:2259-2263.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 2259-2263
    • Nickerson, J.A.1    He, D.C.2    Krochmalnic, G.3    Penman, S.4
  • 77
    • 0030013142 scopus 로고    scopus 로고
    • Transcriptional regulation of interleukin-3 expression in megakaryocytes
    • Nimer S, Zhang J, Avraham H, Miyazaki Y. 1996. Transcriptional regulation of interleukin-3 expression in megakaryocytes. Blood 88:66-74.
    • (1996) Blood , vol.88 , pp. 66-74
    • Nimer, S.1    Zhang, J.2    Avraham, H.3    Miyazaki, Y.4
  • 78
    • 0028066779 scopus 로고
    • PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2β/CBFβ proto-oncoproteins, regulates the murine myeloperoxidase and neutrophil elastase genes in immature myeloid cells
    • Nuchprayoon I, Meyers S, Scott LM, Suzow J, Hiebert SW, Friedman AD. 1994. PEBP2/CBF, the murine homolog of the human myeloid AML1 and PEBP2β/CBFβ proto-oncoproteins, regulates the murine myeloperoxidase and neutrophil elastase genes in immature myeloid cells. Mol Cell Biol 14:5558-5568.
    • (1994) Mol Cell Biol , vol.14 , pp. 5558-5568
    • Nuchprayoon, I.1    Meyers, S.2    Scott, L.M.3    Suzow, J.4    Hiebert, S.W.5    Friedman, A.D.6
  • 79
    • 0029886810 scopus 로고    scopus 로고
    • Interaction of the co-activator CBP with Myb proteins: Effects on Myb- Specific transactivation and on the cooperativity with NF-
    • Oelgeschlager M, Janknecht R, Krieg J, Schreek S, Luscher B. 1996. Interaction of the co-activator CBP with Myb proteins: effects on Myb- specific transactivation and on the cooperativity with NF-EMBO J 15:2771-2780.
    • (1996) EMBO J , vol.15 , pp. 2771-2780
    • Oelgeschlager, M.1    Janknecht, R.2    Krieg, J.3    Schreek, S.4    Luscher, B.5
  • 80
    • 0030606239 scopus 로고    scopus 로고
    • The transcriptional coactivators p300 and CBP are histone acetyltransferases
    • Ogryzko W, Schiltz RL, Russanova V, Howard BH, Nakatani Y. 1996. The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87:953-959.
    • (1996) Cell , vol.87 , pp. 953-959
    • Ogryzko, W.1    Schiltz, R.L.2    Russanova, V.3    Howard, B.H.4    Nakatani, Y.5
  • 81
    • 0025316785 scopus 로고
    • Progressive development of the rat osteoblast phenotype in vitro: Reciprocal relationships in expression of genes associated with osteoblast proliferation and differentiation during formation of the bone extracellular matrix
    • Owen TA, Aronow M, Shalhoub V, Barone LM, Wilming L, Tassinari MS, Kennedy MB, Pockwinse S, Lian JB, Stein GS. 1990. Progressive development of the rat osteoblast phenotype in vitro: reciprocal relationships in expression of genes associated with osteoblast proliferation and differentiation during formation of the bone extracellular matrix. J Cell Physiol 143:420-430.
    • (1990) J Cell Physiol , vol.143 , pp. 420-430
    • Owen, T.A.1    Aronow, M.2    Shalhoub, V.3    Barone, L.M.4    Wilming, L.5    Tassinari, M.S.6    Kennedy, M.B.7    Pockwinse, S.8    Lian, J.B.9    Stein, G.S.10
  • 82
    • 0031736990 scopus 로고    scopus 로고
    • The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes
    • Papoulas O, Beek SJ, Moseley SL, McCallum CM, Sarte M, Shearn A, Tamkun JW. 1998. The Drosophila trithorax group proteins BRM, ASH1 and ASH2 are subunits of distinct protein complexes. Development 125:3955-3966.
    • (1998) Development , vol.125 , pp. 3955-3966
    • Papoulas, O.1    Beek, S.J.2    Moseley, S.L.3    McCallum, C.M.4    Sarte, M.5    Shearn, A.6    Tamkun, J.W.7
  • 83
    • 0023228891 scopus 로고
    • Protein-DNA interactions in vivo upstream of a cell cycle- Regulated human H4 histone gene
    • Pauli U, Chrysogelos S, Stein G, Stein J, Nick H. 1987. Protein-DNA interactions in vivo upstream of a cell cycle- regulated human H4 histone gene. Science 236:1308-1311.
    • (1987) Science , vol.236 , pp. 1308-1311
    • Pauli, U.1    Chrysogelos, S.2    Stein, G.3    Stein, J.4    Nick, H.5
  • 84
    • 0032508694 scopus 로고    scopus 로고
    • Subunits of the yeast SWI/SNF complex are members of the actin- Related protein (ARP) family
    • Peterson CL, Zhao Y, Chait BT. 1998. Subunits of the yeast SWI/SNF complex are members of the actin- related protein (ARP) family. J Biol Chem 273:23641-23644.
    • (1998) J Biol Chem , vol.273 , pp. 23641-23644
    • Peterson, C.L.1    Zhao, Y.2    Chait, B.T.3
  • 85
    • 0030589682 scopus 로고    scopus 로고
    • The localization of sites containing nascent RNA and splicing factors
    • Pombo A, Cook PR. 1996. The localization of sites containing nascent RNA and splicing factors. Exp Cell Res 229:201-203.
    • (1996) Exp Cell Res , vol.229 , pp. 201-203
    • Pombo, A.1    Cook, P.R.2
  • 86
    • 0030971868 scopus 로고    scopus 로고
    • Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix
    • Reyes J-C, Muchardt C, Yaniv M. 1997. Components of the human SWI/SNF complex are enriched in active chromatin and are associated with the nuclear matrix. J Cell Biol 137:263-274.
    • (1997) J Cell Biol , vol.137 , pp. 263-274
    • Reyes, J.-C.1    Muchardt, C.2    Yaniv, M.3
  • 87
    • 0020077227 scopus 로고
    • The ovalbumin gene is associated with the nuclear matrix of chicken oviduct cells
    • Robinson SI, Nelkin BD, Vogelstein B. 1982. The ovalbumin gene is associated with the nuclear matrix of chicken oviduct cells. Cell 28:99-106.
    • (1982) Cell , vol.28 , pp. 99-106
    • Robinson, S.I.1    Nelkin, B.D.2    Vogelstein, B.3
  • 89
    • 0025314719 scopus 로고
    • Adenovirus terminal protein mediates both nuclear matrix association and efficient transcription of adenovirus DNA
    • Schaack J, Ho WY, Freimuth P, Shenk T. 1990. Adenovirus terminal protein mediates both nuclear matrix association and efficient transcription of adenovirus DNA. Genes Dev 4:1197-1208.
    • (1990) Genes Dev , vol.4 , pp. 1197-1208
    • Schaack, J.1    Ho, W.Y.2    Freimuth, P.3    Shenk, T.4
  • 90
    • 0032504102 scopus 로고    scopus 로고
    • Human SWI/SNF interconverts a nucleosome between its base state and a stable remodeled state
    • Schnitzler G, Sif S, Kingston RE. 1998. Human SWI/SNF interconverts a nucleosome between its base state and a stable remodeled state. Cell 94:17-27.
    • (1998) Cell , vol.94 , pp. 17-27
    • Schnitzler, G.1    Sif, S.2    Kingston, R.E.3
  • 91
    • 0000976047 scopus 로고
    • Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization
    • Silver PA, Keegan LP, Ptashine M. 1984. Amino terminus of the yeast GAL4 gene product is sufficient for nuclear localization. Proc Natl Acad Sci USA 81:5951-5955.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5951-5955
    • Silver, P.A.1    Keegan, L.P.2    Ptashine, M.3
  • 94
    • 0025101714 scopus 로고
    • Higher order nuclear organization: Three-dimensional distribution of small nuclear ribonucleoprotein particles
    • Spector DL. 1990. Higher order nuclear organization: three-dimensional distribution of small nuclear ribonucleoprotein particles. Proc Natl Acad Sci USA 87:147-151.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 147-151
    • Spector, D.L.1
  • 95
    • 0031830805 scopus 로고    scopus 로고
    • Interrelationships of nuclear structure and transcriptional control: Functional consequences of being in the right place at the right time
    • Stein GS, van Wijnen AJ, Stein JL, Lian JB, Pockwinse S, McNeil S. 1998. Interrelationships of nuclear structure and transcriptional control: functional consequences of being in the right place at the right time. J Cell Biochem 70:200-212.
    • (1998) J Cell Biochem , vol.70 , pp. 200-212
    • Stein, G.S.1    Van Wijnen, A.J.2    Stein, J.L.3    Lian, J.B.4    Pockwinse, S.5    McNeil, S.6
  • 97
    • 0024948946 scopus 로고
    • A nuclear DNA attachment element mediates elevated and position-independent gene activity
    • Stief A, Winter DM, Stratling WH, Sippel AE. 1989. A nuclear DNA attachment element mediates elevated and position-independent gene activity. Nature 341:343-345.
    • (1989) Nature , vol.341 , pp. 343-345
    • Stief, A.1    Winter, D.M.2    Stratling, W.H.3    Sippel, A.E.4
  • 98
    • 0028998584 scopus 로고
    • Positive and negative regulation of granulocyte-macrophage colony stimulating factor promoter activity by AML1-related transcription factor, PEBP2
    • Takahashi A, Satake M, Yamaguchi-Iwai Y, Bae SC, Lu J, Maruyama M, Zhang YW, Oka H, Arai N, Arai K-I, Ito Y. 1995. Positive and negative regulation of granulocyte-macrophage colony stimulating factor promoter activity by AML1-related transcription factor, PEBP2. Blood 86:607-616.
    • (1995) Blood , vol.86 , pp. 607-616
    • Takahashi, A.1    Satake, M.2    Yamaguchi-Iwai, Y.3    Bae, S.C.4    Lu, J.5    Maruyama, M.6    Zhang, Y.W.7    Oka, H.8    Arai, N.9    Arai, K.-I.10    Ito, Y.11
  • 99
    • 0028048071 scopus 로고
    • Identification of a DNA sequence involved in osteoblast-specific gene expression via interaction with helix-loop-helix (HLH)-type transcription factors
    • Tamura M and Noda M. 1994. Identification of a DNA sequence involved in osteoblast-specific gene expression via interaction with helix-loop-helix (HLH)-type transcription factors. J Cell Biol 126: 773-782.
    • (1994) J Cell Biol , vol.126 , pp. 773-782
    • Tamura, M.1    Noda, M.2
  • 100
    • 0032170325 scopus 로고    scopus 로고
    • Preliminary crystallographic study of the glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBFα2
    • Tang L, Guo B, van Wijnen AJ, Lian JB, Stein JL, Stein GS, Zhou GW. 1998. Preliminary crystallographic study of the glutathione S-transferase fused with the nuclear matrix targeting signal of the transcription factor AML-1/CBFα2. J Struct Biol 123:83-85.
    • (1998) J Struct Biol , vol.123 , pp. 83-85
    • Tang, L.1    Guo, B.2    Van Wijnen, A.J.3    Lian, J.B.4    Stein, J.L.5    Stein, G.S.6    Zhou, G.W.7
  • 101
    • 0032160629 scopus 로고    scopus 로고
    • The DNA-binding and τ2 transactivation domains of the rat glucocorticoid receptor constitute a nuclear matrix targeting signal
    • Tang Y, Getzenberg RH, Vietmeier BN, Stallcup MR, Eggert M, Renkawitz R, DeFranco DB. 1998. The DNA-binding and τ2 transactivation domains of the rat glucocorticoid receptor constitute a nuclear matrix targeting signal. Mol Endocrinol 12:1420-1431.
    • (1998) Mol Endocrinol , vol.12 , pp. 1420-1431
    • Tang, Y.1    Getzenberg, R.H.2    Vietmeier, B.N.3    Stallcup, M.R.4    Eggert, M.5    Renkawitz, R.6    DeFranco, D.B.7
  • 102
    • 0029932598 scopus 로고    scopus 로고
    • A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p
    • Taunton J, Hassig CA, Schreiber SL. 1996. A mammalian histone deacetylase related to the yeast transcriptional regulator Rpd3p. Science 272:408-411.
    • (1996) Science , vol.272 , pp. 408-411
    • Taunton, J.1    Hassig, C.A.2    Schreiber, S.L.3
  • 103
    • 0028286048 scopus 로고
    • Activity of the rat osteocalcin basal promoter in osteoblastic cells is dependent upon homeodomain and CP1 binding motifs
    • Towler DA, Bennett CD, Rodan GA. 1994. Activity of the rat osteocalcin basal promoter in osteoblastic cells is dependent upon homeodomain and CP1 binding motifs. Mol Endocrinol 8:614-624.
    • (1994) Mol Endocrinol , vol.8 , pp. 614-624
    • Towler, D.A.1    Bennett, C.D.2    Rodan, G.A.3
  • 104
    • 0028055116 scopus 로고
    • ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGa transcription factor
    • Tsukiyama T, Becker PB, Wu C. 1994. ATP-dependent nucleosome disruption at a heat-shock promoter mediated by binding of GAGA transcription factor (see comments). Nature 367:525-532.
    • (1994) Nature , vol.367 , pp. 525-532
    • Tsukiyama, T.1    Becker, P.B.2    Wu, C.3
  • 105
    • 0029562736 scopus 로고
    • Purification and properties of an ATP-dependent nucleosome remodeling factor
    • Tsukiyama T and Wu C. 1995. Purification and properties of an ATP-dependent nucleosome remodeling factor. Cell 83:1011-1020.
    • (1995) Cell , vol.83 , pp. 1011-1020
    • Tsukiyama, T.1    Wu, C.2
  • 106
    • 0030886673 scopus 로고    scopus 로고
    • Nuclear export receptors: From importin to exportin
    • Ullman KS, Powers MA, Forbes DJ. 1997. Nuclear export receptors: from importin to exportin. Cell 90:967-970.
    • (1997) Cell , vol.90 , pp. 967-970
    • Ullman, K.S.1    Powers, M.A.2    Forbes, D.J.3
  • 107
    • 0030998534 scopus 로고    scopus 로고
    • Histone acetylation: Influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression
    • Ura K, Kurumizaka H, Dimitrov S, Almouzni G, Wolffe AP. 1997. Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression. EMBO J 16:2096-2107.
    • (1997) EMBO J , vol.16 , pp. 2096-2107
    • Ura, K.1    Kurumizaka, H.2    Dimitrov, S.3    Almouzni, G.4    Wolffe, A.P.5
  • 108
    • 0028914933 scopus 로고
    • Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix
    • van Steensel B, Jenster G, Damm K, Brinkmann AO, van Driel R. 1995. Domains of the human androgen receptor and glucocorticoid receptor involved in binding to the nuclear matrix. J Cell Biochem 57:465-478.
    • (1995) J Cell Biochem , vol.57 , pp. 465-478
    • Van Steensel, B.1    Jenster, G.2    Damm, K.3    Brinkmann, A.O.4    Van Driel, R.5
  • 109
    • 0027240162 scopus 로고
    • Nuclear matrix association of multiple sequence-specific DNA binding activities related to SP-1, ATF, CCAAT, C/EBP, OCT-1, and AP-1
    • van Wijnen AJ, Bidwell JP, Fey EG, Penman S, Lian JB, Stein JL, Stein GS. 1993. Nuclear matrix association of multiple sequence-specific DNA binding activities related to SP-1, ATF, CCAAT, C/EBP, OCT-1, and AP-1. Biochemistry 32:8397-8402.
    • (1993) Biochemistry , vol.32 , pp. 8397-8402
    • Van Wijnen, A.J.1    Bidwell, J.P.2    Fey, E.G.3    Penman, S.4    Lian, J.B.5    Stein, J.L.6    Stein, G.S.7
  • 110
    • 0030839857 scopus 로고    scopus 로고
    • Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II
    • published erratum appears in Nature 1997 Oct 30; 389(6654): 1003
    • Varga-Weisz PD, Wilm M, Bonte E, Dumas K, Mann M, Becker PB. 1997. Chromatin-remodelling factor CHRAC contains the ATPases ISWI and topoisomerase II [published erratum appears in Nature 1997 Oct 30; 389(6654): 1003]. Nature 388:598-602.
    • (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
  • 113
    • 0028127762 scopus 로고
    • Role of the histone amino termini in facilitated binding of a transcription factor
    • Vettese-Dadey M, Walter P, Chen H, Juan L-J, Workman JL. 1994. Role of the histone amino termini in facilitated binding of a transcription factor. Mol Cell Biol 14:970-981.
    • (1994) Mol Cell Biol , vol.14 , pp. 970-981
    • Vettese-Dadey, M.1    Walter, P.2    Chen, H.3    Juan, L.-J.4    Workman, J.L.5
  • 114
    • 0029985730 scopus 로고    scopus 로고
    • Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro
    • Vettese-Dadey M, Grant PA, Hebbes TR, Crane-Robinson C, Allis CD, Workman JL. 1996. Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro. EMBO J 15:2508-2518.
    • (1996) EMBO J , vol.15 , pp. 2508-2518
    • Vettese-Dadey, M.1    Grant, P.A.2    Hebbes, T.R.3    Crane-Robinson, C.4    Allis, C.D.5    Workman, J.L.6
  • 118
    • 0028158682 scopus 로고
    • Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells
    • Weis K, Rambaud S, Lavau C, Jansen J, Carvalho T, Carmo-Fonseca M, Lamond A, Dejean A. 1994. Retinoic acid regulates aberrant nuclear localization of PML-RAR alpha in acute promyelocytic leukemia cells. Cell 76:345-356.
    • (1994) Cell , vol.76 , pp. 345-356
    • Weis, K.1    Rambaud, S.2    Lavau, C.3    Jansen, J.4    Carvalho, T.5    Carmo-Fonseca, M.6    Lamond, A.7    Dejean, A.8
  • 119
    • 0031707751 scopus 로고    scopus 로고
    • Alteration of nucleosome structure as a mechanism of transcriptional regulation
    • Workman JL and Kingston RE. 1998. Alteration of nucleosome structure as a mechanism of transcriptional regulation. Annu Rev Biochem 67:545-79:545-579.
    • (1998) Annu Rev Biochem , vol.67 , pp. 545-579
    • Workman, J.L.1    Kingston, R.E.2
  • 120
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y. 1996. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. Nature 382:319-324.
    • (1996) Nature , vol.382 , pp. 319-324
    • Yang, X.J.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 121
    • 0030790432 scopus 로고    scopus 로고
    • Nuclear punctate distribution of ALL-1 is conferred by distinct elements at the N terminus of the protein
    • Yano T, Nakamura T, Blechman J, Sorio C, Dang CV, Geiger B, Canaani E. 1997. Nuclear punctate distribution of ALL-1 is conferred by distinct elements at the N terminus of the protein. Proc Natl Acad Sci USA 94:7286-7291.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 7286-7291
    • Yano, T.1    Nakamura, T.2    Blechman, J.3    Sorio, C.4    Dang, C.V.5    Geiger, B.6    Canaani, E.7
  • 122
    • 0029968939 scopus 로고    scopus 로고
    • Human p300 protein is a coactivator for the transcription factor MyoD
    • Yuan W, Condorelli G, Caruso M, Felsani A, Giordano A. 1996. Human p300 protein is a coactivator for the transcription factor MyoD. J Biol Chem 271:9009-9013.
    • (1996) J Biol Chem , vol.271 , pp. 9009-9013
    • Yuan, W.1    Condorelli, G.2    Caruso, M.3    Felsani, A.4    Giordano, A.5
  • 126
    • 0032567080 scopus 로고    scopus 로고
    • Rapid and phosphoinositol-dependent binding of the SWI/ SNF-like BAF complex to chromatin after T lymphocyte receptor signaling
    • Zhao K, Wang W, Rando OJ, Xue Y, Swiderek K, Kuo A, Crabtree GR. 1998. Rapid and phosphoinositol-dependent binding of the SWI/ SNF-like BAF complex to chromatin after T lymphocyte receptor signaling. Cell 95:625-636.
    • (1998) Cell , vol.95 , pp. 625-636
    • Zhao, K.1    Wang, W.2    Rando, O.J.3    Xue, Y.4    Swiderek, K.5    Kuo, A.6    Crabtree, G.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.