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Volumn 11, Issue 6, 1997, Pages 682-692

Differential effects of nuclear receptor corepressor (N-CoR) expression levels on retinoic acid receptor-mediated repression support the existence of dynamically regulated corepressor complexes

Author keywords

[No Author keywords available]

Indexed keywords

CELL NUCLEUS RECEPTOR; RETINOIC ACID RECEPTOR; TRANSCRIPTION FACTOR;

EID: 0030998327     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.11.6.682     Document Type: Article
Times cited : (83)

References (65)
  • 1
    • 0029562554 scopus 로고
    • The RXR heterodimers and orphan receptors
    • Mangelsdorf DJ, Evans RM 1995 The RXR heterodimers and orphan receptors. Cell 83:841-850
    • (1995) Cell , vol.83 , pp. 841-850
    • Mangelsdorf, D.J.1    Evans, R.M.2
  • 2
    • 0029182179 scopus 로고
    • The molecular and genetic dissection of the retinoid signaling pathway
    • Chambon P 1995 The molecular and genetic dissection of the retinoid signaling pathway. Recent Prog Horm Res 50:317-332
    • (1995) Recent Prog Horm Res , vol.50 , pp. 317-332
    • Chambon, P.1
  • 3
    • 0028988482 scopus 로고
    • The tau4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing
    • Baniahmad A, Leng X, Burris TP, Tsai SY, Tsai M-J, O'Malley BW 1995 The tau4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing. Mol Cell Biol 15:76-86
    • (1995) Mol Cell Biol , vol.15 , pp. 76-86
    • Baniahmad, A.1    Leng, X.2    Burris, T.P.3    Tsai, S.Y.4    Tsai, M.-J.5    O'Malley, B.W.6
  • 4
    • 0026480387 scopus 로고
    • Kindred S thyroid hormone receptor is an active and constitutive silencer and a repressor for thyroid hormone and retinoic acid responses
    • Baniahmad A, Tsai SY, O'Malley BW, Tsai MJ 1992 Kindred S thyroid hormone receptor is an active and constitutive silencer and a repressor for thyroid hormone and retinoic acid responses. Proc Natl Acad Sci USA 89:10633-10637
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10633-10637
    • Baniahmad, A.1    Tsai, S.Y.2    O'Malley, B.W.3    Tsai, M.J.4
  • 5
    • 0024336324 scopus 로고
    • Protein encoded by v-erbA functions as a thyroid-hormone antagonist
    • Damm K, Thompson CC, Evans RM 1989 Protein encoded by v-erbA functions as a thyroid-hormone antagonist. Nature 339:593-597
    • (1989) Nature , vol.339 , pp. 593-597
    • Damm, K.1    Thompson, C.C.2    Evans, R.M.3
  • 6
    • 0024869336 scopus 로고
    • Thyroid hormone aporeceptor represses T3-inducible promoters and blocks activity of the retinoic acid receptor
    • Brent GA, Dunn MK, Harney JW, Gulick T, Larsen PR, Moore DD 1989 Thyroid hormone aporeceptor represses T3-inducible promoters and blocks activity of the retinoic acid receptor. New Biol 1:329-336
    • (1989) New Biol , vol.1 , pp. 329-336
    • Brent, G.A.1    Dunn, M.K.2    Harney, J.W.3    Gulick, T.4    Larsen, P.R.5    Moore, D.D.6
  • 7
    • 0024400724 scopus 로고
    • Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product
    • Sap J, Munoz A, Schmitt J, Stunnenberg H, Vennstrom B 1989 Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product. Nature 340:242-244
    • (1989) Nature , vol.340 , pp. 242-244
    • Sap, J.1    Munoz, A.2    Schmitt, J.3    Stunnenberg, H.4    Vennstrom, B.5
  • 8
    • 0026557594 scopus 로고
    • A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product, and in the retinoic acid receptor
    • Baniahmad A, Kohne AC, Renkawitz R 1992 A transferable silencing domain is present in the thyroid hormone receptor, in the v-erbA oncogene product, and in the retinoic acid receptor. EMBO J 11:1015-1023
    • (1992) EMBO J , vol.11 , pp. 1015-1023
    • Baniahmad, A.1    Kohne, A.C.2    Renkawitz, R.3
  • 9
    • 0024385540 scopus 로고
    • Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity
    • Graupner G, Wills KN, Tzukerman M, Zhang XK, Pfahl M 1989 Dual regulatory role for thyroid-hormone receptors allows control of retinoic-acid receptor activity. Nature 340:653-656
    • (1989) Nature , vol.340 , pp. 653-656
    • Graupner, G.1    Wills, K.N.2    Tzukerman, M.3    Zhang, X.K.4    Pfahl, M.5
  • 10
    • 0025336820 scopus 로고
    • Modular structure of a chicken lysozyme silencer: Involvement of an unusual thyroid hormone receptor binding site
    • Baniahmad A, Steiner C, Kohne AC, Renkawitz R 1990 Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site. Cell 61:505-514
    • (1990) Cell , vol.61 , pp. 505-514
    • Baniahmad, A.1    Steiner, C.2    Kohne, A.C.3    Renkawitz, R.4
  • 11
    • 0025151993 scopus 로고
    • The C′-terminal interaction domain of the thyroid hormone receptor confers the ability of the DNA site to dictate positive or negative transcriptional activity
    • Holloway JM, Glass CK, Adler S, Nelson CA, Rosenfeld MG 1990 The C′-terminal interaction domain of the thyroid hormone receptor confers the ability of the DNA site to dictate positive or negative transcriptional activity. Proc Natl Acad Sci USA 87:8160-8164
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8160-8164
    • Holloway, J.M.1    Glass, C.K.2    Adler, S.3    Nelson, C.A.4    Rosenfeld, M.G.5
  • 14
    • 0029856508 scopus 로고    scopus 로고
    • Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR
    • Seol W, Mahon MJ, Lee Y-K, Moore DD 1996 Two receptor interacting domains in the nuclear hormone receptor corepressor RIP13/N-CoR. Mol Endocrinol 10:1646-1655
    • (1996) Mol Endocrinol , vol.10 , pp. 1646-1655
    • Seol, W.1    Mahon, M.J.2    Lee, Y.-K.3    Moore, D.D.4
  • 15
    • 0029837730 scopus 로고    scopus 로고
    • A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains
    • Zamir I, Harding HP, Atkins GB, Horlein A, Glass CK, Rosenfeld MG, Lazar MA 1996 A nuclear hormone receptor corepressor mediates transcriptional silencing by receptors with distinct repression domains. Mol Cell Biol 16:5458-5465
    • (1996) Mol Cell Biol , vol.16 , pp. 5458-5465
    • Zamir, I.1    Harding, H.P.2    Atkins, G.B.3    Horlein, A.4    Glass, C.K.5    Rosenfeld, M.G.6    Lazar, M.A.7
  • 16
    • 0029855771 scopus 로고    scopus 로고
    • Function of nuclear co-repressor protein on thyroid hormone response elements is regulated by the receptor A/B domain
    • Hollenberg AN, Monden T, Madura JP, Lee K, Wondisford FE 1996 Function of nuclear co-repressor protein on thyroid hormone response elements is regulated by the receptor A/B domain. J Biol Chem 271:28516-28520
    • (1996) J Biol Chem , vol.271 , pp. 28516-28520
    • Hollenberg, A.N.1    Monden, T.2    Madura, J.P.3    Lee, K.4    Wondisford, F.E.5
  • 17
    • 0029657787 scopus 로고    scopus 로고
    • 3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors
    • 3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors. Mol Endocrinol 10:813-825
    • (1996) Mol Endocrinol , vol.10 , pp. 813-825
    • Sande, S.1    Privalsky, M.L.2
  • 18
    • 0029097233 scopus 로고
    • A transcriptional co-repressor that interacts with nuclear hormone receptors
    • Chen JD, Evans RM 1995 A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature 377:454-457
    • (1995) Nature , vol.377 , pp. 454-457
    • Chen, J.D.1    Evans, R.M.2
  • 19
    • 0023666071 scopus 로고
    • Activation of the yeast HO gene by release from multiple negative controls
    • Sternberg PW, Stern MJ, Clark I, Herskowitz I 1987 Activation of the yeast HO gene by release from multiple negative controls. Cell 48:567-577
    • (1987) Cell , vol.48 , pp. 567-577
    • Sternberg, P.W.1    Stern, M.J.2    Clark, I.3    Herskowitz, I.4
  • 20
    • 0023666079 scopus 로고
    • Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast
    • Nasmyth K, Stillman D, Kipling D 1987 Both positive and negative regulators of HO transcription are required for mother-cell-specific mating-type switching in yeast. Cell 48:579-587
    • (1987) Cell , vol.48 , pp. 579-587
    • Nasmyth, K.1    Stillman, D.2    Kipling, D.3
  • 21
    • 0028940364 scopus 로고
    • An aminoterminal domain of mxi1 mediates anti-myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor sin3
    • Achreiber-Agus N, Chin L, Chen K, Torres R, Rao G, Guida P, Skoultchi Al, DePinho RA 1995 An aminoterminal domain of mxi1 mediates anti-myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor sin3. Cell 80:777-786
    • (1995) Cell , vol.80 , pp. 777-786
    • Achreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Rao, G.5    Guida, P.6    Skoultchi, Al.7    DePinho, R.A.8
  • 22
    • 0028905563 scopus 로고
    • Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor sin3
    • Ayer DE, Lawrence QA, Eisenman RN 1995 Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor sin3. Cell 80:767-776
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 23
    • 0029077733 scopus 로고
    • Effects of the MYC oncogene antagonist, MAD, on proliferation, cell cycling and the malignant phenotype of human brain tumour cells
    • Chen J, Willingham T, Margraf LR, Schreiber-Agus N, DePinho RA, Nisen PD 1995 Effects of the MYC oncogene antagonist, MAD, on proliferation, cell cycling and the malignant phenotype of human brain tumour cells. Nat Med 1:638-643
    • (1995) Nat Med , vol.1 , pp. 638-643
    • Chen, J.1    Willingham, T.2    Margraf, L.R.3    Schreiber-Agus, N.4    DePinho, R.A.5    Nisen, P.D.6
  • 24
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer DE, Kretzner L, Eisenman RN 1993 Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72:211-222
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 25
    • 0026737875 scopus 로고
    • Myc and Max proteins possess distinct transcriptional activities
    • Kretzner L, Blackwood EM, Eisenman RN 1992 Myc and Max proteins possess distinct transcriptional activities. Nature 359:426-429
    • (1992) Nature , vol.359 , pp. 426-429
    • Kretzner, L.1    Blackwood, E.M.2    Eisenman, R.N.3
  • 26
    • 0029588594 scopus 로고
    • Regulation of Myc and Mad during epidermal differentiation and HPV-associated tumorigenesis
    • Hurlin PJ, Foley KP, Ayer DE, Eisenman RN, Hanahan D, Arbeit JM 1995 Regulation of Myc and Mad during epidermal differentiation and HPV-associated tumorigenesis. Oncogene 11:2487-2501
    • (1995) Oncogene , vol.11 , pp. 2487-2501
    • Hurlin, P.J.1    Foley, K.P.2    Ayer, D.E.3    Eisenman, R.N.4    Hanahan, D.5    Arbeit, J.M.6
  • 29
    • 0028889811 scopus 로고
    • Mad3 and Mad4: Novel Max-interacting transcriptional repressers that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation
    • Hurlin PJ, Queva C, Koskinen PJ, Steingrimsson E. Ayer DE, Copeland NG, Jenkins NA, Eisenman RN 1995 Mad3 and Mad4: novel Max-interacting transcriptional repressers that suppress c-myc dependent transformation and are expressed during neural and epidermal differentiation. EMBO J 14:5646-5659
    • (1995) EMBO J , vol.14 , pp. 5646-5659
    • Hurlin, P.J.1    Queva, C.2    Koskinen, P.J.3    Steingrimsson, E.4    Ayer, D.E.5    Copeland, N.G.6    Jenkins, N.A.7    Eisenman, R.N.8
  • 30
    • 0026046959 scopus 로고
    • RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes
    • Vidai M, Strich R, Esposito RE, Gaber RF 1991 RPD1 (SIN3/UME4) is required for maximal activation and repression of diverse yeast genes. Mol Cell Biol 11:6306-6316
    • (1991) Mol Cell Biol , vol.11 , pp. 6306-6316
    • Vidai, M.1    Strich, R.2    Esposito, R.E.3    Gaber, R.F.4
  • 31
    • 0026060619 scopus 로고
    • RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
    • Vidai M, Gaber RF 1991 RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol Cell Biol 11:6317-6327
    • (1991) Mol Cell Biol , vol.11 , pp. 6317-6327
    • Vidai, M.1    Gaber, R.F.2
  • 32
    • 0027490155 scopus 로고
    • The centromere and promoter factor, 1, CPF1, of Saccharomyces cerevisiae modulates gene activity through a family of factors including SPT21, RPD1 (SIN3), RPD3 and CCR4
    • McKenzie EA, Kent NA, Dowell SJ, Moreno F, Bird LE, Mellor J 1993 The centromere and promoter factor, 1, CPF1, of Saccharomyces cerevisiae modulates gene activity through a family of factors including SPT21, RPD1 (SIN3), RPD3 and CCR4. Mol Gen Genet 240:374-386
    • (1993) Mol Gen Genet , vol.240 , pp. 374-386
    • McKenzie, E.A.1    Kent, N.A.2    Dowell, S.J.3    Moreno, F.4    Bird, L.E.5    Mellor, J.6
  • 33
    • 0028297156 scopus 로고
    • Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SW15 transcriptional activator
    • Stillman DJ, Dorland S, Yu Y 1994 Epistasis analysis of suppressor mutations that allow HO expression in the absence of the yeast SW15 transcriptional activator. Genetics 136:781-788
    • (1994) Genetics , vol.136 , pp. 781-788
    • Stillman, D.J.1    Dorland, S.2    Yu, Y.3
  • 34
    • 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
  • 36
    • 0025938132 scopus 로고
    • A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR
    • Mangelsdorf DJ, Umesono K, Kliewer SA, Borgmeyer U, Ong ES, Evans RM 1991 A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR. Cell 66:555-561
    • (1991) Cell , vol.66 , pp. 555-561
    • Mangelsdorf, D.J.1    Umesono, K.2    Kliewer, S.A.3    Borgmeyer, U.4    Ong, E.S.5    Evans, R.M.6
  • 38
    • 0025311121 scopus 로고
    • Transcriptional repression in eukaryotes
    • Renkawitz R 1990 Transcriptional repression in eukaryotes Trends Genet 6:192-197
    • (1990) Trends Genet , vol.6 , pp. 192-197
    • Renkawitz, R.1
  • 39
    • 0029916318 scopus 로고    scopus 로고
    • Short-range transcriptional repressors mediate both quenching and direct repression within complex loci in Drosophila
    • Gray S, Levine M 1996 Short-range transcriptional repressors mediate both quenching and direct repression within complex loci in Drosophila. Genes Dev 10:700-710
    • (1996) Genes Dev , vol.10 , pp. 700-710
    • Gray, S.1    Levine, M.2
  • 40
    • 0029917840 scopus 로고    scopus 로고
    • Repression and activation by multiprotein complexes that alter chromatin structure
    • Kingston RE, Bunker CA, Imbalzano AN 1996 Repression and activation by multiprotein complexes that alter chromatin structure. Genes Dev 10:905-920
    • (1996) Genes Dev , vol.10 , pp. 905-920
    • Kingston, R.E.1    Bunker, C.A.2    Imbalzano, A.N.3
  • 41
    • 0029895168 scopus 로고    scopus 로고
    • Transcriptional repression in development
    • Gray S, Levine M 1996 Transcriptional repression in development. Curr Opin Cell Biol 8:358-364
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 358-364
    • Gray, S.1    Levine, M.2
  • 42
    • 0029978521 scopus 로고    scopus 로고
    • Active repression mechanisms of eukaryotic transcription repressors
    • Hanna-Rose W, Hansen U 1996 Active repression mechanisms of eukaryotic transcription repressors. Trends Genet 12:229-234
    • (1996) Trends Genet , vol.12 , pp. 229-234
    • Hanna-Rose, W.1    Hansen, U.2
  • 44
    • 0028133444 scopus 로고
    • Thyroid abnormalities and hepatocellular carcinoma in mice transgenic for v-erbA
    • Barlow C, Meister B, Lardelli M, Lendahl U, Vennström B 1995 Thyroid abnormalities and hepatocellular carcinoma in mice transgenic for v-erbA. EMBO J 13:4241-4250
    • (1995) EMBO J , vol.13 , pp. 4241-4250
    • Barlow, C.1    Meister, B.2    Lardelli, M.3    Lendahl, U.4    Vennström, B.5
  • 45
    • 0025689050 scopus 로고
    • The viral erbA oncogene protein, a constitutive represser in animal cells, is a hormone-regulated activator in yeast
    • Privalsky ML, Sharif M, Yamamoto KR 1990 The viral erbA oncogene protein, a constitutive represser in animal cells, is a hormone-regulated activator in yeast. Cell 63:1277-1286
    • (1990) Cell , vol.63 , pp. 1277-1286
    • Privalsky, M.L.1    Sharif, M.2    Yamamoto, K.R.3
  • 46
    • 0028588914 scopus 로고
    • The yeast SIN3 gene product negatively regulates the activity of human progesterone receptor and positively regulates the activities of GAL4 and the HAP1 activator
    • Nawaz Z, Baniahmad C, Burris TP, Stillman DJ, O'Malley BW, Tsai M-J 1994 The yeast SIN3 gene product negatively regulates the activity of human progesterone receptor and positively regulates the activities of GAL4 and the HAP1 activator. Mol Gen Genet 245:724-733
    • (1994) Mol Gen Genet , vol.245 , pp. 724-733
    • Nawaz, Z.1    Baniahmad, C.2    Burris, T.P.3    Stillman, D.J.4    O'Malley, B.W.5    Tsai, M.-J.6
  • 47
    • 0029997378 scopus 로고    scopus 로고
    • Targeting chromatin disruption: Transcription regulators that acetylate histones
    • Wolffe AP, Pruss D 1996 Targeting chromatin disruption: transcription regulators that acetylate histones. Cell 84:817-819
    • (1996) Cell , vol.84 , pp. 817-819
    • Wolffe, A.P.1    Pruss, D.2
  • 48
    • 0342936465 scopus 로고    scopus 로고
    • Regulation of gene expression by nucleosomes
    • Svaren J, Hörtz W 1996 Regulation of gene expression by nucleosomes. Curr Opin Genet Dev 6:164-170
    • (1996) Curr Opin Genet Dev , vol.6 , pp. 164-170
    • Svaren, J.1    Hörtz, W.2
  • 50
    • 0024261583 scopus 로고
    • Nucleosome loss activates yeast downstream promoters in vivo
    • Han M, Grunstein M 1988 Nucleosome loss activates yeast downstream promoters in vivo. Cell 55:1137-1145
    • (1988) Cell , vol.55 , pp. 1137-1145
    • Han, M.1    Grunstein, M.2
  • 51
    • 0028239906 scopus 로고
    • Role of chromatin structure in the regulation of transcription by RNA polymerase II
    • Paranjape SM, Kamakaka RT, Kadonaga JT 1995 Role of chromatin structure in the regulation of transcription by RNA polymerase II. Annu Rev Biochem 63:265-297
    • (1995) Annu Rev Biochem , vol.63 , pp. 265-297
    • Paranjape, S.M.1    Kamakaka, R.T.2    Kadonaga, J.T.3
  • 52
    • 0027183088 scopus 로고
    • The inactive × chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression
    • Jeppesen P, Turner BM 1993 The inactive × chromosome in female mammals is distinguished by a lack of histone H4 acetylation, a cytogenetic marker for gene expression. Cell 74:281-9
    • (1993) Cell , vol.74 , pp. 281-289
    • Jeppesen, P.1    Turner, B.M.2
  • 53
    • 0028009294 scopus 로고
    • Acetylated histone H4 on the male × chromosome is associated with dosage compensation in Drosophila
    • Bone JR, Lavender J, Richman R, Palmer MJ, Turner BM, Kuroda MI 1994 Acetylated histone H4 on the male × chromosome is associated with dosage compensation in Drosophila. Genes Dev 8:96-104
    • (1994) Genes Dev , vol.8 , pp. 96-104
    • Bone, J.R.1    Lavender, J.2    Richman, R.3    Palmer, M.J.4    Turner, B.M.5    Kuroda, M.I.6
  • 54
    • 0027465862 scopus 로고
    • A positive role for histone acetylation in transcription factor access to nucleosomal DNA
    • Lee DY, Hayes JJ, Pruss D, Wolffe AP 1993 A positive role for histone acetylation in transcription factor access to nucleosomal DNA. Cell 72:73-84
    • (1993) Cell , vol.72 , pp. 73-84
    • Lee, D.Y.1    Hayes, J.J.2    Pruss, D.3    Wolffe, A.P.4
  • 58
    • 0029773871 scopus 로고    scopus 로고
    • The nuclear hormone receptor coactivator SRC-1 is a specific target of p300
    • Yao T-P, Ku G, Zhou N, Scully R, Livingston DM 1996 The nuclear hormone receptor coactivator SRC-1 is a specific target of p300. Proc Natl Acad Sci 93:10626-10631
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 10626-10631
    • Yao, T.-P.1    Ku, G.2    Zhou, N.3    Scully, R.4    Livingston, D.M.5
  • 59
    • 0030480969 scopus 로고    scopus 로고
    • The CBP co-activator is a histone acetyltransferase
    • Bannister AJ, Kouzarides T 1996 The CBP co-activator is a histone acetyltransferase. Nature 384:641-643
    • (1996) Nature , vol.384 , pp. 641-643
    • Bannister, A.J.1    Kouzarides, T.2
  • 60
    • 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
  • 61
    • 0029665857 scopus 로고    scopus 로고
    • A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
    • Yang X-Y, 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.-Y.1    Ogryzko, V.V.2    Nishikawa, J.3    Howard, B.H.4    Nakatani, Y.5
  • 62
  • 63
    • 0026688440 scopus 로고
    • All-trans and 9-cis retinoic acid induction of CRAB-PII transcription is mediated by RAR-RXR heterodimers bound to DR1 and DR2 repeated motifs
    • Durand B, Saunders M, Leroy P, Leid M, Chambon P 1992 All-trans and 9-cis retinoic acid induction of CRAB-PII transcription is mediated by RAR-RXR heterodimers bound to DR1 and DR2 repeated motifs. Cell 71:73-85
    • (1992) Cell , vol.71 , pp. 73-85
    • Durand, B.1    Saunders, M.2    Leroy, P.3    Leid, M.4    Chambon, P.5
  • 64
    • 0029873038 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 protects entorhinal layer II glutamatergic neurons from axotomy-induced death
    • Peterson DA, Lucidi-Philipi CA, Murphy DP, Ray J, Gage FH 1996 Fibroblast growth factor-2 protects entorhinal layer II glutamatergic neurons from axotomy-induced death. J Neurosci 16:886-898
    • (1996) J Neurosci , vol.16 , pp. 886-898
    • Peterson, D.A.1    Lucidi-Philipi, C.A.2    Murphy, D.P.3    Ray, J.4    Gage, F.H.5
  • 65
    • 0028233383 scopus 로고
    • Estrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
    • Halachmi S, Marden E, Martin G, MacKay H, Abbondanza C, Brown M 1994 Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 264:1455-1458
    • (1994) Science , vol.264 , pp. 1455-1458
    • Halachmi, S.1    Marden, E.2    Martin, G.3    MacKay, H.4    Abbondanza, C.5    Brown, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.