-
1
-
-
0026600841
-
Identification of a conserved region required for hormone-dependent transcriptional activation by steroid hormone receptors
-
Danielian PS, White R, Lees JA, Parker MG. Identification of a conserved region required for hormone-dependent transcriptional activation by steroid hormone receptors. EMBO J. 11:1992;1025-1033.
-
(1992)
EMBO J
, vol.11
, pp. 1025-1033
-
-
Danielian, P.S.1
White, R.2
Lees, J.A.3
Parker, M.G.4
-
2
-
-
0028233763
-
Characterization of the ligand-dependent transactivation by steroid hormone receptors
-
Barettino D, Vivanco Ruiz MM, Stunnenberg HG. Characterization of the ligand-dependent transactivation by steroid hormone receptors. EMBO J. 13:1994;3039-3049.
-
(1994)
EMBO J
, vol.13
, pp. 3039-3049
-
-
Barettino, D.1
Vivanco Ruiz, M.M.2
Stunnenberg, H.G.3
-
3
-
-
0027941792
-
Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: Presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity
-
Durand B, Saunders M, Gaudon C, Roy B, Losson R, Chambon P. Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element on AF-2 activity. EMBO J. 13:1994;5370-5382.
-
(1994)
EMBO J
, vol.13
, pp. 5370-5382
-
-
Durand, B.1
Saunders, M.2
Gaudon, C.3
Roy, B.4
Losson, R.5
Chambon, P.6
-
4
-
-
0027996382
-
Functional analysis of a transactivation domain in the thyroid hormone receptor
-
Tone Y, Collinwood TN, Adams M, Chatterjee VK. Functional analysis of a transactivation domain in the thyroid hormone receptor. J Biol Chem. 269:1994;31157-31161.
-
(1994)
J Biol Chem
, vol.269
, pp. 31157-31161
-
-
Tone, Y.1
Collinwood, T.N.2
Adams, M.3
Chatterjee, V.K.4
-
5
-
-
0029012163
-
Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
-
Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α Nature. 375:1995;377-382.
-
(1995)
Nature
, vol.375
, pp. 377-382
-
-
Bourguet, W.1
Ruff, M.2
Chambon, P.3
Gronemeyer, H.4
Moras, D.5
-
6
-
-
0029643780
-
Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid
-
Renaud J-P, Rochel N, Ruff M, Vivat V, Chambon P, Gronemeyer H, Moras D. Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid. Nature. 378:1995;681-689.
-
(1995)
Nature
, vol.378
, pp. 681-689
-
-
Renaud J-P1
Rochel, N.2
Ruff, M.3
Vivat, V.4
Chambon, P.5
Gronemeyer, H.6
Moras, D.7
-
7
-
-
0029643769
-
A structural role for hormone in the thyroid hormone receptor
-
Wagner RL, Apriletti JW, McGrath ME, West BL, Baxter JD, Fletterick RJ. A structural role for hormone in the thyroid hormone receptor. Nature. 378:1995;690-697.
-
(1995)
Nature
, vol.378
, pp. 690-697
-
-
Wagner, R.L.1
Apriletti, J.W.2
McGrath, M.E.3
West, B.L.4
Baxter, J.D.5
Fletterick, R.J.6
-
8
-
-
0030667676
-
Molecular basis of agonism and antagonism in the oestrogen receptor
-
of outstanding interest. Crystal structures of the estrogen receptor (carboxyl terminus complexed to 17β estrodiol and raloxifene) reveal the striking difference in the position of helix 12, and suggest the molecular basis for antagonism by raloxifene.
-
Brzozowski AM, Pike ACW, Dauter Z, Hubbard RE, Bonn T, Engström O, Öhman L, Greene GL, Gustafsson J-A, Carlquist M. Molecular basis of agonism and antagonism in the oestrogen receptor. of outstanding interest Nature. 389:1997;753-758 Crystal structures of the estrogen receptor (carboxyl terminus complexed to 17β estrodiol and raloxifene) reveal the striking difference in the position of helix 12, and suggest the molecular basis for antagonism by raloxifene.
-
(1997)
Nature
, vol.389
, pp. 753-758
-
-
Brzozowski, A.M.1
Pike, A.C.W.2
Dauter, Z.3
Hubbard, R.E.4
Bonn, T.5
Engström, O.6
Öhman, L.7
Greene, G.L.8
Gustafsson J-A9
Carlquist, M.10
-
10
-
-
0028233383
-
Estrogen receptor-associated proteins: Possible mediators of hormone-induced transcription
-
Halchmi S, Marden E, Martin G, MacKay H, Abbondanza C, Brown M. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science. 264:1994;1455-1458.
-
(1994)
Science
, vol.264
, pp. 1455-1458
-
-
Halchmi, S.1
Marden, E.2
Martin, G.3
MacKay, H.4
Abbondanza, C.5
Brown, M.6
-
12
-
-
0029154931
-
Polarity-specific activities of retinoic acid receptors determined by a co-repressor
-
Kurokawa R, Söderström M, Hörlein A, Halachmi S, Brown M, Rosenfeld MG, Glass CK. Polarity-specific activities of retinoic acid receptors determined by a co-repressor. Nature. 377:1995;451-454.
-
(1995)
Nature
, vol.377
, pp. 451-454
-
-
Kurokawa, R.1
Söderström, M.2
Hörlein, A.3
Halachmi, S.4
Brown, M.5
Rosenfeld, M.G.6
Glass, C.K.7
-
13
-
-
0028846193
-
Sequence and characterization of a co-activator for the steroid hormone receptor superfamily
-
Onate SA, Tsai SY, Tsai M-J, O'Malley BW. Sequence and characterization of a co-activator for the steroid hormone receptor superfamily. Science. 270:1995;1354-1357.
-
(1995)
Science
, vol.270
, pp. 1354-1357
-
-
Onate, S.A.1
Tsai, S.Y.2
Tsai M-J3
O'Malley, B.W.4
-
14
-
-
0242587820
-
A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors
-
Kamei Y, Xu L, Heinzel T, Torchia J, Kurokawa R, Gloss B, Lin SC, Heyman RA, Rose DW, Glass CK, Rosenfeld MG. A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell. 85:1996;403-414.
-
(1996)
Cell
, vol.85
, pp. 403-414
-
-
Kamei, Y.1
Xu, L.2
Heinzel, T.3
Torchia, J.4
Kurokawa, R.5
Gloss, B.6
Lin, S.C.7
Heyman, R.A.8
Rose, D.W.9
Glass, C.K.10
Rosenfeld, M.G.11
-
15
-
-
0029954339
-
TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors
-
Voegel JJ, Heine MJS, Zechel C, Chambon P, Gronemeyer H. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:1996;3667-3675.
-
(1996)
EMBO J
, vol.15
, pp. 3667-3675
-
-
Voegel, J.J.1
Heine, M.J.S.2
Zechel, C.3
Chambon, P.4
Gronemeyer, H.5
-
16
-
-
0029978605
-
GRIP1, a novel mouse protein that serves as a transcriptional co-activator in yeast for the hormone binding domains of steroid receptors
-
Hong H, Kohli K, Trivedi A, Johnson DL, Stallcup MR. GRIP1, a novel mouse protein that serves as a transcriptional co-activator in yeast for the hormone binding domains of steroid receptors. Proc Natl Acad Sci USA. 93:1996;4948-4952.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 4948-4952
-
-
Hong, H.1
Kohli, K.2
Trivedi, A.3
Johnson, D.L.4
Stallcup, M.R.5
-
17
-
-
0030912539
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The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function
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of outstanding interest. The authors report the identification and cloning of a gene encoding a third member of the SRC/NCoA family of proteins, known as p/CIP. Microinjection of antibodies against SRC-1 or p/CIP demonstrates that both are essential co-activators for nuclear hormone dependent transcription. p/CIP is also an essential co-activator for other CBP-dependent transcription factors and coimmunoprecipitiation experiments demonstrate that p/CIP is complexed to CBP/p300. Together with Heery 1997 [27] the authors also identify a novel motif with the consensus amino acid sequence LXXLL that is found in all of the co-activators identified. Mutagenesis studies demonstrate that this motif is functionally and biochemically required for interactions with liganded nuclear receptors.
-
Torchia J, Rose DW, Inostroza J, Kamei Y, Westin S, Glass CK, Rosenfeld MG. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. of outstanding interest Nature. 387:1997;677-684 The authors report the identification and cloning of a gene encoding a third member of the SRC/NCoA family of proteins, known as p/CIP. Microinjection of antibodies against SRC-1 or p/CIP demonstrates that both are essential co-activators for nuclear hormone dependent transcription. p/CIP is also an essential co-activator for other CBP-dependent transcription factors and coimmunoprecipitiation experiments demonstrate that p/CIP is complexed to CBP/p300. Together with Heery 1997 [27] the authors also identify a novel motif with the consensus amino acid sequence LXXLL that is found in all of the co-activators identified. Mutagenesis studies demonstrate that this motif is functionally and biochemically required for interactions with liganded nuclear receptors.
-
(1997)
Nature
, vol.387
, pp. 677-684
-
-
Torchia, J.1
Rose, D.W.2
Inostroza, J.3
Kamei, Y.4
Westin, S.5
Glass, C.K.6
Rosenfeld, M.G.7
-
18
-
-
0030797902
-
AIB1, a steroid receptor co-activator amplified in breast and ovarian cancer
-
of outstanding interest. Using a novel microdissection technique to analyze regions within chromosomes, the authors identify a novel gene referred to as AIB1, within a chromosomal region amplified in breast and ovarian cancers. AIB1, a human homologue of p/CIP, is amplified and overexpressed in several estrogen receptor positive breast and ovarian cancer cell lines, as well as in primary breast cancer specimens.
-
Anzick SL, Kononen J, Walker RL, Azorsa DO, Tanner MM, Guan XY, Sauter G, Kallioniemi OP, Trent JM, Meltzer PS. AIB1, a steroid receptor co-activator amplified in breast and ovarian cancer. of outstanding interest Nature. 277:1997;965-968 Using a novel microdissection technique to analyze regions within chromosomes, the authors identify a novel gene referred to as AIB1, within a chromosomal region amplified in breast and ovarian cancers. AIB1, a human homologue of p/CIP, is amplified and overexpressed in several estrogen receptor positive breast and ovarian cancer cell lines, as well as in primary breast cancer specimens.
-
(1997)
Nature
, vol.277
, pp. 965-968
-
-
Anzick, S.L.1
Kononen, J.2
Walker, R.L.3
Azorsa, D.O.4
Tanner, M.M.5
Guan, X.Y.6
Sauter, G.7
Kallioniemi, O.P.8
Trent, J.M.9
Meltzer, P.S.10
-
19
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0030740253
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Nuclear receptor co-activator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with p/CAF and CBP/p300
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of outstanding interest. Using the liganded retinoic acid X receptor in a yeast two-hybrid screen, the authors identify a co-activator termed ACTR, which is identical to AIB1. ACTR interacts with CBP as well as with the p300/CBP associated factor (p/CAF). Evidence is presented suggesting that CBP, p/CAF and ACTR represent a functional complex. In vitro acetylation assays demonstrate that ACTR possesses intrinsic histone acetyltransferase (HAT) activity and together with SRC-1 defines a novel family of HAT proteins.
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Chen H, Lin RJ, Schiltz RL, Chkravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM. Nuclear receptor co-activator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with p/CAF and CBP/p300. of outstanding interest Cell. 90:1997;569-580 Using the liganded retinoic acid X receptor in a yeast two-hybrid screen, the authors identify a co-activator termed ACTR, which is identical to AIB1. ACTR interacts with CBP as well as with the p300/CBP associated factor (p/CAF). Evidence is presented suggesting that CBP, p/CAF and ACTR represent a functional complex. In vitro acetylation assays demonstrate that ACTR possesses intrinsic histone acetyltransferase (HAT) activity and together with SRC-1 defines a novel family of HAT proteins.
-
(1997)
Cell
, vol.90
, pp. 569-580
-
-
Chen, H.1
Lin, R.J.2
Schiltz, R.L.3
Chkravarti, D.4
Nash, A.5
Nagy, L.6
Privalsky, M.L.7
Nakatani, Y.8
Evans, R.M.9
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20
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0030872716
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AC3, a steroid/nuclear receptor-associated co-activator that is related to SRC-1 and TIF2
-
of special interest. RAC3 is a novel nuclear receptor co-activator protein which is identical to AIB1 and ACTR and is the human homologue of p/CIP.
-
Li H, Gomes PJ, Chen JD. AC3, a steroid/nuclear receptor-associated co-activator that is related to SRC-1 and TIF2. of special interest Proc Natl Acad Sci USA. 94:1997;8479-8484 RAC3 is a novel nuclear receptor co-activator protein which is identical to AIB1 and ACTR and is the human homologue of p/CIP.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 8479-8484
-
-
Li, H.1
Gomes, P.J.2
Chen, J.D.3
-
21
-
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0030786270
-
TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor co-activator-1
-
Takeshita A, Cardona GR, Koibuchi N, Suen CS, Chin WW. TRAM-1, a novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor co-activator-1. J Biol Chem. 272:1997;27629-27634.
-
(1997)
J Biol Chem
, vol.272
, pp. 27629-27634
-
-
Takeshita, A.1
Cardona, G.R.2
Koibuchi, N.3
Suen, C.S.4
Chin, W.W.5
-
22
-
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0032518944
-
The co-activator TIF2 contains three nuclear receptor binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways
-
Voegel JJ, Heine MJS, Tini M, Vivat V, Chambon P, Gronemeyer H. The co-activator TIF2 contains three nuclear receptor binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways. EMBO J. 17:1998;507-519.
-
(1998)
EMBO J
, vol.17
, pp. 507-519
-
-
Voegel, J.J.1
Heine, M.J.S.2
Tini, M.3
Vivat, V.4
Chambon, P.5
Gronemeyer, H.6
-
23
-
-
0032472408
-
Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor
-
Kalkhoven E, Valentine JE, Heery DM, Parker MG. Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor. EMBO J. 17:1998;232-243.
-
(1998)
EMBO J
, vol.17
, pp. 232-243
-
-
Kalkhoven, E.1
Valentine, J.E.2
Heery, D.M.3
Parker, M.G.4
-
24
-
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0032579289
-
Differential use of CREB binding protein-co-activator complexes
-
of special interest. Three E1A domains are defined in CBP, and prove to be differentially utilized for E1A inhibition of nuclear receptor and STAT-1 actions respectively. These data indicate factor-specific regulation by different domains of CBP, implying conformational differences in the co-activator complex bound to different classes of transcription factor. This study suggests the importance of the p/CIP - CBP interaction in nuclear receptor function.
-
Kurokawa R, Kalafus D, Ogliastro MH, Kioussi C, Xu L, Torchia J, Rosenfeld MG, Glass CK. Differential use of CREB binding protein-co-activator complexes. of special interest Science. 279:1998;700-703 Three E1A domains are defined in CBP, and prove to be differentially utilized for E1A inhibition of nuclear receptor and STAT-1 actions respectively. These data indicate factor-specific regulation by different domains of CBP, implying conformational differences in the co-activator complex bound to different classes of transcription factor. This study suggests the importance of the p/CIP - CBP interaction in nuclear receptor function.
-
(1998)
Science
, vol.279
, pp. 700-703
-
-
Kurokawa, R.1
Kalafus, D.2
Ogliastro, M.H.3
Kioussi, C.4
Xu, L.5
Torchia, J.6
Rosenfeld, M.G.7
Glass, C.K.8
-
25
-
-
0343417089
-
The p300/CBP family: Integrating signals with transcription factors and chromatin
-
Shikama N, Lyon J, La Thangue NB. The p300/CBP family: integrating signals with transcription factors and chromatin. Trends Cell Biol. 7:1997;230-236.
-
(1997)
Trends Cell Biol
, vol.7
, pp. 230-236
-
-
Shikama, N.1
Lyon, J.2
La Thangue, N.B.3
-
26
-
-
0029773871
-
The nuclear hormone receptor co-activator SRC-1 is a specific target of p300
-
Yao T-P, Ku G, Zhou N, Scully R, Livingston DM. The nuclear hormone receptor co-activator SRC-1 is a specific target of p300. Proc Natl Acad Sci USA. 93:1996;10626-10631.
-
(1996)
Proc Natl Acad Sci USA
, vol.93
, pp. 10626-10631
-
-
Yao T-P1
Ku, G.2
Zhou, N.3
Scully, R.4
Livingston, D.M.5
-
27
-
-
0030986236
-
A signature motif in co-activators mediates binding to nuclear receptors
-
of outstanding interest. Together with Torchia 1997 [17], the authors define a common motif (LXXLL) found in many nuclear receptor co-activator proteins that is required and sufficient for interactions with liganded nuclear receptors, defining both hydrophobic residues and other amino acids as critical for in vitro function, and implying functional importance in vivo.
-
Heery DM, Kalkoven E, Hoare S, Parker MG. A signature motif in co-activators mediates binding to nuclear receptors. of outstanding interest Nature. 387:1997;733-736 Together with Torchia 1997 [17], the authors define a common motif (LXXLL) found in many nuclear receptor co-activator proteins that is required and sufficient for interactions with liganded nuclear receptors, defining both hydrophobic residues and other amino acids as critical for in vitro function, and implying functional importance in vivo.
-
(1997)
Nature
, vol.387
, pp. 733-736
-
-
Heery, D.M.1
Kalkoven, E.2
Hoare, S.3
Parker, M.G.4
-
28
-
-
0032230231
-
Nuclear receptor binding sites of co-activator glucocorticoid receptor interacting protein GRIP-1 and steroid receptor co-activator (SRC-1)
-
Ding XF, Anderson DM, Ma H, Gond H, Uht M, Kushner P, Stalleup MR. Nuclear receptor binding sites of co-activator glucocorticoid receptor interacting protein GRIP-1 and steroid receptor co-activator (SRC-1). Mol Endocrinol. 12:1998;302-313.
-
(1998)
Mol Endocrinol
, vol.12
, pp. 302-313
-
-
Ding, X.F.1
Anderson, D.M.2
Ma, H.3
Gond, H.4
Uht, M.5
Kushner, P.6
Stalleup, M.R.7
-
29
-
-
0029841744
-
A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors
-
Le Douarin B, Nielsen AL, Garnier JM, Ichinose H, Jeanmougin F, Losson R, Chambon P. A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic control of transcription by nuclear receptors. EMBO J. 15:1996;6701-6715.
-
(1996)
EMBO J
, vol.15
, pp. 6701-6715
-
-
Le Douarin, B.1
Nielsen, A.L.2
Garnier, J.M.3
Ichinose, H.4
Jeanmougin, F.5
Losson, R.6
Chambon, P.7
-
30
-
-
0029022770
-
Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
-
Petrij F, Giles RH, Dauwerse HG, Saris JJ, Hennekam RCM, Masuno M, Tommerup N, Van Ommen G-J, Goodman RH, Peters DJM, Breuning MH. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature. 376:1995;348-351.
-
(1995)
Nature
, vol.376
, pp. 348-351
-
-
Petrij, F.1
Giles, R.H.2
Dauwerse, H.G.3
Saris, J.J.4
Hennekam, R.C.M.5
Masuno, M.6
Tommerup, N.7
Van Ommen G-J8
Goodman, R.H.9
Peters, D.J.M.10
Breuning, M.H.11
-
31
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0030901264
-
Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signaling
-
Akimaru H, Chen Y, Dai P, Hou DX, Nonaka M, Smolik SM, Armstrong S, Goodman RH, Ishii S. Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signaling. Nature. 386:1997;735-738.
-
(1997)
Nature
, vol.386
, pp. 735-738
-
-
Akimaru, H.1
Chen, Y.2
Dai, P.3
Hou, D.X.4
Nonaka, M.5
Smolik, S.M.6
Armstrong, S.7
Goodman, R.H.8
Ishii, S.9
-
32
-
-
0030923585
-
Abnormal skeletal patterning in embryos lacking a single CBP allele: A partial similarity with Rubinstein-Taybi syndrome
-
Tanaka Y, Ichiro N, Maekawa T, Masuya H, Shiroishi T, Ishii S. Abnormal skeletal patterning in embryos lacking a single CBP allele: a partial similarity with Rubinstein-Taybi syndrome. Proc Natl Acad Sci USA. 94:1997;10215-10220.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 10215-10220
-
-
Tanaka, Y.1
Ichiro, N.2
Maekawa, T.3
Masuya, H.4
Shiroishi, T.5
Ishii, S.6
-
33
-
-
0028296414
-
Molecular cloning and functional analysis of the adenovirus E1A-associated 300 kD protein (p300) reveals a protein with properties of a transcriptional adaptor
-
Eckner R, Ewen ME, Newsome D, Gerdes M, DeCaprio JA, Lawrence JB, Livingston DM. Molecular cloning and functional analysis of the adenovirus E1A-associated 300 kD protein (p300) reveals a protein with properties of a transcriptional adaptor. Genes Dev. 8:1994;869-884.
-
(1994)
Genes Dev
, vol.8
, pp. 869-884
-
-
Eckner, R.1
Ewen, M.E.2
Newsome, D.3
Gerdes, M.4
Decaprio, J.A.5
Lawrence, J.B.6
Livingston, D.M.7
-
34
-
-
0000631273
-
The signal-dependent co-activator CBP is a nuclear target for pp90RSK
-
of special interest. The interaction of the C/H3 domain of CBP with pp90RSK1 is demonstrated, and evidence is provided to suggest that this exerts critical functions in modulating CBP function.
-
Nakajima T, Fukamizu A, Takahashi J, Gage FH, Fisher T, Blenis J, Montminy MR. The signal-dependent co-activator CBP is a nuclear target for pp90RSK. of special interest Cell. 86:1996;465-474 The interaction of the C/H3 domain of CBP with pp90RSK1 is demonstrated, and evidence is provided to suggest that this exerts critical functions in modulating CBP function.
-
(1996)
Cell
, vol.86
, pp. 465-474
-
-
Nakajima, T.1
Fukamizu, A.2
Takahashi, J.3
Gage, F.H.4
Fisher, T.5
Blenis, J.6
Montminy, M.R.7
-
35
-
-
0030967951
-
RNA helicase A mediates association of CBP with the RNA polymerase II
-
of outstanding interest. In these studies, the authors establish an in vitro transcription assay for CREB that is dependent on protein kinase A phosphorylation of series 133 and the presence of CBP. They further demonstrate that the C/H3 domain of CBP interacts with RNA helicase A, is cloned using C/H3 domain of CBP and suggests that RNA helicase A serves to recruit RNA polymerase II. Evidence is presented that E1A blocks CREB function by preventing the association of RNA helicase A - RNA polymerase II complexes with CBP.
-
Nakajima T, Uchida C, Anderson SF, Lee CG, Hurwitz J, Parvin JD, Montminy M. RNA helicase A mediates association of CBP with the RNA polymerase II. of outstanding interest Cell. 90:1997;1107-1112 In these studies, the authors establish an in vitro transcription assay for CREB that is dependent on protein kinase A phosphorylation of series 133 and the presence of CBP. They further demonstrate that the C/H3 domain of CBP interacts with RNA helicase A, is cloned using C/H3 domain of CBP and suggests that RNA helicase A serves to recruit RNA polymerase II. Evidence is presented that E1A blocks CREB function by preventing the association of RNA helicase A - RNA polymerase II complexes with CBP.
-
(1997)
Cell
, vol.90
, pp. 1107-1112
-
-
Nakajima, T.1
Uchida, C.2
Anderson, S.F.3
Lee, C.G.4
Hurwitz, J.5
Parvin, J.D.6
Montminy, M.7
-
36
-
-
0029665857
-
A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A
-
of outstanding interest. This study reported the cloning of a p300/CBP associated factor, p/CAF, that is highly related to GCN5 and that possesses an intrinsic histone acetyltransferase (HAT) activity. p/CAF was found to associate with the C/H3 domain of p300/CBP through an amino-terminal domain that is not conserved in GCN5. p/CAF and the adenovirus E1A oncoprotein compete with each other for interaction with the C/H3 domain of p300/CBP. Individual lines of evidence suggest that the p300/CBP - p/CAF interaction is an important target of E1A in altering cell growth and differentiation.
-
Yang XJ, Ogryzko W, Nishikawa J, Howard BH, Nakatani Y. A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. of outstanding interest Nature. 382:1996;319-324 This study reported the cloning of a p300/CBP associated factor, p/CAF, that is highly related to GCN5 and that possesses an intrinsic histone acetyltransferase (HAT) activity. p/CAF was found to associate with the C/H3 domain of p300/CBP through an amino-terminal domain that is not conserved in GCN5. p/CAF and the adenovirus E1A oncoprotein compete with each other for interaction with the C/H3 domain of p300/CBP. Individual lines of evidence suggest that the p300/CBP - p/CAF interaction is an important target of E1A in altering cell growth and differentiation.
-
(1996)
Nature
, vol.382
, pp. 319-324
-
-
Yang, X.J.1
Ogryzko, W.2
Nishikawa, J.3
Howard, B.H.4
Nakatani, Y.5
-
37
-
-
0030606239
-
The transcriptional co-activator p300 and CPB are histone acetyltransferases
-
of outstanding interest. This important study, along with Bannister 1996 [38], established the intrinsic histone acetyltransferase (HAT) functions of CBP and p300, and mapped the domains necessary for enzymatic activity. CBP was demonstrated to acetylate free histones, as well as histones present in nucleosome complexes. In concert with the discovery of p/CAF by Yang 1996 [36], these studies supported a fundamental role of histone acetylation in regulated gene expression and raised the question of why multiple HAT functions might be required.
-
Ogryzko VV, Schlitz RL, Russanova V, Howard BH, Nakatiani Y. The transcriptional co-activator p300 and CPB are histone acetyltransferases. of outstanding interest Cell. 87:1996;953-960 This important study, along with Bannister 1996 [38], established the intrinsic histone acetyltransferase (HAT) functions of CBP and p300, and mapped the domains necessary for enzymatic activity. CBP was demonstrated to acetylate free histones, as well as histones present in nucleosome complexes. In concert with the discovery of p/CAF by Yang 1996 [36], these studies supported a fundamental role of histone acetylation in regulated gene expression and raised the question of why multiple HAT functions might be required.
-
(1996)
Cell
, vol.87
, pp. 953-960
-
-
Ogryzko, V.V.1
Schlitz, R.L.2
Russanova, V.3
Howard, B.H.4
Nakatiani, Y.5
-
38
-
-
0030480969
-
The CBP co-activator is a histone acetyltransferase
-
of outstanding interest. This paper reports the discovery of histone acetyltransferase (HAT) function of CBP in a manner similar to that of Ogryzko 1996 [37].
-
Bannister AJ, Kouzarides T. The CBP co-activator is a histone acetyltransferase. of outstanding interest Nature. 384:1996;641-643 This paper reports the discovery of histone acetyltransferase (HAT) function of CBP in a manner similar to that of Ogryzko 1996 [37].
-
(1996)
Nature
, vol.384
, pp. 641-643
-
-
Bannister, A.J.1
Kouzarides, T.2
-
39
-
-
0032579292
-
Transcription factor-specific requirements for co-activators and their acetyltransferase functions
-
of outstanding interest. This paper demonstrates differential co-activator and histone acetyltransferase (HAT) requirements for nuclear receptors STAT-1 and CREB. Transcriptional activation by the retinoic acid receptor required CBP/p300, p/CIP, SRC-1 and P/CAF, while CRE required CBP/p300, p/CIP and p/CAF, and STAT-1 required CBP/p300 and p/CIP. Intriguingly, the CBP HAT activity was selectively required for transcriptional activation by STAT-1 and CREB. Conversely, the HAT function of p/CAF was selectively required for nuclear receptor function, suggesting that specific transcription exhibit differential co-activator and HAT requirements.
-
Korzus E, Torchia J, Rose DW, Xu L, Kurokawa R, McInerney EM, Mullen TM, Glass CK, Rosenfeld MG. Transcription factor-specific requirements for co-activators and their acetyltransferase functions. of outstanding interest Science. 279:1998;703-707 This paper demonstrates differential co-activator and histone acetyltransferase (HAT) requirements for nuclear receptors STAT-1 and CREB. Transcriptional activation by the retinoic acid receptor required CBP/p300, p/CIP, SRC-1 and P/CAF, while CRE required CBP/p300, p/CIP and p/CAF, and STAT-1 required CBP/p300 and p/CIP. Intriguingly, the CBP HAT activity was selectively required for transcriptional activation by STAT-1 and CREB. Conversely, the HAT function of p/CAF was selectively required for nuclear receptor function, suggesting that specific transcription exhibit differential co-activator and HAT requirements.
-
(1998)
Science
, vol.279
, pp. 703-707
-
-
Korzus, E.1
Torchia, J.2
Rose, D.W.3
Xu, L.4
Kurokawa, R.5
McInerney, E.M.6
Mullen, T.M.7
Glass, C.K.8
Rosenfeld, M.G.9
-
40
-
-
0029984469
-
Tetrahymena histone acetyltransferase A: A homologue to yeast GCN5 linking histone acetylation to gene activation
-
of outstanding interest. This groundbreaking paper identified a surprising function of the genetically identified GCN5 by identifying intrinsic histone acetyltransferase function.
-
Brownell JE, Zhou JX, Allis CD, Berger SL. Tetrahymena histone acetyltransferase A: a homologue to yeast GCN5 linking histone acetylation to gene activation. of outstanding interest Cell. 84:1996;843-851 This groundbreaking paper identified a surprising function of the genetically identified GCN5 by identifying intrinsic histone acetyltransferase function.
-
(1996)
Cell
, vol.84
, pp. 843-851
-
-
Brownell, J.E.1
Zhou, J.X.2
Allis, C.D.3
Berger, S.L.4
-
41
-
-
0031031755
-
Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo
-
of outstanding interest. The role of both the HAT domain and the ADA-2 interaction domain and also of the bromodomain of GCN5 was functionally demonstrated for specific gene targets based on functional assays with domain-deleted proteins.
-
Candau R, Zhou JX, Allis CD, Berger SL. Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo. of outstanding interest EMBO J. 16:1997;555-565 The role of both the HAT domain and the ADA-2 interaction domain and also of the bromodomain of GCN5 was functionally demonstrated for specific gene targets based on functional assays with domain-deleted proteins.
-
(1997)
EMBO J
, vol.16
, pp. 555-565
-
-
Candau, R.1
Zhou, J.X.2
Allis, C.D.3
Berger, S.L.4
-
42
-
-
0031036154
-
Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation
-
Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL. Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. Mol Cell Biol. 1:1997;519-527.
-
(1997)
Mol Cell Biol
, vol.1
, pp. 519-527
-
-
Wang, L.1
Mizzen, C.2
Ying, C.3
Candau, R.4
Barlev, N.5
Brownell, J.6
Allis, C.D.7
Berger, S.L.8
-
43
-
-
0030878878
-
Steroid receptor induction of gene transcription: A two-step model
-
Jenster G, Spencer TE, Burcin MM, Tsai SY, Tsai MJ, O'Malley BW. Steroid receptor induction of gene transcription: a two-step model. Proc Natl Acad Sci USA. 94:1997;7879-7884.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 7879-7884
-
-
Jenster, G.1
Spencer, T.E.2
Burcin, M.M.3
Tsai, S.Y.4
Tsai, M.J.5
O'Malley, B.W.6
-
44
-
-
0030768745
-
Steroid receptor co-activator-1 is a histone acetyltransferase
-
of outstanding interest. The authors demonstrate that SRC-1 is a histone acetyltransferase (HAT) capable of acetylating H3 and H4 both in solution and as mononucleosomes. The HAT activity is localized to a distinct region in the carboxy terminus of the protein that is conserved between members of the SRC/NCoA family of proteins. In addition, SRC-1 interacts, in vivo and in vitro, with the p300/CBP-associated factor, p/CAF.
-
Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW. Steroid receptor co-activator-1 is a histone acetyltransferase. of outstanding interest Nature. 389:1997;194-198 The authors demonstrate that SRC-1 is a histone acetyltransferase (HAT) capable of acetylating H3 and H4 both in solution and as mononucleosomes. The HAT activity is localized to a distinct region in the carboxy terminus of the protein that is conserved between members of the SRC/NCoA family of proteins. In addition, SRC-1 interacts, in vivo and in vitro, with the p300/CBP-associated factor, p/CAF.
-
(1997)
Nature
, vol.389
, pp. 194-198
-
-
Spencer, T.E.1
Jenster, G.2
Burcin, M.M.3
Allis, C.D.4
Zhou, J.5
Mizzen, C.A.6
McKenna, N.J.7
Onate, S.A.8
Tsai, S.Y.9
Tsai, M.J.10
O'Malley, B.W.11
-
45
-
-
10144228410
-
Purification and biochemical heterogeneity of the mammalian SWI-SNF complex
-
Wang W, Cote J, Xue Y, Zhou S, Khavari PA, Biggar SR, Muchardt C, Kalpana GV, Goff SP, Yaniv M, et al. Purification and biochemical heterogeneity of the mammalian SWI-SNF complex. EMBO J. 15:1996;5370-5382.
-
(1996)
EMBO J
, vol.15
, pp. 5370-5382
-
-
Wang, W.1
Cote, J.2
Xue, Y.3
Zhou, S.4
Khavari, P.A.5
Biggar, S.R.6
Muchardt, C.7
Kalpana, G.V.8
Goff, S.P.9
Yaniv, M.10
-
46
-
-
0030797349
-
Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: Characterization of an Ada complex and the SAGA (Spt/Ada) complex
-
Grant PA, Duggan L, Cote J, Roberts SM, Brownell JE, Candau R, Ohba R, Owen-Hughes T, Allis CD, Winston F, et al. Yeast Gcn5 functions in two multisubunit complexes to acetylate nucleosomal histones: characterization of an Ada complex and the SAGA (Spt/Ada) complex. Genes Dev. 13:1997;1640-1650.
-
(1997)
Genes Dev
, vol.13
, pp. 1640-1650
-
-
Grant, P.A.1
Duggan, L.2
Cote, J.3
Roberts, S.M.4
Brownell, J.E.5
Candau, R.6
Ohba, R.7
Owen-Hughes, T.8
Allis, C.D.9
Winston, F.10
-
47
-
-
0031470152
-
Human histone acetyltransferase GCN5 exists in a stable macromolecular complex lacking the adapter ADA2
-
Forsberg EC, Lam LT, Yang XJ, Nakatani Y, Bresnick EH. Human histone acetyltransferase GCN5 exists in a stable macromolecular complex lacking the adapter ADA2. Biochemistry. 36:1997;15918-15924.
-
(1997)
Biochemistry
, vol.36
, pp. 15918-15924
-
-
Forsberg, E.C.1
Lam, L.T.2
Yang, X.J.3
Nakatani, Y.4
Bresnick, E.H.5
-
48
-
-
0030797585
-
Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain
-
of outstanding interest. The authors provide an initial example of a weak substrate, nonhistone substrate for CBP acetyltransferase function, and find a different DNA-binding capacity in response to acetylation. This has implications for functions of other HATs, and provides a model of control of p53 functions. The authors demonstrate, in vivo and in vitro, that p300 can acetylate p53, resulting in an increase in specific DNA binding activity by p53.
-
Gu W, Roeder RG. Activation of p53 sequence-specific DNA binding by acetylation of the p53 C-terminal domain. of outstanding interest Cell. 90:1997;595-606 The authors provide an initial example of a weak substrate, nonhistone substrate for CBP acetyltransferase function, and find a different DNA-binding capacity in response to acetylation. This has implications for functions of other HATs, and provides a model of control of p53 functions. The authors demonstrate, in vivo and in vitro, that p300 can acetylate p53, resulting in an increase in specific DNA binding activity by p53.
-
(1997)
Cell
, vol.90
, pp. 595-606
-
-
Gu, W.1
Roeder, R.G.2
-
49
-
-
0031239891
-
Acetylation of general transcription factors by histone acetyltransferases
-
Imhof A, Yang XJ, Ogryzko VV, Nakatani Y, Wolffe AP, Ge H. Acetylation of general transcription factors by histone acetyltransferases. Curr Biol. 7:1997;689-692.
-
(1997)
Curr Biol
, vol.7
, pp. 689-692
-
-
Imhof, A.1
Yang, X.J.2
Ogryzko, V.V.3
Nakatani, Y.4
Wolffe, A.P.5
Ge, H.6
-
50
-
-
0031310741
-
Differential Roles of p300 and PCAF acetyltransferases in muscle differentiation
-
of outstanding interest. Evidence that p300 and p/CAF HAT domains are differentially required in null culture models of muscle differentiation, indicating that they exert distinct as well as redundant function. Thus, myoD-mediated activation of p21 requires p/CAF HAT, but not p300 HAT function.
-
Puril PL, Sartorelli V, Yang XJ, Hamamori Y, Vasily V, Ogryzko VV, Howard Bruce H, Kedes L, Wang J, Graessmann A, et al. Differential Roles of p300 and PCAF acetyltransferases in muscle differentiation. of outstanding interest Mol Cell. 1:1997;35-45 Evidence that p300 and p/CAF HAT domains are differentially required in null culture models of muscle differentiation, indicating that they exert distinct as well as redundant function. Thus, myoD-mediated activation of p21 requires p/CAF HAT, but not p300 HAT function.
-
(1997)
Mol Cell
, vol.1
, pp. 35-45
-
-
Puril, P.L.1
Sartorelli, V.2
Yang, X.J.3
Hamamori, Y.4
Vasily, V.5
Ogryzko, V.V.6
Howard Bruce, H.7
Kedes, L.8
Wang, J.9
Graessmann, A.10
-
51
-
-
0026557594
-
A transferable silencing domain is present in the thyroid hormone receptors, in the verbA oncogene product and the retinoic acid receptor
-
Baniahmad A, Kohne AC, Renkawitz R. A transferable silencing domain is present in the thyroid hormone receptors, in the verbA oncogene product and the retinoic acid receptor. EMBO J. 11:1992;1015-1023.
-
(1992)
EMBO J
, vol.11
, pp. 1015-1023
-
-
Baniahmad, A.1
Kohne, A.C.2
Renkawitz, R.3
-
52
-
-
0028988482
-
The 4 activation domain of the thyroid hormone receptor is required for the release of a putative co-repressor(s) necessary for transcriptional silencing
-
Baniahmad A, Leng X, Burris TP, Tsai SY, Tsai MJ, O'Malley BW. The 4 activation domain of the thyroid hormone receptor is required for the release of a putative co-repressor(s) necessary for transcriptional silencing. Mol Cell Biol. 15:1995;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
-
53
-
-
0029132202
-
Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
-
Horlein AJ, Naar AM, Heinzel T, Torchia J, Gloss B, Kurokawa R, Ryan A, Kamei Y, Soderstrom M, Glass CK, Rosenfeld MG. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor. Nature. 377:1995;397-404.
-
(1995)
Nature
, vol.377
, pp. 397-404
-
-
Horlein, A.J.1
Naar, A.M.2
Heinzel, T.3
Torchia, J.4
Gloss, B.5
Kurokawa, R.6
Ryan, A.7
Kamei, Y.8
Soderstrom, M.9
Glass, C.K.10
Rosenfeld, M.G.11
-
54
-
-
0029154931
-
Polarity specific activities of retinoic receptors determined by a co-repressor
-
Kurokawa R, Soderstrom M, Horlein A, Halachmi S, Brown M, Rosenfeld M, Glass C. Polarity specific activities of retinoic receptors determined by a co-repressor. Nature. 377:1995;451-454.
-
(1995)
Nature
, vol.377
, pp. 451-454
-
-
Kurokawa, R.1
Soderstrom, M.2
Horlein, A.3
Halachmi, S.4
Brown, M.5
Rosenfeld, M.6
Glass, C.7
-
55
-
-
0028876893
-
Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor
-
Lee JW, Choi HS, Gyuris J, Brent R, Moore DD. Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 9:1995;243-254.
-
(1995)
Mol Endocrinol
, vol.9
, pp. 243-254
-
-
Lee, J.W.1
Choi, H.S.2
Gyuris, J.3
Brent, R.4
Moore, D.D.5
-
56
-
-
0029097233
-
A transcriptional co-repressor that interacts with nuclear hormone receptors
-
Chen JD, Evans RM. A transcriptional co-repressor that interacts with nuclear hormone receptors. Nature. 377:1995;454-457.
-
(1995)
Nature
, vol.377
, pp. 454-457
-
-
Chen, J.D.1
Evans, R.M.2
-
57
-
-
0029657787
-
Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors
-
Sande S, Privalsky MI. Identification of TRACs (T3 receptor-associating cofactors), a family of cofactors that associate with, and modulate the activity of, nuclear hormone receptors. Mol Endocrinol. 10:1996;813-825.
-
(1996)
Mol Endocrinol
, vol.10
, pp. 813-825
-
-
Sande, S.1
Privalsky, M.I.2
-
58
-
-
0030946201
-
Gene silencing by chicken ovalbumin upstream promoter-transcription factor I (COUP-TFI) is mediated by transcriptional co-repressors, nuclear receptor-co-repressor (N-CoR) and silencing mediator for retinoic acid receptor and thyroid hormone receptor (SMRT)
-
Shibata H, Nawaz Z, Tsai SY, O'Malley BW, Tsai MJ. Gene silencing by chicken ovalbumin upstream promoter-transcription factor I (COUP-TFI) is mediated by transcriptional co-repressors, nuclear receptor-co-repressor (N-CoR) and silencing mediator for retinoic acid receptor and thyroid hormone receptor (SMRT). Mol Endocrinol. 11:1997;714-724.
-
(1997)
Mol Endocrinol
, vol.11
, pp. 714-724
-
-
Shibata, H.1
Nawaz, Z.2
Tsai, S.Y.3
O'Malley, B.W.4
Tsai, M.J.5
-
59
-
-
0029837730
-
A nuclear hormone receptor co-repressor mediates transcriptional silencing by receptors with distinct repression domains
-
Zamir I, Harding HP, Atkins GB, Horlein A, Glass CK, Rosenfeld MG, Lazar MA. A nuclear hormone receptor co-repressor mediates transcriptional silencing by receptors with distinct repression domains. Mol Cell Biol. 16:1996;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
-
60
-
-
85030334491
-
Diverse signalling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes
-
in press.
-
Lavinsky RM, Jepsen K, Heinzel T, Torchia J, Mullen TM, Schiff R, Del-Rio LA, Ricote M, Ngo S, Hilsenbeck SG: Diverse signalling pathways modulate nuclear receptor recruitment of N-CoR and SMRT complexes. Proc Natl Acad Sci USA, in press.
-
Proc Natl Acad Sci USA
-
-
Lavinsky, R.M.1
Jepsen, K.2
Heinzel, T.3
Torchia, J.4
Mullen, T.M.5
Schiff, R.6
Del-Rio, L.A.7
Ricote, M.8
Ngo, S.9
Hilsenbeck, S.G.10
-
61
-
-
0030946198
-
Coactivator and co-repressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen
-
Smith CL, Nawaz Z, O'Malley BW. Coactivator and co-repressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol Endocrinol. 11:1997;657-666.
-
(1997)
Mol Endocrinol
, vol.11
, pp. 657-666
-
-
Smith, C.L.1
Nawaz, Z.2
O'Malley, B.W.3
-
62
-
-
0030998328
-
The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding co-activator L7/SPA and the co-repressors N-CoR or SMRT
-
Jackson TA, Richer JK, Bain DL, Takimoto GS, Tung L, Horwitz KB. The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding co-activator L7/SPA and the co-repressors N-CoR or SMRT. Mol Endocrinol. 11:1997;693-705.
-
(1997)
Mol Endocrinol
, vol.11
, pp. 693-705
-
-
Jackson, T.A.1
Richer, J.K.2
Bain, D.L.3
Takimoto, G.S.4
Tung, L.5
Horwitz, K.B.6
-
63
-
-
0030991152
-
Stoichiometric and steric principles governing repression by nuclear hormone receptors
-
of special interest. NCoR and SMRT exhibit distinct preferences for association with specific DNA-bound transcription factors, suggesting specific, as well as redundant, functions.
-
Zamir I, Zhang J, Lazar MA. Stoichiometric and steric principles governing repression by nuclear hormone receptors. of special interest Genes Dev. 11:1997;835-846 NCoR and SMRT exhibit distinct preferences for association with specific DNA-bound transcription factors, suggesting specific, as well as redundant, functions.
-
(1997)
Genes Dev
, vol.11
, pp. 835-846
-
-
Zamir, I.1
Zhang, J.2
Lazar, M.A.3
-
64
-
-
0029686266
-
Proteins of the Myc network: Essential regulators of cell growth and differentiation
-
Henriksson M, Luscher B. Proteins of the Myc network: essential regulators of cell growth and differentiation. Adv Cancer Res. 68:1996;108-169.
-
(1996)
Adv Cancer Res
, vol.68
, pp. 108-169
-
-
Henriksson, M.1
Luscher, B.2
-
65
-
-
0028940364
-
An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
-
Schreiber-Agus N, Chin L, Chen K, Torres R, Rao G, Guida P, Skoultchi AI, DePinho RA. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell. 80:1995;777-786.
-
(1995)
Cell
, vol.80
, pp. 777-786
-
-
Schreiber-Agus, N.1
Chin, L.2
Chen, K.3
Torres, R.4
Rao, G.5
Guida, P.6
Skoultchi, A.I.7
Depinho, R.A.8
-
66
-
-
0028905563
-
Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
-
Ayer DE, Lawrence QA, Eisenman RN. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell. 80:1995;767-776.
-
(1995)
Cell
, vol.80
, pp. 767-776
-
-
Ayer, D.E.1
Lawrence, Q.A.2
Eisenman, R.N.3
-
67
-
-
0026060619
-
RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae
-
Vidal M, Gaber RF. RPD3 encodes a second factor required to achieve maximum positive and negative transcriptional states in Saccharomyces cerevisiae. Mol Cell Biol. 12:1991;6317-6327.
-
(1991)
Mol Cell Biol
, vol.12
, pp. 6317-6327
-
-
Vidal, M.1
Gaber, R.F.2
-
68
-
-
0029932598
-
A mammalian histone deacetylase related to the yeast transcriptional regulator RPD3
-
of special interest. In a landmark paper, the authors use the histone deacetylase inhibitor trapoxin to generate an affinity column and purify proteins, one of which is a human homolog of yeast RPD3, and thus this factor is postulated to be the first identified mammalian histone deacetylase.
-
Taunton J, Hassig CA, Schreiber SL. A mammalian histone deacetylase related to the yeast transcriptional regulator RPD3. of special interest Science. 272:1996;408-411 In a landmark paper, the authors use the histone deacetylase inhibitor trapoxin to generate an affinity column and purify proteins, one of which is a human homolog of yeast RPD3, and thus this factor is postulated to be the first identified mammalian histone deacetylase.
-
(1996)
Science
, vol.272
, pp. 408-411
-
-
Taunton, J.1
Hassig, C.A.2
Schreiber, S.L.3
-
69
-
-
0030834976
-
Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
-
Yang WM, Yao YL, Sun JM, Davie JR, Seto E. Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J Biol Chem. 272:1997;28001-28007.
-
(1997)
J Biol Chem
, vol.272
, pp. 28001-28007
-
-
Yang, W.M.1
Yao, Y.L.2
Sun, J.M.3
Davie, J.R.4
Seto, E.5
-
70
-
-
0030798245
-
Histone acetylation in chromatin structure and transcription
-
Grunstein M. Histone acetylation in chromatin structure and transcription. Nature. 389:1997;349-352.
-
(1997)
Nature
, vol.389
, pp. 349-352
-
-
Grunstein, M.1
-
71
-
-
0031132205
-
Activators and repressors: Making use of chromatin to regulate transcription
-
Wolffe AP, Wong J, Pruss D. Activators and repressors: making use of chromatin to regulate transcription. Genes Dev. 2:1997;291-302.
-
(1997)
Genes Dev
, vol.2
, pp. 291-302
-
-
Wolffe, A.P.1
Wong, J.2
Pruss, D.3
-
72
-
-
17744413444
-
A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression
-
of special interest. The authors establish the connection between transcriptional repression by unliganded TR and recruitment of a histone deacetylase complex that includes NCoR, Sin3 and the histone deacetylase RPD3. Antibodies against each component of the N-CoR/mSin3/RPD3 complex can abolish transcriptional repression by unliganded TR and MAD in a microinjection assay, indicating that each component is essential for function of the complex. Together with [73-77] an important connection is established between histone deacetylation and transcriptional repression by DNA binding proteins.
-
Heinzel T, Lavinsky RM, Mullen TM, Soderstrom M, Laherty CD, Torchia J, Yang WM, Brard G, Ngo SD, Davie JR, et al. A complex containing N-CoR, mSin3 and histone deacetylase mediates transcriptional repression. of special interest Nature. 387:1997;43-48 The authors establish the connection between transcriptional repression by unliganded TR and recruitment of a histone deacetylase complex that includes NCoR, Sin3 and the histone deacetylase RPD3. Antibodies against each component of the N-CoR/mSin3/RPD3 complex can abolish transcriptional repression by unliganded TR and MAD in a microinjection assay, indicating that each component is essential for function of the complex. Together with [73-77] an important connection is established between histone deacetylation and transcriptional repression by DNA binding proteins.
-
(1997)
Nature
, vol.387
, pp. 43-48
-
-
Heinzel, T.1
Lavinsky, R.M.2
Mullen, T.M.3
Soderstrom, M.4
Laherty, C.D.5
Torchia, J.6
Yang, W.M.7
Brard, G.8
Ngo, S.D.9
Davie, J.R.10
-
73
-
-
0030953186
-
Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase
-
of outstanding interest. A complex between SMRT, HDAC and mSin3 factors is established, and histone deacetyltransferase inhibitors are used to suggest the role of this complex in nuclear-receptor-mediated repression.
-
Nagy L, Kao HY, Chakravarti D, Lin RJ, Hassig CA, Ayer DE, Schreiber SL, Evans RM. Nuclear receptor repression mediated by a complex containing SMRT, mSin3A, and histone deacetylase. of outstanding interest Cell. 89:1997;373-380 A complex between SMRT, HDAC and mSin3 factors is established, and histone deacetyltransferase inhibitors are used to suggest the role of this complex in nuclear-receptor-mediated repression.
-
(1997)
Cell
, vol.89
, pp. 373-380
-
-
Nagy, L.1
Kao, H.Y.2
Chakravarti, D.3
Lin, R.J.4
Hassig, C.A.5
Ayer, D.E.6
Schreiber, S.L.7
Evans, R.M.8
-
74
-
-
0030969516
-
Histone deacetylases associated with the mSin3 co-repressor mediate Mad transcriptional repression
-
of outstanding interest. This report makes the critical linkage between mSin3A/B and histone deactyltransferases, and uses histone deacetyltransferase to suggest their functional importance in MAD-dependent transcriptional repression.
-
Laherty CD, Yang WM, Sun JM, Davie JR, Seto E, Eisenman RN. Histone deacetylases associated with the mSin3 co-repressor mediate Mad transcriptional repression. of outstanding interest Cell. 89:1997;349-356 This report makes the critical linkage between mSin3A/B and histone deactyltransferases, and uses histone deacetyltransferase to suggest their functional importance in MAD-dependent transcriptional repression.
-
(1997)
Cell
, vol.89
, pp. 349-356
-
-
Laherty, C.D.1
Yang, W.M.2
Sun, J.M.3
Davie, J.R.4
Seto, E.5
Eisenman, R.N.6
-
75
-
-
0030959244
-
Role for N-CoR and histone deacetylase in mSin3-mediated transcriptional repression
-
of outstanding interest. In this paper the interaction between NCor and Sin3 is established by yeast two hybrid interactions, and evidence is provided for the roles of these factors and histone deacetyltransferase activator in Myc-dependent transcriptional repression.
-
Alland L, Muhle R, Hou H Jr, Potes J, Chin L, Schreiber-Agus N, DePinho RA. Role for N-CoR and histone deacetylase in mSin3-mediated transcriptional repression. of outstanding interest Nature. 387:1997;49-55 In this paper the interaction between NCor and Sin3 is established by yeast two hybrid interactions, and evidence is provided for the roles of these factors and histone deacetyltransferase activator in Myc-dependent transcriptional repression.
-
(1997)
Nature
, vol.387
, pp. 49-55
-
-
Alland, L.1
Muhle, R.2
Hou H., Jr.3
Potes, J.4
Chin, L.5
Schreiber-Agus, N.6
Depinho, R.A.7
-
76
-
-
0030916729
-
Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
-
of outstanding interest. In this manuscript, a biochemical approach is used to isolate and characterize a multicomponent complex containing histone deacetyltransferase and a series of peptides, including a 30 kDa protein as well as a protein referred to as SAP18 and SAP12.
-
Zhang Y, Iratni R, Erdjument-Bromage H, Tempst P, Reinberg D. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. of outstanding interest Cell. 89:1997;357-364 In this manuscript, a biochemical approach is used to isolate and characterize a multicomponent complex containing histone deacetyltransferase and a series of peptides, including a 30 kDa protein as well as a protein referred to as SAP18 and SAP12.
-
(1997)
Cell
, vol.89
, pp. 357-364
-
-
Zhang, Y.1
Iratni, R.2
Erdjument-Bromage, H.3
Tempst, P.4
Reinberg, D.5
-
77
-
-
0031007189
-
Histone deacetylase activity is required for full transcriptional repression by mSin3A
-
of outstanding interest. This manuscript provides evidence that links, biochemically and with use of histone deacetylase inhibitors, the mSin3/HDAC complex as functionally important for repressor events.
-
Hassig CA, Fleischer TC, Billin AN, Schreiber SL, Ayer DE. Histone deacetylase activity is required for full transcriptional repression by mSin3A. of outstanding interest Cell. 89:1997;341-347 This manuscript provides evidence that links, biochemically and with use of histone deacetylase inhibitors, the mSin3/HDAC complex as functionally important for repressor events.
-
(1997)
Cell
, vol.89
, pp. 341-347
-
-
Hassig, C.A.1
Fleischer, T.C.2
Billin, A.N.3
Schreiber, S.L.4
Ayer, D.E.5
-
78
-
-
0030272047
-
Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4
-
Verrault A, Kaufman PD, Kobayushi R, Stillman B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell. 87:1996;95-104.
-
(1996)
Cell
, vol.87
, pp. 95-104
-
-
Verrault, A.1
Kaufman, P.D.2
Kobayushi, R.3
Stillman, B.4
-
79
-
-
0032484989
-
Retinoblastoma protein recruits histone deacetylase to repress transcription
-
Brehm A, Miska EA, McCance DJ, Reid JL, Bannister AJ, Kouzarides T. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature. 391:1998;597-601.
-
(1998)
Nature
, vol.391
, pp. 597-601
-
-
Brehm, A.1
Miska, E.A.2
McCance, D.J.3
Reid, J.L.4
Bannister, A.J.5
Kouzarides, T.6
-
80
-
-
0032484904
-
Retinoblastoma protein represses transcription by recruiting a histone deacetylase
-
of special interest. A connection between the retinoblastoma protein and HDAC is provided on the basis of biochemical data.
-
Magnaghi-Jaulin L, Groisman R, Naguibneva I, Robin P, Lorain S, Le Villain JP, Troalen F, Trouche D, Harel-Bellan A. Retinoblastoma protein represses transcription by recruiting a histone deacetylase. of special interest Nature. 391:1998;601-605 A connection between the retinoblastoma protein and HDAC is provided on the basis of biochemical data.
-
(1998)
Nature
, vol.391
, pp. 601-605
-
-
Magnaghi-Jaulin, L.1
Groisman, R.2
Naguibneva, I.3
Robin, P.4
Lorain, S.5
Le Villain, J.P.6
Troalen, F.7
Trouche, D.8
Harel-Bellan, A.9
-
81
-
-
17144458786
-
Fusion proteins of the retinoic acid receptor-α recruit histone deacetylase in promyelocytic leukemia
-
of outstanding interest. This manuscript links recruitment of the co-repressor, deacetylase complex to fusion proteins causing leukemia, and maps the interaction interfaces.
-
Grignani F, De Matteis S, Nervi C, Tomassoni L, Gelmetti V, Cioce M, Fanelli M, Ruthhardt M, Ferrara FF, Zamir I, et al. Fusion proteins of the retinoic acid receptor-α recruit histone deacetylase in promyelocytic leukemia. of outstanding interest Nature. 391:1998;315-318 This manuscript links recruitment of the co-repressor, deacetylase complex to fusion proteins causing leukemia, and maps the interaction interfaces.
-
(1998)
Nature
, vol.391
, pp. 315-318
-
-
Grignani, F.1
De Matteis, S.2
Nervi, C.3
Tomassoni, L.4
Gelmetti, V.5
Cioce, M.6
Fanelli, M.7
Ruthhardt, M.8
Ferrara, F.F.9
Zamir, I.10
-
82
-
-
0032546017
-
Role of the histone deacetylase complex in acute promyelocytic leukemia
-
of outstanding interest. This manuscript links co-repressor complex binding to retinoic acid receptor fusion proteins associated with leukemia, and shows the ability of histone deacetylases to cause the block in differentiation in PLZF-induced leukemia.
-
Lin RJ, Nagy L, Satoshi I, Shao W, Miller WH Jr, Evans RM. Role of the histone deacetylase complex in acute promyelocytic leukemia. of outstanding interest Nature. 391:1998;811-814 This manuscript links co-repressor complex binding to retinoic acid receptor fusion proteins associated with leukemia, and shows the ability of histone deacetylases to cause the block in differentiation in PLZF-induced leukemia.
-
(1998)
Nature
, vol.391
, pp. 811-814
-
-
Lin, R.J.1
Nagy, L.2
Satoshi, I.3
Shao, W.4
Miller W.H., Jr.5
Evans, R.M.6
-
83
-
-
0030847164
-
SMRT co-repressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia
-
of outstanding interest. This manuscript reports silencing mediator for the retinoic acid receptor and thyroid hormone receptor (SMRT) - PLZF interactions as well as interactions of SMRT with retinoic acid receptor fusion proteins associated with leukemia.
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Hong SH, David G, Wong CW, Dejean A, Privalsky ML. SMRT co-repressor interacts with PLZF and with the PML-retinoic acid receptor alpha (RARalpha) and PLZF-RARalpha oncoproteins associated with acute promyelocytic leukemia. of outstanding interest Proc Natl Acad Sci USA. 94:1997;9028-9033 This manuscript reports silencing mediator for the retinoic acid receptor and thyroid hormone receptor (SMRT) - PLZF interactions as well as interactions of SMRT with retinoic acid receptor fusion proteins associated with leukemia.
-
(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 9028-9033
-
-
Hong, S.H.1
David, G.2
Wong, C.W.3
Dejean, A.4
Privalsky, M.L.5
-
84
-
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0030946171
-
Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: Hormone-regulated chromatin disruption is not sufficient for transcriptional activation
-
of outstanding interest. The Xenopus model system was used to discriminate chromatin regulation from non-chromatin effects of the thyroid receptor in gene activation in vivo, providing evidence that two independent functions are required. The first involves effects on chromatin; the second possibly reflects action on a more distal function.
-
Wong J, Shi YB, Wolffe AP. Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation. of outstanding interest EMBO J. 16:1997;3158-3171 The Xenopus model system was used to discriminate chromatin regulation from non-chromatin effects of the thyroid receptor in gene activation in vivo, providing evidence that two independent functions are required. The first involves effects on chromatin; the second possibly reflects action on a more distal function.
-
(1997)
EMBO J
, vol.16
, pp. 3158-3171
-
-
Wong, J.1
Shi, Y.B.2
Wolffe, A.P.3
-
85
-
-
0032006563
-
P300 and estrogen receptors cooperatively activate transcription via differential enhancement of initiation and reinitiation
-
of outstanding interest. Kraus and Kadonaga examined estrogen and antiestrogen-regulated, AF-2-dependent transcriptional activation by full-length purified human p300 functioning as a transcriptional co-activator. These results suggested a model in which liganded ER and p300 work cooperatively to increase the efficiency of productive transcription initiation, while ER alone promotes the reassembly of transcription pre-initiation process.
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Kraus WL, Kadonaga JT. p300 and estrogen receptors cooperatively activate transcription via differential enhancement of initiation and reinitiation. of outstanding interest Genes Dev. 12:1998;331-342 Kraus and Kadonaga examined estrogen and antiestrogen-regulated, AF-2-dependent transcriptional activation by full-length purified human p300 functioning as a transcriptional co-activator. These results suggested a model in which liganded ER and p300 work cooperatively to increase the efficiency of productive transcription initiation, while ER alone promotes the reassembly of transcription pre-initiation process.
-
(1998)
Genes Dev
, vol.12
, pp. 331-342
-
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Kraus, W.L.1
Kadonaga, J.T.2
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