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Volumn 32, Issue 6, 2004, Pages 1957-1966

Multiple domains of the receptor-interacting protein 140 contribute to transcription inhibition

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL NUCLEUS RECEPTOR; HISTONE DEACETYLASE; HISTONE DEACETYLASE INHIBITOR; RECEPTOR INTERACTING PROTEIN 140; REGULATOR PROTEIN; TRICHOSTATIN A; UNCLASSIFIED DRUG;

EID: 3042750469     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh524     Document Type: Article
Times cited : (67)

References (53)
  • 1
    • 0034032022 scopus 로고    scopus 로고
    • Estrogen receptor interaction with co-activators and co-repressors
    • Klinge,C.M. (2000) Estrogen receptor interaction with co-activators and co-repressors. Steroids, 65, 227-251.
    • (2000) Steroids , vol.65 , pp. 227-251
    • Klinge, C.M.1
  • 2
    • 0037192501 scopus 로고    scopus 로고
    • Molecular determinants for the tissue specificity of SERMs
    • Shang,Y. and Brown,M. (2002) Molecular determinants for the tissue specificity of SERMs. Science, 295, 2465-2468.
    • (2002) Science , vol.295 , pp. 2465-2468
    • Shang, Y.1    Brown, M.2
  • 3
    • 2342528466 scopus 로고    scopus 로고
    • Historic deacetylase activity and estrogen receptor alpha levels modulate the transcriptional activity of partial antiestrogens
    • in press
    • Margueron,R., Duong,V., Bonnet,S., Escande,A., Vignon,F., Balaguer,P. and Cavailles,V. (2004) Historic deacetylase activity and estrogen receptor alpha levels modulate the transcriptional activity of partial antiestrogens. J. Mol. Endocrinol., in press.
    • (2004) J. Mol. Endocrinol.
    • Margueron, R.1    Duong, V.2    Bonnet, S.3    Escande, A.4    Vignon, F.5    Balaguer, P.6    Cavailles, V.7
  • 5
    • 0031924106 scopus 로고    scopus 로고
    • Localisation of receptor interacting protein 140 (RIP140) within 100 kb of D21S13 on 21q11, a gene-poor region of the human genome
    • Katsanis,N., Ives,J.H., Groet,J., Nizetic,D. and Fisher,E.M. (1998) Localisation of receptor interacting protein 140 (RIP140) within 100 kb of D21S13 on 21q11, a gene-poor region of the human genome. Hum. Genet., 102, 221-223.
    • (1998) Hum. Genet. , vol.102 , pp. 221-223
    • Katsanis, N.1    Ives, J.H.2    Groet, J.3    Nizetic, D.4    Fisher, E.M.5
  • 6
    • 0029850086 scopus 로고    scopus 로고
    • RIP-140 interacts with multiple nuclear receptors by means of two distinct sites
    • L'Horset,F., Dauvois,S., Heery,D.M., Cavailles,V. and Parker,M.G. (1996) RIP-140 interacts with multiple nuclear receptors by means of two distinct sites. Mol. Cell. Biol., 16, 6029-6036.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6029-6036
    • L'Horset, F.1    Dauvois, S.2    Heery, D.M.3    Cavailles, V.4    Parker, M.G.5
  • 7
    • 0030669765 scopus 로고    scopus 로고
    • Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators
    • Ikonen,T., Palvimo,J.J. and Janne,O.A. (1997) Interaction between the amino- and carboxyl-terminal regions of the rat androgen receptor modulates transcriptional activity and is influenced by nuclear receptor coactivators. J. Biol. Chem., 272, 29821-29828.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29821-29828
    • Ikonen, T.1    Palvimo, J.J.2    Janne, O.A.3
  • 8
    • 0030771215 scopus 로고    scopus 로고
    • Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction
    • Masuyama,H., Brownfield,C.M., St-Arnaud,R. and MacDonald,P.N. (1997) Evidence for ligand-dependent intramolecular folding of the AF-2 domain in vitamin D receptor-activated transcription and coactivator interaction. Mol. Endocrinol., 11, 1507-1517.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 1507-1517
    • Masuyama, H.1    Brownfield, C.M.2    St-Arnaud, R.3    MacDonald, P.N.4
  • 9
    • 0032567204 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha
    • Miyata,K.S., McCaw,S.E., Meertens,L.M., Patel,H.V., Rachubinski,R.A. and Capone,J.P. (1998) Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha. Mol. Cell. Endocrinol., 146, 69-76.
    • (1998) Mol. Cell. Endocrinol. , vol.146 , pp. 69-76
    • Miyata, K.S.1    McCaw, S.E.2    Meertens, L.M.3    Patel, H.V.4    Rachubinski, R.A.5    Capone, J.P.6
  • 10
    • 0033580993 scopus 로고    scopus 로고
    • Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids
    • Subramaniam,N., Treuter,E. and Okret,S. (1999) Receptor interacting protein RIP140 inhibits both positive and negative gene regulation by glucocorticoids. J. Biol. Chem., 274, 18121-18127.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18121-18127
    • Subramaniam, N.1    Treuter, E.2    Okret, S.3
  • 11
    • 0034927664 scopus 로고    scopus 로고
    • RIP 140 modulates transcription of the steroidogenic acute regulatory protein gene through interactions with both SF-1 and DAX-1
    • Sugawara,T., Abe,S., Sakuragi,N., Fujimoto,Y., Nomura,E., Fujieda,K., Saito.M. and Fujimoto,S. (2001) RIP 140 modulates transcription of the steroidogenic acute regulatory protein gene through interactions with both SF-1 and DAX-1. Endocrinology, 142, 3570-3577.
    • (2001) Endocrinology , vol.142 , pp. 3570-3577
    • Sugawara, T.1    Abe, S.2    Sakuragi, N.3    Fujimoto, Y.4    Nomura, E.5    Fujieda, K.6    Saito, M.7    Fujimoto, S.8
  • 12
    • 0033529692 scopus 로고    scopus 로고
    • Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs
    • Kumar,M.B., Tarpey,R.W. and Perdew,G.H. (1999) Differential recruitment of coactivator RIP140 by Ah and estrogen receptors. Absence of a role for LXXLL motifs. J. Biol. Chem., 274, 22155-22164.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22155-22164
    • Kumar, M.B.1    Tarpey, R.W.2    Perdew, G.H.3
  • 13
    • 0035064047 scopus 로고    scopus 로고
    • Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140
    • Zilliacus,J., Holter,E., Wakui,H., Tazawa,H., Treuter,E. and Gustafsson,J. A. (2001) Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140. Mol. Endocrinol., 15, 501-511.
    • (2001) Mol. Endocrinol. , vol.15 , pp. 501-511
    • Zilliacus, J.1    Holter, E.2    Wakui, H.3    Tazawa, H.4    Treuter, E.5    Gustafsson, J.A.6
  • 14
    • 0037315071 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect
    • Teyssier,C., Beiguise,K., Galtier,F., Cavailles,V. and Chalbos,D. (2003) Receptor-interacting protein 140 binds c-Jun and inhibits estradiol-induced activator protein-1 activity by reversing glucocorticoid receptor-interacting protein 1 effect. Mol. Endocrinol., 17, 287-299.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 287-299
    • Teyssier, C.1    Beiguise, K.2    Galtier, F.3    Cavailles, V.4    Chalbos, D.5
  • 16
    • 0034731401 scopus 로고    scopus 로고
    • Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing
    • Wei,L.N., Hu,X., Chandra,D., Seto,E. and Farooqui,M. (2000) Receptor-interacting protein 140 directly recruits histone deacetylases for gene silencing. J. Biol. Chem., 275, 40782-40787.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40782-40787
    • Wei, L.N.1    Hu, X.2    Chandra, D.3    Seto, E.4    Farooqui, M.5
  • 17
    • 0035724042 scopus 로고    scopus 로고
    • Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP
    • Vo,N., Fjeld,C. and Goodman,R.H. (2001) Acetylation of nuclear hormone receptor-interacting protein RIP140 regulates binding of the transcriptional corepressor CtBP. Mol. Cell. Biol., 21, 6181-6188.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6181-6188
    • Vo, N.1    Fjeld, C.2    Goodman, R.H.3
  • 19
    • 0036190459 scopus 로고    scopus 로고
    • CtBP, an unconventional transcriptional corepressor in development and oncogenesis
    • Chinnadurai,G. (2002) CtBP, an unconventional transcriptional corepressor in development and oncogenesis. Mol. Cell, 9, 213-224.
    • (2002) Mol. Cell , vol.9 , pp. 213-224
    • Chinnadurai, G.1
  • 20
    • 0036314926 scopus 로고    scopus 로고
    • Overlapping and unique roles for C-terminal binding protein 1 (CtBP1) and CtBP2 during mouse development
    • Hildebrand,J.D. and Soriano,P. (2002) Overlapping and unique roles for C-terminal binding protein 1 (CtBP1) and CtBP2 during mouse development. Mol. Cell. Biol., 22, 5296-5307.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5296-5307
    • Hildebrand, J.D.1    Soriano, P.2
  • 21
    • 0035881277 scopus 로고    scopus 로고
    • Functional knockout of the corepressor CtBP by the second exon of adenovirus E1a relieves repression of transcription
    • Sundqvist,A., Bajak,E., Kurup,S.D., Sollerbrant,K. and Svensson,C. (2001) Functional knockout of the corepressor CtBP by the second exon of adenovirus E1a relieves repression of transcription. Exp. Cell Res., 268, 284-293.
    • (2001) Exp. Cell Res. , vol.268 , pp. 284-293
    • Sundqvist, A.1    Bajak, E.2    Kurup, S.D.3    Sollerbrant, K.4    Svensson, C.5
  • 22
    • 0034685893 scopus 로고    scopus 로고
    • mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity
    • Lemercier,C., Verdel,A., Galloo,B., Curtet,S., Brocard,M.P. and Khochbin,S. (2000) mHDA1/HDAC5 histone deacetylase interacts with and represses MEF2A transcriptional activity. J. Biol. Chem., 275, 15594-15599.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15594-15599
    • Lemercier, C.1    Verdel, A.2    Galloo, B.3    Curtet, S.4    Brocard, M.P.5    Khochbin, S.6
  • 25
    • 0032931768 scopus 로고    scopus 로고
    • C-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins
    • Sewalt,R.G., Gunster,M.J., van der Vlag,J., Satijn,D.P. and Otte,A.P. (1999) C-Terminal binding protein is a transcriptional repressor that interacts with a specific class of vertebrate Polycomb proteins. Mol. Cell. Biol., 19, 777-787.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 777-787
    • Sewalt, R.G.1    Gunster, M.J.2    van der Vlag, J.3    Satijn, D.P.4    Otte, A.P.5
  • 26
    • 0032502782 scopus 로고    scopus 로고
    • Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif
    • Schaeper,U., Subramanian,T., Lim,L., Boyd,J.M. and Chinnadurai,G. (1998) Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif. J. Biol. Chem., 273, 8549-8552.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8549-8552
    • Schaeper, U.1    Subramanian, T.2    Lim, L.3    Boyd, J.M.4    Chinnadurai, G.5
  • 28
    • 0030834976 scopus 로고    scopus 로고
    • Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family
    • Yang,W.M., Yao,Y.L., Sun,J.M., Davie,J.R. and Seto,E. (1997) Isolation and characterization of cDNAs corresponding to an additional member of the human histone deacetylase gene family. J. Biol. Chem., 272, 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
  • 29
    • 0033964223 scopus 로고    scopus 로고
    • Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression
    • Kao,H.Y., Downes,M., Ordentlich,P. and Evans,R.M. (2000) Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression. Genes Der., 14, 55-66.
    • (2000) Genes Der. , vol.14 , pp. 55-66
    • Kao, H.Y.1    Downes, M.2    Ordentlich, P.3    Evans, R.M.4
  • 30
    • 0032951135 scopus 로고    scopus 로고
    • The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activity of estrogen receptors ERalpha and ERbeta
    • Johansson,L., Thomsen,J.S., Damdimopoulos,A.E., Spyrou,G., Gustafsson,J.A. and Treuter,E. (1999) The orphan nuclear receptor SHP inhibits agonist-dependent transcriptional activity of estrogen receptors ERalpha and ERbeta. J. Biol. Chem., 274, 345-353.
    • (1999) J. Biol. Chem. , vol.274 , pp. 345-353
    • Johansson, L.1    Thomsen, J.S.2    Damdimopoulos, A.E.3    Spyrou, G.4    Gustafsson, J.A.5    Treuter, E.6
  • 31
    • 0027205024 scopus 로고
    • Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF7 breast cancer cells without affecting c-fos and c-jun synthesis
    • Philips,A., Chalbos,D. and Rochefort,H. (1993) Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF7 breast cancer cells without affecting c-fos and c-jun synthesis. J. Biol. Chem., 268, 14103-14108.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14103-14108
    • Philips, A.1    Chalbos, D.2    Rochefort, H.3
  • 32
    • 0033330261 scopus 로고    scopus 로고
    • Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1 alpha and estrogen receptors
    • Thenot,S., Bonnet,S., Boulahtouf,A., Margeat,E., Royer,C.A., Borgna,J.L. and Cavailles,V. (1999) Effect of ligand and DNA binding on the interaction between human transcription intermediary factor 1 alpha and estrogen receptors. Mol. Endocrinol., 13, 2137-2150.
    • (1999) Mol. Endocrinol. , vol.13 , pp. 2137-2150
    • Thenot, S.1    Bonnet, S.2    Boulahtouf, A.3    Margeat, E.4    Royer, C.A.5    Borgna, J.L.6    Cavailles, V.7
  • 33
    • 0031741654 scopus 로고    scopus 로고
    • Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2
    • Lee,C.H., Chinpaisal,C. and Wei,L.N. (1998) Cloning and characterization of mouse RIP140, a corepressor for nuclear orphan receptor TR2. Mol. Cell. Biol., 18, 6745-6755.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 6745-6755
    • Lee, C.H.1    Chinpaisal, C.2    Wei, L.N.3
  • 34
    • 0032230250 scopus 로고    scopus 로고
    • Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner)
    • Seol,W., Hantein,B., Brown,M. and Moore,D.D. (1998) Inhibition of estrogen receptor action by the orphan receptor SHP (short heterodimer partner). Mol. Endocrinol., 12, 1551-1557.
    • (1998) Mol. Endocrinol. , vol.12 , pp. 1551-1557
    • Seol, W.1    Hantein, B.2    Brown, M.3    Moore, D.D.4
  • 36
    • 0037033108 scopus 로고    scopus 로고
    • Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP)
    • Hickabottom,M., Parker,G.A., Freemont,P., Crook,T. and Allday,M.J. (2002) Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminal-binding protein (CtBP). J. Biol. Chem., 277, 47197-47204.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47197-47204
    • Hickabottom, M.1    Parker, G.A.2    Freemont, P.3    Crook, T.4    Allday, M.J.5
  • 37
    • 0032808135 scopus 로고    scopus 로고
    • XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus development
    • Brannon,M., Brown,J.D., Bates,R., Kimelman,D. and Moon,R.T. (1999) XCtBP is a XTcf-3 co-repressor with roles throughout Xenopus development. Development, 126, 3159-3170.
    • (1999) Development , vol.126 , pp. 3159-3170
    • Brannon, M.1    Brown, J.D.2    Bates, R.3    Kimelman, D.4    Moon, R.T.5
  • 38
    • 0035353203 scopus 로고    scopus 로고
    • The corepressor CtBP interacts with Evi-1 to repress transforming growth factor beta signaling
    • Izutsu,K., Kurokawa,M., Imai,Y., Maki,K., Mitani,K. and Hirai,H. (2001) The corepressor CtBP interacts with Evi-1 to repress transforming growth factor beta signaling. Blood, 97, 2815-2822.
    • (2001) Blood , vol.97 , pp. 2815-2822
    • Izutsu, K.1    Kurokawa, M.2    Imai, Y.3    Maki, K.4    Mitani, K.5    Hirai, H.6
  • 39
    • 0034525302 scopus 로고    scopus 로고
    • RIBEYE, a component of synaptic ribbons: A protein's journey through evolution provides insight into synaptic ribbon function
    • Schmitz,F., Konigstorfer,A. and Sudhof,T.C. (2000) RIBEYE, a component of synaptic ribbons: a protein's journey through evolution provides insight into synaptic ribbon function. Neuron, 28, 857-872.
    • (2000) Neuron , vol.28 , pp. 857-872
    • Schmitz, F.1    Konigstorfer, A.2    Sudhof, T.C.3
  • 40
    • 0034865435 scopus 로고    scopus 로고
    • The CtBP family: Enigmatic and enzymatic transcriptional co-repressors
    • Turner,J. and Crossley,M. (2001) The CtBP family: enigmatic and enzymatic transcriptional co-repressors. Bioessays, 23, 683-690.
    • (2001) Bioessays , vol.23 , pp. 683-690
    • Turner, J.1    Crossley, M.2
  • 42
    • 0037040581 scopus 로고    scopus 로고
    • Regulation of corepressor function by nuclear NADH
    • Zhang,Q., Piston,D.W. and Goodman,R.H. (2002) Regulation of corepressor function by nuclear NADH. Science, 295, 1895-1897.
    • (2002) Science , vol.295 , pp. 1895-1897
    • Zhang, Q.1    Piston, D.W.2    Goodman, R.H.3
  • 43
    • 0038657690 scopus 로고    scopus 로고
    • Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140
    • Tazawa,H., Osman,W., Shoji,Y., Treuter,E., Gustafsson,J.A. and Zilliacus,J. (2003) Regulation of subnuclear localization is associated with a mechanism for nuclear receptor corepression by RIP140. Mol. Cell Biol., 23, 4187-4198.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4187-4198
    • Tazawa, H.1    Osman, W.2    Shoji, Y.3    Treuter, E.4    Gustafsson, J.A.5    Zilliacus, J.6
  • 45
    • 0038022868 scopus 로고    scopus 로고
    • Characterization of receptor-interacting protein RIP140 in the regulation of SF-1 responsive target genes
    • Mellgren,G., Borud,B., Hoang,T., Yri,O.E., Fladeby,C., Lien,E.A. and Lund,J. (2003) Characterization of receptor-interacting protein RIP140 in the regulation of SF-1 responsive target genes. Mol. Cell. Endocrinol., 203, 91-103.
    • (2003) Mol. Cell. Endocrinol. , vol.203 , pp. 91-103
    • Mellgren, G.1    Borud, B.2    Hoang, T.3    Yri, O.E.4    Fladeby, C.5    Lien, E.A.6    Lund, J.7
  • 46
    • 0033564130 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase relieve ETO-mediated repression and induce differentiation of AML1-ETO leukemia cells
    • Wang,J., Saunthararajah,Y., Redner,R.L. and Liu,J.M. (1999) Inhibitors of histone deacetylase relieve ETO-mediated repression and induce differentiation of AML1-ETO leukemia cells. Cancer Res., 59, 2766-2769.
    • (1999) Cancer Res. , vol.59 , pp. 2766-2769
    • Wang, J.1    Saunthararajah, Y.2    Redner, R.L.3    Liu, J.M.4
  • 47
    • 0033568028 scopus 로고    scopus 로고
    • HDAC4 deacetylase associates with and represses the MEF2 transcription factor
    • Miska,E.A., Karlsson,C., Langley,E., Nielsen,S.J., Pines,J. and Kouzarides,T. (1999) HDAC4 deacetylase associates with and represses the MEF2 transcription factor. EMBO J., 18, 5099-5107.
    • (1999) EMBO J. , vol.18 , pp. 5099-5107
    • Miska, E.A.1    Karlsson, C.2    Langley, E.3    Nielsen, S.J.4    Pines, J.5    Kouzarides, T.6
  • 49
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola,A.R. and Yao,T.P. (2002) Molecular cloning and characterization of a novel histone deacetylase HDAC10. J. Biol. Chem., 277, 3350-3356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 50
    • 0035793107 scopus 로고    scopus 로고
    • Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin
    • Furumai,R., Komatsu,Y., Nishino,N., Khochbin,S., Yoshida,M. and Horinouchi,S. (2001) Potent histone deacetylase inhibitors built from trichostatin A and cyclic tetrapeptide antibiotics including trapoxin. Proc. Natl Acad. Sci. USA, 98, 87-92.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 87-92
    • Furumai, R.1    Komatsu, Y.2    Nishino, N.3    Khochbin, S.4    Yoshida, M.5    Horinouchi, S.6
  • 51
    • 0037248643 scopus 로고    scopus 로고
    • Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms
    • Fernandes,I., Bastien,Y., Wai,T., Nygard,K., Lin,R., Cormier,O., Lee,H.S., Eng,F., Bertos,N.R., Pelletier,N. et al. (2003) Ligand-dependent nuclear receptor corepressor LCoR functions by histone deacetylase-dependent and -independent mechanisms. Mol. Cell, 11, 139-150.
    • (2003) Mol. Cell , vol.11 , pp. 139-150
    • Fernandes, I.1    Bastien, Y.2    Wai, T.3    Nygard, K.4    Lin, R.5    Cormier, O.6    Lee, H.S.7    Eng, F.8    Bertos, N.R.9    Pelletier, N.10
  • 52
    • 0035808460 scopus 로고    scopus 로고
    • Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor
    • Zhang,C.L., McKinsey,T.A., Lu,J.R. and Olson,E.N. (2001) Association of COOH-terminal-binding protein (CtBP) and MEF2-interacting transcription repressor (MITR) contributes to transcriptional repression of the MEF2 transcription factor. J. Biol. Chem., 276, 35-39.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35-39
    • Zhang, C.L.1    McKinsey, T.A.2    Lu, J.R.3    Olson, E.N.4
  • 53
    • 2442485925 scopus 로고    scopus 로고
    • Characterisation of four autonomous repression domains in the corepressor RIP140
    • in press
    • Christian,M., Tullet,J.M. and Parker,M.G. (2004) Characterisation of four autonomous repression domains in the corepressor RIP140. J. Biol. Chem., in press.
    • (2004) J. Biol. Chem.
    • Christian, M.1    Tullet, J.M.2    Parker, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.