A transcriptional co-repressor that interacts with nuclear hormone receptors
暂无分享,去创建一个
[1] Thorsten Heinzel,et al. Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor , 1995, Nature.
[2] William Bourguet,et al. Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α , 1995, Nature.
[3] G. Tong,et al. Ligand Modulates the Interaction of Thyroid Hormone Receptor with the Basal Transcription Machinery (*) , 1995, The Journal of Biological Chemistry.
[4] P. Chambon,et al. The N‐terminal part of TIF1, a putative mediator of the ligand‐dependent activation function (AF‐2) of nuclear receptors, is fused to B‐raf in the oncogenic protein T18. , 1995, The EMBO journal.
[5] R. Eisenman,et al. Mad-max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3 , 1995, Cell.
[6] L. Chin,et al. An amino-terminal domain of Mxi1 mediates anti-myc oncogenic activity and interacts with a homolog of the Yeast Transcriptional Repressor SIN3 , 1995, Cell.
[7] Toshihiro Tanaka,et al. Inhibition of skin development by targeted expression of a dominant-negative retinoic acid receptor , 1995, Nature.
[8] D. Moore,et al. Interaction of thyroid-hormone receptor with a conserved transcriptional mediator , 1995, Nature.
[9] B. O’Malley,et al. The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing , 1995, Molecular and cellular biology.
[10] D. Moore,et al. Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors. , 1995, Molecular endocrinology.
[11] Roger Brent,et al. Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins , 1994, Cell.
[12] M. Parker,et al. Interaction of proteins with transcriptionally active estrogen receptors. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[13] U. Lendahl,et al. Thyroid abnormalities and hepatocellular carcinoma in mice transgenic for v‐erbA. , 1994, The EMBO journal.
[14] B. Raaka,et al. Functional evidence for ligand-dependent dissociation of thyroid hormone and retinoic acid receptors from an inhibitory cellular factor , 1994, Molecular and cellular biology.
[15] K. Struhl,et al. Functional dissection of the yeast Cyc8–Tupl transcriptional co-repressor complex , 1994, Nature.
[16] G. Martin,et al. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. , 1994, Science.
[17] R. Evans,et al. Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor alpha. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[18] D. Reinberg,et al. Interaction of human thyroid hormone receptor beta with transcription factor TFIIB may mediate target gene derepression and activation by thyroid hormone. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[19] S. Collins,et al. A dominant negative retinoic acid receptor blocks neutrophil differentiation at the promyelocyte stage. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[20] R. Roeder,et al. Unliganded thyroid hormone receptor inhibits formation of a functional preinitiation complex: implications for active repression. , 1993, Genes & development.
[21] S. Elledge,et al. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. , 1993, Genes & development.
[22] K. Umesono,et al. Functional inhibition of retinoic acid response by dominant negative retinoic acid receptor mutants. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[23] S. Elledge,et al. Durfee, T. et al. The Retinoblastoma protein associates with protein phosphatase type 1 catalytic subunit. Genes Dev. 7, 555-569 , 1993 .
[24] R. Evans,et al. A mutated retinoic acid receptor-alpha exhibiting dominant-negative activity alters the lineage development of a multipotent hematopoietic cell line. , 1992, Genes & development.
[25] B. O’Malley,et al. Kindred S thyroid hormone receptor is an active and constitutive silencer and a repressor for thyroid hormone and retinoic acid responses. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[26] P. Chambon,et al. Multiplicity generates diversity in the retinoic acid signalling pathways. , 1992, Trends in biochemical sciences.
[27] T. Bugge,et al. RXR alpha, a promiscuous partner of retinoic acid and thyroid hormone receptors. , 1992, The EMBO journal.
[28] R. Renkawitz,et al. A transferable silencing domain is present in the thyroid hormone receptor, in the v‐erbA oncogene product and in the retinoic acid receptor. , 1992, The EMBO journal.
[29] Z. Parandoosh,et al. Interaction of glucocorticoid analogues with the human glucocorticoid receptor , 1992, The Journal of Steroid Biochemistry and Molecular Biology.
[30] Alexander D. Johnson,et al. Ssn6-Tup1 is a general repressor of transcription in yeast , 1992, Cell.
[31] K. Umesono,et al. Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signalling , 1992, Nature.
[32] C. Glass,et al. RXRβ: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elements , 1991, Cell.
[33] K. Umesono,et al. A direct repeat in the cellular retinol-binding protein type II gene confers differential regulation by RXR and RAR , 1991, Cell.
[34] R. Evans,et al. Characterization of DNA binding and retinoic acid binding properties of retinoic acid receptor. , 1991, Proceedings of the National Academy of Sciences of the United States of America.
[35] C. Malbon,et al. Immunological approaches for probing receptor structure and function. , 1991, Trends in pharmacological sciences.
[36] H. Beug,et al. v-erbA oncogene activation entails the loss of hormone-dependent regulator activity of c-erbA , 1990, Cell.
[37] R. Evans,et al. Nuclear receptor that identifies a novel retinoic acid response pathway , 1990, Nature.
[38] R. Renkawitz,et al. Modular structure of a chicken lysozyme silencer: Involvement of an unusual thyroid hormone receptor binding site , 1990, Cell.
[39] J. Harney,et al. Thyroid hormone aporeceptor represses T3-inducible promoters and blocks activity of the retinoic acid receptor. , 1989, The New biologist.
[40] M. Levine,et al. Transcriptional repression of eukaryotic promoters , 1989, Cell.
[41] H. Stunnenberg,et al. Repression of transcription mediated at a thyroid hormone response element by the v-erb-A oncogene product , 1989, Nature.
[42] Klaus Damm,et al. Protein encoded by v-erbA functions as a thyroid-hormone receptor antagonist , 1989, Nature.
[43] R. Evans,et al. Multiple and cooperative trans-activation domains of the human glucocorticoid receptor , 1988, Cell.
[44] P. Chambon,et al. The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function , 1988, Cell.
[45] P. Chambon,et al. The yeast UASG is a transcriptional enhancer in human hela cells in the presence of the GAL4 trans-activator , 1988, Cell.
[46] M. Zenke,et al. Characterization of the hormone‐binding domain of the chicken c‐erbA/thyroid hormone receptor protein. , 1988, The EMBO journal.
[47] R. Evans,et al. Identification of a novel thyroid hormone receptor expressed in the mammalian central nervous system. , 1987, Science.
[48] O. Gandrillon,et al. Expression of the v-erbA oncogene in chicken embryo fibroblasts stimulates their proliferation in vitro and enhances tumor growth in vivo , 1987, Cell.
[49] T. Graf,et al. A single point mutation in erbA restores the erythroid transforming potential of a mutant avian erythroblastosis virus (AEV) defective in both erbA and erbB oncogenes. , 1987, The EMBO journal.
[50] R. Evans,et al. The c-erb-A gene encodes a thyroid hormone receptor , 1986, Nature.
[51] H. Beug,et al. The c-erb-A protein is a high-affinity receptor for thyroid hormone , 1986, Nature.
[52] R. Evans,et al. Domain structure of human glucocorticoid receptor and its relationship to the v-erb-A oncogene product , 1985, Nature.