Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor alpha
about
Isolation and characterization of a novel ligand-dependent thyroid hormone receptor-coactivating proteinAlien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamilyNuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormoneUnique forms of human and mouse nuclear receptor corepressor SMRTSpecific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor beta.Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activationAvian erythroleukemia: a model for corepressor function in cancer.Controlling gene networks and cell fate with precision-targeted DNA-binding proteins and small-molecule-based genome readers.Transcriptional regulation in acute promyelocytic leukemia.In vivo transcription factor recruitment during thyroid hormone receptor-mediated activationDirect modulation of simian virus 40 late gene expression by thyroid hormone and its receptor.Genetic dissection of thyroid hormone receptor beta: identification of mutations that separate hormone binding and transcriptional activation.SMRT isoforms mediate repression and anti-repression of nuclear receptor heterodimersAssociation of v-ErbA with Smad4 disrupts TGF-beta signaling.Functional evidence for retinoid X receptor (RXR) as a nonsilent partner in the thyroid hormone receptor/RXR heterodimer.Two silencing sub-domains of v-erbA synergize with each other, but not with RXR.Retinoic acid and retinoic acid receptors in development.Thyroid hormone-independent interaction between the thyroid hormone receptor beta2 amino terminus and coactivators.A role for helix 3 of the TRbeta ligand-binding domain in coactivator recruitment identified by characterization of a third cluster of mutations in resistance to thyroid hormone.The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors.Leukemic transformation by the v-ErbA oncoprotein entails constitutive binding to and repression of an erythroid enhancer in vivo.Nuclear export of the oncoprotein v-ErbA is mediated by acquisition of a viral nuclear export sequence.Molecular cloning and brain localization of HZF-2 alpha, a new member of the Rev-erb subfamily of orphan nuclear receptors.
P2860
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P2860
Identification of a domain required for oncogenic activity and transcriptional suppression by v-erbA and thyroid-hormone receptor alpha
description
1993 nî lūn-bûn
@nan
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
1993年论文
@zh
1993年论文
@zh-cn
name
Identification of a domain req ...... thyroid-hormone receptor alpha
@ast
Identification of a domain req ...... thyroid-hormone receptor alpha
@en
type
label
Identification of a domain req ...... thyroid-hormone receptor alpha
@ast
Identification of a domain req ...... thyroid-hormone receptor alpha
@en
prefLabel
Identification of a domain req ...... thyroid-hormone receptor alpha
@ast
Identification of a domain req ...... thyroid-hormone receptor alpha
@en
P2860
P356
P1476
Identification of a domain req ...... thyroid-hormone receptor alpha
@en
P2860
P304
10668-10672
P356
10.1073/PNAS.90.22.10668
P407
P577
1993-11-01T00:00:00Z