A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor).
about
The novel human DNA helicase hFBH1 is an F-box proteinAdenovirus E1A functions as a cofactor for retinoic acid receptor beta (RAR beta) through direct interaction with RAR betaLigand induction of a transcriptionally active thyroid hormone receptor coactivator complexNuclear factor RIP140 modulates transcriptional activation by the estrogen receptorIsoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptorNuclear receptor corepressors activate rather than suppress basal transcription of genes that are negatively regulated by thyroid hormoneThe tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencingRIP-140 interacts with multiple nuclear receptors by means of two distinct sitesCloning and characterization of RAP250, a novel nuclear receptor coactivatorNew retinoid X receptor subtypes in zebra fish (Danio rerio) differentially modulate transcription and do not bind 9-cis retinoic acidA mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers.Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.Factor recruitment and TIF2/GRIP1 corepressor activity at a collagenase-3 response element that mediates regulation by phorbol esters and hormones.Expression of the thyroid hormone receptor gene, erbAalpha, in B lymphocytes: alternative mRNA processing is independent of differentiation but correlates with antisense RNA levels.Targeting of N-CoR and histone deacetylase 3 by the oncoprotein v-erbA yields a chromatin infrastructure-dependent transcriptional repression pathwayInteraction of proteins with transcriptionally active estrogen receptorsA natural transactivation mutation in the thyroid hormone beta receptor: impaired interaction with putative transcriptional mediators.Genetic dissection of thyroid hormone receptor beta: identification of mutations that separate hormone binding and transcriptional activation.A shift in the ligand responsiveness of thyroid hormone receptor alpha induced by heterodimerization with retinoid X receptor alphaActivation and repression by nuclear hormone receptors: hormone modulates an equilibrium between active and repressive states.Mouse retinoid X receptor contains a separable ligand-binding and transactivation domain in its E region.Mutations in the conserved C-terminal sequence in thyroid hormone receptor dissociate hormone-dependent activation from interference with AP-1 activity.A conformational switch in nuclear hormone receptors is involved in coupling hormone binding to corepressor releaseDesigner monotransregulators provide a basis for a transcriptional therapy for de novo endocrine-resistant breast cancer.Thyroid abnormalities and hepatocellular carcinoma in mice transgenic for v-erbA.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.Distinct binding determinants for 9-cis retinoic acid are located within AF-2 of retinoic acid receptor alpha.AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptorsThe ligand-binding domains of the thyroid hormone/retinoid receptor gene subfamily function in vivo to mediate heterodimerization, gene silencing, and transactivation.Functional domains of the human orphan receptor ARP-1/COUP-TFII involved in active repression and transrepressionNuclear hormone receptor antagonism with AP-1 by inhibition of the JNK pathway.Corepressor SMRT functions as a coactivator for thyroid hormone receptor T3Ralpha from a negative hormone response element.Characterization of the ligand-dependent transactivation domain of thyroid hormone receptorVarious modes of gene regulation by nuclear receptors for steroid and thyroid hormones.Activation function 1 of retinoic acid receptor beta 2 is an acidic activator resembling VP16.The thyroid hormone receptor functions as a ligand-operated developmental switch between proliferation and differentiation of erythroid progenitors.Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine.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.Phosphorylation of human estrogen receptor alpha at serine 118 by two distinct signal transduction pathways revealed by phosphorylation-specific antisera.
P2860
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P2860
A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor).
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
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@ast
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@en
type
label
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@ast
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@en
prefLabel
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@ast
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@en
P2093
P2860
P356
P1476
A conserved C-terminal sequenc ...... the thyroid hormone receptor).
@en
P2093
P2860
P304
P356
10.1128/MCB.13.6.3675
P407
P577
1993-06-01T00:00:00Z