Human Thyroid Nuclear Receptor
Mostrando 1-12 de 48 artigos, teses e dissertações.
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1. Immobilization and sensing ability of human thyroid nuclear receptor in nanostructured thin films / Estudo da imobilização do receptor tireoidiano humano TRβ1 em filmes finos nanoestruturados e aplicações em detecção de hormônios tireoidianos
Manipulation of materials at the nanoscale represents one of the frontiers in nanoscience and nanotechnology, mainly due to the possibility of specific controlling, improved properties, not observed if conventional bulk processing is applied. For biomolecules, in particular, processing via immobilization in the form of nanostructured films has allowed their
Publicado em: 2010
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2. Interaction of the nuclear receptors with its ligands: Structural studies of the thyroid hormone receptor, mineralocorticoid receptor and peroxisome proliferator-activated receptor / Interações dos receptores nucleares com seus ligantes: Estudos estruturais do receptor de hormônio tireoidiano, do receptor de mineralocorticóide e do receptor ativado por proliferadores peroxissomais
Nuclear receptors are a superfamily of hormone-regulated transcriptional factors. This superfamily includes, for example, the receptor for thyroid hormone, estrogen, androgen, gluco and mineralocorticoid. In this work, we used structural biology and bioinformatic tools to study the interactions between some members of the nuclear receptor superfamily and its
Publicado em: 2009
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3. Generalized resistance to thyroid hormone associated with a mutation in the ligand-binding domain of the human thyroid hormone receptor beta.
The syndrome of generalized resistance to thyroid hormone is characterized by elevated circulating levels of thyroid hormone in the presence of an overall eumetabolic state and failure to respond normally to triiodothyronine. We have evaluated a family with inherited generalized resistance to thyroid hormone for abnormalities in the thyroid hormone nuclear r
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4. Ligand selectivity by seeking hydrophobicity in thyroid hormone receptor
Selective therapeutics for nuclear receptors would revolutionize treatment for endocrine disease. Specific control of nuclear receptor activity is challenging because the internal cavities that bind hormones can be virtually identical. Only one highly selective hormone analog is known for the thyroid receptor, GC-24, an agonist for human thyroid hormone rece
National Academy of Sciences.
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5. Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex.
Transcriptional regulation by nuclear hormone receptors is thought to involve interactions with putative cofactors that may potentiate receptor function. Here we show that human thyroid hormone receptor alpha purified from HeLa cells grown in the presence of thyroid hormone (T3) is associated with a group of distinct nuclear proteins termed thyroid hormone r
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6. A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors.
Nuclear hormone receptors are transcription factors that require multiple protein-protein interactions to regulate the expression of their target genes. Using the yeast two-hybrid system, we identified a protein, thyroid hormone receptor uncoupling protein (TRUP), that specifically interacts with a region of the human thyroid hormone receptor (TR) consisting
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7. Thyroid hormone receptors bind to defined regions of the growth hormone and placental lactogen genes.
The intracellular receptor for thyroid hormone is a protein found in chromatin. Since thyroid hormone stimulates transcription of the growth hormone gene through an unknown mechanism, the hypothesis that the thyroid hormone-receptor complex interacts with defined regions of this gene has been investigated in a cell-free system. Nuclear extracts from human ly
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8. Genomic organization of the human thyroid hormone receptor alpha (c-erbA-1) gene.
The thyroid hormone receptor alpha (THRA or c-erbA-1) gene belongs to a family of genes which encode nuclear receptors for various hydrophobic ligands such as steroids, vitamin D, retinoic acid and thyroid hormones. These receptors are composed of several domains important for hormone-binding, DNA-binding, dimerization and activation of transcription. We sho
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9. Ubiquitous receptor: a receptor that modulates gene activation by retinoic acid and thyroid hormone receptors.
The cDNA for a member of the nuclear receptor family was cloned and named ubiquitous receptor (UR), since UR protein and mRNA are detected in many cell types. Rat UR/human retinoid X receptor alpha (hRXR alpha) heterodimers bound preferentially to double-stranded oligonucleotide direct repeats having the consensus half-site sequence AGGTCA and 4-nt spacing (
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10. The TRAP220 component of a thyroid hormone receptor- associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion
Cognate cDNAs are described for 2 of the 10 thyroid hormone receptor-associated proteins (TRAPs) that are immunopurified with thyroid hormone receptor α (TRα) from ligand-treated HeLa (α-2) cells. Both TRAP220 and TRAP100 contain LXXLL domains found in other nuclear receptor-interacting proteins and both appear to reside in a single complex with other TRA
The National Academy of Sciences.
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11. The N-CoR/Histone Deacetylase 3 Complex Is Required for Repression by Thyroid Hormone Receptor
Nuclear receptor corepressors (N-CoR) and silencing mediator for retinoid and thyroid receptors (SMRT) have both been implicated in thyroid hormone receptor (TR)-mediated repression. Here we show that endogenous N-CoR, TBL1, and histone deacetylase 3 (HDAC3), but not HDAC1, -2, or -4, are recruited to a stably integrated reporter gene repressed by unliganded
American Society for Microbiology.
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12. Trans-activation by thyroid hormone receptors: functional parallels with steroid hormone receptors.
The effects of thyroid hormones are mediated through nuclear receptor proteins that modulate the transcription of specific genes in target cells. We previously isolated cDNAs encoding two different mammalian thyroid hormone receptors, one from human placenta (hTR beta) and the other from rat brain (rTR alpha), and showed that their in vitro translation produ