scispace - formally typeset
Journal ArticleDOI

Nuclear receptors enhance our understanding of transcription regulation

TLDR
Receptors for retinoic acid, vitamin D3 and the steroid and thyroid hormones belong to a family of ligand-activated enhancer-binding factors which are composed of a number of functional domains required for ligand and DNA binding, nuclear translocation, dimerization and trans -activation of transcription.
About
This article is published in Trends in Genetics.The article was published on 1988-11-01. It has received 987 citations till now. The article focuses on the topics: Small heterodimer partner & Transcription factor.

read more

Citations
More filters
Journal ArticleDOI

An Antidiabetic Thiazolidinedione Is a High Affinity Ligand for Peroxisome Proliferator-activated Receptor γ (PPARγ)

TL;DR: It is reported that thiazolidinediones are potent and selective activators of peroxisome proliferator-activated receptor γ (PPARγ), a member of the nuclear receptor superfamily recently shown to function in adipogenesis, and raised the intriguing possibility that PPARγ is a target for the therapeutic actions of this class of compounds.
Journal ArticleDOI

Activation of a member of the steroid hormone receptor superfamily by peroxisome proliferators

TL;DR: A member of the steroid hormone receptor superfamily of ligand-activated transcription factors is cloned that is activated by a diverse class of rodent hepatocarcinogens that causes proliferation of peroxisomes.
Journal ArticleDOI

The RXR heterodimers and orphan receptors

TL;DR: The historical links between the steroid and nonsteroid receptor signaling systems are established, the explosive development of the retinoid X receptor (RXR) heterodimer and orphan receptor family is charted, the impact of these discoveries on the authors' understanding of the mechanisms of hormonal signaling is explained, and emerging issues and implications are presented.
Journal ArticleDOI

A decade of molecular biology of retinoic acid receptors.

TL;DR: A review of recent developments in structure‐ function relationships of retinoic acid receptors focuses on recent developments, particularly in the area of structure‐function relationships.
Journal ArticleDOI

G1 events and regulation of cell proliferation.

TL;DR: This work has shown that switches in and out of G1 are the main determinants of post-embryonic cell proliferation rate and are defectively controlled in cancer cells.
References
More filters
Journal ArticleDOI

The steroid and thyroid hormone receptor superfamily

TL;DR: A superfamily of regulatory proteins that include receptors for thyroid hormone and the vertebrate morphogen retinoic acid is identified, suggesting mechanisms underlying morphogenesis and homeostasis may be more ubiquitous than previously expected.
Journal ArticleDOI

A human retinoic acid receptor which belongs to the family of nuclear receptors

TL;DR: The protein is homologous to the receptors for steroid hormones, thyroid hormones and vitamin D3, and appears to be a retinoic acid-inducible {Tans-acting enhancer factor, suggesting that the molecular mechanisms of the effect of vitamin A (vitamin A) on embryonic development, differentiation and tumour cell growth are similar to those described for other members of this nuclear receptor family.
Journal ArticleDOI

Functional domains of the human estrogen receptor.

TL;DR: Deletion of most or all of the hormone-binding domain leads to only about 5% constitutive transcriptional activity, yet these mutants appear to bind efficiently to an ERE in vivo.
Journal ArticleDOI

Identification of a second human retinoic acid receptor

TL;DR: It is shown that retinoic acid (RA) at physiological concentrations is effective in inducing the expression of an oestrogen-responsive reporter gene by the hap-ER chimaeric receptor, demonstrating the existence of two human retinoIC acid receptors designated RAR-α and R AR-β.
Journal ArticleDOI

Functional domains of the human glucocorticoid receptor

TL;DR: Characterization of 27 insertional mutants of the hGR allowed the location of at least four functional domains, two of which correspond to the predicted DNA- and steroid-binding domains, raising the possibility that other regions in the receptor are necessary for full transcriptional activation but are not specifically involved in steroid or DNA binding.
Related Papers (5)