A novel nuclear receptor superfamily member inXenopusthat associates with RXR, and shares extensive sequence similarity to the mammalian vitamin D3 receptor
- 11 January 1994
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 22 (1) , 66-71
- https://doi.org/10.1093/nar/22.1.66
Abstract
We report the isolation of xONR1, a novel member of the nuclear receptor superfamily from Xenopus laevis . xONR1 shares a high degree of amino acid sequence identity with the mammalian receptor for 1α, 25-dihydroxy vitamin D3, particularly within the DNA-binding domain, although it does not bind this ligand. xONR1 DNA binding is stimulated by association with retinoid X receptor gamma (RXR γ ).Keywords
This publication has 27 references indexed in Scilit:
- Multiplicity generates diversity in the retinoic acid signalling pathwaysPublished by Elsevier ,2003
- Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracleNature, 1993
- Promiscuous liaisonsNature, 1993
- Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptorsPublished by Elsevier ,1992
- Cloning and sequencing of a COUP transcription factor gene expressed in Xenopus embryosBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1992
- Retinoid X receptor interacts with nuclear receptors in retinoic acid, thyroid hormone and vitamin D3 signallingNature, 1992
- Diffusible factors in vertebrate embryonic inductionCell, 1992
- New insights into activation of the steroid hormone receptor superfamilyTrends in Pharmacological Sciences, 1992
- RXRβ: A coregulator that enhances binding of retinoic acid, thyroid hormone, and vitamin D receptors to their cognate response elementsCell, 1991
- Direct repeats as selective response elements for the thyroid hormone, retinoic acid, and vitamin D3 receptorsCell, 1991