Therapeutic potential of selective modulators of nuclear receptor action
References (57)
- et al.
The nuclear receptor superfamily: the second decade
Cell
(1995) - et al.
Peroxisome proliferator-activated receptor agonists
Curr Opin Chem Biol
(1997) - et al.
An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway (of outstanding interest)
Cell
(1998) - et al.
The nuclear receptor ligand binding domain: structure and function
Curr Opin Cell Biol
(1998) - et al.
Co-activators and co-repressors in integration of transcriptional responses
Curr Opin Cell Biol
(1998) - et al.
The receptor-associated coactivator 3 activates transcription through CREB-binding protein recruitment and autoregulation
J Biol Chem
(1998) - et al.
Differential interaction of nuclear receptors with the putative human transcriptional coactivator hTIF1
J Biol Chem
(1997) - et al.
Enhancement of estrogen receptor transcriptional activity by the coactivator GRIP-1 highlights the role of activation function 2 in determining estrogen receptor pharmacology
J Biol Chem
(1998) - et al.
What's up and down with histone deacetylation and transcription?
Cell
(1997) - et al.
Distinct domains of the ReIA NF-κB subunit are required for negative crosstalk and direct interaction with the glucocorticoid receptor
J Biol Chem
(1997)
A CBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptor
Cell
Dimerization of the glucocorticoid receptor is not essential for survival (of outstanding interest)
Cell
Two distinct actions of retinoid-receptor ligands
Nature
Effects of novel retinoid X receptor-selective ligands on myeloid leukemia differentiation and proliferation in vitro
Blood
Activation of three distinct RXR/RAR heterodimers induces growth arrest and differentiation of neuroblastoma cells
J Biol Chem
The novel estrogen receptor-β subtype: potential role in the cell- and promoter-specific actions of estrogens and anti-estrogens
FEBS Lett
Crystal structure of the ligand binding domain of the human nuclear receptor RXR alpha
Nature
Crystal structure of the RARγ ligand binding domain bound to all-trans retinoic acid
Nature
A structural role for hormone in the thyroid hormone receptor
Nature
Molecular basis of agonism and antagonism in the oestrogen receptor (of outstanding interest)
Nature
A canonical structure for the ligand-binding domain of nuclear receptors
Nat Struct Biol
A transcriptional co-repressor that interacts with nuclear hormone receptors
Nature
The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways (of special interest)
EMBO J
Isoforms of steroid receptor coactivator 1 differ in their ability to potentiate transcription by estrogen receptor (of special interest)
EMBO J
Nuclear receptor binding sites of coactivators glucocorticoid receptor interacting protein 1(GRIP1) and steroid receptor coactivator 1(SRC1): multiple motifs with different binding specificities
Mol Endocrinol
Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation
EMBO J
Ligand induction of a transcriptionally active thyroid hormone receptor coactivator complex
Proc Nat Acad Sci USA
Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor
Nature
Cited by (67)
Glucocorticoid compounds in drug discovery by targeting glucocorticoid receptor protein
2023, Privileged Scaffolds in Drug DiscoveryRetinoic acid receptors: From molecular mechanisms to cancer therapy
2015, Molecular Aspects of MedicineCitation Excerpt :The inhibition of AP-1 activity by RAR/RXR association involves the expression of several genes such as those of osteocalcin, stromelysin and collagenase (Schüle et al., 1990). As for Stat5 and ERα, close regulatory regions for both RARs and AP-1 have been reported in their gene promoters (Germain et al., 2006a; Lafyatis et al., 1990; Nicholson et al., 1990; Resche-Rigon and Gronemeyer, 1998; Schüle et al., 1990). RARs can exert both genomic and non-genomic effects.
Discovery of a potent and dissociated non-steroidal glucocorticoid receptor agonist containing an alkyl carbinol pharmacophore
2014, Bioorganic and Medicinal Chemistry LettersImmediate early response genes and cell transformation
2013, Pharmacology and TherapeuticsCAC1 negatively regulates RARα activity through cooperation with HDAC
2012, Biochemical and Biophysical Research CommunicationsCitation Excerpt :NRs including RAR are ligand-inducible transcription factors that specifically regulate the expression of target genes. All NRs share a common modular structure consisting of an N-terminal transcriptional activation domain (AF-1), a conserved DNA-binding domain (DBD), a hinge region (D), and a C-terminal ligand-binding domain (LBD) that overlaps with the second transcriptional activation domain (AF-2) [1,2,4]. Retinoid signaling is generated by two families of nuclear receptors, the RAR and retinoid X receptor (RXR), which bind as RAR/RXR heterodimers to cis-acting RA response elements (RAREs) located in the regulatory sequences of target genes [5].
A conserved surface on the ligand binding domain of nuclear receptors for allosteric control
2012, Molecular and Cellular Endocrinology