(Q40948029)

English

Quantity of partial agonist activity for antiglucocorticoids complexed with mutant glucocorticoid receptors is constant in two different transactivation assays but not predictable from steroid structure

scientific article published on February 1999

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scholarly article

1 reference

Europe PubMed Central

25 September 2017

Quantity of partial agonist activity for antiglucocorticoids complexed with mutant glucocorticoid receptors is constant in two different transactivation assays but not predictable from steroid structure (English)

1 reference

Europe PubMed Central

25 September 2017

author name string

N J Sarlis

1

1 reference

Europe PubMed Central

25 September 2017

S F Bayly

2

1 reference

Europe PubMed Central

25 September 2017

D Szapary

3

1 reference

Europe PubMed Central

25 September 2017

S S Simons

4

1 reference

Europe PubMed Central

25 September 2017

publication date

1 February 1999

1 reference

Europe PubMed Central

25 September 2017

The Journal of Steroid Biochemistry and Molecular Biology

1 reference

Europe PubMed Central

25 September 2017

68

1 reference

Europe PubMed Central

25 September 2017

3-4

1 reference

Europe PubMed Central

25 September 2017

89-102

1 reference

Europe PubMed Central

25 September 2017

Promoter context- and response element-dependent specificity of the transcriptional activation and modulating functions of retinoic acid receptors

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Determinants of promoter-specific activity by glucocorticoid receptor

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Identification of multiple, widely spaced estrogen-responsive regions in the rat progesterone receptor gene

1 reference

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Antiglucocorticoid steroids have increased agonist activity in those hepatoma cell lines that are more sensitive to glucocorticoids

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Unlinked regulation of the sensitivity of primary glucocorticoid-inducible responses in mouse mammary tumor virus infected Fu5-5 rat hepatoma cells

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Repression of the alpha-fetoprotein gene promoter by progesterone and chimeric receptors in the presence of hormones and antihormones

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The progesterone antagonist RU486 acquires agonist activity upon stimulation of cAMP signaling pathways

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Phosphorylation sites in ligand-induced and ligand-independent activation of the progesterone receptor

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Dopaminergic and Ligand-Independent Activation of Steroid Hormone Receptors

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Dexamethasone 21-mesylate: an affinity label of glucocorticoid receptors from rat hepatoma tissue culture cells

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Dissociation of Steroid Binding to Receptors and Steroid Induction of Biological Activity in a Glucocorticoid-Responsive Cell

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A negative tyrosine aminotransferase gene element that blocks glucocorticoid modulatory element-regulated modulation of glucocorticoid-induced gene expression

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Induction properties of a transiently transfected glucocorticoid-responsive gene vary with glucocorticoid receptor concentration

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Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. Stability and activity of the steroid binding domain are controlled by sequences in separate domains.

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The mechanism of RU486 antagonism is dependent on the conformation of the carboxy-terminal tail of the human progesterone receptor

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Steroid-induced conformational changes at ends of the hormone-binding domain in the rat glucocorticoid receptor are independent of agonist versus antagonist activity.

1 reference

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Mutations in the glucocorticoid receptor zinc finger region that distinguish interdigitated DNA binding and transcriptional enhancement activities

1 reference

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Intracellular receptors use a common mechanism to interpret signaling information at response elements

1 reference

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7 January 2021

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Three amino acid substitutions selectively disrupt the activation but not the repression function of the glucocorticoid receptor N terminus.

1 reference

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7 January 2021

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Specific mutations in the ligand binding domain selectively abolish the silencing function of human thyroid hormone receptor beta

1 reference

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7 January 2021

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Mutual transrepression of Fos and the glucocorticoid receptor: involvement of a functional domain in Fos which is absent in FosB

1 reference

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7 January 2021

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Transcriptional interference between c-Jun and the glucocorticoid receptor: mutual inhibition of DNA binding due to direct protein-protein interaction.

1 reference

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Novel glucocorticoid receptor complex with DNA element of the hormone-repressed POMC gene.

1 reference

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The rat glucocorticoid receptor mutant K461A differentiates between two different mechanisms of transrepression

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A new function for the C-terminal zinc finger of the glucocorticoid receptor. Repression of RelA transactivation

1 reference

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Hormone-dependent and -independent transcriptional activation by thyroid hormone receptors are mediated by different mechanisms

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Influence of a steroid receptor DNA-binding domain on transcriptional regulatory functions

1 reference

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Intracellular receptor concentration limits glucocorticoid-dependent enhancer activity

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Genetic complementation of a glucocorticoid receptor deficiency by expression of cloned receptor cDNA.

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Zinc finger mutations that alter domain interactions in the glucocorticoid receptor.

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Type II antagonists impair the DNA binding of steroid hormone receptors without affecting dimerization

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Serine 232 and methionine 272 define the ligand binding pocket in retinoic acid receptor subtypes

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Identifiers

10.1016/S0960-0760(99)00021-7

1 reference

Europe PubMed Central

25 September 2017

1 reference

Europe PubMed Central

25 September 2017

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