Distinct modes of interaction of the retinoic acid receptor alpha with natural and synthetic retinoids (Q47683955)

4 February 2018

title

Distinct modes of interaction of the retinoic acid receptor alpha with natural and synthetic retinoids (English)

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4 February 2018

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B Lefebvre

1

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4 February 2018

A Mouchon

series ordinal

2

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4 February 2018

P Formstecher

series ordinal

3

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4 February 2018

P Lefebvre

series ordinal

4

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4 February 2018

publication date

1 April 1998

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4 February 2018

Molecular and Cellular Endocrinology

published in

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4 February 2018

volume

139

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4 February 2018

issue

1-2

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4 February 2018

page(s)

161-169

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4 February 2018

A retinoic acid receptor alpha antagonist selectively counteracts retinoic acid effects

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In vitro binding of retinoids to the nuclear retinoic acid receptor alpha

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Two distinct actions of retinoid-receptor ligands

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Purification and functional characterization of the ligand-binding domain from the retinoic acid receptor alpha: evidence that sulfhydryl groups are involved in ligand-receptor interactions

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Identification of a receptor for the morphogen retinoic acid

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Nuclear receptor coactivators

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Different agonist- and antagonist-induced conformational changes in retinoic acid receptors analyzed by protease mapping

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The tetramerization region of the retinoid X receptor is important for transcriptional activation by the receptor.

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Regulation of retinoid signalling by receptor polarity and allosteric control of ligand binding

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Polarity-specific activities of retinoic acid receptors determined by a co-repressor.

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Analysis of the ligand-binding domain of human retinoic acid receptor alpha by site-directed mutagenesis

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Structural determinants of the ligand-binding site of the human retinoic acid receptor alpha.

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Protein phosphatases 1 and 2A regulate the transcriptional and DNA binding activities of retinoic acid receptors

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The N-terminal portion of domain E of retinoic acid receptors alpha and beta is essential for the recognition of retinoic acid and various analogs

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A novel pathway for vitamin A signaling mediated by RXR heterodimerization with NGFI-B and NURR1

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Identification of amino acids critical for the DNA binding and dimerization properties of the human retinoic acid receptor alpha. Importance of lysine 360, lysine 365, and valine 361

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Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid

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A canonical structure for the ligand-binding domain of nuclear receptors

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10.1016/S0303-7207(98)00065-3

Identifiers

DOI

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4 February 2018

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4 February 2018