The nuclear receptor ligand-binding domain: structure and function (Q47926627)

6 February 2018

review article

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title

The nuclear receptor ligand-binding domain: structure and function (English)

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6 February 2018

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2

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6 February 2018

author name string

Moras D

series ordinal

1

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6 February 2018

publication date

1 June 1998

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6 February 2018

Current Opinion in Cell Biology

published in

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6 February 2018

volume

10

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6 February 2018

issue

3

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6 February 2018

page(s)

384-391

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6 February 2018

Ligand binding was acquired during evolution of nuclear receptors

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Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase

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Stimulation of RARα Activation Function AF-1 through Binding to the General Transcription Factor TFIIH and Phosphorylation by CDK7

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Nuclear receptor coactivators

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Transcriptional control. Sinful repression

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What's up and down with histone deacetylation and transcription?

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Steroid hormone receptors: many actors in search of a plot

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Nonsteroid nuclear receptors: what are genetic studies telling us about their role in real life?

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The RXR heterodimers and orphan receptors

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An Orphan Nuclear Receptor Activated by Pregnanes Defines a Novel Steroid Signaling Pathway

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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha

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

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A structural role for hormone in the thyroid hormone receptor.

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Molecular basis of agonism and antagonism in the oestrogen receptor

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

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A mutation mimicking ligand-induced conformational change yields a constitutive RXR that senses allosteric effects in heterodimers

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The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways

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Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor

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Nuclear Receptor-Binding Sites of Coactivators Glucocorticoid Receptor Interacting Protein 1 (GRIP1) and Steroid Receptor Coactivator 1 (SRC-1): Multiple Motifs with Different Binding Specificities

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A signature motif in transcriptional co-activators mediates binding to nuclear receptors

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Determinants of chromatin disruption and transcriptional regulation instigated by the thyroid hormone receptor: hormone-regulated chromatin disruption is not sufficient for transcriptional activation

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Acetylation of general transcription factors by histone acetyltransferases

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Ligand-independent repression by the thyroid hormone receptor mediated by a nuclear receptor co-repressor

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A transcriptional co-repressor that interacts with nuclear hormone receptors

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Ligand-independent activation of the oestrogen receptor by mutation of a conserved tyrosine

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Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein.

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Ligand- and DNA-induced dissociation of RXR tetramers 1 1Edited by M. Yaniv

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Sequences in the ligand-binding domains of the human androgen and progesterone receptors which determine their distinct ligand identities

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Cloning and characterization of a specific coactivator, ARA70, for the androgen receptor in human prostate cells

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AF-2 activity and recruitment of steroid receptor coactivator 1 to the estrogen receptor depend on a lysine residue conserved in nuclear receptors

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Different positioning of the ligand-binding domain helix 12and the F domain of the estrogen receptor accounts for functional differences between agonists and antagonists

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

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Activation of the ovalbumin gene by the estrogen receptor involves the fos-jun complex

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Differential Ligand Activation of Estrogen Receptors ERα and ERβ at AP1 Sites

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Inhibition of adipogenesis through MAP kinase-mediated phosphorylation of PPARgamma

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Sequence and characterization of a coactivator for the steroid hormone receptor superfamily

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AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer

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TRAM-1, A Novel 160-kDa Thyroid Hormone Receptor Activator Molecule, Exhibits Distinct Properties from Steroid Receptor Coactivator-1

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The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis

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Allosteric effects of DNA on transcriptional regulators

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Identifiers

DOI

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6 February 2018

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6 February 2018