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 RAR alpha 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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Conformational adaptation of agonists to the human nuclear receptor RAR gamma

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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 12 and 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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7 January 2021

Differential ligand activation of estrogen receptors ERalpha and ERbeta 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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RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2

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Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300

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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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7 January 2021

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

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7 January 2021

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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7 January 2021

10.1016/S0955-0674(98)80015-X

Identifiers

DOI

1 reference

6 February 2018

PubMed ID

9640540

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6 February 2018