Metabolism of the vitamin D3 analogue EB1089 alters receptor complex formation and reduces promoter selectivity (Q35040749)

6 August 2017

title

Metabolism of the vitamin D3 analogue EB1089 alters receptor complex formation and reduces promoter selectivity (English)

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6 August 2017

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Quack M

1

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6 August 2017

Mørk Hansen C

2

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6 August 2017

Binderup E

3

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6 August 2017

Kissmeyer AM

4

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6 August 2017

Carlberg C

5

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6 August 2017

language of work or name

English

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publication date

1 October 1998

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British Journal of Pharmacology

6 August 2017

published in

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6 August 2017

volume

125

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6 August 2017

issue

4

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6 August 2017

page(s)

607-614

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Functional conformations of the nuclear 1α,25-dihydroxyvitamin D3 receptor

6 August 2017

cites work

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Natural vitamin D3 response elements formed by inverted palindromes: polarity-directed ligand sensitivity of vitamin D3 receptor-retinoid X receptor heterodimer-mediated transactivation.

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

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Mechanisms of nuclear signalling by vitamin D3. Interplay with retinoid and thyroid hormone signalling

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Two nuclear signalling pathways for vitamin D

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EB1089: a new vitamin D analogue that inhibits the growth of breast cancer cells in vivo and in vitro

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Sensitive induction of apoptosis in breast cancer cells by a novel 1,25-dihydroxyvitamin D3 analogue shows relation to promoter selectivity

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7 January 2021

Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription

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7 January 2021

Functional characterization of a 1,25-dihydroxyvitamin D3 receptor binding site found in the rat atrial natriuretic factor promoter

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7 January 2021

Metabolism of the vitamin D analog EB 1089: identification of in vivo and in vitro liver metabolites and their biological activities

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Pharmacokinetic studies of vitamin D analogues: relationship to vitamin D binding protein (DBP)

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The nuclear receptor superfamily: the second decade

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Evidence for Ligand-Dependent Intramolecular Folding of the AF-2 Domain in Vitamin D Receptor-Activated Transcription and Coactivator Interaction

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7 January 2021

EB 1089, a novel vitamin D analogue, has strong antiproliferative and differentiation inducing effects on cancer cells

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7 January 2021

EB 1089, a novel vitamin D Analog with strong antiproliferative and differentiation-inducing effects on target cells

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7 January 2021

The high affinity ligand binding conformation of the nuclear 1,25-dihydroxyvitamin D3 receptor is functionally linked to the transactivation domain 2 (AF-2)

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7 January 2021

High-affinity nuclear receptor binding of 20-epi analogues of 1,25-dihydroxyvitamin D3 correlates well with gene activation

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Vitamin D3 receptors: structure and function in transcription

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Vitamin D analogues: from molecule to clinical application

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An Improved CAT Assay for Promoter Analysis in Either Transgenic Mice or Tissue Culture Cells

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7 January 2021

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

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7 January 2021

Functional characterization of a novel type of 1 alpha,25-dihydroxyvitamin D3 response element identified in the mouse c-fos promoter

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7 January 2021

Metabolism of the vitamin D analog EB1089 by cultured human cells: redirection of hydroxylation site to distal carbons of the side-chain

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7 January 2021

Conformational change and enhanced stabilization of the vitamin D receptor by the 1,25-dihydroxyvitamin D3 analog KH1060.

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7 January 2021

The mechanisms of vitamin D toxicity

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7 January 2021

Identifiers

DOI

10.1038/SJ.BJP.0702086

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6 August 2017

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6 August 2017

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