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Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α
The crystal structure of the human retinoid-X receptor RXR-α ligand-binding domain reveals a previously undiscovered fold of an antiparallel α-helical sandwich, packed as dimeric units. Two helicesExpand
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A canonical structure for the ligand-binding domain of nuclear receptors
The ability of nuclear receptors (NRs) to activate transcription of target genes requires the binding of cognate ligands to their ligand-binding domains (LBDs). Information provided by theExpand
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Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers
The yeast Kes1p/Osh4p protein functions as a sterol/PI(4)P exchanger between lipid membranes, which suggests the possibility of creating a sterol gradient via phosphoinositide metabolism.
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Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications.
Nuclear receptors are members of a large family of ligand-inducible transcription factors that regulate gene programs underlying a plethora of (patho)physiological phenomena. The recent determinationExpand
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Structural and mechanistic insights into bisphenols action provide guidelines for risk assessment and discovery of bisphenol A substitutes
Bisphenol A (BPA) is an industrial compound and a well known endocrine-disrupting chemical with estrogenic activity. The widespread exposure of individuals to BPA is suspected to affect a variety ofExpand
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Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains.
The crystal structure of a heterodimer between the ligand-binding domains (LBDs) of the human RARalpha bound to a selective antagonist and the constitutively active mouse RXRalphaF318A mutant showsExpand
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Activation of RXR–PPAR heterodimers by organotin environmental endocrine disruptors
The nuclear receptor retinoid X receptor‐α (RXR‐α)–peroxisome proliferator‐activated receptor‐γ (PPAR‐γ) heterodimer was recently reported to have a crucial function in mediating the deleteriousExpand
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Phosphatidylserine transport by ORP/Osh proteins is driven by phosphatidylinositol 4-phosphate
Membrane contact sites promote lipid exchange Most membrane lipids are manufactured in the endoplasmic reticulum (ER). Different organelles and the plasma membrane (PM) have distinct phospholipidExpand
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Peroxisome Proliferator-Activated Receptor γ Is a Target for Halogenated Analogs of Bisphenol A
Background: The occurrence of halogenated analogs of the xenoestrogen bisphenol A (BPA) has been recently demonstrated both in environmental and human samples. These analogs include brominated [e.g.,Expand
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