Hypericum sampsonii induces apoptosis and nuclear export of retinoid X receptor-alpha [PDF]
Carcinogenesis, 2006 Natural products derived from plants provide a rich source for development of new anticancer drugs. Recent studies suggest that modulation of subcellular localization of retinoid X receptor-alpha (RXRalpha) represents a potential approach for inducing cancer cell apoptosis.
Jiao Zeng
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Whole Transcriptome Analysis of Renal Intercalated Cells Predicts Lipopolysaccharide Mediated Inhibition of Retinoid X Receptor alpha Function. [PDF]
Sci Rep, 2019 Saxena V +17 more
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Effect of retinoic acid treatment on the retinoic acid signaling pathway in a human siRNA-based aniridia limbal epithelial cell model, in vitro. [PDF]
PLoS ONEPurposeIn the present study, we evaluate gene and protein expression levels in an in vitro siRNA-mediated PAX6 knockdown limbal epithelial cell (LEC) model after RA treatment.
Shao-Lun Hsu +10 more
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Vitamin D Receptor and Retinoid X Receptor Alpha in Melanocytic Benign Lesions and Melanoma
The American Journal of Dermatopathology, 2023 Abstract: Vitamin D receptor (VDR) exerts its biological effects when it heterodimerizes to a nuclear receptor of the retinoid family called retinoid X receptor α (RXRα), stimulating or inhibiting DNA transcription. VDR stimulation by vitamin D analogs led to in vitro antiproliferative effects, and experimental RXRα knockout led to loss of ...
Juliana Polizel Ocanha‐Xavier +3 more
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Retinoid X receptor alpha forms tetramers in solution. [PDF]
Proceedings of the National Academy of Sciences, 1995 Protein-protein interactions allow the retinoid X receptor (RXR) to bind to cognate DNA as a homo- or a heterodimer and to participate in mediating the effects of a variety of hormones on gene transcription. Here we report a systematic study of the oligomeric state of RXR in the absence of a DNA template.
Sander Kersten +4 more
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Ligand-induced alteration of the protease sensitivity of retinoid X receptor alpha.
Journal of Biological Chemistry, 1994 Ligand-induced structural alterations of retinoid X receptor (RXR) appear to facilitate receptor homodimerization, to enhance DNA binding of RXR homodimeric complexes, and to dictate the transcriptional activation properties of RXR complexes bound to response elements located in the promoter region of 9-cis-retinoic acid responsive genes. The technique
Mark Leid
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Distinct functional modes of SUMOylation for retinoid X receptor alpha [PDF]
Biochemical and Biophysical Research Communications, 2015 The present study investigated human retinoid X receptor alpha (hRXRα) as a substrate for modification with small ubiquitin like modifier (SUMO) and how members of the protein inhibitor of activated STAT (PIAS) family may impact upon this process. In agreement with a previous study, we validate Ubc9 to facilitate SUMOylation of hRXRα at lysine 108 but ...
Wai-Ping Lee +6 more
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DNA binding specificity and function of retinoid X receptor alpha.
Journal of Biological Chemistry, 1994 Retinoid X receptors are members of the erbA superfamily of ligand-inducible transcription factors. Similar to several other members of this gene family, retinoid X receptors are known to bind to the hexameric DNA sequence AGGTCA. After binding to a direct repeat of this hexamer with a one-base pair spacer, retinoid X receptor homodimers are able to ...
José S. Subauste +2 more
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Effects of allicin on human Simpson-Golabi-Behmel syndrome cells in mediating browning phenotype
Frontiers in Endocrinology, 2023 IntroductionObesity is a major health problem because it is associated with increased risk of cardiovascular disease, diabetes, hypertension, and some cancers.
Uzair Ali +3 more
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A Structure-based Approach to Retinoid X Receptor-α Inhibition [PDF]
Journal of Biological Chemistry, 2006 In this paper we describe a structure-based approach designed to identify novel ligands for retinoid X receptor-alpha (RXRalpha). By using a virtual approach based on a modified scoring function, we have selected 200 potential candidates on the basis of their predicted ability of docking into the ligand-binding site of the target.
Stebbins JL +4 more
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