Structural basis for bile acid binding and activation of the nuclear receptor FXR
about
Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptorEstrogen and Estrogen Receptor-α-Mediated Transrepression of Bile Salt Export PumpPotent stimulation of fibroblast growth factor 19 expression in the human ileum by bile acidsStructure of the heterodimeric ecdysone receptor DNA-binding complexBile salts of vertebrates: structural variation and possible evolutionary significanceDiscovery that theonellasterol a marine sponge sterol is a highly selective FXR antagonist that protects against liver injury in cholestasisX-ray crystal structure of the liver X receptor beta ligand binding domain: regulation by a histidine-tryptophan switchIdentification of a potent synthetic FXR agonist with an unexpected mode of binding and activationStructural Conservation of Ligand Binding Reveals a Bile Acid-like Signaling Pathway in NematodesCrystal structures of complexes of vitamin D receptor ligand-binding domain with lithocholic acid derivativesThe antiparasitic drug ivermectin is a novel FXR ligand that regulates metabolismStructure of human N-acylphosphatidylethanolamine-hydrolyzing phospholipase D: regulation of fatty acid ethanolamide biosynthesis by bile acidsRetinoic acid actions through mammalian nuclear receptors.Structural overview of the nuclear receptor superfamily: insights into physiology and therapeutics.The evolution of farnesoid X, vitamin D, and pregnane X receptors: insights from the green-spotted pufferfish (Tetraodon nigriviridis) and other non-mammalian species.Two farnesoid X receptor alpha isoforms in Japanese medaka (Oryzias latipes) are differentially activated in vitro.Oxysterol 22(R)-hydroxycholesterol induces the expression of the bile salt export pump through nuclear receptor farsenoid X receptor but not liver X receptor.The hypolipidemic agent guggulsterone regulates the expression of human bile salt export pump: dominance of transactivation over farsenoid X receptor-mediated antagonismConformational dynamics of human FXR-LBD ligand interactions studied by hydrogen/deuterium exchange mass spectrometry: insights into the antagonism of the hypolipidemic agent Z-guggulsterone.Inhibiting the initiation of Clostridium difficile spore germination using analogs of chenodeoxycholic acid, a bile acid.Structural and functional insights into nuclear receptor signaling.The X-ray structure of a hemipteran ecdysone receptor ligand-binding domain: comparison with a lepidopteran ecdysone receptor ligand-binding domain and implications for insecticide design.Evolution of promiscuous nuclear hormone receptors: LXR, FXR, VDR, PXR, and CARDeciphering the nuclear bile acid receptor FXR paradigm.Regulation of FXR transcriptional activity in health and disease: Emerging roles of FXR cofactors and post-translational modificationsDevelopment of time resolved fluorescence resonance energy transfer-based assay for FXR antagonist discoveryInappropriate ileal conservation of bile acids in cholestatic liver disease: homeostasis gone awryRegulation of drug and bile salt transporters in liver and intestine.Pharmacophore-based discovery of FXR-agonists. Part II: identification of bioactive triterpenes from Ganoderma lucidumAnalysis of HSD3B7 knockout mice reveals that a 3alpha-hydroxyl stereochemistry is required for bile acid functionStructural Basis for Small Molecule NDB (N-Benzyl-N-(3-(tert-butyl)-4-hydroxyphenyl)-2,6-dichloro-4-(dimethylamino) Benzamide) as a Selective Antagonist of Farnesoid X Receptor α (FXRα) in Stabilizing the Homodimerization of the Receptor.The enterohepatic nuclear receptors are major regulators of the enterohepatic circulation of bile salts.Bile acid receptors as targets for the treatment of dyslipidemia and cardiovascular disease.Evolution of the bile salt nuclear receptor FXR in vertebratesQuantitative high-throughput profiling of environmental chemicals and drugs that modulate farnesoid X receptorTarget flexibility: an emerging consideration in drug discovery and design.Understanding nuclear receptor form and function using structural biologyThe membrane protein ATPase class I type 8B member 1 signals through protein kinase C zeta to activate the farnesoid X receptor.Orphan nuclear receptors as targets for drug development.Targeting Bile Acid Receptors: Discovery of a Potent and Selective Farnesoid X Receptor Agonist as a New Lead in the Pharmacological Approach to Liver Diseases.
P2860
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P2860
Structural basis for bile acid binding and activation of the nuclear receptor FXR
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@ast
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@en
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@nl
type
label
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@ast
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@en
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@nl
prefLabel
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@ast
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@en
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@nl
P2093
P1433
P1476
Structural basis for bile acid binding and activation of the nuclear receptor FXR
@en
P2093
Fraydoon Rastinejad
Joel M Harp
Roberto Pellicciari
Sepideh Khorasanizadeh
Srikripa Devarakonda
Timothy M Willson
P304
P356
10.1016/S1097-2765(03)00112-6
P50
P577
2003-04-01T00:00:00Z