Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
about
A restraint molecular dynamics and simulated annealing approach for protein homology modeling utilizing mean anglesStructural evidence for ligand specificity in the binding domain of the human androgen receptor. Implications for pathogenic gene mutationsStructural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptorsIdentification of a novel mitochondrial protein ("mitoNEET") cross-linked specifically by a thiazolidinedione photoprobeExamination of Ligand-Dependent Coactivator Recruitment by Peroxisome Proliferator-Activated Receptor-alpha (PPARalpha).Virtual Screening as a Technique for PPAR Modulator Discovery.Peroxisome proliferator-activated receptors in the cardiovascular system.Ligand-protein interactions in nuclear receptors of hormones.A structural model of the constitutive androstane receptor defines novel interactions that mediate ligand-independent activityStructural basis for HNF-4alpha activation by ligand and coactivator binding.Noncanonical mechanisms to regulate nuclear receptor signaling.Ligand-binding regulation of LXR/RXR and LXR/PPAR heterodimerizations: SPR technology-based kinetic analysis correlated with molecular dynamics simulation.Different ligands-different receptor conformations: modeling of the hER alpha LBD in complex with agonists and antagonists.A microfluidic, high throughput protein crystal growth method for microgravity.The optimal corepressor function of nuclear receptor corepressor (NCoR) for peroxisome proliferator-activated receptor γ requires G protein pathway suppressor 2.Thyroid hormone receptor mutations in cancer and resistance to thyroid hormone: perspective and prognosisThe molecular mechanism of bisphenol A (BPA) as an endocrine disruptor by interacting with nuclear receptors: insights from molecular dynamics (MD) simulations.Ligand and receptor dynamics contribute to the mechanism of graded PPARγ agonism.The toxicology of ligands for peroxisome proliferator-activated receptors (PPAR).Small molecule modulation of nuclear receptor conformational dynamics: implications for function and drug discoveryPPARgamma: The Portrait of a Target Ally to Cancer Chemopreventive AgentsLysophospholipid interactions with protein targets.Three-dimensional modeling of and ligand docking to vitamin D receptor ligand binding domainSulindac derivatives that activate the peroxisome proliferator-activated receptor gamma but lack cyclooxygenase inhibition.PPAR Regulation of Inflammatory Signaling in CNS Diseases.The role of androgen receptor mutations in prostate cancer progression.Orphan nuclear receptors as targets for drug development.The orphan nuclear receptors at their 25-year reunion.A glucocorticoid/retinoic acid receptor chimera that displays cytoplasmic/nuclear translocation in response to retinoic acid. A real time sensing assay for nuclear receptor ligands.A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects.A two-stage differential hydrogen deuterium exchange method for the rapid characterization of protein/ligand interactions.Engineering and optimization of an allosteric biosensor protein for peroxisome proliferator-activated receptor γ ligands.PPARs in the central nervous system: roles in neurodegeneration and neuroinflammation.A novel role for helix 12 of retinoid X receptor in regulating repression.Analysis of PPAR-α/γ Activity by Combining 2-D QSAR and Molecular Simulation.Spectroscopic analyses of the binding kinetics of 15d-PGJ2 to the PPARgamma ligand-binding domain by multi-wavelength global fitting.Alpha,beta-unsaturated ketone is a core moiety of natural ligands for covalent binding to peroxisome proliferator-activated receptor gamma.Identification of residues in the PXR ligand binding domain critical for species specific and constitutive activation.Nuclear receptor corepressor-dependent repression of peroxisome-proliferator-activated receptor delta-mediated transactivation.The tamoxifen-responsive estrogen receptor alpha mutant D351Y shows reduced tamoxifen-dependent interaction with corepressor complexes.
P2860
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P2860
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@ast
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@en
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@nl
type
label
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@ast
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@en
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@nl
prefLabel
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@ast
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@en
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@nl
P2093
P2860
P3181
P356
P1476
Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma
@en
P2093
A Berkenstam
C Svensson
G Bertilsson
J Uppenberg
L Jendeberg
P2860
P304
P3181
P356
10.1074/JBC.273.47.31108
P407
P577
1998-11-20T00:00:00Z