Structural mechanism for signal transduction in RXR nuclear receptor heterodimers. - Wikidata - awgldk - TriplyDB

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

http://www.wikidata.org/entity/Q35990304

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Futures Challenges in Thyroid Hormone Signaling Research Peroxisome proliferator activated receptors at the crossroad of obesity, diabetes, and pancreatic cancer Insulin-Sensitizers, Polycystic Ovary Syndrome and Gynaecological Cancer Risk Novel Allosteric Pathway of Eg5 Regulation Identified through Multivariate Statistical Analysis of Hydrogen-Exchange Mass Spectrometry (HX-MS) Ligand Screening Data.Sequences flanking the core-binding site modulate glucocorticoid receptor structure and activity.Ligand Dependent Switch from RXR Homo- to RXR-NURR1 Heterodimerization.Retinoid X Receptors Intersect the Molecular Clockwork in the Regulation of Liver Metabolism.A network of allosterically coupled residues in the bacteriophage T4 Mre11-Rad50 complex Stage- and subunit-specific functions of polycomb repressive complex 2 in bladder urothelial formation and regeneration.Allosteric pathways in nuclear receptors - Potential targets for drug design.Synergistic Regulation of Coregulator/Nuclear Receptor Interaction by Ligand and DNA.Editor's Highlight: Structure-Based Investigation on the Binding and Activation of Typical Pesticides With Thyroid Receptor.PPARγ helix 12 exhibits an antagonist conformation.Solution Nuclear Magnetic Resonance Studies of the Ligand-Binding Domain of an Orphan Nuclear Receptor Reveal a Dynamic Helix in the Ligand-Binding Pocket.Defining a conformational ensemble that directs activation of PPARγ.Structural insights into the heterodimeric complex of the nuclear receptors FXR and RXR Chemical Crosslinking Mass Spectrometry Reveals the Conformational Landscape of the Activation Helix of PPARγ; a Model for Ligand-Dependent Antagonism In vivo genome-wide binding interactions of mouse and human constitutive androstane receptors reveal novel gene targets Overview of the structure-based non-genomic effects of the nuclear receptor RXRα

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Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

http://www.wikidata.org/entity/Q35990304

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年论文

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name

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

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Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

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Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

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Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

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prefLabel

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

@ast

Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.

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Nature Communications

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Structural mechanism for signal transduction in RXR nuclear receptor heterodimers

@en

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Andrew I Shulman

http://www.w3.org/2001/XMLSchema#string

David P Marciano

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Douglas J Kojetin

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Edna Matta-Camacho

http://www.w3.org/2001/XMLSchema#string

Jason Nowak

http://www.w3.org/2001/XMLSchema#string

John B Bruning

http://www.w3.org/2001/XMLSchema#string

Kendall W Nettles

http://www.w3.org/2001/XMLSchema#string

Mark Rance

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Michael J Chalmers

http://www.w3.org/2001/XMLSchema#string

Patrick R Griffin

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P2860

Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA

Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors

Structural basis for autorepression of retinoid X receptor by tetramer formation and the AF-2 helix

Structural basis for antagonist-mediated recruitment of nuclear co-repressors by PPARalpha

Structural characterization of a subtype-selective ligand reveals a novel mode of estrogen receptor antagonism

Molecular recognition of agonist ligands by RXRs

Crystal structure of the heterodimeric complex of LXR and RXR ligand-binding domains in a fully agonistic conformation

Partial agonists activate PPARgamma using a helix 12 independent mechanism

NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

DNA Binding Site Sequence Directs Glucocorticoid Receptor Structure and Activity

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8013

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scholarly article

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10.1038/NCOMMS9013

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6

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Jerome C Nwachukwu

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2015-08-20T00:00:00Z

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281171923

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26289479

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4547401

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