DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex. - Test2 - elhamkhani - TriplyDB

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

http://www.wikidata.org/entity/Q34927801

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Minireview: Conversing with chromatin: the language of nuclear receptors Structural considerations of vitamin D signaling Structural basis for a molecular allosteric control mechanism of cofactor binding to nuclear receptors Defining the Communication between Agonist and Coactivator Binding in the Retinoid X Receptor Ligand Binding Domain Structure of the full human RXR/VDR nuclear receptor heterodimer complex with its DR3 target DNA p62/SQSTM1 by Binding to Vitamin D Receptor Inhibits Hepatic Stellate Cell Activity, Fibrosis, and Liver Cancer A naturally occurring insertion of a single amino acid rewires transcriptional regulation by glucocorticoid receptor isoforms.Intrinsic disorder in the androgen receptor: identification, characterisation and drugability.Agonist and antagonist switch DNA motifs recognized by human androgen receptor in prostate cancer.Determinants of bacteriophage 933W repressor DNA binding specificity.Cutting edge: Evidence for a dynamically driven T cell signaling mechanism.Agonist and antagonist binding to the nuclear vitamin D receptor: dynamics, mutation effects and functional implications.Vitamin D: Metabolism, Molecular Mechanism of Action, and Pleiotropic Effects.Tumor suppressor microRNAs, miR-100 and -125b, are regulated by 1,25-dihydroxyvitamin D in primary prostate cells and in patient tissue.Differential hydrogen/deuterium exchange mass spectrometry analysis of protein-ligand interactions Influence of domain interactions on conformational mobility of the progesterone receptor detected by hydrogen/deuterium exchange mass spectrometry.Disorder-to-order transition underlies the structural basis for the assembly of a transcriptionally active PGC-1α/ERRγ complex.Phosphorylation of PPARγ Affects the Collective Motions of the PPARγ-RXRα-DNA Complex.ChIP-exo signal associated with DNA-binding motifs provides insight into the genomic binding of the glucocorticoid receptor and cooperating transcription factors.Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.Evidence for DNA-binding domain--ligand-binding domain communications in the androgen receptor.Small molecule modulation of nuclear receptor conformational dynamics: implications for function and drug discovery Vitamin D receptor gene BsmI, FokI, ApaI and TaqI polymorphisms and the risk of systemic lupus erythematosus.Allosteric Pathways in the PPARγ-RXRα nuclear receptor complex.Polymorphic variants in the vitamin D pathway genes and the risk of ovarian cancer among non-carriers of BRCA1/BRCA2 mutations Vitamin D receptor gene BsmI and FokI polymorphisms in relation to ovarian cancer risk in the Polish population Role of CAR and PXR in xenobiotic sensing and metabolism.H/D exchange centroid monitoring is insufficient to show differences in the behavior of protein states.Allosteric modulators of steroid hormone receptors: structural dynamics and gene regulation.Synergistic effect of retinoic acid and vitamin D analog EB1089-induced apoptosis of hepatocellular cancer cells.Cooperative activation of gene expression by agonists and antagonists mediated by estrogen receptor heteroligand dimer complexes.General molecular biology and architecture of nuclear receptors.The sum of many small changes: microRNAs are specifically and potentially globally altered by vitamin D3 metabolites.The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals.Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein.Automated hydrogen/deuterium exchange electron transfer dissociation high resolution mass spectrometry measured at single-amide resolution.Regulation of the structurally dynamic N-terminal domain of progesterone receptor by protein-induced folding.Mass spectrometric analysis of protein-ligand interactions.Understanding nuclear receptor form and function using structural biology Minireview: dynamic structures of nuclear hormone receptors: new promises and challenges.

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P2860

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

http://www.wikidata.org/entity/Q34927801

description

2011 nî lūn-bûn

@nan

2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի ապրիլին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

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2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

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name

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@ast

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@en

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@nl

type

label

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@ast

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@en

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@nl

prefLabel

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@ast

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@en

DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@nl

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Nature Structural & Molecular Biology

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DNA binding alters coactivator interaction surfaces of the intact VDR-RXR complex.

@en

P2093

Bruce D Pascal

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

Douglas J Kojetin

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

Jeffrey A Dodge

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

John B Bruning

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

Jun Zhang

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

Keith R Stayrook

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

Lorri L Burris

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

Michael J Chalmers

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

Monica A Istrate

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

Patrick R Griffin

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

P2860

The crystal structure of the nuclear receptor for vitamin D bound to its natural ligand

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

Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation

Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid

Common angiotensin receptor blockers may directly modulate the immune system via VDR, PPAR and CCR2b

Crystal structure of a heterodimeric complex of RAR and RXR ligand-binding domains

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

Partial agonists activate PPARgamma using a helix 12 independent mechanism

Prediction of the tissue-specificity of selective estrogen receptor modulators by using a single biochemical method

DNA Binding Site Sequence Directs Glucocorticoid Receptor Structure and Activity

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556-563

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scholarly article

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10.1038/NSMB.2046

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5

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18

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2011-04-10T00:00:00Z

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51037814

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21478866

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3087838

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