Active nuclear receptors exhibit highly correlated AF-2 domain motions
about
The retinoid X receptors and their ligandsBiology of PXR: role in drug-hormone interactionsMarine invertebrate xenobiotic-activated nuclear receptors: their application as sensor elements in high-throughput bioassays for marine bioactive compoundsCrystal Structure of the HEAT Domain from the Pre-mRNA Processing Factor SymplekinThe crystal structure of a self-activating G protein alpha subunit reveals its distinct mechanism of signal initiation.Crystal Structure of the Plant Epigenetic Protein Arginine Methyltransferase 10Challenges predicting ligand-receptor interactions of promiscuous proteins: the nuclear receptor PXRAllosteric transitions of supramolecular systems explored by network models: application to chaperonin GroEL.Activation of xenobiotic receptors: driving into the nucleus.Understanding nuclear receptors using computational methods.Engineered allosteric activation of kinases in living cells.Conformational control of the binding of the transactivation domain of the MLL protein and c-Myb to the KIX domain of CREBChIPing the cistrome of PXR in mouse liverFunctional reconstitution of an atypical G protein heterotrimer and regulator of G protein signaling protein (RGS1) from Arabidopsis thaliana.Rifampicin-independent interactions between the pregnane X receptor ligand binding domain and peptide fragments of coactivator and corepressor proteins.Serine 350 of human pregnane X receptor is crucial for its heterodimerization with retinoid X receptor alpha and transactivation of target genes in vitro and in vivoNovel yeast-based strategy unveils antagonist binding regions on the nuclear xenobiotic receptor PXRThe major human pregnane X receptor (PXR) splice variant, PXR.2, exhibits significantly diminished ligand-activated transcriptional regulation.The structural basis of pregnane X receptor binding promiscuity.Orphan nuclear receptors as targets for drug development.Nuclear receptors PXR and CAR: implications for drug metabolism regulation, pharmacogenomics and beyond.Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTRActivation helix orientation of the estrogen receptor is mediated by receptor dimerization: evidence from molecular dynamics simulations.Transcriptional protein-protein cooperativity in POU/HMG/DNA complexes revealed by normal mode analysis.Using TR-FRET to Investigate Protein-Protein Interactions: A Case Study of PXR-Coregulator Interaction.
P2860
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P2860
Active nuclear receptors exhibit highly correlated AF-2 domain motions
description
2008 nî lūn-bûn
@nan
2008 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@ast
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@en
type
label
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@ast
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@en
prefLabel
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@ast
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@en
P2093
P2860
P50
P1476
Active nuclear receptors exhibit highly correlated AF-2 domain motions
@en
P2093
Brenda R S Temple
Denise G Teotico
Monica L Frazier
P2860
P304
P356
10.1371/JOURNAL.PCBI.1000111
P577
2008-07-11T00:00:00Z