The androgen receptor ligand-binding domain stabilizes DNA binding in living cells.
about
Identification of biomolecule mass transport and binding rate parameters in living cells by inverse modelingLigand-specific dynamics of the androgen receptor at its response element in living cellsCompartmentalization of androgen receptor protein-protein interactions in living cellsThe spatiotemporal pattern of Src activation at lipid rafts revealed by diffusion-corrected FRET imagingMolecular characterization of the murine homologue of the DC-derived protein DC-SCRIPTMitotic binding of Esrrb marks key regulatory regions of the pluripotency network.Androgens and the male reproductive tract: an overview of classical roles and current perspectives.Activation of the DNA-dependent protein kinase stimulates nuclear export of the androgen receptor in vitro.The leukemia-associated fusion protein MN1-TEL blocks TEL-specific recognition sequences.DNA damage stabilizes interaction of CSB with the transcription elongation machinery.Heterodimerization with different Jun proteins controls c-Fos intranuclear dynamics and distributionCross-validating FRAP and FCS to quantify the impact of photobleaching on in vivo binding estimates.Biliverdin reductase is a transporter of haem into the nucleus and is essential for regulation of HO-1 gene expression by haematin.Ligand binding shifts highly mobile retinoid X receptor to the chromatin-bound state in a coactivator-dependent manner, as revealed by single-cell imaging.Quantitation of glucocorticoid receptor DNA-binding dynamics by single-molecule microscopy and FRAPVisualizing the action of steroid hormone receptors in living cells.A finite element model for protein transport in vivo.Self-organization versus Watchmaker: stochastic dynamics of cellular organization.Evidence for DNA-binding domain--ligand-binding domain communications in the androgen receptor.Analysis of Protein Kinetics Using Fluorescence Recovery After Photobleaching (FRAP).Assembly of multiprotein complexes that control genome function.Imaging transcription in living cells.Trinucleotide repeats and protein folding and disease: the perspective from studies with the androgen receptor.Quantifying transcription factor kinetics: at work or at play?Single-cell imaging of mechanotransduction in endothelial cells.A multi-parameter imaging assay identifies different stages of ligand-induced androgen receptor activation.Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage.The relationship between intranuclear mobility of the NF-kappaB subunit p65 and its DNA binding affinity.Dissecting the contribution of diffusion and interactions to the mobility of nuclear proteins.Nuclear proteins: finding and binding target sites in chromatin.Androgen receptor association with mitotic chromatin - analysis with introduced deletions and disease-inflicting mutations.Association with Coregulators Is the Major Determinant Governing Peroxisome Proliferator-activated Receptor Mobility in Living Cells
P2860
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P2860
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells.
@en
type
label
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells.
@en
prefLabel
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells.
@en
P2093
P1476
The androgen receptor ligand-binding domain stabilizes DNA binding in living cells
@en
P2093
Adriaan B Houtsmuller
Alex L Nigg
Bart Geverts
Hendrikus J Dubbink
Jan Trapman
Pascal Farla
Remko Hersmus
P356
10.1016/J.JSB.2004.01.002
P50
P577
2004-07-01T00:00:00Z