The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
about
Counterregulation of chromatin deacetylation and histone deacetylase occupancy at the integrated promoter of human immunodeficiency virus type 1 (HIV-1) by the HIV-1 repressor YY1 and HIV-1 activator TatIncreased nuclear factor 1 binding to its nucleosomal site mediated by sequence-dependent DNA structureTargeted histone acetylation at the yeast CUP1 promoter requires the transcriptional activator, the TATA boxes, and the putative histone acetylase encoded by SPT10.The chromatin structure of the long control region of human papillomavirus type 16 represses viral oncoprotein expression.High-mobility-group protein I can modulate binding of transcription factors to the U5 region of the human immunodeficiency virus type 1 proviral promoterHistone acetylation facilitates RNA polymerase II transcription of the Drosophila hsp26 gene in chromatin.Epstein-Barr nuclear antigen 1 binds and destabilizes nucleosomes at the viral origin of latent DNA replication.DNA repair of a single UV photoproduct in a designed nucleosome.Structural and functional cross-talk between a distant enhancer and the epsilon-globin gene promoter shows interdependence of the two elements in chromatin.GAL4 directs nucleosome sliding induced by NURF.Induction of the gene encoding macrophage chemoattractant protein 1 by Orientia tsutsugamushi in human endothelial cells involves activation of transcription factor activator protein 1.Coordination of cell signaling, chromatin remodeling, histone modifications, and regulator recruitment in human matrix metalloproteinase 9 gene transcription.Two-step binding of transcription factors causes sequential chromatin structural changes at the activated IL-2 promoter.Signal transduction pathways linking the activation of alveolar macrophages with the recruitment of neutrophils to lungs in chronic obstructive pulmonary disease.Structure and function of active chromatin and DNase I hypersensitive sites.Addition of positively charged tripeptide to N-terminus of the Fos basic region leucine zipper domain: implications on DNA bending, affinity, and specificity.Interactions of the CCAAT-binding trimer NF-Y with nucleosomes.Chromatin opening and transactivator potentiation by RAP1 in Saccharomyces cerevisiae.Disruption of Epstein-Barr virus latency in the absence of phosphorylation of ZEBRA by protein kinase C.Hyperactivated NF-{kappa}B and AP-1 transcription factors promote highly accessible chromatin and constitutive transcription across the interleukin-6 gene promoter in metastatic breast cancer cellsNature of the accessible chromatin at a glucocorticoid-responsive enhancer.Role of transcription factors in inflammatory lung diseases.Regulation of the cellular prion protein gene expression depends on chromatin conformation.Local sequence features that influence AP-1 cis-regulatory activity.AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent Enhancer Selection.Regions of variant histone His2AvD required for Drosophila development.
P2860
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P2860
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
description
1997 nî lūn-bûn
@nan
1997 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@ast
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@en
type
label
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@ast
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@en
prefLabel
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@ast
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@en
P2093
P2860
P356
P1433
P1476
The binding of a Fos/Jun heterodimer can completely disrupt the structure of a nucleosome
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/16.8.2072
P407
P577
1997-04-01T00:00:00Z