The activation domain of the bovine papillomavirus E2 protein mediates association of DNA-bound dimers to form DNA loops.
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The mitotic chromosome binding activity of the papillomavirus E2 protein correlates with interaction with the cellular chromosomal protein, Brd4.Induction of the rat prodynorphin gene through Gs-coupled receptors may involve phosphorylation-dependent derepression and activationStructure of the intact transactivation domain of the human papillomavirus E2 proteinp53 oligomerization and DNA looping are linked with transcriptional activationPhylogenetic and functional analysis identifies Ets-1 as a novel regulator of the Th2 cytokine gene locus.A point mutation in the DNA-binding domain of HPV-2 E2 protein increases its DNA-binding capacity and reverses its transcriptional regulatory activity on the viral early promoter.DNA looping.During negative regulation of the human papillomavirus-16 E6 promoter, the viral E2 protein can displace Sp1 from a proximal promoter element.Replication and partitioning of papillomavirus genomes.DNA binding and condensation properties of the herpes simplex virus type 1 triplex protein VP19CThe bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex.DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume.Structural analysis of the human papillomavirus type 16-E2 transactivator with antipeptide antibodies reveals a high mobility region linking the transactivation and the DNA-binding domains.Zeste-mediated activation by an enhancer is independent of cooperative DNA binding in vivoThe human papillomavirus type 16 E2 transcription factor binds with low cooperativity to two flanking sites and represses the E6 promoter through displacement of Sp1 and TFIID.Low-affinity E2-binding site mediates downmodulation of E2 transactivation of the human papillomavirus type 8 late promoter.Determination of heat-shock transcription factor 2 stoichiometry at looped DNA complexes using scanning force microscopy.Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.The papillomavirus E2 proteinsFormation of the complex of bovine papillomavirus E1 and E2 proteins is modulated by E2 phosphorylation and depends upon sequences within the carboxyl terminus of E1.DNA looping between the origin of replication of Epstein-Barr virus and its enhancer site: stabilization of an origin complex with Epstein-Barr nuclear antigen 1.Epstein-Barr nuclear antigen 1 mediates a DNA loop within the latent replication origin of Epstein-Barr virus.Regulation of early gene expression from the bovine papillomavirus genome in transiently transfected C127 cells.Transcriptional and replicational activation functions in the bovine papillomavirus type 1 E2 protein are encoded by different structural determinants.The linking regions of EBNA1 are essential for its support of replication and transcription.Long-term episomal maintenance of bovine papillomavirus type 1 plasmids is determined by attachment to host chromosomes, which Is mediated by the viral E2 protein and its binding sites.Oligomerization of the transcription termination factor TTF-I: implications for the structural organization of ribosomal transcription unitsMultiple regions within EBNA1 can link DNAs.Separate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.Dimerization of the human papillomavirus type 16 E2 N terminus results in DNA looping within the upstream regulatory region.A domain of the even-skipped protein represses transcription by preventing TFIID binding to a promoter: repression by cooperative blocking.Bending DNA can repress a eukaryotic basal promoter and inhibit TFIID binding.Cooperative DNA binding of the bovine papillomavirus E2 transcriptional activator is antagonized by truncated E2 polypeptides.DNA-binding domain of bovine papillomavirus type 1 E1 helicase: structural and functional aspects.Mechanism of action of the papillomavirus E2 repressor: repression in the absence of DNA binding.Structural and Functional Basis for an EBNA1 Hexameric Ring in Epstein-Barr Virus Episome Maintenance.The ORFa protein, the putative transposase of maize transposable element Ac, has a basic DNA binding domain.Cooperative binding at a distance by even-skipped protein correlates with repression and suggests a mechanism of silencing.Remodeling of the human papillomavirus type 11 replication origin into discrete nucleoprotein particles and looped structures by the E2 protein.The basic helix-loop-helix-zipper domain of TFE3 mediates enhancer-promoter interaction.
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The activation domain of the bovine papillomavirus E2 protein mediates association of DNA-bound dimers to form DNA loops.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on April 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
The activation domain of the b ...... ound dimers to form DNA loops.
@en
The activation domain of the b ...... ound dimers to form DNA loops.
@nl
type
label
The activation domain of the b ...... ound dimers to form DNA loops.
@en
The activation domain of the b ...... ound dimers to form DNA loops.
@nl
prefLabel
The activation domain of the b ...... ound dimers to form DNA loops.
@en
The activation domain of the b ...... ound dimers to form DNA loops.
@nl
P2093
P2860
P356
P1476
The activation domain of the b ...... ound dimers to form DNA loops.
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.8.3204
P407
P577
1991-04-01T00:00:00Z