Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.

The Journal of biological chemistry - 17 Jul 2009

Silhan Jan, Vacha Petr, Strnadova Pavla, Vecer Jaroslav, Herman Petr, Sulc Miroslav, Teisinger Jan, Obsilova Veronika, Obsil Tomas

Abstract excerpt

The role of 14-3-3 proteins in the regulation of FOXO forkhead transcription factors is at least 2-fold. First, the 14-3-3 binding inhibits the interaction between the FOXO and the target DNA. Second, the 14-3-3 proteins prevent nuclear reimport of FOXO factors by masking their nuclear localizati...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to 14-3-3 Proteins
Share to Cell Cycle Proteins
Share to Electrophoresis, Polyacrylamide Gel

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Polarization

Share to Forkhead Transcription Factors

Share to Protein Multimerization

Share to Protein Structure, Tertiary

Share to Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Source

Open in PubMed Open full text

Identifiers

PMID: 19416966
DOI: 10.1074/jbc.M109.002725
PMCID: PMC2740560

Genes

FOXO4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19416966-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

14-3-3 protein masks the DNA binding interface of forkhead transcription factor FOXO4.PMID 19416966Read ↗

14-3-3 protein C-terminal stretch occupies ligand binding groove and is displaced by phosphopeptide binding.Semantic proximity Read ↗

Structural basis of 14-3-3 protein functions.Semantic proximity Read ↗

FoxO6, a novel member of the FoxO class of transcription factors with distinct shuttling dynamics.Semantic proximity Read ↗

Role of the 14-3-3 C-terminal loop in ligand interaction.Semantic proximity Read ↗

Oncogenic mutations in the DNA-binding domain of FOXO1 disrupt folding: quantitative insights from experiments and molecular simulationsSemantic proximity Read ↗

Oncogenic Mutations in the DNA-Binding Domain of FOXO1 that Disrupt Folding: Quantitative Insights from Experiments and Molecular Simulations.Semantic proximity Read ↗

Effect of mutations mimicking phosphorylation on the structure and properties of human 14-3-3zeta.Semantic proximity Read ↗

Exposed loop domains of complexed 14-3-3 proteins contribute to structural diversity and functional specificity.Semantic proximity Read ↗

Solution structure and backbone dynamics of the DNA-binding domain of FOXP1: insight into its domain swapping and DNA binding.Semantic proximity Read ↗

Identification of the site of interaction of the 14-3-3 protein with phosphorylated tryptophan hydroxylase.Semantic proximity Read ↗

Affinity, kinetic, and structural study of the interaction of 3-O-sulfotransferase isoform 1 with heparan sulfate.Semantic proximity Read ↗

Structural Analysis of the 14-3-3ζ/Chibby Interaction Involved in Wnt/β-Catenin Signaling.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.