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

A Phosphomimetic Study Implicates Ser557 in Regulation of FOXP2 DNA Binding.

The protein journal - 1 Aug 2018

Blane Ashleigh, Dirr Heini W, Fanucchi Sylvia

Abstract excerpt

FOXP2 is a transcription factor expressed in multiple tissues during embryonic development. FOXP2 regulates transcription by binding to DNA at its DNA binding domain, the forkhead domain (FHD) through the recognition helix. Ser557 is a residue located within the recognition helix that has the potential to become phosphorylated posttranslationally. In this study we investigated whether phosphorylation of Ser557...

Read the complete abstract on PubMed

Topics

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

Share to DNA
Share to Forkhead Transcription Factors
Share to Molecular Docking Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Mimicry

Share to Phosphorylation

Share to Protein Conformation

Share to Protein Domains

Share to Serine

Source

Identifiers

PMID: 29845391
DOI: 10.1007/s10930-018-9777-7

Genes

FOXP2

Variants

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A Phosphomimetic Study Implicates Ser557 in Regulation of FOXP2 DNA Binding.PMID 29845391Read ↗

Structure of the forkhead domain of FOXP2 bound to DNA.Semantic proximity Read ↗

A comprehensive in silico analysis of the deleterious nonsynonymous SNPs of human FOXP2 protein.Semantic proximity Read ↗

Structural insights into FOXP2 multimerization and interactions from AlphaFold3 modelingSemantic proximity Read ↗

Structural and biological features of FOXP3 dimerization relevant to regulatory T cell function.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 ↗

Two lysines in the forkhead domain of foxp3 are key to T regulatory cell function.Semantic proximity Read ↗

Different molecular complexes that mediate transcriptional induction and repression by FoxP3.Semantic proximity Read ↗

Structure of a domain-swapped FOXP3 dimer on DNA and its function in regulatory T cells.Semantic proximity Read ↗

FOXP3 recognizes microsatellites and bridges DNA through multimerization.Semantic proximity Read ↗

Clinical and structural impact of mutations affecting the residue Phe367 of FOXP3 in patients with IPEX syndrome.Semantic proximity Read ↗

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.Semantic proximity Read ↗

FoxP3 recognizes microsatellites and bridges DNA through multimerizationSemantic proximity Read ↗

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