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

The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression.

Molecular immunology - 1 Oct 2015

Staab Julia, Riebeling Theresa, Koch Verena, Herrmann-Lingen Christoph, Meyer Thomas

Abstract excerpt

Defective cooperative DNA binding of STAT1 (signal transducer and activator of transcription 1) transcription factor has impact on interferon-γ(IFNγ)-regulated transcriptional responses. In this study, we generated N-terminal gain-of-function mutants of this protein which exhibited hyperactive cooperativity and assessed their functional consequences on gene expression. Our data show that four negatively charged,...

Read the complete abstract on PubMed

Topics

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

Share to Aspartic Acid
Share to Glutamic Acid
Share to Interferon-gamma

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutant Proteins

Share to Phosphotyrosine

Share to Protein Multimerization

Share to Protein Stability

Share to STAT1 Transcription Factor

Source

Identifiers

PMID: 26275341
DOI: 10.1016/j.molimm.2015.07.015

Genes

STAT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

The two interfaces of the STAT1 N-terminus exhibit opposite functions in IFNγ-regulated gene expression.PMID 26275341Read ↗

Clinically relevant dimer interface mutants of STAT1 transcription factor exhibit differential gene expression.Semantic proximity Read ↗

Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle.Semantic proximity Read ↗

A conserved motif in the linker domain of STAT1 transcription factor is required for both recognition and release from high-affinity DNA-binding sites.Semantic proximity Read ↗

A reinterpretation of the dimerization interface of the N-terminal domains of STATs.Semantic proximity Read ↗

Characterization of a pathogenic gain-of-function mutation in the N-terminal domain of STAT1 which is reported to be associated with eosinophilic esophagitisSemantic proximity Read ↗

Structural bases of unphosphorylated STAT1 association and receptor binding.Semantic proximity Read ↗

The Significance of Tetramerization in Promoter Recruitment by Stat5Semantic proximity Read ↗

Structural basis for DNA recognition by STAT6.Semantic proximity Read ↗

Transcriptional Profiling of STAT1 Gain-of-Function Reveals Common and Mutation-Specific Fingerprints.Semantic proximity Read ↗

N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation.Semantic proximity Read ↗

Amino-terminal signal transducer and activator of transcription (STAT) domains regulate nuclear translocation and STAT deactivation.Semantic proximity Read ↗

STAT2 Is a Pervasive Cytokine Regulator due to Its Inhibition of STAT1 in Multiple Signaling PathwaysSemantic proximity Read ↗

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