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

Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain.

Science (New York, N.Y.) - 9 Aug 1996

Xu X, Sun Y L, Hoey T

Abstract excerpt

STAT proteins (signal transducers and activators of transcription) activate distinct target genes despite having similar DNA binding preferences. The transcriptional specificity of STAT proteins was investigated on natural STAT binding sites near the interferon-gamma gene. These sites are arranged in multiple copies and required cooperative interactions for STAT binding. The conserved amino-terminal domain of...

Read the complete abstract on PubMed

Topics

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

Share to Base Sequence
Share to Binding Sites
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Binding Proteins

Share to Molecular Sequence Data

Share to Mutation

Share to Promoter Regions, Genetic

Source

Identifiers

PMID: 8670419
DOI: 10.1126/science.273.5276.794

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

Cooperative DNA binding and sequence-selective recognition conferred by the STAT amino-terminal domain.PMID 8670419Read ↗

Stat Protein Transactivation Domains Recruit p300/CBP through Widely Divergent SequencesSemantic proximity Read ↗

Murine Stat2 is uncharacteristically divergentSemantic proximity Read ↗

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

MER41 Repeat Sequences Contain Inducible STAT1 Binding SitesSemantic proximity Read ↗

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

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

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

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

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

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

Synergistic activity of STAT3 and c-Jun at a specific array of DNA elements in the alpha 2-macroglobulin promoter.Semantic proximity Read ↗

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