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

Functional importance of Stat3 tetramerization in activation of the alpha 2-macroglobulin gene.

The Journal of biological chemistry - 7 Sept 2001

Zhang X, Darnell J E

Abstract excerpt

A tetrameric Stat3 complex was found to be essential in transfection experiments for maximal interleukin-6-inducible activation of alpha2-macroglobulin gene promoter. Stable tetramer formation of purified phosphorylated Stat3 was dependent on protein.protein interaction involving the N-terminal domain of Stat3. The functional importance of tetramer formation was shown by the decreased levels of transcriptional...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Macroglobulins
Share to Deoxyribonuclease I
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glutathione Transferase

Share to Immunoblotting

Share to Interleukin-6

Share to Proto-Oncogene Proteins c-jun

Share to STAT3 Transcription Factor

Source

Identifiers

PMID: 11438543
DOI: 10.1074/jbc.M104978200

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

Functional importance of Stat3 tetramerization in activation of the alpha 2-macroglobulin gene.PMID 11438543Read ↗

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

Aberrant function of pathogenic STAT3 mutant proteins is linked to altered stability of monomers and homodimers.Semantic proximity Read ↗

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

The role of tetramerization in p53 function.Semantic proximity Read ↗

Elevated activity of STAT3C due to higher DNA binding affinity of phosphotyrosine dimer rather than covalent dimer formation.Semantic proximity Read ↗

A new role for STAT3 as a regulator of chromatin topologySemantic proximity Read ↗

Novel Roles of Unphosphorylated STAT3 in Oncogenesis and Transcriptional RegulationSemantic proximity Read ↗

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

A mutant signal transducer and activator of transcription 5b, associated with growth hormone insensitivity and insulin-like growth factor-I deficiency, cannot function as a signal transducer or transcription factor.Semantic proximity Read ↗

Dominant-negative activity of the STAT3-Y705F mutant depends on the N-terminal domain.Semantic proximity Read ↗

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

Consequences of the disease-related L78R mutation for dimerization and activity of STAT3.Semantic proximity Read ↗

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