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

Visualization and quantification of dynamic STAT3 homodimerization in living cells using homoFluoppi

30 Jan 2018

Abstract excerpt

Dimerization in signal transduction is a dynamically regulated process and a key regulatory mechanism. Signal transducer and activator of transcription 3 (STAT3) dimerizes after tyrosine phosphorylation upon cytokine stimulation. Because only the STAT3 dimer possesses the trans-activation activity, dimerization is an indispensable process for cytokine signaling. Here we report the detection of dynamic STAT3...

Read the complete abstract on PubMed

Topics

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

Share to Cytokine Signaling Pathways and Interactions
Share to Monoclonal and Polyclonal Antibodies Research
Share to Protein Tyrosine Phosphatases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 29402895
DOI: 10.1038/s41598-018-20234-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Visualization and quantification of dynamic STAT3 homodimerization in living cells using homoFluoppiPMID 29402895Read ↗

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

STAT-3 Inhibitors: State of the Art and New Horizons for Cancer TreatmentSemantic proximity Read ↗

Intramolecular hydrophobic interactions are critical mediators of STAT5 dimerization.Semantic proximity Read ↗

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

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

Mechanism of homodimeric cytokine receptor activation and dysregulation by oncogenic mutations.Semantic proximity Read ↗

Stat3 isoforms, alpha and beta, demonstrate distinct intracellular dynamics with prolonged nuclear retention of Stat3beta mapping to its unique C-terminal end.Semantic proximity Read ↗

Real time analysis of STAT3 nucleocytoplasmic shuttling.Semantic proximity Read ↗

Somatic mutations activating STAT3 in human inflammatory hepatocellular adenomas.Semantic proximity Read ↗

Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3.Semantic proximity Read ↗

Live Cell Imaging Demonstrates Multiple Routes Toward a STAT1 Gain-of-Function Phenotype.Semantic proximity Read ↗

Crystal structure of unphosphorylated STAT3 core fragment.Semantic proximity Read ↗

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