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

Mutational analysis of the kinetics and thermodynamics of transcription factor NF-kappaB homodimerisation.

Chembiochem : a European journal of chemical biology - 2 Dec 2002

Day Y S N, Bacon S L, Hughes-Thomas Z, Blackburn J M, Sutherland J D

Abstract excerpt

Dimeric transcription factors of the NF-kappaB/Rel family are sequence-specific DNA-binding proteins that mediate the inducible expression of immunologically important eukaryotic genes by competing for kappaB sites. The kinetic and thermodynamic components of these interactions were probed by mutation of the subunit interface of the p50 homodimer, a paradigm for other family members. Guided by the crystal...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Dimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Kinetics

Share to Mutagenesis, Site-Directed

Share to NF-kappa B

Share to NF-kappa B p50 Subunit

Share to Surface Plasmon Resonance

Share to Thermodynamics

Source

Identifiers

PMID: 12465027
DOI: 10.1002/1439-7633(20021202)3:12<1192::AID-CBIC1192>3.0.CO;2-U

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational analysis of the kinetics and thermodynamics of transcription factor NF-kappaB homodimerisation.PMID 12465027Read ↗

Snapshot of protein structure evolution reveals conservation of functional dimerization through intertwined folding.Semantic proximity Read ↗

A mutant Rel-homology domain promotes transcription by p50/NFkappaB1.Semantic proximity Read ↗

Analysis of the RelA:CBP/p300 Interaction Reveals Its Involvement in NF-κB-Driven TranscriptionSemantic proximity Read ↗

Dimerisation of the UBA domain of p62 inhibits ubiquitin binding and regulates NF-kappaB signalling.Semantic proximity Read ↗

Structural and functional analysis of NF-kappa B. Determinants of DNA binding specificity and protein interaction.Semantic proximity Read ↗

Expression, purification and functional characterization of IkappaB kinase-2 (IKK-2) mutants.Semantic proximity Read ↗

Modulating the DNA affinity of Elk-1 with computationally selected mutations.Semantic proximity Read ↗

Functional characterization of hepatocyte nuclear factor-4 alpha dimerization interface mutants.Semantic proximity Read ↗

The role of the p50 and p65 subunits of NF-kappa B in the recognition of cognate sequences.Semantic proximity Read ↗

Molecular determinants of the granulocyte-macrophage colony-stimulating factor receptor complex assembly.Semantic proximity Read ↗

Simulating the effect of DNA polymerase mutations on transition-state energetics and fidelity: evaluating amino acid group contribution and allosteric coupling for ionized residues in human pol beta.Semantic proximity Read ↗

Discreet mutations from c-Rel to v-Rel alter kappaB DNA recognition, IkappaBalpha binding, and dimerization: implications for v-Rel oncogenicity.Semantic proximity Read ↗

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