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 trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.

The Journal of biological chemistry - 2 Jul 2004

Agou Fabrice, Traincard François, Vinolo Emilie, Courtois Gilles, Yamaoka Shoji, Israël Alain, Véron Michel

Abstract excerpt

NEMO (NF-kappaB essential modulator) plays a key role in the canonical NF-kappaB pathway as the scaffold/regulatory component of the IkappaB kinase (IKK) complex. The self-association of NEMO involves the C-terminal halves of the polypeptide chains containing two putative coiled-coil motifs (a CC2 and a LZ leucine zipper), a proline-rich region, and a ZF zinc finger motif. Using purified truncation mutants, we...

Read the complete abstract on PubMed

Topics

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

Share to Anisotropy
Share to Chromatography

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Chromatography, Gel

Share to I-kappa B Kinase

Share to Lipopolysaccharides

Share to NF-kappa B

Share to Precipitin Tests

Share to Zinc Fingers

Source

Identifiers

PMID: 15107419
DOI: 10.1074/jbc.M314278200

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

The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains.PMID 15107419Read ↗

DARPin-assisted crystallography of the CC2-LZ domain of NEMO reveals a coupling between dimerization and ubiquitin binding.Semantic proximity Read ↗

Recruitment of A20 by the C-terminal domain of NEMO suppresses NF-κB activation and autoinflammatory disease.Semantic proximity Read ↗

Analysis of nuclear factor-κB (NF-κB) essential modulator (NEMO) binding to linear and lysine-linked ubiquitin chains and its role in the activation of NF-κB.Semantic proximity Read ↗

NEMO reshapes the protein aggregate interface and promotes aggrephagy by co-condensation with p62Semantic proximity Read ↗

Structural basis for recognition of diubiquitins by NEMO.Semantic proximity Read ↗

Identifying post-translational modifications of NEMO by tandem mass spectrometry after high affinity purification.Semantic proximity Read ↗

Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347.Semantic proximity Read ↗

Identification of a new NEMO/TRAF6 interface affected in incontinentia pigmenti pathology.Semantic proximity Read ↗

Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex.Semantic proximity Read ↗

The NEMO mutation creating the most-upstream premature stop codon is hypomorphic because of a reinitiation of translation.Semantic proximity Read ↗

The zinc finger domain of IKKγ (NEMO) protein in health and disease.Semantic proximity Read ↗

Dendritic cells from humans with hypomorphic mutations in IKBKG/NEMO have impaired mitogen-activated protein kinase activity.Semantic proximity Read ↗

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