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

Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation.

Molecular and cellular biology - 1 Apr 1996

DiDonato J, Mercurio F, Rosette C, Wu-Li J, Suyang H, Ghosh S, Karin M

Abstract excerpt

Extracellular stimuli that activate the transcription factor NF-kappaB cause rapid phosphorylation of the IkappaBalpha inhibitor, which retains NF-kappaB in the cytoplasm of nonstimulated cells. Phosphorylation of IkappaBalpha is followed by its rapid degradation, the inhibition of which prevents...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to DNA-Binding Proteins
Share to HeLa Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Phosphorylation

Share to Precipitin Tests

Share to Protein Serine-Threonine Kinases

Source

Open in PubMed Open full text

Identifiers

PMID: 8657102
DOI: 10.1128/MCB.16.4.1295
PMCID: PMC231113

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8657102-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mapping of the inducible IkappaB phosphorylation sites that signal its ubiquitination and degradation.PMID 8657102Read ↗

Suppression of p65 phosphorylation coincides with inhibition of IkappaBalpha polyubiquitination and degradation.Semantic proximity Read ↗

Site-specific monoubiquitination of IkappaB kinase IKKbeta regulates its phosphorylation and persistent activation.Semantic proximity Read ↗

Immunosuppressant FK506 activates NF-kappaB through the proteasome-mediated degradation of IkappaBalpha. Requirement for Ikappabalpha n-terminal phosphorylation but not ubiquitination sites.Semantic proximity Read ↗

Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation.Semantic proximity Read ↗

Direct phosphorylation of IkappaB by IKKalpha and IKKbeta: discrimination between free and NF-kappaB-bound substrate.Semantic proximity Read ↗

Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation.Semantic proximity Read ↗

Ubiquitination of RIP is required for tumor necrosis factor alpha-induced NF-kappaB activation.Semantic proximity Read ↗

N- and C-terminal sequences control degradation of MAD3/I kappa B alpha in response to inducers of NF-kappa B activity.Semantic proximity Read ↗

Regulation of NF-κB activity by competition between RelA acetylation and ubiquitination.Semantic proximity Read ↗

Regulation of constitutive p50/c-Rel activity via proteasome inhibitor-resistant IkappaBalpha degradation in B cells.Semantic proximity Read ↗

Monoubiquitination of nuclear RelA negatively regulates NF-κB activity independent of proteasomal degradation.Semantic proximity Read ↗

IkappaBalpha deficiency results in a sustained NF-kappaB response and severe widespread dermatitis in mice.Semantic proximity Read ↗

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