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

c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation.

The Journal of biological chemistry - 16 Feb 2001

Das K C

Abstract excerpt

NF-kappaB is a redox-sensitive transcription factor known to be activated by oxidative stress as well as chemical and biological reductants. Its DNA binding activity requires reduced cysteines present in the p65 subunit of the dimer. Thioredoxin (Trx) is an endogenous disulfide oxidoreductase known to modulate several redox-dependent functions in the cell. NF-kappaB was activated by addition of Escherichia coli...

Read the complete abstract on PubMed

Topics

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

Share to Acetylcysteine
Share to Active Transport, Cell Nucleus
Share to I-kappa B Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to JNK Mitogen-Activated Protein Kinases

Share to MAP Kinase Kinase 4

Share to MAP Kinase Kinase Kinase 1

Share to Mitogen-Activated Protein Kinase Kinases

Share to Thioredoxins

Source

Identifiers

PMID: 11063742
DOI: 10.1074/jbc.M006206200

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

c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation.PMID 11063742Read ↗

Thioredoxin promotes ASK1 ubiquitination and degradation to inhibit ASK1-mediated apoptosis in a redox activity-independent manner.Semantic proximity Read ↗

The role of thioredoxin in the aging process: involvement of oxidative stress.Semantic proximity Read ↗

Disulfide Bond-mediated multimerization of Ask1 and its reduction by thioredoxin-1 regulate H(2)O(2)-induced c-Jun NH(2)-terminal kinase activation and apoptosis.Semantic proximity Read ↗

The involvement of thioredoxin and thioredoxin binding protein-2 on cellular proliferation and aging process.Semantic proximity Read ↗

Thioredoxin regulates the redox state and the activity of the human tRNA ligase complexSemantic proximity Read ↗

Thioredoxin-1 phosphorylated at T100 is needed for its anti-apoptotic activity in HepG2 cancer cells.Semantic proximity Read ↗

Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.Semantic proximity Read ↗

Trxlp, a thioredoxin-like effector from Edwardsiella piscicida inhibits cellular redox signaling and nuclear translocation of NF-κB.Semantic proximity Read ↗

Reactive oxygen species-independent oxidation of thioredoxin in hypoxia: inactivation of ribonucleotide reductase and redox-mediated checkpoint control.Semantic proximity Read ↗

The protective role of the transmembrane thioredoxin-related protein TMX in inflammatory liver injury.Semantic proximity Read ↗

Thioredoxin modulates activator protein 1 (AP-1) activity and p27Kip1 degradation through direct interaction with Jab1.Semantic proximity Read ↗

Redox control of caspase-3 activity by thioredoxin and other reduced proteins.Semantic proximity Read ↗

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