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

Deubiquitinating activity of CYLD is impaired by SUMOylation in neuroblastoma cells.

Oncogene - 23 Apr 2015

Kobayashi T, Masoumi K C, Massoumi R

Abstract excerpt

CYLD is a deubiquitinating (DUB) enzyme that has a pivotal role in modulating nuclear factor kappa B (NF-κB) signaling pathways by removing the lysine 63- and linear-linked ubiquitin chain from substrates such as tumor necrosis factor receptor-associated factor 2 (TRAF2) and TRAF6. Loss of CYLD a...

Read the complete abstract on PubMed

Topics

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

Share to Deubiquitinating Enzyme CYLD
Share to Neuroblastoma
Share to NF-kappa B

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Sumoylation

Share to TNF Receptor-Associated Factor 2

Share to TNF Receptor-Associated Factor 6

Share to Tretinoin

Share to Ubiquitination

Source

Identifiers

PMID: 24909169
DOI: 10.1038/onc.2014.159

Genes

CYLD
TRAF2
TRAF6

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026. Prepared record publication-24909169-2026-09-04.2. Manifest publication-graph-cohort-2026-09-04.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Deubiquitinating activity of CYLD is impaired by SUMOylation in neuroblastoma cells.PMID 24909169Read ↗

The tumour suppressor CYLD negatively regulates NF-kappaB signalling by deubiquitination.Semantic proximity Read ↗

CYLD-Mediated Signaling and DiseasesSemantic proximity Read ↗

CYLD Alterations in the Tumorigenesis and Progression of Human Papillomavirus–Associated Head and Neck CancersSemantic proximity Read ↗

CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members.Semantic proximity Read ↗

Tumor Suppressor Function of CYLD in Nonmelanoma Skin CancerSemantic proximity Read ↗

Regulation of natural killer T-cell development by deubiquitinase CYLD.Semantic proximity Read ↗

Impaired regulation of NF-kappaB and increased susceptibility to colitis-associated tumorigenesis in CYLD-deficient mice.Semantic proximity Read ↗

NF-kappaB is essential for induction of CYLD, the negative regulator of NF-kappaB: evidence for a novel inducible autoregulatory feedback pathway.Semantic proximity Read ↗

CYLD negatively regulates cell-cycle progression by inactivating HDAC6 and increasing the levels of acetylated tubulin.Semantic proximity Read ↗

Stabilization of p18 by deubiquitylase CYLD is pivotal for cell cycle progression and viral replicationSemantic proximity Read ↗

Catalytic domain mutation in CYLD inactivates its enzyme function by structural perturbation and induces cell migration and proliferation.Semantic proximity Read ↗

The tumour suppressor CYLD is a negative regulator of RIG-I-mediated antiviral response.Semantic proximity Read ↗

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