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

Stabilization of p18 by deubiquitylase CYLD is pivotal for cell cycle progression and viral replication

2 Mar 2021

Abstract excerpt

p18 is a key negative regulator of cell cycle progression and mediates cell cycle arrest at the G1/S phase. Ubiquitination is the prime mechanism in regulating p18 protein abundance. However, so far no post- translational regulator, especially DUBs, has been identified to regulate the protein stability of p18. In this paper, we identified CYLD as a deubiquitinase of p18, which binds to and removes the K48-linked...

Read the complete abstract on PubMed

Topics

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

Share to Cancer-related Molecular Pathways
Share to Genetics and Neurodevelopmental Disorders
Share to Ubiquitin and proteasome pathways

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33654169
DOI: 10.1038/s41698-021-00153-8

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Stabilization of p18 by deubiquitylase CYLD is pivotal for cell cycle progression and viral replicationPMID 33654169Read ↗

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

Dissenting degradation: Deubiquitinases in cell cycle and cancer.Semantic proximity Read ↗

Deubiquitinases as novel therapeutic targets for diseasesSemantic proximity Read ↗

The Role of Deubiquitinases in Virus Replication and Host Innate Immune ResponseSemantic proximity Read ↗

Role of Deubiquitinases in Human Cancers: Potential Targeted TherapySemantic proximity Read ↗

Deubiquitylating Enzymes in Cancer and ImmunitySemantic proximity Read ↗

Deubiquitinases in cancer: new functions and therapeutic options.Semantic proximity Read ↗

The emerging role of deubiquitinating enzymes in genomic integrity, diseases, and therapeuticsSemantic proximity Read ↗

Deubiquitinase USP18 promotes the progression of pancreatic cancer via enhancing the Notch1-c-Myc axisSemantic proximity Read ↗

Emerging regulatory mechanisms in ubiquitin-dependent cell cycle controlSemantic proximity Read ↗

The N-terminal ubiquitin-associated domain of Cezanne is crucial for its function to suppress NF-κB pathway.Semantic proximity Read ↗

The Ubiquitin–Proteasome System is an Important Driver of EBV-Associated Nasopharyngeal Carcinoma Progression: A Meta-Analysis of Transcriptomics DataSemantic proximity Read ↗

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