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

Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53

25 Nov 2024

Abstract excerpt

Ubiquitin-specific proteases (USPs) represent the largest class of human deubiquitinases (DUBs) and comprise its phylogenetically most distant members USP53 and USP54, which are annotated as catalytically inactive pseudoenzymes. Conspicuously, mutations within the USP domain of USP53 cause progressive familial intrahepatic cholestasis. Here, we report the discovery that USP53 and USP54 are active DUBs with high...

Read the complete abstract on PubMed

Topics

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

Share to Autophagy in Disease and Therapy
Share to Cancer-related Molecular Pathways
Share to Ubiquitin and proteasome pathways

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 39587316
DOI: 10.1038/s41589-024-01777-0

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

Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53PMID 39587316Read ↗

Discovery and mechanism of K63-linkage-directed deubiquitinase activity in USP53Semantic proximity Read ↗

An Overview of the Deubiquitinase USP53: A Promising Diagnostic Marker and Therapeutic Target.Semantic proximity Read ↗

USP3 : Key deubiquitylation enzyme in human diseasesSemantic proximity Read ↗

Deubiquitinases as novel therapeutic targets for diseasesSemantic proximity Read ↗

Deubiquitinating enzymes in cellular signaling and disease regulationSemantic proximity Read ↗

Spotlights on ubiquitin-specific protease 12 (USP12) in diseases: from multifaceted roles to pathophysiological mechanismsSemantic proximity Read ↗

The structure and function of deubiquitinases: lessons from budding yeastSemantic proximity Read ↗

DUBs, the regulation of cell identity and diseaseSemantic proximity Read ↗

Ubiquitin becomes ubiquitous in cancerSemantic proximity Read ↗

Surprising variety in the USP deubiquitinase catalytic mechanismSemantic proximity Read ↗

Friend or foe? Reciprocal regulation between E3 ubiquitin ligases and deubiquitinasesSemantic proximity Read ↗

Ubiquitin-specific protease 8 (USP8/UBPy): a prototypic multidomain deubiquitinating enzyme with pleiotropic functions.Semantic proximity Read ↗

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