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

Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1.

Biomolecular NMR assignments - 1 Oct 2011

Tse Ho-Sum, Hu Hong-Yu, Sze Kong-Hung

Abstract excerpt

Ubiquitin carboxy-terminal hydrolase L1 (UCH-L1), also known as PGP9.5, is a protein of 223 amino acids. Although it was originally characterized as a deubiquitinating enzyme, recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. It is highly abundant in brain, constituting up to 2% of total brain proteins. Down-regulation and extensive oxidative modification of...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Molecular Sequence Data
Share to Mutation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Parkinson Disease

Share to Ubiquitin Thiolesterase

Source

Open in PubMed Open full text

Identifiers

PMID: 21298373
DOI: 10.1007/s12104-011-9292-7
PMCID: PMC3166605

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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

Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1.PMID 21298373Read ↗

The effect of Parkinson's-disease-associated mutations on the deubiquitinating enzyme UCH-L1.Semantic proximity Read ↗

Familial Mutations and Post-translational Modifications of UCH-L1 in Parkinson’s Disease and Neurodegenerative DisordersSemantic proximity Read ↗

Alterations of structure and hydrolase activity of parkinsonism-associated human ubiquitin carboxyl-terminal hydrolase L1 variants.Semantic proximity Read ↗

Familial Mutations and Post-translational Modifications of UCH-L1 in Parkinson's Disease and Neurodegenerative Disorders.Semantic proximity Read ↗

S18Y in ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) associated with decreased risk of Parkinson's disease in Sweden.Semantic proximity Read ↗

Aberrant molecular properties shared by familial Parkinson’s disease-associated mutant UCH-L1 and carbonyl-modified UCH-L1Semantic proximity Read ↗

Association between the ubiquitin carboxyl-terminal esterase L1 gene (UCHL1) S18Y variant and Parkinson's Disease: a HuGE review and meta-analysis.Semantic proximity Read ↗

Novel UCHL1 mutations reveal new insights into ubiquitin processing.Semantic proximity Read ↗

The role of ubiquitin C-terminal hydrolase L1 in neurodegenerative disorders.Semantic proximity Read ↗

UCHL1 is a Parkinson's disease susceptibility gene.Semantic proximity Read ↗

Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases.Semantic proximity Read ↗

Association between ubiquitin carboxy-terminal hydrolase-L1 S18Y variant and risk of Parkinson's disease: the impact of ethnicity and onset age.Semantic proximity Read ↗

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