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

Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy.

The Journal of biological chemistry - 29 Aug 2008

Kabuta Tomohiro, Furuta Akiko, Aoki Shunsuke, Furuta Koh, Wada Keiji

Abstract excerpt

Parkinson disease (PD) is the most common neurodegenerative movement disorder. An increase in the amount of alpha-synuclein protein could constitute a cause of PD. Alpha-synuclein is degraded at least partly by chaperone-mediated autophagy (CMA). The I93M mutation in ubiquitin C-terminal hydrolase L1 (UCH-L1) is associated with familial PD. However, the relationship between alpha-synuclein and UCH-L1 in the...

Read the complete abstract on PubMed

Topics

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

Share to alpha-Synuclein
Share to Autophagy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HSC70 Heat-Shock Proteins

Share to HSP90 Heat-Shock Proteins

Share to Lysosomal-Associated Membrane Protein 2

Share to Lysosomal Membrane Proteins

Share to NIH 3T3 Cells

Share to Ubiquitin Thiolesterase

Source

Open in PubMed Open full text

Identifiers

PMID: 18550537
DOI: 10.1074/jbc.M801918200
PMCID: PMC3259779

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

Aberrant interaction between Parkinson disease-associated mutant UCH-L1 and the lysosomal receptor for chaperone-mediated autophagy.PMID 18550537Read ↗

Insights into links between familial and sporadic Parkinson's disease: Physical relationship between UCH-L1 variants and chaperone-mediated autophagySemantic proximity Read ↗

Role of Chaperone-Mediated Autophagy Dysfunctions in the Pathogenesis of Parkinson’s DiseaseSemantic proximity Read ↗

Inhibition of UCH-L1 in oligodendroglial cells results in microtubule stabilization and prevents α-synuclein aggregate formation by activating the autophagic pathway: implications for multiple system atrophySemantic proximity Read ↗

Parkin-mediated K63-polyubiquitination targets ubiquitin C-terminal hydrolase L1 for degradation by the autophagy-lysosome system.Semantic proximity Read ↗

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

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

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

The role of autophagy-lysosome pathway in neurodegeneration associated with Parkinson's disease.Semantic proximity Read ↗

LAMP2A as a therapeutic target in Parkinson diseaseSemantic proximity Read ↗

Interaction of LRRK2 and α-Synuclein in Parkinson's Disease.Semantic proximity Read ↗

Interplay of LRRK2 with chaperone-mediated autophagy.Semantic proximity Read ↗

UCH-L1 aggresome formation in response to proteasome impairment indicates a role in inclusion formation in Parkinson's disease.Semantic proximity Read ↗

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