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

Misfolded GBA/β-glucocerebrosidase impairs ER-quality control by chaperone-mediated autophagy in Parkinson disease.

Autophagy - 1 Dec 2022

Kuo Sheng-Han, Tasset Inmaculada, Cuervo Ana Maria, Sulzer David

Abstract excerpt

Inhibition of chaperone-mediated autophagy (CMA), a selective type of lysosomal degradation for intracellular proteins, may contribute to pathogenesis in neurodegenerative diseases including Parkinson disease (PD). Pathogenic variants of PD-related proteins that reside in the cytosol, including SNCA/alpha-synuclein, LRRK2 (leucine rich repeat kinase 2), UCHL1 (ubiquitin Cterminal hydrolase 1) and VPS35 (VPS35...

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 Endoplasmic Reticulum
Share to Glucosylceramidase

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

Share to Lysosomes

Share to Mutation

Share to Parkinson Disease

Share to Protein Folding

Share to Quality Control

Source

Open in PubMed Open full text

Identifiers

PMID: 35482760
DOI: 10.1080/15548627.2022.2071383
PMCID: PMC9673922

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Misfolded GBA/β-glucocerebrosidase impairs ER-quality control by chaperone-mediated autophagy in Parkinson disease.PMID 35482760Read ↗

Mutant glucocerebrosidase impairs α-synuclein degradation by blockade of chaperone-mediated autophagy.Semantic proximity Read ↗

GBA1-associated parkinsonism: new insights and therapeutic opportunitiesSemantic proximity Read ↗

Targeting the GBA1 pathway to slow Parkinson disease: Insights into clinical aspects, pathogenic mechanisms and new therapeutic avenues.Semantic proximity Read ↗

GBA Variants and Parkinson Disease: Mechanisms and Treatments.Semantic proximity Read ↗

Glucocerebrosidase Mutations Cause Mitochondrial and Lysosomal Dysfunction in Parkinson’s Disease: Pathogenesis and Therapeutic ImplicationsSemantic proximity Read ↗

The role of glucocerebrosidase in Parkinson disease pathogenesis.Semantic proximity Read ↗

Glucocerebrosidase mutations and Parkinson disease.Semantic proximity Read ↗

The relationship between glucocerebrosidase mutations and Parkinson disease.Semantic proximity Read ↗

Enhancing the Activity of Glucocerebrosidase as a Treatment for Parkinson Disease.Semantic proximity Read ↗

Lysosomal functions and dysfunctions: Molecular and cellular mechanisms underlying Gaucher disease and its association with Parkinson disease.Semantic proximity Read ↗

Glucocerebrosidase and Parkinson Disease: Molecular, Clinical, and Therapeutic Implications.Semantic proximity Read ↗

Multi-omics insights into GBA1-associated Parkinson's disease: interplay of genomics, transcriptomics, proteomics, and lipidomics.Semantic proximity Read ↗

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