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

Preclinical pharmacology of glucosylceramide synthase inhibitor venglustat in a GBA-related synucleinopathy model.

Scientific reports - 22 Oct 2021

Viel Catherine, Clarke Jennifer, Kayatekin Can, Richards Amy M, Chiang Ming Sum R, Park Hyejung, Wang Bing, Shihabuddin Lamya S, Sardi S Pablo

Abstract excerpt

Mutations in GBA, the gene encoding the lysosomal enzyme glucocerebrosidase (GCase), represent the greatest genetic risk factor for developing synucleinopathies including Parkinson's disease (PD). Additionally, PD patients harboring a mutant GBA allele present with an earlier disease onset and an accelerated disease progression of both motor and non-motor symptoms. Preclinical studies in mouse models of...

Read the complete abstract on PubMed

Topics

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

Share to Carbamates
Share to Disease Models, Animal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosylceramidase

Share to Glucosylceramides

Share to Glucosyltransferases

Share to Hippocampus

Share to Mice, Inbred C57BL

Share to Parkinson Disease

Source

Open in PubMed Open full text

Identifiers

PMID: 34686711
DOI: 10.1038/s41598-021-00404-5
PMCID: PMC8536659

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

Preclinical pharmacology of glucosylceramide synthase inhibitor venglustat in a GBA-related synucleinopathy model.PMID 34686711Read ↗

Glucosylceramide synthase inhibition alleviates aberrations in synucleinopathy models.Semantic proximity Read ↗

A novel glucosylceramide synthase inhibitor attenuates alpha synuclein pathology and lysosomal dysfunction in preclinical models of synucleinopathySemantic proximity Read ↗

Glucosylsphingosine Promotes α-Synuclein Pathology in Mutant GBA-Associated Parkinson's Disease.Semantic proximity Read ↗

Neuronopathic GBA1 L444P mutation accelerates Glucosylsphingosine levels and formation of hippocampal alpha-synuclein inclusionsSemantic proximity Read ↗

GBA haploinsufficiency accelerates alpha-synuclein pathology with altered lipid metabolism in a prodromal model of Parkinson’s diseaseSemantic proximity Read ↗

Glucocerebrosidase-associated Parkinson disease: Pathogenic mechanisms and potential drug treatments.Semantic proximity Read ↗

Safety, Pharmacokinetics, and Pharmacodynamics of Oral Venglustat in Patients with Parkinson's Disease and a GBA Mutation: Results from Part 1 of the Randomized, Double-Blinded, Placebo-Controlled MOVES-PD Trial.Semantic proximity Read ↗

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

Neuronopathic GBA1L444P Mutation Accelerates Glucosylsphingosine Levels and Formation of Hippocampal Alpha-Synuclein Inclusions.Semantic proximity Read ↗

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

The GBA1 D409V mutation exacerbates synuclein pathology to differing extents in two alpha-synuclein models.Semantic proximity Read ↗

The interplay between Glucocerebrosidase, α-synuclein and lipids in human models of Parkinson’s diseaseSemantic proximity Read ↗

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