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

Glucocerebrosidase Deficiency in Drosophila Results in α-Synuclein-Independent Protein Aggregation and Neurodegeneration.

PLoS genetics - 1 Mar 2016

Davis Marie Y, Trinh Kien, Thomas Ruth E, Yu Selina, Germanos Alexandre A, Whitley Brittany N, Sardi Sergio Pablo, Montine Thomas J, Pallanck Leo J

Abstract excerpt

Mutations in the glucosidase, beta, acid (GBA1) gene cause Gaucher's disease, and are the most common genetic risk factor for Parkinson's disease (PD) and dementia with Lewy bodies (DLB) excluding variants of low penetrance. Because α-synuclein-containing neuronal aggregates are a defining feature of PD and DLB, it is widely believed that mutations in GBA1 act by enhancing α-synuclein toxicity. To explore this...

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 Dopaminergic Neurons

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gaucher Disease

Share to Glucosylceramidase

Share to Lysosomes

Share to Nerve Degeneration

Share to Parkinson Disease

Share to Protein Aggregation, Pathological

Source

Open in PubMed Open full text

Identifiers

PMID: 27019408
DOI: 10.1371/journal.pgen.1005944
PMCID: PMC4809718

Genes

GBA1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Glucocerebrosidase Deficiency in Drosophila Results in α-Synuclein-Independent Protein Aggregation and Neurodegeneration.PMID 27019408Read ↗

GBA1 Gene Mutations in α-Synucleinopathies-Molecular Mechanisms Underlying Pathology and Their Clinical Significance.Semantic proximity Read ↗

Glucocerebrosidase deficiency accelerates the accumulation of proteinase K-resistant α-synuclein and aggravates neurodegeneration in aDrosophilamodel of Parkinson's diseaseSemantic proximity Read ↗

Mutant GBA1 expression and synucleinopathy risk: first insights from cellular and mouse models.Semantic proximity Read ↗

Glucocerebrosidase and its relevance to Parkinson diseaseSemantic proximity Read ↗

Molecular mechanisms of α-synuclein and GBA1 in Parkinson's disease.Semantic proximity Read ↗

Glucocerebrosidase mutations and synucleinopathies: Toward a model of precision medicineSemantic proximity Read ↗

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

Glucocerebrosidase reduces the spread of protein aggregation in a Drosophila melanogaster model of neurodegeneration by regulating proteins trafficked by extracellular vesicles.Semantic proximity Read ↗

The biochemical basis of interactions between Glucocerebrosidase and alpha-synuclein in GBA1 mutation carriers.Semantic proximity Read ↗

Variant-specific effects of GBA1 mutations on dopaminergic neuron proteostasis.Semantic proximity Read ↗

Acid β-glucosidase mutants linked to Gaucher disease, Parkinson disease, and Lewy body dementia alter α-synuclein processing.Semantic proximity Read ↗

Gaucher-related synucleinopathies: the examination of sporadic neurodegeneration from a rare (disease) angle.Semantic proximity Read ↗

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