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

L444P Gba1 mutation increases formation and spread of α-synuclein deposits in mice injected with mouse α-synuclein pre-formed fibrils.

PloS one - 1 Jan 2020

Migdalska-Richards Anna, Wegrzynowicz Michal, Harrison Ian F, Verona Guglielmo, Bellotti Vittorio, Spillantini Maria Grazia, Schapira Anthony H V

Abstract excerpt

Parkinson disease is the most common neurodegenerative movement disorder, estimated to affect one in twenty-five individuals over the age of 80. Mutations in glucocerebrosidase 1 (GBA1) represent the most common genetic risk factor for Parkinson disease. The link between GBA1 mutations and α-synuclein accumulation, a hallmark of Parkinson disease, is not fully understood. Following our recent finding that Gba1...

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 Gene Knock-In Techniques

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucosylceramidase

Share to Injections

Share to Mutation

Share to Neostriatum

Share to Protein Aggregates

Source

Open in PubMed Open full text

Identifiers

PMID: 32833982
DOI: 10.1371/journal.pone.0238075
PMCID: PMC7444808

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

L444P Gba1 mutation increases formation and spread of α-synuclein deposits in mice injected with mouse α-synuclein pre-formed fibrils.PMID 32833982Read ↗

The L444P Gba1 mutation enhances alpha-synuclein induced loss of nigral dopaminergic neurons in mice.Semantic proximity Read ↗

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

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

D409H GBA1 mutation accelerates the progression of pathology in A53T α-synuclein transgenic mouse model.Semantic proximity Read ↗

α-Synuclein accumulation and GBA deficiency due to L444P GBA mutation contributes to MPTP-induced parkinsonism.Semantic proximity Read ↗

Heterozygous GBA D409V and ATP13a2 mutations do not exacerbate pathological α-synuclein spread in the prodromal preformed fibrils model in young mice.Semantic proximity Read ↗

Glucocerebrosidase Gene Therapy Induces Alpha-Synuclein Clearance and Neuroprotection of Midbrain Dopaminergic Neurons in Mice and Macaques.Semantic proximity Read ↗

A human <i>GBA-L444P</i> transgene drives early and persistent dopamine neurotransmission deficits and alpha-synuclein pathology in a mouse model of early Parkinson’s diseaseSemantic proximity Read ↗

AAV delivery of GBA1 suppresses α-synuclein accumulation in Parkinson’s disease models and restores functions in Gaucher’s disease modelsSemantic proximity Read ↗

AAV delivery of <i>GBA1</i> suppresses α-synuclein accumulation in Parkinson’s disease models and restores motor dysfunction in a Gaucher’s disease modelSemantic proximity Read ↗

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

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

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