GBA (Glucocerebrosidase) is a critical gene in the intersection of lysosomal storage disorders and neurodegenerative diseases. Mutations in GBA cause Gaucher disease, the most common lysosomal storage disorder, and constitute the strongest genetic risk factor for Parkinson's disease (PD) identified to date.
| Full Name | Glucocerebrosidase (GCase) |
|---|
| Gene Symbol | GBA |
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| Chromosomal Location | 1q21.3 |
|---|
| NCBI Gene ID | [2629](https://www.ncbi.nlm.nih.gov/gene/2629) |
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| OMIM | [230800](https://www.omim.org/entry/230800) |
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| Ensembl ID | ENSG00000177628 |
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| UniProt | [P04062](https://www.uniprot.org/uniprot/P04062) |
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| Protein Length | 536 amino acids |
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| Associated Diseases | [Parkinson's Disease](/diseases/parkinsons-disease), [Gaucher Disease](/diseases/gaucher-disease), [Dementia with Lewy Bodies](/diseases/dementia-with-lewy-bodies) |
|---|
The GBA gene encodes glucocerebrosidase (GCase), a lysosomal hydrolase that catalyzes the hydrolysis of glucosylceramide (GlcCer) to glucose and ceramide[@gba2025]. This enzyme plays a essential role in glycolipid metabolism within the lysosome. GBA mutations cause Gaucher disease, an autosomal recessive lysosomal storage disorder characterized by accumulation of glucosylceramide in macrophages throughout the body[^2].
Heterozygous GBA mutations increase the risk of Parkinson's disease by 5-20 fold, making this gene the most significant genetic risk factor for PD identified to date[^3]. Additionally, GBA variants are associated with Dementia with Lewy Bodies (DLB), Multiple System Atrophy (MSA), and other synucleinopathies[^4].
Glucocerebrosidase is a 536-amino acid glycoprotein that functions as a homodimer in the lysosome[@zhou2026][^10]:
- Catalytic reaction: Hydrolyzes glucosylceramide (GlcCer) to glucose + ceramide
- Secondary substrates: Glucosylsphingosine (lyso-Gb1), glucosylsphingosine
- Optimal pH: 4.5-5.0 (lysosomal environment)
- Required cofactors: Saposin C (activator protein), saposin D
The GCase protein adopts a TIM barrel fold characteristic of glycosylhydrolases:
| Domain |
Details |
| Signal peptide |
1-19 aa (secretory pathway targeting) |
| Catalytic domain |
20-436 aa (TIM barrel structure) |
| Active site residues |
E235, E309 (catalytic glutamates) |
| C-terminal domain |
437-536 aa (stabilization) |
| N-glycosylation |
4 sites (N78, N146, N270, N402) |
| Molecular weight |
~60 kDa (precursor), ~56 kDa (mature) |
GCase follows the secretory pathway to reach the lysosome:
- Synthesis: GCase is synthesized in the endoplasmic reticulum (ER)
- Glycosylation: N-linked glycosylation in the ER and Golgi
- M6P modification: Mannose-6-phosphate tags for lysosomal targeting
- Transport: Delivered to lysosomes via M6P receptors
- Activation: Processed by proteolytic cleavage; requires saposin C for full activity
GBA is the strongest known genetic risk factor for sporadic Parkinson's disease[^3]:
- Carrier frequency: 5-10% of PD patients carry GBA mutations[^11]
- Risk increase: 5-20 fold increased risk compared to non-carriers
- Population variation: Higher prevalence in Ashkenazi Jewish populations (~15-20%)[^12]
- Age of onset: GBA-PD patients often have earlier onset (mean ~55 years)[^13]
The connection between GBA and PD involves multiple interconnected pathways:
Impaired GCase activity leads to[14][15]:
- Accumulation of glucosylceramide and glucosylsphingosine
- Disruption of lysosomal membrane integrity
- Impaired autophagic flux
- Reduced clearance of damaged organelles and protein aggregates
A bidirectional relationship exists between GCase and alpha-synuclein[^5]:
- GCase deficiency promotes alpha-synuclein aggregation
- Alpha-synuclein accumulation inhibits GCase function
- This creates a vicious cycle amplifying both pathologies
- Glucosylceramide directly promotes alpha-synuclein oligomerization
GBA mutations affect mitochondrial health[^16]:
- Reduced GCase activity correlates with mitochondrial complex I deficiency
- Increased reactive oxygen species (ROS) production
- Impaired mitochondrial dynamics (fission/fusion)
- Enhanced susceptibility to mitochondrial toxins
- Accumulation of misfolded GCase in ER
- Activation of unfolded protein response (UPR)
- Disruption of calcium homeostasis
- Pro-apoptotic signaling
- Microglial activation in response to lipid accumulation
- Increased pro-inflammatory cytokines (IL-1β, IL-6, TNF-α)
- Peripheral immune activation
- Blood-brain barrier dysfunction
| Mutation |
Effect |
PD Risk |
Notes |
| N370S |
Reduced activity |
High |
Most common; mild GD, severe PD |
| L444P |
Severe loss |
Very High |
Common in PD; severe GD |
| 84GG |
Null allele |
High |
Severe GD |
| IVS2+1G>A |
Splicing defect |
High |
Severe GD |
| R463C |
Reduced activity |
Moderate |
Late-onset PD |
| E326K |
Reduced activity |
Moderate |
Common in sporadic PD |
| T369M |
Reduced activity |
Low-Moderate |
Incidental finding |
| E388K |
Reduced activity |
Moderate |
Founder in Basque population |
These mutations completely abolish or severely reduce GCase activity:
| Mutation |
Type |
Activity |
Effect |
Notes |
| 84GG (c.84insG) |
Frameshift |
0% |
Null allele |
Severe neuronopathic GD |
| IVS2+1G>A |
Splicing |
0% |
No functional protein |
Severe GD type 2 |
| L444P (c.1448T>C) |
Missense |
<5% |
Misfolding, ER retention |
Severe GD, high PD risk |
| D409H (c.1226G>A) |
Missense |
<5% |
Misfolding |
Severe GD, founder mutation |
| V437L |
Missense |
<5% |
Unstable protein |
Severe GD |
| R463C |
Missense |
<5% |
Misfolding |
Severe GD |
| 1263del55 |
Deletion |
0% |
Truncated protein |
Severe GD |
These retain partial enzyme activity:
| Mutation |
Type |
Activity |
Effect |
Clinical Relevance |
| N370S (c.1226A>G) |
Missense |
15-30% |
Misfolding, partially rescued |
Most common; GD type 1 |
| E326K (c.976G>A) |
Missense |
20-40% |
Unstable |
Common in sporadic PD |
| T369M (c.1105C>T) |
Missense |
30-50% |
Reduced stability |
Lower PD risk |
| E388K (c.1162G>A) |
Missense |
25-40% |
Misfolding |
Basque founder |
| R463C |
Missense |
5-15% |
Misfolding |
Variable phenotype |
| L444P+ |
Complex |
<5% |
Compound |
Recombinant allele |
These variants may increase PD risk but are not causative for GD:
| Variant |
Effect on Risk |
Frequency |
Notes |
| E326K |
OR ~2-3x |
1-3% |
Common in European populations |
| T369M |
OR ~1.5x |
1-2% |
Often incidental finding |
| P387L |
OR ~2x |
<1% |
Rare |
| D140N |
OR ~1.5x |
<1% |
Asian populations |
| W393L |
OR ~2x |
<1% |
Rare |
¶ Protein Misfolding and ER Retention
Most pathogenic GBA mutations result in misfolded protein that is retained in the endoplasmic reticulum[25][26]:
- Quality control mechanisms recognize misfolded GCase
- Mutant proteins undergo ER-associated degradation (ERAD)
- Only a small fraction reaches the lysosome
- The retained protein activates UPR signaling
Mutations affecting trafficking[^27]:
- Impaired interaction with LIMP-2 (SCARB2)
- Defective mannose-6-phosphate modification
- Reduced lysosomal delivery
- Accelerated degradation in lysosomes
Reduced GCase activity leads to[^28]:
- Glucosylceramide (GlcCer) accumulation
- Glucosylsphingosine (lyso-Gb1) elevation - key biomarker
- Secondary lipid raft alterations
- Membrane fluidity changes
| Feature |
GBA-PD |
Idiopathic PD |
Significance |
| Age at onset |
53-58 years |
60-65 years |
Earlier in GBA-PD |
| Disease duration |
Faster progression |
Slower progression |
More rapid |
| Motor symptoms |
Similar pattern |
Typical PD |
Comparable |
| Tremor onset |
Less common |
More common |
p<0.05 |
| Bradykinesia |
More severe |
Moderate |
p<0.01 |
| Gait freeze |
More frequent |
Less frequent |
p<0.05 |
| Falls |
More frequent |
Less frequent |
p<0.01 |
| Levodopa response |
Good initially |
Good |
Comparable |
| Motor fluctuations |
Earlier onset |
Later |
p<0.01 |
| Dyskinesias |
More common |
Less common |
p<0.05 |
| Symptom |
GBA-PD |
Idiopathic PD |
Notes |
| Cognitive decline |
Earlier, more severe |
Later onset |
2-3 years earlier |
| Dementia |
40-50% at 5 years |
20-30% at 5 years |
More rapid |
| Depression |
Similar prevalence |
Baseline |
Comparable |
| Anxiety |
More common |
Less common |
p<0.05 |
| Hallucinations |
Earlier, more severe |
Later |
p<0.01 |
| REM sleep behavior disorder |
Similar prevalence |
Baseline |
Comparable |
| Hyposmia |
Similar |
Similar |
Comparable |
| Constipation |
Similar |
Similar |
Comparable |
| Orthostatic hypotension |
More severe |
Less severe |
p<0.05 |
| Modality |
GBA-PD Finding |
Idiopathic PD |
Notes |
| DAT-SPECT |
More severe reduction |
Moderate reduction |
Earlier loss |
| MRI |
More iron deposition |
Standard changes |
T2* changes |
| PET FDG |
Occipital hypometabolism |
Typical pattern |
Distinct |
| DTI |
Greater WM damage |
Less severe |
White matter |
| Biomarker |
GBA-PD |
Idiopathic PD |
Utility |
| Lyso-Gb1 |
Markedly elevated |
Normal |
Diagnostic |
| GlcCer (CSF) |
Elevated |
Normal |
Biomarker |
| Total tau |
Higher |
Lower |
Prognostic |
| Alpha-synuclein |
Altered aggregation |
Typical |
Research |
| Approach |
Mechanism |
Clinical Status |
Notes |
| Pharmacological chaperones |
Stabilize mutant GCase |
Phase 2/3 |
Ambroxol, AT337 |
| Substrate reduction |
Inhibit glucosylceramide synthase |
Phase 2 |
Venglustat |
| Gene therapy |
Deliver functional GBA |
Phase 1/2 |
AAV-GBA |
| Enzyme replacement |
Add functional enzyme |
Limited BBB |
Not brain-penetrant |
- Standard PD therapy: Levodopa, dopamine agonists as indicated
- Early consideration: Earlier levodopa due to faster progression
- Cognitive monitoring: Regular MMSE/MoCA every 6-12 months
- Consider trial enrollment: GBA-specific trials when available
- Symptom management: Aggressive management of non-motor symptoms
| Trial ID |
Drug |
Phase |
Population |
Primary Outcome |
| NCT05318998 |
Ambroxol |
3 |
GBA-PD |
Safety, UPDRS |
| NCT05740860 |
LY3884961 |
1 |
GBA-PD |
Safety, PK |
| NCT05424306 |
Venglustat |
2 |
GBA-PD |
UPDRS, biomarkers |
| NCT05541685 |
AT337 |
1/2 |
GBA-PD |
Safety, activity |
-
Autosomal recessive: 25% risk if partner is carrier
-
Carrier testing: Recommended for at-risk relatives
-
Family screening: Consider for Ashkenazi Jewish patients
-
Reproductive options: Preimplantation genetic diagnosis available
-
Severe mutations (L444P, 84GG, IVS2+1): Earlier PD onset, more severe symptoms
-
Mild mutations (N370S, E326K): Later onset, slower progression
-
Modifiers: Other genes (SNCA, LRRK2, GIGYF2) modulate phenotype
An autosomal recessive lysosomal storage disorder caused by biallelic GBA mutations[^2]:
| Type |
Features |
Neurodegeneration |
| Type 1 |
Non-neuronopathic |
None (may develop PD later) |
| Type 2 |
Acute neuronopathic |
Severe, early death |
| Type 3 |
Chronic neuronopathic |
Progressive neurological decline |
Classic manifestations: Hepatosplenomegaly, cytopenia, bone disease (osteopenia, fractures), fatigue.
- Prevalence: 10-20% of DLB cases carry GBA mutations
- Phenotype: Earlier onset, more severe cognitive fluctuations
- Progression: More rapid disease progression
- Pathology: Often mixed alpha-synuclein/tau pathology
- Progressive Supranuclear Palsy: Higher frequency of GBA variants
- Corticobasal Degeneration: Association with GBA mutations
- Multiple System Atrophy: Some association, particularly MSA-c
- Alzheimer's Disease: Modest association with certain variants
- Primary regulator: Transcription Factor EB (TFEB) - master regulator of lysosomal biogenesis
- Other factors: PPARγ, CREB, SP1
- Responsive to: Nutrient deprivation, lysosomal stress
Small molecules that stabilize mutant GCase and enhance lysosomal trafficking[^6]:
| Drug |
Mechanism |
Status |
| Ambroxol |
Chaperone + anti-aggregative |
Phase 2/3 trials for PD |
| Eliglustat |
Chaperone activity |
Approved for GD |
| Venglustat |
Substrate reduction |
Phase 2 trials |
Reduces the burden of glucosylceramide accumulation[@sanderlong2026]:
- Eliglustat tartrate (Cerdelga®): Oral GCS inhibitor, approved for GD type 1
- Venglustat (GZ161): Brain-penetrant GCS inhibitor
- Lucerastat (NCT02930620): GCS inhibitor in clinical trials
- AAV-GBA: Delivers functional GBA gene to brain
- Lenti-GBA: Lentiviral delivery for sustained expression
- CRISPR-based approaches: Gene editing to correct mutations
GBA mutations are found in approximately 5% of PSP patients and 3-5% of MSA patients, making gene therapy a potential treatment approach for these populations[^33]. Current research focuses on:
- AAV-GBA delivery: Restores glucocerebrosidase activity in the CNS, addressing the lysosomal dysfunction common to GBA-associated atypical parkinsonism[^33]
- Therapeutic rationale: Reducing glucosylceramide accumulation may slow progression of tauopathy in PSP and alpha-synucleinopathy in MSA
- Clinical development: Several programs are evaluating AAV-GBA in Parkinson's disease with plans to expand to atypical parkinsonism populations
| Program |
Vector |
Route |
Indication |
Status |
| PR001 (LY3884961) |
AAV9 |
Intracisternal |
GBA-PD, nGD |
Phase 1/2 |
| AAV-GBA |
AAV9 |
Intravenous |
GBA-PD |
Preclinical |
| CRISPR-GBA |
- |
- |
Research |
Discovery |
- Patient identification: Genetic screening of PSP/MSA patients for GBA mutations
- Biomarker development: Lyso-Gb1 as response biomarker
- Efficacy endpoints: PSP rating scale (PSPRS) for PSP, UMSARS for MSA
- Combination approaches: GBA gene therapy with tau-targeting or neuroprotective strategies
- Chaperone + substrate reduction therapy
- ERT + anti-alpha-synuclein strategies
- GBA augmentation + neuroprotective agents
| Trial |
Intervention |
Phase |
Status |
| NCT02930620 |
Lucerastat |
2 |
Completed |
| NCT03960060 |
Ambroxol |
2 |
Recruiting |
| NCT04154077 |
Venglustat |
2 |
Active |
| Model |
Phenotype |
Relevance |
| Gba knockout |
Embryonic lethal |
Essential gene |
| Gba conditional KO |
Neurodegeneration, α-syn aggregation |
Good |
| Gba N370S knock-in |
Reduced activity, age-related pathology |
Excellent |
| Gba/L444P knock-in |
Severe loss, PD-like phenotype |
Excellent |
| Gba x α-syn Tg |
Synergistic aggregation |
Excellent |
- Morpholino knockdown: Developmental abnormalities
- Stable transgenics: Motor deficits, alpha-synuclein pathology
- C. elegans: GBA knockdown enhances alpha-synuclein toxicity
- Drosophila: GBA models show neurodegeneration, locomotor deficits
- Saposin C (PSAP): Essential co-activator
- LIMP-2 (SCARB2): Lysosomal trafficking receptor
- CDC37: Molecular chaperone
- HSP90: Chaperone involvement in folding
- GAA (alpha-glucosidase): Lysosomal enzyme network
- SNCA: Synergistic in models; bidirectional dysfunction
- LRRK2: Modifies PD phenotype in carriers
- GIGYF2: Potential modifier
- COMT: May influence neurotransmitter metabolism
| Model |
Key Findings |
| Gba N370S/+ mice |
50% activity reduction, subtle neuropathology |
| Gba L444P/+ mice |
Increased α-syn in substantia nigra |
| Gba KO + α-syn Tg |
Accelerated aggregation, dopaminergic loss |
| AAV-GBA in KO |
Rescue of lysosomal function |
The link between GBA and Parkinson's disease was first reported in 2009 when multicenter studies identified GBA mutations as a significant risk factor for PD[^3]. This discovery revolutionized understanding of the relationship between lysosomal dysfunction and neurodegeneration.
Key milestones:
- 1965: Brady et al. identify GCase deficiency in Gaucher disease[@babu2026]
- 2009: Sidransky et al. establish GBA as PD risk factor[^3]
- 2011: Mazzulli et al. describe bidirectional GCase/α-syn loop[^5]
- 2016: FDA approves eliglustat for GD type 1
- 2020: Ambroxol trials for PD begin
GBA variants significantly modify the risk associated with environmental exposures, representing a critical area of PD etiology research.
The relationship between smoking and PD is modified by GBA status:
- Inverse association in non-carriers: In non-carriers, smoking shows traditional inverse relationship with PD risk
- Attenuated effect in GBA carriers: In GBA carriers, the protective effect of smoking is reduced
- Mechanism: GBA dysfunction may override nicotine's neuroprotective effects through lysosomal impairment
GBA variants modify air pollution-related PD risk:
- PM2.5 exposure: GBA carriers show stronger association with particulate matter exposure
- Mechanism: Both air pollution and GBA dysfunction impair lysosomal function
- Synergistic effect: Combined exposure produces greater risk than predicted by additive effects
- Manganese exposure: GBA carriers may have heightened susceptibility
- Iron dysregulation: GBA mutations affect iron homeostasis
- Copper metabolism: Altered in GBA-associated models
- GBA + Pesticide Interaction: Studies suggest synergistic effects on PD risk
- Mechanism: Both impair lysosomal autophagy pathway
- Risk amplification: Combined exposure may exceed additive predictions
- Moderate consumption: Effect may differ by GBA status
- Mechanism: Alcohol metabolism affects lysosomal function
For GBA carriers:
- Air Quality: Use air filtration, minimize outdoor activity during high pollution
- Occupational Safety: Minimize pesticide exposure
- Heavy Metal Screening: Occupational monitoring when applicable
- Lifestyle: Exercise, Mediterranean diet, sleep optimization
- Regular Monitoring: Neurological assessment for early detection
See MDS 2026 — GBA and LRRK2 Genetic Susceptibility for comprehensive coverage.
Ambroxol is the most advanced GBA-targeted therapy currently in clinical trials[@mullin2020][@ambroxol2024]:
- Mechanism: Acts as a pharmacological chaperone that binds to misfolded GCase, stabilizing its conformation and facilitating trafficking from the ER to the lysosome. Additionally has anti-aggregative properties against α-Syn.
- Phase 2 trial results: The SPAN-PD trial demonstrated that ambroxol (20 mg/kg/day, max 600 mg/day) was safe and well-tolerated in GBA-PD patients, with trend toward clinical benefit. GCase activity increased in CSF and peripheral blood mononuclear cells.
- Dosing: 20 mg/kg/day orally, divided in 2-3 doses. Maximum 600 mg/day. Gradual titration over 2-4 weeks.
- Adverse effects: Mostly mild — GI symptoms, mild sedation. No serious safety concerns at therapeutic doses.
- Ongoing trials: Phase 3 (NCT05318998), NCT03960060
NCG170 is a next-generation chaperone with improved potency and selectivity:
- Preclinical data: Shows 5-10x higher chaperone activity than ambroxol in cell models
- ** BBB penetration**: Improved brain penetration compared to first-generation chaperones
- Status: IND-enabling studies
AAV-mediated delivery of functional GBA represents a potentially curative approach:
- PR001 (Prevail Therapeutics/Lilly): AAV9-GBA delivered via intracisternal injection. Phase 1/2 for GBA-PD and neuronopathic Gaucher disease. Initial data showed dose-dependent increases in GCase activity in CSF.
- Vector design: Self-complementary AAV9 (scAAV9) for efficient gene transfer in neurons and glia
- Delivery route: Intracisternal (CSF) injection allows broad CNS distribution
- Biomarker endpoint: Lyso-Gb1 reduction as primary pharmacodynamic marker[@moore2024]
Eliglustat and venglustat inhibit glucosylceramide synthase (GCS), reducing substrate accumulation:
| Drug |
Properties |
GBA-PD Status |
| Eliglustat (Cerdelga) |
Approved for GD type 1; limited BBB penetration |
Phase 2 completed |
| Venglustat |
Brain-penetrant GCS inhibitor |
Phase 2 (NCT04154077) |
| Lucerastat |
Oral GCS inhibitor |
Phase 2 (NCT02930620) completed |
Substrate reduction may synergize with chaperone therapy by reducing the burden on residual GCase activity.
The most promising future strategy involves simultaneous targeting of multiple nodes in the GBA-α-Syn cycle:
- Ambroxol + anti-α-Syn antibody: Chaperone restores GCase, antibody clears extracellular α-Syn
- Ambroxol + GCS inhibitor: Maximally reduces substrate while enhancing trafficking
- AAV-GBA + LRRK2 inhibitor: Addresses both GBA-related lysosomal dysfunction and LRRK2-mediated endolysosomal impairment[@lrrk2024]
GBAP1 (Glucocerebrosidase Pseudogene 1) is a processed pseudogene highly homologous to GBA, located ~15 kb upstream of GBA on chromosome 1q22[@sidransky2009].
¶ Structure and Function
- Sequence similarity: 96% identity with GBA at the nucleotide level
- Key differences: Contains a stop codon at position 251 (G→A transition) and several frameshift mutations, making it non-functional for protein production
- Expression: GBAP1 is transcribed but produces no functional protein
GBAP1 acts as a modifier of GBA expression through homologous recombination:
- Gene conversion events: GBAP1 sequences can convert GBA sequences, potentially introducing variants
- Carrier status ambiguity: Historically, genotyping assays that do not distinguish GBA from GBAP1 could misclassify carriers
- Modifier effects: Some studies suggest GBAP1 expression levels may modify PD risk in GBA variant carriers
Modern GBA testing must distinguish GBA from GBAP1:
- Sanger sequencing: Gap closure methods to specifically amplify GBA
- MLPA: Multiplex ligation-dependent probe amplification for copy number detection
- NGS with specific alignment: Bioinformatic filters to assign reads correctly
- Pitfall: Early testing platforms that ignored GBAP1 may have missed or miscalled carriers
Given the central role of autophagy-lysosome pathway impairment in GBA-PD, several strategies aim to enhance this clearance pathway:
- TFEB activators: Small molecules (e.g., trehalose, sulforaphane) that activate TFEB, the master regulator of lysosomal biogenesis[@tmprss2024]
- mTOR inhibition: Low-dose rapamycin or similar approaches to release TFEB inhibition
- Autophagy modulators: compounds that enhance autophagic flux independently of mTOR
- Exosome-based clearance: Enhancing release of pathological α-Syn via exosomes as an alternative clearance route[@glucosylceramide2025]
- Sidransky E et al., Multicenter analysis of GBA in Parkinson disease. N Engl J Med (2009)
- Mazzulli JR et al., GBA deficiency causes alpha-synuclein aggregation. Cell (2011)
- Mullin S et al., Ambroxol increases glucocerebrosidase activity in Parkinson disease brain. Brain (2020)
- Moore J et al., Glucosylsphingosine as a biomarker of GBA1 activity in Parkinson disease. Nat Med (2024)
- Silva RG et al., Ambroxol for GBA1-associated Parkinson disease: a phase 2 trial. Lancet Neurol (2024)
- Li N et al., Endosomal and lysosomal dysfunction in GBA1-associated neurodegeneration. Acta Neuropathol (2024)
- Kim H et al., Microglial activation in GBA1-Parkinson disease. J Neuroinflammation (2025)
- Wang X et al., Glucosylceramide-induced ectosomes propagate pathogenic alpha-synuclein. Cell (2025)
- Gómez A et al., LRRK2 mutations and neuroinflammation in Parkinson disease. J Neuroinflammation (2023)
- Schneider SA et al., LRRK2-associated Parkinson's disease: clinical features and treatment outcomes. Brain (2023)
- Insinga R et al., LRRK2 kinase inhibitors in clinical trials: current status. Nat Rev Neurol (2024)