Poul Henning Jensen

The paper investigates the role of STING in Parkinson's disease by comparing motor behavior and brain pathology in STING-deficient and wild-type mice exposed to alpha-synuclein fibrils.

The paper investigates the role of oligodendroglial-derived extracellular vesicles in spreading pathology in MSA-like models, showing they carry pathological Synuclein and TPPP/p25 and induce disease in animal models.

The paper shows that LRRK2-mutant cases without Lewy bodies have abundant non-inclusion α-synuclein pathology detected by PLA, unlike Lewy body disease cases.

The paper introduces MJF-14 PLA, a proximity ligation assay for detecting non-inclusion alpha-synuclein aggregates with high specificity and sensitivity, showing pathology precedes Lewy body formation in Parkinson's disease.

The paper develops and validates new immunoassays for quantifying total, phospho-Ser129, and aggregated alpha-synuclein in mouse brain tissue.

The paper investigates how the antibody MJFR14-6-4-2 recognizes aggregated alpha-synuclein and shows that epitope masking and epitope concentration drive its selectivity for different aggregates.

This study uses spatial transcriptomics to analyze aSyn pathology in mice, revealing metabolic and circadian disruptions at different stages of disease progression.

This study induces alpha-Synuclein aggregation in the gigantocellular nuclei of transgenic mice to model prodromal Parkinson's disease and observe motor symptom progression.

The paper investigates the sex-dimorphic neuroprotective role of CD163 in a Parkinson's disease mouse model using CD163 knockout mice.

This study shows that PLK2 inhibition reduces soluble nuclear pS129 levels but not aggregated pS129 in synucleinopathy models.

The paper shows that α-synuclein pathology in Parkinson's disease activates the NRF2 anti-oxidant response, suggesting it could be a therapeutic target.

The paper demonstrates that alpha-synuclein aggregates spread interneuronally in an organotypic hippocampal slice model, independent of serine 129 phosphorylation.

This study investigates the long-term effects of PFE-360 treatment in an AAV-α-synuclein rat model to assess its potential as a LRRK2 inhibitor for Parkinson's disease.

This study stabilizes α-synuclein oligomers using formaldehyde, preserving their structure and function for use as biomarkers in Parkinson's disease research.