Paul T. Kotzbauer

The paper shows that injecting amplified Lewy body dementia fibrils into mice leads to fibril accumulation with LBD structure and neurodegeneration.

This study integrates parietal cortex transcriptomics with GWAS data to refine Parkinson's disease risk gene nominations and identify STAT3 as a potential upstream glial regulator.

The paper reports the high-resolution SSNMR structure of A30P mutant alpha-synuclein fibrils, showing a conserved Greek key fold not including the mutation site, and validates a method for comparing SSNMR spectra of Asyn polymorphs.

The paper identifies two dimethoxyphenyl piperazine analogs that inhibit alpha-synuclein fibril growth in vitro and from Lewy Body Disease brain tissue.

The paper classifies Alpha-synuclein fibril structures into two main polymorph classes using clustering and finds conserved motifs that could guide drug design.

The paper uses structural and chemical biology methods to show EX-6 binds selectively to α-synuclein fibrils in MSA tissue, with a 10-fold preference over PD tissue.

This study shows that TDP-43 aggregate seeds persist in both mouse and human skeletal muscle even after the removal of large TDP-43 inclusions.

This study determines the atomic structure of alpha-synuclein fibrils from Lewy body dementia tissue using a novel amplification method and solid-state NMR.

This study identifies VCP as a suppressor of proteopathic seeding and shows that VCP dysfunction increases seeding of multiple aggregates, contributing to neurodegeneration.

The paper uses GWAS, PRS, and MR to show a genetic link between Parkinson's disease and CSF Aβ42 and APOE locus.

This study identifies TDP-43 oligomers as early intermediates in aggregation, showing ALS-linked mutations accelerate this process and enhance aggregate propagation.