Brian C. Kraemer

TMEM106B C-Terminal fragment aggregation exacerbates α-synuclein and TDP-43 proteinopathy phenotypes.

This study shows TMEM106B C-terminal fragment aggregation synergizes with α-synuclein and TDP-43 to worsen neurodegeneration in C. elegans, but not with tau.

Design of readers for pathological PTM proteoforms in Alzheimer's disease

The paper designs and validates protein readers that specifically detect disease-related modifications in Tau and Abeta in Alzheimer's disease models and human samples.

Dominant α-tubulin mutations rescue tauopathy neurodegenerative phenotypes in C. elegans

This study identifies tubulin gene mutations that rescue tauopathy phenotypes in C. elegans by altering microtubule properties rather than directly affecting tau protein levels or aggregation.

Probing tau citrullination in Alzheimer's disease brains and mouse models of tauopathy

The paper identifies citrullination of tau as a novel posttranslational modification in Alzheimer's disease and tauopathy models, showing its association with disease progression.

TMEM106B C-terminal fragments aggregate and drive neurodegenerative proteinopathy.

This study identifies TMEM106B C-terminal fragments as aggregating proteins linked to neurodegenerative diseases and shows their toxic effects in a C. elegans model.