Bert Houben

This study shows human macrophages and microglia actively produce Aβ42 fibrils, which seed amyloid plaques and tau aggregation, and this process is influenced by genetic factors like TREM2.

This study introduces FoldDelay, a metric quantifying protein folding delays during translation, showing its correlation with misfolding and aggregation risks.

This study shows N-glycosylation prevents protein aggregation by steric hindrance, especially in proteins prone to misfolding, using computational and biochemical analyses.

This study shows heterotypic interactions between Aβ APRs and homologous protein segments accelerate Aβ assembly, alter fibril morphology, and are enriched in AD plaques but not in mouse models.

The paper identifies MOAG-4/SERF as modifiers of amyloid formation through charge complementation, showing that charge interactions drive protein aggregation and toxicity.