T. Sinnige

Islet amyloid polypeptide tagged with green fluorescent protein localises to mitochondria and forms filamentous aggregates in Caenorhabditis elegans

This study shows IAPP-GFP localizes to mitochondria and forms filamentous aggregates in C. elegans, suggesting potential as a tool for screening IAPP-solubilizing compounds for T2D therapy.

Fibril elongation by human islet amyloid polypeptide is the main event linking aggregation to membrane damage

This study investigates how hIAPP aggregation relates to membrane damage, finding that fibril elongation, not oligomers, is the main cause of vesicle leakage.

Membrane-catalyzed aggregation of islet amyloid polypeptide is dominated by secondary nucleation

This study investigates IAPP aggregation on lipid membranes, finding that secondary nucleation dominates the process, with anionic lipids promoting both primary and secondary nucleation but not elongation.

Kinetic analysis reveals the rates and mechanisms of protein aggregation in a multicellular organism

This study quantitatively models protein aggregation in C. elegans using a molecular framework, showing that nucleation rates and stochasticity drive aggregation in vivo, consistent with in vitro findings.

Fast fluorescence lifetime imaging reveals the aggregation processes of α-synuclein and polyglutamine in aging Caenorhabditis elegans

This study uses fast TG-FLIM to analyze α-synuclein and polyglutamine aggregation in aging C. elegans, revealing differences in their aggregation kinetics and amyloid-like features.

Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans

This study shows that age-dependent protein aggregation in C. elegans forms amyloid-like structures and accelerates tissue functional decline, suggesting a role for protein aggregation in aging.