First high-resolution structure of HGSNAT-acetyl-CoA complex, that describes the architecture of a novel transmembrane N-acetyltransferase fold and provides a molecular basis for MPS IIIC causing mutation induced destabilization of HGSNAT.

4-sulfation at the non-reducing end of chondroitin sulfate glycosaminoglycan chains is essential for inhibition of axonal growth.

Lysosomes are highly enriched in chloride, which is essential for their degradative function.

Mutations affecting a nuclear encoded metalloprotease cause of a new form of mitochondriopathy, highlighting the importance of this protease for mitochondrial function in humans.

4,6-Sulfation of chondroitin sulfate proteoglycans prevents sympathetic nerve regeneration into the infarct after myocardial ischemia/reperfusion, and reducing this sulfation promotes nerve regeneration and decreases arrhythmia susceptibility.

Genetic analysis of a CLN4 Drosophila model suggests that the disease-causing alleles act as dominant gain of function mutations that cause CSPα oligomerization and impair secretory and prelysosomal trafficking.