Tag: Enzyme Kinetics and Mechanisms

Regulation of Mutant Huntingtin Mitochondrial Toxicity by Phosphomimetic Mutations within Its N-Terminal Region

Huntington’s disease (HD), a neurodegenerative disease, affects approximately 30,000 people in the United States, with 200,000 more at risk. Mitochondrial dysfunction caused by mutant huntingtin (mHTT) drives early HD pathophysiology. mHTT binds the translocase of the mitochondrial inner membrane (TIM23) complex, inhibiting mitochondrial protein import and altering the mitochondrial proteome. The 17 aa HTT N-terminal sequence… Continue reading Regulation of Mutant Huntingtin Mitochondrial Toxicity by Phosphomimetic Mutations within Its N-Terminal Region

Small molecule targeted protein degradation via the UPS: venturing beyond E3 substrate receptors

The ubiquitin proteasome system (UPS) has been successfully hi-jacked by both bifunctional and monovalent small molecules to affect the degradation of proteins that were once considered undruggable. This field has primarily focused on the targeted recruitment of proteins to substrate receptors on E3 ubiquitin ligases, which are only one part of the UPS. More recently,… Continue reading Small molecule targeted protein degradation via the UPS: venturing beyond E3 substrate receptors

Low-cost synthesis of pearlescent pigments achieved using vanadium phosphates

Thanks to their special iridescence and unmatched beauty, pearls have been highly sought after throughout history. Due to their rarity and demand, the development of pearlescent pigments to mimic the natural beauty of a true pearl became inevitable. Here, researchers utilize plate-like particles to create substrate-free pearlescent pigments, a low-cost and straightforward solution to the… Continue reading Low-cost synthesis of pearlescent pigments achieved using vanadium phosphates

Protein ligation for the assembly and study of nonribosomal peptide synthetase megaenzymes

Nonribosomal peptide synthetases (NRPSs) are biosynthetic enzymes found in bacteria and fungi, that synthesize a plethora of pharmaceutically relevant compounds. NRPSs consist of repeating sets of functional domains called modules, and each module is responsible for the incorporation of a single amino acid to the growing peptidyl intermediate. The synthetic logic of an NRPS resembles… Continue reading Protein ligation for the assembly and study of nonribosomal peptide synthetase megaenzymes