Dominic C. M. Ng

This study uses middle-down phosphoproteomics to analyze how protein partitioning into biomolecular condensates changes under proteostatic stress, revealing phosphorylation-dependent and independent mechanisms.

The paper develops an mPBA enrichment workflow to analyze N-glycoproteome remodeling under ER stress, revealing dynamic changes in glycosylation sites and glycoforms.

The paper identifies widespread isoform usage shifts in fetal and postnatal mouse hearts using proteome-wide ratio quantification, revealing novel isoform switches and evolutionary patterns.

This study uses deuterium labeling to analyze protein turnover kinetics in hiPSCs and identifies fast-turnover proteins involved in cell division and differentiation.

This paper introduces a method to improve protein turnover rate calculation using heavy water labeling and mass spectrometry, increasing coverage of well-fitted peptides by 25-82% in mouse organ proteomes.