Jennifer R. Hryhorenko

This study introduces fMObB, a mass spectrometry method to measure free methionine oxidation in E. coli, revealing higher oxidation under stress and the role of methionine sulfoxide reductases.

This study identifies phosphorylation sites in the SIRT6 C-terminus that enhance PARP1 interaction and oxidative stress resistance, correlating with maximum lifespan in mammals.

This study uses structural proteomics to show that ubiquitination patterns differ between misfolded nascent proteins and mature proteins, influencing their degradation rates.

This study shows that formylation of initiator methionines enhances their enzymatic reduction and mitigates oxidation-related misprocessing.

The paper describes a method to enzymatically synthesize isotopically labeled hydrogen peroxide (H218O2) for use in mass spectrometry to accurately measure methionine oxidation levels.

This study introduces proteome birthdating to measure protein age and finds that ubiquitinated proteins are predominantly newly synthesized, with distinct age distributions across cellular pathways.

This paper introduces MObBa, a mass spectrometry method to quantify methionine oxidation by alkylating unoxidized methionines, enabling accurate measurement of oxidation levels in peptides and proteomes.

TRAIL quantifies protein and cell lifetimes across tissues, showing cell division drives non-selective turnover in proliferative tissues while physicochemical features influence turnover in non-proliferative tissues.

The paper measures protein turnover rates in fibroblasts from long-lived species and finds slower turnover correlates with longer lifespan and reduced ROS.