J. R. Hryhorenko

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.

This study uses mass spectrometry to measure how ribosome binding affects the folding stability of nascent polypeptides, finding that ribosome-induced stability changes depend on localized charge distributions.

This study introduces a method to measure methionine oxidation in mouse brains and finds that oxidation is consistent across individuals but not significantly altered with age.

The paper shows that oxidation rates of buried methionines correlate with protein folding stability, using E. coli and T. thermophilus proteomes to demonstrate this relationship.

This study develops a method to quantify methionine oxidation in the human proteome by isotopic labeling and validates it using artificial proteomes, identifying novel in vivo oxidation sites.

This study quantifies how prion infection affects protein degradation rates in N2a cells, finding increased degradation kinetics for most proteins and reduced prion protein degradation.

The paper quantifies protein folding stabilities in human cell extracts using methionine oxidation rates, identifying stable ontological subsets and showing stability impacts oxidation and TMAO effects.