Ontology highlight
ABSTRACT:
SUBMITTER: Back S
PROVIDER: S-EPMC6465141 | biostudies-literature | 2019 Jan
REPOSITORIES: biostudies-literature
Back Songhee S Gorman Andrew W AW Vogel Christine C Silva Gustavo M GM
Journal of proteome research 20181210 1
During oxidative stress, K63-linked polyubiquitin chains modify a variety of proteins including ribosomes. Knowledge of the precise sites of K63 ubiquitin is key to understand its function during the response to stress. To identify the sites of K63 ubiquitin, we developed a new mass spectrometry based method that quantified >1100 K63 ubiquitination sites in yeast that responded to oxidative stress induced by H<sub>2</sub>O<sub>2</sub>. We determined that under stress, K63 ubiquitin-modified prot ...[more]