Ontology highlight
ABSTRACT:
SUBMITTER: Nakayasu ES
PROVIDER: S-EPMC4561012 | biostudies-literature | 2015 Sep
REPOSITORIES: biostudies-literature
Nakayasu Ernesto S ES Sydor Michael A MA Brown Roslyn N RN Sontag Ryan L RL Sobreira Tiago J P TJ Slysz Gordon W GW Humphrys Daniel R DR Skarina Tatiana T Onoprienko Olena O Di Leo Rosa R Deatherage Kaiser Brooke L BL Li Jie J Ansong Charles C Cambronne Eric D ED Smith Richard D RD Savchenko Alexei A Adkins Joshua N JN
Journal of proteome research 20150806 9
Ubiquitination is a key protein post-translational modification that regulates many important cellular pathways and whose levels are regulated by equilibrium between the activities of ubiquitin ligases and deubiquitinases. Here, we present a method to identify specific deubiquitinase substrates based on treatment of cell lysates with recombinant enzymes, immunoaffinity purification, and global quantitative proteomic analysis. As a model system to identify substrates, we used a virulence-related ...[more]