Ontology highlight
ABSTRACT:
SUBMITTER: Albuquerque CP
PROVIDER: S-EPMC4669148 | biostudies-literature | 2015
REPOSITORIES: biostudies-literature
Albuquerque Claudio P CP Yeung Eyan E Ma Shawn S Fu Ting T Corbett Kevin D KD Zhou Huilin H
PloS one 20151203 12
A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes. A major barrier to understanding the diverse regulatory roles of SUMO has been a lack of suitable methods to identify protein sumoylation sites. Here we developed a mass-spectrometry (MS) based approach combining chemical and enzymatic modificat ...[more]