Ontology highlight
ABSTRACT:
SUBMITTER: Hendriks IA
PROVIDER: S-EPMC4490555 | biostudies-literature | 2015 Jun
REPOSITORIES: biostudies-literature
Hendriks Ivo A IA D'Souza Rochelle C RC Chang Jer-Gung JG Mann Matthias M Vertegaal Alfred C O AC
Nature communications 20150615
SUMOylation is a reversible post-translational modification (PTM) regulating all nuclear processes. Identification of SUMOylation sites by mass spectrometry (MS) has been hampered by bulky tryptic fragments, which thus far necessitated the use of mutated SUMO. Here we present a SUMO-specific protease-based methodology which circumvents this problem, dubbed Protease-Reliant Identification of SUMO Modification (PRISM). PRISM allows for detection of SUMOylated proteins as well as identification of ...[more]