Ontology highlight
ABSTRACT:
SUBMITTER: Wohlschlegel JA
PROVIDER: S-EPMC2535609 | biostudies-literature | 2006 Apr
REPOSITORIES: biostudies-literature
Wohlschlegel James A JA Johnson Erica S ES Reed Steven I SI Yates John R JR
Journal of proteome research 20060401 4
A growing number of biological processes have been found to be regulated by the covalent attachment of the ubiquitin-like protein SUMO to key cellular targets. A critical step in the process of analyzing the role of SUMO in regulating the activity of these proteins is the identification of the lysine residues that are targeted by this modification. Unfortunately, current methods aimed at mapping these attachment-sites are laborious and often ineffective. We report here the development of a platf ...[more]