Ontology highlight
ABSTRACT:
SUBMITTER: Strieter ER
PROVIDER: S-EPMC4805399 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Strieter Eric R ER Korasick David A DA
ACS chemical biology 20120111 1
Protein ubiquitination, the covalent attachment of ubiquitin to target proteins, has emerged as one of the most prevalent posttranslational modifications (PTMs), regulating nearly every cellular pathway. The diversity of signaling associated with this particular PTM stems from the myriad ways in which a target protein can be modified by ubiquitin, e.g., monoubiquitin, multi-monoubiquitin, and polyubiquitin linkages. In this Review, we focus on developments in both enzymatic and chemical methods ...[more]