Ontology highlight
ABSTRACT:
SUBMITTER: Lattouf H
PROVIDER: S-EPMC6294691 | biostudies-literature | 2019 Feb
REPOSITORIES: biostudies-literature
Lattouf Hanine H Kassem Loay L Jacquemetton Julien J Choucair Ali A Poulard Coralie C Trédan Olivier O Corbo Laura L Diab-Assaf Mona M Hussein Nader N Treilleux Isabelle I Le Romancer Muriel M
International journal of cancer 20181031 3
Protein arginine methyltransferase 5 (PRMT5) is the main enzyme responsible for the symmetrical dimethylation of arginine residues on target proteins in both the cytoplasm and the nucleus. Though its activity has been associated with tumor progression in various cancers, the expression pattern of this oncoprotein has been scarcely studied in breast cancer. In the current work, we analyzed its expression in a large cohort of breast cancer patients, revealing higher nuclear PRMT5 levels in ERα-pos ...[more]