Ontology highlight
ABSTRACT:
SUBMITTER: Bonday ZQ
PROVIDER: S-EPMC6047023 | biostudies-literature | 2018 Jul
REPOSITORIES: biostudies-literature
Bonday Zahid Q ZQ Cortez Guillermo S GS Grogan Michael J MJ Antonysamy Stephen S Weichert Ken K Bocchinfuso Wayne P WP Li Fengling F Kennedy Steven S Li Binghui B Mader Mary M MM Arrowsmith Cheryl H CH Brown Peter J PJ Eram Mohammad S MS Szewczyk Magdalena M MM Barsyte-Lovejoy Dalia D Vedadi Masoud M Guccione Ernesto E Campbell Robert M RM
ACS medicinal chemistry letters 20180423 7
Protein arginine methyltransferase 5 (PRMT5) is a type II arginine methyltransferase that catalyzes the formation of symmetric dimethylarginine in a number of nuclear and cytoplasmic proteins. Although the cellular functions of PRMT5 have not been fully unraveled, it has been implicated in a number of cellular processes like RNA processing, signal transduction, and transcriptional regulation. PRMT5 is ubiquitously expressed in most tissues and its expression has been shown to be elevated in seve ...[more]