Ontology highlight
ABSTRACT:
SUBMITTER: Selvi BR
PROVIDER: S-EPMC2844164 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Selvi B Ruthrotha BR Batta Kiran K Kishore A Hari AH Mantelingu Kempegowda K Varier Radhika A RA Balasubramanyam Karanam K Pradhan Suman Kalyan SK Dasgupta Dipak D Sriram Sokalingam S Agrawal Shipra S Kundu Tapas K TK
The Journal of biological chemistry 20091217 10
Methylation of the arginine residues of histones by methyltransferases has important consequences for chromatin structure and gene regulation; however, the molecular mechanism(s) of methyltransferase regulation is still unclear, as is the biological significance of methylation at particular arginine residues. Here, we report a novel specific inhibitor of coactivator-associated arginine methyltransferase 1 (CARM1; also known as PRMT4) that selectively inhibits methylation at arginine 17 of histon ...[more]