A chloroacetamidine-based inactivator of protein arginine methyltransferase 1: Design, synthesis, and in vitro and in vivo evaluation

  • Obiamaka Obianyo
  • , Corey P. Causey
  • , Tanesha C. Osborne
  • , Justin E. Jones
  • , Young-Ho Lee
  • , Michael R. Stallcup
  • , Paul R. Thompson

Research output: Contribution to journalArticlepeer-review

41 Scopus citations
4 Downloads (Pure)

Abstract

(Chemical Equation Presented) Protein arginine methyltransferases (PRMTs) catalyze the post-translational methylation of arginine residues. PRMT1 is the predominant mammalian isozyme and is responsible for generating the majority of the asymmetrically dimethylated arginine found in vivo. Herein, we describe the most potent PRMT1 inhibitor, C21, described to date.

Original languageEnglish
Pages (from-to)1219-1223
Number of pages5
JournalChemBioChem
Volume11
Issue number9
DOIs
StatePublished - Jun 14 2010

Scopus Subject Areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Organic Chemistry

Keywords

  • Cl-amidine
  • Enzymes
  • Inhibitors
  • Protein arginine methyltransferase
  • Transcription

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