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Effects of a novel arginine methyltransferase inhibitor on T-helper cell cytokine production

Academic Article
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Overview

authors

  • Bonham, K.
  • Hemmers, S.
  • Lim, Y. H.
  • Hill, D. M.
  • Finn, M.G.
  • Mowen, Kerri

publication date

  • May 2010

journal

  • FEBS Journal  Journal

abstract

  • The protein arginine methyltransferase (PRMT) family of enzymes catalyzes the transfer of methyl groups from S-adenosylmethionine to the guanidino nitrogen atom of peptidylarginine to form monomethylarginine or dimethylarginine. We created several less polar analogs of the specific PRMT inhibitor arginine methylation inhibitor-1, and one such compound was found to have improved PRMT inhibitory activity over the parent molecule. The newly identified PRMT inhibitor modulated T-helper-cell function and thus may serve as a lead for further inhibitors useful for the treatment of immune-mediated disease.

subject areas

  • Animals
  • Cell Proliferation
  • Cells, Cultured
  • Enzyme Inhibitors
  • Histones
  • Humans
  • Interferon-gamma
  • Interleukin-4
  • Methylation
  • Mice
  • Mice, Inbred BALB C
  • Molecular Structure
  • Promoter Regions, Genetic
  • Protein-Arginine N-Methyltransferases
  • Structure-Activity Relationship
  • T-Lymphocytes, Helper-Inducer
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Research

keywords

  • T-helper cell
  • cytokines
  • inhibitors
  • nuclear factor of activated T cells interacting protein 45 kDa (NIP45)
  • protein arginine methyltransferase
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Identity

PubMed Central ID

  • PMC2903848

International Standard Serial Number (ISSN)

  • 1742-464X

Digital Object Identifier (DOI)

  • 10.1111/j.1742-4658.2010.07623.x

PubMed ID

  • 20345902
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Additional Document Info

start page

  • 2096

end page

  • 2108

volume

  • 277

issue

  • 9

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