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A combinatorial approach to characterize the substrate specificity of protein arginine methyltransferase 1

Academic Article
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Overview

authors

  • Bicker, K. L.
  • Obianyo, O.
  • Rust, H. L.
  • Thompson, Paul

publication date

  • 2011

journal

  • Molecular Biosystems  Journal

abstract

  • The dysregulation of protein arginine methyltransferases (PRMTs) is implicated in a wide variety of disease states. Here we report the design, synthesis, and screening of a combinatorial peptide library used to characterize the substrate specificity of PRMT1. The information gained from this approach was used to develop a PRMT1 inhibitor with enhanced selectivity.

subject areas

  • Amino Acid Sequence
  • Enzyme Inhibitors
  • Humans
  • Molecular Sequence Data
  • Peptide Library
  • Protein-Arginine N-Methyltransferases
  • Substrate Specificity
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Identity

PubMed Central ID

  • PMC2999663

International Standard Serial Number (ISSN)

  • 1742-206X

Digital Object Identifier (DOI)

  • 10.1039/c0mb00015a

PubMed ID

  • 20607165
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Additional Document Info

start page

  • 48

end page

  • 51

volume

  • 7

issue

  • 1

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