Title

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

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date

1-1-2011

Document Type

Article

Subjects

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

Disciplines

Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics

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.

DOI of Published Version

10.1039/c0mb00015a

Source

Mol Biosyst. 2011 Jan;7(1):48-51. doi: 10.1039/c0mb00015a. Link to article on publisher's site. Epub 2010 Jul 6.

Journal/Book/Conference Title

Molecular bioSystems

Comments

At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed

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