Literature DB >> 23765659

Enzymatic characterization of recombinant enzymes of O-GlcNAc cycling.

Eun Ju Kim1, John A Hanover.   

Abstract

The dynamic addition of O-GlcNAc to target proteins is now recognized as a major signaling paradigm impacting phosphorylation, protein turnover, gene expression, and other posttranslational modifications influencing epigenetics. Here we describe the production of and methods for assay of the recombinant enzymes of O-GlcNAc cycling: O-linked GlcNAc Transferase (OGT) and O-GlcNAcase (OGA).

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Year:  2013        PMID: 23765659     DOI: 10.1007/978-1-62703-465-4_11

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  1 in total

1.  Activity Based High-Throughput Screening for Novel O-GlcNAc Transferase Substrates Using a Dynamic Peptide Microarray.

Authors:  Jie Shi; Suhela Sharif; Rob Ruijtenbeek; Roland J Pieters
Journal:  PLoS One       Date:  2016-03-09       Impact factor: 3.240

  1 in total

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