A novel role for protein arginine deiminase 4 in pluripotency: The emerging role of citrullinated histone H1 in cellular programming
Author:
Affiliation:
1. Department of Chemistry; The Scripps Research Institute; Jupiter FL USA
2. Baker Institute for Animal Health; College of Veterinary Medicine; Cornell University; Ithaca NY USA
Funder
National Institute of General Medical Sciences
U.S. Department of Defense
Publisher
Wiley
Subject
General Biochemistry, Genetics and Molecular Biology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/bies.201400057/fullpdf
Reference46 articles.
1. The protein arginine deiminases: structure, function, inhibition, and disease;Bicker;Biopolymers,2013
2. Methylation of arginine residues interferes with citrullination by peptidylarginine deiminases in vitro;Raijmakers;J Mol Biol,2007
3. Autodeimination of protein arginine deiminase 4 alters protein-protein interactions but not activity;Slack;Biochemistry,2011
4. Citrullination regulates pluripotency and histone H1 binding to chromatin;Christophorou;Nature,2014
5. Potential role of peptidylarginine deiminase enzymes and protein citrullination in cancer pathogenesis;Mohanan;Biochem Res Int,2012
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