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Nucleic Acids Research|June 19, 2014
A gain-of-function mouse model identifies PRMT6 as a NF-κB coactivatorAlessandra Di Lorenzo, Yanzhong Yang, Marc Macaluso, et al.The Journal of Biological Chemistry|October 3, 2020
Genetic evidence for partial redundancy between the arginine methyltransferases CARM1 and PRMT6Donghang Cheng, Guozhen Gao, Alessandra Di Lorenzo, et al.Cancer Research|October 25, 2018
Mouse Models of Overexpression Reveal Distinct Oncogenic Roles for Different Type I Protein Arginine MethyltransferasesJianqiang Bao, Alessandra Di Lorenzo, Kevin Lin, et al.The Journal of Biological Chemistry|September 2, 2018
Screening for histone codebreakersMark T BedfordScientific Reports|February 20, 2013
Loss of the major Type I arginine methyltransferase PRMT1 causes substrate scavenging by other PRMTsSurbhi Dhar, Vidyasiri Vemulapalli, Alexander N Patananan, et al.EMBO Reports|February 19, 2002
PABP1 identified as an arginine methyltransferase substrate using high-density protein arraysJaeho Lee, Mark T BedfordBiochemical Society Transactions|April 4, 2023
Effectors and effects of arginine methylationYalong Wang, Mark T BedfordMolecular Cell|May 4, 2005
Arginine methylation an emerging regulator of protein functionMark T Bedford, Stéphane RichardPageof 21