Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate SpecificityMeng-Chiao Ho, David Shechter, Michael Brenowitz et al.|PLoS ONE|2013Cited by 138
Histone H2A and H4 N-terminal Tails Are Positioned by the MEP50 WD Repeat Protein for Efficient Methylation by the PRMT5 Arginine MethyltransferaseEmmanuel S. Burgos, David Shechter, Carola Wilczek et al.|Journal of Biological Chemistry|2015Cited by 93
Correction: Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate SpecificityMeng‐Chiao Ho, David Shechter, Carola Wilczek et al.|PLoS ONE|2013Cited by 26
PRMT5-MEP50 overall structure.Meng‐Chiao Ho, David Shechter, Carola Wilczek et al.|Figshare|2015Cited by 0
MEP50 serves as a substrate presenter for PRMT5Meng‐Chiao Ho, David Shechter, Carola Wilczek et al.|Figshare|2015Cited by 0