FBXO11/PRMT9, a new protein arginine methyltransferase, symmetrically dimethylates arginine residues
- 8 February 2006
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 342 (2) , 472-481
- https://doi.org/10.1016/j.bbrc.2006.01.167
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- PRMT7, a New Protein Arginine Methyltransferase That Synthesizes Symmetric DimethylarginineJournal of Biological Chemistry, 2005
- The SCF ubiquitin ligase: insights into a molecular machineNature Reviews Molecular Cell Biology, 2004
- A Proteomic Analysis of Arginine-methylated Protein ComplexesMolecular & Cellular Proteomics, 2003
- mSin3A/Histone Deacetylase 2- and PRMT5-Containing Brg1 Complex Is Involved in Transcriptional Repression of the Myc Target Gene cadMolecular and Cellular Biology, 2003
- Requirement for Multiple Domains of the Protein Arginine Methyltransferase CARM1 in Its Transcriptional Coactivator FunctionPublished by Elsevier ,2002
- Archaeal Surface Layer Proteins Contain β Propeller, PKD, and β Helix Domains and Are Related to Metazoan Cell Surface ProteinsStructure, 2002
- Crystal Structure of Guanidinoacetate Methyltransferase from Rat Liver: A Model Structure of Protein Arginine MethyltransferaseJournal of Molecular Biology, 2002
- The Arginine-1493 Residue in QRRGRTGR1493G Motif IV of the Hepatitis C Virus NS3 Helicase Domain Is Essential for NS3 Protein Methylation by the Protein Arginine Methyltransferase 1Journal of Virology, 2001
- PRMT5 (Janus Kinase-binding Protein 1) Catalyzes the Formation of Symmetric Dimethylarginine Residues in ProteinsJournal of Biological Chemistry, 2001
- Synergistic, p160 Coactivator-dependent Enhancement of Estrogen Receptor Function by CARM1 and p300Journal of Biological Chemistry, 2000