Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
Epigenetic control via allosteric regulation of mammalian protein arginine methyltransferases
Authors
Keywords
-
Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 114, Issue 38, Pages 10101-10106
Publisher
Proceedings of the National Academy of Sciences
Online
2017-09-06
DOI
10.1073/pnas.1706978114
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Arginine Methylation: The Coming of Age
- (2017) Roméo S. Blanc et al. MOLECULAR CELL
- Discovery and optimization of selective inhibitors of protein arginine methyltransferase 5 by docking-based virtual screening
- (2017) Yan Ye et al. ORGANIC & BIOMOLECULAR CHEMISTRY
- Protein Arginine Methyltransferase Product Specificity Is Mediated by Distinct Active-site Architectures
- (2016) Kanishk Jain et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Discovery of a Potent Class I Protein Arginine Methyltransferase Fragment Inhibitor
- (2016) Renato Ferreira de Freitas et al. JOURNAL OF MEDICINAL CHEMISTRY
- A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase
- (2016) Erik W. Debler et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Histone H3K36 mutations promote sarcomagenesis through altered histone methylation landscape
- (2016) C. Lu et al. SCIENCE
- Comprehensive analysis of histone post-translational modifications in mouse and human male germ cells
- (2016) Lacey J. Luense et al. Epigenetics & Chromatin
- PRMT7 Preserves Satellite Cell Regenerative Capacity
- (2016) Roméo Sébastien Blanc et al. Cell Reports
- A Potent, Selective, and Cell-Active Inhibitor of Human Type I Protein Arginine Methyltransferases
- (2015) Mohammad S. Eram et al. ACS Chemical Biology
- A Potent, Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 3 (PRMT3)
- (2015) H. Ümit Kaniskan et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Chemical Biology of Protein Arginine Modifications in Epigenetic Regulation
- (2015) Jakob Fuhrmann et al. CHEMICAL REVIEWS
- Histone Arginine Methylation by PRMT7 Controls Germinal Center Formation via RegulatingBcl6Transcription
- (2015) Zhengzhou Ying et al. JOURNAL OF IMMUNOLOGY
- The dual epigenetic role of PRMT5 in acute myeloid leukemia: gene activation and repression via histone arginine methylation
- (2015) S S Tarighat et al. LEUKEMIA
- MYC regulates the core pre-mRNA splicing machinery as an essential step in lymphomagenesis
- (2015) Cheryl M. Koh et al. NATURE
- A selective inhibitor of PRMT5 with in vivo and in vitro potency in MCL models
- (2015) Elayne Chan-Penebre et al. Nature Chemical Biology
- PRMT9 is a Type II methyltransferase that methylates the splicing factor SAP145
- (2015) Yanzhong Yang et al. Nature Communications
- Interplay between arginine methylation and ubiquitylation regulates KLF4-mediated genome stability and carcinogenesis
- (2015) Dong Hu et al. Nature Communications
- Protein arginine methyltransferase 7 promotes breast cancer cell invasion through the induction of MMP9 expression
- (2015) R. Mitchell Baldwin et al. Oncotarget
- Substrate Specificity of Human Protein Arginine Methyltransferase 7 (PRMT7)
- (2014) You Feng et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Cross-talk among epigenetic modifications: lessons from histone arginine methylation
- (2013) Diego Molina-Serrano et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Substrate Specificity, Processivity, and Kinetic Mechanism of Protein Arginine Methyltransferase 5
- (2013) Min Wang et al. BIOCHEMISTRY
- Protein post-translational modifications and regulation of pluripotency in human stem cells
- (2013) Yu-Chieh Wang et al. CELL RESEARCH
- Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions
- (2013) You Feng et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity
- (2013) Meng-Chiao Ho et al. PLoS One
- Trans-tail regulation of MLL4-catalyzed H3K4 methylation by H4R3 symmetric dimethylation is mediated by a tandem PHD of MLL4
- (2012) S. S. Dhar et al. GENES & DEVELOPMENT
- Protein Arginine Methyltransferase 7 Regulates Cellular Response to DNA Damage by Methylating Promoter Histones H2A and H4 of the Polymerase δ Catalytic Subunit Gene,POLD1
- (2012) Vrajesh Karkhanis et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Human Protein Arginine Methyltransferase 7 (PRMT7) Is a Type III Enzyme Forming ω-NG-Monomethylated Arginine Residues
- (2012) Cecilia I. Zurita-Lopez et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance
- (2012) Valentina Migliori et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Crystal structure of the human PRMT5:MEP50 complex
- (2012) S. Antonysamy et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A Transient Kinetic Analysis of PRMT1 Catalysis
- (2011) You Feng et al. BIOCHEMISTRY
- Histone H4 Acetylation Differentially Modulates Arginine Methylation by an inCisMechanism
- (2011) You Feng et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- H3K36 Methylation Antagonizes PRC2-mediated H3K27 Methylation
- (2011) Wen Yuan et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Structural insights into protein arginine symmetric dimethylation by PRMT5
- (2011) L. Sun et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Protein Arginine Methylation in Mammals: Who, What, and Why
- (2009) Mark T. Bedford et al. MOLECULAR CELL
- Kinetic Mechanism of Protein Arginine Methyltransferase 1†
- (2008) Obiamaka Obianyo et al. BIOCHEMISTRY
Discover Peeref hubs
Discuss science. Find collaborators. Network.
Join a conversationPublish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn More