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1. Full Text Disordered methionine metabolism in MTAP/CDKN2A deleted cancers leads to dependence on PRMT5
by Mavrakis, Konstantinos J and McDonald, E. Robert and Schlabach, Michael R and Billy, Eric and Hoffman, Gregory R and deWeck, Antoine and Ruddy, David A and Venkatesan, Kavitha and Yu, Jianjun and McAllister, Gregg and Stump, Mark and deBeaumont, Rosalie and Ho, Samuel and Yue, Yingzi and Liu, Yue and Yan-Neale, Yan and Yang, Guizhi and Lin, Fallon and Yin, Hong and Gao, Hui and Kipp, D. Randal and Zhao, Songping and McNamara, Joshua T and Sprague, Elizabeth R and Zheng, Bing and Lin, Ying and Shin Cho, Young and Gu, Justin and Crawford, Ken and Ciccone, David and Vitari, Alberto C and Lai, Albert and Capka, Vladimir and Hurov, Kristen and Porter, Jeffery A and Tallarico, John and Mickanin, Craig and Lees, Emma and Pagliarini, Raymond and Keen, Nicholas and Schmelzle, Tobias and Hofmann, Francesco and Stegmeier, Frank and Sellers, William R and Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Virtual Reality, ISSN 1359-4338, 03/2016, Volume 351, Issue 6278, pp. 1208 - 1213
5-Methylthioadenosine phosphorylase (MTAP) is a key enzyme in the methionine salvage pathway. The MTAP gene is frequently deleted in human cancers because of... 
5-METHYLTHIOADENOSINE | CELLS | METHYLATION | MELANOMA | MULTIDISCIPLINARY SCIENCES | PROLIFERATION | INHIBITOR | Neoplasms - metabolism | RNA, Small Interfering - genetics | Cell Survival | Methionine - metabolism | Humans | Cyclin-Dependent Kinase Inhibitor p16 - genetics | Deoxyadenosines - metabolism | Purine-Nucleoside Phosphorylase - genetics | Neoplasms - drug therapy | Protein-Arginine N-Methyltransferases - metabolism | Neoplasms - genetics | Gene Deletion | Cell Line, Tumor | Cyclin-Dependent Kinase Inhibitor p16 - metabolism | Protein-Arginine N-Methyltransferases - genetics | Thionucleosides - metabolism | Purine-Nucleoside Phosphorylase - metabolism | Enzymes | Cellular biology | Metabolism | Cancer | BASIC BIOLOGICAL SCIENCES | 60 APPLIED LIFE SCIENCES
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2. Full Text Arginine Methylation: The Coming of Age
by Blanc, Roméo S and Richard, Stéphane
Molecular Cell, ISSN 1097-2765, 01/2017, Volume 65, Issue 1, pp. 8 - 24
Arginine methylation is a common post-translational modification functioning as an epigenetic regulator of transcription and playing key roles in pre-mRNA... 
methylarginine | PRMT5 | arginine | methyltransferase | PRMT1 | epigenetic | methylation | and S-adenosyl-methionine | post-translational modification | demethylase | EPITHELIAL-MESENCHYMAL-TRANSITION | MOUSE DEVELOPMENT | SUBSTRATE-SPECIFICITY | METHYLTRANSFERASE 1 PRMT1 | SYMMETRIC DIMETHYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DNA-DAMAGE | GENE-EXPRESSION | STEM-CELL PROLIFERATION | PRE-MESSENGER-RNA | PRODUCT SPECIFICITY | CELL BIOLOGY | Signal Transduction | Humans | Enzyme Inhibitors - pharmacology | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Mice, Transgenic | Protein-Arginine N-Methyltransferases - metabolism | Animals | Protein Processing, Post-Translational - drug effects | Transcription, Genetic | Cell Differentiation | Protein-Arginine N-Methyltransferases - genetics | DNA Damage | Methylation | Arginine - metabolism | Post-translational modification | Epigenetic inheritance | Methyltransferases | Arginine | RNA | Analysis | Genetic engineering | Genetic transcription | Genetic translation | Cells
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3. Full Text Discovery of four recessive developmental disorders using probabilistic genotype and phenotype matching among 4,125 families
by Akawi, Nadia and McRae, Jeremy and Ansari, Morad and Balasubramanian, Meena and Blyth, Moira and Brady, Angela F and Clayton, Stephen and Cole, Trevor and Deshpande, Charu and Fitzgerald, Tomas W and Foulds, Nicola and Francis, Richard and Gabriel, George and Gerety, Sebastian S and Goodship, Judith and Hobson, Emma and Jones, Wendy D and Joss, Shelagh and King, Daniel and Klena, Nikolai and Kumar, Ajith and Lees, Melissa and Lelliott, Chris and Lord, Jenny and McMullan, Dominic and O'Regan, Mary and Osio, Deborah and Piombo, Virginia and Prigmore, Elena and Rajan, Diana and Rosser, Elisabeth and Sifrim, Alejandro and Smith, Audrey and Swaminathan, Ganesh J and Turnpenny, Peter and Whitworth, James and Wright, Caroline F and Firth, Helen V and Barrett, Jeffrey C and Lo, Cecilia W and FitzPatrick, David R and Hurles, Matthew E and DDD Study and DDD study and the DDD study
Nature Genetics, ISSN 1061-4036, 11/2015, Volume 47, Issue 11, pp. 1363 - 1369
Discovery of most autosomal recessive disease-associated genes has involved analysis of large, often consanguineous multiplex families or small cohorts of... 
INTELLECTUAL DISABILITY | VARIANTS | GENETICS | MOUSE | GENETICS & HEREDITY | GENOME-WIDE | GENERATION | MICE | FUNCTION MUTATION | FEATURES | REVEALS | Genetic Predisposition to Disease - genetics | Humans | Genetic Association Studies - methods | Family Health | Genotype | Male | United Kingdom | Developmental Disabilities - genetics | Developmental Disabilities - classification | Genes, Recessive | Genetic Variation | Exome - genetics | Phenotype | Pedigree | Matrix Metalloproteinases, Secreted - genetics | Cell Cycle Proteins - genetics | Female | Protein-Arginine N-Methyltransferases - genetics | Ubiquitin-Protein Ligases - genetics | Sequence Analysis, DNA - methods | Disease susceptibility | Genetic aspects | Identification and classification | Familial diseases | Risk factors | Datasets | Mutation | Genes | Methods
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4. Full Text MTAP deletion confers enhanced dependency on the PRMT5 arginine methyltransferase in cancer cells
by Kryukov, Gregory V and Wilson, Frederick H and Ruth, Jason R and Paulk, Joshiawa and Tsherniak, Aviad and Marlow, Sara E and Vazquez, Francisca and Weir, Barbara A and Fitzgerald, Mark E and Tanaka, Minoru and Bielski, Craig M and Scott, Justin M and Dennis, Courtney and Cowley, Glenn S and Boehm, Jesse S and Root, David E and Golub, Todd R and Clish, Clary B and Bradner, James E and Hahn, William C and Garraway, Levi A
Hernia, ISSN 1265-4906, 03/2016, Volume 351, Issue 6278, pp. 1214 - 1218
The discovery of cancer dependencies has the potential to inform therapeutic strategies and to identify putative drug targets. Integrating data from... 
METHYLTHIOADENOSINE PHOSPHORYLASE | HOMOZYGOUS DELETION | METHYLATION | CODELETION | GENE | MULTIDISCIPLINARY SCIENCES | DEFICIENT | TUMOR-SUPPRESSOR | INHIBITOR | METHYLOSOME | HISTONE | Humans | Enzyme Inhibitors - pharmacology | Neoplasms - enzymology | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Thionucleosides - pharmacology | Deoxyadenosines - metabolism | Pyrimidines - pharmacology | Purine-Nucleoside Phosphorylase - genetics | Neoplasms - drug therapy | Protein-Arginine N-Methyltransferases - metabolism | Isoquinolines - pharmacology | Gene Deletion | Cell Line, Tumor | Protein-Arginine N-Methyltransferases - genetics | Transcription Factors | Deoxyadenosines - pharmacology | Thionucleosides - metabolism | Purine-Nucleoside Phosphorylase - metabolism | Arginine | Transferases | Cancer | Methyltransferases | Health aspects | Cancer cells | Enzymes | Cellular biology | Metabolism
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5. Full Text Dysregulation of PRMT1 and PRMT6, Type I arginine methyltransferases, is involved in various types of human cancers
by Yoshimatsu, Masanori and Toyokawa, Gouji and Hayami, Shinya and Unoki, Motoko and Tsunoda, Tatsuhiko and Field, Helen I and Kelly, John D and Neal, David E and Maehara, Yoshihiko and Ponder, Bruce A.J and Nakamura, Yusuke and Hamamoto, Ryuji
International Journal of Cancer, ISSN 0020-7136, 02/2011, Volume 128, Issue 3, pp. 562 - 573
Protein arginine methylation is a novel post‐translational modification regulating a diversity of cellular processes, including histone functions, but the... 
PRMT6 | ADMA | PRMT1 | epigenetics | Type I protein arginine methyltransferase | ANDROGEN RECEPTOR | CELLS | METHYLATION | PROTEIN | ASYMMETRIC DIMETHYLARGININE | GENE-EXPRESSION PROFILES | N-METHYLTRANSFERASE | ONCOLOGY | CDNA MICROARRAYS | HISTONE H4 | ARTERY-DISEASE | Carcinoma, Non-Small-Cell Lung - pathology | Lung Neoplasms - genetics | Anthracenes | RNA, Small Interfering - genetics | Enzyme-Linked Immunosorbent Assay | Oligonucleotide Array Sequence Analysis | Carcinoma, Non-Small-Cell Lung - genetics | Humans | Gene Expression Regulation, Neoplastic | Repressor Proteins - genetics | DNA Replication | Lung Neoplasms - pathology | Gene Expression Profiling | Arginine - analogs & derivatives | Urinary Bladder Neoplasms - genetics | Neoplasms - genetics | Propane - analogs & derivatives | Arginine - blood | Cell Division | Urinary Bladder Neoplasms - pathology | Cell Line, Tumor | Propane - blood | Protein-Arginine N-Methyltransferases - genetics | Nuclear Proteins - genetics | Index Medicus
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6. Full Text A TGFβ-PRMT5-MEP50 axis regulates cancer cell invasion through histone H3 and H4 arginine methylation coupled transcriptional activation and repression
by Chen, H and Lorton, B and Gupta, V and Shechter, D
Oncogene, ISSN 0950-9232, 01/2017, Volume 36, Issue 3, pp. 373 - 386
Protein arginine methyltransferase 5 (PRMT5) complexed with MEP50/WDR77 catalyzes arginine methylation on histones and other proteins. PRMT5-MEP50 activity is... 
PRMT5 | METHYLTRANSFERASE | PROTEIN | DNA METHYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | VALIDATION | EMT | CELL BIOLOGY | ONCOLOGY | SYMMETRIC DIMETHYLATION | GENETICS & HEREDITY | LUNG ADENOCARCINOMA | EXPRESSION | PROGRESSION | Adenocarcinoma - pathology | Prognosis | Adenocarcinoma of Lung | Carcinoma, Squamous Cell - genetics | Carcinoma, Squamous Cell - pathology | Epigenesis, Genetic | Humans | Gene Expression Regulation, Neoplastic | Lung Neoplasms - pathology | MCF-7 Cells | Neoplasms - genetics | Epithelial-Mesenchymal Transition | Female | Transcription, Genetic | Adenocarcinoma - genetics | Protein-Arginine N-Methyltransferases - genetics | Lung Neoplasms - genetics | A549 Cells | Neoplasm Invasiveness | Gene Expression Profiling - methods | Sequence Analysis, RNA - methods | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Adaptor Proteins, Signal Transducing - genetics | Histones - metabolism | Methylation | Neoplasms - pathology | Transforming Growth Factor beta - metabolism | Arginine - metabolism | cancer epigenetics | cancer invasion | transcriptome | Arginine methylation
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7. Full Text A methyl transferase links the circadian clock to the regulation of alternative splicing
by Sanchez, Sabrina E and Petrillo, Ezequiel and Beckwith, Esteban J and Zhang, Xu and Rugnone, Matias L and Hernando, C. Esteban and Cuevas, Juan C and Godoy Herz, Micaela A and Depetris-Chauvin, Ana and Simpson, Craig G and Brown, John W. S and Cerdán, Pablo D and Borevitz, Justin O and Mas, Paloma and Ceriani, M. Fernanda and Kornblihtt, Alberto R and Yanovsky, Marcelo J
Nature, ISSN 0028-0836, 11/2010, Volume 468, Issue 7320, pp. 112 - 116
Circadian rhythms allow organisms to time biological processes to the most appropriate phases of the day-night cycle(1). Posttranscriptional regulation is... 
ARABIDOPSIS-THALIANA | METHYLTRANSFERASE | GENE | DROSOPHILA-MELANOGASTER | BEHAVIOR | MULTIDISCIPLINARY SCIENCES | PHOSPHOLIPASE-C | REQUIRES | ARGININE METHYLATION | EXPRESSION | RECIPROCAL REGULATION | Darkness | Arabidopsis - physiology | Arabidopsis - enzymology | Drosophila melanogaster - physiology | Protein Methyltransferases - genetics | Circadian Clocks - genetics | Gene Expression Profiling | Drosophila Proteins - metabolism | RNA, Messenger - metabolism | Drosophila melanogaster - genetics | Protein Methyltransferases - metabolism | Arabidopsis Proteins - metabolism | Arabidopsis - radiation effects | Spliceosomes - metabolism | Period Circadian Proteins - genetics | Base Sequence | Light | Gene Expression Regulation, Plant | RNA Precursors - metabolism | Protein-Arginine N-Methyltransferases - genetics | Drosophila melanogaster - radiation effects | Arabidopsis Proteins - genetics | RNA Splice Sites - genetics | Alternative Splicing - genetics | RNA, Messenger - genetics | Circadian Rhythm - genetics | RNA Precursors - genetics | Circadian Rhythm - physiology | Transcription Factors - genetics | Protein-Arginine N-Methyltransferases - metabolism | Arabidopsis - genetics | Phenotype | Animals | Drosophila melanogaster - enzymology | Drosophila Proteins - genetics | Mutation | Methylation | Circadian Clocks - physiology | Arabidopsis thaliana | Circadian rhythms | Methyltransferases | Physiological aspects | Genetic aspects | Research | RNA splicing | Proteins | Fourier transforms | Insects | Rodents | Epigenetics | Circadian rhythm | Gene expression | Arrays | Life Sciences | Neurons and Cognition | Other
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8. Full Text SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination
by Yanling Zhao, Dorothy and Gish, Gerald and Braunschweig, Ulrich and Li, Yue and Ni, Zuyao and Schmitges, Frank W and Zhong, Guoqing and Liu, Ke and Li, Weiguo and Moffat, Jason and Vedadi, Masoud and Min, Jinrong and Pawson, Tony J and Blencowe, Benjamin J and Greenblatt, Jack F
Nature, ISSN 0028-0836, 01/2016, Volume 529, Issue 7584, pp. 48 - 53
The carboxy-terminal domain (CTD) of the RNA polymerase II (RNAP II) subunit POLR2A is a platform for modifications specifying the recruitment of factors that... 
RECRUITMENT | METHYLATION | COMPLEX | PROTEIN | METHYLTRANSFERASE | SPINAL MUSCULAR-ATROPHY | CHROMATIN | TDP-43 | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTIONAL PAUSE SITES | ALS | Protein Structure, Tertiary | Cell Line | RNA Helicases - metabolism | Humans | Neurodegenerative Diseases - genetics | RNA Polymerase II - metabolism | Survival of Motor Neuron 1 Protein - metabolism | Protein-Arginine N-Methyltransferases - metabolism | Transcription Elongation, Genetic | Transcription Termination, Genetic | Survival of Motor Neuron 1 Protein - genetics | Protein Binding | RNA Helicases - genetics | Protein-Arginine N-Methyltransferases - genetics | DNA Damage | Methylation | RNA Polymerase II - chemistry | Arginine - metabolism | Influence | Research | Arginine | Gene expression | Analysis | RNA polymerases | Proteins | Phosphorylation | Immunoglobulins | RNA polymerase | Peptides
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9. Full Text Small molecule inhibitors that discriminate between protein arginine N-methyltransferases PRMT1 and CARM1
by Dowden, James and Pike, Richard A and Parry, Richard V and Hong, Wei and Muhsen, Usama A and Ward, Stephen G
Organic and Biomolecular Chemistry, ISSN 1477-0520, 10/2011, Volume 9, Issue 22, pp. 7814 - 7821
Protein arginine N-methyltransferases (PRMTs) selectively replace N-H for N-CH3 at substrate protein guanidines, a post-translational modification important... 
CORE | ANDROGEN RECEPTOR | METHYLATION | DESIGN | DOCKING | CHEMISTRY, ORGANIC | TRANSCRIPTIONAL COACTIVATOR | EXPRESSION | BINDING | Molecular Weight | Epigenesis, Genetic | Escherichia coli | Humans | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Substrate Specificity | Crystallography, X-Ray | Enzyme Inhibitors - chemical synthesis | Recombinant Fusion Proteins - metabolism | Repressor Proteins - antagonists & inhibitors | Transformation, Bacterial | Arginine - antagonists & inhibitors | Protein-Arginine N-Methyltransferases - genetics | Binding Sites | Protein-Arginine N-Methyltransferases - chemistry | Repressor Proteins - metabolism | Repressor Proteins - chemistry | Enzyme Inhibitors - pharmacology | Models, Molecular | Repressor Proteins - genetics | Recombinant Fusion Proteins - chemistry | Protein-Arginine N-Methyltransferases - metabolism | Plasmids | Protein Binding | Recombinant Fusion Proteins - genetics | Protein Processing, Post-Translational | S-Adenosylmethionine - antagonists & inhibitors | Methylation | Arginine - metabolism | S-Adenosylmethionine - metabolism
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10. Full Text Histone arginine methylation
by Di Lorenzo, Alessandra and Bedford, Mark T
FEBS Letters, ISSN 0014-5793, 07/2011, Volume 585, Issue 13, pp. 2024 - 2031
Arginine methylation is a common posttranslational modification (PTM). This type of PTM occurs on both nuclear and cytoplasmic proteins, and is particularly... 
ChIP-seq | Tudor domain | CARM1 | Histone code | Arginine methylation | TRANSCRIPTIONAL ACTIVATION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYMMETRIC DIMETHYLARGININE | MASS-SPECTROMETRY | CELL BIOLOGY | N-METHYLTRANSFERASE | SUBSTRATE-SPECIFICITY | BIOPHYSICS | STRUCTURAL BASIS | ESTROGEN-RECEPTOR-ALPHA | GENE-EXPRESSION | PROTEIN METHYLTRANSFERASE | Animals | Humans | Protein-Arginine N-Methyltransferases - genetics | Histones - metabolism | Methylation | Arginine - metabolism | Protein-Arginine N-Methyltransferases - metabolism | Post-translational modification | Histones | DNA binding proteins | Methyltransferases | Arginine | histone code | arginine methylation | tudor domain
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