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science & technology (1060) 1060
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1. 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
methylarginine | PRMT5 | arginine | methyltransferase | PRMT1 | epigenetic | methylation | and S-adenosyl-methionine | post-translational modification | demethylase | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | 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 | Index Medicus
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2. Full Text Arginine demethylation of G3BP1 promotes stress granule assembly
by Tsai, Wei-Chih and Gayatri, Sitaram and Reineke, Lucas C and Sbardella, Gianluca and Bedford, Mark T and Lloyd, Richard E
The Journal of biological chemistry, ISSN 0021-9258, 10/2016, Volume 291, Issue 43, pp. 22671 - 22685
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | Arsenites - pharmacology | Humans | Repressor Proteins - genetics | Protein-Arginine N-Methyltransferases - metabolism | Carrier Proteins - genetics | Poly-ADP-Ribose Binding Proteins | DNA Helicases | RNA Helicases | Carrier Proteins - metabolism | Arginine - genetics | Cytoplasmic Granules - metabolism | Cytoplasmic Granules - genetics | Cell Line, Tumor | Protein-Arginine N-Methyltransferases - genetics | Stress, Physiological - drug effects | Methylation | RNA Recognition Motif Proteins | Arginine - metabolism | Repressor Proteins - metabolism | Index Medicus | post-translational modification (PTM) | protein arginine N-methyltransferase (PRMT) | stress granule | RNA binding protein | G3BP1 | mRNA | protein arginine N-methyltransferase 5 (PRMT5) | Cell Biology
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3. Full Text Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive
by Cesaroni, Matteo and Lüscher, Bernhard and Amati, Bruno and Bassi, Christian and Casadio, Fabio and Guccione, Ernesto and Martinato, Francesca and Schuchlautz, Henning
Nature (London), ISSN 0028-0836, 10/2007, Volume 449, Issue 7164, pp. 933 - 937
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Fundamental and applied biological sciences. Psychology | Biological and medical sciences | Chromatin. Chromosome | Molecular and cellular biology | Molecular genetics | Cell Line | Histone-Lysine N-Methyltransferase - genetics | Histones - chemistry | Epigenesis, Genetic | Humans | Gene Expression Regulation | Nuclear Proteins - metabolism | Promoter Regions, Genetic - genetics | Protein-Arginine N-Methyltransferases - metabolism | DNA-Binding Proteins - metabolism | Transcription Factors - metabolism | Multiprotein Complexes - metabolism | Animals | Chromatin Immunoprecipitation | Histone-Lysine N-Methyltransferase - metabolism | Embryo, Mammalian - cytology | Cell Line, Tumor | Lysine - metabolism | Mice | Protein-Arginine N-Methyltransferases - genetics | Histones - metabolism | Methylation | Nuclear Proteins - genetics | Arginine - metabolism | Histones | Research | RNA | Analysis | Enzymes | Amino acids | Eukaryotes | Cellular biology | Genomics | Index Medicus
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4. Full Text N η-Substituted Arginyl Peptide Inhibitors of Protein Arginine N-Methyltransferases
by Lakowski, Ted M and ’t Hart, Peter and Ahern, Christopher A and Martin, Nathaniel I and Frankel, Adam
ACS chemical biology, ISSN 1554-8929, 11/2010, Volume 5, Issue 11, pp. 1053 - 1063
Repressor Proteins - chemistry | Peptides - chemistry | Humans | Enzyme Inhibitors - pharmacology | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Repressor Proteins - genetics | Enzyme Inhibitors - chemical synthesis | Nuclear Proteins - chemistry | Repressor Proteins - antagonists & inhibitors | Arginine - chemistry | Peptides - pharmacology | Peptides - chemical synthesis | Methylation - drug effects | Protein Processing, Post-Translational - drug effects | Enzyme Inhibitors - chemistry | Nuclear Proteins - antagonists & inhibitors | Protein Conformation | Protein-Arginine N-Methyltransferases - genetics | Nuclear Proteins - genetics | Protein-Arginine N-Methyltransferases - chemistry | Arginine - metabolism | Index Medicus
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5. 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
Science (American Association for the Advancement of Science), ISSN 1265-4906, 03/2016, Volume 351, Issue 6278, pp. 1214 - 1218
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | 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 | Index Medicus
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6. Full Text The PAF complex regulation of Prmt5 facilitates the progression and maintenance of MLL fusion leukemia
by Serio, J and Ropa, J and Chen, W and Mysliwski, M and Saha, N and Chen, L and Wang, J and Miao, H and Cierpicki, T and Grembecka, J and Muntean, A.G
Oncogene, ISSN 0950-9232, 01/2018, Volume 37, Issue 4, pp. 450 - 460
Biochemistry & Molecular Biology | Oncology | Genetics & Heredity | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Myeloid Ecotropic Viral Integration Site 1 Protein - metabolism | Epigenesis, Genetic | Homeodomain Proteins - metabolism | Humans | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Gene Knockdown Techniques | Tumor Suppressor Proteins - genetics | Myeloid Ecotropic Viral Integration Site 1 Protein - genetics | Female | Protein-Arginine N-Methyltransferases - genetics | Nuclear Proteins - genetics | Cell Proliferation - genetics | Histone-Lysine N-Methyltransferase - genetics | Tumor Suppressor Proteins - metabolism | Leukemia, Myeloid, Acute - pathology | Mice, Transgenic | Nuclear Proteins - metabolism | Gene Expression Regulation, Leukemic | Disease Progression | G1 Phase Cell Cycle Checkpoints - genetics | Homeodomain Proteins - genetics | Protein-Arginine N-Methyltransferases - metabolism | Xenograft Model Antitumor Assays | Animals | Histones - genetics | Myeloid-Lymphoid Leukemia Protein - genetics | Oncogene Proteins, Fusion - genetics | Cell Line, Tumor | Mice | Leukemia, Myeloid, Acute - genetics | Epigenetic inheritance | Gene expression | Health aspects | Oncogenes | Translocation | Transcription | Platelet-activating factor | Myeloid leukemia | Therapeutic applications | Leukemia | Protein arginine methyltransferase | Stat5 protein | Ribonucleic acid--RNA | Hemopoiesis | Latency | Arginine | Epigenetics | Acute myeloid leukemia | Index Medicus | small molecule inhibitors | PRMT5 | PAFc | MLL
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7. Full Text Selective inhibition of protein arginine methyltransferase 5 blocks initiation and maintenance of B-cell transformation
by Alinari, Lapo and Mahasenan, Kiran V and Yan, Fengting and Karkhanis, Vrajesh and Chung, Ji-Hyun and Smith, Emily M and Quinion, Carl and Smith, Porsha L and Kim, Lisa and Patton, John T and Lapalombella, Rosa and Yu, Bo and Wu, Yun and Roy, Satavisha and De Leo, Alessandra and Pileri, Stefano and Agostinelli, Claudio and Ayers, Leona and Bradner, James E and Chen-Kiang, Selina and Elemento, Olivier and Motiwala, Tasneem and Majumder, Sarmila and Byrd, John C and Jacob, Samson and Sif, Said and Li, Chenglong and Baiocchi, Robert A
Blood, ISSN 0006-4971, 04/2015, Volume 125, Issue 16, pp. 2530 - 2543
Life Sciences & Biomedicine | Hematology | Science & Technology | Small Molecule Libraries - pharmacology | Cell Transformation, Viral - drug effects | Humans | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | MicroRNAs - metabolism | Host-Pathogen Interactions - drug effects | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - genetics | Transcription Factor RelA - genetics | Lymphoma - metabolism | RNA Interference | Tumor Suppressor Proteins - genetics | B-Lymphocytes - virology | Cell Transformation, Viral - genetics | Protein-Arginine N-Methyltransferases - genetics | B-Lymphocytes - metabolism | Tumor Suppressor Proteins - metabolism | Histone Deacetylases - genetics | Herpesvirus 4, Human - physiology | Cells, Cultured | Enzyme Inhibitors - pharmacology | Lymphoma - genetics | Histone Deacetylases - metabolism | Transcriptome - drug effects | Transcriptome - genetics | Mice, SCID | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Protein-Arginine N-Methyltransferases - metabolism | B-Lymphocytes - drug effects | Microscopy, Confocal | Animals | Transcription Factor RelA - metabolism | Receptor-Like Protein Tyrosine Phosphatases, Class 3 - metabolism | MicroRNAs - genetics | Cell Line, Transformed | Lymphoma - virology | Index Medicus | Abridged Index Medicus | Lymphoid Neoplasia
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8. Full Text H4R3 methylation facilitates β-globin transcription by regulating histone acetyltransferase binding and H3 acetylation
by Li, Xingguo and Hu, Xin and Patel, Bhavita and Zhou, Zhuo and Liang, Shermi and Ybarra, River and Qiu, Yi and Felsenfeld, Gary and Bungert, Jörg and Huang, Suming
Blood, ISSN 0006-4971, 03/2010, Volume 115, Issue 10, pp. 2028 - 2037
Life Sciences & Biomedicine | Hematology | Science & Technology | Hematologic and hematopoietic diseases | Biological and medical sciences | Medical sciences | Embryo, Mammalian | Cells, Cultured | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Histone Acetyltransferases - physiology | beta-Globins - genetics | Protein-Arginine N-Methyltransferases - metabolism | Animals | beta-Globins - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Histone Acetyltransferases - metabolism | Histones - physiology | Protein-Arginine N-Methyltransferases - physiology | Transcription, Genetic | Mice | Protein-Arginine N-Methyltransferases - genetics | Acetylation | Histones - metabolism | Methylation | Arginine - metabolism | Histone-Lysine N-Methyltransferase - physiology | Gene Expression Regulation, Developmental - physiology | Protein Binding - physiology | Index Medicus | Abridged Index Medicus | Red Cells, Iron, and Erythropoiesis
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9. Full Text Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2
by Hadjikyriacou, Andrea and Yang, Yanzhong and Espejo, Alexsandra and Bedford, Mark T and Clarke, Steven G
The Journal of biological chemistry, ISSN 0021-9258, 07/2015, Volume 290, Issue 27, pp. 16723 - 16743
Life Sciences & Biomedicine | Biochemistry & Molecular Biology | Science & Technology | RNA-Binding Proteins - genetics | Humans | Protein Methyltransferases - genetics | Molecular Sequence Data | Substrate Specificity | Crystallography, X-Ray | Protein Methyltransferases - metabolism | RNA Splicing | Arginine - genetics | Protein-Arginine N-Methyltransferases - genetics | Protein-Arginine N-Methyltransferases - chemistry | Amino Acid Sequence | Biocatalysis | F-Box Proteins - metabolism | F-Box Proteins - chemistry | RNA-Binding Proteins - chemistry | RNA Splicing Factors | Amino Acid Motifs | Protein-Arginine N-Methyltransferases - metabolism | Animals | Mice | Methylation | F-Box Proteins - genetics | Arginine - metabolism | RNA-Binding Proteins - metabolism | Index Medicus | S-adenosylmethionine (SAM) | protein methylation | symmetric dimethylarginine | protein arginine N-methyltransferase 5 (PRMT5) | Enzymology | PRMT | protein arginine methylation | PRMT9 | enzyme mutation | RNA splicing | protein methyltransferase
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