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Nature (London), ISSN 1476-4687, 2010, Volume 464, Issue 7290, pp. 927 - 931
Journal Article
Molecular Oncology, ISSN 1574-7891, 12/2016, Volume 10, Issue 10, pp. 1497 - 1515
Histone methyltransferases (HMTs) catalyze the methylation of lysine and arginine residues on histone tails and non-histone targets. These important... 
Histone methyltransferase | Chromatin | Breast cancer | Inhibitors | Transcription | SELECTIVE-INHIBITION | DNA METHYLATION | TUMOR-SUPPRESSOR GENE | TRANSCRIPTIONAL REPRESSION | CELL-PROLIFERATION | MESENCHYMAL TRANSITION | POTENT ANTITUMOR-ACTIVITY | LYSINE METHYLTRANSFERASE | ONCOLOGY | POOR-PROGNOSIS | PROTEIN ARGININE METHYLTRANSFERASES | Humans | Transcriptional Activation - drug effects | Protein-Arginine N-Methyltransferases - antagonists & inhibitors | Antineoplastic Agents - therapeutic use | Histone-Lysine N-Methyltransferase - analysis | Molecular Targeted Therapy | Breast Neoplasms - metabolism | Histone-Lysine N-Methyltransferase - antagonists & inhibitors | Histone Code - drug effects | Female | Antineoplastic Agents - pharmacology | Epigenesis, Genetic - drug effects | Protein-Arginine N-Methyltransferases - genetics | Gene Expression Regulation, Neoplastic - drug effects | Breast - pathology | Histone-Lysine N-Methyltransferase - genetics | Protein-Arginine N-Methyltransferases - analysis | Enzyme Inhibitors - pharmacology | Breast Neoplasms - drug therapy | Drug Discovery | Enzyme Inhibitors - therapeutic use | Protein-Arginine N-Methyltransferases - metabolism | Animals | Breast Neoplasms - genetics | Histone-Lysine N-Methyltransferase - metabolism | Breast - drug effects | Breast Neoplasms - pathology | Care and treatment | Methyltransferases | Lysine | Stem cells | Genetic transcription | Methylation | Cancer | CRISPR | Medical research | Genomes | Gene expression | Arginine | DNA methylation | Tumorigenesis | Binding sites | Deoxyribonucleic acid--DNA | Tumors | Review
Journal Article
Blood, ISSN 0006-4971, 03/2013, Volume 121, Issue 13, pp. 2533 - 2541
Journal Article
Journal Article
Nature, ISSN 0028-0836, 08/2018, Volume 560, Issue 7719, pp. 504 - 508
Histone H3 lysine 9 methylation (H3K9me) mediates heterochromatic gene silencing and is important for genome stability and the regulation of gene... 
SITE | METHYLATION | JMJC DOMAIN PROTEIN | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | HETEROCHROMATIN | HISTONE LYSINE METHYLTRANSFERASE | DYNAMICS | INHERITANCE | EXPRESSION | Methyltransferases - chemistry | Schizosaccharomyces pombe Proteins - chemistry | Histones - chemistry | Epigenesis, Genetic | Humans | Methyltransferases - metabolism | Cell Cycle Proteins - metabolism | Gene Silencing | Heterochromatin - chemistry | Cell Cycle Proteins - chemistry | Histone-Lysine N-Methyltransferase - chemistry | Schizosaccharomyces - genetics | Heterochromatin - genetics | Histone Methyltransferases - chemistry | Heterochromatin - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Schizosaccharomyces pombe Proteins - metabolism | Protein Conformation | Schizosaccharomyces - enzymology | Histone Methyltransferases - metabolism | Histones - metabolism | Methylation | Evolution, Molecular | Epigenetic inheritance | Methyltransferases | Analysis | Physiological aspects | Genetic research | Genetic regulation | Phosphorylation | Yeast | Peptides | Methyltransferase | Conservation | Amino acids | Homology | Genomes | Feedback loops | Catalytic activity | Positive feedback | Crystallography | Proteins | Demethylation | Heterochromatin | DNA methylation | Catalysis | Inhibition | Boundary element method | Deoxyribonucleic acid--DNA | Crystal structure | Enzymes | Stability | Gene expression | Substrates | Domains | Gene silencing | Hypotheses | Lysine | Proteomics | Epigenetics | Instability | Software | Scientific imaging | Mutation | Mass spectrometry | Histone H3 | Conformation
Journal Article
Journal Article