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Nature, ISSN 0028-0836, 07/2010, Volume 466, Issue 7305, pp. 508 - 512
While reversible histone modifications are linked to an ever-expanding range of biological functions(1-5), the demethylases for histone H4 lysine 20 and their... 
METHYLATION | PROTEIN | CHROMOSOME STRUCTURE | MENTAL-RETARDATION | STABILITY | MULTIDISCIPLINARY SCIENCES | HEAT REPEATS | S-PHASE | IDENTIFICATION | BINDING | GENOME | Chromatin - metabolism | Phosphorylation | Transcription Factors - chemistry | Histones - chemistry | Humans | Transcription Factors - deficiency | Histone Demethylases - genetics | Host Cell Factor C1 - metabolism | DNA-Binding Proteins - metabolism | Multiprotein Complexes - metabolism | Lysine - metabolism | Protein Structure, Tertiary | Cell Line | Promoter Regions, Genetic | Chromosomal Proteins, Non-Histone - metabolism | Histone Demethylases - chemistry | Adenosine Triphosphatases - metabolism | Transcription Factors - genetics | DNA-Binding Proteins - chemistry | Chromosomal Proteins, Non-Histone - deficiency | Host Cell Factor C1 - genetics | Chromosomal Proteins, Non-Histone - genetics | Transcription Factors - metabolism | Histone Demethylases - metabolism | Multiprotein Complexes - chemistry | Histone-Lysine N-Methyltransferase - metabolism | Cell Cycle - physiology | Adenosine Triphosphatases - chemistry | HeLa Cells | Histones - metabolism | Methylation | Chromosomal Proteins, Non-Histone - chemistry | Physiological aspects | Histones | Genetic aspects | Research | DNA damage | Cell cycle | Proteins | Enzymes | Binding sites | Progressions | Lysine | Genes | Clusters | Condensing | Maintenance | Chromosomes
Journal Article
Genes & development, ISSN 0890-9369, 2004, Volume 18, Issue 11, pp. 1251 - 1262
Histone lysine methylation is a central modification to mark functionally distinct chromatin regions. In particular, H3-K9 trimethylation has emerged as a... 
Mono-, di-, trimethylation | Heterochromatin | Combinatorial histone methyl marks | Histone H4 Lys 20 | Histone code | Suv4-20h HMTases | X-INACTIVATION | PROTEIN | CHROMATIN | DROSOPHILA-MELANOGASTER | mono-, di | METHYLTRANSFERASE ACTIVITY | FUNCTIONAL-CHARACTERIZATION | DEVELOPMENTAL BIOLOGY | heterochromatin | SET DOMAIN | combinatorial histone methyl marks | HISTONE LYSINE METHYLATION | POSITION-EFFECT VARIEGATION | histone H4 Lys 20 | GENETICS & HEREDITY | histone code | trimethylation | Protein Methyltransferases | Methyltransferases - metabolism | Genes, Suppressor | Methyltransferases - genetics | Molecular Sequence Data | Substrate Specificity | Drosophila Proteins - metabolism | Heterochromatin - metabolism | Conserved Sequence | Fibroblasts | Female | Lysine - metabolism | Repressor Proteins - metabolism | Drosophila - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Histone-Lysine N-Methyltransferase - genetics | Chromosomal Proteins, Non-Histone - metabolism | Histones - immunology | Cells, Cultured | Gene Silencing | Repressor Proteins - genetics | Mammals | Chromosomal Proteins, Non-Histone - genetics | Animals | Heterochromatin - genetics | Histone Methyltransferases | Histone-Lysine N-Methyltransferase - metabolism | Mice | Drosophila Proteins - genetics | Histones - metabolism | Methylation | Histones | Gene silencing | Genetic aspects | Research | Research Papers | mono-, di-, trimethylation
Journal Article
Cell Reports, ISSN 2211-1247, 2013, Volume 4, Issue 3, pp. 601 - 608
Journal Article
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 728 - 13
Bilateral symmetry is a striking feature of the vertebrate body plan organization. Vertebral precursors, called somites, provide one of the best illustrations... 
FGF8 | PROTEIN IDENTIFICATION TECHNOLOGY | MOUSE EMBRYOGENESIS | SHOTGUN PROTEOMICS | BILATERAL SYMMETRY | MULTIDISCIPLINARY SCIENCES | TRANSCRIPTION | SOMITE SEGMENTATION | DYNAMIC EXPRESSION | HISTONE DEACETYLASE | G9A | Histones - chemistry | Epigenesis, Genetic | E1A-Associated p300 Protein - genetics | E1A-Associated p300 Protein - physiology | Histone Deacetylase 2 - physiology | Somites - growth & development | E1A-Associated p300 Protein - metabolism | Histone Deacetylase 1 - physiology | Embryo, Mammalian - metabolism | Somites - ultrastructure | Repressor Proteins - physiology | Tretinoin - metabolism | Histone Deacetylase 1 - genetics | Repressor Proteins - metabolism | Tretinoin - physiology | Somites - metabolism | Histone Deacetylase 2 - genetics | Proteins - physiology | Histone-Lysine N-Methyltransferase - genetics | Nerve Tissue Proteins - physiology | Signal Transduction | Repressor Proteins - genetics | Mice, Transgenic | Embryonic Development | Nerve Tissue Proteins - genetics | Nerve Tissue Proteins - metabolism | Proteins - genetics | Animals | Proteins - metabolism | Histone-Lysine N-Methyltransferase - metabolism | Embryo, Mammalian - cytology | Proteomics | Mice | Histone Deacetylase 2 - metabolism | Histones - metabolism | Histone-Lysine N-Methyltransferase - physiology | Histone Deacetylase 1 - metabolism | Histone deacetylase | Regulators | Vertebrae | Somites | Somitogenesis | Ribonucleic acid--RNA | Embryos | DNA-directed RNA polymerase | Mutants | Recruitment | Polymerase | Proteins | Acids | Rodents | Histone methyltransferase | HDAC2 protein | Retinoic acid | RNA polymerase II | Symmetry
Journal Article
Journal Article
Pharmacology & therapeutics (Oxford), ISSN 0163-7258, 2016, Volume 167, pp. 85 - 99
Epigenetic modifications are increasingly recognized as playing an important role in the pathogenesis of infectious diseases. They represent a critical... 
Chromatin | Immune regulation | Epigenetic | MYCOBACTERIUM-TUBERCULOSIS | CD4(+) T-CELLS | BET BROMODOMAIN INHIBITION | INFLAMMATORY GENE-EXPRESSION | INNATE IMMUNE-RESPONSES | IMMUNODEFICIENCY-VIRUS TYPE-1 | TRANSCRIPTIONAL CONTROL | PHARMACOLOGY & PHARMACY | GASTRIC EPITHELIAL-CELLS | HISTONE DEACETYLASE INHIBITORS | MACROPHAGE POLARIZATION | Anti-HIV Agents - pharmacology | Sepsis - immunology | Bacterial Infections - drug therapy | Epigenesis, Genetic | HIV Infections - genetics | Humans | Immunity, Innate | Sepsis - genetics | HIV Infections - immunology | Sepsis - drug therapy | Bacterial Infections - genetics | Macrophages - metabolism | Animals | Bacterial Infections - immunology | Drug Design | HIV Infections - drug therapy | Anti-Bacterial Agents - pharmacology | Histones - metabolism | Epigenetic inheritance | Bacterial infections | Health aspects | HIV infection | Medical colleges | T cells | HIV (Viruses) | Biological response modifiers | Macrophages | Hematopoietic stem cells | Oligomers | Killer cells | Interleukins | Bone morphogenetic proteins | Protein kinases | Protein binding | Niacinamide | Antiviral agents | Adenosine | Immune response | Heat shock proteins | Transforming growth factors | MicroRNA | Hospitals | Lysine | Analysis | Nitric oxide | Interferon | Adenylic acid | Methylation | Mitogens | NO, Nitric oxide | H3K4me3, Histone 3 lysine 4 trimethylation | HSPC, Hematopoietic stem cells | RomA, Regulator of methylation A | HSP70, Heat shock protein 70 | BET, Bromodomain and extra terminal domain family of proteins | IRAK, Interleukin receptor-associated kinase | IL-10, Interleukin 10 | SAHA, Suberoylanilide hydroxamic | SIRT, Silent mating type information regulator | EZH2, Enhancer of Zeste 2 | H3K27ac, Histone 3 lysine 27 acetylation | LPS, Lipopolysaccharide | Treg, Regulatory T-cells | TF, Transcription factor | miRNA, microRNA | AMPK, Adenosine monophosphate activated protein kinase | enhancer binding protein-α | mTOR, Mammalian target of rapamycin | NF-κΒ, Nuclear factor-κΒ | JMJD, Jumonji domain | Associate editor | TLR, Toll-like receptor | HAT, Histone acetyl transferase | H3T3, Histone 3 threonine 3 | H3K9meSe10phosK14ac, Histone 3 lysine 9 methylation, serine 10 phosphorylation and lysine 14 acetylation | NLR, Nucleotide-binding oligomerization domain protein like receptors | A. Doseff | EBPα, CCAAT | H3K23, Histone lysine 23 | HKMT, Histone lysine methyltransferase inhibitors | H3S10, Histone 3 serine 10 | H3K4me1, Histone 3 lysine 4 monomethylation | HIF-1α, Hypoxia-inducible factor | Tfh, Follicular T helper cells | PRR, Pattern recognition receptor | Chip-seq, Chromatin immunoprecipitation and sequencing | MBD2, Methyl-CpG binding domain protein 2 | NK, Natural killer cells | PTMs, Histone post-translational modifications | ROR, Retinoic acid receptor-related orphan receptor | NAD, Nicotinamide adenine dinucleotide | PAMPs, Pathogen associated microbial patterns | IL-4, Interleukin 4 | TGF-β, Transforming growth factor beta | HDAC, Histone deacetylase | HDACi, Histone deacytelase inhibitor | H3, Histone H3 | BCG, Bacille Calmette–Guerin | IFN, Interferon | ROS, Reactive oxygen species | TSA, Trichostatin A | ART, Anti-retroviral therapies | RLR, Retinoic acid inducible gene 1 like receptors | SET, Suvar3–9, enhancer-of-zeste, trithorax | TNF, Tumor necrosis factor | cagPAI, Cytotoxin-associated gene A pathogenicity island | IL-12, Interleukin 12
Journal Article
Nature (London), ISSN 1476-4687, 2012, Volume 489, Issue 7415, pp. 313 - 317
Cornelia de Lange syndrome (CdLS) is a dominantly inherited congenital malformation disorder, caused by mutations in the cohesin-loading protein NIPBL1,2 for... 
SISTER-CHROMATID COHESION | NIPPED-B | COMPLEX | NIPBL | HUMAN GENOME | RNA-SEQ | MULTIDISCIPLINARY SCIENCES | X-CHROMOSOME-INACTIVATION | S-PHASE | PROTEINS | BINDING | Chromatin - metabolism | Chondroitin Sulfate Proteoglycans - chemistry | Humans | Crystallography, X-Ray | Male | Phosphoproteins - metabolism | Cell Cycle Proteins - chemistry | Chromatin Immunoprecipitation | Repressor Proteins - deficiency | De Lange Syndrome - metabolism | Fibroblasts | Female | Transcription, Genetic | Acetylation | Binding Sites | Repressor Proteins - metabolism | De Lange Syndrome - genetics | Repressor Proteins - chemistry | Chromosomal Proteins, Non-Histone - metabolism | Histone Deacetylases - genetics | Cell Cycle Proteins - metabolism | Chondroitin Sulfate Proteoglycans - metabolism | Histone Deacetylases - chemistry | Histone Deacetylases - deficiency | Mutant Proteins - genetics | Prophase | Models, Molecular | Repressor Proteins - genetics | Histone Deacetylases - metabolism | Mutant Proteins - metabolism | Nuclear Proteins - metabolism | Mutation - genetics | Proteins - genetics | Mutant Proteins - chemistry | Protein Conformation | HeLa Cells | Adaptor Proteins, Signal Transducing - metabolism | Anaphase | Chromatin - genetics | Chromosomal Proteins, Non-Histone - chemistry | Genetics | De Lange syndrome | Genetic aspects | Research | Mutation (Biology) | Proteins | Cell culture | Genes | Cell cycle | Mutation | Females | Chromosomes | Crystal structure | Chromatin | Repressor Proteins | Life Sciences | Phosphoproteins | Chromosomal Proteins, Non-Histone | Histone Deacetylases | De Lange Syndrome | Chondroitin Sulfate Proteoglycans | Nuclear Proteins | Mutant Proteins | Adaptor Proteins, Signal Transducing | Development Biology | Cell Cycle Proteins
Journal Article