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2004, Novartis Foundation symposium, ISBN 0470862610, Volume 259, x, 300
Chair's Introduction (E. Verdin). Beyond the double helix: writing and reading the histone code (Y. Wang, et al.). The indexing potential of histone lysine... 
Proteins | Histone deacetylase | Chromatin | Chemical modification | Histones | Acetylation | Structure | Life Sciences | Biochemistry | SCIENCE
Book
2004, Methods in Molecular Biology, ISBN 158829336X, Volume 287, xi, 302
Recent advances in epigenetic research as well as the development of exciting new technologies have helped greatly in unraveling the many mysteries of... 
Chromatin | Epigenesis | Laboratory manuals | Telomere | ADP-ribosylation | Human genetics | Human Genetics | Biomedicine
Book
Journal of Mammary Gland Biology and Neoplasia, ISSN 1083-3021, 3/2010, Volume 15, Issue 1, pp. 19 - 33
The role of epigenetic phenomena in cancer biology is increasingly being recognized. Here we focus on the mechanisms and enzymes involved in regulating histone... 
Medicine & Public Health | Estrogen | Histone variants | Epigenetics | Oncology | Cancer Research | Breast cancer | Acetylation | Methylation | STEM-CELLS | PHYSIOLOGY | TUMOR-SUPPRESSOR GENE | H2A VARIANTS | NUCLEOSOME CORE PARTICLE | ER-ALPHA | EARLY MAMMALIAN DEVELOPMENT | DOMAIN-CONTAINING PROTEINS | ONCOLOGY | LYSINE METHYLATION | ESTROGEN-RECEPTOR-ALPHA | ENDOCRINOLOGY & METABOLISM | ARGININE METHYLATION | Epigenesis, Genetic | Humans | Gene Expression Regulation, Neoplastic | Histone Acetyltransferases - genetics | Histone Demethylases - genetics | Breast Neoplasms - metabolism | Genetic Variation | Breast Neoplasms - enzymology | Isoenzymes - metabolism | Histone Acetyltransferases - metabolism | Female | Protein-Arginine N-Methyltransferases - genetics | Histone-Lysine N-Methyltransferase - genetics | Histone Deacetylases - genetics | Isoenzymes - genetics | Histone Deacetylases - metabolism | Protein-Arginine N-Methyltransferases - metabolism | Histone Demethylases - metabolism | Animals | Breast Neoplasms - genetics | Histones - genetics | Histone-Lysine N-Methyltransferase - metabolism | Histones - metabolism | Enzymes | Development and progression | Genetic aspects | Gene expression | Acetates | Cancer | Histone Acetyltransferases | Histone-Lysine N-Methyltransferase | Isoenzymes | Biochemistry, Molecular Biology | Histone Deacetylases | Breast Neoplasms | Protein-Arginine N-Methyltransferases | Life Sciences | Histone Demethylases | Histones
Journal Article
1971, ISBN 9780306304569, xii, 305
Book
2003, Current topics in microbiology and immunology, ISBN 3540442081, Volume 274., vii, 296
Book
Journal Article
Neuropharmacology, ISSN 0028-3908, 05/2014, Volume 80, pp. 95 - 102
Alzheimer’ s disease (AD) is the most common form of dementia causing an increasing emotional and economical burden to our societies. Although much progress... 
HDAC inhibitors | Histone-acetylation | Alzheimer | Gene-expression | Memomry | LONG-TERM-MEMORY | RUBINSTEIN-TAYBI-SYNDROME | DNA-DAMAGE | SYNAPTIC PLASTICITY | NEUROSCIENCES | ACETYLTRANSFERASE ACTIVITY | MOUSE MODEL | DEACETYLASE INHIBITORS | CREB-BINDING-PROTEIN | POLY(ADP-RIBOSE) POLYMERASE-1 | PHARMACOLOGY & PHARMACY | DEPENDENT NEURODEGENERATION | Histone Acetyltransferases - chemistry | Humans | Brain - enzymology | Histone Acetyltransferases - genetics | Molecular Targeted Therapy | Histone Demethylases - genetics | Brain - metabolism | Protein Processing, Post-Translational - drug effects | Histone Acetyltransferases - metabolism | Epigenesis, Genetic - drug effects | Neurons - metabolism | Neurons - drug effects | Nerve Tissue Proteins - antagonists & inhibitors | Histone-Lysine N-Methyltransferase - genetics | Histone Demethylases - chemistry | Nerve Tissue Proteins - agonists | Gene Expression Regulation | Alzheimer Disease - drug therapy | Nootropic Agents - therapeutic use | Alzheimer Disease - enzymology | Nerve Tissue Proteins - genetics | Brain - drug effects | Histone-Lysine N-Methyltransferase - chemistry | Nerve Tissue Proteins - metabolism | Up-Regulation - drug effects | Histone Demethylases - metabolism | Acetylation - drug effects | Animals | Histone-Lysine N-Methyltransferase - metabolism | Methylation - drug effects | Models, Biological | Neurons - enzymology | Alzheimer Disease - metabolism | Histone Deacetylase Inhibitors - pharmacology | Histone Deacetylase Inhibitors - therapeutic use | Histones - metabolism | Nootropic Agents - pharmacology | Psychotherapy | Enzymes | Alzheimer's disease | Health aspects
Journal Article
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 and Development, ISSN 0890-9369, 06/2004, 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
Nature, ISSN 0028-0836, 09/2012, 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
Pharmacology and Therapeutics, ISSN 0163-7258, 11/2016, 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