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2017, Methods in molecular biology, ISBN 1493966286, Volume 1528
Web Resource
2017, Methods in molecular biology, ISBN 1493966286, Volume 1528
Web Resource
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 | Electronic books | local
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
2003, Current topics in microbiology and immunology, ISBN 3540442081, Volume 274., vii, 296
Book
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, 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 | Index Medicus
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 | Index Medicus | Research Papers | mono-, di-, trimethylation
Journal Article
Journal Article
2006, Results and problems in cell differentiation, ISBN 3540336850, Volume 41., viii, 151
This volume includes timely reviews of several aspects of chromatin biology written by scientists at the forefront of this rapidly moving field. Topics covered... 
Chromatin | Cytology | Life Sciences | Biochemistry, general | Cell Biology
Book
FEBS Letters, ISSN 0014-5793, 12/2015, Volume 589, Issue 24, pp. 4061 - 4070
Histone residues can serve as platforms for specific regulatory function. Here we constructed a map of regulatory associations between histone residues and a... 
Histone modification | Histone residue | Nucleosome positioning | Gene expression profile | transcription factor | nucleosome-free region | Pol II | ORF | chromatin modifier | histone acetyltransferase | PTM | open reading frame | post-translational modification | histone deacetylase | transcription start site | Kolmogorov–Smirnov | TSS | histone residue | nucleosome | HAT | NFR | NUC | RNA polymerase II | HDAC | RNA-POLYMERASE-II | CODING REGIONS | ACETYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | SACCHAROMYCES-CEREVISIAE | NUCLEOSOME ORGANIZATION | CELL BIOLOGY | HUMAN GENOME | BIOPHYSICS | H3K4 METHYLATION | GENE-EXPRESSION | GLOBULAR DOMAIN | TRANSCRIPTIONAL ELONGATION | Acetyltransferases - metabolism | Oligonucleotide Array Sequence Analysis | Histones - chemistry | Methyltransferases - metabolism | Methyltransferases - genetics | Gene Expression Profiling | Acetyltransferases - genetics | Saccharomyces cerevisiae - metabolism | Jumonji Domain-Containing Histone Demethylases - chemistry | Transcription, Genetic | Lysine - metabolism | Acetylation | Methyltransferases - chemistry | Histone-Lysine N-Methyltransferase - genetics | Chromatin Assembly and Disassembly | Nucleosomes - metabolism | Saccharomyces cerevisiae Proteins - genetics | Jumonji Domain-Containing Histone Demethylases - genetics | Acetyltransferases - chemistry | Protein Interaction Mapping | Histone-Lysine N-Methyltransferase - chemistry | Point Mutation | Histones - genetics | Histone-Lysine N-Methyltransferase - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Protein Processing, Post-Translational | Histones - metabolism | Gene Expression Regulation, Bacterial | Methylation | Databases, Nucleic Acid | Jumonji Domain-Containing Histone Demethylases - metabolism | Saccharomyces cerevisiae - growth & development | Saccharomyces cerevisiae Proteins - chemistry | Genomics | Analysis | Post-translational modification | Chromatin | Genes | Gene expression | Anopheles | Gene mutations | Lysine | Genetic research | Histones | Genetic engineering | Index Medicus
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 | Embryos | DNA-directed RNA polymerase | Mutants | Recruitment | Polymerase | Proteins | Acids | Ribonucleic acids | Rodents | Histone methyltransferase | HDAC2 protein | Retinoic acid | RNA polymerase II | Symmetry | Index Medicus
Journal Article
Nature, ISSN 0028-0836, 08/2012, Volume 488, Issue 7411, pp. 404 - 408
Journal Article