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A time-resolved atlas of histone modifications during mitotic entry
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Histone Acetylation and Histone Deacetylation
Molecular Biotechnology, 2002Regulation of inflammatory gene transcription is controlled, at least in part, by the degree of local unwinding of nucleosomal DNA. This unwinding is regulated by histone acetylation--increased acetylation results in a more loosely wound structure allowing access of basal transcription factors and RNA polymerase II.
Kazuhiro, Ito, Ian M, Adcock
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Molecular Microbiology, 2004
SummaryThe histones are responsible for packaging and regulating access to eukaryotic genomes. Trypanosomatids are flagellated protists that diverged early from the eukaryotic lineage and include parasites that cause disease in humans and other mammals.
Alsford, Sam, Horn, David
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SummaryThe histones are responsible for packaging and regulating access to eukaryotic genomes. Trypanosomatids are flagellated protists that diverged early from the eukaryotic lineage and include parasites that cause disease in humans and other mammals.
Alsford, Sam, Horn, David
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Current Opinion in Pharmacology, 2003
Post-translational modification of the histones of chromatin has a fundamental role in regulating gene expression. Enzymes involved in these epigenetic events include histone deacetylases (class I and class II), which can be inhibited by a structurally diverse group of small molecules.
Paul A, Marks +2 more
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Post-translational modification of the histones of chromatin has a fundamental role in regulating gene expression. Enzymes involved in these epigenetic events include histone deacetylases (class I and class II), which can be inhibited by a structurally diverse group of small molecules.
Paul A, Marks +2 more
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Annual Review of Biochemistry, 2001
▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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▪ Abstract Transcriptional regulation in eukaryotes occurs within a chromatin setting and is strongly influenced by nucleosomal barriers imposed by histone proteins. Among the well-known covalent modifications of histones, the reversible acetylation of internal lysine residues in histone amino-terminal domains has long been positively linked to ...
S Y, Roth, J M, Denu, C D, Allis
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Histone Genes and Histone Messengers
Annual Review of Biochemistry, 1979PERSPECfIVES AND SUMMARY . INTRODUCfION . HISTONE GENE ORGANIZATION . General Features . The Special Case 01 L Pictus .. O:; :: :::; cd;; .. ·:::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::: Drosophila Melanogaster . Chromomeric localization . Cloned Drosophila histone genes . Histone Genes 01
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Science, 1976
Highly specific antibodies were raised to histone 1 (H1) and the histone complexes H3 2 -H4 2 and H2A-H2B, isolated by salt extraction. Antibody to H1 could detect irreversible conformational changes in acid- or urea-treated H1. The antibodies showed different reactivities with chromosomes as
N, Mihalakis, O J, Miller, B F, Erlanger
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Highly specific antibodies were raised to histone 1 (H1) and the histone complexes H3 2 -H4 2 and H2A-H2B, isolated by salt extraction. Antibody to H1 could detect irreversible conformational changes in acid- or urea-treated H1. The antibodies showed different reactivities with chromosomes as
N, Mihalakis, O J, Miller, B F, Erlanger
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The International Journal of Biochemistry & Cell Biology, 1997
Linker histones of which histone H1 is a representative are a diverse family of architectural proteins within the eukaryotic nucleus. These proteins have a variety of structures, but invariably contain a region enriched in lysine, serine, alanine and proline.
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Linker histones of which histone H1 is a representative are a diverse family of architectural proteins within the eukaryotic nucleus. These proteins have a variety of structures, but invariably contain a region enriched in lysine, serine, alanine and proline.
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