Histone deacetylase is a component of the internal nuclear matrix.
Open Access
- 1 November 1991
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (32) , 21936-21942
- https://doi.org/10.1016/s0021-9258(18)54727-x
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- A matrix/scaffold attachment region binding protein: Identification, purification, and mode of bindingCell, 1991
- Factors affecting nucleosome structure in transcriptionally active chromatinEuropean Journal of Biochemistry, 1990
- Patterns of histone acetylationEuropean Journal of Biochemistry, 1990
- Acetylation and deacetylation of histone H4 continue through metaphase with depletion of more-acetylated isoforms and altered site usageExperimental Cell Research, 1989
- Chromosomal loop/nuclear matrix organization of transcriptionally active and inactive RNA polymerases in HeLa nucleiJournal of Molecular Biology, 1988
- Gene-specific differences in the supranucleosomal organization of rat liver chromatinBiochemistry, 1987
- A Chinese hamster ovary cell histone deacetylase that is associated with a unique class of mononucleosomesBiochemistry, 1987
- Affinity chromatographic purification of nucleosomes containing transcriptionally active DNA sequencesJournal of Molecular Biology, 1987
- Nucleosome disruption precedes transcription and is largely limited to the transcribed domain of globin genes in murine erythroleukemia cellsJournal of Molecular Biology, 1985
- Histone deacetylase from HeLa cells: properties of the high molecular weight complexBiochemistry, 1983