Characterization of the Stability and Folding of H2A.Z Chromatin Particles
Open Access
- 1 November 2001
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 276 (45) , 41945-41949
- https://doi.org/10.1074/jbc.m108217200
Abstract
No abstract availableKeywords
This publication has 56 references indexed in Scilit:
- Nucleosomes and the chromatin fiberCurrent Opinion in Genetics & Development, 2001
- Mechanisms for ATP-dependent chromatin remodellingCurrent Opinion in Genetics & Development, 2001
- What does ‘chromatin remodeling’ mean?Trends in Biochemical Sciences, 2000
- Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variantsNucleic Acids Research, 2000
- Review: Chromatin Structural Features and Targets That Regulate TranscriptionJournal of Structural Biology, 2000
- Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote ChromosomeCell, 1999
- A likely histone H2A.F/Z variant in Saccharomyces cerevisiaeTrends in Biochemical Sciences, 1996
- Sequence of cDNAs for mammalian H2A.Z, an evolutionarily diverged but highly conserved basal histone H2A isoprotein speciesNucleic Acids Research, 1988
- Drosophilahas a single copy of the gene encoding a highly conserved histone H2A variant of the H2A. F/Z typeNucleic Acids Research, 1988
- Histone variants specific to the transcriptionally active, amitotically dividing macronucleus of the unicellular eucaryote, tetrahymena thermophilaCell, 1980