Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1756-8935
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3 ; volume:9 ; number:1 ; day:30 ; month:4 ; year:2016 ; pages:1-14 ; date:12.2016
Epigenetics & chromatin ; 9, Heft 1 (30.4.2016), 1-14, 12.2016
- Creator
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Hainer, Sarah J.
- Contributor
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Martens, Joseph A.
SpringerLink (Online service)
- DOI
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10.1186/s13072-016-0066-4
- URN
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urn:nbn:de:1111-201605041188
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:54 AM CEST
Data provider
This object is provided by:
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Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Hainer, Sarah J.
- Martens, Joseph A.
- SpringerLink (Online service)
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The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats
Dynamic networks observed in the nucleosome core particles couple the histone globular domains with DNA
Dot1 regulates nucleosome dynamics by its inherent histone chaperone activity in yeast
Accessibility of the histone H3 tail in the nucleosome for binding of paired readers
Functional characterization of histone modifications : H3K64 acetylation ; a novel histone modification on the H3 globular domain
A systematic analysis of nucleosome core particle and nucleosome-nucleosome stacking structure
Extragalactic globular cluster systems
Extragalactic globular cluster systems
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Structural and biochemical analyses of the nuclear pore complex component ELYS identify residues responsible for nucleosome binding
Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin