Structural basis for histone H3 acetylation by Rtt109 in complex with histone chaperones Asf1 and Vps75
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Hannover, Gottfried Wilhelm Leibniz Universität Hannover, Dissertation, 2020
- Keyword
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Acetylation
- Event
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Veröffentlichung
- (where)
-
Hannover
- (who)
-
Gottfried Wilhelm Leibniz Universität Hannover
- (when)
-
2020
- Creator
-
Danilenko, Nataliya
- DOI
-
10.15488/9776
- URN
-
urn:nbn:de:101:1-2020043002382613966348
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:49 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Danilenko, Nataliya
- Gottfried Wilhelm Leibniz Universität Hannover
Time of origin
- 2020
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From histones to chromosomes : in vivo and in vitro analysis of structural changes caused by linker histone H1, histone acetylation and histone chaperone NAP1
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Involvement of histone acetylation in neuroprotection against brain ischemic injury
Functional characterization of histone modifications : H3K64 acetylation ; a novel histone modification on the H3 globular domain
Nitric oxide affects histone acetylation by inhibiting histone deacetylase activity in Arabidopsis
Histone acetylation and histone acetyltransferases show significant alterations in human abdominal aortic aneurysm
Histone acetylation and expression of corresponding histone actyltransferases in human abdominal aortic aneurysm
From histones to chromosomes : in vivo and in vitro analysis of structural changes caused by linker histone H1, histone acetylation and histone chaperone NAP1
Structural characterization of the Asf1-Rtt109 interaction and its role in histone acetylation
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