Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
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In: ChemBioChem 21 (2020), pp. 256-264
- Event
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Veröffentlichung
- (where)
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Stuttgart
- (who)
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Universitätsbibliothek der Universität Stuttgart
- (when)
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2019
- Creator
-
Weirich, Sara
Schuhmacher, Maren Kirstin
Kudithipudi, Srikanth
Lungu, Cristiana
Ferguson, Andrew D.
Jeltsch, Albert
- DOI
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10.18419/opus-10720
- URN
-
urn:nbn:de:bsz:93-opus-ds-107378
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:46 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
- Weirich, Sara
- Schuhmacher, Maren Kirstin
- Kudithipudi, Srikanth
- Lungu, Cristiana
- Ferguson, Andrew D.
- Jeltsch, Albert
- Universitätsbibliothek der Universität Stuttgart
Time of origin
- 2019
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Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Characterization of histone lysine demethylation
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Investigation of the specificity of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Lysine Ethylation by Histone Lysine Methyltransferases
Characterization of the substrate specificity of the Dnmt2 methyltransferase
Histone lysine methylation in the context of nuclear architecture
Functional characterization of histone modifications : survey of novel histone modifications reveals PCMT1 as a new histone methyltransferase
Structure, activity and function of the NSD3 protein lysine methyltransferase
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
The histone 3 lysine 4 methyltransferase, Mll2, is only required briefly in development and spermatogenesis
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Characterization of histone lysine demethylation
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Investigation of the specificity of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Lysine Ethylation by Histone Lysine Methyltransferases
Characterization of the substrate specificity of the Dnmt2 methyltransferase
Histone lysine methylation in the context of nuclear architecture
Functional characterization of histone modifications : survey of novel histone modifications reveals PCMT1 as a new histone methyltransferase
Structure, activity and function of the NSD3 protein lysine methyltransferase
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase