Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Scientific reports 5 (2015), 13813. URL http://dx.doi.org./10.1038/srep13813
- Classification
-
Biowissenschaften, Biologie
- Keyword
-
Enzym ; Proteine
- Event
-
Veröffentlichung
- (where)
-
Stuttgart
- (who)
-
Universitätsbibliothek der Universität Stuttgart
- (when)
-
2015
- Contributor
- URN
-
urn:nbn:de:bsz:93-opus-103860
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:48 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
- Kusevic, Denis
- Kudithipudi, Srikanth
- Jeltsch, Albert
- Universitätsbibliothek der Universität Stuttgart
Time of origin
- 2015
Other Objects (12)
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Structure, activity and function of the NSD3 protein lysine methyltransferase
Histone lysine methylation in the context of nuclear architecture
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Mechanistic insights into the allosteric regulation of the Clr4 protein lysine methyltransferase by autoinhibition and automethylation
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Quantitative profile of lysine methylation and acetylation of histones by LC-MS/MS
Identification of protein lysine methylation readers with a yeast three-hybrid approach
Site-specific RNA methylation by a methyltransferase ribozyme
Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues
Structure, activity and function of the NSD3 protein lysine methyltransferase
Histone lysine methylation in the context of nuclear architecture
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Mechanistic insights into the allosteric regulation of the Clr4 protein lysine methyltransferase by autoinhibition and automethylation
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Quantitative profile of lysine methylation and acetylation of histones by LC-MS/MS
Identification of protein lysine methylation readers with a yeast three-hybrid approach
Site-specific RNA methylation by a methyltransferase ribozyme
Distinct specificities of the HEMK2 protein methyltransferase in methylation of glutamine and lysine residues
Structure, activity and function of the NSD3 protein lysine methyltransferase
Histone lysine methylation in the context of nuclear architecture
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Mechanistic insights into the allosteric regulation of the Clr4 protein lysine methyltransferase by autoinhibition and automethylation
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Regulation of DNA methylation during development : alternative isoforms of DNA methyltransferase
Modes of Interaction of KMT2 Histone H3 Lysine 4 Methyltransferase/COMPASS Complexes with Chromatin
Quantitative profile of lysine methylation and acetylation of histones by LC-MS/MS
Identification of protein lysine methylation readers with a yeast three-hybrid approach