Hochschulschrift
Investigation of the specificity of protein lysine methyltransferases
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Bremen, Jacobs Univ., Diss., 2013
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Bremen
- (who)
-
IRC-Library, Information Resource Center der Jacobs University Bremen
- (when)
-
2013
- Creator
-
Raafiq, Qazi Muhammad
- URN
-
urn:nbn:de:101:1-201307119383
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:52 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.
Object type
- Hochschulschrift
Associated
- Raafiq, Qazi Muhammad
- IRC-Library, Information Resource Center der Jacobs University Bremen
Time of origin
- 2013
Other Objects (12)
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
Molecular dynamics simulations of the substrate- and product specificity and mechanism of DNA- and protein lysine methyltransferases
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Investigation of proteins responsible for the establishment and recognition of prominent lysine modifications
Enzymatic characterization of protein lysine methyltransferases
Biochemical investigation of the substrate specificity of protein methyltransferases and the identification of novel substrates
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Structure, activity and function of the NSD3 protein lysine methyltransferase
Determining targeting specificity of nuclearly encoded organelle proteins
Characterization of histone lysine demethylation
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
Molecular dynamics simulations of the substrate- and product specificity and mechanism of DNA- and protein lysine methyltransferases
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Investigation of proteins responsible for the establishment and recognition of prominent lysine modifications
Enzymatic characterization of protein lysine methyltransferases
Biochemical investigation of the substrate specificity of protein methyltransferases and the identification of novel substrates
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Structure, activity and function of the NSD3 protein lysine methyltransferase
Determining targeting specificity of nuclearly encoded organelle proteins
Characterization of histone lysine demethylation
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
Molecular dynamics simulations of the substrate- and product specificity and mechanism of DNA- and protein lysine methyltransferases
Analysis of the substrate specificity of the SMYD2 protein lysine methyltransferase and discovery of novel non-histone substrates
Investigation of proteins responsible for the establishment and recognition of prominent lysine modifications
Enzymatic characterization of protein lysine methyltransferases
Biochemical investigation of the substrate specificity of protein methyltransferases and the identification of novel substrates
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Structure, activity and function of the NSD3 protein lysine methyltransferase
Determining targeting specificity of nuclearly encoded organelle proteins