- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
1868-7083
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
Clinicopathologic significance of protein lysine methyltransferases in cancer ; volume:12 ; number:1 ; day:13 ; month:10 ; year:2020 ; pages:1-19 ; date:12.2020
Clinical epigenetics ; 12, Heft 1 (13.10.2020), 1-19, 12.2020
- Creator
-
Vougiouklakis, Theodore
Bernard, Benjamin J.
Nigam, Nupur
Burkitt, Kyunghee
Nakamura, Yusuke
Saloura, Vassiliki
- Contributor
-
SpringerLink (Online service)
- DOI
-
10.1186/s13148-020-00897-3
- URN
-
urn:nbn:de:101:1-2020112820534079400915
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:33 AM CEST
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
- Vougiouklakis, Theodore
- Bernard, Benjamin J.
- Nigam, Nupur
- Burkitt, Kyunghee
- Nakamura, Yusuke
- Saloura, Vassiliki
- SpringerLink (Online service)
Other Objects (12)
Enzymatic characterization of protein lysine methyltransferases
Lysine Ethylation by Histone Lysine Methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Novel pharmacological maps of protein lysine methyltransferases: key for target deorphanization
Structure, activity and function of the Suv39h1 and Suv39h2 protein lysine methyltransferases
Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Enzymatic characterization of protein lysine methyltransferases
Lysine Ethylation by Histone Lysine Methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Novel pharmacological maps of protein lysine methyltransferases: key for target deorphanization
Structure, activity and function of the Suv39h1 and Suv39h2 protein lysine methyltransferases
Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Enzymatic characterization of protein lysine methyltransferases
Lysine Ethylation by Histone Lysine Methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Identifying Novel Substrates by Specificity Profile Analysis of Protein Lysine Methyltransferases
Biochemical characterization and identification of novel substrates of protein lysine methyltransferases
Novel pharmacological maps of protein lysine methyltransferases: key for target deorphanization
Structure, activity and function of the Suv39h1 and Suv39h2 protein lysine methyltransferases
Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases
Biochemical characterization of protein lysine methyltransferases-regulation, specificity and effect of somatic cancer mutants