MDC1 methylation mediated by lysine methyltransferases EHMT1 and EHMT2 regulates active ATM accumulation flanking DNA damage sites
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2045-2322
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
online resource.
- Bibliographic citation
-
MDC1 methylation mediated by lysine methyltransferases EHMT1 and EHMT2 regulates active ATM accumulation flanking DNA damage sites ; volume:8 ; number:1 ; day:18 ; month:7 ; year:2018 ; pages:1-10 ; date:12.2018
Scientific reports ; 8, Heft 1 (18.7.2018), 1-10, 12.2018
- Classification
-
Biowissenschaften, Biologie
- Creator
-
Watanabe, Sugiko
- Contributor
-
Iimori, Makoto
Chan, David Virya
Hara, Eiji
Kitao, Hiroyuki
Maehara, Yoshihiko
SpringerLink (Online service)
- DOI
-
10.1038/s41598-018-29239-3
- URN
-
urn:nbn:de:101:1-2018092022124246085569
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:37 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
- Watanabe, Sugiko
- Iimori, Makoto
- Chan, David Virya
- Hara, Eiji
- Kitao, Hiroyuki
- Maehara, Yoshihiko
- SpringerLink (Online service)
Other Objects (12)
Lysine Ethylation by Histone Lysine Methyltransferases
Enzymatic characterization of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
DNA methylation and DNA methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Clinicopathologic significance of protein lysine methyltransferases in cancer
Fine-tuning of lysine side chain modulates the activity of histone lysine 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
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Lysine Ethylation by Histone Lysine Methyltransferases
Enzymatic characterization of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
DNA methylation and DNA methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Clinicopathologic significance of protein lysine methyltransferases in cancer
Fine-tuning of lysine side chain modulates the activity of histone lysine 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
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Lysine Ethylation by Histone Lysine Methyltransferases
Enzymatic characterization of protein lysine methyltransferases
Characterization of novel histone lysine mono-methyltransferases
Tumor-suppressive functions of protein lysine methyltransferases
DNA methylation and DNA methyltransferases
Investigation of the specificity of protein lysine methyltransferases
Clinicopathologic significance of protein lysine methyltransferases in cancer
Fine-tuning of lysine side chain modulates the activity of histone lysine 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