The lysine‐specific methyltransferase KMT 2C/MLL 3 regulates DNA repair components in cancer
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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The lysine‐specific methyltransferase KMT 2C/MLL 3 regulates DNA repair components in cancer ; volume:20 ; number:3 ; year:2019 ; extent:20
EMBO reports / European Molecular Biology Organization ; 20, Heft 3 (2019) (gesamt 20)
- Creator
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Rampias, Theodoros
Karagiannis, Dimitris
Avgeris, Margaritis
Polyzos, Alexander
Kokkalis, Antonis
Kanaki, Zoi
Kousidou, Evgenia
Tzetis, Maria
Kanavakis, Emmanouil
Stravodimos, Konstantinos
Manola, Kalliopi N.
Pantelias, Gabriel E.
Scorilas, Andreas
Klinakis, Apostolos
- DOI
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10.15252/embr.201846821
- URN
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urn:nbn:de:101:1-2022073007210841128533
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:22 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
- Rampias, Theodoros
- Karagiannis, Dimitris
- Avgeris, Margaritis
- Polyzos, Alexander
- Kokkalis, Antonis
- Kanaki, Zoi
- Kousidou, Evgenia
- Tzetis, Maria
- Kanavakis, Emmanouil
- Stravodimos, Konstantinos
- Manola, Kalliopi N.
- Pantelias, Gabriel E.
- Scorilas, Andreas
- Klinakis, Apostolos
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Structure, activity and function of the NSD3 protein lysine methyltransferase
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Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase
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WTZ MLL
Targeting the histone H3 lysine 79 methyltransferase DOT1L in MLL-rearranged leukemias
Lysine methyltransferase SMYD2 promotes triple negative breast cancer progression
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Charakterisierung der DNA-Bindung durch die Methyltransferase (MT-)-Homologiedomäne des Protoonkoproteins MLL
Structure, activity and function of the NSD3 protein lysine methyltransferase
The emerging role of lysine methyltransferase SETD8 in human diseases
Lysine-specific methyltransferase Set7/9 in stemness, differentiation, and development
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase
Histone lysine methyltransferase Pr‐set7/SETD8 promotes neural stem cell reactivation
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase
WTZ MLL
Targeting the histone H3 lysine 79 methyltransferase DOT1L in MLL-rearranged leukemias
Lysine methyltransferase SMYD2 promotes triple negative breast cancer progression
Why are so many MLL lysine methyltransferases required for normal mammalian development?
Charakterisierung der DNA-Bindung durch die Methyltransferase (MT-)-Homologiedomäne des Protoonkoproteins MLL
Structure, activity and function of the NSD3 protein lysine methyltransferase
The emerging role of lysine methyltransferase SETD8 in human diseases
Lysine-specific methyltransferase Set7/9 in stemness, differentiation, and development
Assay development and inhibitor optimization for the histone lysine methyltransferase KMT9
Discovery of an Allosteric Ligand Binding Site in SMYD3 Lysine Methyltransferase
Histone lysine methyltransferase Pr‐set7/SETD8 promotes neural stem cell reactivation
Investigation of the methylation of Numb by the SET8 protein lysine methyltransferase