Interaction of DNA Methyltransferase Dnmt3a with Phosphorus Analogs of S-Adenosylmethionine and S-Adenosylhomocysteine
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource, 1 online resource.
- Language
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Englisch
- Bibliographic citation
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Interaction of DNA Methyltransferase Dnmt3a with Phosphorus Analogs of S-Adenosylmethionine and S-Adenosylhomocysteine ; volume:57 ; number:4 ; day:8 ; month:8 ; year:2023 ; pages:747-754 ; date:8.2023
Molecular biology ; 57, Heft 4 (8.8.2023), 747-754, 8.2023
- Creator
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Filonov, V. L.
Khomutov, M. A.
Sergeev, A. V.
Khandazhinskaya, A. L.
Kochetkov, S. N.
Gromova, E. S.
Khomutov, A. R.
- Contributor
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SpringerLink (Online service)
- DOI
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10.1134/S0026893323040064
- URN
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urn:nbn:de:101:1-2023110208523525087739
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
14.08.2025, 11:02 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
- Filonov, V. L.
- Khomutov, M. A.
- Sergeev, A. V.
- Khandazhinskaya, A. L.
- Kochetkov, S. N.
- Gromova, E. S.
- Khomutov, A. R.
- SpringerLink (Online service)
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Quaternary structure and regulation of mammalian DNA methyltransferase 3a (Dnmt3a)
DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation
Conserved motif VIII of murine DNA methyltransferase Dnmt3a is essential for methylation activity
Role of DNA methyltransferase 3A (DNMT3A) in intestinal epithelial cells during homeostasis and inflammation
Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction
The inhibition of the mammalian DNA methyltransferase 3a (Dnmt3a) by dietary black tea and coffee polyphenols
The methyltransferase domain of DNMT1 is an essential domain in acute myeloid leukemia independent of DNMT3A mutation
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Mechanistic study on the DNA methyltransferase DNMT3A
Mechanistic study on the DNA methyltransferase DNMT3A
Protein design of the mammalian DNA methyltransferase Dnmt3a
Quaternary structure and regulation of mammalian DNA methyltransferase 3a (Dnmt3a)
DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation
Conserved motif VIII of murine DNA methyltransferase Dnmt3a is essential for methylation activity
Role of DNA methyltransferase 3A (DNMT3A) in intestinal epithelial cells during homeostasis and inflammation
Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction
The inhibition of the mammalian DNA methyltransferase 3a (Dnmt3a) by dietary black tea and coffee polyphenols
The methyltransferase domain of DNMT1 is an essential domain in acute myeloid leukemia independent of DNMT3A mutation
On the role of DNA methyltransferase 3A (DNMT3A) in myeloid cells in intestinal homeostasis and inflammatory responses
Studies of interaction proteins controlling DNA methyltransferase 1
Mechanistic study on the DNA methyltransferase DNMT3A
Mechanistic study on the DNA methyltransferase DNMT3A
Protein design of the mammalian DNA methyltransferase Dnmt3a
Quaternary structure and regulation of mammalian DNA methyltransferase 3a (Dnmt3a)
DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation
Conserved motif VIII of murine DNA methyltransferase Dnmt3a is essential for methylation activity
Role of DNA methyltransferase 3A (DNMT3A) in intestinal epithelial cells during homeostasis and inflammation
Structural basis for the H2AK119ub1-specific DNMT3A-nucleosome interaction
The inhibition of the mammalian DNA methyltransferase 3a (Dnmt3a) by dietary black tea and coffee polyphenols
The methyltransferase domain of DNMT1 is an essential domain in acute myeloid leukemia independent of DNMT3A mutation
On the role of DNA methyltransferase 3A (DNMT3A) in myeloid cells in intestinal homeostasis and inflammatory responses