A. Jeltsch, P. Bashtrykov, and S. Adam. Dataset, (2020)Related to: Sabrina Adam, Hiwot Anteneh, Maximilian Hornisch, Vincent Wagner, Jiuwei Lu, Nicole E. Radde, Pavel Bashtrykov, Jikui Song, Albert Jeltsch (2020) DNA sequence-dependent activity and base flipping mechanisms of DNMT1 regulate genome-wide DNA methylation. Nat Commun. 11(1):3723. doi: 10.1038/s41467-020-17531-8.
A. Jeltsch, P. Bashtrykov, and S. Adam. Dataset, (2021)Related to: Adam et al.: Flanking sequences influence the activity of TET1 and TET2 methylcytosine dioxygenases and affect genomic 5hmC patterns. Communications Biology, 5:92 (2022). doi: 10.1038/s42003-022-03033-4.
A. Jeltsch, P. Bashtrykov, and S. Adam. Dataset, (2023)Related to: Sabrina Adam, Viviane Klingel, Nicole E Radde, Pavel Bashtrykov, Albert Jeltsch (2023) On the accuracy of the epigenetic copy machine: comprehensive specificity analysis of the DNMT1 DNA methyltransferase. Nucleic Acids Research, gkad465. doi: 10.1093/nar/gkad465.
A. Jeltsch, P. Bashtrykov, and S. Adam. Dataset, (2020)Related to: Sabrina Adam, Hiwot Anteneh, Maximilian Hornisch, Vincent Wagner, Jiuwei Lu, Nicole E. Radde, Pavel Bashtrykov, Jikui Song, Albert Jeltsch: DNA sequence-dependent activity and base flipping mechanisms of DNMT1 regulate genome-wide DNA methylation. Nat Commun. 2020 Jul 24;11(1):3723. doi: 10.1038/s41467-020-17531-8.
A. Jeltsch, P. Bashtrykov, S. Adam, and S. Kunert. Dataset, (2021)Related to: Emperle M, Bangalore DM, Adam S, Kunert S, Heil HS, Heinze KG, Bashtrykov P, Tessmer I, Jeltsch A. Structural and biochemical insight into the mechanism of dual CpG site binding and methylation by the DNMT3A DNA methyltransferase. Nucleic Acids Res,Volume 49, Issue 14, 20 August 2021, Pages 8294-8308. doi: 10.1093/nar/gkab600.
A. Jeltsch, P. Bashtrykov, S. Adam, A. Mack, and M. Emperle. Dataset, (2021)Related to: Alexandra Mack, Max Emperle, Philipp Schnee, Sabrina Adam, Jürgen Pleiss, Pavel Bashtrykov, & Albert Jeltsch: Preferential interaction of DNMT3A subunits containing the R882H cancer mutation leads to dominant changes of flanking sequence effects. Submitted for publication.
A. Jeltsch, P. Bashtrykov, and C. Albrecht. Dataset, (2024)Related to: Albrecht, C.; Rajaram, N.; Broche, J.; Bashtrykov, P.; Jeltsch, A. Locus specific and stable DNA demethylation at the H19/IGF2 ICR1 by epigenome editing using a dCas9-SunTag system and the catalytic domain of TET1. Genes 2024, 15(1), 80. doi: 10.3390/genes15010080.
A. Jeltsch, P. Bashtrykov, A. Bröhm, M. Dukatz, and S. Adam. Dataset, (2021)Related to: Bröhm et al., Methylation of recombinant mononucleosomes by DNMT3A demonstrates efficient linker DNA methylation and a role of H3K36me3. Commun. Biol. 5(1):192, 2022. doi: 10.1038/s42003-022-03119-z.
A. Jeltsch, P. Bashtrykov, L. Dossmann, and M. Emperle. Dataset, (2024)Related to: Dossmann L, Emperle M, Dukatz M, de Mendoza A, Bashtrykov P, Jeltsch A. Specific DNMT3C flanking sequence preferences facilitate methylation of young murine retrotransposons. Communications Biology 7:582 (2024). doi: 10.1038/s42003-024-06252-z.
A. Jeltsch, P. Bashtrykov, M. Dukatz, and S. Adam. Dataset, (2022)Related to: Dukatz et al.: "DNA methyltransferase DNMT3A forms interaction networks with the CpG site and flanking sequence elements for efficient methylation", Journal of Biological Chemistry, 2022. doi: 10.1016/j.jbc.2022.102462.
A. Jeltsch, P. Bashtrykov, M. Dukatz, and S. Adam. Dataset, (2020)Related to: Michael Dukatz, Sabrina Adam, Mahamaya Biswal, Jikui Song, Pavel Bashtrykov, & Albert Jeltsch: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase. Nucleic Acids Res. 2020 Nov 18;48(20):11495-11509. doi: 10.1093/nar/gkaa938.
A. Jeltsch, P. Bashtrykov, M. Emperle, S. Adam, and M. Dukatz. Dataset, (2020)Related to: Linfeng Gao, Max Emperle, Hidetaka Uryu, Sara A Grimm, Wendan Ren, Sabrina Adam, Dongliang Chen, Zhi-Min Zhang, Yiran Guo, Jiekai Yin, Michael Dukatz, Hiwot Anteneh, Renata Z. Jurkowska, Jiuwei Lu, Yinsheng Wang, Pavel Bashtrykov, Paul A Wade, Gang Greg Wang, Albert Jeltsch, Jikui Song. Comprehensive structure-function characterization of DNMT3B and DNMT3A reveals distinctive de novo DNA methylation mechanisms. Nat Commun. 2020 Jul 3;11(1):3355. doi: 10.1038/s41467-020-17109-4.
A. Jeltsch, P. Bashtrykov, and N. Rajaram. Dataset, (2023)Related to: Rajaram N, Kouroukli AG, Bens S, Bashtrykov P, Jeltsch A. (2023) Development of super-specific epigenome editing by targeted allele-specific DNA methylation. Epigenetics & Chromatin 16, 41. doi: 10.1186/s13072-023-00515-5.
A. Jeltsch, and J. Broche. Dataset, (2023)Related to: Broche et al., Genome-wide deposition of 6-methyladenine in human DNA reduces the viability of HEK293 cells and directly influences gene expression, Communications Biology, in press.
A. Jeltsch, P. Schnee, M. Khella, S. Weirich, J. Pleiss, and P. Bashtrykov. Software, (2023)Related to: Mina S. Khella, Philipp Schnee, Sara Weirich, Tan Bui, Alexander Bröhm, Pavel Bashtrykov, Jürgen Pleiss, Albert Jeltsch: The T1150A cancer mutant of the protein lysine methyltransferase NSD2 can introduce H3K36 trimethylation. J Biol Chem, 2023, 5, 104796. doi: 10.1016/j.jbc.2023.104796.
A. Jeltsch, P. Schnee, and J. Pleiss. Software, (2022)Related to: Philipp Schnee, Michel Choudalakis, Sara Weirich, Mina S. Khella, Henrique Carvalho, Jürgen Pleiss & Albert Jeltsch (2022) Mechanistic basis of the increased methylation activity of the SETD2 protein lysine methyltransferase towards a designed super-substrate peptide. Communications Chemistry, 5, 139. doi: 10.1038/s42004-022-00753-w.
A. Jeltsch, P. Schnee, and J. Pleiss. Software, (2022)Related to: Alexandra Mack, Max Emperle, Philipp Schnee, Sabrina Adam, Jürgen Pleiss, Pavel Bashtrykov, & Albert Jeltsch: Preferential interaction of DNMT3A subunits containing the R882H cancer mutation leads to dominant changes of flanking sequence effects. Submitted for publication.
A. Jeltsch, P. Schnee, J. Pleiss, and S. Weirich. Software, (2024)Related to: Weirich S, Kusevic D, Schnee P, Reiter J, Pleiss J & Jeltsch A. Discovery of new NSD2 non-histone substrates and design of a super-substrate. Communications Biology 7:707 (2024). doi: 10.1038/s42003-024-06395-z.