801 to 810 of 850 Results
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 15.2 MB -
MD5: eaffc720c83d51a0e58b16522c61838a
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 15.0 MB -
MD5: 96ee894dbc6909dce97ae740b009936f
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 13.3 MB -
MD5: b43754e5779e36d566d8361578ddc377
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 12.5 MB -
MD5: cd6de1453f57c2d4bb3342947fb6bc34
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 11.2 MB -
MD5: d42704b83063e6e40cae05a5cb076fb0
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 15.0 MB -
MD5: fc2fcb757de4ed53040ddf013be25311
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 14.1 MB -
MD5: c4c63430ab2a66e40753a1427c1a17c0
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 16.9 MB -
MD5: 1bcd220c1e7250d3a92ecc8705b0167b
|
Jun 18, 2020 -
Deep enzymology data related to Dukatz et al.: Complex DNA sequence readout mechanisms of the DNMT3B DNA methyltransferase.
Plain Text - 15.8 MB -
MD5: a45369e148334f7c9fc784d9d890ccf5
|
Jan 30, 2020 - Amplicon based bisulfite NGS data
Jeltsch, Albert; Bashtrykov, Pavel; Emperle, Max; Adam, Sabrina; Dukatz, Michael, 2020, "Deep enzymology data related to Gao et al.: Comprehensive structure-function characterization of DNMT3B and DNMT3A reveals distinctive de novo DNA methylation mechanisms", https://doi.org/10.18419/DARUS-627, DaRUS, V1
Experimental procedures: Libraries of double stranded DNA substrates with CpG, CpH or CpN sites in randomized sequence context were methlyated by DNMT3A or DNMT3B. Reactions were stopped by shock freezing in liquid nitrogen, then treated with proteinase K for 2 hours. Afterwards, the DNA was digested with the BsaI-HFv2 enzyme and a hairpin was liga... |