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To discover small molecule inhibitors for EZH2 methyltransferase activity, we performed an inhibitor screen with catalytically active EZH2 protein complex and identified tanshindiols as EZH2 inhibitors.
Since EZH2 requires a binding partner for its histone methyltransferase activity, we surmised that evaluating interacting proteins might shed light on how the activity of EZH2 is regulated.
To evaluate how the NMR-mapped residues in METTL3 ZFD participate in methyltransferase activity, we introduced alanine mutations to residues 316 323.
To examine the mechanism underlying the discrepancy of intrinsic versus overall H3 K4 methyltransferase activity, we decided to perform SAM binding assays for Ash2L in the context of different MLL1SET mutants.
To determine which parts of DNMT1 are required for cellular methyltransferase activity, we generated a collection of cDNAs expressing DNMT1 mutants that differ from each other in the sequence of a stretch of amino acids (Table 1).
To test RM.Eco29kI DNA methyltransferase activity, we used DE-filters assay according to [ 35].
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To address this hypothesis and also to address the issue of other methyltransferase activities, we generated Icmt-deficient mice.
Because 5′-Aza-2′-DC inhibits methylation of CpG islands by inhibiting DNA methyltransferase (DNMT) activity, we used 5′-Aza-2′-DC to treat HBx-transfected SMMC-7721 cells.
We assessed the methyltransferase activity for the heterodimer between METTL3 (including both the ZFD and MTD, and spanning residues 259 580) and METTL14.
To explore the underlying regulatory mechanism of METTL3 on JAK2 and SOSC3 expression, we tested whether the methyltransferase activity of METTL3 is required.
Given the reported presence of a SET domain independent methyltransferase activity in the MLL1 core complex [18], we tested whether RbBP5 and Ash2L possess intrinsic histone methyltransferase activity.
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