A direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases

@article{Guitot2017ADL,
  title={A direct label-free MALDI-TOF mass spectrometry based assay for the characterization of inhibitors of protein lysine methyltransferases},
  author={Karine Guitot and Thierry Drujon and Fabienne Burlina and Sandrine Sagan and Sandra Beaupierre and Olivier Pamlard and Robert H Dodd and Catherine Guillou and G{\'e}rard Bolbach and Emmanuelle Sachon and Dominique Guianvarc'h},
  journal={Analytical and Bioanalytical Chemistry},
  year={2017},
  volume={409},
  pages={3767-3777}
}
Histone lysine methylation is associated with essential biological functions like transcription activation or repression, depending on the position and the degree of methylation. This post-translational modification is introduced by protein lysine methyltransferases (KMTs) which catalyze the transfer of one to three methyl groups from the methyl donor S-adenosyl-l-methionine (AdoMet) to the amino group on the side chain of lysines. The regulation of protein lysine methylation plays a primary… Expand
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