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Robertson, K.D., Ait-Si-Ali, S., Yokochi, T., Wade, P.A., Jones, P.L. and Wolffe, A.P. (2000) DNMT1 Forms a Complex with Rb, E2F1 and HDAC1 and Represses Transcription from E2F-Responsive Promoters. Nature Genetics, 25, 338-342.
http://dx.doi.org/10.1038/77124

has been cited by the following article:

• TITLE: DNA Methyltransferases Directed Anti-Cancerous Plant Medicine (Xanthomicrol and Galloyl) Based Molecular Docking and Dynamics Simulation

  AUTHORS: Ehsan Heidari Soureshjani, Ali Kazemi Babaheydari, Elahe Saberi

  KEYWORDS: DNA Methyltransferases 1, Decitabine, Molecular Dynamics, Galloyl, Xanthomicrol

  JOURNAL NAME: Computational Molecular Bioscience, Vol.5 No.2, June 30, 2015

  ABSTRACT: DNA methyltransferases 1 (DNMT1) has been looked as crucial targets against various types of cancers. MD simulations have advanced to a point where the atomic level information of biological macromolecule (protein or DNA-protein or protein-protein) can easily be advantageous to predict the functionality. In this study we utilize xanthomicrol and galloyl compounds to investigate potential compounds for the inhibition of DNMT1, and the results of these two compounds are compared with drug decitabine. Xanthomicrol and galloyl are found to dock successfully within the active site of DNMT1. A comparison of the inhibitory potential of screened xanthomicrol inhibited DNMT1 approximately is identical with those of their corresponding drugs, decitabine. The stability of the DNMT1 with the best docked xanthomicrol, were further analysed in molecular dynamics (MD) simulation and compared with those of the respective drugs namely decitabine which revealed stabilization of these complexes within 300 ns of simulation with better stability of DNMT1.