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Biochemistry|November 9, 2005
Mechanism of allosteric regulation of Dnmt1's processivityZeljko M Svedruzić, Norbert O Reich
Biochimica Et Biophysica Acta|February 15, 2015
De novo DNA methyltransferase DNMT3A: Regulation of oligomeric state and mechanism of action in response to pH changesCeleste Holz-Schietinger, Norbert O Reich
The Journal of Biological Chemistry|November 11, 2020
p53 and TDG are dominant in regulating the activity of the human de novo DNA methyltransferase DNMT3A on nucleosomesJonathan E Sandoval, Norbert O Reich
The Journal of Biological Chemistry|June 24, 2004
Simultaneous DNA binding, bending, and base flipping: evidence for a novel M.EcoRI methyltransferase-DNA complexBen B Hopkins, Norbert O Reich
The Journal of Biological Chemistry|July 16, 2010
The inherent processivity of the human de novo methyltransferase 3A (DNMT3A) is enhanced by DNMT3LCeleste Holz-Schietinger, Norbert O Reich
The Journal of Biological Chemistry|October 24, 2019
The R882H substitution in the human de novo DNA methyltransferase DNMT3A disrupts allosteric regulation by the tumor supressor p53Jonathan E Sandoval, Norbert O Reich
Nucleic Acids Research|June 26, 2012
RNA modulation of the human DNA methyltransferase 3ACeleste Holz-Schietinger, Norbert O Reich
The Journal of Biological Chemistry|May 8, 2009
Escherichia coli DNA adenine methyltransferase: the structural basis of processive catalysis and indirect read-outStephanie R Coffin, Norbert O Reich
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