PDB/2QRV[Secondary Source ID] - Search Results

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The R882H substitution in the human de novo DNA methyltransferase DNMT3A disrupts allosteric regulation by the tumor supressor p53.

Sandoval JE, Reich NO. Sandoval JE, et al. J Biol Chem. 2019 Nov 29;294(48):18207-18219. doi: 10.1074/jbc.RA119.010827. Epub 2019 Oct 22. J Biol Chem. 2019. PMID: 31640986 Free PMC article.

Mutations in the DNMT3A DNA methyltransferase in acute myeloid leukemia patients cause both loss and gain of function and differential regulation by protein partners.

Sandoval JE, Huang YH, Muise A, Goodell MA, Reich NO. Sandoval JE, et al. J Biol Chem. 2019 Mar 29;294(13):4898-4910. doi: 10.1074/jbc.RA118.006795. Epub 2019 Jan 31. J Biol Chem. 2019. PMID: 30705090 Free PMC article.

The R882H DNMT3A hot spot mutation stabilizes the formation of large DNMT3A oligomers with low DNA methyltransferase activity.

Nguyen TV, Yao S, Wang Y, Rolfe A, Selvaraj A, Darman R, Ke J, Warmuth M, Smith PG, Larsen NA, Yu L, Zhu P, Fekkes P, Vaillancourt FH, Bolduc DM. Nguyen TV, et al. J Biol Chem. 2019 Nov 8;294(45):16966-16977. doi: 10.1074/jbc.RA119.010126. Epub 2019 Oct 3. J Biol Chem. 2019. PMID: 31582562 Free PMC article.

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