Multidomain interaction governs the filamentous assembly of the dominant-negative DNMT3A R882H mutant.

doi:10.1073/pnas.2609226123

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Community

Back to search

Article

Multidomain interaction governs the filamentous assembly of the dominant-negative DNMT3A R882H mutant.

Proceedings of the National Academy of Sciences of the United States of America - 1 Sept 2026

Chen Jianbin, Lu Jiuwei, Long Zhixu, Yoon Sol, Fukunaga Megan, Song Jikui

Abstract excerpt

DNA methyltransferase DNMT3A-mediated de novo DNA methylation is important for proper regulation of gene expression and genomic stability in development. The DNMT3A R882H (DNMT3AR882H) mutation, a hot-spot mutation in acute myeloid leukemia and developmental disorders, exerts a dominant-negative effect in DNMT3A-mediated DNA methylation through promoting high-order protein assembly. However, due to the lack of...

Read the complete abstract on PubMed