Discover Community Create You

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

Article

Structure-guided functional suppression of AML-associated DNMT3A hotspot mutations.

Nature communications - 10 Apr 2024

Lu Jiuwei, Guo Yiran, Yin Jiekai, Chen Jianbin, Wang Yinsheng, Wang Gang Greg, Song Jikui

Abstract excerpt

DNA methyltransferases DNMT3A- and DNMT3B-mediated DNA methylation critically regulate epigenomic and transcriptomic patterning during development. The hotspot DNMT3A mutations at the site of Arg822 (R882) promote polymerization, leading to aberrant DNA methylation that may contribute to the pathogenesis of acute myeloid leukemia (AML). However, the molecular basis underlying the mutation-induced functional...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to DNA
Share to DNA (Cytosine-5-)-Methyltransferases
Share to DNA Methylation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Methyltransferase 3A

Share to Leukemia, Myeloid, Acute

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 38600075
DOI: 10.1038/s41467-024-47398-y
PMCID: PMC11006857

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structure-guided functional suppression of AML-associated DNMT3A hotspot mutations.PMID 38600075Read ↗

Structural basis for impairment of DNA methylation by the DNMT3A R882H mutation.Semantic proximity Read ↗

The R882H DNMT3A hot spot mutation stabilizes the formation of large DNMT3A oligomers with low DNA methyltransferase activitySemantic proximity Read ↗

The R882H DNMT3A mutation associated with AML dominantly inhibits wild-type DNMT3A by blocking its ability to form active tetramers.Semantic proximity Read ↗

AML-Associated Mutations in DNA Methyltransferase DNMT3A.Semantic proximity Read ↗

Structural basis for DNMT3A-mediated de novo DNA methylation.Semantic proximity Read ↗

The acute myeloid leukemia variant DNMT3A Arg882His is a DNMT3B-like enzyme.Semantic proximity Read ↗

Structural insight into hierarchical DNMT3A autoinhibition and its dysregulation in disease.Semantic proximity Read ↗

Mutations in DNA Methyltransferase (DNMT3A) Observed in Acute Myeloid Leukemia Patients Disrupt Processive MethylationSemantic proximity Read ↗

Significance of targeting DNMT3A mutations in AML.Semantic proximity Read ↗

Comprehensive structure-function characterization of DNMT3B and DNMT3A reveals distinctive de novo DNA methylation mechanisms.Semantic proximity Read ↗

Mutations in the DNMT3A DNA methyltransferase in acute myeloid leukemia patients cause both loss and gain of function and differential regulation by protein partnersSemantic proximity Read ↗

Structure of DNMT3B homo-oligomer reveals vulnerability to impairment by ICF mutations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.