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

Dissection of structure and function of the N-terminal domain of mouse DNMT1 using regional frame-shift mutagenesis.

PloS one - 23 Mar 2010

D'Aiuto Leonardo, Marzulli Marco, Mohan K Naga, Borowczyk Ewa, Saporiti Federica, Vandemark Andrew, Chaillet J Richard

Abstract excerpt

Deletion analysis of mouse DNMT1, the primary maintenance methyltransferase in mammals, showed that most of the N-terminal regulatory domain (amino acid residues 412-1112) is required for its enzymatic activity. Although analysis of deletion mutants helps to identify regions of a protein sequence required for a particular activity, amino acid deletions can have drastic effects on protein structure and/or...

Read the complete abstract on PubMed

Topics

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

Share to DNA, Complementary
Share to DNA (Cytosine-5-)-Methyltransferase 1

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to DNA (Cytosine-5-)-Methyltransferases

Share to Embryonic Stem Cells

Share to Frameshift Mutation

Share to Mutagenesis

Share to Mutagenesis, Site-Directed

Share to Protein Folding

Source

Open in PubMed Open full text

Identifiers

PMID: 20352123
DOI: 10.1371/journal.pone.0009831
PMCID: PMC2843745

Genes

DNMT1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dissection of structure and function of the N-terminal domain of mouse DNMT1 using regional frame-shift mutagenesis.PMID 20352123Read ↗

Mouse DNA methyltransferase (MTase) deletion mutants that retain the catalytic domain display neither de novo nor maintenance methylation activity in vivo.Semantic proximity Read ↗

Identification of a region of the DNMT1 methyltransferase that regulates the maintenance of genomic imprints.Semantic proximity Read ↗

Disease-Associated Mutations G589A and V590F Relieve Replication Focus Targeting Sequence-Mediated Autoinhibition of DNA Methyltransferase 1.Semantic proximity Read ↗

Crystal Structure of Human DNA Methyltransferase 1.Semantic proximity Read ↗

Using human disease mutations to understand de novo DNA methyltransferase function.Semantic proximity Read ↗

Major and essential role for the DNA methylation mark in mouse embryogenesis and stable association of DNMT1 with newly replicated regions.Semantic proximity Read ↗

Site-directed mutagenesis of mouse thymidylate synthase: alteration of Arg44 to Val44 in a conserved loop guarding the active site has striking effects on catalysis and nucleotide binding.Semantic proximity Read ↗

DNMT1 but not its interaction with the replication machinery is required for maintenance of DNA methylation in human cells.Semantic proximity Read ↗

Allosteric activator domain of maintenance human DNA (cytosine-5) methyltransferase and its role in methylation spreading.Semantic proximity Read ↗

Deficiency in a glutamine-specific methyltransferase for release factor causes mouse embryonic lethality.Semantic proximity Read ↗

Structural basis for substrate recognition by the human N-terminal methyltransferase 1.Semantic proximity Read ↗

Structural basis for activation of DNMT1Semantic proximity Read ↗

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