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

Biochemical and mechanistic analysis of the cleavage of branched DNA by human ANKLE1.

Nucleic acids research - 23 Jun 2023

Freeman Alasdair D J, Déclais Anne-Cécile, Wilson Timothy J, Lilley David M J

Abstract excerpt

ANKLE1 is a nuclease that provides a final opportunity to process unresolved junctions in DNA that would otherwise create chromosomal linkages blocking cell division. It is a GIY-YIG nuclease. We have expressed an active domain of human ANKLE1 containing the GIY-YIG nuclease domain in bacteria, that is monomeric in solution and when bound to a DNA Y-junction, and unilaterally cleaves a cruciform junction. Using...

Read the complete abstract on PubMed

Topics

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

Share to DNA
Share to Endonucleases
Share to Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 37216589
DOI: 10.1093/nar/gkad416
PMCID: PMC10287932

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

Biochemical and mechanistic analysis of the cleavage of branched DNA by human ANKLE1.PMID 37216589Read ↗

A conserved loop-wedge motif moderates reaction site search and recognition by FEN1.Semantic proximity Read ↗

AP-endonuclease 1 sculpts DNA through an anchoring tyrosine residue on the DNA intercalating loop.Semantic proximity Read ↗

A Dynamic Search Mechanism Enables APE1 to Identify AP-Sites in DNASemantic proximity Read ↗

A unified genetic, computational and experimental framework identifies functionally relevant residues of the homing endonuclease I-BmoI.Semantic proximity Read ↗

Substrate preference of Gen endonucleases highlights the importance of branched structures as DNA damage repair intermediates.Semantic proximity Read ↗

Structural and biochemical basis for DNA and RNA catalysis by human Topoisomerase 3βSemantic proximity Read ↗

Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III.Semantic proximity Read ↗

Interaction interface of human flap endonuclease-1 with its DNA substrates.Semantic proximity Read ↗

Structural characterization of Class 2 OLD family nucleases supports a two-metal catalysis mechanism for cleavageSemantic proximity Read ↗

Novel DNA endonuclease activity of human ERK1 proteinSemantic proximity Read ↗

Role of a tryptophan anchor in human topoisomerase I structure, function and inhibition.Semantic proximity Read ↗

Structure of an aprataxin-DNA complex with insights into AOA1 neurodegenerative disease.Semantic proximity Read ↗

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