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

A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases.

Journal of molecular biology - 3 Aug 2007

Yeeles Joseph T P, Dillingham Mark S

Abstract excerpt

Nature has devised many strategies for repairing DNA breaks. In homology-dependent pathways, the break is first processed to a 3'-ssDNA overhang that serves as a substrate for DNA strand exchange. Here, we demonstrate a distinct biochemical mechanism for DNA break processing employed by the AddAB...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Bacterial Proteins
Share to Deoxyribonucleases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Damage

Share to DNA Repair

Share to Exodeoxyribonucleases

Share to Protein Structure, Tertiary

Share to Recombination, Genetic

Source

Identifiers

PMID: 17570399
DOI: 10.1016/j.jmb.2007.05.053

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17570399-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases.PMID 17570399Read ↗

Insights into Chi recognition from the structure of an AddAB-type helicase-nuclease complex.Semantic proximity Read ↗

Chi hotspots trigger a conformational change in the helicase-like domain of AddAB to activate homologous recombination.Semantic proximity Read ↗

Structures and single-molecule analysis of bacterial motor nuclease AdnAB illuminate the mechanism of DNA double-strand break resection.Semantic proximity Read ↗

The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain.Semantic proximity Read ↗

Homologous recombination mediated by the mycobacterial AdnAB helicase without end resection by the AdnAB nucleases.Semantic proximity Read ↗

AdnAB: a new DSB-resecting motor-nuclease from mycobacteria.Semantic proximity Read ↗

Coordination of DNA replication and recombination activities in the maintenance of genome stabilitySemantic proximity Read ↗

RAG proteins shepherd double-strand breaks to a specific pathway, suppressing error-prone repair, but RAG nicking initiates homologous recombination.Semantic proximity Read ↗

A structural model for the damage-sensing complex in bacterial nucleotide excision repair.Semantic proximity Read ↗

Double strand break unwinding and resection by the mycobacterial helicase-nuclease AdnAB in the presence of single strand DNA-binding protein (SSB).Semantic proximity Read ↗

Protein-mediated stabilization and nicking of the non-template DNA strand dramatically affect R-loop formation <i>in vitro</i>Semantic proximity Read ↗

Small-molecule sensitization of RecBCD helicase-nuclease to a Chi hotspot-activated state.Semantic proximity Read ↗

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