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

Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.

Nucleic acids research - 20 Apr 2017

Newman Joseph A, Aitkenhead Hazel, Savitsky Pavel, Gileadi Opher

Abstract excerpt

RecQ helicases are important maintainers of genome integrity with distinct roles in almost every cellular process requiring access to DNA. RECQL5 is one of five human RecQ proteins and is particularly versatile in this regard, forming protein complexes with a diverse set of cellular partners in order to coordinate its helicase activity to various processes including replication, recombination and DNA repair. In...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Models, Molecular
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Conformation, alpha-Helical

Share to RecQ Helicases

Share to Scattering, Small Angle

Share to X-Ray Diffraction

Source

Open in PubMed Open full text

Identifiers

PMID: 28100692
DOI: 10.1093/nar/gkw1362
PMCID: PMC5397160

Genes

RECQL5

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Insights into the RecQ helicase mechanism revealed by the structure of the helicase domain of human RECQL5.PMID 28100692Read ↗

Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain.Semantic proximity Read ↗

Crystal structure of the Bloom's syndrome helicase indicates a role for the HRDC domain in conformational changes.Semantic proximity Read ↗

A prominent -hairpin structure in the winged-helix domain of RECQ1 is required for DNA unwinding and oligomer formationSemantic proximity Read ↗

Human RECQL5 participates in the removal of endogenous DNA damageSemantic proximity Read ↗

RECQ5: A Mysterious Helicase at the Interface of DNA Replication and TranscriptionSemantic proximity Read ↗

Human RECQL5β stimulates flap endonuclease 1Semantic proximity Read ↗

RAPADILINO RECQL4 mutant protein lacks helicase and ATPase activity.Semantic proximity Read ↗

Mutations in conserved functional domains of human RecQ helicases are associated with diseases and cancer: A review.Semantic proximity Read ↗

Coupling DNA-binding and ATP hydrolysis in Escherichia coli RecQ: role of a highly conserved aromatic-rich sequence.Semantic proximity Read ↗

Human RecQL4 helicase plays multifaceted roles in the genomic stability of normal and cancer cells.Semantic proximity Read ↗

RECQL5/Recql5 helicase regulates homologous recombination and suppresses tumor formation via disruption of Rad51 presynaptic filaments.Semantic proximity Read ↗

Human RecQ Helicases in DNA Double-Strand Break RepairSemantic proximity Read ↗

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