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

Crystal structure of human XLF: a twist in nonhomologous DNA end-joining.

Molecular cell - 28 Dec 2007

Andres Sara N, Modesti Mauro, Tsai Chun J, Chu Gilbert, Junop Murray S

Abstract excerpt

DNA double-strand breaks represent one of the most severe forms of DNA damage in mammalian cells. One pathway for repairing these breaks occurs via nonhomologous end-joining (NHEJ) and depends on XRCC4, LigaseIV, and Cernunnos, also called XLF. Although XLF stimulates XRCC4/LigaseIV to ligate mis...

Read the complete abstract on PubMed

Topics

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

Share to Crystallization
Share to Dimerization
Share to DNA Ligase ATP

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA Ligases

Share to DNA Repair

Share to DNA Repair Enzymes

Share to Electrophoresis, Polyacrylamide Gel

Share to Electrophoretic Mobility Shift Assay

Source

Identifiers

PMID: 18158905
DOI: 10.1016/j.molcel.2007.10.024

Genes

XRCC4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-18158905-2026-09-02.2. 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

Crystal structure of human XLF: a twist in nonhomologous DNA end-joining.PMID 18158905Read ↗

Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.Semantic proximity Read ↗

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.Semantic proximity Read ↗

Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity.Semantic proximity Read ↗

Evolutionary and functional conservation of the DNA non-homologous end-joining protein, XLF/Cernunnos.Semantic proximity Read ↗

The spatial organization of non-homologous end joining: From bridging to end joiningSemantic proximity Read ↗

PAXX binding to the NHEJ machinery explains functional redundancy with XLFSemantic proximity Read ↗

XRCC4's interaction with XLF is required for coding (but not signal) end joining.Semantic proximity Read ↗

Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF.Semantic proximity Read ↗

Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4Semantic proximity Read ↗

Cooperative assembly of a protein-DNA filament for nonhomologous end joining.Semantic proximity Read ↗

PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repairSemantic proximity Read ↗

Interplay between Cernunnos-XLF and Nonhomologous End-joining Proteins at DNA Ends in the CellSemantic proximity Read ↗

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