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

The XBP-Bax1 helicase-nuclease complex unwinds and cleaves DNA: implications for eukaryal and archaeal nucleotide excision repair.

The Journal of biological chemistry - 2 Apr 2010

Rouillon Christophe, White Malcolm F

Abstract excerpt

XPB helicase is an integral part of transcription factor TFIIH, required for both transcription initiation and nucleotide excision repair (NER). Along with the XPD helicase, XPB plays a crucial but only partly understood role in defining and extending the DNA repair bubble around lesions in NER. Archaea encode clear homologues of XPB and XPD, and structural studies of these proteins have yielded key insights...

Read the complete abstract on PubMed

Topics

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

Share to Archaeal Proteins
Share to DNA, Archaeal
Share to Electrophoretic Mobility Shift Assay

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

Share to Endodeoxyribonucleases

Share to Endonucleases

Share to Eukaryota

Share to Magnesium

Share to Sulfolobus solfataricus

Source

Open in PubMed Open full text

Identifiers

PMID: 20139443
DOI: 10.1074/jbc.M109.094763
PMCID: PMC2856306

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

The XBP-Bax1 helicase-nuclease complex unwinds and cleaves DNA: implications for eukaryal and archaeal nucleotide excision repair.PMID 20139443Read ↗

XPB: An essential helicase involved in both transcription and repair of DNA.Semantic proximity Read ↗

XPB: An unconventional SF2 DNA helicaseSemantic proximity Read ↗

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

Structure, function and evolution of the XPD family of iron-sulfur-containing 5'-->3' DNA helicases.Semantic proximity Read ↗

Structural comparison of AP endonucleases from the exonuclease III family reveals new amino acid residues in human AP endonuclease 1 that are involved in incision of damaged DNA.Semantic proximity Read ↗

Bacterial NHEJ: a never ending storySemantic proximity Read ↗

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

Structural basis of TFIIH activation for nucleotide excision repairSemantic proximity Read ↗

Giardia duodenalis: Base excision repair pathway enzyme FEN1 carries out catalytic activities pertaining to NER pathwaySemantic proximity Read ↗

Mechanisms and regulation of dsDNA break repair in the Sulfolobus genus of thermophilic archaeaSemantic proximity Read ↗

The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repairSemantic proximity Read ↗

Structural basis for the mutually exclusive anchoring of P body components EDC3 and Tral to the DEAD box protein DDX6/Me31B.Semantic proximity Read ↗

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