Evidence map›Paper›PMID 18510925›Full record

ArticleCell2008

Structure of the DNA repair helicase XPD.

Huanting Liu, Jana Rudolf, Kenneth A Johnson, Stephen A McMahon, Muse Oke, Lester Carter, Anne-Marie McRobbie, Sara E Brown, James H Naismith, Malcolm F White

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 156 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
156citing papers in PubMed, 3 pooled it
8.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

156 citing papers in PubMed, 3 syntheses or guidelines pooled it, 258 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. A new crystal form of the DNA-free full-length XPD helicase from Thermoplasma acidophilum.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Structure, function and evolution of the bacterial DinG-like proteins.Computational and structural biotechnology journal · 2025
    Review
  18. Article
  19. Article
  20. Article

96 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Huanting LiuCentre for Biomolecular Sciences, University of St. Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK.
Jana Rudolf
Kenneth A Johnson
Stephen A McMahon
Muse Oke
Lester Carter
Anne-Marie McRobbie
Sara E Brown
James H Naismith
Malcolm F White
University of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/B/14426Medical Research Council G0500367Wellcome Trust
6 · The paper itself

Abstract

The XPD helicase (Rad3 in Saccharomyces cerevisiae) is a component of transcription factor IIH (TFIIH), which functions in transcription initiation and Nucleotide Excision Repair in eukaryotes, catalyzing DNA duplex opening localized to the transcription start site or site of DNA damage, respectively. XPD has a 5' to 3' polarity and the helicase activity is dependent on an iron-sulfur cluster binding domain, a feature that is conserved in related helicases such as FancJ. The xpd gene is the target of mutation in patients with xeroderma pigmentosum, trichothiodystrophy, and Cockayne's syndrome, characterized by a wide spectrum of symptoms ranging from cancer susceptibility to neurological and developmental defects. The 2.25 A crystal structure of XPD from the crenarchaeon Sulfolobus tokodaii, presented here together with detailed biochemical analyses, allows a molecular understanding of the structural basis for helicase activity and explains the phenotypes of xpd mutations in humans.

Indexed as

Amino Acid SubstitutionArchaeal ProteinsCockayne SyndromeCrystallography, X-RayIron-Sulfur ProteinsModels, MolecularMutagenesis, Site-DirectedProtein Structure, TertiarySequence Homology, Amino AcidStructural Homology, ProteinSulfolobusTrichothiodystrophy SyndromesXeroderma PigmentosumXeroderma Pigmentosum Group D ProteinArchaeal ProteinsIron-Sulfur ProteinsXeroderma Pigmentosum Group D Protein

Identifiers

PMID18510925
PMCPMC3326533
OpenAlexW2080380418

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.