Evidence map›Paper›PMID 38806694›Full record

ArticleNature structural & molecular biology2024

XPD stalled on cross-linked DNA provides insight into damage verification.

Jochen Kuper, Tamsanqa Hove, Sarah Maidl, Hermann Neitz, Florian Sauer, Maximilian Kempf, Till Schroeder, Elke Greiter, Claudia Höbartner, Caroline Kisker

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. A new crystal form of the DNA-free full-length XPD helicase from Thermoplasma acidophilum.Acta crystallographica. Section F, Structural biology communications · 2026
    Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Review
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.

Jochen Kuper *Rudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany. jochen.kuper@virchow.uni-wuerzburg.de.ORCID http://orcid.org/0000-0001-7553-5825
Tamsanqa Hove *Rudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Sarah MaidlRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Hermann NeitzInstitute of Organic Chemistry, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0001-9088-5727
Florian SauerRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-2367-9568
Maximilian KempfRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Till SchroederRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0009-0002-6943-9495
Elke GreiterRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany.
Claudia HöbartnerInstitute of Organic Chemistry, University of Würzburg, Würzburg, Germany.ORCID http://orcid.org/0000-0002-4548-2299
Caroline KiskerRudolf Virchow Center for Integrative and Translational Bioimaging, University of Würzburg, Würzburg, Germany. caroline.kisker@virchow.uni-wuerzburg.de.ORCID http://orcid.org/0000-0002-0216-6026

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The superfamily 2 helicase XPD is a central component of the general transcription factor II H (TFIIH), which is essential for transcription and nucleotide excision DNA repair (NER). Within these two processes, the helicase function of XPD is vital for NER but not for transcription initiation, where XPD acts only as a scaffold for other factors. Using cryo-EM, we deciphered one of the most enigmatic steps in XPD helicase action: the active separation of double-stranded DNA (dsDNA) and its stalling upon approaching a DNA interstrand cross-link, a highly toxic form of DNA damage. The structure shows how dsDNA is separated and reveals a highly unusual involvement of the Arch domain in active dsDNA separation. Combined with mutagenesis and biochemical analyses, we identified distinct functional regions important for helicase activity. Surprisingly, those areas also affect core TFIIH translocase activity, revealing a yet unencountered function of XPD within the TFIIH scaffold. In summary, our data provide a universal basis for NER bubble formation, XPD damage verification and XPG incision.

Indexed as

Cryoelectron MicroscopyDNADNA DamageDNA RepairModels, MolecularXeroderma Pigmentosum Group D ProteinHumansTranscription Factor TFIIHDNAERCC2 protein, humanTranscription Factor TFIIHXeroderma Pigmentosum Group D Protein

Identifiers

PMID38806694
PMCPMC11479942

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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.