ArticleThe Journal of biological chemistry2014
Strand-specific recognition of DNA damages by XPD provides insights into nucleotide excision repair substrate versatility.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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.
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.
Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- Integrating Structural, Biochemical, and Cellular Perspectives on the TFIIH Helicases XPB and XPD.Biomolecules · 2026Review
- Base-pair scale dynamics of a repair helicase on DNA lesions reveal varied damage-sensing mechanisms.bioRxiv : the preprint server for biology · 2026Article
- A new crystal form of the DNA-free full-length XPD helicase from Thermoplasma acidophilum.Acta crystallographica. Section F, Structural biology communications · 2026Article
- Transcription-Coupled Nucleotide Excision Repair: A Faster Solution or the Only Option?Biomolecules · 2025Review
- Differing structures and dynamics of two photolesions portray verification differences by the human XPD helicase.Nucleic acids research · 2023Article
- Phosphorylation of XPD drives its mitotic role independently of its DNA repair and transcription functions.Science advances · 2022Article
- Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair.Nature communications · 2021Article
- The Interaction Efficiency of XPD-p44 With Bulky DNA Damages Depends on the Structure of the Damage.Frontiers in cell and developmental biology · 2021Article
- The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repair.Nucleic acids research · 2020Article
- Envisioning how the prototypic molecular machine TFIIH functions in transcription initiation and DNA repair.DNA repair · 2020Review
- SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication.Nucleic acids research · 2020Article
- Article
- The Structures of Eukaryotic Transcription Pre-initiation Complexes and Their Functional Implications.Sub-cellular biochemistry · 2019Review
- RecQ and Fe-S helicases have unique roles in DNA metabolism dictated by their unwinding directionality, substrate specificity, and protein interactions.Biochemical Society transactions · 2018Review
- Studying protein-DNA interactions using atomic force microscopy.Seminars in cell & developmental biology · 2018Review
- Mechanistic and biological considerations of oxidatively damaged DNA for helicase-dependent pathways of nucleic acid metabolism.Free radical biology & medicine · 2017Review
- Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair.Journal of visualized experiments : JoVE · 2017Article
- Conservation and Divergence in Nucleotide Excision Repair Lesion Recognition.The Journal of biological chemistry · 2016Article
- Rational elicitation of cold-sensitive phenotypes.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mechanism of DNA loading by the DNA repair helicase XPD.Nucleic acids research · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recognition and removal of DNA damages is essential for cellular and organismal viability. Nucleotide excision repair (NER) is the sole mechanism in humans for the repair of carcinogenic UV irradiation-induced photoproducts in the DNA, such as cyclobutane pyrimidine dimers. The broad substrate versatility of NER further includes, among others, various bulky DNA adducts. It has been proposed that the 5'-3' helicase XPD (xeroderma pigmentosum group D) protein plays a decisive role in damage verification. However, despite recent advances such as the identification of a DNA-binding channel and central pore in the protein, through which the DNA is threaded, as well as a dedicated lesion recognition pocket near the pore, the exact process of target site recognition and verification in eukaryotic NER still remained elusive. Our single molecule analysis by atomic force microscopy reveals for the first time that XPD utilizes different recognition strategies to verify structurally diverse lesions. Bulky fluorescein damage is preferentially detected on the translocated strand, whereas the opposite strand preference is observed for a cyclobutane pyrimidine dimer lesion. Both states, however, lead to similar conformational changes in the resulting specific complexes, indicating a merge to a "final" verification state, which may then trigger the recruitment of further NER proteins.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.