Evidence map›Paper›PMID 29168508›Full record

ArticleNature2017

Structural basis for the initiation of eukaryotic transcription-coupled DNA repair.

Jun Xu, Indrajit Lahiri, Wei Wang, Adam Wier, Michael A Cianfrocco, Jenny Chong, Alissa A Hare, Peter B Dervan, Frank DiMaio, Andres E Leschziner and 1 more

Open access · greenAbstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 137 papers.

0numbers the graph read from it
0cells of the map it votes in
137citing papers in PubMed
7.9field-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

137 citing papers in PubMed, 209 citations in OpenAlex.

  1. Article
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  15. Article
  16. Transcription-Coupled Repair and R-Loop Crosstalk in Genome Stability.International journal of molecular sciences · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Mechanisms of DNA repair and mutagenesis induced by acetaldehyde, acrolein, aristolochic acids, and vinyl chloride.Journal of environmental science and health. Part C, Toxicology and carcinogenesis · 2025
    Review

77 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

11 authors at 4 institutions in 1 country.

Jun XuDivision of Pharmaceutical Sciences, Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California San Diego, La Jolla, California 92093, USA.
Indrajit LahiriDepartment of Cellular & Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.
Wei WangDivision of Pharmaceutical Sciences, Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California San Diego, La Jolla, California 92093, USA.
Adam WierDepartment of Cellular & Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.
Michael A CianfroccoDepartment of Cellular & Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.
Jenny ChongDivision of Pharmaceutical Sciences, Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California San Diego, La Jolla, California 92093, USA.
Alissa A HareDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Peter B DervanDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
Frank DiMaioDepartment of Biochemistry, University of Washington, Seattle, Washington 98195, USA.
Andres E LeschzinerDepartment of Cellular & Molecular Medicine, School of Medicine, University of California San Diego, La Jolla, California 92093, USA.
Dong WangDivision of Pharmaceutical Sciences, Skaggs School of Pharmacy & Pharmaceutical Sciences, University of California San Diego, La Jolla, California 92093, USA.
University of California, San Diego · USCalifornia Institute of Technology · USUniversity of Montana · USUniversity of Washington · US

Funding

Molecular Mechanisms for DNA Damage Processing by Transcription MachineryR01GM102362 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI WANG, DONG · 2013 to 2025
$5.6M
SEQUENCE SPECIFIC RECOGNITION OF DOUBLE HELICAL DNAR01GM027681 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DERVAN, PETER B · 1985 to 2017
$4.5M
A comparative structural study of ATP-dependent chromatin remodeling complexesR01GM092895 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI LESCHZINER, ANDRES · 2011 to 2021
$3.0M
Protein structure determination from low-resolution experimental dataR01GM123089 · NIGMS · UNIVERSITY OF WASHINGTON · PI DIMAIO, FRANK P · 2017 to 2025
$2.6M
SEQUENCE SPECIFIC RECOGNITION OF DNAR37GM027681 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DERVAN, PETER B · 1996 to 2005
$1.9M
NIGMS NIH HHS R01 GM027681NIGMS NIH HHS R01 GM092895NIGMS NIH HHS R01 GM102362NIGMS NIH HHS R01 GM123089NIGMS NIH HHS R37 GM027681NIH HHS GM092895NIH HHS GM102362NIH HHS GM102362-S1
6 · The paper itself

Abstract

Eukaryotic transcription-coupled repair (TCR) is an important and well-conserved sub-pathway of nucleotide excision repair that preferentially removes DNA lesions from the template strand that block translocation of RNA polymerase II (Pol II). Cockayne syndrome group B (CSB, also known as ERCC6) protein in humans (or its yeast orthologues, Rad26 in Saccharomyces cerevisiae and Rhp26 in Schizosaccharomyces pombe) is among the first proteins to be recruited to the lesion-arrested Pol II during the initiation of eukaryotic TCR. Mutations in CSB are associated with the autosomal-recessive neurological disorder Cockayne syndrome, which is characterized by progeriod features, growth failure and photosensitivity. The molecular mechanism of eukaryotic TCR initiation remains unclear, with several long-standing unanswered questions. How cells distinguish DNA lesion-arrested Pol II from other forms of arrested Pol II, the role of CSB in TCR initiation, and how CSB interacts with the arrested Pol II complex are all unknown. The lack of structures of CSB or the Pol II-CSB complex has hindered our ability to address these questions. Here we report the structure of the S. cerevisiae Pol II-Rad26 complex solved by cryo-electron microscopy. The structure reveals that Rad26 binds to the DNA upstream of Pol II, where it markedly alters its path. Our structural and functional data suggest that the conserved Swi2/Snf2-family core ATPase domain promotes the forward movement of Pol II, and elucidate key roles for Rad26 in both TCR and transcription elongation.

Indexed as

Cryoelectron MicroscopyDNA RepairTranscription, GeneticAdenosine TriphosphatasesDNAProtein DomainsRNA Polymerase IISaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Elongation, GeneticTranscription FactorsAdenosine TriphosphatasesDNARAD26 protein, S cerevisiaeRNA Polymerase IISaccharomyces cerevisiae ProteinsSNF2 protein, S cerevisiaeTranscription Factors

Identifiers

PMID29168508
PMCPMC5907806
OpenAlexW2770404833

What OpenQuestion holds

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Registered trials

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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.