Evidence map›Paper›PMID 19892827›Full record

ArticleNucleic acids research2010

Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5R-thymine glycol lesion and structure of the cis-(5R,6S) thymine glycol epimer in the 5'-GTgG-3' sequence: destabilization of two base pairs at the lesion site.

Kyle L Brown, Marina Roginskaya, Yue Zou, Alvin Altamirano, Ashis K Basu, Michael P Stone

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

19 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Genotoxic effects of PMEnvironmental geochemistry and health · 2019
    Article
  5. Article
  6. Article
  7. Article
  8. Repair-Resistant DNA Lesions.Chemical research in toxicology · 2017
    Review
  9. Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Structure of (5'S)-8,5'-cyclo-2'-deoxyguanosine in DNA.Journal of the American Chemical Society · 2011
    Article
  17. Article
  18. Review
  19. Article
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

6 authors at 3 institutions in 1 country.

Kyle L BrownDepartment of Chemistry and Center in Molecular Toxicology, Vanderbilt University, Nashville, TN 37235, USA.
Marina Roginskaya
Yue Zou
Alvin Altamirano
Ashis K Basu
Michael P Stone
East Tennessee State University · USUniversity of Connecticut · USVanderbilt University · US

Funding

Structural Biology Facility CoreP30ES000267 · NIEHS · VANDERBILT UNIVERSITY · PI GUENGERICH, F PETER · 1985 to 2014
$20.3M
DNA Adduct-Induced MutagenesisR01CA055678 · NCI · VANDERBILT UNIVERSITY · PI STONE, MICHAEL P · 1992 to 2016
$4.0M
BIOLOGICAL EFFECTS OF DNA ADDUCTS FORMED BY NITROPYRENESR01ES009127 · NIEHS · UNIVERSITY OF CONNECTICUT STORRS · PI BASU, ASHIS K, SUO, ZUCAI · 1998 to 2014
$3.5M
Ring-Opened and Tandem DNA DamagesR01ES013324 · NIEHS · UNIVERSITY OF CONNECTICUT STORRS · PI BASU, ASHIS K · 2006 to 2010
$1.5M
NCI NIH HHS R01 CA-055678NCI NIH HHS R01 CA-55678NIEHS NIH HHS P30 ES-000267NIEHS NIH HHS R01 ES009127NIEHS NIH HHS R01 ES-013324NIEHS NIH HHS R01 ES013324
6 · The paper itself

Abstract

The 5R thymine glycol (5R-Tg) DNA lesion exists as a mixture of cis-(5R,6S) and trans-(5R,6R) epimers; these modulate base excision repair. We examine the 7:3 cis-(5R,6S):trans-(5R,6R) mixture of epimers paired opposite adenine in the 5'-GTgG-3' sequence with regard to nucleotide excision repair. Human XPA recognizes the lesion comparably to the C8-dG acetylaminoflourene (AAF) adduct, whereas XPC/HR23B recognition of Tg is superior. 5R-Tg is processed by the Escherichia coli UvrA and UvrABC proteins less efficiently than the C8-dG AAF adduct. For the cis-(5R, 6S) epimer Tg and A are inserted into the helix, remaining in the Watson-Crick alignment. The Tg N3H imine and A N(6) amine protons undergo increased solvent exchange. Stacking between Tg and the 3'-neighbor G*C base pair is disrupted. The solvent accessible surface and T(2) relaxation of Tg increases. Molecular dynamics calculations predict that the axial conformation of the Tg CH(3) group is favored; propeller twisting of the Tg*A pair and hydrogen bonding between Tg OH6 and the N7 atom of the 3'-neighbor guanine alleviate steric clash with the 5'-neighbor base pair. Tg also destabilizes the 5'-neighbor G*C base pair. This may facilitate flipping both base pairs from the helix, enabling XPC/HR23B recognition prior to recruitment of XPA.

Indexed as

DNA DamageBase PairingBase SequenceBinding SitesDNADNA-Binding ProteinsDNA Repair EnzymesEndodeoxyribonucleasesEscherichia coli ProteinsHumansModels, MolecularNuclear Magnetic Resonance, BiomolecularProtonsStereoisomerismThymineXeroderma Pigmentosum Group A ProteinDNADNA-Binding ProteinsDNA Repair EnzymesEndodeoxyribonucleasesendodeoxyribonuclease uvrABCEscherichia coli ProteinsProtonsRAD23B protein, humanThyminethymine glycolXeroderma Pigmentosum Group A ProteinXPA protein, human

Identifiers

PMID19892827
PMCPMC2811006
OpenAlexW1988398583

What OpenQuestion holds

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LicenceCC BY-NC
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.