Evidence map›Paper›PMID 23112169›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Alkyltransferase-like protein (Atl1) distinguishes alkylated guanines for DNA repair using cation-π interactions.

Oliver J Wilkinson, Vitaly Latypov, Julie L Tubbs, Christopher L Millington, Rihito Morita, Hannah Blackburn, Andrew Marriott, Gail McGown, Mary Thorncroft, Amanda J Watson and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. 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
1.5field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Review
  3. Bracken Fern Carcinogen, Ptaquiloside, Forms a GuanineJournal of agricultural and food chemistry · 2025
    Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Alkyltransferase-like protein clusters scan DNA rapidly over long distances and recruit NER to alkyl-DNA lesions.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

17 authors at 6 institutions in 3 countries.

Oliver J WilkinsonCentre for Chemical Biology, Department of Chemistry, Krebs Institute, University of Sheffield, Sheffield S3 7HF, United Kingdom.
Vitaly Latypov
Julie L Tubbs
Christopher L Millington
Rihito Morita
Hannah Blackburn
Andrew Marriott
Gail McGown
Mary Thorncroft
Amanda J Watson
Bernard A Connolly
Jane A Grasby
Ryoji Masui
Christopher A Hunter
John A Tainer
Geoffrey P Margison
David M Williams
Cancer Research UK Manchester Institute · GBUniversity of Sheffield · GBScripps Research Institute · USNewcastle University · GBOsaka University · JPUniversity of Liverpool · GB

Funding

Structural Biochemistry of DNA DealkylationR01CA097209 · NCI · SCRIPPS RESEARCH INSTITUTE, THE · PI TAINER, JOHN A. · 2002 to 2014
$4.4M
Biotechnology and Biological Sciences Research CouncilCancer Research UKNCI NIH HHS CA097209NCI NIH HHS R01 CA097209
6 · The paper itself

Abstract

Alkyltransferase-like (ATL) proteins in Schizosaccharomyces pombe (Atl1) and Thermus thermophilus (TTHA1564) protect against the adverse effects of DNA alkylation damage by flagging O(6)-alkylguanine lesions for nucleotide excision repair (NER). We show that both ATL proteins bind with high affinity to oligodeoxyribonucleotides containing O(6)-alkylguanines differing in size, polarity, and charge of the alkyl group. However, Atl1 shows a greater ability than TTHA1564 to distinguish between O(6)-alkylguanine and guanine and in an unprecedented mechanism uses Arg69 to probe the electrostatic potential surface of O(6)-alkylguanine, as determined using molecular mechanics calculations. An unexpected consequence of this feature is the recognition of 2,6-diaminopurine and 2-aminopurine, as confirmed in crystal structures of respective Atl1-DNA complexes. O(6)-Alkylguanine and guanine discrimination is diminished for Atl1 R69A and R69F mutants, and S. pombe R69A and R69F mutants are more sensitive toward alkylating agent toxicity, revealing the key role of Arg69 in identifying O(6)-alkylguanines critical for NER recognition.

Indexed as

Alkyl and Aryl TransferasesAlkylationAmino Acid SubstitutionBacterial ProteinsCrystallography, X-RayDNA RepairGuanineMutation, MissenseOligodeoxyribonucleotidesProtein BindingProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsThermus thermophilusAlkyl and Aryl TransferasesATL1 protein, S pombeBacterial ProteinsGuanineOligodeoxyribonucleotidesSchizosaccharomyces pombe Proteins

Identifiers

PMID23112169
PMCPMC3503161
OpenAlexW2121128278

What OpenQuestion holds

Textmetadata
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.