Evidence map›Paper›PMID 19074258›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

Recognition and repair of UV lesions in loop structures of duplex DNA by DASH-type cryptochrome.

Richard Pokorny, Tobias Klar, Ulrich Hennecke, Thomas Carell, Alfred Batschauer, Lars-Oliver Essen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
15.6field-weighted citation impact, top 1% 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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 176 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Sensing a rainbow of colors: algal photoreceptors.Frontiers in plant science · 2025
    Review
  6. Article
  7. Review
  8. A structural decryption of cryptochromes.Frontiers in chemistry · 2024
    Review
  9. Review
  10. Review
  11. Signaling Mechanisms by Arabidopsis Cryptochromes.Frontiers in plant science · 2022
    Review
  12. Article
  13. Review
  14. Article
  15. Investigation of the pH-dependence of the oxidation of FAD in VcCRY-1, a member of the cryptochrome-DASH family.Photochemical & photobiological sciences : Official journal of the European Photochemistry Association and the European Society for Photobiology · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

12 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

6 authors at 2 institutions in 1 country.

Richard PokornyDepartment of Biology, Philipps University, Karl-von-Frisch-Strasse 8, D-35032 Marburg, Germany.
Tobias Klar
Ulrich Hennecke
Thomas Carell
Alfred Batschauer
Lars-Oliver Essen
Philipps University of Marburg · DECenter for Integrated Protein Science Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA photolyases and cryptochromes (cry) form a family of flavoproteins that use light energy in the blue/UV-A region for the repair of UV-induced DNA lesions or for signaling, respectively. Very recently, it was shown that members of the DASH cryptochrome subclade repair specifically cyclobutane pyrimidine dimers (CPDs) in UV-damaged single-stranded DNA. Here, we report the crystal structure of Arabidopsis cryptochrome 3 with an in-situ-repaired CPD substrate in single-stranded DNA. The structure shows a binding mode similar to that of conventional DNA photolyases. Furthermore, CPD lesions in double-stranded DNA are bound and repaired with similar efficiency as in single-stranded DNA if the CPD lesion is present in a loop structure. Together, these data reveal that DASH cryptochromes catalyze light-driven DNA repair like conventional photolyases but lack an efficient flipping mechanism for interaction with CPD lesions within duplex DNA.

Indexed as

ArabidopsisArabidopsis ProteinsCryptochromesCrystallography, X-RayDeoxyribodipyrimidine Photo-LyaseDNA DamageDNA, PlantDNA RepairDNA, Single-StrandedProtein Structure, SecondaryProtein Structure, TertiaryPyrimidine DimersUltraviolet RaysArabidopsis ProteinsCry3 protein, ArabidopsisCryptochromesDeoxyribodipyrimidine Photo-LyaseDNA, PlantDNA, Single-StrandedPyrimidine Dimers

Identifiers

PMID19074258
PMCPMC2634942
OpenAlexW2011204918

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.