Evidence map›Paper›PMID 40298610›Full record

ArticleJournal of the American Chemical Society2025

Redox-State-Dependent Structural Changes within a Prokaryotic 6-4 Photolyase.

Po-Hsun Wang, Yuhei Hosokawa, Jessica C Soares, Hans-Joachim Emmerich, Valeri Fuchs, Nicolas Caramello, Sylvain Engilberge, Andrea Bologna, Christian Joshua Rosner, Mai Nakamura and 14 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of the American Chemical Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. The Quantum Environment in Cryptochrome Enhances Light Absorption of FAD.bioRxiv : the preprint server for biology · 2026
    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

24 authors.

Po-Hsun WangDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.
Yuhei HosokawaDepartment of Chemistry, National Taiwan University, 1, Roosevelt Rd. Sec. 4, Taipei 106, Taiwan.ORCID 0000-0001-9559-8567
Jessica C SoaresBiochemistry, Faculty of Chemistry, University of Kaiserslautern, Kaiserslautern D-67663, Germany.ORCID 0009-0004-8682-8374
Hans-Joachim EmmerichDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.
Valeri FuchsDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.
Nicolas CaramelloEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.
Sylvain EngilbergeEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.
Andrea BolognaDepartment of Science and Technology, University of Sannio, Via Francesco de Sanctis, snc, 82100 Benevento, Italy.
Christian Joshua RosnerDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.
Mai NakamuraDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Mohamed WatadDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.
Fangjia LuoJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.ORCID 0000-0003-0631-6236
Shigeki OwadaJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Takehiko ToshaRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0002-8971-0759
Jungmin KangRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.ORCID 0000-0002-3506-6400
Kensuke TonoJapan Synchrotron Radiation Research Institute, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5198, Japan.
Yoshitaka BesshoInstitute of Biological Chemistry, Academia Sinica, 128 Academia Rd. Sec. 2, Nankang, Taipei 115, Taiwan.ORCID 0000-0001-9297-7473
Eriko NangoRIKEN SPring-8 Center, 1-1-1 Kouto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.
Antonio J PierikBiochemistry, Faculty of Chemistry, University of Kaiserslautern, Kaiserslautern D-67663, Germany.ORCID 0000-0002-1509-6370
Antoine RoyantEuropean Synchrotron Radiation Facility, 38043 Grenoble, France.
Ming-Daw TsaiInstitute of Biological Chemistry, Academia Sinica, 128 Academia Rd. Sec. 2, Nankang, Taipei 115, Taiwan.ORCID 0000-0003-1374-0414
Junpei YamamotoDivision of Chemistry, Graduate School of Engineering Science, Osaka University, 1-3 Machikaneyama, Toyonaka, Osaka 560-8531, Japan.
Manuel Maestre-ReynaInstitute of Biological Chemistry, Academia Sinica, 128 Academia Rd. Sec. 2, Nankang, Taipei 115, Taiwan.
Lars-Oliver EssenDepartment of Chemistry, Philipps University Marburg, Hans-Meerwein Strasse 4, Marburg 35032, Germany.ORCID 0000-0003-4272-4026

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photolyases repair UV damage to DNA by using absorbed blue light. Within the photolyase/cryptochrome superfamily (PCSf), a major subgroup consists of prokaryotic (6-4) photolyases. These enzymes rely on flavin adenine dinucleotide (FAD) as a catalytic cofactor, besides an ancillary antenna chromophore, and a [4Fe-4S] cluster with yet unknown function. For the prokaryotic 6-4 photolyase of

Indexed as

Caulobacter crescentusDeoxyribodipyrimidine Photo-LyaseCrystallography, X-RayFlavin-Adenine DinucleotideIron-Sulfur ProteinsModels, MolecularOxidation-ReductionDeoxyribodipyrimidine Photo-LyaseFlavin-Adenine DinucleotideIron-Sulfur Proteins

Identifiers

PMID40298610
PMCPMC12082625

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.