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Cited by 90

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function

Michel, Maurice, Benítez-Buelga, Carlos, Calvo, Patricia A., Hanna, Bishoy M. F., Mortusewicz, Oliver, Masuyer, Geoffrey, Davies, Jonathan, Wallner, Olov, Sanjiv, Kumar, Albers, Julian J., Castañeda-Zegarra, Sergio, Jemth, Ann-Sofie, Visnes, Torkild, Sastre-Perona, Ana, Danda, Akhilesh N., Homan, Evert J., Marimuthu, Karthick, Zhenjun, Zhao, Chi, Celestine N., Sarno, Antonio, Wiita, Elisée, von Nicolai, Catharina, Komor, Anna J., Rajagopal, Varshni, Müller, Sarah, Hank, Emily C., Varga, Marek, Scaletti, Emma R., Pandey, Monica, Karsten, Stella, Haslene-Hox, Hanne, Loevenich, Simon, Marttila, Petra, Rasti, Azita, Mamonov, Kirill, Ortis, Florian, Schömberg, Fritz, Loseva, Olga, Stewart, Josephine, D’Arcy-Evans, Nicholas, Koolmeister, Tobias, Henriksson, Martin, Michel, Dana, de Ory, Ana, Acero, Lucia, Calvete, Oriol, Scobie, Martin, Hertweck, Christian, Vilotijevic, Ivan, Kalderén, Christina, Osorio, Ana, Perona, Rosario, Stolz, Alexandra, Stenmark, Pål, Berglund, Ulrika Warpman, de Vega, Miguel, Helleday, Thomas·2022·Science
DOI 10.1126/science.abf8980
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Abstract

Oxidative DNA damage is recognized by 8-oxoguanine (8-oxoG) DNA glycosylase 1 (OGG1), which excises 8-oxoG, leaving a substrate for apurinic endonuclease 1 (APE1) and initiating repair. Here, we describe a small molecule (TH10785) that interacts with the phenylalanine-319 and glycine-42 amino acids of OGG1, increases the enzyme activity 10-fold, and generates a previously undescribed β,δ-lyase enzymatic function. TH10785 controls the catalytic activity mediated by a nitrogen base within its molecular structure. In cells, TH10785 increases OGG1 recruitment to and repair of oxidative DNA damage. This alters the repair process, which no longer requires APE1 but instead is dependent on polynucleotide kinase phosphatase (PNKP1) activity. The increased repair of oxidative DNA lesions with a small molecule may have therapeutic applications in various diseases and aging.

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Crossref · 10.1126/science.abf8980

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Metadata

Authors
Michel, M., Benítez-Buelga, C., Calvo, P. A., Hanna, B. M. F., Mortusewicz, O., Masuyer, G., Davies, J., Wallner, O., Sanjiv, K., Albers, J. J., Castañeda-Zegarra, S., Jemth, A.-S., Visnes, T., Sastre-Perona, A., Danda, A. N., Homan, E. J., Marimuthu, K., Zhenjun, Z., Chi, C. N., Sarno, A., Wiita, E., von Nicolai, C., Komor, A. J., Rajagopal, V., Müller, S., Hank, E. C., Varga, M., Scaletti, E. R., Pandey, M., Karsten, S., Haslene-Hox, H., Loevenich, S., Marttila, P., Rasti, A., Mamonov, K., Ortis, F., Schömberg, F., Loseva, O., Stewart, J., D’Arcy-Evans, N., Koolmeister, T., Henriksson, M., Michel, D., de Ory, A., Acero, L., Calvete, O., Scobie, M., Hertweck, C., Vilotijevic, I., Kalderén, C., Osorio, A., Perona, R., Stolz, A., Stenmark, P., Berglund, U. W., de Vega, M., & Helleday, T.
Affiliations
  • Science for Life Laboratory, Department of Oncology-Pathology, Karolinska Institutet, 171 76 Stockholm, Sweden.
  • Centro de Biología Molecular “Severo Ochoa” (CSIC-UAM), 28049 Madrid, Spain.
  • Department of Pharmacy and Pharmacology, Centre for Therapeutic Innovation, University of Bath, Bath BA2 7AY, UK.
  • Department of Biochemistry and Biophysics, Stockholm University, 106 91 Stockholm, Sweden.
  • Department of Biotechnology and Nanomedicine, SINTEF Industry, N-7465 Trondheim, Norway.
  • Experimental Therapies and Novel Biomarkers in Cancer, Hospital La Paz Institute for Health Research (IdiPAZ), Madrid, Spain.
  • Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden.
  • Department of Environment and New Resources, SINTEF Ocean, N-7496 Trondheim, Norway.
  • Leibniz Institute for Natural Product Research and Infection Biology – Hans Knöll Institute, Department of Biomolecular Chemistry, 07745 Jena, Germany.
  • Institute of Organic and Macromolecular Chemistry, Friedrich Schiller University Jena, 07743 Jena, Germany.
  • Chemical Processes and Pharmaceutical Development, Unit Process Chemistry I, Research Institutes of Sweden – RISE, 151 36 Södertälje, Sweden.
  • Department of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, 106 91 Stockholm, Sweden.
  • Familial Cancer Clinical Unit, Human Cancer Genetics Programme, Spanish National Cancer Research Centre (CNIO), 28029 Madrid, Spain.
  • Instituto de Investigaciones Biomédicas Alberto Sols (CSIC/UAM), 28029 Madrid, Spain.
  • Institute of Biochemistry II and Buchmann Institute for Molecular Life Science, Goethe University Frankfurt, 60590 Frankfurt, Germany.
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2022-06-24
Volume
376
Issue
6600
Pages
1471-1476
ISSN
  • 0036-8075
  • 1095-9203
DOI
10.1126/science.abf8980
Cited by
90
References
29
Language
en

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CoChat. (2026). Citation check: Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function. https://app.cochat.ai/papers/10.1126/science.abf8980
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Michel, M., Benítez-Buelga, C., Calvo, P. A., Hanna, B. M. F., Mortusewicz, O., Masuyer, G., Davies, J., Wallner, O., Sanjiv, K., Albers, J. J., Castañeda-Zegarra, S., Jemth, A.-S., Visnes, T., Sastre-Perona, A., Danda, A. N., Homan, E. J., Marimuthu, K., Zhenjun, Z., Chi, C. N., . . . Helleday, T. (2022). Small-molecule activation of OGG1 increases oxidative DNA damage repair by gaining a new function. Science. https://doi.org/10.1126/science.abf8980

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.