Publication: Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor
Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor
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Günter, J., Wenger, R. H., & Scholz, C. C. (2020). Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor. Journal of Photochemistry and Photobiology B: Biology, 210, 111980. https://doi.org/10.1016/j.jphotobiol.2020.111980
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The three hypoxia-inducible factor (HIF) prolyl-4-hydroxylase domain (PHD) 1–3 enzymes confer oxygen sensitivity to the HIF pathway and are novel therapeutic targets for treatment of renal anemia. Inhibition of the PHDs may further be beneficial in other hypoxia-associated diseases, including ischemia and chronic inflammation. Several pharmacologic PHD inhibitors (PHIs) are available, but our understanding of their selectivity and its chemical basis is limited. We here report that the PHI JNJ-42041935 (JNJ-1935) is structurally simila
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- Günter, Julia
- Wenger, Roland H
- Scholz, Carsten C
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Junior Grant of the NCCR Kidney.CH
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Citations
Günter, J., Wenger, R. H., & Scholz, C. C. (2020). Inhibition of firefly luciferase activity by a HIF prolyl hydroxylase inhibitor. Journal of Photochemistry and Photobiology B: Biology, 210, 111980. https://doi.org/10.1016/j.jphotobiol.2020.111980
