ArticleNature communications2017
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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.
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Systemic engineering and global regulation enabling high-level bilirubin biosynthesis.Nature communications · 2025Article
- Biliverdin reductase A is a major determinant of protective NRF2 signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bilisense: An affordable sensor for on-site diagnosis of jaundice and prevention of kernicterus.Biosensors & bioelectronics · 2025Article
- Loss of Biliverdin Reductase Increases Oxidative Stress in the CyanobacteriumMicroorganisms · 2023Article
- Biliverdin reductase bridges focal adhesion kinase to Src to modulate synaptic signaling.Science signaling · 2022Article
- Recent Advances in the Understanding of the Reaction Chemistries of the Heme Catabolizing Enzymes HO and BVR Based on High Resolution Protein Structures.Current medicinal chemistry · 2020Review
- Structure of aBiochemistry · 2019Article
Corrections and comments
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Authors and funding
17 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biliverdin reductase catalyses the last step in haem degradation and produces the major lipophilic antioxidant bilirubin via reduction of biliverdin, using NAD(P)H as a cofactor. Despite the importance of biliverdin reductase in maintaining the redox balance, the molecular details of the reaction it catalyses remain unknown. Here we present the crystal structure of biliverdin reductase in complex with biliverdin and NADP
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Registered trials
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