ArticleProceedings of the National Academy of Sciences of the United States of America2025
Soluble guanylyl cyclase, the NO receptor, drives vasorelaxation via endothelial S-nitrosation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- The Emerging Role of Endothelial Ion Channels in the Control of Human Microcirculation.International journal of molecular sciences · 2026Review
- NO- and S-nitrosothiols-dependent relaxation in large and small resistance blood vessels.Frontiers in physiology · 2026Review
- Transcriptional and electrical identity in endothelial cells is orchestrated by intercellular coupling.Frontiers in physiology · 2025Article
Corrections and comments
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Authors and funding
10 authors.
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Abstract
We previously demonstrated that the NO-stimulated soluble guanylyl cyclase (GC1), which produces cGMP, also has the ability to transfer S-nitrosothiols (SNO) to other proteins in a reaction involving oxidized Thioredoxin 1 (oTrx1). This transnitrosation cascade was established in vitro and involved Cys 610 (C610) of GC1 as the major SNO-donor. To assay the relevance of GC1 transnitrosation under physiological conditions and in oxidative pathologies, we studied a knock-in mouse in which C610 was replaced with a serine (KI αC
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