ArticleProceedings of the National Academy of Sciences of the United States of America2025
Structural and functional dynamics of human cone cGMP-phosphodiesterase important for photopic vision.
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. An erratum has been issued. Cited by 4 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed.
- Progressive cone dystrophy in PDE6C-associated achromatopsia with a likely pathogenic variant and a VUS.Documenta ophthalmologica. Advances in ophthalmology · 2026Article
- Structural basis of phosphodiesterase-5 conformational organization revealed by a PDE6/PDE5 chimera.The Journal of biological chemistry · 2026Article
- Molecular Determinants of Allosteric Inhibitor Affinity and Selectivity in PDE5.bioRxiv : the preprint server for biology · 2026Article
- Roles of Cyclic Nucleotide Phosphodiesterases in Signal Transduction Pathways in the NematodeCells · 2025Review
Corrections and comments
- Erratum issued
Authors and funding
4 authors.
Funding
Abstract
Cone cGMP-phosphodiesterase (PDE6) is the key effector enzyme for daylight vision, and its properties are critical for shaping distinct physiology of cone photoreceptors. We determined the structures of human cone PDE6C in various liganded states by single-particle cryo-EM that reveal essential functional dynamics and adaptations of the enzyme. Our analysis exposed the dynamic nature of PDE6C association with its regulatory γ-subunit (Pγ) which allows openings of the catalytic pocket in the absence of phototransduction signaling, thereby controlling photoreceptor noise and sensitivity. We demonstrate evolutionarily recent adaptations of PDE6C stemming from residue substitutions in the Pγ subunit and the noncatalytic cGMP binding site and influencing the Pγ dynamics in holoPDE6C. Thus, our structural analysis sheds light on the previously unrecognized molecular evolution of the effector enzyme in cones that advances adaptation for photopic vision.
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.