ArticleScience advances2019
Cryo-EM structure of phosphodiesterase 6 reveals insights into the allosteric regulation of type I phosphodiesterases.
Article in Science advances, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 47 citations in OpenAlex.
- Article
- Structural basis of phosphodiesterase-5 conformational organization revealed by a PDE6/PDE5 chimera.The Journal of biological chemistry · 2026Article
- Cyclic nucleotide phosphodiesterases as drug targets.Pharmacological reviews · 2025Review
- Photopic flicker optoretinography captures the light-driven length modulation of photoreceptors during phototransduction.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural and functional dynamics of human cone cGMP-phosphodiesterase important for photopic vision.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Probing the mechanism by which the retinal G protein transducin activates its biological effector PDE6.The Journal of biological chemistry · 2024Article
- Reconstitution of the phosphodiesterase 6 maturation process important for photoreceptor cell function.The Journal of biological chemistry · 2024Article
- Identification and Characterization of Retinitis Pigmentosa in a Novel Mouse Model Caused by PDE6B-T592I.Biomedicines · 2023Article
- Stress resilience-enhancing drugs preserve tissue structure and function in degenerating retina via phosphodiesterase inhibition.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- From Deep Mutational Mapping of Allosteric Protein Landscapes to Deep Learning of Allostery and Hidden Allosteric Sites: Zooming in on "Allosteric Intersection" of Biochemical and Big Data Approaches.International journal of molecular sciences · 2023Review
- Machine learning and protein allostery.Trends in biochemical sciences · 2023Review
- Structural view of G protein-coupled receptor signaling in the retinal rod outer segment.Trends in biochemical sciences · 2023Review
- Reproducibility of the Rod Photoreceptor Response Depends Critically on the Concentration of the Phosphodiesterase Effector Enzyme.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- The Emerging Role of the Interaction of Extracellular Vesicle and Autophagy-Novel Insights into Neurological Disorders.Journal of inflammation research · 2022Review
- Photoreceptor Phosphodiesterase (PDE6): Structure, Regulatory Mechanisms, and Implications for Treatment of Retinal Diseases.Advances in experimental medicine and biology · 2022Review
- Article
- Photoreceptor phosphodiesterase (PDE6): activation and inactivation mechanisms during visual transduction in rods and cones.Pflugers Archiv : European journal of physiology · 2021Review
- New focus on regulation of the rod photoreceptor phosphodiesterase.Current opinion in structural biology · 2021Review
- Structural insights into the mechanism of rhodopsin phosphodiesterase.Nature communications · 2020Article
- The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cyclic nucleotide phosphodiesterases (PDEs) work in conjunction with adenylate/guanylate cyclases to regulate the key second messengers of G protein-coupled receptor signaling. Previous attempts to determine the full-length structure of PDE family members at high-resolution have been hindered by structural flexibility, especially in their linker regions and N- and C-terminal ends. Therefore, most structure-activity relationship studies have so far focused on truncated and conserved catalytic domains rather than the regulatory domains that allosterically govern the activity of most PDEs. Here, we used single-particle cryo-electron microscopy to determine the structure of the full-length PDE6αβ2γ complex. The final density map resolved at 3.4 Å reveals several previously unseen structural features, including a coiled N-terminal domain and the interface of PDE6γ subunits with the PDE6αβ heterodimer. Comparison of the PDE6αβ2γ complex with the closed state of PDE2A sheds light on the conformational changes associated with the allosteric activation of type I PDEs.
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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 OpenQuestion graph.